HEADER    SIGNALING PROTEIN                       02-SEP-19   6KUW              
TITLE     CRYSTAL STRUCTURE OF HUMAN ALPHA2C ADRENERGIC G PROTEIN-COUPLED       
TITLE    2 RECEPTOR.                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-2C ADRENERGIC RECEPTOR;                              
COMPND   3 CHAIN: A, B;                                                         
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    ALPHA2C ADRENERGIC RECEPTOR, ANTAGONIST, GPCR, SIGNALING PROTEIN      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.Y.CHEN,L.J.WU,D.WU,G.S.ZHONG                                        
REVDAT   1   04-DEC-19 6KUW    0                                                
JRNL        AUTH   X.Y.CHEN,D.WU,L.J.WU,G.W.HAN,Y.GUO,G.S.ZHONG                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN ALPHA2C ADRENERGIC G              
JRNL        TITL 2 PROTEIN-COUPLED RECEPTOR.                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 26777                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.216                          
REMARK   3   R VALUE            (WORKING SET)  : 0.213                          
REMARK   3   FREE R VALUE                      : 0.262                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.860                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1302                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.91                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 83.15                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2620                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2285                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2483                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2242                   
REMARK   3   BIN FREE R VALUE                        : 0.3088                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.23                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 137                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7370                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 243                                     
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 79.97                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.35300                                             
REMARK   3    B22 (A**2) : 2.84130                                              
REMARK   3    B33 (A**2) : 3.51160                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.410               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.389               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7819   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10596  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2669   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 1275   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7819   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 999    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9309   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.62                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.17                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|41 - 454 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.6640  -14.8453   42.5422           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0142 T22:   -0.1668                                    
REMARK   3     T33:   -0.2213 T12:   -0.0397                                    
REMARK   3     T13:   -0.0020 T23:   -0.0017                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7913 L22:    1.6143                                    
REMARK   3     L33:    3.7110 L12:    0.2385                                    
REMARK   3     L13:    0.7299 L23:    0.6163                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0429 S12:   -0.0058 S13:   -0.0128                     
REMARK   3     S21:   -0.0950 S22:    0.0044 S23:    0.0260                     
REMARK   3     S31:    0.0654 S32:   -0.2193 S33:    0.0385                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|1001 - 1196 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.5118  -26.5342   -4.8486           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3163 T22:   -0.2570                                    
REMARK   3     T33:   -0.4493 T12:   -0.1423                                    
REMARK   3     T13:    0.1600 T23:   -0.0430                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1014 L22:    4.7556                                    
REMARK   3     L33:    9.7294 L12:    0.0118                                    
REMARK   3     L13:   -0.8367 L23:    1.4480                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2245 S12:    0.4141 S13:   -0.3984                     
REMARK   3     S21:   -0.5396 S22:   -0.1411 S23:   -0.5338                     
REMARK   3     S31:   -0.0761 S32:   -0.0857 S33:    0.3656                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B|41 - 453 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):   -7.9262    4.5465   43.2563           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1098 T22:   -0.0674                                    
REMARK   3     T33:   -0.2769 T12:   -0.1802                                    
REMARK   3     T13:    0.0533 T23:   -0.0344                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5677 L22:    1.5324                                    
REMARK   3     L33:    3.5257 L12:   -0.1863                                    
REMARK   3     L13:   -0.4776 L23:    0.4448                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1167 S12:    0.1369 S13:    0.1740                     
REMARK   3     S21:   -0.2713 S22:    0.2219 S23:   -0.2212                     
REMARK   3     S31:   -0.6100 S32:    0.8170 S33:   -0.1051                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { B|1001 - 1196 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.7115   12.3845   -6.7691           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2734 T22:   -0.0929                                    
REMARK   3     T33:   -0.4832 T12:    0.2657                                    
REMARK   3     T13:    0.0628 T23:    0.0026                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.2038 L22:    5.5790                                    
REMARK   3     L33:    7.7060 L12:   -1.4977                                    
REMARK   3     L13:   -1.2195 L23:    1.1890                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1983 S12:   -0.1834 S13:    0.1528                     
REMARK   3     S21:   -0.3868 S22:   -0.4140 S23:    0.0932                     
REMARK   3     S31:   -1.0885 S32:   -0.6297 S33:    0.2158                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6KUW 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_1300012369.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-18                          
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) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26778                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 3.740                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.23                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.740                              
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: 4S0V                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE MONOBASIC (0.1M),       
REMARK 280  HEPES PH6.5-6.9 (0.1M), PEG400 24-35%, LIPIDIC CUBIC PHASE,         
REMARK 280  TEMPERATURE 293.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.24000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.22500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.37000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.22500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.24000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.37000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     VAL A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     TRP A    39                                                      
REMARK 465     GLY A    40                                                      
REMARK 465     TYR A   191                                                      
REMARK 465     ARG A   192                                                      
REMARK 465     GLN A   193                                                      
REMARK 465     PRO A   194                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     GLY A   196                                                      
REMARK 465     ARG A   455                                                      
REMARK 465     ARG A   456                                                      
REMARK 465     ARG A   457                                                      
REMARK 465     ARG A   458                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     VAL B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     ASN B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     TRP B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     GLN B   193                                                      
REMARK 465     PRO B   194                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     ALA B   198                                                      
REMARK 465     TYR B   199                                                      
REMARK 465     ARG B   454                                                      
REMARK 465     ARG B   455                                                      
REMARK 465     ARG B   456                                                      
REMARK 465     ARG B   457                                                      
REMARK 465     ARG B   458                                                      
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     GLN A  45    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 238    CG   CD   CE   NZ                                   
REMARK 470     TYR A1011    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1021    CG   CD   CE   NZ                                   
REMARK 470     ARG A1043    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1061    CG   CD   CE   NZ                                   
REMARK 470     LYS A1062    CG   CD   CE   NZ                                   
REMARK 470     LYS A1074    CG   CD   CE   NZ                                   
REMARK 470     LYS A1094    CG   CD   CE   NZ                                   
REMARK 470     LEU A1171    CG   CD1  CD2                                       
REMARK 470     ASP A1180    CG   OD1  OD2                                       
REMARK 470     LYS A1189    CG   CD   CE   NZ                                   
REMARK 470     GLU A 410    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 238    CG   CD   CE   NZ                                   
REMARK 470     ARG B 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B1041    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B1043    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1053    CG   CD   CE   NZ                                   
REMARK 470     LYS B1062    CG   CD   CE   NZ                                   
REMARK 470     GLU B1078    CG   CD   OE1  OE2                                  
REMARK 470     LEU B1171    CG   CD1  CD2                                       
REMARK 470     PHE B 380    CG   CD1  CD2  CE1  CE2  CZ                         
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    ARG A  83       25.11    -78.01                                   
REMARK 500    VAL A 104      -58.41   -120.93                                   
REMARK 500    GLN A 155       40.47   -100.21                                   
REMARK 500    PHE A 184       70.10     38.91                                   
REMARK 500    ALA A 198      -76.02    -62.25                                   
REMARK 500    PHE A 219      -56.94   -138.39                                   
REMARK 500    ARG A 240       53.22    -97.17                                   
REMARK 500    ILE A1002      150.93    -46.46                                   
REMARK 500    SER A1010        9.40    -64.84                                   
REMARK 500    THR A1013      -54.25   -128.27                                   
REMARK 500    GLN A1045      -87.65   -127.69                                   
REMARK 500    ILE A1117       79.01   -117.64                                   
REMARK 500    PRO A1118       57.58    -93.15                                   
REMARK 500    ASP A1180       95.66    -67.68                                   
REMARK 500    ILE A 407      -75.17    -81.53                                   
REMARK 500    ARG A 409     -112.68     45.22                                   
REMARK 500    CYS A 412       52.70   -145.42                                   
REMARK 500    THR B  78      -49.05   -147.82                                   
REMARK 500    THR B 154      -81.45    -60.51                                   
REMARK 500    ARG B 163       92.13    -65.77                                   
REMARK 500    PHE B 219      -67.62   -126.21                                   
REMARK 500    PHE B1006      -61.18   -128.72                                   
REMARK 500    TRP B1007       80.14    -69.33                                   
REMARK 500    VAL B1033       98.97    -57.71                                   
REMARK 500    GLN B1045      -58.20    -16.27                                   
REMARK 500    SER B1111      -44.25   -149.40                                   
REMARK 500    PRO B1118       44.80    -91.84                                   
REMARK 500    PHE B1124      -60.48   -100.50                                   
REMARK 500    ILE B1149      -60.20    -99.22                                   
REMARK 500    THR B1151     -159.08   -115.05                                   
REMARK 500    ARG B 409     -123.17     50.46                                   
REMARK 500    CYS B 412       39.48   -148.20                                   
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     OLC A 1203                                                       
REMARK 610     OLC A 1204                                                       
REMARK 610     OLC A 1205                                                       
REMARK 610     OLC A 1206                                                       
REMARK 610     OLC A 1207                                                       
REMARK 610     OLC B 1203                                                       
REMARK 610     OLC B 1204                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E33 A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E33 B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 1204                
DBREF  6KUW A   29   458  PDB    6KUW     6KUW            29    458             
DBREF  6KUW B   29   458  PDB    6KUW     6KUW            29    458             
SEQRES   1 A  496  GLY GLY VAL ALA ASN ALA SER GLY ALA SER TRP GLY PRO          
SEQRES   2 A  496  PRO ARG GLY GLN TYR SER ALA GLY ALA VAL ALA GLY LEU          
SEQRES   3 A  496  ALA ALA VAL VAL GLY PHE LEU ILE VAL PHE THR VAL VAL          
SEQRES   4 A  496  GLY ASN VAL LEU VAL VAL ILE ALA VAL LEU THR SER ARG          
SEQRES   5 A  496  ALA LEU ARG ALA PRO GLN ASN LEU PHE LEU VAL SER LEU          
SEQRES   6 A  496  ALA SER ALA ASP ILE LEU VAL ALA THR LEU VAL MET PRO          
SEQRES   7 A  496  PHE SER LEU ALA ASN GLU LEU MET ALA TYR TRP TYR PHE          
SEQRES   8 A  496  GLY GLN TRP TRP CYS GLY VAL TYR LEU ALA LEU ASP VAL          
SEQRES   9 A  496  LEU PHE CYS THR SER SER ALA VAL HIS LEU CYS ALA ILE          
SEQRES  10 A  496  SER LEU ASP ARG TYR TRP SER VAL THR GLN ALA VAL GLU          
SEQRES  11 A  496  TYR ASN LEU LYS ARG THR PRO ARG ARG VAL LYS ALA THR          
SEQRES  12 A  496  ILE VAL ALA VAL TRP LEU ILE SER ALA VAL ILE SER PHE          
SEQRES  13 A  496  PRO PRO LEU VAL SER LEU TYR ARG GLN PRO ASP GLY ALA          
SEQRES  14 A  496  ALA TYR PRO GLN CYS GLY LEU ASN ASP GLU THR TRP TYR          
SEQRES  15 A  496  ILE LEU SER SER CYS ILE GLY SER PHE PHE ALA PRO CYS          
SEQRES  16 A  496  LEU ILE MET GLY LEU VAL TYR ALA ARG ILE TYR ARG VAL          
SEQRES  17 A  496  ALA LYS LEU ARG THR GLY ILE ASP CYS SER PHE TRP ASN          
SEQRES  18 A  496  GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS          
SEQRES  19 A  496  SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR          
SEQRES  20 A  496  PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY          
SEQRES  21 A  496  VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER          
SEQRES  22 A  496  LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY          
SEQRES  23 A  496  LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU          
SEQRES  24 A  496  GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET          
SEQRES  25 A  496  LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL          
SEQRES  26 A  496  ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY          
SEQRES  27 A  496  LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO          
SEQRES  28 A  496  ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR          
SEQRES  29 A  496  ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY          
SEQRES  30 A  496  GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER          
SEQRES  31 A  496  ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS          
SEQRES  32 A  496  ARG ALA MET SER PHE SER VAL ALA GLN ALA ARG GLU LYS          
SEQRES  33 A  496  ARG PHE THR PHE VAL LEU ALA VAL VAL MET GLY VAL TRP          
SEQRES  34 A  496  VAL LEU CYS TRP PHE PRO PHE PHE PHE SER TYR SER LEU          
SEQRES  35 A  496  TYR GLY ILE CYS ARG GLU ALA CYS GLN VAL PRO GLY PRO          
SEQRES  36 A  496  LEU PHE LYS PHE PHE PHE TRP ILE GLY TYR CYS ASN SER          
SEQRES  37 A  496  SER LEU ASN PRO VAL ILE TYR THR VAL PHE ASN GLN ASP          
SEQRES  38 A  496  PHE ARG ARG SER PHE LYS HIS ILE LEU PHE ARG ARG ARG          
SEQRES  39 A  496  ARG ARG                                                      
SEQRES   1 B  496  GLY GLY VAL ALA ASN ALA SER GLY ALA SER TRP GLY PRO          
SEQRES   2 B  496  PRO ARG GLY GLN TYR SER ALA GLY ALA VAL ALA GLY LEU          
SEQRES   3 B  496  ALA ALA VAL VAL GLY PHE LEU ILE VAL PHE THR VAL VAL          
SEQRES   4 B  496  GLY ASN VAL LEU VAL VAL ILE ALA VAL LEU THR SER ARG          
SEQRES   5 B  496  ALA LEU ARG ALA PRO GLN ASN LEU PHE LEU VAL SER LEU          
SEQRES   6 B  496  ALA SER ALA ASP ILE LEU VAL ALA THR LEU VAL MET PRO          
SEQRES   7 B  496  PHE SER LEU ALA ASN GLU LEU MET ALA TYR TRP TYR PHE          
SEQRES   8 B  496  GLY GLN TRP TRP CYS GLY VAL TYR LEU ALA LEU ASP VAL          
SEQRES   9 B  496  LEU PHE CYS THR SER SER ALA VAL HIS LEU CYS ALA ILE          
SEQRES  10 B  496  SER LEU ASP ARG TYR TRP SER VAL THR GLN ALA VAL GLU          
SEQRES  11 B  496  TYR ASN LEU LYS ARG THR PRO ARG ARG VAL LYS ALA THR          
SEQRES  12 B  496  ILE VAL ALA VAL TRP LEU ILE SER ALA VAL ILE SER PHE          
SEQRES  13 B  496  PRO PRO LEU VAL SER LEU TYR ARG GLN PRO ASP GLY ALA          
SEQRES  14 B  496  ALA TYR PRO GLN CYS GLY LEU ASN ASP GLU THR TRP TYR          
SEQRES  15 B  496  ILE LEU SER SER CYS ILE GLY SER PHE PHE ALA PRO CYS          
SEQRES  16 B  496  LEU ILE MET GLY LEU VAL TYR ALA ARG ILE TYR ARG VAL          
SEQRES  17 B  496  ALA LYS LEU ARG THR GLY ILE ASP CYS SER PHE TRP ASN          
SEQRES  18 B  496  GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS          
SEQRES  19 B  496  SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR          
SEQRES  20 B  496  PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY          
SEQRES  21 B  496  VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER          
SEQRES  22 B  496  LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY          
SEQRES  23 B  496  LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU          
SEQRES  24 B  496  GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET          
SEQRES  25 B  496  LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL          
SEQRES  26 B  496  ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY          
SEQRES  27 B  496  LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO          
SEQRES  28 B  496  ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR          
SEQRES  29 B  496  ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY          
SEQRES  30 B  496  GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER          
SEQRES  31 B  496  ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS          
SEQRES  32 B  496  ARG ALA MET SER PHE SER VAL ALA GLN ALA ARG GLU LYS          
SEQRES  33 B  496  ARG PHE THR PHE VAL LEU ALA VAL VAL MET GLY VAL TRP          
SEQRES  34 B  496  VAL LEU CYS TRP PHE PRO PHE PHE PHE SER TYR SER LEU          
SEQRES  35 B  496  TYR GLY ILE CYS ARG GLU ALA CYS GLN VAL PRO GLY PRO          
SEQRES  36 B  496  LEU PHE LYS PHE PHE PHE TRP ILE GLY TYR CYS ASN SER          
SEQRES  37 B  496  SER LEU ASN PRO VAL ILE TYR THR VAL PHE ASN GLN ASP          
SEQRES  38 B  496  PHE ARG ARG SER PHE LYS HIS ILE LEU PHE ARG ARG ARG          
SEQRES  39 B  496  ARG ARG                                                      
HET    E33  A1201      25                                                       
HET    CLR  A1202      28                                                       
HET    OLC  A1203      11                                                       
HET    OLC  A1204      22                                                       
HET    OLC  A1205      13                                                       
HET    OLC  A1206      13                                                       
HET    OLC  A1207      18                                                       
HET    OLA  A1208      20                                                       
HET    OLA  A1209      20                                                       
HET    E33  B1201      25                                                       
HET    CLR  B1202      28                                                       
HET    OLC  B1203      12                                                       
HET    OLC  B1204       8                                                       
HETNAM     E33 (8~{A}~{R},12~{A}~{S},13~{A}~{R})-12-ETHYLSULFONYL-3-            
HETNAM   2 E33  METHOXY-5,6,8,8~{A},9,10,11,12~{A},13,13~{A}-                   
HETNAM   3 E33  DECAHYDROISOQUINOLINO[2,1-G][1,6]NAPHTHYRIDINE                  
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLA OLEIC ACID                                                       
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  E33    2(C19 H28 N2 O3 S)                                           
FORMUL   4  CLR    2(C27 H46 O)                                                 
FORMUL   5  OLC    7(C21 H40 O4)                                                
FORMUL  10  OLA    2(C18 H34 O2)                                                
FORMUL  16  HOH   *2(H2 O)                                                      
HELIX    1 AA1 SER A   47  SER A   79  1                                  33    
HELIX    2 AA2 ARG A   80  ARG A   83  5                                   4    
HELIX    3 AA3 ALA A   84  GLN A   86  5                                   3    
HELIX    4 AA4 ASN A   87  VAL A  104  1                                  18    
HELIX    5 AA5 VAL A  104  ALA A  115  1                                  12    
HELIX    6 AA6 PHE A  119  GLN A  155  1                                  37    
HELIX    7 AA7 GLN A  155  LEU A  161  1                                   7    
HELIX    8 AA8 THR A  164  PHE A  184  1                                  21    
HELIX    9 AA9 GLU A  207  PHE A  219  1                                  13    
HELIX   10 AB1 PHE A  219  ARG A  240  1                                  22    
HELIX   11 AB2 SER A 1015  GLY A 1028  1                                  14    
HELIX   12 AB3 GLY A 1047  SER A 1060  1                                  14    
HELIX   13 AB4 LYS A 1061  GLN A 1065  5                                   5    
HELIX   14 AB5 ASP A 1076  HIS A 1090  1                                  15    
HELIX   15 AB6 SER A 1101  GLY A 1110  1                                  10    
HELIX   16 AB7 GLY A 1125  GLY A 1135  1                                  11    
HELIX   17 AB8 GLY A 1144  ILE A 1150  1                                   7    
HELIX   18 AB9 ASP A 1162  ARG A 1178  1                                  17    
HELIX   19 AC1 LEU A 1181  ARG A  409  1                                  54    
HELIX   20 AC2 GLU A  410  GLN A  413  5                                   4    
HELIX   21 AC3 PRO A  415  ASN A  429  1                                  15    
HELIX   22 AC4 LEU A  432  ASN A  441  1                                  10    
HELIX   23 AC5 ASN A  441  PHE A  453  1                                  13    
HELIX   24 AC6 SER B   47  LEU B   77  1                                  31    
HELIX   25 AC7 ALA B   84  GLN B   86  5                                   3    
HELIX   26 AC8 ASN B   87  VAL B  104  1                                  18    
HELIX   27 AC9 VAL B  104  ALA B  115  1                                  12    
HELIX   28 AD1 PHE B  119  GLN B  155  1                                  37    
HELIX   29 AD2 VAL B  157  LYS B  162  1                                   6    
HELIX   30 AD3 THR B  164  PHE B  184  1                                  21    
HELIX   31 AD4 GLU B  207  PHE B  219  1                                  13    
HELIX   32 AD5 PHE B  219  LYS B  238  1                                  20    
HELIX   33 AD6 ASN B 1008  LEU B 1012  5                                   5    
HELIX   34 AD7 SER B 1015  PHE B 1027  1                                  13    
HELIX   35 AD8 GLY B 1047  SER B 1059  1                                  13    
HELIX   36 AD9 ASP B 1076  HIS B 1090  1                                  15    
HELIX   37 AE1 SER B 1101  GLY B 1110  1                                  10    
HELIX   38 AE2 GLY B 1125  LEU B 1134  1                                  10    
HELIX   39 AE3 GLY B 1145  ILE B 1150  1                                   6    
HELIX   40 AE4 ASP B 1162  ARG B 1178  1                                  17    
HELIX   41 AE5 LEU B 1181  ARG B  409  1                                  54    
HELIX   42 AE6 GLU B  410  CYS B  412  5                                   3    
HELIX   43 AE7 PRO B  415  ASN B  441  1                                  27    
HELIX   44 AE8 ASN B  441  PHE B  453  1                                  13    
SHEET    1 AA1 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA1 6 MET A1067  ILE A1072  1  N  PHE A1069   O  LYS A1094           
SHEET    3 AA1 6 VAL A1033  PHE A1037  1  N  VAL A1033   O  ARG A1068           
SHEET    4 AA1 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5 AA1 6 ILE A1137  SER A1141  1  O  ILE A1139   N  ILE A1117           
SHEET    6 AA1 6 ILE A1156  VAL A1158  1  O  VAL A1158   N  ALA A1140           
SHEET    1 AA2 6 VAL B1093  ILE B1096  0                                        
SHEET    2 AA2 6 ARG B1068  ILE B1072  1  N  ILE B1071   O  ILE B1096           
SHEET    3 AA2 6 THR B1034  PHE B1037  1  N  PHE B1035   O  ARG B1068           
SHEET    4 AA2 6 PHE B1114  ILE B1117  1  O  ILE B1116   N  MET B1036           
SHEET    5 AA2 6 ILE B1137  SER B1141  1  O  ILE B1139   N  ILE B1117           
SHEET    6 AA2 6 ILE B1156  VAL B1158  1  O  ILE B1156   N  PRO B1138           
SSBOND   1 CYS A  124    CYS A  202                          1555   1555  2.04  
SSBOND   2 CYS A  408    CYS A  412                          1555   1555  2.04  
SSBOND   3 CYS B  124    CYS B  202                          1555   1555  2.04  
SSBOND   4 CYS B  408    CYS B  412                          1555   1555  2.04  
SITE     1 AC1 14 TYR A 127  ASP A 131  VAL A 132  CYS A 135                    
SITE     2 AC1 14 LEU A 204  SER A 214  SER A 218  TRP A 395                    
SITE     3 AC1 14 PHE A 398  PHE A 399  TYR A 402  PHE A 419                    
SITE     4 AC1 14 PHE A 423  TYR A 427                                          
SITE     1 AC2  6 TYR A  46  VAL A  58  PHE A  64  PHE A 421                    
SITE     2 AC2  6 SER A 431  OLC A1207                                          
SITE     1 AC3  5 TRP A 151  GLN A 155  GLU A 158  TYR A 159                    
SITE     2 AC3  5 LYS A 162                                                     
SITE     1 AC4  4 VAL A 140  CYS A 143  ILE A 182  ILE A 225                    
SITE     1 AC5  4 LEU A  88  VAL A  91  LYS A 169  TRP B 209                    
SITE     1 AC6  7 GLN A  45  TYR A  46  CLR A1202  OLA A1208                    
SITE     2 AC6  7 GLN B 413  VAL B 414  PRO B 415                               
SITE     1 AC7  9 GLY A  49  ALA A  50  GLY A  53  VAL A  57                    
SITE     2 AC7  9 ALA A 170  VAL A 173  LEU A 177  OLC A1207                    
SITE     3 AC7  9 LEU B 404                                                     
SITE     1 AC8  4 PHE A 400  SER A 401  GLN A 413  GLN B  45                    
SITE     1 AC9 15 TYR B 127  LEU B 128  ASP B 131  VAL B 132                    
SITE     2 AC9 15 CYS B 135  LEU B 204  SER B 214  SER B 218                    
SITE     3 AC9 15 TRP B 395  PHE B 398  PHE B 399  TYR B 402                    
SITE     4 AC9 15 PHE B 419  PHE B 423  TYR B 427                               
SITE     1 AD1  6 LEU A 418  TYR B  46  PHE B  60  PHE B 421                    
SITE     2 AD1  6 TRP B 424  CYS B 428                                          
SITE     1 AD2  3 TYR B 234  PHE B 382  ALA B 385                               
SITE     1 AD3  2 CYS B 223  ALA B 385                                          
CRYST1   74.480   78.740  190.450  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013426  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012700  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005251        0.00000                         
ATOM      1  N   PRO A  41     -40.697  -4.060  76.946  1.00115.79           N  
ANISOU    1  N   PRO A  41    16852  16067  11075    588    925  -1325       N  
ATOM      2  CA  PRO A  41     -40.242  -3.977  75.547  1.00112.92           C  
ANISOU    2  CA  PRO A  41    16414  15537  10953    623    798  -1256       C  
ATOM      3  C   PRO A  41     -38.719  -4.074  75.398  1.00112.18           C  
ANISOU    3  C   PRO A  41    16522  15124  10978    535    606  -1128       C  
ATOM      4  O   PRO A  41     -37.989  -3.559  76.250  1.00112.48           O  
ANISOU    4  O   PRO A  41    16775  15024  10939    562    520  -1146       O  
ATOM      5  CB  PRO A  41     -40.807  -2.640  75.059  1.00115.72           C  
ANISOU    5  CB  PRO A  41    16707  15916  11346    921    772  -1414       C  
ATOM      6  CG  PRO A  41     -40.935  -1.805  76.304  1.00122.70           C  
ANISOU    6  CG  PRO A  41    17751  16830  12038   1059    799  -1548       C  
ATOM      7  CD  PRO A  41     -41.017  -2.732  77.506  1.00119.33           C  
ANISOU    7  CD  PRO A  41    17376  16541  11422    849    923  -1502       C  
ATOM      8  N   PRO A  42     -38.208  -4.734  74.336  1.00104.08           N  
ANISOU    8  N   PRO A  42    15425  13990  10130    429    536  -1004       N  
ATOM      9  CA  PRO A  42     -36.748  -4.855  74.189  1.00101.10           C  
ANISOU    9  CA  PRO A  42    15206  13348   9861    352    361   -894       C  
ATOM     10  C   PRO A  42     -36.115  -3.617  73.595  1.00100.68           C  
ANISOU   10  C   PRO A  42    15223  13106   9925    504    217   -942       C  
ATOM     11  O   PRO A  42     -36.670  -3.051  72.651  1.00 99.85           O  
ANISOU   11  O   PRO A  42    15002  13028   9908    630    227   -997       O  
ATOM     12  CB  PRO A  42     -36.566  -6.066  73.264  1.00101.41           C  
ANISOU   12  CB  PRO A  42    15130  13374  10029    194    362   -762       C  
ATOM     13  CG  PRO A  42     -37.922  -6.449  72.808  1.00106.96           C  
ANISOU   13  CG  PRO A  42    15618  14314  10707    187    522   -803       C  
ATOM     14  CD  PRO A  42     -38.910  -5.415  73.236  1.00104.63           C  
ANISOU   14  CD  PRO A  42    15267  14185  10304    373    610   -966       C  
ATOM     15  N   ARG A  43     -34.945  -3.212  74.139  1.00 95.09           N  
ANISOU   15  N   ARG A  43    14712  12208   9211    479     74   -918       N  
ATOM     16  CA  ARG A  43     -34.187  -2.049  73.673  1.00 93.71           C  
ANISOU   16  CA  ARG A  43    14643  11836   9128    570    -76   -951       C  
ATOM     17  C   ARG A  43     -33.740  -2.267  72.233  1.00 94.42           C  
ANISOU   17  C   ARG A  43    14614  11840   9421    525   -136   -868       C  
ATOM     18  O   ARG A  43     -33.177  -3.321  71.905  1.00 93.90           O  
ANISOU   18  O   ARG A  43    14481  11761   9433    381   -151   -754       O  
ATOM     19  CB  ARG A  43     -32.988  -1.716  74.591  1.00 93.87           C  
ANISOU   19  CB  ARG A  43    14879  11694   9091    507   -217   -934       C  
ATOM     20  CG  ARG A  43     -31.840  -2.728  74.550  1.00103.88           C  
ANISOU   20  CG  ARG A  43    16144  12888  10437    330   -307   -797       C  
ATOM     21  CD  ARG A  43     -30.555  -2.175  75.129  1.00118.23           C  
ANISOU   21  CD  ARG A  43    18138  14543  12243    284   -481   -791       C  
ATOM     22  NE  ARG A  43     -30.520  -2.274  76.590  1.00130.85           N  
ANISOU   22  NE  ARG A  43    19899  16167  13651    265   -484   -820       N  
ATOM     23  CZ  ARG A  43     -30.083  -3.335  77.263  1.00146.87           C  
ANISOU   23  CZ  ARG A  43    21964  18221  15620    151   -504   -735       C  
ATOM     24  NH1 ARG A  43     -29.651  -4.411  76.615  1.00131.02           N  
ANISOU   24  NH1 ARG A  43    19840  16212  13730     60   -524   -622       N  
ATOM     25  NH2 ARG A  43     -30.085  -3.332  78.590  1.00137.86           N  
ANISOU   25  NH2 ARG A  43    20993  17098  14289    137   -510   -766       N  
ATOM     26  N   GLY A  44     -34.079  -1.305  71.382  1.00 87.57           N  
ANISOU   26  N   GLY A  44    13729  10922   8620    660   -164   -932       N  
ATOM     27  CA  GLY A  44     -33.728  -1.344  69.974  1.00 84.14           C  
ANISOU   27  CA  GLY A  44    13203  10407   8360    629   -217   -866       C  
ATOM     28  C   GLY A  44     -32.325  -0.823  69.786  1.00 83.34           C  
ANISOU   28  C   GLY A  44    13238  10097   8332    546   -377   -818       C  
ATOM     29  O   GLY A  44     -31.879   0.042  70.545  1.00 82.25           O  
ANISOU   29  O   GLY A  44    13284   9855   8114    575   -460   -875       O  
ATOM     30  N   GLN A  45     -31.614  -1.359  68.786  1.00 76.86           N  
ANISOU   30  N   GLN A  45    12322   9225   7655    434   -418   -720       N  
ATOM     31  CA  GLN A  45     -30.255  -0.920  68.457  1.00 74.86           C  
ANISOU   31  CA  GLN A  45    12152   8813   7481    332   -558   -675       C  
ATOM     32  C   GLN A  45     -30.250   0.314  67.519  1.00 73.05           C  
ANISOU   32  C   GLN A  45    12004   8454   7300    392   -623   -714       C  
ATOM     33  O   GLN A  45     -29.185   0.899  67.287  1.00 72.65           O  
ANISOU   33  O   GLN A  45    12048   8269   7288    293   -738   -691       O  
ATOM     34  CB  GLN A  45     -29.478  -2.078  67.818  1.00 75.03           C  
ANISOU   34  CB  GLN A  45    12028   8858   7620    196   -565   -564       C  
ATOM     35  N   TYR A  46     -31.447   0.710  67.005  1.00 64.51           N  
ANISOU   35  N   TYR A  46    10890   7418   6203    549   -556   -775       N  
ATOM     36  CA  TYR A  46     -31.619   1.788  66.037  1.00 61.94           C  
ANISOU   36  CA  TYR A  46    10654   6968   5912    630   -619   -809       C  
ATOM     37  C   TYR A  46     -32.290   3.040  66.543  1.00 63.62           C  
ANISOU   37  C   TYR A  46    11060   7107   6007    821   -658   -933       C  
ATOM     38  O   TYR A  46     -33.404   2.991  67.076  1.00 65.34           O  
ANISOU   38  O   TYR A  46    11226   7461   6141    986   -570  -1019       O  
ATOM     39  CB  TYR A  46     -32.386   1.290  64.808  1.00 60.97           C  
ANISOU   39  CB  TYR A  46    10353   6936   5878    678   -546   -779       C  
ATOM     40  CG  TYR A  46     -31.662   0.206  64.062  1.00 59.59           C  
ANISOU   40  CG  TYR A  46    10024   6793   5824    503   -526   -662       C  
ATOM     41  CD1 TYR A  46     -30.728   0.515  63.084  1.00 60.81           C  
ANISOU   41  CD1 TYR A  46    10213   6825   6066    392   -603   -602       C  
ATOM     42  CD2 TYR A  46     -31.887  -1.135  64.353  1.00 59.49           C  
ANISOU   42  CD2 TYR A  46     9846   6933   5825    445   -432   -616       C  
ATOM     43  CE1 TYR A  46     -30.039  -0.484  62.405  1.00 61.69           C  
ANISOU   43  CE1 TYR A  46    10178   6980   6281    252   -581   -510       C  
ATOM     44  CE2 TYR A  46     -31.193  -2.141  63.695  1.00 59.17           C  
ANISOU   44  CE2 TYR A  46     9688   6907   5886    308   -425   -520       C  
ATOM     45  CZ  TYR A  46     -30.274  -1.811  62.716  1.00 67.89           C  
ANISOU   45  CZ  TYR A  46    10809   7903   7082    225   -497   -473       C  
ATOM     46  OH  TYR A  46     -29.594  -2.797  62.055  1.00 70.59           O  
ANISOU   46  OH  TYR A  46    11029   8274   7518    112   -485   -393       O  
ATOM     47  N   SER A  47     -31.650   4.175  66.278  1.00 55.08           N  
ANISOU   47  N   SER A  47    10198   5813   4915    801   -788   -947       N  
ATOM     48  CA  SER A  47     -32.179   5.482  66.608  1.00 55.27           C  
ANISOU   48  CA  SER A  47    10460   5711   4827    989   -857  -1065       C  
ATOM     49  C   SER A  47     -33.248   5.862  65.566  1.00 59.69           C  
ANISOU   49  C   SER A  47    10985   6283   5411   1186   -841  -1108       C  
ATOM     50  O   SER A  47     -33.246   5.313  64.456  1.00 59.10           O  
ANISOU   50  O   SER A  47    10755   6251   5448   1115   -812  -1026       O  
ATOM     51  CB  SER A  47     -31.046   6.503  66.594  1.00 58.49           C  
ANISOU   51  CB  SER A  47    11139   5870   5216    856  -1016  -1050       C  
ATOM     52  OG  SER A  47     -30.305   6.396  65.390  1.00 67.71           O  
ANISOU   52  OG  SER A  47    12261   6966   6501    680  -1056   -944       O  
ATOM     53  N   ALA A  48     -34.138   6.827  65.911  1.00 56.16           N  
ANISOU   53  N   ALA A  48    10692   5794   4852   1445   -871  -1242       N  
ATOM     54  CA  ALA A  48     -35.201   7.347  65.049  1.00 55.96           C  
ANISOU   54  CA  ALA A  48    10664   5772   4825   1684   -885  -1308       C  
ATOM     55  C   ALA A  48     -34.715   7.696  63.626  1.00 61.98           C  
ANISOU   55  C   ALA A  48    11510   6358   5680   1588   -982  -1216       C  
ATOM     56  O   ALA A  48     -35.394   7.367  62.650  1.00 61.38           O  
ANISOU   56  O   ALA A  48    11278   6374   5668   1668   -946  -1198       O  
ATOM     57  CB  ALA A  48     -35.844   8.552  65.693  1.00 58.40           C  
ANISOU   57  CB  ALA A  48    11215   5985   4988   1962   -955  -1467       C  
ATOM     58  N   GLY A  49     -33.541   8.323  63.538  1.00 59.49           N  
ANISOU   58  N   GLY A  49    11434   5808   5363   1398  -1099  -1157       N  
ATOM     59  CA  GLY A  49     -32.895   8.704  62.285  1.00 58.90           C  
ANISOU   59  CA  GLY A  49    11470   5556   5352   1250  -1188  -1063       C  
ATOM     60  C   GLY A  49     -32.525   7.508  61.438  1.00 60.55           C  
ANISOU   60  C   GLY A  49    11391   5914   5702   1060  -1095   -939       C  
ATOM     61  O   GLY A  49     -32.822   7.493  60.240  1.00 60.49           O  
ANISOU   61  O   GLY A  49    11347   5890   5747   1080  -1103   -897       O  
ATOM     62  N   ALA A  50     -31.903   6.485  62.066  1.00 55.46           N  
ANISOU   62  N   ALA A  50    10553   5413   5107    890  -1013   -886       N  
ATOM     63  CA  ALA A  50     -31.535   5.227  61.400  1.00 53.06           C  
ANISOU   63  CA  ALA A  50     9976   5257   4928    727   -922   -779       C  
ATOM     64  C   ALA A  50     -32.780   4.476  60.901  1.00 55.84           C  
ANISOU   64  C   ALA A  50    10101   5798   5318    885   -816   -797       C  
ATOM     65  O   ALA A  50     -32.770   3.982  59.784  1.00 56.01           O  
ANISOU   65  O   ALA A  50    10004   5853   5425    820   -791   -728       O  
ATOM     66  CB  ALA A  50     -30.734   4.343  62.341  1.00 52.67           C  
ANISOU   66  CB  ALA A  50     9804   5309   4899    567   -876   -740       C  
ATOM     67  N   VAL A  51     -33.851   4.422  61.715  1.00 50.95           N  
ANISOU   67  N   VAL A  51     9423   5311   4626   1085   -756   -896       N  
ATOM     68  CA  VAL A  51     -35.121   3.778  61.373  1.00 49.17           C  
ANISOU   68  CA  VAL A  51     8970   5296   4416   1232   -655   -932       C  
ATOM     69  C   VAL A  51     -35.724   4.445  60.117  1.00 51.52           C  
ANISOU   69  C   VAL A  51     9326   5517   4733   1373   -726   -950       C  
ATOM     70  O   VAL A  51     -35.968   3.756  59.136  1.00 51.10           O  
ANISOU   70  O   VAL A  51     9104   5550   4761   1324   -685   -890       O  
ATOM     71  CB  VAL A  51     -36.111   3.773  62.580  1.00 53.53           C  
ANISOU   71  CB  VAL A  51     9464   6016   4859   1414   -578  -1053       C  
ATOM     72  CG1 VAL A  51     -37.492   3.245  62.183  1.00 52.73           C  
ANISOU   72  CG1 VAL A  51     9117   6155   4762   1565   -481  -1107       C  
ATOM     73  CG2 VAL A  51     -35.546   2.962  63.739  1.00 52.91           C  
ANISOU   73  CG2 VAL A  51     9326   6021   4755   1255   -505  -1019       C  
ATOM     74  N   ALA A  52     -35.932   5.767  60.144  1.00 47.73           N  
ANISOU   74  N   ALA A  52     9105   4861   4170   1546   -843  -1029       N  
ATOM     75  CA  ALA A  52     -36.505   6.549  59.052  1.00 47.94           C  
ANISOU   75  CA  ALA A  52     9249   4778   4186   1712   -941  -1055       C  
ATOM     76  C   ALA A  52     -35.663   6.415  57.785  1.00 52.68           C  
ANISOU   76  C   ALA A  52     9894   5248   4872   1495   -985   -922       C  
ATOM     77  O   ALA A  52     -36.215   6.243  56.696  1.00 51.53           O  
ANISOU   77  O   ALA A  52     9669   5143   4768   1556   -993   -900       O  
ATOM     78  CB  ALA A  52     -36.610   7.997  59.467  1.00 50.62           C  
ANISOU   78  CB  ALA A  52     9928   4899   4406   1902  -1077  -1154       C  
ATOM     79  N   GLY A  53     -34.339   6.402  57.963  1.00 50.06           N  
ANISOU   79  N   GLY A  53     9660   4796   4565   1234  -1004   -838       N  
ATOM     80  CA  GLY A  53     -33.366   6.270  56.886  1.00 49.05           C  
ANISOU   80  CA  GLY A  53     9565   4566   4505    994  -1030   -718       C  
ATOM     81  C   GLY A  53     -33.439   4.924  56.214  1.00 52.52           C  
ANISOU   81  C   GLY A  53     9698   5202   5054    896   -914   -645       C  
ATOM     82  O   GLY A  53     -33.607   4.851  54.996  1.00 51.17           O  
ANISOU   82  O   GLY A  53     9511   5011   4919    881   -928   -597       O  
ATOM     83  N   LEU A  54     -33.342   3.845  57.028  1.00 49.51           N  
ANISOU   83  N   LEU A  54     9095   5003   4714    832   -806   -638       N  
ATOM     84  CA  LEU A  54     -33.417   2.458  56.591  1.00 47.66           C  
ANISOU   84  CA  LEU A  54     8588   4951   4571    739   -696   -576       C  
ATOM     85  C   LEU A  54     -34.780   2.087  55.984  1.00 51.89           C  
ANISOU   85  C   LEU A  54     8971   5631   5115    909   -652   -615       C  
ATOM     86  O   LEU A  54     -34.810   1.502  54.902  1.00 51.72           O  
ANISOU   86  O   LEU A  54     8846   5648   5158    841   -628   -554       O  
ATOM     87  CB  LEU A  54     -33.013   1.517  57.716  1.00 46.93           C  
ANISOU   87  CB  LEU A  54     8360   4981   4491    645   -616   -564       C  
ATOM     88  CG  LEU A  54     -31.506   1.420  57.930  1.00 51.16           C  
ANISOU   88  CG  LEU A  54     8949   5430   5060    427   -649   -496       C  
ATOM     89  CD1 LEU A  54     -31.180   0.677  59.216  1.00 49.92           C  
ANISOU   89  CD1 LEU A  54     8709   5370   4888    378   -602   -500       C  
ATOM     90  CD2 LEU A  54     -30.815   0.764  56.719  1.00 52.98           C  
ANISOU   90  CD2 LEU A  54     9075   5671   5385    269   -626   -405       C  
ATOM     91  N   ALA A  55     -35.897   2.485  56.625  1.00 48.11           N  
ANISOU   91  N   ALA A  55     8480   5236   4564   1134   -648   -723       N  
ATOM     92  CA  ALA A  55     -37.239   2.252  56.092  1.00 47.80           C  
ANISOU   92  CA  ALA A  55     8280   5359   4522   1310   -619   -779       C  
ATOM     93  C   ALA A  55     -37.411   2.964  54.731  1.00 52.47           C  
ANISOU   93  C   ALA A  55     8999   5814   5122   1386   -728   -762       C  
ATOM     94  O   ALA A  55     -38.091   2.422  53.865  1.00 50.78           O  
ANISOU   94  O   ALA A  55     8627   5719   4947   1418   -705   -750       O  
ATOM     95  CB  ALA A  55     -38.293   2.726  57.077  1.00 49.93           C  
ANISOU   95  CB  ALA A  55     8525   5747   4698   1550   -603   -916       C  
ATOM     96  N   ALA A  56     -36.768   4.154  54.537  1.00 50.09           N  
ANISOU   96  N   ALA A  56     9001   5257   4774   1393   -851   -754       N  
ATOM     97  CA  ALA A  56     -36.802   4.924  53.280  1.00 49.50           C  
ANISOU   97  CA  ALA A  56     9116   5010   4684   1439   -970   -725       C  
ATOM     98  C   ALA A  56     -36.046   4.223  52.120  1.00 54.92           C  
ANISOU   98  C   ALA A  56     9738   5677   5450   1195   -936   -598       C  
ATOM     99  O   ALA A  56     -36.623   4.074  51.054  1.00 55.27           O  
ANISOU   99  O   ALA A  56     9736   5755   5510   1254   -959   -582       O  
ATOM    100  CB  ALA A  56     -36.250   6.313  53.497  1.00 50.61           C  
ANISOU  100  CB  ALA A  56     9621   4872   4736   1467  -1104   -743       C  
ATOM    101  N   VAL A  57     -34.779   3.779  52.326  1.00 51.75           N  
ANISOU  101  N   VAL A  57     9327   5241   5096    934   -883   -517       N  
ATOM    102  CA  VAL A  57     -33.965   3.086  51.309  1.00 49.88           C  
ANISOU  102  CA  VAL A  57     9016   5007   4928    708   -838   -411       C  
ATOM    103  C   VAL A  57     -34.576   1.734  50.971  1.00 53.04           C  
ANISOU  103  C   VAL A  57     9125   5626   5402    712   -732   -398       C  
ATOM    104  O   VAL A  57     -34.761   1.463  49.802  1.00 53.47           O  
ANISOU  104  O   VAL A  57     9149   5689   5479    687   -736   -357       O  
ATOM    105  CB  VAL A  57     -32.450   3.013  51.636  1.00 53.04           C  
ANISOU  105  CB  VAL A  57     9463   5336   5352    452   -817   -346       C  
ATOM    106  CG1 VAL A  57     -31.950   4.371  52.113  1.00 54.57           C  
ANISOU  106  CG1 VAL A  57     9955   5320   5460    438   -927   -369       C  
ATOM    107  CG2 VAL A  57     -32.124   1.945  52.670  1.00 51.78           C  
ANISOU  107  CG2 VAL A  57     9089   5337   5248    387   -718   -348       C  
ATOM    108  N   VAL A  58     -34.973   0.935  51.977  1.00 49.86           N  
ANISOU  108  N   VAL A  58     8532   5393   5019    746   -646   -437       N  
ATOM    109  CA  VAL A  58     -35.653  -0.339  51.773  1.00 49.86           C  
ANISOU  109  CA  VAL A  58     8277   5596   5070    739   -551   -431       C  
ATOM    110  C   VAL A  58     -37.028  -0.068  51.098  1.00 56.38           C  
ANISOU  110  C   VAL A  58     9053   6501   5867    936   -592   -491       C  
ATOM    111  O   VAL A  58     -37.399  -0.770  50.163  1.00 57.06           O  
ANISOU  111  O   VAL A  58     9019   6670   5992    899   -568   -459       O  
ATOM    112  CB  VAL A  58     -35.754  -1.180  53.083  1.00 53.72           C  
ANISOU  112  CB  VAL A  58     8617   6232   5561    710   -457   -455       C  
ATOM    113  CG1 VAL A  58     -36.562  -2.470  52.880  1.00 52.39           C  
ANISOU  113  CG1 VAL A  58     8215   6266   5426    685   -364   -450       C  
ATOM    114  CG2 VAL A  58     -34.364  -1.492  53.648  1.00 52.71           C  
ANISOU  114  CG2 VAL A  58     8535   6030   5463    529   -439   -395       C  
ATOM    115  N   GLY A  59     -37.724   0.973  51.536  1.00 54.24           N  
ANISOU  115  N   GLY A  59     8885   6199   5524   1151   -665   -581       N  
ATOM    116  CA  GLY A  59     -39.000   1.380  50.957  1.00 55.32           C  
ANISOU  116  CA  GLY A  59     8983   6412   5625   1379   -729   -654       C  
ATOM    117  C   GLY A  59     -38.809   1.656  49.492  1.00 59.89           C  
ANISOU  117  C   GLY A  59     9682   6860   6215   1345   -814   -590       C  
ATOM    118  O   GLY A  59     -39.521   1.103  48.648  1.00 59.68           O  
ANISOU  118  O   GLY A  59     9509   6954   6211   1375   -810   -587       O  
ATOM    119  N   PHE A  60     -37.761   2.440  49.188  1.00 57.54           N  
ANISOU  119  N   PHE A  60     9649   6318   5894   1245   -883   -530       N  
ATOM    120  CA  PHE A  60     -37.351   2.758  47.826  1.00 57.15           C  
ANISOU  120  CA  PHE A  60     9759   6120   5836   1162   -955   -453       C  
ATOM    121  C   PHE A  60     -37.078   1.454  47.056  1.00 58.33           C  
ANISOU  121  C   PHE A  60     9705   6394   6065    974   -853   -378       C  
ATOM    122  O   PHE A  60     -37.655   1.264  45.985  1.00 58.95           O  
ANISOU  122  O   PHE A  60     9752   6506   6140   1018   -889   -366       O  
ATOM    123  CB  PHE A  60     -36.128   3.711  47.790  1.00 59.20           C  
ANISOU  123  CB  PHE A  60    10321   6122   6051   1017  -1018   -396       C  
ATOM    124  CG  PHE A  60     -35.590   3.873  46.390  1.00 61.27           C  
ANISOU  124  CG  PHE A  60    10726   6258   6295    872  -1058   -305       C  
ATOM    125  CD1 PHE A  60     -36.349   4.499  45.402  1.00 65.02           C  
ANISOU  125  CD1 PHE A  60    11352   6646   6705   1026  -1178   -314       C  
ATOM    126  CD2 PHE A  60     -34.375   3.305  46.027  1.00 62.94           C  
ANISOU  126  CD2 PHE A  60    10899   6463   6551    591   -972   -216       C  
ATOM    127  CE1 PHE A  60     -35.902   4.552  44.086  1.00 65.85           C  
ANISOU  127  CE1 PHE A  60    11584   6652   6782    881  -1205   -227       C  
ATOM    128  CE2 PHE A  60     -33.926   3.361  44.702  1.00 65.21           C  
ANISOU  128  CE2 PHE A  60    11294   6671   6814    451   -988   -138       C  
ATOM    129  CZ  PHE A  60     -34.692   3.984  43.745  1.00 64.08           C  
ANISOU  129  CZ  PHE A  60    11317   6432   6598    587  -1101   -140       C  
ATOM    130  N   LEU A  61     -36.250   0.549  47.633  1.00 52.33           N  
ANISOU  130  N   LEU A  61     8814   5701   5367    785   -738   -336       N  
ATOM    131  CA  LEU A  61     -35.897  -0.743  47.043  1.00 50.66           C  
ANISOU  131  CA  LEU A  61     8428   5594   5225    618   -642   -274       C  
ATOM    132  C   LEU A  61     -37.123  -1.594  46.697  1.00 53.67           C  
ANISOU  132  C   LEU A  61     8601   6166   5627    706   -612   -310       C  
ATOM    133  O   LEU A  61     -37.223  -2.014  45.550  1.00 53.20           O  
ANISOU  133  O   LEU A  61     8518   6115   5579    653   -619   -271       O  
ATOM    134  CB  LEU A  61     -34.883  -1.524  47.904  1.00 49.54           C  
ANISOU  134  CB  LEU A  61     8196   5491   5137    452   -546   -242       C  
ATOM    135  CG  LEU A  61     -34.398  -2.890  47.362  1.00 53.85           C  
ANISOU  135  CG  LEU A  61     8588   6125   5749    295   -455   -185       C  
ATOM    136  CD1 LEU A  61     -33.883  -2.797  45.940  1.00 54.82           C  
ANISOU  136  CD1 LEU A  61     8795   6167   5869    200   -473   -128       C  
ATOM    137  CD2 LEU A  61     -33.333  -3.498  48.260  1.00 55.48           C  
ANISOU  137  CD2 LEU A  61     8738   6346   5994    170   -391   -161       C  
ATOM    138  N   ILE A  62     -38.053  -1.815  47.658  1.00 50.14           N  
ANISOU  138  N   ILE A  62     8005   5875   5171    827   -580   -385       N  
ATOM    139  CA  ILE A  62     -39.288  -2.596  47.471  1.00 50.10           C  
ANISOU  139  CA  ILE A  62     7777   6085   5173    891   -547   -430       C  
ATOM    140  C   ILE A  62     -40.040  -2.093  46.256  1.00 57.36           C  
ANISOU  140  C   ILE A  62     8739   6992   6064   1019   -653   -448       C  
ATOM    141  O   ILE A  62     -40.355  -2.887  45.364  1.00 58.44           O  
ANISOU  141  O   ILE A  62     8771   7210   6225    946   -639   -420       O  
ATOM    142  CB  ILE A  62     -40.195  -2.614  48.735  1.00 53.36           C  
ANISOU  142  CB  ILE A  62     8045   6675   5554   1015   -502   -524       C  
ATOM    143  CG1 ILE A  62     -39.522  -3.415  49.888  1.00 52.48           C  
ANISOU  143  CG1 ILE A  62     7876   6600   5465    858   -390   -494       C  
ATOM    144  CG2 ILE A  62     -41.598  -3.168  48.387  1.00 53.47           C  
ANISOU  144  CG2 ILE A  62     7829   6930   5557   1095   -490   -586       C  
ATOM    145  CD1 ILE A  62     -40.054  -3.205  51.295  1.00 54.95           C  
ANISOU  145  CD1 ILE A  62     8124   7030   5724    954   -343   -576       C  
ATOM    146  N   VAL A  63     -40.285  -0.769  46.204  1.00 54.32           N  
ANISOU  146  N   VAL A  63     8533   6488   5618   1209   -772   -494       N  
ATOM    147  CA  VAL A  63     -41.007  -0.107  45.105  1.00 54.43           C  
ANISOU  147  CA  VAL A  63     8635   6460   5585   1371   -905   -517       C  
ATOM    148  C   VAL A  63     -40.268  -0.292  43.807  1.00 56.62           C  
ANISOU  148  C   VAL A  63     9042   6599   5871   1205   -927   -415       C  
ATOM    149  O   VAL A  63     -40.886  -0.679  42.829  1.00 59.04           O  
ANISOU  149  O   VAL A  63     9276   6981   6174   1226   -965   -411       O  
ATOM    150  CB  VAL A  63     -41.295   1.383  45.394  1.00 59.42           C  
ANISOU  150  CB  VAL A  63     9490   6950   6137   1616  -1041   -585       C  
ATOM    151  CG1 VAL A  63     -42.084   2.012  44.252  1.00 60.81           C  
ANISOU  151  CG1 VAL A  63     9766   7083   6258   1805  -1198   -609       C  
ATOM    152  CG2 VAL A  63     -42.037   1.554  46.717  1.00 59.60           C  
ANISOU  152  CG2 VAL A  63     9373   7130   6140   1795  -1007   -702       C  
ATOM    153  N   PHE A  64     -38.947  -0.069  43.804  1.00 51.14           N  
ANISOU  153  N   PHE A  64     8522   5725   5182   1029   -897   -337       N  
ATOM    154  CA  PHE A  64     -38.099  -0.231  42.628  1.00 49.79           C  
ANISOU  154  CA  PHE A  64     8472   5437   5008    847   -894   -243       C  
ATOM    155  C   PHE A  64     -38.131  -1.656  42.079  1.00 51.72           C  
ANISOU  155  C   PHE A  64     8506   5833   5314    709   -795   -210       C  
ATOM    156  O   PHE A  64     -38.221  -1.822  40.866  1.00 52.43           O  
ANISOU  156  O   PHE A  64     8642   5898   5379    670   -830   -174       O  
ATOM    157  CB  PHE A  64     -36.669   0.236  42.918  1.00 51.32           C  
ANISOU  157  CB  PHE A  64     8842   5461   5195    671   -863   -182       C  
ATOM    158  CG  PHE A  64     -35.725   0.128  41.746  1.00 53.10           C  
ANISOU  158  CG  PHE A  64     9184   5589   5403    471   -843    -93       C  
ATOM    159  CD1 PHE A  64     -35.910   0.903  40.607  1.00 58.90           C  
ANISOU  159  CD1 PHE A  64    10140   6187   6051    501   -951    -62       C  
ATOM    160  CD2 PHE A  64     -34.610  -0.699  41.807  1.00 54.15           C  
ANISOU  160  CD2 PHE A  64     9218   5766   5592    256   -721    -45       C  
ATOM    161  CE1 PHE A  64     -35.022   0.808  39.529  1.00 60.57           C  
ANISOU  161  CE1 PHE A  64    10461   6323   6228    298   -917     18       C  
ATOM    162  CE2 PHE A  64     -33.719  -0.794  40.734  1.00 56.96           C  
ANISOU  162  CE2 PHE A  64     9661   6060   5921     75   -688     24       C  
ATOM    163  CZ  PHE A  64     -33.933  -0.047  39.600  1.00 57.59           C  
ANISOU  163  CZ  PHE A  64     9953   6019   5910     85   -778     56       C  
ATOM    164  N   THR A  65     -38.100  -2.675  42.961  1.00 47.05           N  
ANISOU  164  N   THR A  65     7705   5386   4786    639   -682   -226       N  
ATOM    165  CA  THR A  65     -38.146  -4.096  42.563  1.00 46.60           C  
ANISOU  165  CA  THR A  65     7471   5456   4780    508   -593   -200       C  
ATOM    166  C   THR A  65     -39.523  -4.409  41.956  1.00 52.38           C  
ANISOU  166  C   THR A  65     8075   6333   5493    614   -646   -247       C  
ATOM    167  O   THR A  65     -39.601  -5.019  40.887  1.00 50.60           O  
ANISOU  167  O   THR A  65     7835   6125   5267    537   -650   -216       O  
ATOM    168  CB  THR A  65     -37.839  -5.027  43.774  1.00 49.74           C  
ANISOU  168  CB  THR A  65     7717   5950   5230    420   -480   -206       C  
ATOM    169  OG1 THR A  65     -36.540  -4.750  44.287  1.00 50.62           O  
ANISOU  169  OG1 THR A  65     7933   5941   5358    326   -447   -167       O  
ATOM    170  CG2 THR A  65     -37.934  -6.495  43.434  1.00 42.13           C  
ANISOU  170  CG2 THR A  65     6610   5093   4305    293   -403   -183       C  
ATOM    171  N   VAL A  66     -40.607  -3.983  42.649  1.00 50.92           N  
ANISOU  171  N   VAL A  66     7793   6268   5288    794   -688   -331       N  
ATOM    172  CA  VAL A  66     -41.974  -4.243  42.201  1.00 51.36           C  
ANISOU  172  CA  VAL A  66     7684   6507   5324    904   -742   -393       C  
ATOM    173  C   VAL A  66     -42.238  -3.619  40.829  1.00 56.10           C  
ANISOU  173  C   VAL A  66     8427   7014   5876    991   -876   -379       C  
ATOM    174  O   VAL A  66     -42.540  -4.390  39.923  1.00 55.88           O  
ANISOU  174  O   VAL A  66     8324   7055   5851    907   -879   -358       O  
ATOM    175  CB  VAL A  66     -43.075  -3.889  43.239  1.00 55.47           C  
ANISOU  175  CB  VAL A  66     8042   7212   5824   1090   -751   -502       C  
ATOM    176  CG1 VAL A  66     -44.464  -4.242  42.710  1.00 56.08           C  
ANISOU  176  CG1 VAL A  66     7909   7519   5881   1182   -803   -571       C  
ATOM    177  CG2 VAL A  66     -42.828  -4.604  44.561  1.00 54.48           C  
ANISOU  177  CG2 VAL A  66     7789   7183   5730    976   -611   -507       C  
ATOM    178  N   VAL A  67     -42.081  -2.271  40.654  1.00 53.00           N  
ANISOU  178  N   VAL A  67     8264   6447   5425   1143   -992   -384       N  
ATOM    179  CA  VAL A  67     -42.395  -1.644  39.359  1.00 55.13           C  
ANISOU  179  CA  VAL A  67     8701   6617   5630   1236  -1138   -368       C  
ATOM    180  C   VAL A  67     -41.531  -2.219  38.229  1.00 54.45           C  
ANISOU  180  C   VAL A  67     8719   6426   5542   1012  -1097   -268       C  
ATOM    181  O   VAL A  67     -42.086  -2.562  37.192  1.00 54.99           O  
ANISOU  181  O   VAL A  67     8761   6548   5583   1020  -1157   -264       O  
ATOM    182  CB  VAL A  67     -42.461  -0.080  39.303  1.00 62.42           C  
ANISOU  182  CB  VAL A  67     9900   7348   6470   1448  -1294   -390       C  
ATOM    183  CG1 VAL A  67     -43.115   0.513  40.562  1.00 62.96           C  
ANISOU  183  CG1 VAL A  67     9886   7500   6535   1672  -1315   -497       C  
ATOM    184  CG2 VAL A  67     -41.101   0.563  39.017  1.00 62.23           C  
ANISOU  184  CG2 VAL A  67    10187   7048   6411   1293  -1289   -294       C  
ATOM    185  N   GLY A  68     -40.229  -2.382  38.467  1.00 45.81           N  
ANISOU  185  N   GLY A  68     7717   5214   4475    821   -992   -199       N  
ATOM    186  CA  GLY A  68     -39.304  -2.919  37.484  1.00 42.54           C  
ANISOU  186  CA  GLY A  68     7388   4722   4055    614   -932   -117       C  
ATOM    187  C   GLY A  68     -39.717  -4.287  37.007  1.00 44.17           C  
ANISOU  187  C   GLY A  68     7395   5087   4300    525   -870   -122       C  
ATOM    188  O   GLY A  68     -39.865  -4.498  35.810  1.00 45.40           O  
ANISOU  188  O   GLY A  68     7613   5225   4410    488   -915    -96       O  
ATOM    189  N   ASN A  69     -39.946  -5.219  37.932  1.00 39.29           N  
ANISOU  189  N   ASN A  69     6557   4619   3753    485   -776   -155       N  
ATOM    190  CA  ASN A  69     -40.300  -6.599  37.594  1.00 38.55           C  
ANISOU  190  CA  ASN A  69     6296   4661   3690    373   -714   -158       C  
ATOM    191  C   ASN A  69     -41.735  -6.727  37.075  1.00 45.12           C  
ANISOU  191  C   ASN A  69     7007   5645   4492    479   -812   -215       C  
ATOM    192  O   ASN A  69     -41.979  -7.563  36.201  1.00 45.34           O  
ANISOU  192  O   ASN A  69     6996   5723   4508    386   -814   -203       O  
ATOM    193  CB  ASN A  69     -39.990  -7.568  38.735  1.00 34.44           C  
ANISOU  193  CB  ASN A  69     5627   4223   3237    271   -588   -164       C  
ATOM    194  CG  ASN A  69     -38.505  -7.827  38.907  1.00 44.69           C  
ANISOU  194  CG  ASN A  69     7018   5396   4564    137   -495   -107       C  
ATOM    195  OD1 ASN A  69     -37.908  -8.728  38.299  1.00 40.49           O  
ANISOU  195  OD1 ASN A  69     6497   4844   4043     10   -436    -74       O  
ATOM    196  ND2 ASN A  69     -37.871  -7.039  39.741  1.00 37.97           N  
ANISOU  196  ND2 ASN A  69     6235   4468   3724    169   -484   -101       N  
ATOM    197  N   VAL A  70     -42.664  -5.864  37.542  1.00 43.41           N  
ANISOU  197  N   VAL A  70     6737   5502   4253    683   -904   -282       N  
ATOM    198  CA  VAL A  70     -44.023  -5.836  37.001  1.00 45.13           C  
ANISOU  198  CA  VAL A  70     6830   5883   4436    813  -1019   -347       C  
ATOM    199  C   VAL A  70     -43.850  -5.460  35.509  1.00 51.95           C  
ANISOU  199  C   VAL A  70     7899   6606   5233    820  -1129   -299       C  
ATOM    200  O   VAL A  70     -44.374  -6.172  34.657  1.00 52.58           O  
ANISOU  200  O   VAL A  70     7905   6777   5296    759  -1163   -303       O  
ATOM    201  CB  VAL A  70     -44.971  -4.877  37.777  1.00 49.73           C  
ANISOU  201  CB  VAL A  70     7325   6571   4999   1069  -1102   -442       C  
ATOM    202  CG1 VAL A  70     -46.147  -4.404  36.922  1.00 50.60           C  
ANISOU  202  CG1 VAL A  70     7394   6782   5051   1265  -1275   -505       C  
ATOM    203  CG2 VAL A  70     -45.472  -5.534  39.051  1.00 49.32           C  
ANISOU  203  CG2 VAL A  70     7010   6738   4993   1035   -989   -503       C  
ATOM    204  N   LEU A  71     -43.016  -4.428  35.204  1.00 48.93           N  
ANISOU  204  N   LEU A  71     7790   5994   4806    855  -1173   -247       N  
ATOM    205  CA  LEU A  71     -42.708  -3.997  33.827  1.00 49.62           C  
ANISOU  205  CA  LEU A  71     8120   5925   4809    834  -1266   -188       C  
ATOM    206  C   LEU A  71     -42.097  -5.130  32.972  1.00 54.11           C  
ANISOU  206  C   LEU A  71     8687   6490   5382    604  -1169   -132       C  
ATOM    207  O   LEU A  71     -42.401  -5.209  31.784  1.00 54.83           O  
ANISOU  207  O   LEU A  71     8864   6563   5405    596  -1252   -115       O  
ATOM    208  CB  LEU A  71     -41.777  -2.772  33.802  1.00 49.14           C  
ANISOU  208  CB  LEU A  71     8361   5617   4692    850  -1299   -133       C  
ATOM    209  CG  LEU A  71     -42.333  -1.455  34.236  1.00 54.10           C  
ANISOU  209  CG  LEU A  71     9110   6173   5274   1098  -1443   -180       C  
ATOM    210  CD1 LEU A  71     -41.220  -0.474  34.431  1.00 54.36           C  
ANISOU  210  CD1 LEU A  71     9431   5961   5263   1035  -1435   -118       C  
ATOM    211  CD2 LEU A  71     -43.313  -0.930  33.247  1.00 58.64           C  
ANISOU  211  CD2 LEU A  71     9777   6742   5760   1284  -1637   -206       C  
ATOM    212  N   VAL A  72     -41.242  -5.992  33.567  1.00 49.06           N  
ANISOU  212  N   VAL A  72     7963   5864   4813    432  -1004   -107       N  
ATOM    213  CA  VAL A  72     -40.676  -7.141  32.857  1.00 48.16           C  
ANISOU  213  CA  VAL A  72     7841   5754   4704    242   -911    -72       C  
ATOM    214  C   VAL A  72     -41.833  -8.078  32.430  1.00 55.21           C  
ANISOU  214  C   VAL A  72     8563   6817   5596    238   -959   -119       C  
ATOM    215  O   VAL A  72     -41.923  -8.408  31.247  1.00 56.33           O  
ANISOU  215  O   VAL A  72     8787   6937   5677    183  -1003   -101       O  
ATOM    216  CB  VAL A  72     -39.591  -7.888  33.668  1.00 49.45           C  
ANISOU  216  CB  VAL A  72     7943   5904   4942     98   -746    -50       C  
ATOM    217  CG1 VAL A  72     -39.198  -9.191  32.974  1.00 48.34           C  
ANISOU  217  CG1 VAL A  72     7779   5785   4802    -57   -665    -36       C  
ATOM    218  CG2 VAL A  72     -38.373  -7.008  33.884  1.00 48.79           C  
ANISOU  218  CG2 VAL A  72     8026   5667   4846     66   -704     -3       C  
ATOM    219  N   VAL A  73     -42.745  -8.445  33.374  1.00 52.39           N  
ANISOU  219  N   VAL A  73     7977   6637   5293    290   -955   -180       N  
ATOM    220  CA  VAL A  73     -43.931  -9.282  33.093  1.00 52.97           C  
ANISOU  220  CA  VAL A  73     7861   6905   5361    266  -1003   -233       C  
ATOM    221  C   VAL A  73     -44.683  -8.660  31.912  1.00 58.50           C  
ANISOU  221  C   VAL A  73     8637   7610   5979    388  -1175   -249       C  
ATOM    222  O   VAL A  73     -44.906  -9.343  30.917  1.00 60.88           O  
ANISOU  222  O   VAL A  73     8957   7934   6240    293  -1210   -241       O  
ATOM    223  CB  VAL A  73     -44.872  -9.446  34.326  1.00 56.87           C  
ANISOU  223  CB  VAL A  73     8097   7608   5901    323   -983   -304       C  
ATOM    224  CG1 VAL A  73     -46.136 -10.228  33.968  1.00 57.47           C  
ANISOU  224  CG1 VAL A  73     7969   7910   5959    276  -1041   -362       C  
ATOM    225  CG2 VAL A  73     -44.151 -10.087  35.504  1.00 55.09           C  
ANISOU  225  CG2 VAL A  73     7822   7368   5742    199   -824   -283       C  
ATOM    226  N   ILE A  74     -44.989  -7.345  31.999  1.00 53.24           N  
ANISOU  226  N   ILE A  74     8051   6899   5280    601  -1291   -268       N  
ATOM    227  CA  ILE A  74     -45.699  -6.577  30.979  1.00 53.50           C  
ANISOU  227  CA  ILE A  74     8187   6916   5225    763  -1482   -285       C  
ATOM    228  C   ILE A  74     -44.984  -6.647  29.628  1.00 56.78           C  
ANISOU  228  C   ILE A  74     8858   7154   5561    647  -1502   -207       C  
ATOM    229  O   ILE A  74     -45.634  -6.995  28.650  1.00 58.17           O  
ANISOU  229  O   ILE A  74     9026   7397   5681    643  -1603   -222       O  
ATOM    230  CB  ILE A  74     -46.002  -5.129  31.436  1.00 56.92           C  
ANISOU  230  CB  ILE A  74     8708   7287   5630   1025  -1600   -318       C  
ATOM    231  CG1 ILE A  74     -46.941  -5.119  32.674  1.00 56.74           C  
ANISOU  231  CG1 ILE A  74     8394   7495   5668   1163  -1590   -420       C  
ATOM    232  CG2 ILE A  74     -46.590  -4.306  30.280  1.00 58.53           C  
ANISOU  232  CG2 ILE A  74     9087   7425   5726   1198  -1816   -322       C  
ATOM    233  CD1 ILE A  74     -47.073  -3.747  33.353  1.00 60.69           C  
ANISOU  233  CD1 ILE A  74     8992   7920   6148   1424  -1675   -462       C  
ATOM    234  N   ALA A  75     -43.661  -6.403  29.584  1.00 50.77           N  
ANISOU  234  N   ALA A  75     8304   6196   4792    537  -1398   -132       N  
ATOM    235  CA  ALA A  75     -42.876  -6.470  28.342  1.00 50.34           C  
ANISOU  235  CA  ALA A  75     8488   5991   4650    407  -1386    -62       C  
ATOM    236  C   ALA A  75     -42.982  -7.839  27.639  1.00 54.67           C  
ANISOU  236  C   ALA A  75     8948   6630   5196    246  -1332    -69       C  
ATOM    237  O   ALA A  75     -43.277  -7.883  26.442  1.00 54.76           O  
ANISOU  237  O   ALA A  75     9078   6617   5112    236  -1427    -57       O  
ATOM    238  CB  ALA A  75     -41.422  -6.133  28.616  1.00 49.65           C  
ANISOU  238  CB  ALA A  75     8561   5737   4567    289  -1250      4       C  
ATOM    239  N   VAL A  76     -42.791  -8.950  28.389  1.00 50.10           N  
ANISOU  239  N   VAL A  76     8179   6147   4709    127  -1193    -90       N  
ATOM    240  CA  VAL A  76     -42.872 -10.297  27.817  1.00 50.33           C  
ANISOU  240  CA  VAL A  76     8150   6241   4733    -29  -1144   -102       C  
ATOM    241  C   VAL A  76     -44.281 -10.564  27.278  1.00 58.75           C  
ANISOU  241  C   VAL A  76     9098   7462   5761     23  -1296   -156       C  
ATOM    242  O   VAL A  76     -44.427 -11.115  26.184  1.00 60.12           O  
ANISOU  242  O   VAL A  76     9352   7628   5863    -58  -1342   -154       O  
ATOM    243  CB  VAL A  76     -42.403 -11.417  28.790  1.00 52.60           C  
ANISOU  243  CB  VAL A  76     8294   6576   5116   -158   -983   -113       C  
ATOM    244  CG1 VAL A  76     -42.459 -12.798  28.128  1.00 52.04           C  
ANISOU  244  CG1 VAL A  76     8216   6534   5020   -314   -948   -126       C  
ATOM    245  CG2 VAL A  76     -41.004 -11.143  29.340  1.00 51.03           C  
ANISOU  245  CG2 VAL A  76     8188   6247   4955   -195   -847    -68       C  
ATOM    246  N   LEU A  77     -45.305 -10.124  28.003  1.00 57.25           N  
ANISOU  246  N   LEU A  77     8721   7421   5610    163  -1381   -212       N  
ATOM    247  CA  LEU A  77     -46.678 -10.392  27.588  1.00 59.68           C  
ANISOU  247  CA  LEU A  77     8865   7924   5887    211  -1525   -278       C  
ATOM    248  C   LEU A  77     -47.218  -9.442  26.499  1.00 66.19           C  
ANISOU  248  C   LEU A  77     9831   8710   6609    379  -1729   -280       C  
ATOM    249  O   LEU A  77     -48.238  -9.749  25.885  1.00 66.14           O  
ANISOU  249  O   LEU A  77     9720   8853   6559    399  -1862   -329       O  
ATOM    250  CB  LEU A  77     -47.621 -10.440  28.812  1.00 60.25           C  
ANISOU  250  CB  LEU A  77     8634   8224   6034    282  -1521   -353       C  
ATOM    251  CG  LEU A  77     -47.280 -11.466  29.912  1.00 63.19           C  
ANISOU  251  CG  LEU A  77     8864   8654   6491    104  -1339   -353       C  
ATOM    252  CD1 LEU A  77     -48.377 -11.550  30.918  1.00 64.83           C  
ANISOU  252  CD1 LEU A  77     8773   9120   6739    151  -1347   -432       C  
ATOM    253  CD2 LEU A  77     -46.996 -12.851  29.354  1.00 63.61           C  
ANISOU  253  CD2 LEU A  77     8958   8682   6530   -136  -1271   -330       C  
ATOM    254  N   THR A  78     -46.541  -8.319  26.240  1.00 64.96           N  
ANISOU  254  N   THR A  78     9926   8354   6402    485  -1762   -226       N  
ATOM    255  CA  THR A  78     -47.019  -7.376  25.234  1.00 66.79           C  
ANISOU  255  CA  THR A  78    10339   8518   6519    650  -1968   -220       C  
ATOM    256  C   THR A  78     -46.117  -7.331  24.013  1.00 73.12           C  
ANISOU  256  C   THR A  78    11461   9113   7211    527  -1954   -136       C  
ATOM    257  O   THR A  78     -46.638  -7.362  22.907  1.00 76.77           O  
ANISOU  257  O   THR A  78    12017   9582   7572    548  -2096   -139       O  
ATOM    258  CB  THR A  78     -47.308  -5.962  25.814  1.00 72.51           C  
ANISOU  258  CB  THR A  78    11122   9192   7237    914  -2081   -240       C  
ATOM    259  OG1 THR A  78     -47.909  -5.177  24.782  1.00 79.97           O  
ANISOU  259  OG1 THR A  78    12244  10080   8060   1084  -2309   -241       O  
ATOM    260  CG2 THR A  78     -46.053  -5.220  26.317  1.00 65.62           C  
ANISOU  260  CG2 THR A  78    10471   8089   6373    882  -1967   -168       C  
ATOM    261  N   SER A  79     -44.791  -7.248  24.197  1.00 68.62           N  
ANISOU  261  N   SER A  79    11048   8374   6648    399  -1787    -68       N  
ATOM    262  CA  SER A  79     -43.814  -7.105  23.118  1.00 68.98           C  
ANISOU  262  CA  SER A  79    11394   8238   6580    272  -1746      9       C  
ATOM    263  C   SER A  79     -43.802  -8.260  22.130  1.00 73.75           C  
ANISOU  263  C   SER A  79    12004   8888   7131    112  -1711      3       C  
ATOM    264  O   SER A  79     -43.553  -9.390  22.537  1.00 73.60           O  
ANISOU  264  O   SER A  79    11822   8950   7193    -19  -1571    -23       O  
ATOM    265  CB  SER A  79     -42.423  -6.878  23.699  1.00 72.30           C  
ANISOU  265  CB  SER A  79    11904   8529   7038    159  -1556     63       C  
ATOM    266  OG  SER A  79     -41.406  -6.833  22.714  1.00 85.36           O  
ANISOU  266  OG  SER A  79    13807  10045   8579      8  -1481    128       O  
ATOM    267  N   ARG A  80     -44.046  -7.976  20.829  1.00 70.78           N  
ANISOU  267  N   ARG A  80    11843   8445   6607    123  -1844     28       N  
ATOM    268  CA  ARG A  80     -44.021  -8.996  19.774  1.00 70.54           C  
ANISOU  268  CA  ARG A  80    11864   8440   6500    -25  -1824     20       C  
ATOM    269  C   ARG A  80     -42.686  -9.765  19.794  1.00 72.66           C  
ANISOU  269  C   ARG A  80    12178   8643   6786   -223  -1581     46       C  
ATOM    270  O   ARG A  80     -42.680 -11.001  19.836  1.00 73.14           O  
ANISOU  270  O   ARG A  80    12111   8784   6894   -333  -1495      4       O  
ATOM    271  CB  ARG A  80     -44.278  -8.376  18.391  1.00 71.39           C  
ANISOU  271  CB  ARG A  80    12253   8449   6422     16  -1993     58       C  
ATOM    272  N   ALA A  81     -41.569  -9.018  19.867  1.00 66.29           N  
ANISOU  272  N   ALA A  81    11543   7697   5946   -262  -1476    108       N  
ATOM    273  CA  ALA A  81     -40.201  -9.523  19.916  1.00 63.70           C  
ANISOU  273  CA  ALA A  81    11253   7322   5627   -424  -1249    128       C  
ATOM    274  C   ALA A  81     -39.913 -10.338  21.163  1.00 64.76           C  
ANISOU  274  C   ALA A  81    11130   7543   5931   -450  -1109     87       C  
ATOM    275  O   ALA A  81     -38.950 -11.110  21.171  1.00 64.75           O  
ANISOU  275  O   ALA A  81    11116   7539   5949   -565   -939     78       O  
ATOM    276  CB  ALA A  81     -39.234  -8.364  19.834  1.00 64.59           C  
ANISOU  276  CB  ALA A  81    11579   7296   5666   -457  -1197    200       C  
ATOM    277  N   LEU A  82     -40.729 -10.166  22.216  1.00 58.96           N  
ANISOU  277  N   LEU A  82    10199   6890   5313   -335  -1182     57       N  
ATOM    278  CA  LEU A  82     -40.552 -10.893  23.472  1.00 57.00           C  
ANISOU  278  CA  LEU A  82     9721   6722   5214   -360  -1063     23       C  
ATOM    279  C   LEU A  82     -41.668 -11.921  23.782  1.00 65.28           C  
ANISOU  279  C   LEU A  82    10557   7922   6326   -363  -1120    -41       C  
ATOM    280  O   LEU A  82     -41.546 -12.659  24.761  1.00 66.35           O  
ANISOU  280  O   LEU A  82    10528   8116   6566   -409  -1022    -66       O  
ATOM    281  CB  LEU A  82     -40.383  -9.928  24.668  1.00 55.05           C  
ANISOU  281  CB  LEU A  82     9411   6455   5052   -262  -1052     39       C  
ATOM    282  CG  LEU A  82     -39.267  -8.909  24.628  1.00 56.05           C  
ANISOU  282  CG  LEU A  82     9725   6439   5131   -287   -990    100       C  
ATOM    283  CD1 LEU A  82     -39.474  -7.894  25.708  1.00 54.58           C  
ANISOU  283  CD1 LEU A  82     9496   6232   5008   -163  -1040    103       C  
ATOM    284  CD2 LEU A  82     -37.887  -9.571  24.714  1.00 52.25           C  
ANISOU  284  CD2 LEU A  82     9243   5936   4672   -438   -788    111       C  
ATOM    285  N   ARG A  83     -42.726 -11.991  22.967  1.00 63.56           N  
ANISOU  285  N   ARG A  83    10347   7768   6036   -331  -1279    -66       N  
ATOM    286  CA  ARG A  83     -43.838 -12.890  23.231  1.00 64.39           C  
ANISOU  286  CA  ARG A  83    10243   8037   6187   -359  -1343   -128       C  
ATOM    287  C   ARG A  83     -43.576 -14.358  22.867  1.00 68.10           C  
ANISOU  287  C   ARG A  83    10723   8508   6646   -536  -1256   -151       C  
ATOM    288  O   ARG A  83     -44.541 -15.088  22.644  1.00 70.97           O  
ANISOU  288  O   ARG A  83    10984   8984   6995   -596  -1343   -197       O  
ATOM    289  CB  ARG A  83     -45.115 -12.378  22.556  1.00 70.34           C  
ANISOU  289  CB  ARG A  83    10972   8885   6869   -250  -1563   -157       C  
ATOM    290  CG  ARG A  83     -46.080 -11.691  23.524  1.00 86.62           C  
ANISOU  290  CG  ARG A  83    12816  11091   9006    -86  -1657   -197       C  
ATOM    291  CD  ARG A  83     -47.518 -11.704  23.023  1.00106.65           C  
ANISOU  291  CD  ARG A  83    15218  13807  11498    -10  -1861   -259       C  
ATOM    292  NE  ARG A  83     -48.042 -13.069  22.901  1.00123.26           N  
ANISOU  292  NE  ARG A  83    17175  16046  13612   -195  -1841   -304       N  
ATOM    293  CZ  ARG A  83     -49.330 -13.395  22.949  1.00139.75           C  
ANISOU  293  CZ  ARG A  83    19030  18363  15704   -192  -1966   -376       C  
ATOM    294  NH1 ARG A  83     -50.254 -12.459  23.133  1.00129.14           N1+
ANISOU  294  NH1 ARG A  83    17548  17160  14361     20  -2121   -421       N1+
ATOM    295  NH2 ARG A  83     -49.704 -14.662  22.826  1.00124.20           N  
ANISOU  295  NH2 ARG A  83    16966  16491  13733   -400  -1941   -408       N  
ATOM    296  N   ALA A  84     -42.300 -14.807  22.844  1.00 60.43           N  
ANISOU  296  N   ALA A  84     9865   7419   5675   -618  -1090   -128       N  
ATOM    297  CA  ALA A  84     -41.931 -16.207  22.584  1.00 57.95           C  
ANISOU  297  CA  ALA A  84     9587   7081   5350   -755  -1002   -159       C  
ATOM    298  C   ALA A  84     -42.215 -17.032  23.864  1.00 60.80           C  
ANISOU  298  C   ALA A  84     9755   7517   5829   -807   -946   -186       C  
ATOM    299  O   ALA A  84     -42.142 -16.469  24.970  1.00 58.32           O  
ANISOU  299  O   ALA A  84     9316   7237   5607   -738   -909   -170       O  
ATOM    300  CB  ALA A  84     -40.463 -16.301  22.223  1.00 57.37           C  
ANISOU  300  CB  ALA A  84     9676   6882   5240   -785   -848   -137       C  
ATOM    301  N   PRO A  85     -42.550 -18.352  23.741  1.00 57.40           N  
ANISOU  301  N   PRO A  85     9321   7105   5385   -937   -945   -225       N  
ATOM    302  CA  PRO A  85     -42.901 -19.146  24.947  1.00 55.77           C  
ANISOU  302  CA  PRO A  85     8959   6963   5267  -1014   -902   -243       C  
ATOM    303  C   PRO A  85     -41.783 -19.350  25.964  1.00 57.16           C  
ANISOU  303  C   PRO A  85     9138   7055   5526   -994   -749   -223       C  
ATOM    304  O   PRO A  85     -42.077 -19.306  27.154  1.00 58.79           O  
ANISOU  304  O   PRO A  85     9192   7330   5814   -992   -726   -218       O  
ATOM    305  CB  PRO A  85     -43.411 -20.470  24.384  1.00 58.40           C  
ANISOU  305  CB  PRO A  85     9357   7295   5536  -1174   -947   -284       C  
ATOM    306  CG  PRO A  85     -43.721 -20.169  22.926  1.00 64.52           C  
ANISOU  306  CG  PRO A  85    10256   8061   6195  -1160  -1056   -295       C  
ATOM    307  CD  PRO A  85     -42.718 -19.153  22.511  1.00 59.10           C  
ANISOU  307  CD  PRO A  85     9688   7280   5487  -1031   -996   -255       C  
ATOM    308  N   GLN A  86     -40.522 -19.514  25.542  1.00 49.39           N  
ANISOU  308  N   GLN A  86     8308   5943   4517   -971   -648   -215       N  
ATOM    309  CA  GLN A  86     -39.415 -19.656  26.496  1.00 46.87           C  
ANISOU  309  CA  GLN A  86     7975   5560   4275   -935   -517   -202       C  
ATOM    310  C   GLN A  86     -39.288 -18.445  27.440  1.00 53.28           C  
ANISOU  310  C   GLN A  86     8661   6417   5166   -838   -499   -165       C  
ATOM    311  O   GLN A  86     -38.847 -18.595  28.590  1.00 53.81           O  
ANISOU  311  O   GLN A  86     8653   6478   5315   -824   -428   -156       O  
ATOM    312  CB  GLN A  86     -38.086 -19.935  25.790  1.00 47.19           C  
ANISOU  312  CB  GLN A  86     8172   5494   4264   -911   -414   -214       C  
ATOM    313  CG  GLN A  86     -37.546 -18.795  24.916  1.00 63.05           C  
ANISOU  313  CG  GLN A  86    10257   7490   6210   -854   -400   -188       C  
ATOM    314  CD  GLN A  86     -38.056 -18.725  23.482  1.00 69.70           C  
ANISOU  314  CD  GLN A  86    11233   8326   6925   -889   -483   -198       C  
ATOM    315  OE1 GLN A  86     -39.040 -19.357  23.062  1.00 56.96           O  
ANISOU  315  OE1 GLN A  86     9633   6739   5271   -950   -584   -224       O  
ATOM    316  NE2 GLN A  86     -37.381 -17.917  22.698  1.00 66.72           N  
ANISOU  316  NE2 GLN A  86    10964   7917   6471   -863   -446   -175       N  
ATOM    317  N   ASN A  87     -39.723 -17.255  26.972  1.00 49.91           N  
ANISOU  317  N   ASN A  87     8229   6026   4708   -768   -579   -144       N  
ATOM    318  CA  ASN A  87     -39.644 -16.012  27.743  1.00 48.88           C  
ANISOU  318  CA  ASN A  87     8022   5917   4633   -666   -582   -114       C  
ATOM    319  C   ASN A  87     -40.571 -15.983  28.971  1.00 50.07           C  
ANISOU  319  C   ASN A  87     7979   6182   4863   -644   -617   -129       C  
ATOM    320  O   ASN A  87     -40.453 -15.073  29.782  1.00 48.06           O  
ANISOU  320  O   ASN A  87     7662   5939   4658   -556   -608   -113       O  
ATOM    321  CB  ASN A  87     -39.860 -14.790  26.838  1.00 50.58           C  
ANISOU  321  CB  ASN A  87     8334   6110   4772   -590   -674    -89       C  
ATOM    322  CG  ASN A  87     -38.736 -14.515  25.874  1.00 65.16           C  
ANISOU  322  CG  ASN A  87    10370   7849   6538   -617   -607    -62       C  
ATOM    323  OD1 ASN A  87     -38.966 -14.227  24.703  1.00 70.09           O  
ANISOU  323  OD1 ASN A  87    11127   8447   7057   -623   -677    -54       O  
ATOM    324  ND2 ASN A  87     -37.498 -14.593  26.327  1.00 51.04           N  
ANISOU  324  ND2 ASN A  87     8593   6010   4788   -638   -471    -51       N  
ATOM    325  N   LEU A  88     -41.453 -16.995  29.128  1.00 47.06           N  
ANISOU  325  N   LEU A  88     7512   5887   4483   -739   -651   -162       N  
ATOM    326  CA  LEU A  88     -42.340 -17.131  30.284  1.00 47.42           C  
ANISOU  326  CA  LEU A  88     7365   6067   4584   -757   -664   -182       C  
ATOM    327  C   LEU A  88     -41.528 -17.455  31.573  1.00 51.04           C  
ANISOU  327  C   LEU A  88     7800   6475   5118   -772   -543   -163       C  
ATOM    328  O   LEU A  88     -42.007 -17.199  32.679  1.00 51.16           O  
ANISOU  328  O   LEU A  88     7673   6586   5180   -751   -532   -170       O  
ATOM    329  CB  LEU A  88     -43.414 -18.208  30.037  1.00 49.07           C  
ANISOU  329  CB  LEU A  88     7507   6381   4756   -903   -723   -218       C  
ATOM    330  CG  LEU A  88     -44.578 -17.884  29.079  1.00 55.71           C  
ANISOU  330  CG  LEU A  88     8291   7345   5533   -889   -869   -251       C  
ATOM    331  CD1 LEU A  88     -45.302 -19.149  28.678  1.00 56.99           C  
ANISOU  331  CD1 LEU A  88     8442   7567   5644  -1080   -911   -283       C  
ATOM    332  CD2 LEU A  88     -45.590 -16.959  29.735  1.00 59.30           C  
ANISOU  332  CD2 LEU A  88     8528   7985   6019   -777   -939   -280       C  
ATOM    333  N   PHE A  89     -40.292 -17.979  31.437  1.00 46.38           N  
ANISOU  333  N   PHE A  89     7346   5744   4531   -794   -455   -145       N  
ATOM    334  CA  PHE A  89     -39.447 -18.223  32.608  1.00 45.69           C  
ANISOU  334  CA  PHE A  89     7244   5606   4508   -785   -359   -129       C  
ATOM    335  C   PHE A  89     -39.073 -16.915  33.285  1.00 49.18           C  
ANISOU  335  C   PHE A  89     7628   6059   5000   -667   -343   -108       C  
ATOM    336  O   PHE A  89     -38.901 -16.894  34.508  1.00 50.58           O  
ANISOU  336  O   PHE A  89     7733   6253   5231   -655   -298   -101       O  
ATOM    337  CB  PHE A  89     -38.161 -18.957  32.230  1.00 47.55           C  
ANISOU  337  CB  PHE A  89     7624   5709   4734   -796   -283   -128       C  
ATOM    338  CG  PHE A  89     -38.347 -20.336  31.657  1.00 49.99           C  
ANISOU  338  CG  PHE A  89     8037   5968   4990   -899   -294   -155       C  
ATOM    339  CD1 PHE A  89     -38.859 -21.366  32.437  1.00 52.35           C  
ANISOU  339  CD1 PHE A  89     8323   6272   5294  -1002   -300   -160       C  
ATOM    340  CD2 PHE A  89     -37.931 -20.629  30.361  1.00 52.16           C  
ANISOU  340  CD2 PHE A  89     8448   6176   5195   -901   -296   -175       C  
ATOM    341  CE1 PHE A  89     -39.007 -22.646  31.910  1.00 54.46           C  
ANISOU  341  CE1 PHE A  89     8725   6466   5500  -1107   -322   -185       C  
ATOM    342  CE2 PHE A  89     -38.075 -21.911  29.834  1.00 55.13           C  
ANISOU  342  CE2 PHE A  89     8946   6487   5512   -988   -313   -208       C  
ATOM    343  CZ  PHE A  89     -38.618 -22.908  30.608  1.00 53.94           C  
ANISOU  343  CZ  PHE A  89     8795   6328   5370  -1091   -332   -212       C  
ATOM    344  N   LEU A  90     -38.938 -15.826  32.475  1.00 43.39           N  
ANISOU  344  N   LEU A  90     6951   5302   4235   -589   -385    -96       N  
ATOM    345  CA  LEU A  90     -38.608 -14.463  32.885  1.00 40.65           C  
ANISOU  345  CA  LEU A  90     6600   4935   3909   -484   -392    -75       C  
ATOM    346  C   LEU A  90     -39.788 -13.886  33.623  1.00 46.66           C  
ANISOU  346  C   LEU A  90     7224   5814   4691   -412   -463    -98       C  
ATOM    347  O   LEU A  90     -39.583 -13.175  34.619  1.00 47.76           O  
ANISOU  347  O   LEU A  90     7319   5954   4872   -342   -442    -94       O  
ATOM    348  CB  LEU A  90     -38.269 -13.580  31.693  1.00 39.81           C  
ANISOU  348  CB  LEU A  90     6633   4759   3734   -448   -433    -54       C  
ATOM    349  CG  LEU A  90     -37.284 -14.094  30.650  1.00 42.43           C  
ANISOU  349  CG  LEU A  90     7098   5010   4013   -519   -369    -44       C  
ATOM    350  CD1 LEU A  90     -36.937 -12.999  29.689  1.00 42.54           C  
ANISOU  350  CD1 LEU A  90     7254   4961   3949   -496   -401    -13       C  
ATOM    351  CD2 LEU A  90     -36.018 -14.605  31.273  1.00 42.11           C  
ANISOU  351  CD2 LEU A  90     7050   4928   4023   -550   -247    -43       C  
ATOM    352  N   VAL A  91     -41.028 -14.228  33.166  1.00 41.94           N  
ANISOU  352  N   VAL A  91     6548   5329   4059   -431   -546   -131       N  
ATOM    353  CA  VAL A  91     -42.287 -13.832  33.812  1.00 42.40           C  
ANISOU  353  CA  VAL A  91     6431   5551   4128   -364   -612   -172       C  
ATOM    354  C   VAL A  91     -42.356 -14.484  35.202  1.00 49.91           C  
ANISOU  354  C   VAL A  91     7261   6574   5131   -433   -524   -182       C  
ATOM    355  O   VAL A  91     -42.601 -13.798  36.204  1.00 51.36           O  
ANISOU  355  O   VAL A  91     7350   6822   5342   -344   -515   -199       O  
ATOM    356  CB  VAL A  91     -43.517 -14.153  32.944  1.00 46.35           C  
ANISOU  356  CB  VAL A  91     6857   6179   4574   -390   -720   -211       C  
ATOM    357  CG1 VAL A  91     -44.810 -13.948  33.714  1.00 46.56           C  
ANISOU  357  CG1 VAL A  91     6654   6423   4612   -340   -767   -269       C  
ATOM    358  CG2 VAL A  91     -43.511 -13.306  31.682  1.00 46.97           C  
ANISOU  358  CG2 VAL A  91     7071   6186   4591   -291   -826   -200       C  
ATOM    359  N   SER A  92     -42.079 -15.793  35.262  1.00 45.98           N  
ANISOU  359  N   SER A  92     6793   6044   4633   -588   -462   -170       N  
ATOM    360  CA  SER A  92     -42.051 -16.559  36.502  1.00 45.03           C  
ANISOU  360  CA  SER A  92     6610   5959   4541   -680   -383   -167       C  
ATOM    361  C   SER A  92     -40.940 -16.066  37.456  1.00 51.12           C  
ANISOU  361  C   SER A  92     7430   6629   5363   -605   -310   -138       C  
ATOM    362  O   SER A  92     -41.166 -15.988  38.672  1.00 50.99           O  
ANISOU  362  O   SER A  92     7324   6682   5367   -602   -272   -146       O  
ATOM    363  CB  SER A  92     -41.869 -18.034  36.192  1.00 45.06           C  
ANISOU  363  CB  SER A  92     6704   5899   4518   -848   -354   -156       C  
ATOM    364  OG  SER A  92     -42.024 -18.776  37.386  1.00 50.70           O  
ANISOU  364  OG  SER A  92     7375   6651   5240   -951   -296   -150       O  
ATOM    365  N   LEU A  93     -39.755 -15.721  36.900  1.00 48.13           N  
ANISOU  365  N   LEU A  93     7186   6104   4996   -555   -291   -110       N  
ATOM    366  CA  LEU A  93     -38.616 -15.209  37.669  1.00 46.92           C  
ANISOU  366  CA  LEU A  93     7076   5864   4887   -497   -233    -86       C  
ATOM    367  C   LEU A  93     -38.956 -13.821  38.237  1.00 51.80           C  
ANISOU  367  C   LEU A  93     7637   6528   5518   -373   -269    -97       C  
ATOM    368  O   LEU A  93     -38.751 -13.599  39.422  1.00 51.48           O  
ANISOU  368  O   LEU A  93     7553   6501   5507   -348   -232    -98       O  
ATOM    369  CB  LEU A  93     -37.353 -15.177  36.778  1.00 45.67           C  
ANISOU  369  CB  LEU A  93     7051   5579   4724   -494   -203    -64       C  
ATOM    370  CG  LEU A  93     -35.978 -14.905  37.403  1.00 46.94           C  
ANISOU  370  CG  LEU A  93     7250   5661   4925   -466   -138    -44       C  
ATOM    371  CD1 LEU A  93     -35.687 -15.804  38.569  1.00 45.77           C  
ANISOU  371  CD1 LEU A  93     7069   5511   4812   -500    -93    -44       C  
ATOM    372  CD2 LEU A  93     -34.904 -15.100  36.382  1.00 47.81           C  
ANISOU  372  CD2 LEU A  93     7457   5696   5013   -486   -100    -39       C  
ATOM    373  N   ALA A  94     -39.577 -12.940  37.423  1.00 50.00           N  
ANISOU  373  N   ALA A  94     7418   6325   5256   -291   -353   -111       N  
ATOM    374  CA  ALA A  94     -40.027 -11.595  37.822  1.00 50.51           C  
ANISOU  374  CA  ALA A  94     7458   6418   5315   -145   -414   -132       C  
ATOM    375  C   ALA A  94     -40.941 -11.637  39.051  1.00 56.43           C  
ANISOU  375  C   ALA A  94     8041   7319   6079   -109   -401   -178       C  
ATOM    376  O   ALA A  94     -40.842 -10.778  39.914  1.00 56.60           O  
ANISOU  376  O   ALA A  94     8058   7335   6113     -9   -400   -192       O  
ATOM    377  CB  ALA A  94     -40.760 -10.934  36.668  1.00 52.01           C  
ANISOU  377  CB  ALA A  94     7686   6624   5451    -61   -527   -147       C  
ATOM    378  N   SER A  95     -41.818 -12.653  39.125  1.00 53.94           N  
ANISOU  378  N   SER A  95     7599   7143   5753   -206   -388   -202       N  
ATOM    379  CA  SER A  95     -42.770 -12.885  40.211  1.00 53.32           C  
ANISOU  379  CA  SER A  95     7344   7246   5669   -218   -359   -248       C  
ATOM    380  C   SER A  95     -42.032 -13.267  41.473  1.00 55.81           C  
ANISOU  380  C   SER A  95     7684   7511   6011   -280   -261   -221       C  
ATOM    381  O   SER A  95     -42.428 -12.813  42.544  1.00 56.35           O  
ANISOU  381  O   SER A  95     7662   7675   6074   -218   -236   -255       O  
ATOM    382  CB  SER A  95     -43.746 -13.993  39.833  1.00 56.30           C  
ANISOU  382  CB  SER A  95     7608   7770   6014   -364   -365   -269       C  
ATOM    383  OG  SER A  95     -44.212 -13.820  38.504  1.00 64.30           O  
ANISOU  383  OG  SER A  95     8634   8796   7000   -331   -462   -282       O  
ATOM    384  N   ALA A  96     -40.949 -14.090  41.361  1.00 50.04           N  
ANISOU  384  N   ALA A  96     7078   6634   5301   -386   -211   -168       N  
ATOM    385  CA  ALA A  96     -40.154 -14.497  42.526  1.00 47.96           C  
ANISOU  385  CA  ALA A  96     6856   6308   5058   -433   -137   -140       C  
ATOM    386  C   ALA A  96     -39.625 -13.232  43.186  1.00 50.96           C  
ANISOU  386  C   ALA A  96     7260   6642   5461   -295   -143   -146       C  
ATOM    387  O   ALA A  96     -39.844 -13.064  44.375  1.00 50.91           O  
ANISOU  387  O   ALA A  96     7197   6699   5446   -277   -109   -164       O  
ATOM    388  CB  ALA A  96     -39.015 -15.429  42.127  1.00 47.40           C  
ANISOU  388  CB  ALA A  96     6919   6085   5005   -515   -107    -95       C  
ATOM    389  N   ASP A  97     -39.086 -12.289  42.377  1.00 46.62           N  
ANISOU  389  N   ASP A  97     6799   5993   4922   -205   -192   -137       N  
ATOM    390  CA  ASP A  97     -38.590 -10.974  42.793  1.00 46.24           C  
ANISOU  390  CA  ASP A  97     6813   5875   4882    -88   -217   -141       C  
ATOM    391  C   ASP A  97     -39.720 -10.051  43.335  1.00 50.66           C  
ANISOU  391  C   ASP A  97     7286   6549   5413     51   -264   -202       C  
ATOM    392  O   ASP A  97     -39.552  -9.469  44.402  1.00 51.30           O  
ANISOU  392  O   ASP A  97     7372   6627   5493    114   -248   -221       O  
ATOM    393  CB  ASP A  97     -37.799 -10.305  41.655  1.00 47.91           C  
ANISOU  393  CB  ASP A  97     7162   5952   5091    -69   -259   -110       C  
ATOM    394  CG  ASP A  97     -36.595 -11.106  41.156  1.00 65.48           C  
ANISOU  394  CG  ASP A  97     9456   8087   7338   -181   -203    -67       C  
ATOM    395  OD1 ASP A  97     -35.991 -11.858  41.972  1.00 65.27           O  
ANISOU  395  OD1 ASP A  97     9406   8053   7340   -237   -144    -56       O  
ATOM    396  OD2 ASP A  97     -36.238 -10.965  39.949  1.00 76.61           O1-
ANISOU  396  OD2 ASP A  97    10946   9435   8725   -202   -222    -48       O1-
ATOM    397  N   ILE A  98     -40.875  -9.957  42.644  1.00 46.77           N  
ANISOU  397  N   ILE A  98     6708   6172   4891    106   -324   -243       N  
ATOM    398  CA  ILE A  98     -42.023  -9.158  43.104  1.00 46.79           C  
ANISOU  398  CA  ILE A  98     6599   6319   4862    265   -372   -320       C  
ATOM    399  C   ILE A  98     -42.467  -9.592  44.514  1.00 53.07           C  
ANISOU  399  C   ILE A  98     7255   7263   5648    230   -287   -356       C  
ATOM    400  O   ILE A  98     -42.801  -8.752  45.354  1.00 55.89           O  
ANISOU  400  O   ILE A  98     7579   7673   5982    368   -293   -412       O  
ATOM    401  CB  ILE A  98     -43.208  -9.214  42.096  1.00 49.55           C  
ANISOU  401  CB  ILE A  98     6844   6803   5181    315   -454   -362       C  
ATOM    402  CG1 ILE A  98     -42.889  -8.421  40.822  1.00 48.79           C  
ANISOU  402  CG1 ILE A  98     6914   6556   5068    402   -561   -336       C  
ATOM    403  CG2 ILE A  98     -44.523  -8.700  42.734  1.00 50.64           C  
ANISOU  403  CG2 ILE A  98     6793   7165   5284    469   -484   -462       C  
ATOM    404  CD1 ILE A  98     -43.673  -8.823  39.638  1.00 45.96           C  
ANISOU  404  CD1 ILE A  98     6499   6281   4683    386   -634   -348       C  
ATOM    405  N   LEU A  99     -42.442 -10.893  44.768  1.00 47.79           N  
ANISOU  405  N   LEU A  99     6529   6645   4982     44   -209   -326       N  
ATOM    406  CA  LEU A  99     -42.897 -11.453  46.027  1.00 47.07           C  
ANISOU  406  CA  LEU A  99     6325   6696   4862    -33   -123   -349       C  
ATOM    407  C   LEU A  99     -41.873 -11.387  47.156  1.00 51.60           C  
ANISOU  407  C   LEU A  99     7007   7152   5447    -51    -66   -315       C  
ATOM    408  O   LEU A  99     -42.322 -11.330  48.291  1.00 52.91           O  
ANISOU  408  O   LEU A  99     7094   7435   5572    -43    -12   -353       O  
ATOM    409  CB  LEU A  99     -43.428 -12.866  45.823  1.00 46.33           C  
ANISOU  409  CB  LEU A  99     6151   6706   4746   -241    -77   -331       C  
ATOM    410  CG  LEU A  99     -44.669 -12.911  44.955  1.00 49.44           C  
ANISOU  410  CG  LEU A  99     6388   7282   5114   -232   -133   -385       C  
ATOM    411  CD1 LEU A  99     -44.888 -14.283  44.410  1.00 48.29           C  
ANISOU  411  CD1 LEU A  99     6237   7158   4952   -457   -114   -349       C  
ATOM    412  CD2 LEU A  99     -45.887 -12.316  45.673  1.00 50.64           C  
ANISOU  412  CD2 LEU A  99     6326   7695   5219   -126   -122   -482       C  
ATOM    413  N   VAL A 100     -40.527 -11.338  46.876  1.00 46.43           N  
ANISOU  413  N   VAL A 100     6517   6285   4838    -69    -79   -252       N  
ATOM    414  CA  VAL A 100     -39.493 -11.141  47.920  1.00 45.20           C  
ANISOU  414  CA  VAL A 100     6457   6022   4694    -69    -47   -226       C  
ATOM    415  C   VAL A 100     -39.677  -9.705  48.412  1.00 48.02           C  
ANISOU  415  C   VAL A 100     6831   6382   5034    104    -87   -280       C  
ATOM    416  O   VAL A 100     -39.575  -9.430  49.590  1.00 47.45           O  
ANISOU  416  O   VAL A 100     6764   6329   4936    133    -55   -301       O  
ATOM    417  CB  VAL A 100     -38.024 -11.276  47.438  1.00 48.76           C  
ANISOU  417  CB  VAL A 100     7049   6281   5195   -113    -60   -164       C  
ATOM    418  CG1 VAL A 100     -37.087 -11.492  48.623  1.00 48.79           C  
ANISOU  418  CG1 VAL A 100     7113   6221   5204   -149    -26   -139       C  
ATOM    419  CG2 VAL A 100     -37.850 -12.386  46.442  1.00 48.66           C  
ANISOU  419  CG2 VAL A 100     7050   6238   5200   -223    -52   -127       C  
ATOM    420  N   ALA A 101     -39.899  -8.793  47.465  1.00 44.14           N  
ANISOU  420  N   ALA A 101     6374   5850   4546    221   -166   -301       N  
ATOM    421  CA  ALA A 101     -40.104  -7.387  47.663  1.00 43.76           C  
ANISOU  421  CA  ALA A 101     6387   5768   4474    404   -233   -352       C  
ATOM    422  C   ALA A 101     -41.292  -7.117  48.569  1.00 51.22           C  
ANISOU  422  C   ALA A 101     7189   6906   5365    518   -212   -443       C  
ATOM    423  O   ALA A 101     -41.181  -6.324  49.504  1.00 52.19           O  
ANISOU  423  O   ALA A 101     7365   7006   5458    623   -215   -485       O  
ATOM    424  CB  ALA A 101     -40.316  -6.731  46.320  1.00 44.46           C  
ANISOU  424  CB  ALA A 101     6542   5790   4560    489   -330   -352       C  
ATOM    425  N   THR A 102     -42.414  -7.799  48.332  1.00 49.05           N  
ANISOU  425  N   THR A 102     6730   6837   5071    488   -186   -480       N  
ATOM    426  CA  THR A 102     -43.644  -7.557  49.096  1.00 49.29           C  
ANISOU  426  CA  THR A 102     6581   7104   5042    596   -157   -581       C  
ATOM    427  C   THR A 102     -43.812  -8.455  50.338  1.00 51.64           C  
ANISOU  427  C   THR A 102     6779   7539   5301    447    -31   -582       C  
ATOM    428  O   THR A 102     -44.244  -7.968  51.386  1.00 51.33           O  
ANISOU  428  O   THR A 102     6683   7614   5206    543     10   -654       O  
ATOM    429  CB  THR A 102     -44.865  -7.658  48.163  1.00 48.71           C  
ANISOU  429  CB  THR A 102     6336   7216   4955    655   -209   -636       C  
ATOM    430  OG1 THR A 102     -44.902  -8.985  47.634  1.00 50.48           O  
ANISOU  430  OG1 THR A 102     6496   7484   5199    425   -163   -576       O  
ATOM    431  CG2 THR A 102     -44.809  -6.661  47.005  1.00 41.29           C  
ANISOU  431  CG2 THR A 102     5516   6142   4030    830   -350   -642       C  
ATOM    432  N   LEU A 103     -43.501  -9.755  50.221  1.00 47.28           N  
ANISOU  432  N   LEU A 103     6225   6974   4765    217     28   -506       N  
ATOM    433  CA  LEU A 103     -43.765 -10.716  51.303  1.00 47.42           C  
ANISOU  433  CA  LEU A 103     6172   7119   4727     48    139   -498       C  
ATOM    434  C   LEU A 103     -42.646 -10.972  52.260  1.00 50.98           C  
ANISOU  434  C   LEU A 103     6783   7410   5177    -27    178   -436       C  
ATOM    435  O   LEU A 103     -42.923 -11.518  53.325  1.00 52.97           O  
ANISOU  435  O   LEU A 103     6998   7768   5360   -131    263   -440       O  
ATOM    436  CB  LEU A 103     -44.247 -12.080  50.764  1.00 47.24           C  
ANISOU  436  CB  LEU A 103     6068   7187   4694   -176    175   -458       C  
ATOM    437  CG  LEU A 103     -45.533 -12.119  49.945  1.00 54.07           C  
ANISOU  437  CG  LEU A 103     6730   8272   5541   -161    148   -523       C  
ATOM    438  CD1 LEU A 103     -45.905 -13.541  49.618  1.00 55.61           C  
ANISOU  438  CD1 LEU A 103     6880   8539   5711   -427    190   -478       C  
ATOM    439  CD2 LEU A 103     -46.698 -11.458  50.667  1.00 58.03           C  
ANISOU  439  CD2 LEU A 103     7019   9054   5974    -36    185   -641       C  
ATOM    440  N   VAL A 104     -41.392 -10.644  51.895  1.00 44.09           N  
ANISOU  440  N   VAL A 104     6083   6299   4370      8    119   -378       N  
ATOM    441  CA  VAL A 104     -40.226 -10.977  52.705  1.00 41.84           C  
ANISOU  441  CA  VAL A 104     5941   5866   4092    -66    138   -318       C  
ATOM    442  C   VAL A 104     -39.423  -9.753  53.132  1.00 47.83           C  
ANISOU  442  C   VAL A 104     6815   6493   4866     75     87   -335       C  
ATOM    443  O   VAL A 104     -39.290  -9.535  54.332  1.00 51.71           O  
ANISOU  443  O   VAL A 104     7340   7001   5307     90    118   -355       O  
ATOM    444  CB  VAL A 104     -39.368 -12.037  51.988  1.00 43.11           C  
ANISOU  444  CB  VAL A 104     6187   5888   4305   -203    125   -233       C  
ATOM    445  CG1 VAL A 104     -38.016 -12.203  52.656  1.00 42.02           C  
ANISOU  445  CG1 VAL A 104     6190   5588   4187   -230    115   -181       C  
ATOM    446  CG2 VAL A 104     -40.105 -13.373  51.924  1.00 43.22           C  
ANISOU  446  CG2 VAL A 104     6135   6010   4277   -377    180   -212       C  
ATOM    447  N   MET A 105     -38.929  -8.952  52.185  1.00 41.33           N  
ANISOU  447  N   MET A 105     6064   5542   4097    162      9   -328       N  
ATOM    448  CA  MET A 105     -38.124  -7.771  52.439  1.00 41.71           C  
ANISOU  448  CA  MET A 105     6247   5445   4154    263    -52   -337       C  
ATOM    449  C   MET A 105     -38.662  -6.842  53.522  1.00 48.24           C  
ANISOU  449  C   MET A 105     7081   6336   4914    400    -50   -418       C  
ATOM    450  O   MET A 105     -37.816  -6.363  54.276  1.00 49.20           O  
ANISOU  450  O   MET A 105     7322   6347   5026    405    -70   -410       O  
ATOM    451  CB  MET A 105     -37.858  -6.971  51.154  1.00 44.66           C  
ANISOU  451  CB  MET A 105     6699   5704   4568    330   -135   -327       C  
ATOM    452  CG  MET A 105     -36.606  -7.402  50.389  1.00 47.34           C  
ANISOU  452  CG  MET A 105     7118   5902   4968    208   -147   -247       C  
ATOM    453  SD  MET A 105     -36.380  -6.551  48.796  1.00 51.57           S  
ANISOU  453  SD  MET A 105     7752   6321   5524    250   -228   -229       S  
ATOM    454  CE  MET A 105     -36.323  -5.005  49.372  1.00 49.69           C  
ANISOU  454  CE  MET A 105     7647   5991   5241    383   -299   -274       C  
ATOM    455  N   PRO A 106     -39.987  -6.531  53.659  1.00 46.10           N  
ANISOU  455  N   PRO A 106     6684   6243   4588    519    -32   -504       N  
ATOM    456  CA  PRO A 106     -40.393  -5.589  54.730  1.00 46.76           C  
ANISOU  456  CA  PRO A 106     6790   6379   4598    674    -30   -594       C  
ATOM    457  C   PRO A 106     -40.238  -6.170  56.140  1.00 52.08           C  
ANISOU  457  C   PRO A 106     7454   7122   5212    577     61   -592       C  
ATOM    458  O   PRO A 106     -39.853  -5.428  57.054  1.00 53.00           O  
ANISOU  458  O   PRO A 106     7682   7171   5283    653     44   -627       O  
ATOM    459  CB  PRO A 106     -41.861  -5.255  54.409  1.00 49.60           C  
ANISOU  459  CB  PRO A 106     6982   6947   4916    831    -29   -695       C  
ATOM    460  CG  PRO A 106     -42.151  -5.852  53.067  1.00 53.55           C  
ANISOU  460  CG  PRO A 106     7399   7473   5475    762    -56   -651       C  
ATOM    461  CD  PRO A 106     -41.157  -6.963  52.861  1.00 48.03           C  
ANISOU  461  CD  PRO A 106     6756   6661   4831    530    -19   -536       C  
ATOM    462  N   PHE A 107     -40.507  -7.505  56.308  1.00 45.80           N  
ANISOU  462  N   PHE A 107     6552   6446   4406    397    148   -546       N  
ATOM    463  CA  PHE A 107     -40.423  -8.206  57.594  1.00 43.54           C  
ANISOU  463  CA  PHE A 107     6274   6224   4044    278    233   -531       C  
ATOM    464  C   PHE A 107     -38.989  -8.387  58.013  1.00 46.10           C  
ANISOU  464  C   PHE A 107     6775   6339   4400    199    191   -451       C  
ATOM    465  O   PHE A 107     -38.708  -8.337  59.209  1.00 45.80           O  
ANISOU  465  O   PHE A 107     6810   6299   4294    184    216   -460       O  
ATOM    466  CB  PHE A 107     -41.198  -9.537  57.587  1.00 44.88           C  
ANISOU  466  CB  PHE A 107     6308   6569   4175     97    326   -504       C  
ATOM    467  CG  PHE A 107     -42.628  -9.352  57.133  1.00 47.08           C  
ANISOU  467  CG  PHE A 107     6376   7091   4423    166    362   -592       C  
ATOM    468  CD1 PHE A 107     -43.560  -8.724  57.956  1.00 49.66           C  
ANISOU  468  CD1 PHE A 107     6590   7624   4654    287    421   -705       C  
ATOM    469  CD2 PHE A 107     -43.012  -9.691  55.837  1.00 48.73           C  
ANISOU  469  CD2 PHE A 107     6495   7325   4695    138    324   -575       C  
ATOM    470  CE1 PHE A 107     -44.861  -8.484  57.513  1.00 51.50           C  
ANISOU  470  CE1 PHE A 107     6602   8106   4860    381    442   -802       C  
ATOM    471  CE2 PHE A 107     -44.315  -9.438  55.388  1.00 52.06           C  
ANISOU  471  CE2 PHE A 107     6708   7981   5090    223    335   -665       C  
ATOM    472  CZ  PHE A 107     -45.232  -8.841  56.233  1.00 51.12           C  
ANISOU  472  CZ  PHE A 107     6459   8085   4881    348    393   -781       C  
ATOM    473  N   SER A 108     -38.061  -8.507  57.038  1.00 42.62           N  
ANISOU  473  N   SER A 108     6402   5734   4057    162    122   -383       N  
ATOM    474  CA  SER A 108     -36.629  -8.616  57.343  1.00 42.66           C  
ANISOU  474  CA  SER A 108     6546   5563   4100    102     72   -320       C  
ATOM    475  C   SER A 108     -36.147  -7.323  57.972  1.00 52.12           C  
ANISOU  475  C   SER A 108     7855   6673   5275    214     14   -366       C  
ATOM    476  O   SER A 108     -35.364  -7.363  58.920  1.00 53.47           O  
ANISOU  476  O   SER A 108     8118   6781   5418    174     -2   -348       O  
ATOM    477  CB  SER A 108     -35.812  -8.918  56.095  1.00 43.16           C  
ANISOU  477  CB  SER A 108     6630   5506   4263     51     22   -257       C  
ATOM    478  OG  SER A 108     -35.651 -10.312  55.900  1.00 51.09           O  
ANISOU  478  OG  SER A 108     7610   6520   5282    -79     56   -196       O  
ATOM    479  N   LEU A 109     -36.638  -6.175  57.460  1.00 50.42           N  
ANISOU  479  N   LEU A 109     7648   6448   5061    358    -28   -428       N  
ATOM    480  CA  LEU A 109     -36.261  -4.863  57.953  1.00 50.53           C  
ANISOU  480  CA  LEU A 109     7803   6355   5043    470    -96   -479       C  
ATOM    481  C   LEU A 109     -36.958  -4.590  59.272  1.00 57.27           C  
ANISOU  481  C   LEU A 109     8651   7321   5787    552    -46   -559       C  
ATOM    482  O   LEU A 109     -36.281  -4.247  60.244  1.00 59.20           O  
ANISOU  482  O   LEU A 109     9016   7488   5988    541    -71   -564       O  
ATOM    483  CB  LEU A 109     -36.562  -3.792  56.912  1.00 50.89           C  
ANISOU  483  CB  LEU A 109     7896   6328   5112    598   -171   -514       C  
ATOM    484  CG  LEU A 109     -36.390  -2.379  57.397  1.00 57.59           C  
ANISOU  484  CG  LEU A 109     8918   7058   5907    731   -250   -578       C  
ATOM    485  CD1 LEU A 109     -34.928  -1.976  57.422  1.00 58.07           C  
ANISOU  485  CD1 LEU A 109     9142   6923   6000    617   -323   -519       C  
ATOM    486  CD2 LEU A 109     -37.250  -1.429  56.614  1.00 61.28           C  
ANISOU  486  CD2 LEU A 109     9414   7512   6356    917   -311   -644       C  
ATOM    487  N   ALA A 110     -38.299  -4.762  59.325  1.00 52.69           N  
ANISOU  487  N   ALA A 110     7923   6941   5155    628     28   -626       N  
ATOM    488  CA  ALA A 110     -39.059  -4.569  60.559  1.00 52.66           C  
ANISOU  488  CA  ALA A 110     7885   7090   5032    703    100   -714       C  
ATOM    489  C   ALA A 110     -38.476  -5.429  61.699  1.00 56.77           C  
ANISOU  489  C   ALA A 110     8456   7614   5500    540    156   -659       C  
ATOM    490  O   ALA A 110     -38.158  -4.887  62.748  1.00 57.59           O  
ANISOU  490  O   ALA A 110     8676   7676   5529    586    144   -697       O  
ATOM    491  CB  ALA A 110     -40.521  -4.893  60.332  1.00 54.16           C  
ANISOU  491  CB  ALA A 110     7860   7537   5181    758    186   -784       C  
ATOM    492  N   ASN A 111     -38.232  -6.729  61.467  1.00 52.65           N  
ANISOU  492  N   ASN A 111     7881   7111   5014    356    196   -565       N  
ATOM    493  CA  ASN A 111     -37.626  -7.587  62.490  1.00 52.41           C  
ANISOU  493  CA  ASN A 111     7931   7056   4928    210    225   -503       C  
ATOM    494  C   ASN A 111     -36.284  -6.992  62.977  1.00 54.48           C  
ANISOU  494  C   ASN A 111     8371   7118   5210    228    122   -479       C  
ATOM    495  O   ASN A 111     -36.058  -6.942  64.177  1.00 56.94           O  
ANISOU  495  O   ASN A 111     8775   7431   5428    213    131   -494       O  
ATOM    496  CB  ASN A 111     -37.465  -9.029  61.969  1.00 53.78           C  
ANISOU  496  CB  ASN A 111     8060   7229   5145     31    251   -405       C  
ATOM    497  CG  ASN A 111     -36.874 -10.027  62.934  1.00 71.79           C  
ANISOU  497  CG  ASN A 111    10448   9467   7361   -113    264   -334       C  
ATOM    498  OD1 ASN A 111     -37.478 -10.389  63.944  1.00 65.32           O  
ANISOU  498  OD1 ASN A 111     9635   8769   6415   -175    346   -351       O  
ATOM    499  ND2 ASN A 111     -35.690 -10.531  62.617  1.00 63.63           N  
ANISOU  499  ND2 ASN A 111     9503   8268   6405   -167    182   -254       N  
ATOM    500  N   GLU A 112     -35.444  -6.479  62.070  1.00 47.94           N  
ANISOU  500  N   GLU A 112     7590   6135   4488    253     27   -451       N  
ATOM    501  CA  GLU A 112     -34.144  -5.901  62.415  1.00 47.63           C  
ANISOU  501  CA  GLU A 112     7695   5928   4473    243    -74   -430       C  
ATOM    502  C   GLU A 112     -34.306  -4.648  63.289  1.00 52.93           C  
ANISOU  502  C   GLU A 112     8483   6573   5057    364   -105   -520       C  
ATOM    503  O   GLU A 112     -33.824  -4.614  64.437  1.00 53.27           O  
ANISOU  503  O   GLU A 112     8627   6589   5026    335   -124   -526       O  
ATOM    504  CB  GLU A 112     -33.325  -5.593  61.133  1.00 48.23           C  
ANISOU  504  CB  GLU A 112     7778   5876   4670    222   -152   -386       C  
ATOM    505  CG  GLU A 112     -31.922  -5.035  61.376  1.00 57.03           C  
ANISOU  505  CG  GLU A 112     9012   6844   5813    175   -254   -364       C  
ATOM    506  CD  GLU A 112     -31.010  -5.933  62.193  1.00 82.37           C  
ANISOU  506  CD  GLU A 112    12240  10045   9012     76   -274   -311       C  
ATOM    507  OE1 GLU A 112     -30.971  -7.157  61.922  1.00 74.99           O1-
ANISOU  507  OE1 GLU A 112    11229   9154   8109     10   -237   -254       O1-
ATOM    508  OE2 GLU A 112     -30.344  -5.412  63.118  1.00 83.58           O  
ANISOU  508  OE2 GLU A 112    12499  10140   9117     70   -339   -330       O  
ATOM    509  N   LEU A 113     -35.020  -3.639  62.742  1.00 49.57           N  
ANISOU  509  N   LEU A 113     8056   6150   4630    510   -118   -594       N  
ATOM    510  CA  LEU A 113     -35.312  -2.356  63.395  1.00 50.08           C  
ANISOU  510  CA  LEU A 113     8247   6174   4607    665   -157   -697       C  
ATOM    511  C   LEU A 113     -35.944  -2.507  64.791  1.00 57.77           C  
ANISOU  511  C   LEU A 113     9221   7287   5443    706    -74   -764       C  
ATOM    512  O   LEU A 113     -35.525  -1.806  65.716  1.00 59.89           O  
ANISOU  512  O   LEU A 113     9648   7475   5635    747   -123   -810       O  
ATOM    513  CB  LEU A 113     -36.187  -1.465  62.491  1.00 49.19           C  
ANISOU  513  CB  LEU A 113     8116   6067   4507    842   -181   -768       C  
ATOM    514  CG  LEU A 113     -35.632  -1.092  61.121  1.00 50.14           C  
ANISOU  514  CG  LEU A 113     8281   6035   4734    815   -269   -711       C  
ATOM    515  CD1 LEU A 113     -36.574  -0.193  60.402  1.00 50.48           C  
ANISOU  515  CD1 LEU A 113     8337   6080   4761   1012   -307   -789       C  
ATOM    516  CD2 LEU A 113     -34.256  -0.425  61.214  1.00 50.10           C  
ANISOU  516  CD2 LEU A 113     8471   5815   4749    723   -378   -670       C  
ATOM    517  N   MET A 114     -36.875  -3.475  64.949  1.00 54.57           N  
ANISOU  517  N   MET A 114     8648   7089   4999    666     50   -765       N  
ATOM    518  CA  MET A 114     -37.623  -3.738  66.179  1.00 56.44           C  
ANISOU  518  CA  MET A 114     8855   7501   5089    677    158   -827       C  
ATOM    519  C   MET A 114     -36.920  -4.558  67.247  1.00 60.13           C  
ANISOU  519  C   MET A 114     9412   7945   5490    513    174   -757       C  
ATOM    520  O   MET A 114     -37.330  -4.502  68.409  1.00 60.94           O  
ANISOU  520  O   MET A 114     9556   8148   5449    530    242   -815       O  
ATOM    521  CB  MET A 114     -38.944  -4.406  65.853  1.00 59.99           C  
ANISOU  521  CB  MET A 114     9082   8201   5512    673    287   -858       C  
ATOM    522  CG  MET A 114     -39.832  -3.552  65.056  1.00 64.92           C  
ANISOU  522  CG  MET A 114     9609   8895   6164    874    273   -955       C  
ATOM    523  SD  MET A 114     -41.491  -4.121  65.300  1.00 72.03           S  
ANISOU  523  SD  MET A 114    10242  10164   6963    893    441  -1043       S  
ATOM    524  CE  MET A 114     -42.192  -3.579  63.764  1.00 69.21           C  
ANISOU  524  CE  MET A 114     9746   9837   6714   1063    376  -1090       C  
ATOM    525  N   ALA A 115     -35.894  -5.341  66.875  1.00 55.32           N  
ANISOU  525  N   ALA A 115     8835   7213   4973    364    113   -639       N  
ATOM    526  CA  ALA A 115     -35.148  -6.192  67.818  1.00 54.69           C  
ANISOU  526  CA  ALA A 115     8852   7092   4834    223    100   -565       C  
ATOM    527  C   ALA A 115     -35.983  -7.422  68.312  1.00 62.36           C  
ANISOU  527  C   ALA A 115     9751   8236   5705     98    231   -534       C  
ATOM    528  O   ALA A 115     -35.594  -8.117  69.276  1.00 63.30           O  
ANISOU  528  O   ALA A 115     9980   8340   5731    -10    234   -483       O  
ATOM    529  CB  ALA A 115     -34.605  -5.364  68.987  1.00 55.38           C  
ANISOU  529  CB  ALA A 115     9116   7102   4824    277     38   -617       C  
ATOM    530  N   TYR A 116     -37.118  -7.704  67.609  1.00 58.21           N  
ANISOU  530  N   TYR A 116     9049   7873   5195    101    332   -561       N  
ATOM    531  CA  TYR A 116     -38.009  -8.830  67.886  1.00 57.64           C  
ANISOU  531  CA  TYR A 116     8889   7982   5031    -46    461   -534       C  
ATOM    532  C   TYR A 116     -39.029  -9.026  66.764  1.00 60.78           C  
ANISOU  532  C   TYR A 116     9076   8524   5493    -40    526   -559       C  
ATOM    533  O   TYR A 116     -39.254  -8.123  65.940  1.00 59.96           O  
ANISOU  533  O   TYR A 116     8892   8413   5475    121    485   -621       O  
ATOM    534  CB  TYR A 116     -38.666  -8.764  69.301  1.00 59.19           C  
ANISOU  534  CB  TYR A 116     9125   8339   5026    -66    570   -597       C  
ATOM    535  CG  TYR A 116     -39.884  -7.879  69.428  1.00 61.67           C  
ANISOU  535  CG  TYR A 116     9293   8872   5268     88    669   -743       C  
ATOM    536  CD1 TYR A 116     -41.161  -8.382  69.205  1.00 64.98           C  
ANISOU  536  CD1 TYR A 116     9504   9555   5630     24    810   -783       C  
ATOM    537  CD2 TYR A 116     -39.767  -6.555  69.831  1.00 63.00           C  
ANISOU  537  CD2 TYR A 116     9536   8994   5410    297    621   -850       C  
ATOM    538  CE1 TYR A 116     -42.289  -7.570  69.315  1.00 68.36           C  
ANISOU  538  CE1 TYR A 116     9769  10215   5990    192    897   -933       C  
ATOM    539  CE2 TYR A 116     -40.889  -5.742  69.986  1.00 65.85           C  
ANISOU  539  CE2 TYR A 116     9771   9557   5692    475    705   -999       C  
ATOM    540  CZ  TYR A 116     -42.150  -6.251  69.720  1.00 76.75           C  
ANISOU  540  CZ  TYR A 116    10914  11221   7027    433    844  -1044       C  
ATOM    541  OH  TYR A 116     -43.264  -5.457  69.896  1.00 79.49           O  
ANISOU  541  OH  TYR A 116    11112  11799   7292    632    925  -1206       O  
ATOM    542  N   TRP A 117     -39.624 -10.233  66.731  1.00 57.16           N  
ANISOU  542  N   TRP A 117     8547   8188   4984   -226    617   -505       N  
ATOM    543  CA  TRP A 117     -40.637 -10.605  65.758  1.00 57.10           C  
ANISOU  543  CA  TRP A 117     8336   8342   5017   -265    682   -523       C  
ATOM    544  C   TRP A 117     -41.994 -10.266  66.336  1.00 65.35           C  
ANISOU  544  C   TRP A 117     9216   9688   5928   -231    821   -640       C  
ATOM    545  O   TRP A 117     -42.392 -10.820  67.370  1.00 67.41           O  
ANISOU  545  O   TRP A 117     9501  10080   6031   -373    927   -637       O  
ATOM    546  CB  TRP A 117     -40.539 -12.091  65.412  1.00 54.84           C  
ANISOU  546  CB  TRP A 117     8080   8021   4737   -503    698   -407       C  
ATOM    547  CG  TRP A 117     -41.472 -12.502  64.322  1.00 55.22           C  
ANISOU  547  CG  TRP A 117     7934   8211   4835   -560    743   -419       C  
ATOM    548  CD1 TRP A 117     -42.612 -13.237  64.451  1.00 59.82           C  
ANISOU  548  CD1 TRP A 117     8385   9028   5314   -733    865   -433       C  
ATOM    549  CD2 TRP A 117     -41.363 -12.165  62.935  1.00 53.63           C  
ANISOU  549  CD2 TRP A 117     7648   7940   4790   -456    664   -423       C  
ATOM    550  NE1 TRP A 117     -43.211 -13.399  63.223  1.00 58.90           N  
ANISOU  550  NE1 TRP A 117     8101   8991   5287   -739    857   -447       N  
ATOM    551  CE2 TRP A 117     -42.465 -12.749  62.275  1.00 58.52           C  
ANISOU  551  CE2 TRP A 117     8086   8753   5396   -563    734   -440       C  
ATOM    552  CE3 TRP A 117     -40.425 -11.447  62.181  1.00 52.81           C  
ANISOU  552  CE3 TRP A 117     7611   7631   4823   -304    542   -411       C  
ATOM    553  CZ2 TRP A 117     -42.657 -12.631  60.899  1.00 57.15           C  
ANISOU  553  CZ2 TRP A 117     7805   8565   5343   -503    676   -446       C  
ATOM    554  CZ3 TRP A 117     -40.637 -11.300  60.830  1.00 53.85           C  
ANISOU  554  CZ3 TRP A 117     7642   7754   5067   -249    497   -417       C  
ATOM    555  CH2 TRP A 117     -41.733 -11.905  60.197  1.00 55.55           C  
ANISOU  555  CH2 TRP A 117     7687   8152   5268   -341    559   -432       C  
ATOM    556  N   TYR A 118     -42.690  -9.337  65.677  1.00 61.63           N  
ANISOU  556  N   TYR A 118     8580   9328   5508    -34    816   -747       N  
ATOM    557  CA  TYR A 118     -43.975  -8.811  66.115  1.00 63.30           C  
ANISOU  557  CA  TYR A 118     8601   9844   5606     70    931   -889       C  
ATOM    558  C   TYR A 118     -45.188  -9.515  65.465  1.00 67.91           C  
ANISOU  558  C   TYR A 118     8922  10703   6177    -47   1027   -912       C  
ATOM    559  O   TYR A 118     -46.248  -9.612  66.075  1.00 70.15           O  
ANISOU  559  O   TYR A 118     9036  11293   6326    -86   1165  -1001       O  
ATOM    560  CB  TYR A 118     -43.959  -7.282  65.845  1.00 65.13           C  
ANISOU  560  CB  TYR A 118     8840  10014   5891    394    842  -1005       C  
ATOM    561  CG  TYR A 118     -45.285  -6.566  65.961  1.00 70.60           C  
ANISOU  561  CG  TYR A 118     9315  11007   6503    590    922  -1175       C  
ATOM    562  CD1 TYR A 118     -45.717  -6.050  67.179  1.00 75.32           C  
ANISOU  562  CD1 TYR A 118     9916  11761   6942    687   1014  -1289       C  
ATOM    563  CD2 TYR A 118     -46.101  -6.381  64.847  1.00 71.95           C  
ANISOU  563  CD2 TYR A 118     9275  11313   6750    697    899  -1231       C  
ATOM    564  CE1 TYR A 118     -46.950  -5.411  67.297  1.00 79.37           C  
ANISOU  564  CE1 TYR A 118    10207  12577   7372    890   1092  -1463       C  
ATOM    565  CE2 TYR A 118     -47.341  -5.755  64.955  1.00 75.30           C  
ANISOU  565  CE2 TYR A 118     9473  12040   7096    898    964  -1399       C  
ATOM    566  CZ  TYR A 118     -47.754  -5.254  66.179  1.00 85.56           C  
ANISOU  566  CZ  TYR A 118    10765  13504   8239   1005   1062  -1520       C  
ATOM    567  OH  TYR A 118     -48.966  -4.615  66.292  1.00 89.19           O  
ANISOU  567  OH  TYR A 118    10989  14282   8618   1234   1126  -1703       O  
ATOM    568  N   PHE A 119     -45.015 -10.028  64.252  1.00 63.45           N  
ANISOU  568  N   PHE A 119     8323  10041   5744   -118    956   -836       N  
ATOM    569  CA  PHE A 119     -46.050 -10.573  63.365  1.00 64.34           C  
ANISOU  569  CA  PHE A 119     8197  10372   5878   -206   1002   -856       C  
ATOM    570  C   PHE A 119     -46.656 -11.979  63.725  1.00 70.28           C  
ANISOU  570  C   PHE A 119     8882  11304   6516   -548   1130   -796       C  
ATOM    571  O   PHE A 119     -47.519 -12.479  62.983  1.00 70.18           O  
ANISOU  571  O   PHE A 119     8671  11479   6515   -653   1164   -812       O  
ATOM    572  CB  PHE A 119     -45.497 -10.568  61.930  1.00 64.07           C  
ANISOU  572  CB  PHE A 119     8200  10125   6019   -156    864   -791       C  
ATOM    573  CG  PHE A 119     -44.780  -9.272  61.610  1.00 64.20           C  
ANISOU  573  CG  PHE A 119     8333   9932   6129    121    738   -826       C  
ATOM    574  CD1 PHE A 119     -45.481  -8.169  61.141  1.00 68.29           C  
ANISOU  574  CD1 PHE A 119     8722  10559   6667    381    698   -949       C  
ATOM    575  CD2 PHE A 119     -43.413  -9.140  61.829  1.00 63.86           C  
ANISOU  575  CD2 PHE A 119     8536   9588   6139    119    653   -742       C  
ATOM    576  CE1 PHE A 119     -44.821  -6.969  60.860  1.00 68.35           C  
ANISOU  576  CE1 PHE A 119     8880  10348   6742    615    573   -976       C  
ATOM    577  CE2 PHE A 119     -42.760  -7.935  61.566  1.00 65.85           C  
ANISOU  577  CE2 PHE A 119     8904   9653   6461    336    540   -774       C  
ATOM    578  CZ  PHE A 119     -43.468  -6.860  61.080  1.00 65.13           C  
ANISOU  578  CZ  PHE A 119     8719   9646   6383    573    501   -886       C  
ATOM    579  N   GLY A 120     -46.268 -12.551  64.870  1.00 67.50           N  
ANISOU  579  N   GLY A 120     8699  10906   6042   -719   1195   -735       N  
ATOM    580  CA  GLY A 120     -46.790 -13.834  65.329  1.00 67.98           C  
ANISOU  580  CA  GLY A 120     8753  11108   5966  -1058   1312   -671       C  
ATOM    581  C   GLY A 120     -46.141 -15.067  64.738  1.00 70.68           C  
ANISOU  581  C   GLY A 120     9273  11216   6367  -1285   1241   -517       C  
ATOM    582  O   GLY A 120     -45.591 -15.028  63.634  1.00 68.54           O  
ANISOU  582  O   GLY A 120     9032  10754   6258  -1195   1119   -477       O  
ATOM    583  N   GLN A 121     -46.243 -16.184  65.474  1.00 69.97           N  
ANISOU  583  N   GLN A 121     9313  11145   6129  -1585   1319   -435       N  
ATOM    584  CA  GLN A 121     -45.678 -17.503  65.163  1.00 70.06           C  
ANISOU  584  CA  GLN A 121     9547  10928   6144  -1826   1259   -288       C  
ATOM    585  C   GLN A 121     -46.025 -18.039  63.778  1.00 75.11           C  
ANISOU  585  C   GLN A 121    10077  11566   6894  -1903   1210   -266       C  
ATOM    586  O   GLN A 121     -45.160 -18.649  63.149  1.00 72.65           O  
ANISOU  586  O   GLN A 121     9955  10973   6677  -1926   1095   -170       O  
ATOM    587  CB  GLN A 121     -46.061 -18.528  66.237  1.00 73.79           C  
ANISOU  587  CB  GLN A 121    10156  11484   6396  -2154   1371   -224       C  
ATOM    588  CG  GLN A 121     -45.578 -18.134  67.635  1.00104.33           C  
ANISOU  588  CG  GLN A 121    14192  15310  10140  -2097   1403   -226       C  
ATOM    589  CD  GLN A 121     -46.190 -18.960  68.740  1.00133.64           C  
ANISOU  589  CD  GLN A 121    17999  19176  13601  -2418   1545   -188       C  
ATOM    590  OE1 GLN A 121     -45.528 -19.814  69.337  1.00132.48           O  
ANISOU  590  OE1 GLN A 121    18169  18807  13359  -2582   1498    -66       O  
ATOM    591  NE2 GLN A 121     -47.459 -18.710  69.055  1.00127.03           N  
ANISOU  591  NE2 GLN A 121    16894  18731  12640  -2512   1718   -294       N  
ATOM    592  N   TRP A 122     -47.279 -17.818  63.308  1.00 74.60           N  
ANISOU  592  N   TRP A 122     9705  11825   6813  -1934   1293   -364       N  
ATOM    593  CA  TRP A 122     -47.745 -18.287  62.004  1.00 74.43           C  
ANISOU  593  CA  TRP A 122     9557  11841   6881  -2016   1248   -356       C  
ATOM    594  C   TRP A 122     -47.017 -17.579  60.873  1.00 77.80           C  
ANISOU  594  C   TRP A 122     9989  12057   7513  -1731   1100   -364       C  
ATOM    595  O   TRP A 122     -46.429 -18.238  60.004  1.00 77.25           O  
ANISOU  595  O   TRP A 122    10057  11761   7532  -1790   1005   -280       O  
ATOM    596  CB  TRP A 122     -49.271 -18.146  61.842  1.00 75.63           C  
ANISOU  596  CB  TRP A 122     9354  12424   6959  -2103   1364   -472       C  
ATOM    597  CG  TRP A 122     -49.749 -18.574  60.477  1.00 76.84           C  
ANISOU  597  CG  TRP A 122     9373  12618   7203  -2178   1300   -470       C  
ATOM    598  CD1 TRP A 122     -49.949 -19.852  60.051  1.00 80.44           C  
ANISOU  598  CD1 TRP A 122     9922  13030   7613  -2505   1297   -382       C  
ATOM    599  CD2 TRP A 122     -49.972 -17.730  59.331  1.00 75.46           C  
ANISOU  599  CD2 TRP A 122     9002  12491   7179  -1914   1208   -551       C  
ATOM    600  NE1 TRP A 122     -50.300 -19.858  58.722  1.00 79.68           N  
ANISOU  600  NE1 TRP A 122     9681  12964   7629  -2464   1215   -409       N  
ATOM    601  CE2 TRP A 122     -50.348 -18.568  58.262  1.00 79.73           C  
ANISOU  601  CE2 TRP A 122     9502  13038   7755  -2105   1161   -512       C  
ATOM    602  CE3 TRP A 122     -49.924 -16.344  59.114  1.00 76.10           C  
ANISOU  602  CE3 TRP A 122     8955  12603   7354  -1540   1155   -654       C  
ATOM    603  CZ2 TRP A 122     -50.664 -18.072  56.993  1.00 78.53           C  
ANISOU  603  CZ2 TRP A 122     9179  12932   7728  -1932   1064   -570       C  
ATOM    604  CZ3 TRP A 122     -50.253 -15.850  57.863  1.00 77.27           C  
ANISOU  604  CZ3 TRP A 122     8946  12789   7622  -1369   1057   -708       C  
ATOM    605  CH2 TRP A 122     -50.596 -16.711  56.813  1.00 78.10           C  
ANISOU  605  CH2 TRP A 122     9009  12904   7761  -1562   1011   -664       C  
ATOM    606  N   TRP A 123     -47.056 -16.240  60.878  1.00 73.73           N  
ANISOU  606  N   TRP A 123     9340  11611   7061  -1425   1081   -467       N  
ATOM    607  CA  TRP A 123     -46.381 -15.479  59.843  1.00 70.80           C  
ANISOU  607  CA  TRP A 123     8991  11044   6864  -1170    945   -473       C  
ATOM    608  C   TRP A 123     -44.866 -15.673  59.925  1.00 73.75           C  
ANISOU  608  C   TRP A 123     9662  11051   7311  -1135    848   -366       C  
ATOM    609  O   TRP A 123     -44.196 -15.538  58.901  1.00 72.63           O  
ANISOU  609  O   TRP A 123     9577  10718   7302  -1035    742   -333       O  
ATOM    610  CB  TRP A 123     -46.810 -14.007  59.811  1.00 69.23           C  
ANISOU  610  CB  TRP A 123     8617  10986   6700   -859    934   -607       C  
ATOM    611  CG  TRP A 123     -46.227 -13.272  58.649  1.00 68.50           C  
ANISOU  611  CG  TRP A 123     8560  10699   6768   -636    794   -606       C  
ATOM    612  CD1 TRP A 123     -45.266 -12.307  58.703  1.00 70.27           C  
ANISOU  612  CD1 TRP A 123     8932  10703   7065   -417    708   -606       C  
ATOM    613  CD2 TRP A 123     -46.410 -13.580  57.252  1.00 67.40           C  
ANISOU  613  CD2 TRP A 123     8354  10530   6723   -658    720   -584       C  
ATOM    614  NE1 TRP A 123     -44.892 -11.938  57.426  1.00 68.69           N  
ANISOU  614  NE1 TRP A 123     8751  10354   6993   -301    594   -589       N  
ATOM    615  CE2 TRP A 123     -45.583 -12.702  56.518  1.00 69.78           C  
ANISOU  615  CE2 TRP A 123     8761  10606   7147   -435    598   -576       C  
ATOM    616  CE3 TRP A 123     -47.224 -14.483  56.547  1.00 69.19           C  
ANISOU  616  CE3 TRP A 123     8447  10909   6934   -855    742   -573       C  
ATOM    617  CZ2 TRP A 123     -45.554 -12.696  55.120  1.00 68.00           C  
ANISOU  617  CZ2 TRP A 123     8513  10305   7021   -394    507   -558       C  
ATOM    618  CZ3 TRP A 123     -47.200 -14.468  55.164  1.00 69.48           C  
ANISOU  618  CZ3 TRP A 123     8457  10868   7075   -801    642   -561       C  
ATOM    619  CH2 TRP A 123     -46.358 -13.599  54.465  1.00 68.54           C  
ANISOU  619  CH2 TRP A 123     8450  10520   7070   -572    528   -551       C  
ATOM    620  N   CYS A 124     -44.330 -16.097  61.099  1.00 69.84           N  
ANISOU  620  N   CYS A 124     9354  10467   6717  -1238    884   -310       N  
ATOM    621  CA  CYS A 124     -42.901 -16.402  61.182  1.00 67.36           C  
ANISOU  621  CA  CYS A 124     9303   9827   6464  -1211    781   -212       C  
ATOM    622  C   CYS A 124     -42.551 -17.592  60.261  1.00 67.78           C  
ANISOU  622  C   CYS A 124     9465   9718   6570  -1365    721   -119       C  
ATOM    623  O   CYS A 124     -41.608 -17.494  59.475  1.00 66.11           O  
ANISOU  623  O   CYS A 124     9335   9298   6488  -1248    616    -85       O  
ATOM    624  CB  CYS A 124     -42.443 -16.644  62.617  1.00 68.09           C  
ANISOU  624  CB  CYS A 124     9579   9863   6429  -1283    814   -173       C  
ATOM    625  SG  CYS A 124     -40.718 -17.187  62.757  1.00 70.50           S  
ANISOU  625  SG  CYS A 124    10192   9797   6797  -1257    674    -58       S  
ATOM    626  N   GLY A 125     -43.348 -18.658  60.340  1.00 62.99           N  
ANISOU  626  N   GLY A 125     8854   9222   5856  -1629    790    -87       N  
ATOM    627  CA  GLY A 125     -43.173 -19.878  59.562  1.00 61.99           C  
ANISOU  627  CA  GLY A 125     8857   8951   5747  -1804    739     -5       C  
ATOM    628  C   GLY A 125     -43.363 -19.675  58.079  1.00 64.50           C  
ANISOU  628  C   GLY A 125     9036   9272   6198  -1719    681    -36       C  
ATOM    629  O   GLY A 125     -42.635 -20.262  57.270  1.00 62.45           O  
ANISOU  629  O   GLY A 125     8918   8796   6015  -1718    593     21       O  
ATOM    630  N   VAL A 126     -44.344 -18.825  57.718  1.00 61.16           N  
ANISOU  630  N   VAL A 126     8340   9102   5795  -1633    727   -135       N  
ATOM    631  CA  VAL A 126     -44.636 -18.513  56.325  1.00 59.48           C  
ANISOU  631  CA  VAL A 126     7987   8917   5695  -1538    666   -173       C  
ATOM    632  C   VAL A 126     -43.540 -17.605  55.787  1.00 62.66           C  
ANISOU  632  C   VAL A 126     8458   9112   6237  -1269    567   -173       C  
ATOM    633  O   VAL A 126     -43.058 -17.841  54.679  1.00 63.33           O  
ANISOU  633  O   VAL A 126     8600   9049   6414  -1239    489   -141       O  
ATOM    634  CB  VAL A 126     -46.067 -17.960  56.090  1.00 64.53           C  
ANISOU  634  CB  VAL A 126     8315   9903   6301  -1526    727   -281       C  
ATOM    635  CG1 VAL A 126     -46.304 -17.677  54.613  1.00 64.23           C  
ANISOU  635  CG1 VAL A 126     8165   9867   6374  -1423    641   -311       C  
ATOM    636  CG2 VAL A 126     -47.127 -18.928  56.598  1.00 66.48           C  
ANISOU  636  CG2 VAL A 126     8482  10379   6400  -1839    834   -279       C  
ATOM    637  N   TYR A 127     -43.103 -16.611  56.580  1.00 57.56           N  
ANISOU  637  N   TYR A 127     7825   8449   5596  -1092    571   -207       N  
ATOM    638  CA  TYR A 127     -42.048 -15.679  56.169  1.00 55.53           C  
ANISOU  638  CA  TYR A 127     7640   8003   5455   -866    480   -208       C  
ATOM    639  C   TYR A 127     -40.711 -16.379  55.900  1.00 57.57           C  
ANISOU  639  C   TYR A 127     8113   7990   5773   -900    409   -116       C  
ATOM    640  O   TYR A 127     -40.069 -16.084  54.896  1.00 55.38           O  
ANISOU  640  O   TYR A 127     7856   7585   5599   -799    337   -106       O  
ATOM    641  CB  TYR A 127     -41.913 -14.530  57.182  1.00 56.91           C  
ANISOU  641  CB  TYR A 127     7805   8218   5601   -701    498   -266       C  
ATOM    642  CG  TYR A 127     -40.549 -13.878  57.266  1.00 57.01           C  
ANISOU  642  CG  TYR A 127     7971   7999   5690   -558    414   -238       C  
ATOM    643  CD1 TYR A 127     -40.129 -12.961  56.304  1.00 57.30           C  
ANISOU  643  CD1 TYR A 127     7997   7943   5832   -395    335   -260       C  
ATOM    644  CD2 TYR A 127     -39.710 -14.116  58.348  1.00 58.01           C  
ANISOU  644  CD2 TYR A 127     8256   8014   5773   -593    410   -194       C  
ATOM    645  CE1 TYR A 127     -38.890 -12.332  56.397  1.00 55.91           C  
ANISOU  645  CE1 TYR A 127     7950   7578   5715   -296    264   -237       C  
ATOM    646  CE2 TYR A 127     -38.476 -13.481  58.460  1.00 57.80           C  
ANISOU  646  CE2 TYR A 127     8344   7806   5812   -474    330   -178       C  
ATOM    647  CZ  TYR A 127     -38.073 -12.587  57.485  1.00 62.34           C  
ANISOU  647  CZ  TYR A 127     8892   8303   6491   -336    262   -200       C  
ATOM    648  OH  TYR A 127     -36.852 -11.979  57.605  1.00 63.78           O  
ANISOU  648  OH  TYR A 127     9182   8325   6728   -255    187   -184       O  
ATOM    649  N   LEU A 128     -40.318 -17.315  56.779  1.00 54.89           N  
ANISOU  649  N   LEU A 128     7929   7570   5356  -1039    427    -53       N  
ATOM    650  CA  LEU A 128     -39.075 -18.063  56.662  1.00 53.69           C  
ANISOU  650  CA  LEU A 128     7981   7176   5243  -1052    353     23       C  
ATOM    651  C   LEU A 128     -39.059 -19.024  55.479  1.00 57.78           C  
ANISOU  651  C   LEU A 128     8543   7610   5802  -1140    317     59       C  
ATOM    652  O   LEU A 128     -38.050 -19.076  54.765  1.00 57.53           O  
ANISOU  652  O   LEU A 128     8585   7413   5861  -1042    244     79       O  
ATOM    653  CB  LEU A 128     -38.734 -18.783  57.973  1.00 54.49           C  
ANISOU  653  CB  LEU A 128     8258   7212   5232  -1159    366     77       C  
ATOM    654  CG  LEU A 128     -38.281 -17.905  59.162  1.00 58.75           C  
ANISOU  654  CG  LEU A 128     8823   7758   5740  -1047    369     54       C  
ATOM    655  CD1 LEU A 128     -38.092 -18.746  60.390  1.00 60.31           C  
ANISOU  655  CD1 LEU A 128     9208   7902   5806  -1180    380    112       C  
ATOM    656  CD2 LEU A 128     -36.978 -17.185  58.882  1.00 58.68           C  
ANISOU  656  CD2 LEU A 128     8854   7593   5849   -858    274     51       C  
ATOM    657  N   ALA A 129     -40.186 -19.745  55.243  1.00 53.42           N  
ANISOU  657  N   ALA A 129     7936   7184   5177  -1327    368     58       N  
ATOM    658  CA  ALA A 129     -40.368 -20.706  54.150  1.00 51.60           C  
ANISOU  658  CA  ALA A 129     7754   6889   4961  -1442    336     85       C  
ATOM    659  C   ALA A 129     -40.253 -20.033  52.806  1.00 54.07           C  
ANISOU  659  C   ALA A 129     7953   7198   5393  -1295    290     45       C  
ATOM    660  O   ALA A 129     -39.598 -20.565  51.909  1.00 54.46           O  
ANISOU  660  O   ALA A 129     8108   7090   5496  -1278    231     72       O  
ATOM    661  CB  ALA A 129     -41.724 -21.362  54.264  1.00 53.78           C  
ANISOU  661  CB  ALA A 129     7954   7352   5128  -1683    406     78       C  
ATOM    662  N   LEU A 130     -40.904 -18.863  52.664  1.00 48.88           N  
ANISOU  662  N   LEU A 130     7094   6713   4766  -1181    313    -23       N  
ATOM    663  CA  LEU A 130     -40.930 -18.059  51.450  1.00 46.46           C  
ANISOU  663  CA  LEU A 130     6685   6417   4552  -1037    264    -63       C  
ATOM    664  C   LEU A 130     -39.559 -17.476  51.181  1.00 48.48           C  
ANISOU  664  C   LEU A 130     7042   6480   4897   -870    207    -43       C  
ATOM    665  O   LEU A 130     -39.024 -17.639  50.096  1.00 46.50           O  
ANISOU  665  O   LEU A 130     6840   6121   4707   -837    160    -29       O  
ATOM    666  CB  LEU A 130     -41.985 -16.936  51.560  1.00 46.99           C  
ANISOU  666  CB  LEU A 130     6537   6709   4607   -936    291   -145       C  
ATOM    667  CG  LEU A 130     -43.472 -17.351  51.560  1.00 53.36           C  
ANISOU  667  CG  LEU A 130     7167   7773   5334  -1084    345   -189       C  
ATOM    668  CD1 LEU A 130     -44.381 -16.149  51.677  1.00 53.66           C  
ANISOU  668  CD1 LEU A 130     6987   8034   5366   -923    358   -286       C  
ATOM    669  CD2 LEU A 130     -43.833 -18.193  50.341  1.00 55.75           C  
ANISOU  669  CD2 LEU A 130     7469   8064   5649  -1213    305   -170       C  
ATOM    670  N   ASP A 131     -38.965 -16.840  52.177  1.00 46.58           N  
ANISOU  670  N   ASP A 131     6837   6205   4655   -780    213    -45       N  
ATOM    671  CA  ASP A 131     -37.647 -16.239  52.045  1.00 46.35           C  
ANISOU  671  CA  ASP A 131     6888   6019   4701   -647    160    -31       C  
ATOM    672  C   ASP A 131     -36.664 -17.221  51.370  1.00 51.88           C  
ANISOU  672  C   ASP A 131     7715   6557   5441   -683    120     17       C  
ATOM    673  O   ASP A 131     -36.072 -16.911  50.328  1.00 53.64           O  
ANISOU  673  O   ASP A 131     7937   6710   5732   -611     86     13       O  
ATOM    674  CB  ASP A 131     -37.196 -15.724  53.410  1.00 48.12           C  
ANISOU  674  CB  ASP A 131     7156   6233   4894   -596    170    -34       C  
ATOM    675  CG  ASP A 131     -35.717 -15.680  53.598  1.00 58.65           C  
ANISOU  675  CG  ASP A 131     8602   7403   6277   -533    115     -2       C  
ATOM    676  OD1 ASP A 131     -35.107 -14.680  53.213  1.00 59.70           O1-
ANISOU  676  OD1 ASP A 131     8717   7493   6472   -424     79    -22       O1-
ATOM    677  OD2 ASP A 131     -35.173 -16.652  54.107  1.00 67.78           O  
ANISOU  677  OD2 ASP A 131     9871   8478   7405   -595    102     41       O  
ATOM    678  N   VAL A 132     -36.595 -18.426  51.904  1.00 47.25           N  
ANISOU  678  N   VAL A 132     7240   5915   4796   -799    127     58       N  
ATOM    679  CA  VAL A 132     -35.820 -19.538  51.360  1.00 46.39           C  
ANISOU  679  CA  VAL A 132     7272   5652   4701   -827     85     94       C  
ATOM    680  C   VAL A 132     -36.386 -19.970  49.974  1.00 51.96           C  
ANISOU  680  C   VAL A 132     7948   6371   5422   -884     82     83       C  
ATOM    681  O   VAL A 132     -35.581 -20.102  49.043  1.00 52.37           O  
ANISOU  681  O   VAL A 132     8044   6323   5530   -811     47     80       O  
ATOM    682  CB  VAL A 132     -35.761 -20.700  52.403  1.00 48.63           C  
ANISOU  682  CB  VAL A 132     7722   5863   4893   -941     80    141       C  
ATOM    683  CG1 VAL A 132     -35.393 -22.028  51.775  1.00 47.55           C  
ANISOU  683  CG1 VAL A 132     7751   5578   4740   -996     35    171       C  
ATOM    684  CG2 VAL A 132     -34.805 -20.359  53.545  1.00 47.67           C  
ANISOU  684  CG2 VAL A 132     7662   5681   4769   -848     52    155       C  
ATOM    685  N   LEU A 133     -37.760 -20.138  49.834  1.00 47.76           N  
ANISOU  685  N   LEU A 133     7330   5981   4835  -1012    118     68       N  
ATOM    686  CA  LEU A 133     -38.443 -20.549  48.586  1.00 45.71           C  
ANISOU  686  CA  LEU A 133     7035   5756   4577  -1086    106     53       C  
ATOM    687  C   LEU A 133     -38.164 -19.646  47.439  1.00 46.63           C  
ANISOU  687  C   LEU A 133     7072   5871   4773   -947     77     22       C  
ATOM    688  O   LEU A 133     -37.663 -20.108  46.438  1.00 45.96           O  
ANISOU  688  O   LEU A 133     7066   5684   4713   -936     46     28       O  
ATOM    689  CB  LEU A 133     -39.958 -20.761  48.729  1.00 46.55           C  
ANISOU  689  CB  LEU A 133     7023   6053   4609  -1248    145     33       C  
ATOM    690  CG  LEU A 133     -40.730 -21.113  47.427  1.00 51.19           C  
ANISOU  690  CG  LEU A 133     7556   6699   5195  -1329    118     11       C  
ATOM    691  CD1 LEU A 133     -40.338 -22.496  46.880  1.00 51.84           C  
ANISOU  691  CD1 LEU A 133     7846   6607   5245  -1450     82     49       C  
ATOM    692  CD2 LEU A 133     -42.211 -21.090  47.658  1.00 53.87           C  
ANISOU  692  CD2 LEU A 133     7721   7281   5468  -1467    156    -24       C  
ATOM    693  N   PHE A 134     -38.465 -18.374  47.563  1.00 43.90           N  
ANISOU  693  N   PHE A 134     6595   5629   4456   -840     84    -11       N  
ATOM    694  CA  PHE A 134     -38.189 -17.416  46.504  1.00 43.56           C  
ANISOU  694  CA  PHE A 134     6509   5569   4472   -714     48    -34       C  
ATOM    695  C   PHE A 134     -36.686 -17.322  46.132  1.00 49.22           C  
ANISOU  695  C   PHE A 134     7333   6124   5245   -631     29    -12       C  
ATOM    696  O   PHE A 134     -36.365 -17.181  44.951  1.00 50.41           O  
ANISOU  696  O   PHE A 134     7503   6229   5421   -598      7    -16       O  
ATOM    697  CB  PHE A 134     -38.780 -16.064  46.861  1.00 45.13           C  
ANISOU  697  CB  PHE A 134     6585   5885   4675   -604     46    -75       C  
ATOM    698  CG  PHE A 134     -40.268 -16.113  47.089  1.00 47.58           C  
ANISOU  698  CG  PHE A 134     6751   6397   4932   -663     65   -116       C  
ATOM    699  CD1 PHE A 134     -41.105 -16.764  46.188  1.00 49.83           C  
ANISOU  699  CD1 PHE A 134     6984   6757   5193   -763     48   -127       C  
ATOM    700  CD2 PHE A 134     -40.843 -15.457  48.172  1.00 50.94           C  
ANISOU  700  CD2 PHE A 134     7080   6953   5324   -612     99   -155       C  
ATOM    701  CE1 PHE A 134     -42.482 -16.772  46.374  1.00 51.54           C  
ANISOU  701  CE1 PHE A 134     7032   7195   5357   -823     63   -174       C  
ATOM    702  CE2 PHE A 134     -42.226 -15.465  48.355  1.00 54.43           C  
ANISOU  702  CE2 PHE A 134     7352   7620   5709   -657    125   -208       C  
ATOM    703  CZ  PHE A 134     -43.033 -16.132  47.459  1.00 52.25           C  
ANISOU  703  CZ  PHE A 134     7005   7434   5415   -767    107   -217       C  
ATOM    704  N   CYS A 135     -35.777 -17.486  47.105  1.00 45.65           N  
ANISOU  704  N   CYS A 135     6946   5599   4801   -608     37      9       N  
ATOM    705  CA  CYS A 135     -34.344 -17.509  46.818  1.00 46.10           C  
ANISOU  705  CA  CYS A 135     7074   5539   4905   -536     20     19       C  
ATOM    706  C   CYS A 135     -33.991 -18.741  45.992  1.00 52.89           C  
ANISOU  706  C   CYS A 135     8026   6312   5755   -577     11     27       C  
ATOM    707  O   CYS A 135     -33.228 -18.627  45.022  1.00 53.91           O  
ANISOU  707  O   CYS A 135     8170   6396   5918   -521      6     14       O  
ATOM    708  CB  CYS A 135     -33.521 -17.472  48.098  1.00 46.75           C  
ANISOU  708  CB  CYS A 135     7195   5580   4990   -500     15     34       C  
ATOM    709  SG  CYS A 135     -31.733 -17.465  47.802  1.00 50.44           S  
ANISOU  709  SG  CYS A 135     7700   5949   5514   -407    -11     31       S  
ATOM    710  N   THR A 136     -34.523 -19.926  46.416  1.00 48.84           N  
ANISOU  710  N   THR A 136     7596   5776   5187   -680      9     45       N  
ATOM    711  CA  THR A 136     -34.329 -21.232  45.780  1.00 48.26           C  
ANISOU  711  CA  THR A 136     7655   5597   5083   -728    -12     49       C  
ATOM    712  C   THR A 136     -34.896 -21.282  44.360  1.00 52.52           C  
ANISOU  712  C   THR A 136     8172   6164   5621   -765    -15     27       C  
ATOM    713  O   THR A 136     -34.236 -21.845  43.498  1.00 52.82           O  
ANISOU  713  O   THR A 136     8295   6112   5662   -726    -29     13       O  
ATOM    714  CB  THR A 136     -34.884 -22.340  46.658  1.00 53.03           C  
ANISOU  714  CB  THR A 136     8376   6163   5610   -858    -20     81       C  
ATOM    715  OG1 THR A 136     -34.303 -22.254  47.964  1.00 48.32           O  
ANISOU  715  OG1 THR A 136     7817   5536   5006   -814    -25    103       O  
ATOM    716  CG2 THR A 136     -34.654 -23.706  46.071  1.00 52.67           C  
ANISOU  716  CG2 THR A 136     8514   5976   5521   -903    -58     84       C  
ATOM    717  N   SER A 137     -36.101 -20.698  44.106  1.00 49.17           N  
ANISOU  717  N   SER A 137     7631   5869   5183   -827     -7     18       N  
ATOM    718  CA  SER A 137     -36.693 -20.693  42.764  1.00 48.73           C  
ANISOU  718  CA  SER A 137     7551   5846   5117   -858    -26     -4       C  
ATOM    719  C   SER A 137     -35.888 -19.862  41.815  1.00 53.73           C  
ANISOU  719  C   SER A 137     8169   6449   5796   -736    -29    -19       C  
ATOM    720  O   SER A 137     -35.745 -20.303  40.688  1.00 56.02           O  
ANISOU  720  O   SER A 137     8524   6692   6070   -747    -41    -33       O  
ATOM    721  CB  SER A 137     -38.167 -20.322  42.748  1.00 51.37           C  
ANISOU  721  CB  SER A 137     7753   6344   5421   -940    -32    -19       C  
ATOM    722  OG  SER A 137     -38.485 -19.580  43.909  1.00 66.70           O  
ANISOU  722  OG  SER A 137     9590   8382   7369   -909     -5    -20       O  
ATOM    723  N   SER A 138     -35.247 -18.748  42.260  1.00 47.27           N  
ANISOU  723  N   SER A 138     7291   5645   5024   -634    -15    -17       N  
ATOM    724  CA  SER A 138     -34.353 -17.994  41.362  1.00 45.26           C  
ANISOU  724  CA  SER A 138     7042   5355   4798   -551    -11    -25       C  
ATOM    725  C   SER A 138     -33.198 -18.907  40.913  1.00 47.90           C  
ANISOU  725  C   SER A 138     7469   5595   5134   -528      7    -35       C  
ATOM    726  O   SER A 138     -32.897 -18.974  39.724  1.00 48.30           O  
ANISOU  726  O   SER A 138     7557   5626   5169   -518     14    -53       O  
ATOM    727  CB  SER A 138     -33.808 -16.746  42.041  1.00 46.95           C  
ANISOU  727  CB  SER A 138     7202   5587   5049   -477     -4    -19       C  
ATOM    728  OG  SER A 138     -34.850 -15.820  42.294  1.00 59.11           O  
ANISOU  728  OG  SER A 138     8670   7209   6581   -462    -28    -24       O  
ATOM    729  N   ALA A 139     -32.617 -19.671  41.851  1.00 42.77           N  
ANISOU  729  N   ALA A 139     6868   4891   4491   -513      8    -30       N  
ATOM    730  CA  ALA A 139     -31.543 -20.610  41.564  1.00 42.21           C  
ANISOU  730  CA  ALA A 139     6886   4735   4418   -456     11    -52       C  
ATOM    731  C   ALA A 139     -31.974 -21.659  40.521  1.00 49.68           C  
ANISOU  731  C   ALA A 139     7941   5623   5311   -504     -2    -71       C  
ATOM    732  O   ALA A 139     -31.268 -21.854  39.532  1.00 52.03           O  
ANISOU  732  O   ALA A 139     8273   5895   5601   -447     16   -107       O  
ATOM    733  CB  ALA A 139     -31.111 -21.294  42.845  1.00 42.55           C  
ANISOU  733  CB  ALA A 139     6986   4720   4461   -430    -13    -38       C  
ATOM    734  N   VAL A 140     -33.146 -22.301  40.726  1.00 44.85           N  
ANISOU  734  N   VAL A 140     7382   5003   4656   -622    -29    -53       N  
ATOM    735  CA  VAL A 140     -33.672 -23.353  39.861  1.00 44.00           C  
ANISOU  735  CA  VAL A 140     7398   4833   4487   -701    -55    -69       C  
ATOM    736  C   VAL A 140     -34.136 -22.747  38.546  1.00 48.25           C  
ANISOU  736  C   VAL A 140     7881   5437   5016   -718    -51    -88       C  
ATOM    737  O   VAL A 140     -34.017 -23.389  37.500  1.00 50.41           O  
ANISOU  737  O   VAL A 140     8256   5651   5247   -724    -61   -118       O  
ATOM    738  CB  VAL A 140     -34.754 -24.224  40.567  1.00 47.92           C  
ANISOU  738  CB  VAL A 140     7968   5311   4928   -858    -87    -41       C  
ATOM    739  CG1 VAL A 140     -35.249 -25.361  39.661  1.00 48.52           C  
ANISOU  739  CG1 VAL A 140     8200   5304   4931   -960   -124    -60       C  
ATOM    740  CG2 VAL A 140     -34.233 -24.795  41.890  1.00 47.48           C  
ANISOU  740  CG2 VAL A 140     8000   5174   4865   -839    -97    -15       C  
ATOM    741  N   HIS A 141     -34.616 -21.498  38.582  1.00 42.99           N  
ANISOU  741  N   HIS A 141     7074   4882   4380   -713    -45    -73       N  
ATOM    742  CA  HIS A 141     -35.046 -20.776  37.383  1.00 42.45           C  
ANISOU  742  CA  HIS A 141     6966   4869   4295   -713    -57    -85       C  
ATOM    743  C   HIS A 141     -33.877 -20.568  36.450  1.00 44.81           C  
ANISOU  743  C   HIS A 141     7314   5121   4592   -630    -21   -107       C  
ATOM    744  O   HIS A 141     -34.000 -20.856  35.267  1.00 45.56           O  
ANISOU  744  O   HIS A 141     7477   5196   4637   -651    -29   -129       O  
ATOM    745  CB  HIS A 141     -35.698 -19.433  37.723  1.00 42.55           C  
ANISOU  745  CB  HIS A 141     6843   4988   4334   -691    -71    -69       C  
ATOM    746  CG  HIS A 141     -37.180 -19.521  37.790  1.00 46.64           C  
ANISOU  746  CG  HIS A 141     7292   5606   4823   -777   -117    -72       C  
ATOM    747  ND1 HIS A 141     -37.839 -19.676  38.992  1.00 48.52           N  
ANISOU  747  ND1 HIS A 141     7456   5914   5067   -831   -111    -64       N  
ATOM    748  CD2 HIS A 141     -38.086 -19.521  36.788  1.00 49.52           C  
ANISOU  748  CD2 HIS A 141     7644   6026   5145   -825   -168    -89       C  
ATOM    749  CE1 HIS A 141     -39.122 -19.731  38.692  1.00 49.06           C  
ANISOU  749  CE1 HIS A 141     7445   6097   5099   -910   -151    -80       C  
ATOM    750  NE2 HIS A 141     -39.318 -19.665  37.374  1.00 49.96           N  
ANISOU  750  NE2 HIS A 141     7593   6203   5186   -906   -194    -96       N  
ATOM    751  N   LEU A 142     -32.723 -20.155  36.995  1.00 39.71           N  
ANISOU  751  N   LEU A 142     6632   4465   3990   -546     21   -106       N  
ATOM    752  CA  LEU A 142     -31.532 -19.908  36.214  1.00 39.84           C  
ANISOU  752  CA  LEU A 142     6661   4475   4000   -480     72   -133       C  
ATOM    753  C   LEU A 142     -30.971 -21.206  35.611  1.00 49.72           C  
ANISOU  753  C   LEU A 142     8025   5656   5212   -446     86   -182       C  
ATOM    754  O   LEU A 142     -30.429 -21.133  34.514  1.00 53.38           O  
ANISOU  754  O   LEU A 142     8516   6131   5635   -421    125   -215       O  
ATOM    755  CB  LEU A 142     -30.503 -19.095  37.005  1.00 38.81           C  
ANISOU  755  CB  LEU A 142     6441   4379   3925   -421    106   -125       C  
ATOM    756  CG  LEU A 142     -30.989 -17.742  37.584  1.00 41.20           C  
ANISOU  756  CG  LEU A 142     6665   4731   4257   -442     86    -84       C  
ATOM    757  CD1 LEU A 142     -30.021 -17.191  38.602  1.00 39.92           C  
ANISOU  757  CD1 LEU A 142     6436   4586   4145   -399    105    -79       C  
ATOM    758  CD2 LEU A 142     -31.222 -16.710  36.505  1.00 42.29           C  
ANISOU  758  CD2 LEU A 142     6817   4893   4357   -469     85    -73       C  
ATOM    759  N   CYS A 143     -31.228 -22.391  36.230  1.00 46.24           N  
ANISOU  759  N   CYS A 143     7672   5136   4763   -455     49   -187       N  
ATOM    760  CA  CYS A 143     -30.870 -23.719  35.682  1.00 46.73           C  
ANISOU  760  CA  CYS A 143     7887   5097   4771   -417     39   -237       C  
ATOM    761  C   CYS A 143     -31.756 -24.083  34.509  1.00 51.22           C  
ANISOU  761  C   CYS A 143     8548   5644   5269   -507     14   -251       C  
ATOM    762  O   CYS A 143     -31.243 -24.562  33.501  1.00 51.76           O  
ANISOU  762  O   CYS A 143     8706   5676   5286   -456     35   -304       O  
ATOM    763  CB  CYS A 143     -30.927 -24.798  36.751  1.00 47.37           C  
ANISOU  763  CB  CYS A 143     8074   5075   4849   -413    -10   -229       C  
ATOM    764  SG  CYS A 143     -29.843 -24.478  38.154  1.00 51.44           S  
ANISOU  764  SG  CYS A 143     8501   5609   5436   -294     -1   -218       S  
ATOM    765  N   ALA A 144     -33.095 -23.898  34.655  1.00 47.94           N  
ANISOU  765  N   ALA A 144     8107   5262   4844   -639    -35   -210       N  
ATOM    766  CA  ALA A 144     -34.106 -24.158  33.616  1.00 47.80           C  
ANISOU  766  CA  ALA A 144     8151   5249   4761   -745    -79   -219       C  
ATOM    767  C   ALA A 144     -33.797 -23.293  32.412  1.00 51.86           C  
ANISOU  767  C   ALA A 144     8633   5819   5252   -701    -49   -235       C  
ATOM    768  O   ALA A 144     -33.640 -23.833  31.321  1.00 53.44           O  
ANISOU  768  O   ALA A 144     8950   5973   5382   -699    -48   -277       O  
ATOM    769  CB  ALA A 144     -35.495 -23.829  34.135  1.00 48.21           C  
ANISOU  769  CB  ALA A 144     8110   5386   4822   -872   -130   -178       C  
ATOM    770  N   ILE A 145     -33.639 -21.952  32.621  1.00 46.25           N  
ANISOU  770  N   ILE A 145     7788   5196   4588   -664    -23   -203       N  
ATOM    771  CA  ILE A 145     -33.319 -20.989  31.564  1.00 45.03           C  
ANISOU  771  CA  ILE A 145     7623   5086   4399   -640      3   -204       C  
ATOM    772  C   ILE A 145     -32.013 -21.368  30.850  1.00 51.10           C  
ANISOU  772  C   ILE A 145     8460   5826   5131   -569     83   -254       C  
ATOM    773  O   ILE A 145     -31.981 -21.346  29.623  1.00 52.37           O  
ANISOU  773  O   ILE A 145     8698   5988   5212   -586     96   -277       O  
ATOM    774  CB  ILE A 145     -33.306 -19.525  32.072  1.00 46.51           C  
ANISOU  774  CB  ILE A 145     7692   5342   4637   -618      8   -159       C  
ATOM    775  CG1 ILE A 145     -34.678 -19.093  32.616  1.00 46.59           C  
ANISOU  775  CG1 ILE A 145     7627   5407   4670   -661    -72   -128       C  
ATOM    776  CG2 ILE A 145     -32.869 -18.564  30.975  1.00 47.07           C  
ANISOU  776  CG2 ILE A 145     7796   5435   4653   -612     34   -153       C  
ATOM    777  CD1 ILE A 145     -34.647 -17.808  33.649  1.00 44.45           C  
ANISOU  777  CD1 ILE A 145     7242   5184   4462   -611    -72    -92       C  
ATOM    778  N   SER A 146     -30.951 -21.730  31.605  1.00 47.40           N  
ANISOU  778  N   SER A 146     7957   5344   4708   -485    134   -277       N  
ATOM    779  CA  SER A 146     -29.658 -22.081  31.013  1.00 47.64           C  
ANISOU  779  CA  SER A 146     8012   5384   4704   -394    214   -341       C  
ATOM    780  C   SER A 146     -29.762 -23.262  30.059  1.00 53.88           C  
ANISOU  780  C   SER A 146     8963   6099   5408   -378    205   -404       C  
ATOM    781  O   SER A 146     -29.283 -23.167  28.934  1.00 56.25           O  
ANISOU  781  O   SER A 146     9304   6434   5634   -361    263   -447       O  
ATOM    782  CB  SER A 146     -28.597 -22.315  32.085  1.00 49.89           C  
ANISOU  782  CB  SER A 146     8219   5680   5058   -289    245   -362       C  
ATOM    783  OG  SER A 146     -28.823 -23.503  32.827  1.00 58.38           O  
ANISOU  783  OG  SER A 146     9383   6652   6147   -250    187   -375       O  
ATOM    784  N   LEU A 147     -30.425 -24.353  30.491  1.00 48.48           N  
ANISOU  784  N   LEU A 147     8388   5309   4721   -400    131   -408       N  
ATOM    785  CA  LEU A 147     -30.632 -25.566  29.712  1.00 47.98           C  
ANISOU  785  CA  LEU A 147     8515   5142   4571   -399    100   -466       C  
ATOM    786  C   LEU A 147     -31.422 -25.275  28.435  1.00 53.82           C  
ANISOU  786  C   LEU A 147     9315   5904   5229   -500     79   -464       C  
ATOM    787  O   LEU A 147     -31.075 -25.773  27.374  1.00 55.80           O  
ANISOU  787  O   LEU A 147     9687   6125   5391   -464    105   -528       O  
ATOM    788  CB  LEU A 147     -31.357 -26.604  30.582  1.00 47.56           C  
ANISOU  788  CB  LEU A 147     8573   4970   4529   -457     11   -448       C  
ATOM    789  CG  LEU A 147     -30.492 -27.352  31.608  1.00 50.89           C  
ANISOU  789  CG  LEU A 147     9038   5312   4987   -330      9   -472       C  
ATOM    790  CD1 LEU A 147     -31.324 -27.872  32.754  1.00 49.40           C  
ANISOU  790  CD1 LEU A 147     8907   5044   4820   -435    -69   -414       C  
ATOM    791  CD2 LEU A 147     -29.771 -28.492  30.962  1.00 55.29           C  
ANISOU  791  CD2 LEU A 147     9780   5761   5468   -201      9   -566       C  
ATOM    792  N   ASP A 148     -32.448 -24.425  28.535  1.00 50.30           N  
ANISOU  792  N   ASP A 148     8783   5520   4807   -611     29   -396       N  
ATOM    793  CA  ASP A 148     -33.288 -23.995  27.425  1.00 50.79           C  
ANISOU  793  CA  ASP A 148     8885   5616   4798   -699    -16   -385       C  
ATOM    794  C   ASP A 148     -32.463 -23.258  26.346  1.00 57.28           C  
ANISOU  794  C   ASP A 148     9716   6493   5556   -650     65   -406       C  
ATOM    795  O   ASP A 148     -32.797 -23.346  25.159  1.00 58.96           O  
ANISOU  795  O   ASP A 148    10039   6697   5668   -693     44   -427       O  
ATOM    796  CB  ASP A 148     -34.442 -23.113  27.946  1.00 51.65           C  
ANISOU  796  CB  ASP A 148     8866   5800   4957   -781    -89   -316       C  
ATOM    797  CG  ASP A 148     -35.222 -22.425  26.842  1.00 60.02           C  
ANISOU  797  CG  ASP A 148     9946   6911   5947   -837   -148   -301       C  
ATOM    798  OD1 ASP A 148     -35.981 -23.110  26.142  1.00 60.09           O  
ANISOU  798  OD1 ASP A 148    10053   6893   5884   -915   -219   -326       O  
ATOM    799  OD2 ASP A 148     -35.035 -21.205  26.655  1.00 67.63           O1-
ANISOU  799  OD2 ASP A 148    10845   7933   6917   -804   -131   -266       O1-
ATOM    800  N   ARG A 149     -31.400 -22.531  26.761  1.00 52.17           N  
ANISOU  800  N   ARG A 149     8957   5907   4957   -578    156   -398       N  
ATOM    801  CA  ARG A 149     -30.505 -21.816  25.857  1.00 51.85           C  
ANISOU  801  CA  ARG A 149     8914   5936   4849   -560    251   -415       C  
ATOM    802  C   ARG A 149     -29.536 -22.805  25.247  1.00 57.76           C  
ANISOU  802  C   ARG A 149     9745   6673   5530   -472    332   -512       C  
ATOM    803  O   ARG A 149     -29.176 -22.660  24.081  1.00 58.97           O  
ANISOU  803  O   ARG A 149     9969   6864   5574   -484    393   -548       O  
ATOM    804  CB  ARG A 149     -29.720 -20.710  26.591  1.00 52.61           C  
ANISOU  804  CB  ARG A 149     8858   6114   5018   -542    314   -375       C  
ATOM    805  CG  ARG A 149     -30.561 -19.655  27.354  1.00 62.25           C  
ANISOU  805  CG  ARG A 149     9999   7343   6310   -597    237   -289       C  
ATOM    806  CD  ARG A 149     -31.796 -19.183  26.605  1.00 62.04           C  
ANISOU  806  CD  ARG A 149    10048   7301   6223   -669    140   -250       C  
ATOM    807  NE  ARG A 149     -31.456 -18.404  25.416  1.00 50.10           N  
ANISOU  807  NE  ARG A 149     8619   5814   4603   -710    177   -240       N  
ATOM    808  CZ  ARG A 149     -32.343 -17.732  24.700  1.00 62.74           C  
ANISOU  808  CZ  ARG A 149    10298   7402   6137   -758     90   -199       C  
ATOM    809  NH1 ARG A 149     -33.624 -17.731  25.048  1.00 54.29           N1+
ANISOU  809  NH1 ARG A 149     9200   6321   5106   -762    -36   -176       N1+
ATOM    810  NH2 ARG A 149     -31.954 -17.016  23.657  1.00 57.33           N  
ANISOU  810  NH2 ARG A 149     9715   6727   5340   -804    125   -183       N  
ATOM    811  N   TYR A 150     -29.117 -23.819  26.032  1.00 55.08           N  
ANISOU  811  N   TYR A 150     9407   6277   5242   -374    330   -559       N  
ATOM    812  CA  TYR A 150     -28.205 -24.866  25.582  1.00 56.82           C  
ANISOU  812  CA  TYR A 150     9713   6474   5402   -246    389   -667       C  
ATOM    813  C   TYR A 150     -28.835 -25.761  24.484  1.00 64.29           C  
ANISOU  813  C   TYR A 150    10876   7322   6229   -276    342   -717       C  
ATOM    814  O   TYR A 150     -28.208 -25.972  23.438  1.00 65.44           O  
ANISOU  814  O   TYR A 150    11091   7505   6269   -221    420   -795       O  
ATOM    815  CB  TYR A 150     -27.682 -25.695  26.774  1.00 57.35           C  
ANISOU  815  CB  TYR A 150     9757   6482   5552   -119    367   -698       C  
ATOM    816  CG  TYR A 150     -26.817 -26.873  26.377  1.00 60.58           C  
ANISOU  816  CG  TYR A 150    10277   6845   5895     52    401   -821       C  
ATOM    817  CD1 TYR A 150     -25.550 -26.683  25.839  1.00 63.94           C  
ANISOU  817  CD1 TYR A 150    10608   7408   6279    172    526   -907       C  
ATOM    818  CD2 TYR A 150     -27.265 -28.177  26.540  1.00 62.43           C  
ANISOU  818  CD2 TYR A 150    10718   6902   6099     93    307   -857       C  
ATOM    819  CE1 TYR A 150     -24.757 -27.762  25.452  1.00 67.88           C  
ANISOU  819  CE1 TYR A 150    11201   7881   6711    362    556  -1037       C  
ATOM    820  CE2 TYR A 150     -26.475 -29.267  26.174  1.00 65.85           C  
ANISOU  820  CE2 TYR A 150    11284   7274   6464    278    324   -978       C  
ATOM    821  CZ  TYR A 150     -25.221 -29.057  25.621  1.00 76.34           C  
ANISOU  821  CZ  TYR A 150    12501   8751   7754    430    449  -1075       C  
ATOM    822  OH  TYR A 150     -24.437 -30.127  25.226  1.00 78.10           O  
ANISOU  822  OH  TYR A 150    12845   8929   7900    644    466  -1213       O  
ATOM    823  N   TRP A 151     -30.068 -26.261  24.717  1.00 60.40           N  
ANISOU  823  N   TRP A 151    10484   6720   5745   -375    218   -677       N  
ATOM    824  CA  TRP A 151     -30.764 -27.138  23.784  1.00 61.55           C  
ANISOU  824  CA  TRP A 151    10842   6765   5781   -432    150   -720       C  
ATOM    825  C   TRP A 151     -31.293 -26.423  22.523  1.00 65.25           C  
ANISOU  825  C   TRP A 151    11346   7295   6151   -534    146   -701       C  
ATOM    826  O   TRP A 151     -31.432 -27.060  21.474  1.00 65.50           O  
ANISOU  826  O   TRP A 151    11555   7270   6061   -544    131   -763       O  
ATOM    827  CB  TRP A 151     -31.869 -27.906  24.506  1.00 60.59           C  
ANISOU  827  CB  TRP A 151    10801   6526   5693   -534     21   -683       C  
ATOM    828  CG  TRP A 151     -31.362 -28.899  25.511  1.00 62.70           C  
ANISOU  828  CG  TRP A 151    11132   6683   6006   -436      8   -715       C  
ATOM    829  CD1 TRP A 151     -30.252 -29.682  25.402  1.00 66.72           C  
ANISOU  829  CD1 TRP A 151    11740   7132   6480   -254     58   -810       C  
ATOM    830  CD2 TRP A 151     -31.989 -29.264  26.753  1.00 62.15           C  
ANISOU  830  CD2 TRP A 151    11057   6547   6011   -512    -70   -655       C  
ATOM    831  NE1 TRP A 151     -30.137 -30.500  26.503  1.00 66.57           N  
ANISOU  831  NE1 TRP A 151    11792   6994   6509   -200      1   -809       N  
ATOM    832  CE2 TRP A 151     -31.200 -30.278  27.339  1.00 67.11           C  
ANISOU  832  CE2 TRP A 151    11808   7051   6638   -373    -74   -710       C  
ATOM    833  CE3 TRP A 151     -33.151 -28.839  27.423  1.00 62.58           C  
ANISOU  833  CE3 TRP A 151    11014   6642   6120   -681   -138   -566       C  
ATOM    834  CZ2 TRP A 151     -31.525 -30.866  28.571  1.00 66.54           C  
ANISOU  834  CZ2 TRP A 151    11791   6878   6613   -415   -145   -666       C  
ATOM    835  CZ3 TRP A 151     -33.493 -29.449  28.623  1.00 64.24           C  
ANISOU  835  CZ3 TRP A 151    11259   6774   6374   -735   -192   -530       C  
ATOM    836  CH2 TRP A 151     -32.661 -30.415  29.208  1.00 65.76           C  
ANISOU  836  CH2 TRP A 151    11593   6830   6561   -608   -194   -572       C  
ATOM    837  N   SER A 152     -31.566 -25.112  22.620  1.00 60.29           N  
ANISOU  837  N   SER A 152    10574   6768   5565   -600    150   -618       N  
ATOM    838  CA  SER A 152     -32.033 -24.314  21.494  1.00 60.63           C  
ANISOU  838  CA  SER A 152    10663   6862   5513   -684    132   -590       C  
ATOM    839  C   SER A 152     -30.930 -24.177  20.456  1.00 67.85           C  
ANISOU  839  C   SER A 152    11637   7831   6311   -627    263   -652       C  
ATOM    840  O   SER A 152     -31.234 -24.196  19.269  1.00 71.02           O  
ANISOU  840  O   SER A 152    12180   8224   6580   -679    247   -673       O  
ATOM    841  CB  SER A 152     -32.528 -22.944  21.951  1.00 63.74           C  
ANISOU  841  CB  SER A 152    10912   7330   5976   -742     94   -490       C  
ATOM    842  OG  SER A 152     -31.487 -22.051  22.317  1.00 75.30           O  
ANISOU  842  OG  SER A 152    12256   8871   7482   -694    205   -469       O  
ATOM    843  N   VAL A 153     -29.659 -24.045  20.888  1.00 63.37           N  
ANISOU  843  N   VAL A 153    10958   7336   5785   -527    393   -688       N  
ATOM    844  CA  VAL A 153     -28.509 -23.996  19.978  1.00 64.12           C  
ANISOU  844  CA  VAL A 153    11075   7522   5767   -471    541   -765       C  
ATOM    845  C   VAL A 153     -28.083 -25.409  19.521  1.00 72.32           C  
ANISOU  845  C   VAL A 153    12254   8496   6727   -348    568   -894       C  
ATOM    846  O   VAL A 153     -27.843 -25.603  18.325  1.00 74.41           O  
ANISOU  846  O   VAL A 153    12645   8784   6842   -347    628   -959       O  
ATOM    847  CB  VAL A 153     -27.291 -23.166  20.463  1.00 66.95           C  
ANISOU  847  CB  VAL A 153    11237   8026   6176   -436    676   -759       C  
ATOM    848  CG1 VAL A 153     -27.484 -21.693  20.166  1.00 66.31           C  
ANISOU  848  CG1 VAL A 153    11117   8011   6067   -578    686   -659       C  
ATOM    849  CG2 VAL A 153     -26.954 -23.399  21.939  1.00 65.55           C  
ANISOU  849  CG2 VAL A 153    10906   7840   6162   -346    657   -752       C  
ATOM    850  N   THR A 154     -28.009 -26.392  20.451  1.00 69.69           N  
ANISOU  850  N   THR A 154    11926   8070   6482   -241    519   -932       N  
ATOM    851  CA  THR A 154     -27.559 -27.750  20.120  1.00 72.01           C  
ANISOU  851  CA  THR A 154    12381   8277   6704    -95    529  -1060       C  
ATOM    852  C   THR A 154     -28.599 -28.599  19.363  1.00 80.71           C  
ANISOU  852  C   THR A 154    13742   9222   7703   -172    412  -1082       C  
ATOM    853  O   THR A 154     -28.312 -29.081  18.259  1.00 82.50           O  
ANISOU  853  O   THR A 154    14123   9438   7784   -125    458  -1176       O  
ATOM    854  CB  THR A 154     -27.041 -28.488  21.349  1.00 76.92           C  
ANISOU  854  CB  THR A 154    12952   8837   7436     55    505  -1094       C  
ATOM    855  OG1 THR A 154     -28.051 -28.496  22.351  1.00 77.77           O  
ANISOU  855  OG1 THR A 154    13055   8844   7652    -53    375   -991       O  
ATOM    856  CG2 THR A 154     -25.747 -27.905  21.883  1.00 74.54           C  
ANISOU  856  CG2 THR A 154    12414   8707   7201    174    631  -1120       C  
ATOM    857  N   GLN A 155     -29.788 -28.801  19.956  1.00 77.28           N  
ANISOU  857  N   GLN A 155    13352   8678   7335   -297    266  -1002       N  
ATOM    858  CA  GLN A 155     -30.843 -29.624  19.356  1.00 77.91           C  
ANISOU  858  CA  GLN A 155    13661   8616   7324   -403    139  -1019       C  
ATOM    859  C   GLN A 155     -31.904 -28.738  18.681  1.00 79.87           C  
ANISOU  859  C   GLN A 155    13887   8927   7533   -585     71   -936       C  
ATOM    860  O   GLN A 155     -33.090 -29.038  18.746  1.00 79.68           O  
ANISOU  860  O   GLN A 155    13931   8835   7510   -725    -67   -895       O  
ATOM    861  CB  GLN A 155     -31.463 -30.535  20.445  1.00 79.46           C  
ANISOU  861  CB  GLN A 155    13928   8663   7600   -440     19   -995       C  
ATOM    862  CG  GLN A 155     -30.499 -31.570  21.043  1.00 93.06           C  
ANISOU  862  CG  GLN A 155    15741  10280   9337   -245     48  -1082       C  
ATOM    863  CD  GLN A 155     -30.449 -32.860  20.259  1.00124.99           C  
ANISOU  863  CD  GLN A 155    20095  14157  13239   -183      2  -1198       C  
ATOM    864  OE1 GLN A 155     -30.502 -32.895  19.015  1.00121.71           O  
ANISOU  864  OE1 GLN A 155    19796  13756  12691   -199     26  -1256       O  
ATOM    865  NE2 GLN A 155     -30.332 -33.961  20.980  1.00124.20           N  
ANISOU  865  NE2 GLN A 155    20160  13880  13151   -106    -70  -1234       N  
ATOM    866  N   ALA A 156     -31.457 -27.674  17.998  1.00 75.84           N  
ANISOU  866  N   ALA A 156    13293   8549   6973   -585    164   -916       N  
ATOM    867  CA  ALA A 156     -32.254 -26.627  17.350  1.00 75.34           C  
ANISOU  867  CA  ALA A 156    13208   8553   6864   -721    108   -835       C  
ATOM    868  C   ALA A 156     -33.564 -27.077  16.692  1.00 80.43           C  
ANISOU  868  C   ALA A 156    14011   9120   7429   -852    -54   -829       C  
ATOM    869  O   ALA A 156     -34.594 -26.438  16.927  1.00 78.91           O  
ANISOU  869  O   ALA A 156    13731   8964   7287   -957   -166   -745       O  
ATOM    870  CB  ALA A 156     -31.401 -25.872  16.339  1.00 76.75           C  
ANISOU  870  CB  ALA A 156    13400   8837   6925   -696    240   -856       C  
ATOM    871  N   VAL A 157     -33.517 -28.149  15.862  1.00 79.14           N  
ANISOU  871  N   VAL A 157    14075   8860   7134   -839    -69   -925       N  
ATOM    872  CA  VAL A 157     -34.662 -28.677  15.101  1.00 80.63           C  
ANISOU  872  CA  VAL A 157    14441   8974   7220   -973   -222   -937       C  
ATOM    873  C   VAL A 157     -35.703 -29.345  16.020  1.00 83.43           C  
ANISOU  873  C   VAL A 157    14777   9253   7671  -1084   -366   -904       C  
ATOM    874  O   VAL A 157     -36.881 -28.970  15.986  1.00 82.47           O  
ANISOU  874  O   VAL A 157    14593   9179   7562  -1226   -498   -842       O  
ATOM    875  CB  VAL A 157     -34.210 -29.629  13.948  1.00 87.59           C  
ANISOU  875  CB  VAL A 157    15594   9767   7920   -922   -189  -1060       C  
ATOM    876  CG1 VAL A 157     -35.354 -29.929  12.974  1.00 88.58           C  
ANISOU  876  CG1 VAL A 157    15901   9840   7916  -1076   -347  -1066       C  
ATOM    877  CG2 VAL A 157     -32.995 -29.078  13.201  1.00 88.08           C  
ANISOU  877  CG2 VAL A 157    15651   9928   7888   -803     -8  -1107       C  
ATOM    878  N   GLU A 158     -35.255 -30.334  16.827  1.00 79.53           N  
ANISOU  878  N   GLU A 158    14338   8648   7230  -1018   -341   -949       N  
ATOM    879  CA  GLU A 158     -36.081 -31.111  17.750  1.00 78.87           C  
ANISOU  879  CA  GLU A 158    14277   8474   7217  -1134   -457   -923       C  
ATOM    880  C   GLU A 158     -36.619 -30.308  18.910  1.00 78.33           C  
ANISOU  880  C   GLU A 158    13942   8515   7305  -1197   -480   -817       C  
ATOM    881  O   GLU A 158     -37.796 -30.438  19.246  1.00 77.90           O  
ANISOU  881  O   GLU A 158    13844   8479   7275  -1368   -601   -773       O  
ATOM    882  CB  GLU A 158     -35.301 -32.323  18.287  1.00 81.39           C  
ANISOU  882  CB  GLU A 158    14763   8627   7535  -1019   -421   -998       C  
ATOM    883  CG  GLU A 158     -35.328 -33.532  17.365  1.00 98.12           C  
ANISOU  883  CG  GLU A 158    17214  10577   9491  -1027   -478  -1104       C  
ATOM    884  CD  GLU A 158     -34.459 -33.468  16.120  1.00126.55           C  
ANISOU  884  CD  GLU A 158    20928  14198  12957   -879   -377  -1201       C  
ATOM    885  OE1 GLU A 158     -33.512 -32.648  16.082  1.00128.59           O1-
ANISOU  885  OE1 GLU A 158    21017  14590  13250   -734   -232  -1202       O1-
ATOM    886  OE2 GLU A 158     -34.723 -34.256  15.182  1.00121.27           O  
ANISOU  886  OE2 GLU A 158    20525  13416  12137   -920   -441  -1281       O  
ATOM    887  N   TYR A 159     -35.749 -29.502  19.539  1.00 71.78           N  
ANISOU  887  N   TYR A 159    12931   7767   6576  -1063   -361   -784       N  
ATOM    888  CA  TYR A 159     -36.059 -28.717  20.726  1.00 68.80           C  
ANISOU  888  CA  TYR A 159    12310   7483   6347  -1086   -364   -695       C  
ATOM    889  C   TYR A 159     -37.077 -27.617  20.521  1.00 71.13           C  
ANISOU  889  C   TYR A 159    12451   7914   6660  -1186   -441   -622       C  
ATOM    890  O   TYR A 159     -37.936 -27.457  21.386  1.00 72.20           O  
ANISOU  890  O   TYR A 159    12449   8104   6881  -1275   -510   -569       O  
ATOM    891  CB  TYR A 159     -34.790 -28.140  21.383  1.00 67.90           C  
ANISOU  891  CB  TYR A 159    12061   7417   6321   -918   -223   -688       C  
ATOM    892  CG  TYR A 159     -35.078 -27.496  22.718  1.00 66.50           C  
ANISOU  892  CG  TYR A 159    11669   7310   6290   -939   -231   -605       C  
ATOM    893  CD1 TYR A 159     -35.403 -28.269  23.830  1.00 67.92           C  
ANISOU  893  CD1 TYR A 159    11857   7417   6534   -985   -277   -591       C  
ATOM    894  CD2 TYR A 159     -35.113 -26.111  22.851  1.00 66.01           C  
ANISOU  894  CD2 TYR A 159    11420   7377   6285   -927   -203   -540       C  
ATOM    895  CE1 TYR A 159     -35.719 -27.681  25.050  1.00 67.70           C  
ANISOU  895  CE1 TYR A 159    11638   7462   6625  -1011   -281   -520       C  
ATOM    896  CE2 TYR A 159     -35.419 -25.510  24.069  1.00 65.94           C  
ANISOU  896  CE2 TYR A 159    11226   7430   6400   -939   -215   -474       C  
ATOM    897  CZ  TYR A 159     -35.730 -26.300  25.165  1.00 74.06           C  
ANISOU  897  CZ  TYR A 159    12248   8402   7490   -980   -249   -466       C  
ATOM    898  OH  TYR A 159     -36.039 -25.725  26.371  1.00 74.33           O  
ANISOU  898  OH  TYR A 159    12106   8504   7632   -993   -253   -406       O  
ATOM    899  N   ASN A 160     -36.970 -26.837  19.443  1.00 65.79           N  
ANISOU  899  N   ASN A 160    11797   7298   5902  -1162   -428   -621       N  
ATOM    900  CA  ASN A 160     -37.878 -25.716  19.201  1.00 65.49           C  
ANISOU  900  CA  ASN A 160    11636   7377   5872  -1219   -517   -555       C  
ATOM    901  C   ASN A 160     -39.345 -26.135  18.961  1.00 71.39           C  
ANISOU  901  C   ASN A 160    12394   8149   6582  -1375   -689   -555       C  
ATOM    902  O   ASN A 160     -40.249 -25.356  19.253  1.00 72.77           O  
ANISOU  902  O   ASN A 160    12403   8440   6808  -1412   -777   -504       O  
ATOM    903  CB  ASN A 160     -37.349 -24.805  18.102  1.00 66.45           C  
ANISOU  903  CB  ASN A 160    11818   7535   5894  -1161   -468   -549       C  
ATOM    904  CG  ASN A 160     -36.260 -23.920  18.654  1.00 87.42           C  
ANISOU  904  CG  ASN A 160    14356  10234   8624  -1054   -328   -515       C  
ATOM    905  OD1 ASN A 160     -35.101 -24.332  18.816  1.00 76.08           O  
ANISOU  905  OD1 ASN A 160    12947   8767   7194   -972   -195   -561       O  
ATOM    906  ND2 ASN A 160     -36.627 -22.701  19.026  1.00 80.48           N  
ANISOU  906  ND2 ASN A 160    13340   9433   7806  -1050   -366   -439       N  
ATOM    907  N   LEU A 161     -39.585 -27.378  18.545  1.00 68.07           N  
ANISOU  907  N   LEU A 161    12157   7628   6078  -1465   -738   -616       N  
ATOM    908  CA  LEU A 161     -40.938 -27.914  18.368  1.00 68.63           C  
ANISOU  908  CA  LEU A 161    12239   7728   6108  -1647   -900   -623       C  
ATOM    909  C   LEU A 161     -41.521 -28.346  19.752  1.00 70.35           C  
ANISOU  909  C   LEU A 161    12315   7974   6441  -1748   -924   -593       C  
ATOM    910  O   LEU A 161     -42.670 -28.794  19.834  1.00 71.44           O  
ANISOU  910  O   LEU A 161    12418   8168   6558  -1928  -1046   -595       O  
ATOM    911  CB  LEU A 161     -40.911 -29.109  17.366  1.00 70.46           C  
ANISOU  911  CB  LEU A 161    12762   7821   6189  -1722   -946   -704       C  
ATOM    912  CG  LEU A 161     -41.055 -28.838  15.847  1.00 75.51           C  
ANISOU  912  CG  LEU A 161    13547   8470   6675  -1724  -1004   -737       C  
ATOM    913  CD1 LEU A 161     -42.465 -28.435  15.478  1.00 76.18           C  
ANISOU  913  CD1 LEU A 161    13527   8686   6732  -1861  -1185   -709       C  
ATOM    914  CD2 LEU A 161     -40.008 -27.843  15.314  1.00 77.51           C  
ANISOU  914  CD2 LEU A 161    13798   8750   6901  -1552   -877   -723       C  
ATOM    915  N   LYS A 162     -40.711 -28.195  20.826  1.00 62.89           N  
ANISOU  915  N   LYS A 162    11286   7003   5605  -1643   -807   -566       N  
ATOM    916  CA  LYS A 162     -41.050 -28.501  22.218  1.00 60.90           C  
ANISOU  916  CA  LYS A 162    10912   6772   5457  -1714   -802   -531       C  
ATOM    917  C   LYS A 162     -41.068 -27.218  23.071  1.00 62.57           C  
ANISOU  917  C   LYS A 162    10853   7129   5791  -1621   -757   -468       C  
ATOM    918  O   LYS A 162     -41.418 -27.256  24.254  1.00 61.75           O  
ANISOU  918  O   LYS A 162    10614   7076   5772  -1672   -749   -435       O  
ATOM    919  CB  LYS A 162     -40.087 -29.547  22.794  1.00 61.55           C  
ANISOU  919  CB  LYS A 162    11167   6674   5545  -1664   -723   -560       C  
ATOM    920  CG  LYS A 162     -40.140 -30.885  22.044  1.00 63.97           C  
ANISOU  920  CG  LYS A 162    11773   6811   5721  -1754   -783   -629       C  
ATOM    921  CD  LYS A 162     -39.635 -32.053  22.878  1.00 70.42           C  
ANISOU  921  CD  LYS A 162    12767   7448   6543  -1756   -760   -648       C  
ATOM    922  CE  LYS A 162     -38.170 -31.984  23.266  1.00 71.89           C  
ANISOU  922  CE  LYS A 162    12977   7558   6781  -1510   -633   -670       C  
ATOM    923  NZ  LYS A 162     -37.305 -32.433  22.156  1.00 78.03           N1+
ANISOU  923  NZ  LYS A 162    13966   8228   7453  -1370   -594   -760       N1+
ATOM    924  N   ARG A 163     -40.748 -26.076  22.441  1.00 57.19           N  
ANISOU  924  N   ARG A 163    10115   6510   5105  -1498   -736   -451       N  
ATOM    925  CA  ARG A 163     -40.730 -24.749  23.048  1.00 55.10           C  
ANISOU  925  CA  ARG A 163     9642   6360   4934  -1398   -708   -396       C  
ATOM    926  C   ARG A 163     -42.144 -24.112  22.902  1.00 59.25           C  
ANISOU  926  C   ARG A 163    10009   7047   5455  -1462   -848   -380       C  
ATOM    927  O   ARG A 163     -42.330 -23.072  22.273  1.00 58.77           O  
ANISOU  927  O   ARG A 163     9914   7049   5367  -1383   -897   -363       O  
ATOM    928  CB  ARG A 163     -39.651 -23.915  22.351  1.00 53.91           C  
ANISOU  928  CB  ARG A 163     9557   6175   4752  -1256   -624   -389       C  
ATOM    929  CG  ARG A 163     -38.299 -23.906  23.043  1.00 59.18           C  
ANISOU  929  CG  ARG A 163    10221   6779   5486  -1147   -476   -386       C  
ATOM    930  CD  ARG A 163     -37.457 -22.807  22.423  1.00 71.28           C  
ANISOU  930  CD  ARG A 163    11764   8331   6987  -1048   -404   -367       C  
ATOM    931  NE  ARG A 163     -36.353 -22.361  23.271  1.00 76.27           N  
ANISOU  931  NE  ARG A 163    12309   8964   7706   -954   -282   -349       N  
ATOM    932  CZ  ARG A 163     -35.598 -21.297  23.011  1.00 84.88           C  
ANISOU  932  CZ  ARG A 163    13379  10087   8786   -895   -212   -322       C  
ATOM    933  NH1 ARG A 163     -35.833 -20.555  21.939  1.00 77.07           N  
ANISOU  933  NH1 ARG A 163    12469   9116   7698   -914   -251   -303       N  
ATOM    934  NH2 ARG A 163     -34.608 -20.963  23.827  1.00 62.35           N1+
ANISOU  934  NH2 ARG A 163    10435   7243   6010   -829   -109   -311       N1+
ATOM    935  N   THR A 164     -43.127 -24.774  23.497  1.00 56.37           N  
ANISOU  935  N   THR A 164     9555   6753   5109  -1610   -913   -390       N  
ATOM    936  CA  THR A 164     -44.555 -24.501  23.452  1.00 57.07           C  
ANISOU  936  CA  THR A 164     9470   7026   5188  -1702  -1048   -397       C  
ATOM    937  C   THR A 164     -45.012 -23.857  24.765  1.00 63.00           C  
ANISOU  937  C   THR A 164     9963   7924   6049  -1670  -1024   -369       C  
ATOM    938  O   THR A 164     -44.498 -24.219  25.832  1.00 63.27           O  
ANISOU  938  O   THR A 164     9986   7904   6149  -1681   -923   -350       O  
ATOM    939  CB  THR A 164     -45.214 -25.867  23.193  1.00 63.63           C  
ANISOU  939  CB  THR A 164    10402   7831   5942  -1928  -1117   -437       C  
ATOM    940  OG1 THR A 164     -44.764 -26.316  21.918  1.00 63.23           O  
ANISOU  940  OG1 THR A 164    10599   7644   5781  -1926  -1141   -470       O  
ATOM    941  CG2 THR A 164     -46.736 -25.852  23.239  1.00 64.05           C  
ANISOU  941  CG2 THR A 164    10255   8103   5979  -2079  -1253   -457       C  
ATOM    942  N   PRO A 165     -45.994 -22.926  24.740  1.00 59.00           N  
ANISOU  942  N   PRO A 165     9252   7608   5557  -1619  -1123   -374       N  
ATOM    943  CA  PRO A 165     -46.450 -22.329  26.009  1.00 57.69           C  
ANISOU  943  CA  PRO A 165     8840   7594   5486  -1575  -1095   -362       C  
ATOM    944  C   PRO A 165     -46.843 -23.363  27.061  1.00 61.03           C  
ANISOU  944  C   PRO A 165     9191   8065   5931  -1769  -1045   -368       C  
ATOM    945  O   PRO A 165     -46.436 -23.200  28.214  1.00 61.51           O  
ANISOU  945  O   PRO A 165     9186   8118   6068  -1727   -945   -342       O  
ATOM    946  CB  PRO A 165     -47.641 -21.462  25.593  1.00 60.63           C  
ANISOU  946  CB  PRO A 165     9021   8179   5838  -1510  -1241   -391       C  
ATOM    947  CG  PRO A 165     -47.431 -21.180  24.144  1.00 64.61           C  
ANISOU  947  CG  PRO A 165     9704   8591   6252  -1446  -1328   -393       C  
ATOM    948  CD  PRO A 165     -46.727 -22.369  23.582  1.00 60.36           C  
ANISOU  948  CD  PRO A 165     9412   7869   5652  -1581  -1271   -396       C  
ATOM    949  N   ARG A 166     -47.580 -24.444  26.664  1.00 55.90           N  
ANISOU  949  N   ARG A 166     8583   7450   5207  -1994  -1116   -399       N  
ATOM    950  CA  ARG A 166     -48.050 -25.497  27.583  1.00 55.91           C  
ANISOU  950  CA  ARG A 166     8549   7492   5201  -2229  -1082   -401       C  
ATOM    951  C   ARG A 166     -46.898 -26.273  28.216  1.00 59.75           C  
ANISOU  951  C   ARG A 166     9257   7740   5706  -2243   -961   -366       C  
ATOM    952  O   ARG A 166     -46.961 -26.635  29.400  1.00 57.66           O  
ANISOU  952  O   ARG A 166     8938   7498   5473  -2334   -893   -344       O  
ATOM    953  CB  ARG A 166     -49.004 -26.480  26.891  1.00 55.57           C  
ANISOU  953  CB  ARG A 166     8547   7511   5055  -2487  -1194   -441       C  
ATOM    954  CG  ARG A 166     -50.224 -25.844  26.281  1.00 67.56           C  
ANISOU  954  CG  ARG A 166     9830   9292   6547  -2490  -1333   -487       C  
ATOM    955  CD  ARG A 166     -51.417 -25.859  27.208  1.00 80.82           C  
ANISOU  955  CD  ARG A 166    11199  11266   8242  -2643  -1345   -512       C  
ATOM    956  NE  ARG A 166     -52.631 -25.374  26.547  1.00 86.09           N  
ANISOU  956  NE  ARG A 166    11630  12208   8874  -2648  -1498   -572       N  
ATOM    957  CZ  ARG A 166     -53.332 -26.070  25.657  1.00 96.60           C  
ANISOU  957  CZ  ARG A 166    12998  13595  10109  -2849  -1624   -612       C  
ATOM    958  NH1 ARG A 166     -52.940 -27.283  25.295  1.00 75.65           N1+
ANISOU  958  NH1 ARG A 166    10635  10726   7383  -3061  -1613   -598       N1+
ATOM    959  NH2 ARG A 166     -54.422 -25.551  25.111  1.00 92.34           N  
ANISOU  959  NH2 ARG A 166    12216  13327   9542  -2827  -1772   -671       N  
ATOM    960  N   ARG A 167     -45.855 -26.536  27.408  1.00 56.40           N  
ANISOU  960  N   ARG A 167     9083   7095   5251  -2147   -939   -366       N  
ATOM    961  CA  ARG A 167     -44.660 -27.258  27.817  1.00 55.30           C  
ANISOU  961  CA  ARG A 167     9163   6725   5121  -2110   -842   -350       C  
ATOM    962  C   ARG A 167     -43.802 -26.387  28.706  1.00 59.19           C  
ANISOU  962  C   ARG A 167     9560   7211   5718  -1913   -737   -313       C  
ATOM    963  O   ARG A 167     -43.252 -26.889  29.695  1.00 60.57           O  
ANISOU  963  O   ARG A 167     9794   7294   5926  -1924   -665   -290       O  
ATOM    964  CB  ARG A 167     -43.896 -27.739  26.587  1.00 55.33           C  
ANISOU  964  CB  ARG A 167     9429   6543   5050  -2052   -854   -381       C  
ATOM    965  CG  ARG A 167     -44.542 -28.945  25.947  1.00 61.10           C  
ANISOU  965  CG  ARG A 167    10335   7212   5669  -2273   -946   -419       C  
ATOM    966  CD  ARG A 167     -43.924 -29.211  24.608  1.00 70.94           C  
ANISOU  966  CD  ARG A 167    11812   8312   6829  -2194   -967   -461       C  
ATOM    967  NE  ARG A 167     -44.188 -30.571  24.140  1.00 86.89           N  
ANISOU  967  NE  ARG A 167    14085  10191   8736  -2381  -1035   -502       N  
ATOM    968  CZ  ARG A 167     -43.527 -31.647  24.551  1.00 98.20           C  
ANISOU  968  CZ  ARG A 167    15758  11413  10141  -2405   -995   -513       C  
ATOM    969  NH1 ARG A 167     -42.584 -31.541  25.485  1.00 74.00           N1+
ANISOU  969  NH1 ARG A 167    12687   8274   7158  -2255   -889   -486       N1+
ATOM    970  NH2 ARG A 167     -43.816 -32.840  24.049  1.00 93.47           N  
ANISOU  970  NH2 ARG A 167    15419  10670   9425  -2576  -1074   -554       N  
ATOM    971  N   VAL A 168     -43.705 -25.076  28.381  1.00 53.88           N  
ANISOU  971  N   VAL A 168     8754   6630   5089  -1739   -739   -305       N  
ATOM    972  CA  VAL A 168     -42.967 -24.130  29.205  1.00 52.26           C  
ANISOU  972  CA  VAL A 168     8452   6428   4976  -1567   -652   -272       C  
ATOM    973  C   VAL A 168     -43.714 -23.987  30.568  1.00 58.20           C  
ANISOU  973  C   VAL A 168     9003   7329   5783  -1634   -636   -256       C  
ATOM    974  O   VAL A 168     -43.067 -24.041  31.619  1.00 58.82           O  
ANISOU  974  O   VAL A 168     9085   7349   5915  -1595   -552   -230       O  
ATOM    975  CB  VAL A 168     -42.671 -22.783  28.480  1.00 54.39           C  
ANISOU  975  CB  VAL A 168     8679   6731   5258  -1386   -667   -265       C  
ATOM    976  CG1 VAL A 168     -42.056 -21.760  29.424  1.00 52.08           C  
ANISOU  976  CG1 VAL A 168     8280   6452   5054  -1239   -593   -231       C  
ATOM    977  CG2 VAL A 168     -41.751 -22.999  27.286  1.00 54.05           C  
ANISOU  977  CG2 VAL A 168     8848   6540   5151  -1334   -647   -278       C  
ATOM    978  N   LYS A 169     -45.067 -23.907  30.552  1.00 54.04           N  
ANISOU  978  N   LYS A 169     8302   7001   5229  -1748   -716   -280       N  
ATOM    979  CA  LYS A 169     -45.866 -23.832  31.786  1.00 53.61           C  
ANISOU  979  CA  LYS A 169     8040   7124   5206  -1832   -692   -278       C  
ATOM    980  C   LYS A 169     -45.601 -25.058  32.688  1.00 57.00           C  
ANISOU  980  C   LYS A 169     8596   7447   5615  -2010   -625   -254       C  
ATOM    981  O   LYS A 169     -45.494 -24.900  33.907  1.00 56.52           O  
ANISOU  981  O   LYS A 169     8455   7425   5596  -2003   -553   -230       O  
ATOM    982  CB  LYS A 169     -47.364 -23.692  31.469  1.00 57.61           C  
ANISOU  982  CB  LYS A 169     8332   7886   5670  -1940   -792   -323       C  
ATOM    983  CG  LYS A 169     -47.778 -22.298  31.029  1.00 64.94           C  
ANISOU  983  CG  LYS A 169     9087   8958   6628  -1728   -863   -348       C  
ATOM    984  CD  LYS A 169     -49.186 -22.311  30.481  1.00 77.39           C  
ANISOU  984  CD  LYS A 169    10476  10778   8152  -1824   -987   -405       C  
ATOM    985  CE  LYS A 169     -49.682 -20.951  30.073  1.00 91.06           C  
ANISOU  985  CE  LYS A 169    12044  12653   9901  -1591  -1081   -437       C  
ATOM    986  NZ  LYS A 169     -49.032 -20.479  28.823  1.00104.86           N1+
ANISOU  986  NZ  LYS A 169    13994  14225  11622  -1450  -1145   -418       N1+
ATOM    987  N   ALA A 170     -45.429 -26.259  32.072  1.00 53.42           N  
ANISOU  987  N   ALA A 170     8373   6836   5088  -2156   -656   -259       N  
ATOM    988  CA  ALA A 170     -45.107 -27.514  32.756  1.00 53.64           C  
ANISOU  988  CA  ALA A 170     8599   6709   5075  -2316   -619   -235       C  
ATOM    989  C   ALA A 170     -43.740 -27.404  33.425  1.00 59.33           C  
ANISOU  989  C   ALA A 170     9435   7251   5856  -2132   -531   -203       C  
ATOM    990  O   ALA A 170     -43.621 -27.746  34.599  1.00 60.10           O  
ANISOU  990  O   ALA A 170     9548   7324   5962  -2192   -481   -171       O  
ATOM    991  CB  ALA A 170     -45.124 -28.679  31.782  1.00 55.12           C  
ANISOU  991  CB  ALA A 170     9040   6739   5165  -2460   -688   -259       C  
ATOM    992  N   THR A 171     -42.727 -26.855  32.718  1.00 55.19           N  
ANISOU  992  N   THR A 171     8974   6625   5370  -1913   -512   -213       N  
ATOM    993  CA  THR A 171     -41.386 -26.694  33.296  1.00 52.67           C  
ANISOU  993  CA  THR A 171     8733   6168   5110  -1734   -433   -193       C  
ATOM    994  C   THR A 171     -41.376 -25.668  34.437  1.00 54.97           C  
ANISOU  994  C   THR A 171     8818   6585   5484  -1646   -378   -162       C  
ATOM    995  O   THR A 171     -40.709 -25.918  35.428  1.00 55.81           O  
ANISOU  995  O   THR A 171     8977   6609   5618  -1610   -327   -137       O  
ATOM    996  CB  THR A 171     -40.333 -26.417  32.226  1.00 50.65           C  
ANISOU  996  CB  THR A 171     8583   5805   4858  -1557   -417   -218       C  
ATOM    997  OG1 THR A 171     -40.456 -27.412  31.206  1.00 49.30           O  
ANISOU  997  OG1 THR A 171     8611   5526   4596  -1647   -471   -255       O  
ATOM    998  CG2 THR A 171     -38.916 -26.446  32.792  1.00 43.04           C  
ANISOU  998  CG2 THR A 171     7697   4714   3944  -1392   -340   -210       C  
ATOM    999  N   ILE A 172     -42.124 -24.550  34.320  1.00 48.78           N  
ANISOU  999  N   ILE A 172     7814   5990   4730  -1603   -398   -170       N  
ATOM   1000  CA  ILE A 172     -42.222 -23.515  35.366  1.00 46.42           C  
ANISOU 1000  CA  ILE A 172     7325   5814   4498  -1509   -355   -153       C  
ATOM   1001  C   ILE A 172     -42.887 -24.154  36.609  1.00 51.04           C  
ANISOU 1001  C   ILE A 172     7859   6475   5060  -1679   -327   -138       C  
ATOM   1002  O   ILE A 172     -42.487 -23.883  37.746  1.00 50.09           O  
ANISOU 1002  O   ILE A 172     7704   6351   4977  -1626   -268   -114       O  
ATOM   1003  CB  ILE A 172     -43.011 -22.290  34.835  1.00 48.76           C  
ANISOU 1003  CB  ILE A 172     7431   6286   4811  -1420   -409   -178       C  
ATOM   1004  CG1 ILE A 172     -42.257 -21.571  33.687  1.00 48.23           C  
ANISOU 1004  CG1 ILE A 172     7447   6126   4751  -1261   -430   -180       C  
ATOM   1005  CG2 ILE A 172     -43.401 -21.342  35.965  1.00 47.14           C  
ANISOU 1005  CG2 ILE A 172     7028   6230   4654  -1343   -377   -177       C  
ATOM   1006  CD1 ILE A 172     -43.093 -20.688  32.810  1.00 50.17           C  
ANISOU 1006  CD1 ILE A 172     7591   6497   4976  -1202   -519   -204       C  
ATOM   1007  N   VAL A 173     -43.892 -25.031  36.378  1.00 47.98           N  
ANISOU 1007  N   VAL A 173     7477   6155   4596  -1902   -372   -152       N  
ATOM   1008  CA  VAL A 173     -44.551 -25.754  37.465  1.00 47.41           C  
ANISOU 1008  CA  VAL A 173     7383   6155   4475  -2116   -341   -134       C  
ATOM   1009  C   VAL A 173     -43.468 -26.650  38.102  1.00 52.27           C  
ANISOU 1009  C   VAL A 173     8259   6523   5077  -2122   -303    -91       C  
ATOM   1010  O   VAL A 173     -43.303 -26.613  39.323  1.00 53.88           O  
ANISOU 1010  O   VAL A 173     8445   6738   5290  -2132   -247    -61       O  
ATOM   1011  CB  VAL A 173     -45.788 -26.550  36.975  1.00 51.61           C  
ANISOU 1011  CB  VAL A 173     7887   6806   4916  -2385   -402   -159       C  
ATOM   1012  CG1 VAL A 173     -46.277 -27.515  38.034  1.00 52.43           C  
ANISOU 1012  CG1 VAL A 173     8045   6931   4943  -2651   -364   -129       C  
ATOM   1013  CG2 VAL A 173     -46.914 -25.619  36.549  1.00 51.81           C  
ANISOU 1013  CG2 VAL A 173     7614   7117   4955  -2358   -447   -209       C  
ATOM   1014  N   ALA A 174     -42.674 -27.370  37.265  1.00 46.93           N  
ANISOU 1014  N   ALA A 174     7823   5627   4380  -2083   -337    -96       N  
ATOM   1015  CA  ALA A 174     -41.606 -28.238  37.733  1.00 45.90           C  
ANISOU 1015  CA  ALA A 174     7950   5257   4234  -2045   -323    -71       C  
ATOM   1016  C   ALA A 174     -40.559 -27.479  38.535  1.00 52.65           C  
ANISOU 1016  C   ALA A 174     8749   6081   5174  -1825   -263    -52       C  
ATOM   1017  O   ALA A 174     -40.208 -27.950  39.618  1.00 54.73           O  
ANISOU 1017  O   ALA A 174     9111   6264   5422  -1852   -242    -18       O  
ATOM   1018  CB  ALA A 174     -40.976 -28.991  36.583  1.00 46.31           C  
ANISOU 1018  CB  ALA A 174     8235   5112   4248  -1997   -370   -102       C  
ATOM   1019  N   VAL A 175     -40.130 -26.272  38.081  1.00 48.71           N  
ANISOU 1019  N   VAL A 175     8095   5656   4755  -1628   -241    -70       N  
ATOM   1020  CA  VAL A 175     -39.123 -25.476  38.814  1.00 47.20           C  
ANISOU 1020  CA  VAL A 175     7845   5446   4642  -1437   -189    -55       C  
ATOM   1021  C   VAL A 175     -39.684 -25.068  40.160  1.00 54.74           C  
ANISOU 1021  C   VAL A 175     8667   6526   5606  -1496   -154    -28       C  
ATOM   1022  O   VAL A 175     -38.965 -25.152  41.138  1.00 54.14           O  
ANISOU 1022  O   VAL A 175     8648   6376   5548  -1437   -127     -2       O  
ATOM   1023  CB  VAL A 175     -38.424 -24.285  38.071  1.00 48.01           C  
ANISOU 1023  CB  VAL A 175     7850   5578   4813  -1239   -172    -75       C  
ATOM   1024  CG1 VAL A 175     -38.108 -24.618  36.617  1.00 47.75           C  
ANISOU 1024  CG1 VAL A 175     7928   5466   4750  -1210   -199   -108       C  
ATOM   1025  CG2 VAL A 175     -39.204 -22.989  38.171  1.00 46.95           C  
ANISOU 1025  CG2 VAL A 175     7495   5629   4715  -1208   -171    -77       C  
ATOM   1026  N   TRP A 176     -40.972 -24.695  40.226  1.00 55.02           N  
ANISOU 1026  N   TRP A 176     8528   6759   5619  -1612   -158    -39       N  
ATOM   1027  CA  TRP A 176     -41.587 -24.316  41.491  1.00 56.31           C  
ANISOU 1027  CA  TRP A 176     8550   7070   5775  -1670   -113    -26       C  
ATOM   1028  C   TRP A 176     -41.690 -25.526  42.451  1.00 65.78           C  
ANISOU 1028  C   TRP A 176     9910   8190   6893  -1864    -97     13       C  
ATOM   1029  O   TRP A 176     -41.344 -25.361  43.618  1.00 68.24           O  
ANISOU 1029  O   TRP A 176    10227   8494   7208  -1833    -54     40       O  
ATOM   1030  CB  TRP A 176     -42.917 -23.579  41.278  1.00 55.07           C  
ANISOU 1030  CB  TRP A 176     8142   7171   5611  -1716   -122    -66       C  
ATOM   1031  CG  TRP A 176     -42.735 -22.142  40.864  1.00 54.37           C  
ANISOU 1031  CG  TRP A 176     7909   7152   5597  -1489   -134    -93       C  
ATOM   1032  CD1 TRP A 176     -42.924 -21.615  39.622  1.00 56.80           C  
ANISOU 1032  CD1 TRP A 176     8175   7485   5922  -1407   -193   -122       C  
ATOM   1033  CD2 TRP A 176     -42.362 -21.042  41.713  1.00 53.37           C  
ANISOU 1033  CD2 TRP A 176     7689   7065   5523  -1326    -95    -94       C  
ATOM   1034  NE1 TRP A 176     -42.689 -20.256  39.640  1.00 54.75           N  
ANISOU 1034  NE1 TRP A 176     7817   7267   5718  -1206   -196   -135       N  
ATOM   1035  CE2 TRP A 176     -42.348 -19.878  40.910  1.00 55.89           C  
ANISOU 1035  CE2 TRP A 176     7928   7421   5888  -1154   -137   -121       C  
ATOM   1036  CE3 TRP A 176     -42.006 -20.933  43.072  1.00 54.28           C  
ANISOU 1036  CE3 TRP A 176     7807   7174   5642  -1311    -37    -73       C  
ATOM   1037  CZ2 TRP A 176     -41.968 -18.627  41.412  1.00 54.53           C  
ANISOU 1037  CZ2 TRP A 176     7691   7264   5764   -975   -124   -129       C  
ATOM   1038  CZ3 TRP A 176     -41.672 -19.686  43.577  1.00 54.62           C  
ANISOU 1038  CZ3 TRP A 176     7764   7252   5737  -1131    -21    -86       C  
ATOM   1039  CH2 TRP A 176     -41.637 -18.553  42.749  1.00 54.58           C  
ANISOU 1039  CH2 TRP A 176     7693   7268   5777   -968    -66   -113       C  
ATOM   1040  N   LEU A 177     -42.040 -26.739  41.967  1.00 62.35           N  
ANISOU 1040  N   LEU A 177     9646   7667   6379  -2055   -138     20       N  
ATOM   1041  CA  LEU A 177     -42.093 -27.918  42.842  1.00 64.01           C  
ANISOU 1041  CA  LEU A 177    10065   7764   6494  -2251   -136     66       C  
ATOM   1042  C   LEU A 177     -40.710 -28.382  43.304  1.00 65.39           C  
ANISOU 1042  C   LEU A 177    10479   7683   6682  -2101   -150     96       C  
ATOM   1043  O   LEU A 177     -40.584 -28.899  44.423  1.00 66.77           O  
ANISOU 1043  O   LEU A 177    10782   7789   6799  -2184   -138    141       O  
ATOM   1044  CB  LEU A 177     -42.851 -29.100  42.208  1.00 66.95           C  
ANISOU 1044  CB  LEU A 177    10588   8089   6762  -2515   -188     65       C  
ATOM   1045  CG  LEU A 177     -44.288 -28.849  41.747  1.00 73.88           C  
ANISOU 1045  CG  LEU A 177    11232   9234   7607  -2703   -190     30       C  
ATOM   1046  CD1 LEU A 177     -44.859 -30.079  41.083  1.00 75.74           C  
ANISOU 1046  CD1 LEU A 177    11656   9387   7736  -2970   -255     30       C  
ATOM   1047  CD2 LEU A 177     -45.187 -28.387  42.907  1.00 77.43           C  
ANISOU 1047  CD2 LEU A 177    11453   9940   8025  -2827   -114     35       C  
ATOM   1048  N   ILE A 178     -39.687 -28.233  42.441  1.00 57.32           N  
ANISOU 1048  N   ILE A 178     9520   6532   5726  -1887   -179     69       N  
ATOM   1049  CA  ILE A 178     -38.306 -28.582  42.777  1.00 55.61           C  
ANISOU 1049  CA  ILE A 178     9485   6112   5533  -1704   -197     78       C  
ATOM   1050  C   ILE A 178     -37.819 -27.611  43.846  1.00 61.56           C  
ANISOU 1050  C   ILE A 178    10091   6947   6353  -1571   -149     96       C  
ATOM   1051  O   ILE A 178     -37.097 -28.022  44.751  1.00 63.69           O  
ANISOU 1051  O   ILE A 178    10499   7096   6605  -1517   -164    124       O  
ATOM   1052  CB  ILE A 178     -37.400 -28.531  41.533  1.00 57.14           C  
ANISOU 1052  CB  ILE A 178     9724   6209   5777  -1513   -220     29       C  
ATOM   1053  CG1 ILE A 178     -37.739 -29.677  40.551  1.00 58.59           C  
ANISOU 1053  CG1 ILE A 178    10121   6264   5877  -1633   -279      7       C  
ATOM   1054  CG2 ILE A 178     -35.921 -28.548  41.927  1.00 56.05           C  
ANISOU 1054  CG2 ILE A 178     9669   5940   5686  -1281   -225     22       C  
ATOM   1055  CD1 ILE A 178     -37.252 -29.495  39.126  1.00 59.85           C  
ANISOU 1055  CD1 ILE A 178    10278   6396   6066  -1496   -289    -50       C  
ATOM   1056  N   SER A 179     -38.223 -26.323  43.739  1.00 56.29           N  
ANISOU 1056  N   SER A 179     9159   6477   5753  -1512   -104     76       N  
ATOM   1057  CA  SER A 179     -37.858 -25.245  44.657  1.00 54.13           C  
ANISOU 1057  CA  SER A 179     8737   6290   5539  -1388    -63     84       C  
ATOM   1058  C   SER A 179     -38.494 -25.473  45.993  1.00 60.69           C  
ANISOU 1058  C   SER A 179     9571   7187   6302  -1533    -32    119       C  
ATOM   1059  O   SER A 179     -37.899 -25.112  46.991  1.00 61.21           O  
ANISOU 1059  O   SER A 179     9639   7233   6384  -1445    -17    137       O  
ATOM   1060  CB  SER A 179     -38.313 -23.897  44.117  1.00 53.54           C  
ANISOU 1060  CB  SER A 179     8422   6391   5529  -1307    -38     50       C  
ATOM   1061  OG  SER A 179     -37.828 -23.692  42.808  1.00 51.02           O  
ANISOU 1061  OG  SER A 179     8113   6020   5252  -1205    -63     22       O  
ATOM   1062  N   ALA A 180     -39.715 -26.041  46.019  1.00 58.62           N  
ANISOU 1062  N   ALA A 180     9300   7018   5954  -1767    -21    126       N  
ATOM   1063  CA  ALA A 180     -40.432 -26.360  47.250  1.00 59.27           C  
ANISOU 1063  CA  ALA A 180     9390   7186   5945  -1954     22    159       C  
ATOM   1064  C   ALA A 180     -39.782 -27.582  47.878  1.00 64.19           C  
ANISOU 1064  C   ALA A 180    10328   7575   6488  -2025    -19    214       C  
ATOM   1065  O   ALA A 180     -39.521 -27.534  49.059  1.00 63.83           O  
ANISOU 1065  O   ALA A 180    10332   7515   6406  -2023      3    248       O  
ATOM   1066  CB  ALA A 180     -41.896 -26.632  46.958  1.00 61.39           C  
ANISOU 1066  CB  ALA A 180     9541   7644   6140  -2201     46    143       C  
ATOM   1067  N   VAL A 181     -39.482 -28.657  47.093  1.00 62.04           N  
ANISOU 1067  N   VAL A 181    10286   7107   6180  -2068    -88    220       N  
ATOM   1068  CA  VAL A 181     -38.816 -29.872  47.578  1.00 62.81           C  
ANISOU 1068  CA  VAL A 181    10727   6945   6195  -2100   -152    264       C  
ATOM   1069  C   VAL A 181     -37.447 -29.509  48.161  1.00 65.85           C  
ANISOU 1069  C   VAL A 181    11154   7218   6647  -1829   -177    267       C  
ATOM   1070  O   VAL A 181     -37.220 -29.833  49.330  1.00 67.37           O  
ANISOU 1070  O   VAL A 181    11484   7341   6774  -1863   -189    314       O  
ATOM   1071  CB  VAL A 181     -38.774 -31.001  46.515  1.00 68.33           C  
ANISOU 1071  CB  VAL A 181    11665   7455   6843  -2167   -229    252       C  
ATOM   1072  CG1 VAL A 181     -37.743 -32.073  46.848  1.00 68.58           C  
ANISOU 1072  CG1 VAL A 181    12054   7185   6817  -2074   -318    277       C  
ATOM   1073  CG2 VAL A 181     -40.146 -31.635  46.350  1.00 70.46           C  
ANISOU 1073  CG2 VAL A 181    11965   7807   7000  -2512   -218    269       C  
ATOM   1074  N   ILE A 182     -36.577 -28.778  47.393  1.00 59.84           N  
ANISOU 1074  N   ILE A 182    10262   6464   6009  -1577   -183    217       N  
ATOM   1075  CA  ILE A 182     -35.261 -28.281  47.852  1.00 58.98           C  
ANISOU 1075  CA  ILE A 182    10135   6299   5977  -1324   -202    207       C  
ATOM   1076  C   ILE A 182     -35.394 -27.414  49.116  1.00 63.21           C  
ANISOU 1076  C   ILE A 182    10533   6964   6520  -1326   -154    234       C  
ATOM   1077  O   ILE A 182     -34.684 -27.675  50.085  1.00 64.20           O  
ANISOU 1077  O   ILE A 182    10786   6989   6617  -1257   -194    261       O  
ATOM   1078  CB  ILE A 182     -34.461 -27.514  46.762  1.00 61.00           C  
ANISOU 1078  CB  ILE A 182    10235   6592   6351  -1109   -194    148       C  
ATOM   1079  CG1 ILE A 182     -33.924 -28.458  45.682  1.00 61.59           C  
ANISOU 1079  CG1 ILE A 182    10487   6505   6410  -1039   -248    112       C  
ATOM   1080  CG2 ILE A 182     -33.315 -26.676  47.395  1.00 60.47           C  
ANISOU 1080  CG2 ILE A 182    10064   6549   6364   -901   -192    138       C  
ATOM   1081  CD1 ILE A 182     -33.340 -27.721  44.454  1.00 69.24           C  
ANISOU 1081  CD1 ILE A 182    11296   7541   7470   -880   -220     52       C  
ATOM   1082  N   SER A 183     -36.285 -26.389  49.102  1.00 59.51           N  
ANISOU 1082  N   SER A 183     9815   6713   6082  -1389    -79    218       N  
ATOM   1083  CA  SER A 183     -36.525 -25.496  50.248  1.00 59.32           C  
ANISOU 1083  CA  SER A 183     9655   6827   6056  -1386    -27    228       C  
ATOM   1084  C   SER A 183     -37.057 -26.220  51.469  1.00 67.25           C  
ANISOU 1084  C   SER A 183    10806   7815   6929  -1575    -14    281       C  
ATOM   1085  O   SER A 183     -36.724 -25.839  52.588  1.00 66.41           O  
ANISOU 1085  O   SER A 183    10705   7724   6804  -1527     -3    299       O  
ATOM   1086  CB  SER A 183     -37.527 -24.407  49.890  1.00 60.24           C  
ANISOU 1086  CB  SER A 183     9503   7175   6212  -1413     40    189       C  
ATOM   1087  OG  SER A 183     -36.918 -23.413  49.087  1.00 66.41           O  
ANISOU 1087  OG  SER A 183    10151   7976   7107  -1219     31    149       O  
ATOM   1088  N   PHE A 184     -37.873 -27.257  51.223  1.00 68.84           N  
ANISOU 1088  N   PHE A 184    11139   7985   7032  -1802    -16    306       N  
ATOM   1089  CA  PHE A 184     -38.648 -28.087  52.143  1.00 72.85           C  
ANISOU 1089  CA  PHE A 184    11800   8495   7386  -2067      7    360       C  
ATOM   1090  C   PHE A 184     -39.251 -27.238  53.280  1.00 85.68           C  
ANISOU 1090  C   PHE A 184    13244  10336   8973  -2122    100    359       C  
ATOM   1091  O   PHE A 184     -38.812 -27.320  54.443  1.00 87.74           O  
ANISOU 1091  O   PHE A 184    13631  10533   9171  -2109     95    398       O  
ATOM   1092  CB  PHE A 184     -37.894 -29.337  52.635  1.00 75.29           C  
ANISOU 1092  CB  PHE A 184    12485   8521   7602  -2089    -86    419       C  
ATOM   1093  CG  PHE A 184     -38.874 -30.346  53.173  1.00 78.20           C  
ANISOU 1093  CG  PHE A 184    13046   8874   7794  -2428    -67    477       C  
ATOM   1094  CD1 PHE A 184     -39.736 -31.027  52.317  1.00 81.55           C  
ANISOU 1094  CD1 PHE A 184    13510   9310   8166  -2649    -67    472       C  
ATOM   1095  CD2 PHE A 184     -38.998 -30.556  54.543  1.00 80.82           C  
ANISOU 1095  CD2 PHE A 184    13508   9201   8001  -2552    -44    535       C  
ATOM   1096  CE1 PHE A 184     -40.688 -31.912  52.823  1.00 85.02           C  
ANISOU 1096  CE1 PHE A 184    14113   9759   8432  -3004    -42    526       C  
ATOM   1097  CE2 PHE A 184     -39.939 -31.452  55.048  1.00 85.51           C  
ANISOU 1097  CE2 PHE A 184    14278   9798   8414  -2902    -13    592       C  
ATOM   1098  CZ  PHE A 184     -40.773 -32.131  54.185  1.00 85.06           C  
ANISOU 1098  CZ  PHE A 184    14255   9755   8308  -3135    -12    587       C  
ATOM   1099  N   PRO A 185     -40.257 -26.384  52.933  1.00 85.96           N  
ANISOU 1099  N   PRO A 185    12984  10635   9043  -2162    179    305       N  
ATOM   1100  CA  PRO A 185     -40.860 -25.487  53.942  1.00 87.86           C  
ANISOU 1100  CA  PRO A 185    13031  11102   9249  -2177    271    282       C  
ATOM   1101  C   PRO A 185     -41.458 -26.125  55.231  1.00 96.37           C  
ANISOU 1101  C   PRO A 185    14229  12236  10152  -2428    334    331       C  
ATOM   1102  O   PRO A 185     -41.273 -25.462  56.257  1.00 94.80           O  
ANISOU 1102  O   PRO A 185    13982  12105   9932  -2347    376    325       O  
ATOM   1103  CB  PRO A 185     -41.923 -24.740  53.130  1.00 89.52           C  
ANISOU 1103  CB  PRO A 185    12935  11567   9510  -2185    322    210       C  
ATOM   1104  CG  PRO A 185     -41.362 -24.738  51.715  1.00 91.38           C  
ANISOU 1104  CG  PRO A 185    13185  11672   9862  -2045    242    193       C  
ATOM   1105  CD  PRO A 185     -40.853 -26.132  51.602  1.00 87.02           C  
ANISOU 1105  CD  PRO A 185    12944  10874   9247  -2163    178    254       C  
ATOM   1106  N   PRO A 186     -42.088 -27.351  55.283  1.00 98.46           N  
ANISOU 1106  N   PRO A 186    14672  12460  10279  -2732    339    381       N  
ATOM   1107  CA  PRO A 186     -42.631 -27.857  56.565  1.00101.83           C  
ANISOU 1107  CA  PRO A 186    15218  12951  10522  -2986    409    431       C  
ATOM   1108  C   PRO A 186     -41.755 -27.711  57.820  1.00110.04           C  
ANISOU 1108  C   PRO A 186    16431  13864  11516  -2872    391    474       C  
ATOM   1109  O   PRO A 186     -42.315 -27.541  58.913  1.00111.73           O  
ANISOU 1109  O   PRO A 186    16612  14236  11605  -3011    485    483       O  
ATOM   1110  CB  PRO A 186     -42.914 -29.326  56.261  1.00104.94           C  
ANISOU 1110  CB  PRO A 186    15901  13178  10792  -3275    360    497       C  
ATOM   1111  CG  PRO A 186     -43.309 -29.311  54.856  1.00108.20           C  
ANISOU 1111  CG  PRO A 186    16164  13645  11302  -3266    333    446       C  
ATOM   1112  CD  PRO A 186     -42.434 -28.287  54.191  1.00101.12           C  
ANISOU 1112  CD  PRO A 186    15109  12711  10602  -2887    287    391       C  
ATOM   1113  N   LEU A 187     -40.409 -27.754  57.685  1.00106.72           N  
ANISOU 1113  N   LEU A 187    16178  13183  11187  -2621    274    495       N  
ATOM   1114  CA  LEU A 187     -39.544 -27.564  58.851  1.00106.42           C  
ANISOU 1114  CA  LEU A 187    16287  13038  11112  -2497    239    529       C  
ATOM   1115  C   LEU A 187     -38.358 -26.624  58.564  1.00106.44           C  
ANISOU 1115  C   LEU A 187    16180  12971  11289  -2142    171    484       C  
ATOM   1116  O   LEU A 187     -37.293 -27.060  58.118  1.00106.41           O  
ANISOU 1116  O   LEU A 187    16332  12745  11352  -1984     56    500       O  
ATOM   1117  CB  LEU A 187     -39.098 -28.907  59.464  1.00108.22           C  
ANISOU 1117  CB  LEU A 187    16934  12995  11189  -2631    150    624       C  
ATOM   1118  CG  LEU A 187     -38.767 -28.929  60.970  1.00113.80           C  
ANISOU 1118  CG  LEU A 187    17820  13656  11763  -2655    148    676       C  
ATOM   1119  CD1 LEU A 187     -39.805 -28.163  61.826  1.00114.31           C  
ANISOU 1119  CD1 LEU A 187    17662  14033  11738  -2806    311    647       C  
ATOM   1120  CD2 LEU A 187     -38.627 -30.360  61.458  1.00118.36           C  
ANISOU 1120  CD2 LEU A 187    18835  13976  12158  -2851     62    775       C  
ATOM   1121  N   VAL A 188     -38.578 -25.319  58.813  1.00 99.20           N  
ANISOU 1121  N   VAL A 188    14991  12260  10439  -2023    244    422       N  
ATOM   1122  CA  VAL A 188     -37.586 -24.250  58.655  1.00 95.99           C  
ANISOU 1122  CA  VAL A 188    14464  11826  10180  -1730    196    378       C  
ATOM   1123  C   VAL A 188     -37.423 -23.440  59.971  1.00 96.73           C  
ANISOU 1123  C   VAL A 188    14529  12001  10222  -1667    229    367       C  
ATOM   1124  O   VAL A 188     -36.297 -23.117  60.340  1.00 94.34           O  
ANISOU 1124  O   VAL A 188    14297  11577   9972  -1489    147    372       O  
ATOM   1125  CB  VAL A 188     -37.818 -23.340  57.409  1.00 98.75           C  
ANISOU 1125  CB  VAL A 188    14546  12293  10680  -1603    218    306       C  
ATOM   1126  CG1 VAL A 188     -37.344 -24.016  56.122  1.00 97.93           C  
ANISOU 1126  CG1 VAL A 188    14517  12036  10656  -1565    143    314       C  
ATOM   1127  CG2 VAL A 188     -39.270 -22.881  57.291  1.00 99.42           C  
ANISOU 1127  CG2 VAL A 188    14404  12646  10725  -1733    330    257       C  
ATOM   1128  N   SER A 189     -38.551 -23.188  60.693  1.00 93.52           N  
ANISOU 1128  N   SER A 189    14028  11807   9700  -1826    348    349       N  
ATOM   1129  CA  SER A 189     -38.706 -22.422  61.952  1.00 92.71           C  
ANISOU 1129  CA  SER A 189    13882  11829   9515  -1801    411    324       C  
ATOM   1130  C   SER A 189     -38.005 -22.997  63.196  1.00 95.48           C  
ANISOU 1130  C   SER A 189    14516  12022   9739  -1841    355    395       C  
ATOM   1131  O   SER A 189     -37.682 -24.190  63.234  1.00 96.03           O  
ANISOU 1131  O   SER A 189    14843  11905   9739  -1952    285    473       O  
ATOM   1132  CB  SER A 189     -40.192 -22.230  62.258  1.00 96.80           C  
ANISOU 1132  CB  SER A 189    14221  12636   9923  -1984    563    280       C  
ATOM   1133  OG  SER A 189     -40.429 -21.469  63.433  1.00102.47           O  
ANISOU 1133  OG  SER A 189    14886  13498  10551  -1952    638    241       O  
ATOM   1134  N   LEU A 190     -37.837 -22.126  64.236  1.00 90.71           N  
ANISOU 1134  N   LEU A 190    13878  11496   9093  -1751    383    364       N  
ATOM   1135  CA  LEU A 190     -37.234 -22.367  65.560  1.00102.32           C  
ANISOU 1135  CA  LEU A 190    15583  12861  10434  -1764    336    414       C  
ATOM   1136  C   LEU A 190     -35.827 -22.932  65.473  1.00115.31           C  
ANISOU 1136  C   LEU A 190    17446  14227  12140  -1627    160    470       C  
ATOM   1137  O   LEU A 190     -34.870 -22.166  65.524  1.00 73.68           O  
ANISOU 1137  O   LEU A 190    12118   8904   6974  -1411     80    437       O  
ATOM   1138  CB  LEU A 190     -38.137 -23.233  66.469  1.00104.70           C  
ANISOU 1138  CB  LEU A 190    16046  13231  10504  -2059    429    470       C  
ATOM   1139  CG  LEU A 190     -37.748 -23.386  67.959  1.00110.91           C  
ANISOU 1139  CG  LEU A 190    17073  13950  11116  -2102    406    518       C  
ATOM   1140  CD1 LEU A 190     -38.056 -22.119  68.770  1.00110.98           C  
ANISOU 1140  CD1 LEU A 190    16909  14167  11092  -2011    500    434       C  
ATOM   1141  CD2 LEU A 190     -38.474 -24.575  68.588  1.00115.92           C  
ANISOU 1141  CD2 LEU A 190    17945  14579  11519  -2430    467    603       C  
ATOM   1142  N   ALA A 197     -39.992 -17.982  74.731  1.00107.68           N  
ANISOU 1142  N   ALA A 197    16341  14631   9943  -1908   1010     85       N  
ATOM   1143  CA  ALA A 197     -39.838 -16.739  73.982  1.00105.54           C  
ANISOU 1143  CA  ALA A 197    15830  14392   9877  -1628    973    -25       C  
ATOM   1144  C   ALA A 197     -40.721 -15.603  74.558  1.00111.16           C  
ANISOU 1144  C   ALA A 197    16356  15381  10497  -1526   1122   -174       C  
ATOM   1145  O   ALA A 197     -41.915 -15.513  74.231  1.00111.14           O  
ANISOU 1145  O   ALA A 197    16115  15651  10463  -1585   1277   -249       O  
ATOM   1146  CB  ALA A 197     -40.133 -16.974  72.504  1.00104.75           C  
ANISOU 1146  CB  ALA A 197    15532  14301   9965  -1619    962    -22       C  
ATOM   1147  N   ALA A 198     -40.118 -14.755  75.453  1.00108.43           N  
ANISOU 1147  N   ALA A 198    16129  14969  10100  -1368   1067   -223       N  
ATOM   1148  CA  ALA A 198     -40.756 -13.595  76.118  1.00108.96           C  
ANISOU 1148  CA  ALA A 198    16081  15249  10070  -1226   1179   -374       C  
ATOM   1149  C   ALA A 198     -41.157 -12.615  75.015  1.00109.21           C  
ANISOU 1149  C   ALA A 198    15836  15367  10293  -1002   1179   -485       C  
ATOM   1150  O   ALA A 198     -42.332 -12.592  74.632  1.00109.63           O  
ANISOU 1150  O   ALA A 198    15648  15685  10321  -1034   1323   -560       O  
ATOM   1151  CB  ALA A 198     -39.791 -12.948  77.117  1.00109.55           C  
ANISOU 1151  CB  ALA A 198    16381  15159  10084  -1098   1068   -387       C  
ATOM   1152  N   TYR A 199     -40.176 -11.877  74.454  1.00101.68           N  
ANISOU 1152  N   TYR A 199    14920  14190   9526   -795   1010   -490       N  
ATOM   1153  CA  TYR A 199     -40.381 -11.058  73.266  1.00 98.99           C  
ANISOU 1153  CA  TYR A 199    14372  13864   9376   -602    974   -564       C  
ATOM   1154  C   TYR A 199     -39.885 -11.979  72.168  1.00 95.22           C  
ANISOU 1154  C   TYR A 199    13890  13232   9057   -707    887   -442       C  
ATOM   1155  O   TYR A 199     -38.709 -12.360  72.174  1.00 93.90           O  
ANISOU 1155  O   TYR A 199    13903  12821   8953   -728    747   -345       O  
ATOM   1156  CB  TYR A 199     -39.659  -9.709  73.324  1.00100.33           C  
ANISOU 1156  CB  TYR A 199    14607  13888   9627   -350    854   -640       C  
ATOM   1157  CG  TYR A 199     -40.611  -8.598  73.706  1.00105.32           C  
ANISOU 1157  CG  TYR A 199    15119  14728  10168   -169    956   -809       C  
ATOM   1158  CD1 TYR A 199     -41.454  -8.019  72.760  1.00107.37           C  
ANISOU 1158  CD1 TYR A 199    15148  15129  10520    -21    995   -903       C  
ATOM   1159  CD2 TYR A 199     -40.729  -8.179  75.028  1.00108.66           C  
ANISOU 1159  CD2 TYR A 199    15664  15224  10399   -138   1015   -881       C  
ATOM   1160  CE1 TYR A 199     -42.362  -7.021  73.113  1.00110.64           C  
ANISOU 1160  CE1 TYR A 199    15450  15745  10844    178   1081  -1072       C  
ATOM   1161  CE2 TYR A 199     -41.648  -7.198  75.398  1.00111.92           C  
ANISOU 1161  CE2 TYR A 199    15965  15845  10713     48   1116  -1051       C  
ATOM   1162  CZ  TYR A 199     -42.452  -6.609  74.434  1.00122.04           C  
ANISOU 1162  CZ  TYR A 199    17013  17260  12097    218   1145  -1149       C  
ATOM   1163  OH  TYR A 199     -43.341  -5.621  74.795  1.00127.32           O  
ANISOU 1163  OH  TYR A 199    17577  18132  12668    441   1229  -1330       O  
ATOM   1164  N   PRO A 200     -40.820 -12.515  71.354  1.00 86.88           N  
ANISOU 1164  N   PRO A 200    12642  12336   8031   -804    979   -443       N  
ATOM   1165  CA  PRO A 200     -40.447 -13.568  70.398  1.00 83.57           C  
ANISOU 1165  CA  PRO A 200    12246  11779   7726   -937    911   -325       C  
ATOM   1166  C   PRO A 200     -39.471 -13.181  69.301  1.00 80.98           C  
ANISOU 1166  C   PRO A 200    11919  11230   7619   -783    754   -299       C  
ATOM   1167  O   PRO A 200     -39.418 -12.024  68.878  1.00 79.64           O  
ANISOU 1167  O   PRO A 200    11655  11060   7545   -577    715   -383       O  
ATOM   1168  CB  PRO A 200     -41.790 -14.005  69.820  1.00 86.59           C  
ANISOU 1168  CB  PRO A 200    12401  12421   8079  -1061   1050   -361       C  
ATOM   1169  CG  PRO A 200     -42.688 -12.821  70.004  1.00 92.45           C  
ANISOU 1169  CG  PRO A 200    12935  13407   8784   -879   1142   -519       C  
ATOM   1170  CD  PRO A 200     -42.269 -12.226  71.299  1.00 89.17           C  
ANISOU 1170  CD  PRO A 200    12682  12956   8242   -801   1145   -557       C  
ATOM   1171  N   GLN A 201     -38.714 -14.182  68.834  1.00 73.35           N  
ANISOU 1171  N   GLN A 201    11071  10078   6722   -887    665   -183       N  
ATOM   1172  CA  GLN A 201     -37.760 -14.036  67.742  1.00 69.90           C  
ANISOU 1172  CA  GLN A 201    10629   9448   6481   -777    530   -149       C  
ATOM   1173  C   GLN A 201     -38.128 -14.960  66.589  1.00 72.56           C  
ANISOU 1173  C   GLN A 201    10887   9789   6894   -888    544    -98       C  
ATOM   1174  O   GLN A 201     -38.755 -15.999  66.818  1.00 73.36           O  
ANISOU 1174  O   GLN A 201    11024   9961   6887  -1088    618    -50       O  
ATOM   1175  CB  GLN A 201     -36.331 -14.311  68.218  1.00 70.09           C  
ANISOU 1175  CB  GLN A 201    10867   9241   6525   -756    389    -76       C  
ATOM   1176  CG  GLN A 201     -35.755 -13.240  69.145  1.00 79.67           C  
ANISOU 1176  CG  GLN A 201    12156  10417   7699   -626    336   -131       C  
ATOM   1177  CD  GLN A 201     -35.777 -11.823  68.617  1.00 99.97           C  
ANISOU 1177  CD  GLN A 201    14603  13009  10374   -440    317   -227       C  
ATOM   1178  OE1 GLN A 201     -35.582 -11.540  67.418  1.00 94.51           O  
ANISOU 1178  OE1 GLN A 201    13808  12267   9835   -372    273   -230       O  
ATOM   1179  NE2 GLN A 201     -35.997 -10.897  69.532  1.00 92.56           N  
ANISOU 1179  NE2 GLN A 201    13700  12132   9337   -356    343   -308       N  
ATOM   1180  N   CYS A 202     -37.760 -14.582  65.348  1.00 66.24           N  
ANISOU 1180  N   CYS A 202     9991   8911   6267   -773    474   -107       N  
ATOM   1181  CA  CYS A 202     -38.054 -15.408  64.185  1.00 65.07           C  
ANISOU 1181  CA  CYS A 202     9777   8753   6192   -864    476    -65       C  
ATOM   1182  C   CYS A 202     -36.779 -15.798  63.498  1.00 67.68           C  
ANISOU 1182  C   CYS A 202    10212   8854   6647   -816    348      1       C  
ATOM   1183  O   CYS A 202     -36.211 -15.003  62.740  1.00 67.71           O  
ANISOU 1183  O   CYS A 202    10151   8795   6783   -670    284    -28       O  
ATOM   1184  CB  CYS A 202     -39.007 -14.702  63.229  1.00 65.32           C  
ANISOU 1184  CB  CYS A 202     9580   8946   6294   -785    528   -146       C  
ATOM   1185  SG  CYS A 202     -39.595 -15.735  61.857  1.00 68.70           S  
ANISOU 1185  SG  CYS A 202     9917   9403   6783   -924    541   -105       S  
ATOM   1186  N   GLY A 203     -36.349 -17.026  63.745  1.00 62.90           N  
ANISOU 1186  N   GLY A 203     9775   8131   5992   -939    310     86       N  
ATOM   1187  CA  GLY A 203     -35.123 -17.542  63.154  1.00 60.85           C  
ANISOU 1187  CA  GLY A 203     9617   7668   5835   -880    187    140       C  
ATOM   1188  C   GLY A 203     -35.230 -18.929  62.580  1.00 62.25           C  
ANISOU 1188  C   GLY A 203     9892   7763   5997  -1011    173    206       C  
ATOM   1189  O   GLY A 203     -36.132 -19.691  62.927  1.00 63.23           O  
ANISOU 1189  O   GLY A 203    10071   7956   5999  -1194    247    235       O  
ATOM   1190  N   LEU A 204     -34.282 -19.262  61.711  1.00 56.62           N  
ANISOU 1190  N   LEU A 204     9211   6903   5399   -924     79    227       N  
ATOM   1191  CA  LEU A 204     -34.207 -20.552  61.034  1.00 56.11           C  
ANISOU 1191  CA  LEU A 204     9262   6725   5334  -1006     43    280       C  
ATOM   1192  C   LEU A 204     -33.657 -21.636  61.932  1.00 61.04           C  
ANISOU 1192  C   LEU A 204    10152   7194   5846  -1062    -34    350       C  
ATOM   1193  O   LEU A 204     -33.070 -21.333  62.959  1.00 61.48           O  
ANISOU 1193  O   LEU A 204    10287   7218   5854  -1001    -81    357       O  
ATOM   1194  CB  LEU A 204     -33.296 -20.434  59.804  1.00 54.51           C  
ANISOU 1194  CB  LEU A 204     8993   6430   5287   -860    -30    262       C  
ATOM   1195  CG  LEU A 204     -33.910 -20.003  58.502  1.00 57.49           C  
ANISOU 1195  CG  LEU A 204     9191   6897   5756   -856     25    221       C  
ATOM   1196  CD1 LEU A 204     -32.831 -19.773  57.493  1.00 56.48           C  
ANISOU 1196  CD1 LEU A 204     9017   6682   5761   -709    -44    202       C  
ATOM   1197  CD2 LEU A 204     -34.858 -21.049  57.968  1.00 60.45           C  
ANISOU 1197  CD2 LEU A 204     9611   7285   6073  -1025     68    248       C  
ATOM   1198  N   ASN A 205     -33.789 -22.898  61.511  1.00 59.48           N  
ANISOU 1198  N   ASN A 205    10113   6883   5603  -1167    -63    401       N  
ATOM   1199  CA  ASN A 205     -33.219 -24.048  62.201  1.00 61.26           C  
ANISOU 1199  CA  ASN A 205    10638   6917   5719  -1203   -162    472       C  
ATOM   1200  C   ASN A 205     -31.676 -23.916  62.117  1.00 65.40           C  
ANISOU 1200  C   ASN A 205    11192   7309   6348   -957   -306    456       C  
ATOM   1201  O   ASN A 205     -31.132 -23.528  61.081  1.00 64.35           O  
ANISOU 1201  O   ASN A 205    10903   7183   6363   -819   -327    409       O  
ATOM   1202  CB  ASN A 205     -33.747 -25.352  61.574  1.00 64.54           C  
ANISOU 1202  CB  ASN A 205    11219   7230   6072  -1364   -166    518       C  
ATOM   1203  CG  ASN A 205     -33.075 -26.611  62.043  1.00100.24           C  
ANISOU 1203  CG  ASN A 205    16088  11507  10491  -1367   -298    587       C  
ATOM   1204  OD1 ASN A 205     -32.712 -26.767  63.212  1.00103.57           O  
ANISOU 1204  OD1 ASN A 205    16686  11862  10803  -1365   -353    628       O  
ATOM   1205  ND2 ASN A 205     -32.906 -27.542  61.130  1.00 94.71           N  
ANISOU 1205  ND2 ASN A 205    15511  10661   9814  -1362   -359    598       N  
ATOM   1206  N   ASP A 206     -31.011 -24.161  63.234  1.00 64.27           N  
ANISOU 1206  N   ASP A 206    11229   7073   6118   -910   -398    491       N  
ATOM   1207  CA  ASP A 206     -29.576 -23.991  63.461  1.00 64.70           C  
ANISOU 1207  CA  ASP A 206    11302   7038   6242   -688   -542    472       C  
ATOM   1208  C   ASP A 206     -28.740 -25.298  63.280  1.00 67.64           C  
ANISOU 1208  C   ASP A 206    11915   7196   6589   -591   -694    506       C  
ATOM   1209  O   ASP A 206     -27.522 -25.280  63.495  1.00 68.24           O  
ANISOU 1209  O   ASP A 206    12005   7210   6712   -393   -828    484       O  
ATOM   1210  CB  ASP A 206     -29.405 -23.423  64.900  1.00 68.45           C  
ANISOU 1210  CB  ASP A 206    11836   7552   6620   -690   -565    483       C  
ATOM   1211  CG  ASP A 206     -28.066 -22.785  65.220  1.00 89.53           C  
ANISOU 1211  CG  ASP A 206    14435  10209   9372   -483   -689    444       C  
ATOM   1212  OD1 ASP A 206     -27.539 -22.044  64.356  1.00 91.38           O  
ANISOU 1212  OD1 ASP A 206    14442  10512   9764   -369   -686    383       O  
ATOM   1213  OD2 ASP A 206     -27.546 -23.019  66.343  1.00 97.90           O1-
ANISOU 1213  OD2 ASP A 206    15671  11197  10330   -449   -794    474       O1-
ATOM   1214  N   GLU A 207     -29.380 -26.414  62.893  1.00 61.18           N  
ANISOU 1214  N   GLU A 207    11287   6270   5691   -724   -682    552       N  
ATOM   1215  CA  GLU A 207     -28.678 -27.688  62.736  1.00 61.32           C  
ANISOU 1215  CA  GLU A 207    11576   6059   5663   -625   -833    580       C  
ATOM   1216  C   GLU A 207     -27.643 -27.695  61.614  1.00 63.96           C  
ANISOU 1216  C   GLU A 207    11775   6367   6159   -382   -905    508       C  
ATOM   1217  O   GLU A 207     -27.930 -27.171  60.545  1.00 62.80           O  
ANISOU 1217  O   GLU A 207    11397   6334   6131   -391   -807    461       O  
ATOM   1218  CB  GLU A 207     -29.684 -28.835  62.564  1.00 63.98           C  
ANISOU 1218  CB  GLU A 207    12168   6278   5863   -857   -799    645       C  
ATOM   1219  CG  GLU A 207     -30.497 -29.150  63.810  1.00 71.24           C  
ANISOU 1219  CG  GLU A 207    13307   7185   6578  -1100   -759    726       C  
ATOM   1220  CD  GLU A 207     -29.691 -29.355  65.079  1.00 85.21           C  
ANISOU 1220  CD  GLU A 207    15303   8834   8240   -998   -899    767       C  
ATOM   1221  OE1 GLU A 207     -28.611 -29.991  65.010  1.00 75.30           O1-
ANISOU 1221  OE1 GLU A 207    14215   7394   7001   -779  -1078    763       O1-
ATOM   1222  OE2 GLU A 207     -30.131 -28.853  66.140  1.00 63.90           O  
ANISOU 1222  OE2 GLU A 207    12606   6235   5437  -1122   -834    795       O  
ATOM   1223  N   THR A 208     -26.451 -28.294  61.854  1.00 60.85           N  
ANISOU 1223  N   THR A 208    11525   5833   5761   -161  -1079    497       N  
ATOM   1224  CA  THR A 208     -25.334 -28.374  60.890  1.00 60.36           C  
ANISOU 1224  CA  THR A 208    11333   5766   5836     96  -1156    416       C  
ATOM   1225  C   THR A 208     -25.731 -29.018  59.555  1.00 65.07           C  
ANISOU 1225  C   THR A 208    11951   6303   6470     69  -1106    394       C  
ATOM   1226  O   THR A 208     -25.465 -28.435  58.506  1.00 63.31           O  
ANISOU 1226  O   THR A 208    11469   6203   6385    145  -1039    325       O  
ATOM   1227  CB  THR A 208     -24.097 -29.068  61.509  1.00 69.41           C  
ANISOU 1227  CB  THR A 208    12662   6772   6938    342  -1366    404       C  
ATOM   1228  OG1 THR A 208     -23.641 -28.348  62.662  1.00 72.33           O  
ANISOU 1228  OG1 THR A 208    12973   7222   7288    377  -1418    413       O  
ATOM   1229  CG2 THR A 208     -22.947 -29.257  60.506  1.00 64.28           C  
ANISOU 1229  CG2 THR A 208    11869   6139   6415    619  -1442    306       C  
ATOM   1230  N   TRP A 209     -26.346 -30.223  59.599  1.00 63.90           N  
ANISOU 1230  N   TRP A 209    12134   5960   6187    -50  -1143    452       N  
ATOM   1231  CA  TRP A 209     -26.797 -30.983  58.423  1.00 63.12           C  
ANISOU 1231  CA  TRP A 209    12121   5770   6092   -101  -1114    438       C  
ATOM   1232  C   TRP A 209     -27.758 -30.132  57.638  1.00 64.86           C  
ANISOU 1232  C   TRP A 209    12062   6185   6395   -281   -931    422       C  
ATOM   1233  O   TRP A 209     -27.762 -30.218  56.421  1.00 65.35           O  
ANISOU 1233  O   TRP A 209    12030   6263   6536   -239   -894    371       O  
ATOM   1234  CB  TRP A 209     -27.469 -32.334  58.811  1.00 63.58           C  
ANISOU 1234  CB  TRP A 209    12614   5583   5961   -273  -1180    520       C  
ATOM   1235  CG  TRP A 209     -28.735 -32.199  59.616  1.00 64.85           C  
ANISOU 1235  CG  TRP A 209    12845   5799   5996   -610  -1073    608       C  
ATOM   1236  CD1 TRP A 209     -28.846 -32.209  60.978  1.00 68.62           C  
ANISOU 1236  CD1 TRP A 209    13483   6246   6342   -701  -1106    677       C  
ATOM   1237  CD2 TRP A 209     -30.057 -31.960  59.108  1.00 64.35           C  
ANISOU 1237  CD2 TRP A 209    12659   5867   5925   -894   -908    624       C  
ATOM   1238  NE1 TRP A 209     -30.157 -32.017  61.350  1.00 68.15           N  
ANISOU 1238  NE1 TRP A 209    13409   6297   6187  -1030   -959    733       N  
ATOM   1239  CE2 TRP A 209     -30.919 -31.832  60.224  1.00 69.10           C  
ANISOU 1239  CE2 TRP A 209    13336   6531   6388  -1147   -838    697       C  
ATOM   1240  CE3 TRP A 209     -30.598 -31.815  57.811  1.00 64.75           C  
ANISOU 1240  CE3 TRP A 209    12530   6005   6067   -955   -814    578       C  
ATOM   1241  CZ2 TRP A 209     -32.288 -31.549  60.086  1.00 68.42           C  
ANISOU 1241  CZ2 TRP A 209    13121   6614   6260  -1446   -675    716       C  
ATOM   1242  CZ3 TRP A 209     -31.950 -31.527  57.675  1.00 66.10           C  
ANISOU 1242  CZ3 TRP A 209    12585   6330   6201  -1247   -669    602       C  
ATOM   1243  CH2 TRP A 209     -32.781 -31.403  58.802  1.00 67.77           C  
ANISOU 1243  CH2 TRP A 209    12848   6621   6280  -1485   -599    667       C  
ATOM   1244  N   TYR A 210     -28.576 -29.310  58.330  1.00 58.72           N  
ANISOU 1244  N   TYR A 210    11161   5559   5592   -469   -822    460       N  
ATOM   1245  CA  TYR A 210     -29.540 -28.468  57.655  1.00 56.47           C  
ANISOU 1245  CA  TYR A 210    10614   5465   5375   -619   -663    440       C  
ATOM   1246  C   TYR A 210     -28.846 -27.329  56.931  1.00 56.97           C  
ANISOU 1246  C   TYR A 210    10354   5680   5610   -441   -628    362       C  
ATOM   1247  O   TYR A 210     -29.075 -27.165  55.733  1.00 57.07           O  
ANISOU 1247  O   TYR A 210    10235   5747   5703   -443   -568    323       O  
ATOM   1248  CB  TYR A 210     -30.661 -27.982  58.600  1.00 58.38           C  
ANISOU 1248  CB  TYR A 210    10825   5833   5525   -853   -558    489       C  
ATOM   1249  CG  TYR A 210     -31.469 -26.845  58.013  1.00 59.29           C  
ANISOU 1249  CG  TYR A 210    10621   6176   5729   -929   -414    447       C  
ATOM   1250  CD1 TYR A 210     -32.352 -27.064  56.957  1.00 60.76           C  
ANISOU 1250  CD1 TYR A 210    10743   6410   5934  -1057   -342    435       C  
ATOM   1251  CD2 TYR A 210     -31.279 -25.529  58.447  1.00 59.37           C  
ANISOU 1251  CD2 TYR A 210    10404   6345   5811   -850   -367    413       C  
ATOM   1252  CE1 TYR A 210     -33.030 -26.006  56.350  1.00 62.42           C  
ANISOU 1252  CE1 TYR A 210    10665   6823   6229  -1088   -233    390       C  
ATOM   1253  CE2 TYR A 210     -31.965 -24.463  57.859  1.00 59.19           C  
ANISOU 1253  CE2 TYR A 210    10114   6508   5867   -884   -256    369       C  
ATOM   1254  CZ  TYR A 210     -32.837 -24.706  56.804  1.00 70.20           C  
ANISOU 1254  CZ  TYR A 210    11444   7949   7279   -994   -192    358       C  
ATOM   1255  OH  TYR A 210     -33.522 -23.671  56.201  1.00 71.25           O  
ANISOU 1255  OH  TYR A 210    11328   8261   7485  -1007   -102    312       O  
ATOM   1256  N   ILE A 211     -27.995 -26.547  57.637  1.00 50.77           N  
ANISOU 1256  N   ILE A 211     9457   4961   4872   -304   -669    342       N  
ATOM   1257  CA  ILE A 211     -27.309 -25.386  57.052  1.00 47.48           C  
ANISOU 1257  CA  ILE A 211     8746   4692   4603   -171   -636    275       C  
ATOM   1258  C   ILE A 211     -26.665 -25.760  55.719  1.00 53.31           C  
ANISOU 1258  C   ILE A 211     9428   5402   5428    -36   -655    217       C  
ATOM   1259  O   ILE A 211     -26.988 -25.155  54.694  1.00 52.36           O  
ANISOU 1259  O   ILE A 211     9127   5383   5386    -71   -562    184       O  
ATOM   1260  CB  ILE A 211     -26.341 -24.694  58.034  1.00 48.54           C  
ANISOU 1260  CB  ILE A 211     8811   4875   4759    -48   -707    260       C  
ATOM   1261  CG1 ILE A 211     -27.109 -24.137  59.221  1.00 46.64           C  
ANISOU 1261  CG1 ILE A 211     8598   4689   4432   -193   -659    305       C  
ATOM   1262  CG2 ILE A 211     -25.550 -23.591  57.323  1.00 48.53           C  
ANISOU 1262  CG2 ILE A 211     8527   5013   4898     64   -680    190       C  
ATOM   1263  CD1 ILE A 211     -26.289 -23.733  60.335  1.00 49.48           C  
ANISOU 1263  CD1 ILE A 211     8972   5056   4770   -101   -749    304       C  
ATOM   1264  N   LEU A 212     -25.869 -26.831  55.731  1.00 51.86           N  
ANISOU 1264  N   LEU A 212     9426   5070   5209    113   -775    205       N  
ATOM   1265  CA  LEU A 212     -25.162 -27.368  54.572  1.00 52.18           C  
ANISOU 1265  CA  LEU A 212     9449   5071   5307    275   -807    138       C  
ATOM   1266  C   LEU A 212     -26.108 -27.946  53.502  1.00 58.22           C  
ANISOU 1266  C   LEU A 212    10297   5775   6048    146   -737    145       C  
ATOM   1267  O   LEU A 212     -25.969 -27.564  52.334  1.00 57.73           O  
ANISOU 1267  O   LEU A 212    10064   5801   6070    186   -671     90       O  
ATOM   1268  CB  LEU A 212     -24.076 -28.373  55.009  1.00 53.13           C  
ANISOU 1268  CB  LEU A 212     9760   5046   5382    500   -972    114       C  
ATOM   1269  CG  LEU A 212     -23.130 -27.856  56.110  1.00 56.34           C  
ANISOU 1269  CG  LEU A 212    10088   5517   5803    628  -1063    105       C  
ATOM   1270  CD1 LEU A 212     -22.222 -28.964  56.631  1.00 57.59           C  
ANISOU 1270  CD1 LEU A 212    10477   5513   5892    851  -1249     88       C  
ATOM   1271  CD2 LEU A 212     -22.379 -26.573  55.680  1.00 53.65           C  
ANISOU 1271  CD2 LEU A 212     9384   5403   5598    697  -1001     37       C  
ATOM   1272  N   SER A 213     -27.090 -28.808  53.886  1.00 55.16           N  
ANISOU 1272  N   SER A 213    10167   5253   5540    -31   -748    212       N  
ATOM   1273  CA  SER A 213     -28.084 -29.349  52.930  1.00 54.36           C  
ANISOU 1273  CA  SER A 213    10145   5106   5404   -193   -688    221       C  
ATOM   1274  C   SER A 213     -28.749 -28.217  52.130  1.00 55.93           C  
ANISOU 1274  C   SER A 213    10048   5508   5695   -295   -550    199       C  
ATOM   1275  O   SER A 213     -28.801 -28.292  50.904  1.00 55.61           O  
ANISOU 1275  O   SER A 213     9948   5482   5700   -273   -516    155       O  
ATOM   1276  CB  SER A 213     -29.180 -30.116  53.655  1.00 57.07           C  
ANISOU 1276  CB  SER A 213    10744   5339   5599   -439   -693    305       C  
ATOM   1277  OG  SER A 213     -28.615 -31.294  54.188  1.00 75.04           O  
ANISOU 1277  OG  SER A 213    13354   7384   7774   -349   -835    328       O  
ATOM   1278  N   SER A 214     -29.230 -27.170  52.834  1.00 49.24           N  
ANISOU 1278  N   SER A 214     9034   4809   4865   -389   -481    225       N  
ATOM   1279  CA  SER A 214     -29.916 -26.048  52.233  1.00 47.55           C  
ANISOU 1279  CA  SER A 214     8568   4776   4723   -470   -369    207       C  
ATOM   1280  C   SER A 214     -28.983 -25.145  51.380  1.00 50.97           C  
ANISOU 1280  C   SER A 214     8784   5302   5282   -302   -351    142       C  
ATOM   1281  O   SER A 214     -29.446 -24.654  50.351  1.00 50.50           O  
ANISOU 1281  O   SER A 214     8595   5324   5269   -345   -284    118       O  
ATOM   1282  CB  SER A 214     -30.689 -25.264  53.285  1.00 51.32           C  
ANISOU 1282  CB  SER A 214     8963   5371   5165   -596   -311    243       C  
ATOM   1283  OG  SER A 214     -29.840 -24.706  54.273  1.00 65.35           O  
ANISOU 1283  OG  SER A 214    10707   7163   6959   -481   -354    242       O  
ATOM   1284  N   CYS A 215     -27.688 -24.971  51.760  1.00 45.80           N  
ANISOU 1284  N   CYS A 215     8093   4639   4670   -123   -415    113       N  
ATOM   1285  CA  CYS A 215     -26.720 -24.181  50.997  1.00 44.80           C  
ANISOU 1285  CA  CYS A 215     7763   4613   4646     10   -395     51       C  
ATOM   1286  C   CYS A 215     -26.370 -24.848  49.671  1.00 50.66           C  
ANISOU 1286  C   CYS A 215     8530   5312   5405     89   -391      0       C  
ATOM   1287  O   CYS A 215     -26.173 -24.163  48.661  1.00 50.97           O  
ANISOU 1287  O   CYS A 215     8408   5452   5508    103   -326    -39       O  
ATOM   1288  CB  CYS A 215     -25.472 -23.921  51.824  1.00 46.34           C  
ANISOU 1288  CB  CYS A 215     7908   4831   4869    159   -470     29       C  
ATOM   1289  SG  CYS A 215     -25.730 -22.780  53.203  1.00 50.83           S  
ANISOU 1289  SG  CYS A 215     8401   5482   5430     77   -462     69       S  
ATOM   1290  N   ILE A 216     -26.293 -26.192  49.676  1.00 48.02           N  
ANISOU 1290  N   ILE A 216     8423   4818   5002    138   -464      0       N  
ATOM   1291  CA  ILE A 216     -25.982 -26.999  48.506  1.00 48.16           C  
ANISOU 1291  CA  ILE A 216     8516   4766   5014    229   -474    -56       C  
ATOM   1292  C   ILE A 216     -27.193 -27.052  47.579  1.00 51.36           C  
ANISOU 1292  C   ILE A 216     8945   5172   5397     50   -400    -37       C  
ATOM   1293  O   ILE A 216     -27.048 -26.838  46.382  1.00 52.17           O  
ANISOU 1293  O   ILE A 216     8955   5330   5537     82   -349    -86       O  
ATOM   1294  CB  ILE A 216     -25.484 -28.416  48.913  1.00 52.93           C  
ANISOU 1294  CB  ILE A 216     9396   5174   5540    360   -599    -67       C  
ATOM   1295  CG1 ILE A 216     -24.125 -28.345  49.644  1.00 54.30           C  
ANISOU 1295  CG1 ILE A 216     9510   5376   5745    586   -687   -108       C  
ATOM   1296  CG2 ILE A 216     -25.426 -29.379  47.706  1.00 53.24           C  
ANISOU 1296  CG2 ILE A 216     9574   5108   5548    430   -611   -124       C  
ATOM   1297  CD1 ILE A 216     -23.775 -29.655  50.545  1.00 60.28           C  
ANISOU 1297  CD1 ILE A 216    10587   5916   6402    709   -846    -91       C  
ATOM   1298  N   GLY A 217     -28.357 -27.361  48.131  1.00 46.38           N  
ANISOU 1298  N   GLY A 217     8435   4489   4697   -142   -398     29       N  
ATOM   1299  CA  GLY A 217     -29.583 -27.509  47.364  1.00 46.26           C  
ANISOU 1299  CA  GLY A 217     8443   4485   4649   -327   -345     46       C  
ATOM   1300  C   GLY A 217     -30.053 -26.222  46.742  1.00 52.13           C  
ANISOU 1300  C   GLY A 217     8931   5410   5464   -383   -253     36       C  
ATOM   1301  O   GLY A 217     -30.475 -26.221  45.586  1.00 53.16           O  
ANISOU 1301  O   GLY A 217     9033   5565   5600   -427   -220     11       O  
ATOM   1302  N   SER A 218     -29.964 -25.112  47.511  1.00 48.70           N  
ANISOU 1302  N   SER A 218     8334   5093   5077   -375   -223     53       N  
ATOM   1303  CA  SER A 218     -30.431 -23.770  47.119  1.00 46.50           C  
ANISOU 1303  CA  SER A 218     7841   4970   4856   -417   -152     47       C  
ATOM   1304  C   SER A 218     -29.374 -22.865  46.466  1.00 49.02           C  
ANISOU 1304  C   SER A 218     8010   5359   5256   -284   -130      2       C  
ATOM   1305  O   SER A 218     -29.786 -21.872  45.863  1.00 50.40           O  
ANISOU 1305  O   SER A 218     8056   5629   5463   -322    -81     -3       O  
ATOM   1306  CB  SER A 218     -31.083 -23.042  48.300  1.00 46.24           C  
ANISOU 1306  CB  SER A 218     7738   5020   4810   -496   -130     84       C  
ATOM   1307  OG  SER A 218     -32.179 -23.751  48.863  1.00 45.14           O  
ANISOU 1307  OG  SER A 218     7707   4861   4585   -656   -128    124       O  
ATOM   1308  N   PHE A 219     -28.049 -23.153  46.583  1.00 42.64           N  
ANISOU 1308  N   PHE A 219     7212   4517   4474   -135   -167    -32       N  
ATOM   1309  CA  PHE A 219     -27.060 -22.286  45.948  1.00 41.35           C  
ANISOU 1309  CA  PHE A 219     6889   4450   4375    -46   -133    -76       C  
ATOM   1310  C   PHE A 219     -25.938 -22.989  45.282  1.00 49.64           C  
ANISOU 1310  C   PHE A 219     7955   5476   5429     97   -149   -140       C  
ATOM   1311  O   PHE A 219     -25.717 -22.695  44.113  1.00 51.60           O  
ANISOU 1311  O   PHE A 219     8132   5783   5691    105    -93   -177       O  
ATOM   1312  CB  PHE A 219     -26.484 -21.239  46.903  1.00 42.77           C  
ANISOU 1312  CB  PHE A 219     6947   4708   4596    -22   -141    -67       C  
ATOM   1313  CG  PHE A 219     -25.411 -20.328  46.315  1.00 44.47           C  
ANISOU 1313  CG  PHE A 219     7001   5029   4865     32   -107   -110       C  
ATOM   1314  CD1 PHE A 219     -25.751 -19.129  45.695  1.00 45.60           C  
ANISOU 1314  CD1 PHE A 219     7051   5246   5028    -52    -50   -101       C  
ATOM   1315  CD2 PHE A 219     -24.057 -20.642  46.437  1.00 47.20           C  
ANISOU 1315  CD2 PHE A 219     7292   5409   5232    161   -140   -161       C  
ATOM   1316  CE1 PHE A 219     -24.763 -18.269  45.211  1.00 45.25           C  
ANISOU 1316  CE1 PHE A 219     6882   5295   5015    -41    -18   -132       C  
ATOM   1317  CE2 PHE A 219     -23.074 -19.787  45.932  1.00 48.53           C  
ANISOU 1317  CE2 PHE A 219     7294   5704   5439    176    -99   -202       C  
ATOM   1318  CZ  PHE A 219     -23.434 -18.609  45.325  1.00 44.74           C  
ANISOU 1318  CZ  PHE A 219     6745   5285   4971     58    -35   -182       C  
ATOM   1319  N   PHE A 220     -25.167 -23.848  46.006  1.00 46.96           N  
ANISOU 1319  N   PHE A 220     7704   5066   5074    225   -226   -159       N  
ATOM   1320  CA  PHE A 220     -23.964 -24.466  45.447  1.00 47.74           C  
ANISOU 1320  CA  PHE A 220     7790   5170   5179    408   -248   -239       C  
ATOM   1321  C   PHE A 220     -24.229 -25.436  44.281  1.00 52.67           C  
ANISOU 1321  C   PHE A 220     8549   5708   5756    436   -236   -279       C  
ATOM   1322  O   PHE A 220     -23.548 -25.295  43.256  1.00 52.87           O  
ANISOU 1322  O   PHE A 220     8472   5819   5796    515   -182   -349       O  
ATOM   1323  CB  PHE A 220     -23.082 -25.082  46.531  1.00 50.98           C  
ANISOU 1323  CB  PHE A 220     8260   5530   5581    566   -354   -257       C  
ATOM   1324  CG  PHE A 220     -22.469 -23.997  47.401  1.00 53.05           C  
ANISOU 1324  CG  PHE A 220     8340   5921   5897    564   -360   -247       C  
ATOM   1325  CD1 PHE A 220     -21.476 -23.147  46.898  1.00 57.95           C  
ANISOU 1325  CD1 PHE A 220     8729   6715   6575    609   -310   -305       C  
ATOM   1326  CD2 PHE A 220     -22.936 -23.767  48.690  1.00 53.75           C  
ANISOU 1326  CD2 PHE A 220     8491   5963   5967    491   -408   -179       C  
ATOM   1327  CE1 PHE A 220     -20.950 -22.099  47.683  1.00 57.69           C  
ANISOU 1327  CE1 PHE A 220     8542   6793   6583    575   -321   -294       C  
ATOM   1328  CE2 PHE A 220     -22.412 -22.722  49.466  1.00 56.43           C  
ANISOU 1328  CE2 PHE A 220     8679   6414   6349    479   -416   -173       C  
ATOM   1329  CZ  PHE A 220     -21.414 -21.905  48.963  1.00 55.02           C  
ANISOU 1329  CZ  PHE A 220     8282   6392   6230    520   -380   -230       C  
ATOM   1330  N   ALA A 221     -25.219 -26.349  44.378  1.00 49.91           N  
ANISOU 1330  N   ALA A 221     8420   5203   5341    352   -276   -239       N  
ATOM   1331  CA  ALA A 221     -25.550 -27.247  43.253  1.00 50.92           C  
ANISOU 1331  CA  ALA A 221     8697   5237   5414    355   -271   -277       C  
ATOM   1332  C   ALA A 221     -26.194 -26.453  42.089  1.00 57.02           C  
ANISOU 1332  C   ALA A 221     9350   6113   6203    225   -174   -275       C  
ATOM   1333  O   ALA A 221     -25.663 -26.564  40.979  1.00 58.30           O  
ANISOU 1333  O   ALA A 221     9482   6311   6358    308   -134   -343       O  
ATOM   1334  CB  ALA A 221     -26.422 -28.406  43.694  1.00 52.24           C  
ANISOU 1334  CB  ALA A 221     9144   5210   5496    266   -347   -231       C  
ATOM   1335  N   PRO A 222     -27.195 -25.531  42.289  1.00 52.65           N  
ANISOU 1335  N   PRO A 222     8704   5629   5670     49   -135   -208       N  
ATOM   1336  CA  PRO A 222     -27.666 -24.720  41.153  1.00 50.97           C  
ANISOU 1336  CA  PRO A 222     8385   5514   5469    -36    -63   -213       C  
ATOM   1337  C   PRO A 222     -26.537 -23.925  40.488  1.00 55.28           C  
ANISOU 1337  C   PRO A 222     8766   6182   6055     62     -1   -265       C  
ATOM   1338  O   PRO A 222     -26.514 -23.863  39.257  1.00 55.61           O  
ANISOU 1338  O   PRO A 222     8802   6255   6071     55     48   -301       O  
ATOM   1339  CB  PRO A 222     -28.735 -23.831  41.776  1.00 50.94           C  
ANISOU 1339  CB  PRO A 222     8302   5569   5484   -183    -53   -144       C  
ATOM   1340  CG  PRO A 222     -29.241 -24.626  42.915  1.00 56.16           C  
ANISOU 1340  CG  PRO A 222     9093   6136   6108   -234   -110   -103       C  
ATOM   1341  CD  PRO A 222     -28.000 -25.226  43.491  1.00 53.16           C  
ANISOU 1341  CD  PRO A 222     8774   5692   5735    -70   -157   -134       C  
ATOM   1342  N   CYS A 223     -25.552 -23.411  41.265  1.00 50.73           N  
ANISOU 1342  N   CYS A 223     8068   5678   5528    146     -4   -275       N  
ATOM   1343  CA  CYS A 223     -24.391 -22.740  40.666  1.00 50.91           C  
ANISOU 1343  CA  CYS A 223     7928   5837   5578    216     58   -331       C  
ATOM   1344  C   CYS A 223     -23.562 -23.712  39.837  1.00 57.52           C  
ANISOU 1344  C   CYS A 223     8808   6669   6379    365     71   -423       C  
ATOM   1345  O   CYS A 223     -23.103 -23.326  38.770  1.00 56.69           O  
ANISOU 1345  O   CYS A 223     8617   6666   6258    366    150   -469       O  
ATOM   1346  CB  CYS A 223     -23.529 -22.043  41.708  1.00 51.22           C  
ANISOU 1346  CB  CYS A 223     7826   5964   5672    257     41   -327       C  
ATOM   1347  SG  CYS A 223     -24.247 -20.516  42.347  1.00 54.02           S  
ANISOU 1347  SG  CYS A 223     8098   6366   6062     94     55   -245       S  
ATOM   1348  N   LEU A 224     -23.372 -24.970  40.311  1.00 56.81           N  
ANISOU 1348  N   LEU A 224     8867   6456   6263    495     -9   -452       N  
ATOM   1349  CA  LEU A 224     -22.596 -25.970  39.572  1.00 58.91           C  
ANISOU 1349  CA  LEU A 224     9198   6700   6485    676    -12   -554       C  
ATOM   1350  C   LEU A 224     -23.258 -26.309  38.258  1.00 65.93           C  
ANISOU 1350  C   LEU A 224    10200   7539   7312    608     35   -573       C  
ATOM   1351  O   LEU A 224     -22.571 -26.329  37.235  1.00 68.29           O  
ANISOU 1351  O   LEU A 224    10434   7930   7583    690    105   -655       O  
ATOM   1352  CB  LEU A 224     -22.369 -27.226  40.387  1.00 60.38           C  
ANISOU 1352  CB  LEU A 224     9571   6728   6642    831   -130   -575       C  
ATOM   1353  CG  LEU A 224     -21.413 -28.231  39.769  1.00 67.60           C  
ANISOU 1353  CG  LEU A 224    10548   7623   7512   1074   -151   -697       C  
ATOM   1354  CD1 LEU A 224     -19.967 -27.903  40.126  1.00 69.13           C  
ANISOU 1354  CD1 LEU A 224    10513   7999   7753   1265   -147   -778       C  
ATOM   1355  CD2 LEU A 224     -21.785 -29.651  40.178  1.00 70.52           C  
ANISOU 1355  CD2 LEU A 224    11240   7742   7814   1161   -277   -698       C  
ATOM   1356  N   ILE A 225     -24.598 -26.509  38.270  1.00 61.10           N  
ANISOU 1356  N   ILE A 225     9738   6806   6673    444      3   -499       N  
ATOM   1357  CA  ILE A 225     -25.400 -26.786  37.065  1.00 59.99           C  
ANISOU 1357  CA  ILE A 225     9708   6616   6470    349     30   -506       C  
ATOM   1358  C   ILE A 225     -25.317 -25.634  36.039  1.00 62.75           C  
ANISOU 1358  C   ILE A 225     9894   7124   6826    272    133   -511       C  
ATOM   1359  O   ILE A 225     -24.966 -25.880  34.893  1.00 64.38           O  
ANISOU 1359  O   ILE A 225    10127   7358   6978    321    185   -579       O  
ATOM   1360  CB  ILE A 225     -26.850 -27.158  37.451  1.00 61.51           C  
ANISOU 1360  CB  ILE A 225    10054   6682   6636    171    -33   -426       C  
ATOM   1361  CG1 ILE A 225     -26.856 -28.514  38.186  1.00 62.32           C  
ANISOU 1361  CG1 ILE A 225    10390   6597   6693    236   -133   -432       C  
ATOM   1362  CG2 ILE A 225     -27.779 -27.162  36.229  1.00 60.29           C  
ANISOU 1362  CG2 ILE A 225     9964   6518   6426     40    -10   -424       C  
ATOM   1363  CD1 ILE A 225     -28.020 -28.764  39.076  1.00 68.64           C  
ANISOU 1363  CD1 ILE A 225    11298   7308   7474     55   -191   -342       C  
ATOM   1364  N   MET A 226     -25.585 -24.391  36.465  1.00 57.59           N  
ANISOU 1364  N   MET A 226     9090   6564   6227    161    159   -443       N  
ATOM   1365  CA  MET A 226     -25.550 -23.191  35.618  1.00 56.66           C  
ANISOU 1365  CA  MET A 226     8850   6572   6106     72    239   -430       C  
ATOM   1366  C   MET A 226     -24.189 -22.986  34.961  1.00 62.89           C  
ANISOU 1366  C   MET A 226     9524   7493   6879    169    325   -511       C  
ATOM   1367  O   MET A 226     -24.143 -22.560  33.812  1.00 64.72           O  
ANISOU 1367  O   MET A 226     9744   7789   7056    112    396   -528       O  
ATOM   1368  CB  MET A 226     -25.842 -21.934  36.448  1.00 57.51           C  
ANISOU 1368  CB  MET A 226     8837   6740   6276    -24    233   -354       C  
ATOM   1369  CG  MET A 226     -27.283 -21.690  36.775  1.00 60.31           C  
ANISOU 1369  CG  MET A 226     9249   7034   6634   -146    181   -281       C  
ATOM   1370  SD  MET A 226     -27.357 -20.676  38.285  1.00 64.36           S  
ANISOU 1370  SD  MET A 226     9646   7587   7220   -177    154   -219       S  
ATOM   1371  CE  MET A 226     -26.502 -19.261  37.790  1.00 60.69           C  
ANISOU 1371  CE  MET A 226     9051   7241   6768   -200    220   -223       C  
ATOM   1372  N   GLY A 227     -23.107 -23.210  35.717  1.00 58.60           N  
ANISOU 1372  N   GLY A 227     8884   7005   6376    302    318   -557       N  
ATOM   1373  CA  GLY A 227     -21.740 -23.018  35.254  1.00 58.49           C  
ANISOU 1373  CA  GLY A 227     8713   7160   6350    398    401   -645       C  
ATOM   1374  C   GLY A 227     -21.433 -23.990  34.149  1.00 63.92           C  
ANISOU 1374  C   GLY A 227     9490   7837   6957    514    440   -743       C  
ATOM   1375  O   GLY A 227     -21.056 -23.587  33.043  1.00 63.32           O  
ANISOU 1375  O   GLY A 227     9355   7881   6823    473    543   -785       O  
ATOM   1376  N   LEU A 228     -21.692 -25.274  34.429  1.00 61.64           N  
ANISOU 1376  N   LEU A 228     9380   7389   6652    642    353   -775       N  
ATOM   1377  CA  LEU A 228     -21.482 -26.357  33.485  1.00 63.08           C  
ANISOU 1377  CA  LEU A 228     9701   7516   6750    776    366   -875       C  
ATOM   1378  C   LEU A 228     -22.277 -26.170  32.186  1.00 68.80           C  
ANISOU 1378  C   LEU A 228    10526   8217   7397    633    421   -860       C  
ATOM   1379  O   LEU A 228     -21.686 -26.283  31.105  1.00 70.55           O  
ANISOU 1379  O   LEU A 228    10726   8535   7546    694    511   -949       O  
ATOM   1380  CB  LEU A 228     -21.747 -27.721  34.140  1.00 63.41           C  
ANISOU 1380  CB  LEU A 228     9968   7346   6779    912    237   -893       C  
ATOM   1381  CG  LEU A 228     -20.821 -28.114  35.304  1.00 67.64           C  
ANISOU 1381  CG  LEU A 228    10442   7892   7366   1109    165   -931       C  
ATOM   1382  CD1 LEU A 228     -21.353 -29.330  36.041  1.00 67.15           C  
ANISOU 1382  CD1 LEU A 228    10659   7576   7279   1179     22   -910       C  
ATOM   1383  CD2 LEU A 228     -19.388 -28.313  34.845  1.00 71.41           C  
ANISOU 1383  CD2 LEU A 228    10761   8547   7824   1341    225  -1076       C  
ATOM   1384  N   VAL A 229     -23.589 -25.831  32.285  1.00 63.99           N  
ANISOU 1384  N   VAL A 229    10011   7504   6799    443    371   -752       N  
ATOM   1385  CA  VAL A 229     -24.441 -25.580  31.110  1.00 63.86           C  
ANISOU 1385  CA  VAL A 229    10086   7468   6710    301    400   -729       C  
ATOM   1386  C   VAL A 229     -23.907 -24.374  30.310  1.00 69.35           C  
ANISOU 1386  C   VAL A 229    10624   8345   7380    225    517   -730       C  
ATOM   1387  O   VAL A 229     -23.732 -24.492  29.097  1.00 70.94           O  
ANISOU 1387  O   VAL A 229    10878   8589   7488    225    585   -786       O  
ATOM   1388  CB  VAL A 229     -25.950 -25.448  31.443  1.00 66.17           C  
ANISOU 1388  CB  VAL A 229    10477   7643   7020    129    312   -625       C  
ATOM   1389  CG1 VAL A 229     -26.751 -25.057  30.205  1.00 65.83           C  
ANISOU 1389  CG1 VAL A 229    10500   7610   6904     -4    331   -606       C  
ATOM   1390  CG2 VAL A 229     -26.498 -26.738  32.034  1.00 66.21           C  
ANISOU 1390  CG2 VAL A 229    10675   7468   7016    162    207   -628       C  
ATOM   1391  N   TYR A 230     -23.584 -23.251  30.985  1.00 64.82           N  
ANISOU 1391  N   TYR A 230     9875   7876   6876    158    542   -672       N  
ATOM   1392  CA  TYR A 230     -23.048 -22.082  30.292  1.00 65.16           C  
ANISOU 1392  CA  TYR A 230     9796   8077   6883     58    647   -665       C  
ATOM   1393  C   TYR A 230     -21.633 -22.274  29.766  1.00 70.50           C  
ANISOU 1393  C   TYR A 230    10349   8925   7512    164    762   -778       C  
ATOM   1394  O   TYR A 230     -21.222 -21.548  28.856  1.00 71.37           O  
ANISOU 1394  O   TYR A 230    10405   9165   7549     66    868   -788       O  
ATOM   1395  CB  TYR A 230     -23.160 -20.808  31.117  1.00 65.26           C  
ANISOU 1395  CB  TYR A 230     9694   8133   6970    -61    631   -572       C  
ATOM   1396  CG  TYR A 230     -24.348 -19.997  30.670  1.00 66.62           C  
ANISOU 1396  CG  TYR A 230     9962   8236   7115   -218    594   -481       C  
ATOM   1397  CD1 TYR A 230     -24.292 -19.218  29.517  1.00 68.93           C  
ANISOU 1397  CD1 TYR A 230    10284   8591   7316   -328    661   -468       C  
ATOM   1398  CD2 TYR A 230     -25.552 -20.053  31.361  1.00 66.94           C  
ANISOU 1398  CD2 TYR A 230    10070   8156   7206   -251    487   -412       C  
ATOM   1399  CE1 TYR A 230     -25.402 -18.501  29.073  1.00 69.86           C  
ANISOU 1399  CE1 TYR A 230    10507   8636   7400   -444    605   -389       C  
ATOM   1400  CE2 TYR A 230     -26.669 -19.344  30.925  1.00 67.71           C  
ANISOU 1400  CE2 TYR A 230    10241   8211   7277   -365    441   -344       C  
ATOM   1401  CZ  TYR A 230     -26.587 -18.559  29.788  1.00 78.05           C  
ANISOU 1401  CZ  TYR A 230    11587   9567   8500   -450    491   -332       C  
ATOM   1402  OH  TYR A 230     -27.693 -17.858  29.373  1.00 82.99           O  
ANISOU 1402  OH  TYR A 230    12295  10144   9094   -536    424   -268       O  
ATOM   1403  N   ALA A 231     -20.911 -23.269  30.293  1.00 66.62           N  
ANISOU 1403  N   ALA A 231     9823   8440   7049    366    740   -867       N  
ATOM   1404  CA  ALA A 231     -19.587 -23.606  29.804  1.00 68.07           C  
ANISOU 1404  CA  ALA A 231     9875   8805   7184    510    841   -999       C  
ATOM   1405  C   ALA A 231     -19.767 -24.323  28.464  1.00 72.22           C  
ANISOU 1405  C   ALA A 231    10557   9297   7587    556    894  -1076       C  
ATOM   1406  O   ALA A 231     -19.029 -24.046  27.522  1.00 73.19           O  
ANISOU 1406  O   ALA A 231    10588   9598   7622    546   1026  -1149       O  
ATOM   1407  CB  ALA A 231     -18.880 -24.510  30.795  1.00 69.80           C  
ANISOU 1407  CB  ALA A 231    10040   9015   7466    745    770  -1074       C  
ATOM   1408  N   ARG A 232     -20.793 -25.203  28.374  1.00 67.85           N  
ANISOU 1408  N   ARG A 232    10246   8518   7016    581    791  -1055       N  
ATOM   1409  CA  ARG A 232     -21.164 -25.965  27.172  1.00 68.36           C  
ANISOU 1409  CA  ARG A 232    10509   8504   6961    611    809  -1120       C  
ATOM   1410  C   ARG A 232     -21.744 -25.032  26.090  1.00 71.38           C  
ANISOU 1410  C   ARG A 232    10927   8932   7264    393    876  -1056       C  
ATOM   1411  O   ARG A 232     -21.600 -25.313  24.892  1.00 73.61           O  
ANISOU 1411  O   ARG A 232    11295   9251   7423    406    950  -1128       O  
ATOM   1412  CB  ARG A 232     -22.176 -27.070  27.523  1.00 66.09           C  
ANISOU 1412  CB  ARG A 232    10475   7955   6680    649    663  -1098       C  
ATOM   1413  CG  ARG A 232     -21.575 -28.447  27.696  1.00 77.38           C  
ANISOU 1413  CG  ARG A 232    12019   9299   8082    908    616  -1222       C  
ATOM   1414  CD  ARG A 232     -22.551 -29.371  28.404  1.00 89.94           C  
ANISOU 1414  CD  ARG A 232    13851  10625   9696    898    457  -1168       C  
ATOM   1415  NE  ARG A 232     -22.316 -30.779  28.080  1.00104.89           N  
ANISOU 1415  NE  ARG A 232    15979  12368  11507   1099    400  -1284       N  
ATOM   1416  CZ  ARG A 232     -21.471 -31.571  28.734  1.00123.08           C  
ANISOU 1416  CZ  ARG A 232    18304  14633  13826   1351    349  -1370       C  
ATOM   1417  NH1 ARG A 232     -20.759 -31.099  29.753  1.00111.39           N1+
ANISOU 1417  NH1 ARG A 232    16606  13271  12445   1426    349  -1353       N1+
ATOM   1418  NH2 ARG A 232     -21.327 -32.841  28.371  1.00108.79           N  
ANISOU 1418  NH2 ARG A 232    16749  12660  11925   1540    285  -1478       N  
ATOM   1419  N   ILE A 233     -22.407 -23.938  26.520  1.00 63.59           N  
ANISOU 1419  N   ILE A 233     9889   7933   6338    206    841   -925       N  
ATOM   1420  CA  ILE A 233     -22.972 -22.933  25.632  1.00 62.46           C  
ANISOU 1420  CA  ILE A 233     9789   7818   6124     10    877   -851       C  
ATOM   1421  C   ILE A 233     -21.841 -22.138  24.968  1.00 67.96           C  
ANISOU 1421  C   ILE A 233    10340   8734   6747    -42   1035   -893       C  
ATOM   1422  O   ILE A 233     -21.906 -21.928  23.762  1.00 69.41           O  
ANISOU 1422  O   ILE A 233    10614   8958   6802   -123   1106   -908       O  
ATOM   1423  CB  ILE A 233     -23.995 -22.015  26.364  1.00 63.57           C  
ANISOU 1423  CB  ILE A 233     9927   7878   6351   -138    778   -711       C  
ATOM   1424  CG1 ILE A 233     -25.276 -22.791  26.731  1.00 62.44           C  
ANISOU 1424  CG1 ILE A 233     9936   7546   6241   -134    639   -674       C  
ATOM   1425  CG2 ILE A 233     -24.324 -20.751  25.538  1.00 64.16           C  
ANISOU 1425  CG2 ILE A 233    10026   8001   6351   -319    815   -638       C  
ATOM   1426  CD1 ILE A 233     -26.245 -22.062  27.645  1.00 66.47           C  
ANISOU 1426  CD1 ILE A 233    10411   8000   6843   -237    544   -561       C  
ATOM   1427  N  ATYR A 234     -20.815 -21.703  25.728  0.50 65.55           N  
ANISOU 1427  N  ATYR A 234     9818   8579   6510    -11   1091   -912       N  
ATOM   1428  N  BTYR A 234     -20.821 -21.727  25.759  0.50 63.88           N  
ANISOU 1428  N  BTYR A 234     9606   8364   6301     -7   1088   -912       N  
ATOM   1429  CA ATYR A 234     -19.741 -20.892  25.160  0.50 67.40           C  
ANISOU 1429  CA ATYR A 234     9896   9045   6669   -102   1246   -947       C  
ATOM   1430  CA BTYR A 234     -19.641 -20.967  25.331  0.50 64.95           C  
ANISOU 1430  CA BTYR A 234     9561   8741   6376    -78   1241   -955       C  
ATOM   1431  C  ATYR A 234     -18.736 -21.682  24.280  0.50 75.79           C  
ANISOU 1431  C  ATYR A 234    10903  10271   7622     37   1378  -1107       C  
ATOM   1432  C  BTYR A 234     -18.800 -21.693  24.268  0.50 74.61           C  
ANISOU 1432  C  BTYR A 234    10766  10110   7472     35   1373  -1103       C  
ATOM   1433  O  ATYR A 234     -18.042 -21.052  23.479  0.50 77.26           O  
ANISOU 1433  O  ATYR A 234    11005  10651   7700    -78   1524  -1136       O  
ATOM   1434  O  BTYR A 234     -18.233 -21.038  23.393  0.50 75.98           O  
ANISOU 1434  O  BTYR A 234    10881  10456   7531    -94   1512  -1122       O  
ATOM   1435  CB ATYR A 234     -19.049 -20.039  26.230  0.50 68.18           C  
ANISOU 1435  CB ATYR A 234     9778   9261   6868   -159   1254   -909       C  
ATOM   1436  CB BTYR A 234     -18.754 -20.628  26.549  0.50 64.71           C  
ANISOU 1436  CB BTYR A 234     9294   8833   6461    -34   1241   -964       C  
ATOM   1437  CG ATYR A 234     -19.923 -18.877  26.672  0.50 68.67           C  
ANISOU 1437  CG ATYR A 234     9907   9207   6976   -350   1172   -757       C  
ATOM   1438  CG BTYR A 234     -17.726 -19.542  26.303  0.50 66.02           C  
ANISOU 1438  CG BTYR A 234     9267   9240   6577   -191   1376   -969       C  
ATOM   1439  CD1ATYR A 234     -20.587 -18.080  25.739  0.50 70.32           C  
ANISOU 1439  CD1ATYR A 234    10268   9364   7086   -530   1184   -679       C  
ATOM   1440  CD1BTYR A 234     -18.028 -18.203  26.541  0.50 66.76           C  
ANISOU 1440  CD1BTYR A 234     9369   9314   6684   -423   1361   -844       C  
ATOM   1441  CD2ATYR A 234     -20.100 -18.584  28.021  0.50 68.15           C  
ANISOU 1441  CD2ATYR A 234     9769   9081   7045   -335   1074   -697       C  
ATOM   1442  CD2BTYR A 234     -16.439 -19.853  25.875  0.50 68.70           C  
ANISOU 1442  CD2BTYR A 234     9417   9835   6853   -111   1516  -1105       C  
ATOM   1443  CE1ATYR A 234     -21.422 -17.039  26.138  0.50 68.53           C  
ANISOU 1443  CE1ATYR A 234    10120   9022   6898   -666   1093   -553       C  
ATOM   1444  CE1BTYR A 234     -17.087 -17.198  26.322  0.50 68.47           C  
ANISOU 1444  CE1BTYR A 234     9436   9739   6840   -603   1480   -842       C  
ATOM   1445  CE2ATYR A 234     -20.920 -17.532  28.432  0.50 67.40           C  
ANISOU 1445  CE2ATYR A 234     9743   8880   6986   -482    997   -573       C  
ATOM   1446  CE2BTYR A 234     -15.493 -18.856  25.637  0.50 70.90           C  
ANISOU 1446  CE2BTYR A 234     9508  10359   7073   -293   1649  -1111       C  
ATOM   1447  CZ ATYR A 234     -21.575 -16.761  27.485  0.50 74.71           C  
ANISOU 1447  CZ ATYR A 234    10819   9753   7816   -638   1004   -505       C  
ATOM   1448  CZ BTYR A 234     -15.819 -17.529  25.870  0.50 77.19           C  
ANISOU 1448  CZ BTYR A 234    10340  11112   7877   -554   1629   -974       C  
ATOM   1449  OH ATYR A 234     -22.368 -15.710  27.872  0.50 78.67           O  
ANISOU 1449  OH ATYR A 234    11398  10150   8345   -752    918   -394       O  
ATOM   1450  OH BTYR A 234     -14.891 -16.538  25.652  0.50 79.36           O  
ANISOU 1450  OH BTYR A 234    10457  11614   8082   -767   1753   -973       O  
ATOM   1451  N   ARG A 235     -18.711 -23.031  24.349  1.00 73.85           N  
ANISOU 1451  N   ARG A 235    10732   9943   7384    273   1329  -1209       N  
ATOM   1452  CA  ARG A 235     -17.877 -23.837  23.428  1.00 77.90           C  
ANISOU 1452  CA  ARG A 235    11229  10591   7777    435   1446  -1374       C  
ATOM   1453  C   ARG A 235     -18.572 -23.858  22.068  1.00 85.35           C  
ANISOU 1453  C   ARG A 235    12397  11461   8570    324   1484  -1363       C  
ATOM   1454  O   ARG A 235     -17.943 -23.569  21.047  1.00 87.23           O  
ANISOU 1454  O   ARG A 235    12588  11884   8670    267   1639  -1429       O  
ATOM   1455  CB  ARG A 235     -17.661 -25.288  23.921  1.00 81.06           C  
ANISOU 1455  CB  ARG A 235    11688  10891   8219    742   1360  -1491       C  
ATOM   1456  CG  ARG A 235     -17.053 -25.424  25.318  1.00 99.50           C  
ANISOU 1456  CG  ARG A 235    13843  13264  10697    884   1289  -1502       C  
ATOM   1457  CD  ARG A 235     -15.534 -25.447  25.352  1.00117.67           C  
ANISOU 1457  CD  ARG A 235    15857  15870  12983   1040   1408  -1647       C  
ATOM   1458  NE  ARG A 235     -15.048 -25.464  26.734  1.00130.24           N  
ANISOU 1458  NE  ARG A 235    17284  17489  14714   1152   1316  -1640       N  
ATOM   1459  CZ  ARG A 235     -13.974 -26.127  27.147  1.00147.39           C  
ANISOU 1459  CZ  ARG A 235    19289  19806  16905   1424   1314  -1784       C  
ATOM   1460  NH1 ARG A 235     -13.252 -26.837  26.288  1.00134.26           N  
ANISOU 1460  NH1 ARG A 235    17592  18287  15135   1628   1410  -1957       N  
ATOM   1461  NH2 ARG A 235     -13.614 -26.088  28.423  1.00137.06           N1+
ANISOU 1461  NH2 ARG A 235    17851  18507  15719   1509   1212  -1762       N1+
ATOM   1462  N   VAL A 236     -19.894 -24.134  22.085  1.00 81.82           N  
ANISOU 1462  N   VAL A 236    12185  10757   8146    270   1339  -1275       N  
ATOM   1463  CA  VAL A 236     -20.777 -24.176  20.921  1.00 82.14           C  
ANISOU 1463  CA  VAL A 236    12460  10691   8058    159   1326  -1247       C  
ATOM   1464  C   VAL A 236     -20.828 -22.804  20.231  1.00 88.36           C  
ANISOU 1464  C   VAL A 236    13223  11586   8763    -90   1410  -1155       C  
ATOM   1465  O   VAL A 236     -20.643 -22.751  19.021  1.00 89.36           O  
ANISOU 1465  O   VAL A 236    13437  11789   8727   -146   1511  -1202       O  
ATOM   1466  CB  VAL A 236     -22.177 -24.743  21.285  1.00 84.21           C  
ANISOU 1466  CB  VAL A 236    12934  10681   8382    145   1138  -1171       C  
ATOM   1467  CG1 VAL A 236     -23.154 -24.623  20.123  1.00 83.95           C  
ANISOU 1467  CG1 VAL A 236    13120  10555   8223      4   1105  -1130       C  
ATOM   1468  CG2 VAL A 236     -22.074 -26.196  21.742  1.00 84.69           C  
ANISOU 1468  CG2 VAL A 236    13085  10616   8475    373   1063  -1272       C  
ATOM   1469  N   ALA A 237     -21.014 -21.705  21.004  1.00 85.79           N  
ANISOU 1469  N   ALA A 237    12794  11265   8536   -233   1370  -1031       N  
ATOM   1470  CA  ALA A 237     -21.057 -20.320  20.510  1.00 86.53           C  
ANISOU 1470  CA  ALA A 237    12892  11429   8555   -471   1425   -930       C  
ATOM   1471  C   ALA A 237     -19.749 -19.917  19.821  1.00 96.78           C  
ANISOU 1471  C   ALA A 237    14054  12989   9729   -535   1629  -1008       C  
ATOM   1472  O   ALA A 237     -19.773 -19.079  18.911  1.00 97.85           O  
ANISOU 1472  O   ALA A 237    14279  13175   9724   -731   1700   -956       O  
ATOM   1473  CB  ALA A 237     -21.364 -19.360  21.653  1.00 85.18           C  
ANISOU 1473  CB  ALA A 237    12631  11208   8524   -565   1336   -808       C  
ATOM   1474  N   LYS A 238     -18.616 -20.528  20.244  1.00 96.80           N  
ANISOU 1474  N   LYS A 238    13842  13166   9771   -370   1719  -1136       N  
ATOM   1475  CA  LYS A 238     -17.281 -20.288  19.686  1.00 99.89           C  
ANISOU 1475  CA  LYS A 238    14045  13858  10051   -406   1924  -1239       C  
ATOM   1476  C   LYS A 238     -17.083 -21.050  18.371  1.00106.93           C  
ANISOU 1476  C   LYS A 238    15050  14816  10762   -326   2035  -1364       C  
ATOM   1477  O   LYS A 238     -16.542 -20.489  17.423  1.00107.98           O  
ANISOU 1477  O   LYS A 238    15166  15133  10730   -484   2196  -1385       O  
ATOM   1478  CB  LYS A 238     -16.187 -20.655  20.702  1.00103.10           C  
ANISOU 1478  CB  LYS A 238    14157  14440  10575   -234   1957  -1339       C  
ATOM   1479  N   LEU A 239     -17.541 -22.309  18.309  1.00104.67           N  
ANISOU 1479  N   LEU A 239    14904  14373  10494    -97   1947  -1443       N  
ATOM   1480  CA  LEU A 239     -17.430 -23.149  17.118  1.00107.26           C  
ANISOU 1480  CA  LEU A 239    15373  14727  10651      8   2029  -1572       C  
ATOM   1481  C   LEU A 239     -18.475 -22.803  16.043  1.00114.18           C  
ANISOU 1481  C   LEU A 239    16540  15450  11391   -178   1990  -1481       C  
ATOM   1482  O   LEU A 239     -18.166 -22.887  14.852  1.00116.36           O  
ANISOU 1482  O   LEU A 239    16901  15837  11475   -216   2120  -1555       O  
ATOM   1483  CB  LEU A 239     -17.511 -24.639  17.494  1.00107.39           C  
ANISOU 1483  CB  LEU A 239    15464  14609  10731    323   1932  -1694       C  
ATOM   1484  CG  LEU A 239     -16.189 -25.351  17.822  1.00114.11           C  
ANISOU 1484  CG  LEU A 239    16083  15677  11596    593   2030  -1879       C  
ATOM   1485  CD1 LEU A 239     -15.805 -25.193  19.301  1.00113.06           C  
ANISOU 1485  CD1 LEU A 239    15726  15568  11663    670   1949  -1843       C  
ATOM   1486  CD2 LEU A 239     -16.270 -26.829  17.470  1.00117.35           C  
ANISOU 1486  CD2 LEU A 239    16682  15956  11951    884   1978  -2030       C  
ATOM   1487  N   ARG A 240     -19.706 -22.429  16.456  1.00110.25           N  
ANISOU 1487  N   ARG A 240    16191  14713  10985   -286   1809  -1327       N  
ATOM   1488  CA  ARG A 240     -20.805 -22.088  15.543  1.00110.46           C  
ANISOU 1488  CA  ARG A 240    16484  14585  10899   -445   1732  -1235       C  
ATOM   1489  C   ARG A 240     -20.938 -20.582  15.325  1.00115.41           C  
ANISOU 1489  C   ARG A 240    17118  15257  11476   -713   1756  -1091       C  
ATOM   1490  O   ARG A 240     -22.030 -20.033  15.469  1.00111.92           O  
ANISOU 1490  O   ARG A 240    16810  14638  11077   -816   1602   -959       O  
ATOM   1491  CB  ARG A 240     -22.157 -22.687  15.997  1.00109.53           C  
ANISOU 1491  CB  ARG A 240    16537  14192  10889   -388   1510  -1173       C  
ATOM   1492  CG  ARG A 240     -22.227 -24.205  16.217  1.00123.81           C  
ANISOU 1492  CG  ARG A 240    18418  15891  12734   -154   1448  -1295       C  
ATOM   1493  CD  ARG A 240     -21.437 -25.099  15.254  1.00133.96           C  
ANISOU 1493  CD  ARG A 240    19763  17276  13858     -4   1580  -1471       C  
ATOM   1494  NE  ARG A 240     -20.392 -25.853  15.956  1.00144.64           N  
ANISOU 1494  NE  ARG A 240    20940  18728  15288    239   1641  -1604       N  
ATOM   1495  CZ  ARG A 240     -20.618 -26.817  16.850  1.00159.37           C  
ANISOU 1495  CZ  ARG A 240    22841  20433  17277    421   1510  -1637       C  
ATOM   1496  NH1 ARG A 240     -21.861 -27.157  17.175  1.00144.56           N  
ANISOU 1496  NH1 ARG A 240    21156  18305  15466    364   1326  -1546       N  
ATOM   1497  NH2 ARG A 240     -19.603 -27.431  17.441  1.00146.81           N1+
ANISOU 1497  NH2 ARG A 240    21097  18944  15742    656   1559  -1760       N1+
ATOM   1498  N   THR A 241     -19.832 -19.932  14.934  1.00117.01           N  
ANISOU 1498  N   THR A 241    17187  15699  11573   -826   1947  -1123       N  
ATOM   1499  CA  THR A 241     -19.759 -18.492  14.667  1.00118.58           C  
ANISOU 1499  CA  THR A 241    17413  15950  11690  -1102   1992   -995       C  
ATOM   1500  C   THR A 241     -20.719 -18.059  13.561  1.00125.63           C  
ANISOU 1500  C   THR A 241    18617  16697  12420  -1250   1921   -906       C  
ATOM   1501  O   THR A 241     -20.949 -18.806  12.605  1.00125.65           O  
ANISOU 1501  O   THR A 241    18776  16674  12290  -1184   1940   -982       O  
ATOM   1502  CB  THR A 241     -18.316 -18.029  14.410  1.00129.39           C  
ANISOU 1502  CB  THR A 241    18575  17632  12956  -1211   2227  -1066       C  
ATOM   1503  OG1 THR A 241     -17.490 -19.137  14.025  1.00129.10           O  
ANISOU 1503  OG1 THR A 241    18418  17773  12859  -1013   2366  -1256       O  
ATOM   1504  CG2 THR A 241     -17.721 -17.287  15.606  1.00127.10           C  
ANISOU 1504  CG2 THR A 241    18040  17433  12818  -1279   2231  -1014       C  
ATOM   1505  N   GLY A1001     -21.299 -16.877  13.751  1.00107.38           N  
ANISOU 1505  N   GLY A1001    19863  11888   9048  -1742  -1044    -64       N  
ATOM   1506  CA  GLY A1001     -22.280 -16.311  12.839  1.00107.19           C  
ANISOU 1506  CA  GLY A1001    20013  11720   8993  -1540   -855   -155       C  
ATOM   1507  C   GLY A1001     -21.709 -15.694  11.582  1.00113.15           C  
ANISOU 1507  C   GLY A1001    20804  12293   9894  -1696   -819   -141       C  
ATOM   1508  O   GLY A1001     -20.677 -15.013  11.622  1.00115.39           O  
ANISOU 1508  O   GLY A1001    21199  12454  10191  -2022   -948   -150       O  
ATOM   1509  N   ILE A1002     -22.430 -15.905  10.464  1.00108.25           N  
ANISOU 1509  N   ILE A1002    20108  11673   9349  -1486   -634   -130       N  
ATOM   1510  CA  ILE A1002     -22.160 -15.423   9.107  1.00108.36           C  
ANISOU 1510  CA  ILE A1002    20196  11525   9450  -1555   -545   -101       C  
ATOM   1511  C   ILE A1002     -21.786 -13.930   9.033  1.00117.43           C  
ANISOU 1511  C   ILE A1002    21870  12320  10428  -1722   -618   -168       C  
ATOM   1512  O   ILE A1002     -22.232 -13.136   9.864  1.00118.89           O  
ANISOU 1512  O   ILE A1002    22449  12347  10377  -1615   -703   -286       O  
ATOM   1513  CB  ILE A1002     -23.405 -15.753   8.222  1.00109.34           C  
ANISOU 1513  CB  ILE A1002    20258  11740   9546  -1191   -384   -132       C  
ATOM   1514  CG1 ILE A1002     -23.060 -15.806   6.711  1.00108.56           C  
ANISOU 1514  CG1 ILE A1002    20092  11583   9574  -1262   -270    -58       C  
ATOM   1515  CG2 ILE A1002     -24.584 -14.813   8.516  1.00111.37           C  
ANISOU 1515  CG2 ILE A1002    20900  11899   9519   -834   -398   -275       C  
ATOM   1516  CD1 ILE A1002     -24.250 -16.036   5.791  1.00110.19           C  
ANISOU 1516  CD1 ILE A1002    20255  11905   9706   -918   -164   -108       C  
ATOM   1517  N   ASP A1003     -20.976 -13.559   8.022  1.00116.71           N  
ANISOU 1517  N   ASP A1003    21824  12084  10437  -1997   -554   -100       N  
ATOM   1518  CA  ASP A1003     -20.606 -12.170   7.741  1.00120.32           C  
ANISOU 1518  CA  ASP A1003    22849  12140  10725  -2223   -567   -142       C  
ATOM   1519  C   ASP A1003     -21.732 -11.658   6.829  1.00125.66           C  
ANISOU 1519  C   ASP A1003    23903  12614  11226  -1792   -457   -147       C  
ATOM   1520  O   ASP A1003     -21.666 -11.817   5.609  1.00124.40           O  
ANISOU 1520  O   ASP A1003    23687  12449  11131  -1788   -326    -53       O  
ATOM   1521  CB  ASP A1003     -19.228 -12.100   7.045  1.00123.38           C  
ANISOU 1521  CB  ASP A1003    23069  12521  11287  -2753   -505    -58       C  
ATOM   1522  CG  ASP A1003     -18.407 -10.863   7.361  1.00134.91           C  
ANISOU 1522  CG  ASP A1003    24987  13663  12610  -3244   -575   -130       C  
ATOM   1523  OD1 ASP A1003     -18.946  -9.738   7.227  1.00136.98           O  
ANISOU 1523  OD1 ASP A1003    25951  13484  12613  -3151   -553   -185       O  
ATOM   1524  OD2 ASP A1003     -17.220 -11.018   7.721  1.00141.72           O1-
ANISOU 1524  OD2 ASP A1003    25515  14720  13614  -3721   -652   -140       O1-
ATOM   1525  N   CYS A1004     -22.817 -11.156   7.444  1.00124.91           N  
ANISOU 1525  N   CYS A1004    24137  12424  10899  -1375   -515   -266       N  
ATOM   1526  CA  CYS A1004     -24.030 -10.680   6.771  1.00126.26           C  
ANISOU 1526  CA  CYS A1004    24615  12489  10868   -836   -462   -301       C  
ATOM   1527  C   CYS A1004     -23.749  -9.667   5.664  1.00132.02           C  
ANISOU 1527  C   CYS A1004    25916  12786  11459   -896   -405   -219       C  
ATOM   1528  O   CYS A1004     -24.261  -9.831   4.553  1.00131.33           O  
ANISOU 1528  O   CYS A1004    25798  12763  11339   -623   -335   -147       O  
ATOM   1529  CB  CYS A1004     -25.039 -10.147   7.786  1.00128.98           C  
ANISOU 1529  CB  CYS A1004    25243  12794  10970   -408   -531   -471       C  
ATOM   1530  SG  CYS A1004     -25.610 -11.385   8.987  1.00130.52           S  
ANISOU 1530  SG  CYS A1004    24811  13522  11259   -293   -535   -552       S  
ATOM   1531  N   SER A1005     -22.897  -8.660   5.956  1.00130.57           N  
ANISOU 1531  N   SER A1005    26264  12170  11176  -1304   -433   -229       N  
ATOM   1532  CA  SER A1005     -22.487  -7.598   5.030  1.00133.15           C  
ANISOU 1532  CA  SER A1005    27264  11993  11335  -1490   -349   -141       C  
ATOM   1533  C   SER A1005     -21.679  -8.109   3.827  1.00132.98           C  
ANISOU 1533  C   SER A1005    26937  12096  11493  -1865   -194     26       C  
ATOM   1534  O   SER A1005     -21.948  -7.691   2.699  1.00134.19           O  
ANISOU 1534  O   SER A1005    27472  12027  11487  -1700    -96    134       O  
ATOM   1535  CB  SER A1005     -21.720  -6.504   5.773  1.00141.76           C  
ANISOU 1535  CB  SER A1005    28961  12617  12286  -1959   -400   -227       C  
ATOM   1536  OG  SER A1005     -20.802  -7.034   6.717  1.00150.49           O  
ANISOU 1536  OG  SER A1005    29572  14009  13598  -2466   -487   -293       O  
ATOM   1537  N   PHE A1006     -20.703  -9.013   4.070  1.00125.10           N  
ANISOU 1537  N   PHE A1006    25268  11464  10800  -2325   -171     45       N  
ATOM   1538  CA  PHE A1006     -19.827  -9.612   3.058  1.00123.43           C  
ANISOU 1538  CA  PHE A1006    24663  11446  10788  -2687      1    169       C  
ATOM   1539  C   PHE A1006     -20.579 -10.526   2.081  1.00123.88           C  
ANISOU 1539  C   PHE A1006    24380  11788  10899  -2251     87    237       C  
ATOM   1540  O   PHE A1006     -20.395 -10.405   0.868  1.00123.78           O  
ANISOU 1540  O   PHE A1006    24526  11684  10820  -2321    247    343       O  
ATOM   1541  CB  PHE A1006     -18.660 -10.370   3.732  1.00124.15           C  
ANISOU 1541  CB  PHE A1006    24088  11903  11181  -3163    -35    142       C  
ATOM   1542  CG  PHE A1006     -17.597 -10.894   2.791  1.00126.02           C  
ANISOU 1542  CG  PHE A1006    23901  12358  11624  -3562    163    236       C  
ATOM   1543  CD1 PHE A1006     -17.722 -12.147   2.199  1.00125.57           C  
ANISOU 1543  CD1 PHE A1006    23264  12676  11769  -3323    259    290       C  
ATOM   1544  CD2 PHE A1006     -16.460 -10.145   2.515  1.00132.37           C  
ANISOU 1544  CD2 PHE A1006    24885  13002  12409  -4204    277    249       C  
ATOM   1545  CE1 PHE A1006     -16.745 -12.626   1.324  1.00127.01           C  
ANISOU 1545  CE1 PHE A1006    23069  13064  12123  -3642    470    353       C  
ATOM   1546  CE2 PHE A1006     -15.481 -10.627   1.641  1.00135.94           C  
ANISOU 1546  CE2 PHE A1006    24898  13713  13040  -4562    500    316       C  
ATOM   1547  CZ  PHE A1006     -15.633 -11.863   1.050  1.00130.41           C  
ANISOU 1547  CZ  PHE A1006    23634  13382  12533  -4243    596    367       C  
ATOM   1548  N   TRP A1007     -21.391 -11.460   2.611  1.00117.58           N  
ANISOU 1548  N   TRP A1007    23127  11344  10204  -1856     -6    166       N  
ATOM   1549  CA  TRP A1007     -22.134 -12.433   1.813  1.00114.69           C  
ANISOU 1549  CA  TRP A1007    22390  11292   9897  -1508     60    184       C  
ATOM   1550  C   TRP A1007     -23.476 -11.865   1.319  1.00119.20           C  
ANISOU 1550  C   TRP A1007    23358  11761  10172   -940     -1    151       C  
ATOM   1551  O   TRP A1007     -24.537 -12.130   1.888  1.00116.85           O  
ANISOU 1551  O   TRP A1007    22902  11673   9824   -527   -101     39       O  
ATOM   1552  CB  TRP A1007     -22.277 -13.770   2.565  1.00110.16           C  
ANISOU 1552  CB  TRP A1007    21150  11135   9570  -1452     23    127       C  
ATOM   1553  CG  TRP A1007     -20.968 -14.367   3.012  1.00110.90           C  
ANISOU 1553  CG  TRP A1007    20842  11361   9932  -1896     48    171       C  
ATOM   1554  CD1 TRP A1007     -20.444 -14.340   4.270  1.00114.39           C  
ANISOU 1554  CD1 TRP A1007    21181  11839  10443  -2086    -90    135       C  
ATOM   1555  CD2 TRP A1007     -20.024 -15.081   2.201  1.00110.47           C  
ANISOU 1555  CD2 TRP A1007    20420  11464  10090  -2157    207    246       C  
ATOM   1556  NE1 TRP A1007     -19.234 -14.994   4.297  1.00114.09           N  
ANISOU 1556  NE1 TRP A1007    20701  11997  10650  -2422    -56    190       N  
ATOM   1557  CE2 TRP A1007     -18.954 -15.464   3.041  1.00114.91           C  
ANISOU 1557  CE2 TRP A1007    20623  12178  10858  -2458    142    253       C  
ATOM   1558  CE3 TRP A1007     -19.986 -15.456   0.848  1.00111.54           C  
ANISOU 1558  CE3 TRP A1007    20487  11652  10240  -2136    396    295       C  
ATOM   1559  CZ2 TRP A1007     -17.849 -16.183   2.568  1.00114.70           C  
ANISOU 1559  CZ2 TRP A1007    20145  12367  11069  -2698    270    303       C  
ATOM   1560  CZ3 TRP A1007     -18.883 -16.151   0.376  1.00113.37           C  
ANISOU 1560  CZ3 TRP A1007    20318  12062  10697  -2412    554    339       C  
ATOM   1561  CH2 TRP A1007     -17.837 -16.519   1.232  1.00114.64           C  
ANISOU 1561  CH2 TRP A1007    20090  12388  11082  -2666    495    340       C  
ATOM   1562  N   ASN A1008     -23.392 -11.052   0.252  1.00119.61           N  
ANISOU 1562  N   ASN A1008    23936  11503  10006   -924     66    251       N  
ATOM   1563  CA  ASN A1008     -24.511 -10.380  -0.416  1.00122.35           C  
ANISOU 1563  CA  ASN A1008    24751  11715  10021   -356    -12    257       C  
ATOM   1564  C   ASN A1008     -24.086  -9.962  -1.825  1.00129.40           C  
ANISOU 1564  C   ASN A1008    26058  12370  10737   -486    119    420       C  
ATOM   1565  O   ASN A1008     -22.905  -9.671  -2.044  1.00129.41           O  
ANISOU 1565  O   ASN A1008    26232  12134  10803  -1054    278    518       O  
ATOM   1566  CB  ASN A1008     -24.953  -9.135   0.377  1.00127.63           C  
ANISOU 1566  CB  ASN A1008    26070  11980  10446    -85   -137    197       C  
ATOM   1567  CG  ASN A1008     -26.354  -8.631   0.081  1.00156.44           C  
ANISOU 1567  CG  ASN A1008    30018  15638  13784    697   -274    142       C  
ATOM   1568  OD1 ASN A1008     -26.930  -8.850  -0.996  1.00155.35           O  
ANISOU 1568  OD1 ASN A1008    29834  15681  13512   1022   -295    194       O  
ATOM   1569  ND2 ASN A1008     -26.935  -7.928   1.042  1.00148.93           N  
ANISOU 1569  ND2 ASN A1008    29378  14519  12690   1043   -381     20       N  
ATOM   1570  N   GLU A1009     -25.047  -9.917  -2.776  1.00128.85           N  
ANISOU 1570  N   GLU A1009    26143  12397  10416     27     52    444       N  
ATOM   1571  CA  GLU A1009     -24.773  -9.498  -4.157  1.00132.75           C  
ANISOU 1571  CA  GLU A1009    27113  12668  10659    -23    161    613       C  
ATOM   1572  C   GLU A1009     -24.766  -7.971  -4.279  1.00142.92           C  
ANISOU 1572  C   GLU A1009    29416  13305  11581    100    135    736       C  
ATOM   1573  O   GLU A1009     -25.480  -7.388  -5.100  1.00145.85           O  
ANISOU 1573  O   GLU A1009    30321  13515  11581    599     44    825       O  
ATOM   1574  CB  GLU A1009     -25.689 -10.185  -5.198  1.00133.90           C  
ANISOU 1574  CB  GLU A1009    26984  13229  10664    417     85    588       C  
ATOM   1575  CG  GLU A1009     -27.189 -10.059  -4.967  1.00147.86           C  
ANISOU 1575  CG  GLU A1009    28693  15246  12240   1175   -183    457       C  
ATOM   1576  CD  GLU A1009     -28.021 -10.527  -6.144  1.00171.30           C  
ANISOU 1576  CD  GLU A1009    31500  18600  14988   1569   -287    436       C  
ATOM   1577  OE1 GLU A1009     -27.908 -11.717  -6.521  1.00165.54           O  
ANISOU 1577  OE1 GLU A1009    30154  18285  14460   1318   -203    357       O  
ATOM   1578  OE2 GLU A1009     -28.788  -9.703  -6.692  1.00169.64           O  
ANISOU 1578  OE2 GLU A1009    31805  18271  14381   2146   -466    492       O  
ATOM   1579  N   SER A1010     -23.903  -7.333  -3.467  1.00141.42           N  
ANISOU 1579  N   SER A1010    29524  12728  11482   -382    213    739       N  
ATOM   1580  CA  SER A1010     -23.710  -5.889  -3.393  1.00146.72           C  
ANISOU 1580  CA  SER A1010    31215  12689  11843   -428    229    830       C  
ATOM   1581  C   SER A1010     -23.144  -5.303  -4.695  1.00154.90           C  
ANISOU 1581  C   SER A1010    32924  13333  12598   -706    430   1061       C  
ATOM   1582  O   SER A1010     -22.784  -4.126  -4.726  1.00160.13           O  
ANISOU 1582  O   SER A1010    34507  13337  13000   -909    508   1163       O  
ATOM   1583  CB  SER A1010     -22.831  -5.526  -2.199  1.00150.79           C  
ANISOU 1583  CB  SER A1010    31767  12976  12552  -1013    269    735       C  
ATOM   1584  OG  SER A1010     -23.293  -6.119  -0.996  1.00157.61           O  
ANISOU 1584  OG  SER A1010    32027  14213  13644   -793    103    539       O  
ATOM   1585  N   TYR A1011     -23.084  -6.114  -5.770  1.00149.18           N  
ANISOU 1585  N   TYR A1011    31802  12987  11893   -727    532   1137       N  
ATOM   1586  CA  TYR A1011     -22.643  -5.660  -7.081  1.00152.95           C  
ANISOU 1586  CA  TYR A1011    32894  13165  12056   -941    738   1359       C  
ATOM   1587  C   TYR A1011     -23.740  -4.758  -7.628  1.00160.87           C  
ANISOU 1587  C   TYR A1011    34766  13804  12555   -160    539   1475       C  
ATOM   1588  O   TYR A1011     -23.489  -3.569  -7.833  1.00166.70           O  
ANISOU 1588  O   TYR A1011    36530  13849  12961   -258    621   1636       O  
ATOM   1589  CB  TYR A1011     -22.398  -6.841  -8.038  1.00151.33           C  
ANISOU 1589  CB  TYR A1011    32009  13509  11981  -1085    881   1369       C  
ATOM   1590  N   LEU A1012     -24.980  -5.310  -7.786  1.00154.50           N  
ANISOU 1590  N   LEU A1012    33547  13469  11685    628    265   1377       N  
ATOM   1591  CA  LEU A1012     -26.168  -4.643  -8.344  1.00158.23           C  
ANISOU 1591  CA  LEU A1012    34635  13799  11687   1525      7   1454       C  
ATOM   1592  C   LEU A1012     -25.789  -4.066  -9.721  1.00167.63           C  
ANISOU 1592  C   LEU A1012    36677  14584  12430   1416    158   1740       C  
ATOM   1593  O   LEU A1012     -26.221  -2.976 -10.111  1.00172.04           O  
ANISOU 1593  O   LEU A1012    37847  14798  12721   1844     51   1912       O  
ATOM   1594  CB  LEU A1012     -26.720  -3.567  -7.379  1.00161.30           C  
ANISOU 1594  CB  LEU A1012    35642  13714  11930   1999   -164   1399       C  
ATOM   1595  CG  LEU A1012     -28.236  -3.439  -7.309  1.00167.17           C  
ANISOU 1595  CG  LEU A1012    36328  14747  12443   3087   -518   1291       C  
ATOM   1596  CD1 LEU A1012     -28.710  -3.364  -5.879  1.00165.76           C  
ANISOU 1596  CD1 LEU A1012    35829  14665  12488   3336   -633   1047       C  
ATOM   1597  CD2 LEU A1012     -28.723  -2.242  -8.087  1.00172.88           C  
ANISOU 1597  CD2 LEU A1012    37434  15269  12985   3552   -623   1512       C  
ATOM   1598  N   THR A1013     -24.930  -4.818 -10.438  1.00161.89           N  
ANISOU 1598  N   THR A1013    35556  14110  11844    777    426   1792       N  
ATOM   1599  CA  THR A1013     -24.382  -4.437 -11.734  1.00165.75           C  
ANISOU 1599  CA  THR A1013    36741  14292  11946    500    659   2050       C  
ATOM   1600  C   THR A1013     -24.570  -5.540 -12.798  1.00165.85           C  
ANISOU 1600  C   THR A1013    36158  14936  11923    578    674   2021       C  
ATOM   1601  O   THR A1013     -25.141  -5.257 -13.853  1.00169.73           O  
ANISOU 1601  O   THR A1013    37186  15382  11920   1047    557   2172       O  
ATOM   1602  CB  THR A1013     -22.912  -3.967 -11.589  1.00174.35           C  
ANISOU 1602  CB  THR A1013    37942  15029  13274   -506   1065   2156       C  
ATOM   1603  OG1 THR A1013     -22.164  -4.909 -10.818  1.00171.07           O  
ANISOU 1603  OG1 THR A1013    36719  14954  13327  -1095   1212   1948       O  
ATOM   1604  CG2 THR A1013     -22.791  -2.563 -10.982  1.00173.49           C  
ANISOU 1604  CG2 THR A1013    37945  14557  13416   -537   1012   2258       C  
ATOM   1605  N   GLY A1014     -24.113  -6.764 -12.508  1.00154.81           N  
ANISOU 1605  N   GLY A1014    33717  14094  11009    159    800   1825       N  
ATOM   1606  CA  GLY A1014     -24.193  -7.898 -13.428  1.00151.53           C  
ANISOU 1606  CA  GLY A1014    32721  14250  10604    150    854   1750       C  
ATOM   1607  C   GLY A1014     -25.423  -8.773 -13.284  1.00150.32           C  
ANISOU 1607  C   GLY A1014    31859  14719  10536    779    497   1520       C  
ATOM   1608  O   GLY A1014     -26.076  -8.761 -12.237  1.00148.04           O  
ANISOU 1608  O   GLY A1014    31249  14542  10456   1109    261   1372       O  
ATOM   1609  N   SER A1015     -25.742  -9.541 -14.347  1.00145.43           N  
ANISOU 1609  N   SER A1015    31000  14524   9733    906    474   1472       N  
ATOM   1610  CA  SER A1015     -26.879 -10.473 -14.403  1.00142.35           C  
ANISOU 1610  CA  SER A1015    29916  14787   9384   1387    163   1226       C  
ATOM   1611  C   SER A1015     -26.421 -11.899 -14.058  1.00139.38           C  
ANISOU 1611  C   SER A1015    28584  14848   9525    909    349    994       C  
ATOM   1612  O   SER A1015     -25.276 -12.254 -14.343  1.00138.72           O  
ANISOU 1612  O   SER A1015    28439  14660   9610    317    714   1046       O  
ATOM   1613  CB  SER A1015     -27.533 -10.444 -15.784  1.00149.63           C  
ANISOU 1613  CB  SER A1015    31200  15910   9744   1806    -10   1287       C  
ATOM   1614  OG  SER A1015     -28.588 -11.385 -15.911  1.00155.85           O  
ANISOU 1614  OG  SER A1015    31279  17380  10555   2171   -303   1015       O  
ATOM   1615  N   ARG A1016     -27.319 -12.713 -13.460  1.00130.89           N  
ANISOU 1615  N   ARG A1016    26786  14263   8683   1175    116    738       N  
ATOM   1616  CA  ARG A1016     -27.046 -14.095 -13.042  1.00125.09           C  
ANISOU 1616  CA  ARG A1016    25213  13902   8416    797    259    515       C  
ATOM   1617  C   ARG A1016     -26.479 -14.957 -14.180  1.00126.53           C  
ANISOU 1617  C   ARG A1016    25292  14252   8533    464    502    476       C  
ATOM   1618  O   ARG A1016     -25.419 -15.565 -14.012  1.00123.47           O  
ANISOU 1618  O   ARG A1016    24630  13801   8482    -38    826    463       O  
ATOM   1619  CB  ARG A1016     -28.303 -14.727 -12.412  1.00124.36           C  
ANISOU 1619  CB  ARG A1016    24501  14305   8446   1166    -41    257       C  
ATOM   1620  CG  ARG A1016     -28.079 -16.084 -11.740  1.00132.49           C  
ANISOU 1620  CG  ARG A1016    24759  15616   9963    782    105     47       C  
ATOM   1621  CD  ARG A1016     -29.202 -17.056 -12.079  1.00150.32           C  
ANISOU 1621  CD  ARG A1016    26510  18451  12154    968    -87   -226       C  
ATOM   1622  NE  ARG A1016     -29.163 -17.514 -13.475  1.00162.86           N  
ANISOU 1622  NE  ARG A1016    28226  20205  13450    901    -43   -271       N  
ATOM   1623  CZ  ARG A1016     -28.502 -18.589 -13.896  1.00173.19           C  
ANISOU 1623  CZ  ARG A1016    29302  21562  14939    474    224   -371       C  
ATOM   1624  NH1 ARG A1016     -27.811 -19.331 -13.038  1.00159.73           N1+
ANISOU 1624  NH1 ARG A1016    27222  19754  13714    107    455   -415       N1+
ATOM   1625  NH2 ARG A1016     -28.525 -18.929 -15.177  1.00159.01           N  
ANISOU 1625  NH2 ARG A1016    27681  19916  12821    446    256   -429       N  
ATOM   1626  N   ASP A1017     -27.166 -14.966 -15.343  1.00124.43           N  
ANISOU 1626  N   ASP A1017    25269  14207   7803    776    339    455       N  
ATOM   1627  CA  ASP A1017     -26.758 -15.712 -16.536  1.00124.12           C  
ANISOU 1627  CA  ASP A1017    25230  14336   7595    523    547    398       C  
ATOM   1628  C   ASP A1017     -25.448 -15.167 -17.109  1.00127.21           C  
ANISOU 1628  C   ASP A1017    26160  14298   7877    105    950    644       C  
ATOM   1629  O   ASP A1017     -24.637 -15.944 -17.619  1.00125.51           O  
ANISOU 1629  O   ASP A1017    25743  14166   7780   -297   1287    575       O  
ATOM   1630  CB  ASP A1017     -27.868 -15.699 -17.597  1.00129.86           C  
ANISOU 1630  CB  ASP A1017    26150  15412   7778    992    216    322       C  
ATOM   1631  CG  ASP A1017     -29.137 -16.407 -17.169  1.00138.55           C  
ANISOU 1631  CG  ASP A1017    26598  17066   8980   1298   -141     18       C  
ATOM   1632  OD1 ASP A1017     -29.959 -15.777 -16.466  1.00141.22           O1-
ANISOU 1632  OD1 ASP A1017    26896  17463   9298   1737   -443     24       O1-
ATOM   1633  OD2 ASP A1017     -29.310 -17.594 -17.534  1.00139.73           O  
ANISOU 1633  OD2 ASP A1017    26283  17589   9219   1081    -97   -242       O  
ATOM   1634  N   GLU A1018     -25.233 -13.839 -16.991  1.00125.54           N  
ANISOU 1634  N   GLU A1018    26634  13622   7442    183    941    915       N  
ATOM   1635  CA  GLU A1018     -24.013 -13.168 -17.451  1.00127.69           C  
ANISOU 1635  CA  GLU A1018    27471  13457   7589   -285   1343   1160       C  
ATOM   1636  C   GLU A1018     -22.798 -13.536 -16.576  1.00126.84           C  
ANISOU 1636  C   GLU A1018    26874  13264   8056   -887   1687   1118       C  
ATOM   1637  O   GLU A1018     -21.723 -13.793 -17.128  1.00128.00           O  
ANISOU 1637  O   GLU A1018    27005  13390   8240  -1369   2099   1156       O  
ATOM   1638  CB  GLU A1018     -24.198 -11.637 -17.528  1.00133.74           C  
ANISOU 1638  CB  GLU A1018    29189  13694   7931    -48   1226   1452       C  
ATOM   1639  CG  GLU A1018     -25.200 -11.161 -18.571  1.00148.75           C  
ANISOU 1639  CG  GLU A1018    31711  15637   9171    561    920   1557       C  
ATOM   1640  CD  GLU A1018     -24.828 -11.405 -20.021  1.00172.16           C  
ANISOU 1640  CD  GLU A1018    35042  18681  11691    384   1148   1639       C  
ATOM   1641  OE1 GLU A1018     -24.183 -10.518 -20.627  1.00171.27           O1-
ANISOU 1641  OE1 GLU A1018    35769  18100  11205    154   1407   1927       O1-
ATOM   1642  OE2 GLU A1018     -25.194 -12.478 -20.557  1.00160.40           O  
ANISOU 1642  OE2 GLU A1018    33042  17709  10195    451   1082   1408       O  
ATOM   1643  N   ARG A1019     -22.978 -13.580 -15.221  1.00117.36           N  
ANISOU 1643  N   ARG A1019    25250  12062   7280   -835   1514   1028       N  
ATOM   1644  CA  ARG A1019     -21.928 -13.927 -14.250  1.00113.01           C  
ANISOU 1644  CA  ARG A1019    24197  11480   7261  -1322   1745    978       C  
ATOM   1645  C   ARG A1019     -21.545 -15.381 -14.393  1.00114.23           C  
ANISOU 1645  C   ARG A1019    23620  12039   7742  -1500   1926    771       C  
ATOM   1646  O   ARG A1019     -20.374 -15.718 -14.224  1.00113.04           O  
ANISOU 1646  O   ARG A1019    23165  11899   7886  -1944   2247    767       O  
ATOM   1647  CB  ARG A1019     -22.382 -13.676 -12.809  1.00107.27           C  
ANISOU 1647  CB  ARG A1019    23243  10689   6824  -1144   1469    920       C  
ATOM   1648  CG  ARG A1019     -22.630 -12.216 -12.452  1.00112.41           C  
ANISOU 1648  CG  ARG A1019    24631  10866   7214   -988   1320   1098       C  
ATOM   1649  CD  ARG A1019     -22.875 -12.031 -10.965  1.00107.47           C  
ANISOU 1649  CD  ARG A1019    23749  10184   6903   -900   1119   1012       C  
ATOM   1650  NE  ARG A1019     -23.998 -12.828 -10.461  1.00 97.54           N  
ANISOU 1650  NE  ARG A1019    21937   9341   5783   -445    836    808       N  
ATOM   1651  CZ  ARG A1019     -25.230 -12.363 -10.271  1.00108.63           C  
ANISOU 1651  CZ  ARG A1019    23535  10785   6956    148    515    769       C  
ATOM   1652  NH1 ARG A1019     -25.520 -11.096 -10.546  1.00102.97           N  
ANISOU 1652  NH1 ARG A1019    23615   9664   5845    440    408    933       N  
ATOM   1653  NH2 ARG A1019     -26.179 -13.159  -9.794  1.00 83.16           N1+
ANISOU 1653  NH2 ARG A1019    19716   8003   3879    455    312    559       N1+
ATOM   1654  N   LYS A1020     -22.543 -16.242 -14.693  1.00110.27           N  
ANISOU 1654  N   LYS A1020    22837  11880   7180  -1146   1714    584       N  
ATOM   1655  CA  LYS A1020     -22.383 -17.680 -14.897  1.00108.58           C  
ANISOU 1655  CA  LYS A1020    22038  12002   7217  -1255   1857    360       C  
ATOM   1656  C   LYS A1020     -21.543 -17.936 -16.152  1.00120.03           C  
ANISOU 1656  C   LYS A1020    23676  13470   8460  -1524   2239    383       C  
ATOM   1657  O   LYS A1020     -20.568 -18.688 -16.064  1.00120.19           O  
ANISOU 1657  O   LYS A1020    23295  13570   8802  -1823   2556    304       O  
ATOM   1658  CB  LYS A1020     -23.761 -18.376 -14.977  1.00108.72           C  
ANISOU 1658  CB  LYS A1020    21818  12354   7136   -867   1524    145       C  
ATOM   1659  CG  LYS A1020     -23.711 -19.908 -14.980  1.00103.89           C  
ANISOU 1659  CG  LYS A1020    20642  12018   6813   -999   1647   -113       C  
ATOM   1660  CD  LYS A1020     -25.082 -20.532 -14.732  1.00103.39           C  
ANISOU 1660  CD  LYS A1020    20284  12277   6725   -726   1314   -339       C  
ATOM   1661  CE  LYS A1020     -25.797 -20.957 -15.993  1.00103.83           C  
ANISOU 1661  CE  LYS A1020    20473  12612   6365   -600   1220   -505       C  
ATOM   1662  NZ  LYS A1020     -27.047 -21.710 -15.699  1.00102.23           N1+
ANISOU 1662  NZ  LYS A1020    19870  12785   6189   -454    935   -776       N1+
ATOM   1663  N   LYS A1021     -21.902 -17.290 -17.304  1.00121.94           N  
ANISOU 1663  N   LYS A1021    24545  13644   8142  -1387   2214    497       N  
ATOM   1664  CA  LYS A1021     -21.191 -17.411 -18.586  1.00126.26           C  
ANISOU 1664  CA  LYS A1021    25386  14205   8382  -1629   2588    536       C  
ATOM   1665  C   LYS A1021     -19.743 -16.936 -18.460  1.00133.39           C  
ANISOU 1665  C   LYS A1021    26337  14889   9457  -2142   3033    693       C  
ATOM   1666  O   LYS A1021     -18.847 -17.603 -18.979  1.00134.55           O  
ANISOU 1666  O   LYS A1021    26237  15188   9699  -2428   3435    605       O  
ATOM   1667  CB  LYS A1021     -21.916 -16.651 -19.716  1.00133.48           C  
ANISOU 1667  CB  LYS A1021    27056  15052   8609  -1346   2421    674       C  
ATOM   1668  N   SER A1022     -19.524 -15.803 -17.743  1.00131.16           N  
ANISOU 1668  N   SER A1022    26348  14272   9216  -2263   2965    898       N  
ATOM   1669  CA  SER A1022     -18.213 -15.200 -17.467  1.00133.51           C  
ANISOU 1669  CA  SER A1022    26684  14368   9678  -2819   3336   1035       C  
ATOM   1670  C   SER A1022     -17.349 -16.160 -16.645  1.00135.57           C  
ANISOU 1670  C   SER A1022    26067  14896  10547  -3057   3505    856       C  
ATOM   1671  O   SER A1022     -16.159 -16.299 -16.933  1.00137.55           O  
ANISOU 1671  O   SER A1022    26100  15248  10915  -3486   3931    853       O  
ATOM   1672  CB  SER A1022     -18.381 -13.872 -16.729  1.00138.28           C  
ANISOU 1672  CB  SER A1022    27792  14543  10206  -2850   3136   1235       C  
ATOM   1673  OG  SER A1022     -17.179 -13.410 -16.131  1.00148.52           O  
ANISOU 1673  OG  SER A1022    28955  15703  11774  -3429   3415   1298       O  
ATOM   1674  N   LEU A1023     -17.965 -16.827 -15.636  1.00128.29           N  
ANISOU 1674  N   LEU A1023    24649  14109   9985  -2757   3175    707       N  
ATOM   1675  CA  LEU A1023     -17.345 -17.802 -14.737  1.00124.97           C  
ANISOU 1675  CA  LEU A1023    23452  13916  10116  -2851   3239    552       C  
ATOM   1676  C   LEU A1023     -16.953 -19.074 -15.491  1.00129.59           C  
ANISOU 1676  C   LEU A1023    23663  14792  10783  -2832   3525    367       C  
ATOM   1677  O   LEU A1023     -15.808 -19.518 -15.397  1.00129.95           O  
ANISOU 1677  O   LEU A1023    23275  14991  11108  -3082   3846    315       O  
ATOM   1678  CB  LEU A1023     -18.316 -18.131 -13.600  1.00120.55           C  
ANISOU 1678  CB  LEU A1023    22636  13378   9791  -2503   2810    466       C  
ATOM   1679  CG  LEU A1023     -17.802 -19.081 -12.541  1.00122.81           C  
ANISOU 1679  CG  LEU A1023    22226  13839  10599  -2542   2812    343       C  
ATOM   1680  CD1 LEU A1023     -17.550 -18.354 -11.225  1.00121.98           C  
ANISOU 1680  CD1 LEU A1023    22046  13588  10712  -2670   2625    436       C  
ATOM   1681  CD2 LEU A1023     -18.756 -20.233 -12.361  1.00123.23           C  
ANISOU 1681  CD2 LEU A1023    22005  14059  10757  -2195   2617    159       C  
ATOM   1682  N   LEU A1024     -17.903 -19.642 -16.252  1.00126.46           N  
ANISOU 1682  N   LEU A1024    23438  14490  10122  -2525   3406    249       N  
ATOM   1683  CA  LEU A1024     -17.697 -20.857 -17.027  1.00127.29           C  
ANISOU 1683  CA  LEU A1024    23305  14820  10238  -2477   3653     38       C  
ATOM   1684  C   LEU A1024     -16.749 -20.646 -18.220  1.00138.71           C  
ANISOU 1684  C   LEU A1024    24988  16309  11407  -2757   4133     83       C  
ATOM   1685  O   LEU A1024     -16.171 -21.613 -18.705  1.00140.19           O  
ANISOU 1685  O   LEU A1024    24887  16683  11696  -2781   4451    -93       O  
ATOM   1686  CB  LEU A1024     -19.038 -21.485 -17.443  1.00125.76           C  
ANISOU 1686  CB  LEU A1024    23235  14731   9818  -2133   3354   -132       C  
ATOM   1687  CG  LEU A1024     -19.882 -22.090 -16.299  1.00125.59           C  
ANISOU 1687  CG  LEU A1024    22833  14758  10127  -1912   2993   -253       C  
ATOM   1688  CD1 LEU A1024     -21.308 -22.324 -16.738  1.00125.42           C  
ANISOU 1688  CD1 LEU A1024    22986  14875   9792  -1640   2660   -393       C  
ATOM   1689  CD2 LEU A1024     -19.285 -23.395 -15.783  1.00125.42           C  
ANISOU 1689  CD2 LEU A1024    22277  14817  10560  -1951   3179   -427       C  
ATOM   1690  N   SER A1025     -16.540 -19.392 -18.655  1.00139.79           N  
ANISOU 1690  N   SER A1025    25666  16254  11192  -2980   4222    317       N  
ATOM   1691  CA  SER A1025     -15.574 -19.099 -19.715  1.00145.37           C  
ANISOU 1691  CA  SER A1025    26614  16998  11621  -3330   4731    384       C  
ATOM   1692  C   SER A1025     -14.178 -19.001 -19.088  1.00151.18           C  
ANISOU 1692  C   SER A1025    26835  17833  12775  -3746   5072    404       C  
ATOM   1693  O   SER A1025     -13.206 -19.444 -19.701  1.00154.42           O  
ANISOU 1693  O   SER A1025    26992  18473  13209  -3961   5547    312       O  
ATOM   1694  CB  SER A1025     -15.920 -17.801 -20.443  1.00153.68           C  
ANISOU 1694  CB  SER A1025    28536  17767  12087  -3428   4706    644       C  
ATOM   1695  OG  SER A1025     -15.052 -17.568 -21.544  1.00169.25           O  
ANISOU 1695  OG  SER A1025    30801  19782  13725  -3791   5233    711       O  
ATOM   1696  N   LYS A1026     -14.091 -18.427 -17.863  1.00145.86           N  
ANISOU 1696  N   LYS A1026    25983  17023  12413  -3847   4823    502       N  
ATOM   1697  CA  LYS A1026     -12.849 -18.250 -17.097  1.00147.08           C  
ANISOU 1697  CA  LYS A1026    25608  17308  12967  -4247   5037    510       C  
ATOM   1698  C   LYS A1026     -12.190 -19.584 -16.729  1.00148.88           C  
ANISOU 1698  C   LYS A1026    24995  17909  13664  -4091   5176    282       C  
ATOM   1699  O   LYS A1026     -10.961 -19.682 -16.759  1.00152.03           O  
ANISOU 1699  O   LYS A1026    24932  18576  14255  -4397   5550    234       O  
ATOM   1700  CB  LYS A1026     -13.089 -17.388 -15.844  1.00147.99           C  
ANISOU 1700  CB  LYS A1026    25792  17180  13259  -4331   4660    635       C  
ATOM   1701  CG  LYS A1026     -12.967 -15.889 -16.107  1.00169.12           C  
ANISOU 1701  CG  LYS A1026    29194  19497  15565  -4739   4741    868       C  
ATOM   1702  CD  LYS A1026     -13.481 -15.065 -14.932  1.00177.02           C  
ANISOU 1702  CD  LYS A1026    30411  20183  16664  -4698   4316    962       C  
ATOM   1703  CE  LYS A1026     -13.544 -13.594 -15.263  1.00191.65           C  
ANISOU 1703  CE  LYS A1026    33161  21569  18088  -5012   4369   1193       C  
ATOM   1704  NZ  LYS A1026     -14.231 -12.819 -14.198  1.00197.46           N1+
ANISOU 1704  NZ  LYS A1026    34215  21951  18860  -4848   3935   1260       N1+
ATOM   1705  N   PHE A1027     -13.002 -20.607 -16.404  1.00140.06           N  
ANISOU 1705  N   PHE A1027    23694  16814  12710  -3614   4889    136       N  
ATOM   1706  CA  PHE A1027     -12.510 -21.945 -16.079  1.00138.43           C  
ANISOU 1706  CA  PHE A1027    22831  16863  12903  -3380   4997    -70       C  
ATOM   1707  C   PHE A1027     -12.153 -22.748 -17.335  1.00144.55           C  
ANISOU 1707  C   PHE A1027    23613  17815  13495  -3304   5430   -240       C  
ATOM   1708  O   PHE A1027     -11.150 -23.463 -17.342  1.00145.92           O  
ANISOU 1708  O   PHE A1027    23256  18252  13934  -3278   5750   -373       O  
ATOM   1709  CB  PHE A1027     -13.531 -22.712 -15.228  1.00135.14           C  
ANISOU 1709  CB  PHE A1027    22309  16340  12699  -2967   4556   -153       C  
ATOM   1710  CG  PHE A1027     -13.625 -22.258 -13.793  1.00133.73           C  
ANISOU 1710  CG  PHE A1027    21926  16075  12810  -2989   4194    -44       C  
ATOM   1711  CD1 PHE A1027     -12.549 -22.409 -12.926  1.00137.63           C  
ANISOU 1711  CD1 PHE A1027    21845  16755  13693  -3102   4255    -43       C  
ATOM   1712  CD2 PHE A1027     -14.809 -21.733 -13.291  1.00132.54           C  
ANISOU 1712  CD2 PHE A1027    22132  15699  12528  -2859   3780     36       C  
ATOM   1713  CE1 PHE A1027     -12.640 -21.999 -11.595  1.00136.31           C  
ANISOU 1713  CE1 PHE A1027    21524  16519  13750  -3129   3904     44       C  
ATOM   1714  CE2 PHE A1027     -14.902 -21.329 -11.957  1.00133.12           C  
ANISOU 1714  CE2 PHE A1027    22047  15693  12839  -2870   3469    116       C  
ATOM   1715  CZ  PHE A1027     -13.818 -21.464 -11.118  1.00132.15           C  
ANISOU 1715  CZ  PHE A1027    21408  15728  13075  -3021   3529    122       C  
ATOM   1716  N   GLY A1028     -12.976 -22.621 -18.373  1.00141.68           N  
ANISOU 1716  N   GLY A1028    23846  17326  12661  -3234   5425   -245       N  
ATOM   1717  CA  GLY A1028     -12.796 -23.321 -19.639  1.00144.91           C  
ANISOU 1717  CA  GLY A1028    24390  17871  12796  -3165   5806   -419       C  
ATOM   1718  C   GLY A1028     -13.884 -24.340 -19.900  1.00147.05           C  
ANISOU 1718  C   GLY A1028    24817  18077  12978  -2782   5564   -624       C  
ATOM   1719  O   GLY A1028     -13.601 -25.524 -20.101  1.00147.78           O  
ANISOU 1719  O   GLY A1028    24645  18272  13232  -2583   5767   -862       O  
ATOM   1720  N   MET A1029     -15.138 -23.878 -19.904  1.00141.17           N  
ANISOU 1720  N   MET A1029    24510  17168  11961  -2677   5134   -549       N  
ATOM   1721  CA  MET A1029     -16.324 -24.699 -20.122  1.00138.86           C  
ANISOU 1721  CA  MET A1029    24363  16858  11539  -2390   4843   -749       C  
ATOM   1722  C   MET A1029     -17.350 -23.968 -20.993  1.00142.96           C  
ANISOU 1722  C   MET A1029    25513  17341  11465  -2352   4607   -674       C  
ATOM   1723  O   MET A1029     -17.090 -22.856 -21.464  1.00145.34           O  
ANISOU 1723  O   MET A1029    26211  17571  11440  -2524   4705   -446       O  
ATOM   1724  CB  MET A1029     -16.937 -25.090 -18.771  1.00136.56           C  
ANISOU 1724  CB  MET A1029    23727  16488  11671  -2215   4438   -771       C  
ATOM   1725  CG  MET A1029     -16.273 -26.280 -18.140  1.00139.88           C  
ANISOU 1725  CG  MET A1029    23638  16938  12572  -2106   4608   -931       C  
ATOM   1726  SD  MET A1029     -16.293 -26.257 -16.328  1.00140.22           S  
ANISOU 1726  SD  MET A1029    23234  16892  13150  -2031   4268   -806       S  
ATOM   1727  CE  MET A1029     -15.302 -27.667 -16.010  1.00138.13           C  
ANISOU 1727  CE  MET A1029    22502  16670  13309  -1848   4569   -981       C  
ATOM   1728  N   ASP A1030     -18.500 -24.616 -21.228  1.00137.11           N  
ANISOU 1728  N   ASP A1030    24876  16659  10560  -2133   4300   -872       N  
ATOM   1729  CA  ASP A1030     -19.624 -24.085 -21.997  1.00137.87           C  
ANISOU 1729  CA  ASP A1030    25480  16809  10096  -2006   3979   -850       C  
ATOM   1730  C   ASP A1030     -20.756 -23.783 -21.008  1.00136.83           C  
ANISOU 1730  C   ASP A1030    25217  16665  10106  -1805   3437   -807       C  
ATOM   1731  O   ASP A1030     -20.721 -24.283 -19.881  1.00132.76           O  
ANISOU 1731  O   ASP A1030    24244  16109  10089  -1792   3357   -860       O  
ATOM   1732  CB  ASP A1030     -20.104 -25.117 -23.040  1.00142.10           C  
ANISOU 1732  CB  ASP A1030    26161  17515  10315  -1939   4029  -1172       C  
ATOM   1733  CG  ASP A1030     -18.996 -25.851 -23.769  1.00154.45           C  
ANISOU 1733  CG  ASP A1030    27693  19104  11886  -2079   4598  -1326       C  
ATOM   1734  OD1 ASP A1030     -18.427 -26.799 -23.183  1.00153.44           O1-
ANISOU 1734  OD1 ASP A1030    27128  18936  12238  -2071   4800  -1482       O1-
ATOM   1735  OD2 ASP A1030     -18.705 -25.484 -24.930  1.00164.47           O  
ANISOU 1735  OD2 ASP A1030    29400  20434  12657  -2166   4848  -1291       O  
ATOM   1736  N   GLU A1031     -21.757 -22.977 -21.424  1.00133.89           N  
ANISOU 1736  N   GLU A1031    25249  16346   9275  -1615   3072   -712       N  
ATOM   1737  CA  GLU A1031     -22.924 -22.608 -20.602  1.00130.43           C  
ANISOU 1737  CA  GLU A1031    24695  15965   8896  -1363   2560   -690       C  
ATOM   1738  C   GLU A1031     -23.847 -23.811 -20.307  1.00130.93           C  
ANISOU 1738  C   GLU A1031    24350  16270   9127  -1292   2336  -1026       C  
ATOM   1739  O   GLU A1031     -24.407 -24.417 -21.227  1.00133.53           O  
ANISOU 1739  O   GLU A1031    24795  16819   9121  -1270   2272  -1260       O  
ATOM   1740  CB  GLU A1031     -23.705 -21.425 -21.218  1.00134.72           C  
ANISOU 1740  CB  GLU A1031    25797  16527   8864  -1099   2240   -505       C  
ATOM   1741  CG  GLU A1031     -23.968 -21.551 -22.713  1.00147.24           C  
ANISOU 1741  CG  GLU A1031    27827  18288   9831  -1044   2265   -590       C  
ATOM   1742  CD  GLU A1031     -25.052 -20.645 -23.258  1.00166.64           C  
ANISOU 1742  CD  GLU A1031    30747  20864  11704   -655   1810   -474       C  
ATOM   1743  OE1 GLU A1031     -24.836 -19.412 -23.293  1.00168.76           O1-
ANISOU 1743  OE1 GLU A1031    31518  20860  11744   -552   1796   -143       O1-
ATOM   1744  OE2 GLU A1031     -26.113 -21.169 -23.666  1.00157.63           O  
ANISOU 1744  OE2 GLU A1031    29485  20094  10313   -453   1464   -721       O  
ATOM   1745  N   GLY A1032     -23.952 -24.160 -19.025  1.00121.95           N  
ANISOU 1745  N   GLY A1032    22766  15081   8487  -1305   2243  -1053       N  
ATOM   1746  CA  GLY A1032     -24.760 -25.277 -18.543  1.00119.08           C  
ANISOU 1746  CA  GLY A1032    22023  14887   8334  -1317   2079  -1342       C  
ATOM   1747  C   GLY A1032     -25.080 -25.202 -17.066  1.00116.74           C  
ANISOU 1747  C   GLY A1032    21359  14539   8457  -1271   1893  -1276       C  
ATOM   1748  O   GLY A1032     -24.747 -24.215 -16.399  1.00114.16           O  
ANISOU 1748  O   GLY A1032    21077  14055   8241  -1196   1842  -1018       O  
ATOM   1749  N   VAL A1033     -25.741 -26.253 -16.548  1.00111.35           N  
ANISOU 1749  N   VAL A1033    20351  13975   7981  -1349   1806  -1520       N  
ATOM   1750  CA  VAL A1033     -26.141 -26.353 -15.136  1.00107.63           C  
ANISOU 1750  CA  VAL A1033    19535  13485   7876  -1337   1654  -1491       C  
ATOM   1751  C   VAL A1033     -24.899 -26.657 -14.281  1.00109.05           C  
ANISOU 1751  C   VAL A1033    19571  13345   8518  -1446   1942  -1342       C  
ATOM   1752  O   VAL A1033     -24.331 -27.750 -14.377  1.00108.54           O  
ANISOU 1752  O   VAL A1033    19433  13156   8650  -1578   2204  -1470       O  
ATOM   1753  CB  VAL A1033     -27.305 -27.356 -14.893  1.00111.20           C  
ANISOU 1753  CB  VAL A1033    19721  14184   8347  -1447   1491  -1800       C  
ATOM   1754  CG1 VAL A1033     -27.886 -27.183 -13.495  1.00108.53           C  
ANISOU 1754  CG1 VAL A1033    19073  13892   8271  -1403   1310  -1741       C  
ATOM   1755  CG2 VAL A1033     -28.404 -27.203 -15.940  1.00114.10           C  
ANISOU 1755  CG2 VAL A1033    20180  14949   8225  -1368   1219  -2002       C  
ATOM   1756  N   THR A1034     -24.461 -25.666 -13.479  1.00104.15           N  
ANISOU 1756  N   THR A1034    18936  12595   8043  -1369   1881  -1081       N  
ATOM   1757  CA  THR A1034     -23.260 -25.772 -12.643  1.00102.30           C  
ANISOU 1757  CA  THR A1034    18533  12131   8207  -1460   2091   -928       C  
ATOM   1758  C   THR A1034     -23.544 -26.253 -11.227  1.00102.58           C  
ANISOU 1758  C   THR A1034    18270  12122   8583  -1457   1971   -931       C  
ATOM   1759  O   THR A1034     -24.539 -25.862 -10.619  1.00100.71           O  
ANISOU 1759  O   THR A1034    17980  12003   8282  -1369   1703   -940       O  
ATOM   1760  CB  THR A1034     -22.445 -24.473 -12.634  1.00112.54           C  
ANISOU 1760  CB  THR A1034    20008  13301   9452  -1474   2138   -665       C  
ATOM   1761  OG1 THR A1034     -22.696 -23.730 -13.830  1.00118.33           O  
ANISOU 1761  OG1 THR A1034    21135  14087   9740  -1425   2123   -629       O  
ATOM   1762  CG2 THR A1034     -20.955 -24.738 -12.495  1.00109.81           C  
ANISOU 1762  CG2 THR A1034    19495  12833   9394  -1631   2466   -583       C  
ATOM   1763  N   PHE A1035     -22.640 -27.100 -10.717  1.00 98.91           N  
ANISOU 1763  N   PHE A1035    17623  11502   8456  -1524   2183   -922       N  
ATOM   1764  CA  PHE A1035     -22.661 -27.714  -9.392  1.00 97.38           C  
ANISOU 1764  CA  PHE A1035    17205  11215   8582  -1521   2125   -896       C  
ATOM   1765  C   PHE A1035     -21.333 -27.408  -8.733  1.00 99.40           C  
ANISOU 1765  C   PHE A1035    17313  11347   9107  -1507   2227   -695       C  
ATOM   1766  O   PHE A1035     -20.316 -27.383  -9.425  1.00101.12           O  
ANISOU 1766  O   PHE A1035    17527  11550   9346  -1531   2460   -669       O  
ATOM   1767  CB  PHE A1035     -22.913 -29.228  -9.514  1.00100.71           C  
ANISOU 1767  CB  PHE A1035    17610  11556   9098  -1582   2271  -1107       C  
ATOM   1768  CG  PHE A1035     -24.281 -29.536 -10.078  1.00103.66           C  
ANISOU 1768  CG  PHE A1035    18069  12113   9202  -1678   2143  -1342       C  
ATOM   1769  CD1 PHE A1035     -25.391 -29.623  -9.244  1.00105.31           C  
ANISOU 1769  CD1 PHE A1035    18154  12446   9413  -1738   1937  -1401       C  
ATOM   1770  CD2 PHE A1035     -24.473 -29.670 -11.450  1.00109.41           C  
ANISOU 1770  CD2 PHE A1035    18979  12950   9642  -1719   2219  -1517       C  
ATOM   1771  CE1 PHE A1035     -26.666 -29.851  -9.771  1.00109.84           C  
ANISOU 1771  CE1 PHE A1035    18716  13291   9728  -1850   1802  -1644       C  
ATOM   1772  CE2 PHE A1035     -25.749 -29.890 -11.976  1.00111.92           C  
ANISOU 1772  CE2 PHE A1035    19326  13516   9680  -1817   2048  -1754       C  
ATOM   1773  CZ  PHE A1035     -26.836 -29.980 -11.132  1.00110.38           C  
ANISOU 1773  CZ  PHE A1035    18940  13485   9515  -1887   1836  -1823       C  
ATOM   1774  N   MET A1036     -21.335 -27.115  -7.425  1.00 93.02           N  
ANISOU 1774  N   MET A1036    16369  10499   8474  -1482   2052   -566       N  
ATOM   1775  CA  MET A1036     -20.115 -26.680  -6.747  1.00 93.15           C  
ANISOU 1775  CA  MET A1036    16219  10465   8710  -1495   2082   -388       C  
ATOM   1776  C   MET A1036     -19.926 -27.223  -5.309  1.00 95.40           C  
ANISOU 1776  C   MET A1036    16313  10680   9254  -1428   1968   -311       C  
ATOM   1777  O   MET A1036     -20.872 -27.234  -4.527  1.00 93.58           O  
ANISOU 1777  O   MET A1036    16129  10445   8981  -1414   1785   -320       O  
ATOM   1778  CB  MET A1036     -20.093 -25.136  -6.766  1.00 95.53           C  
ANISOU 1778  CB  MET A1036    16667  10790   8838  -1576   1949   -258       C  
ATOM   1779  CG  MET A1036     -18.825 -24.513  -6.253  1.00100.20           C  
ANISOU 1779  CG  MET A1036    17106  11367   9598  -1699   1988   -108       C  
ATOM   1780  SD  MET A1036     -19.239 -22.942  -5.490  1.00103.77           S  
ANISOU 1780  SD  MET A1036    17792  11739   9898  -1774   1713     19       S  
ATOM   1781  CE  MET A1036     -17.881 -22.743  -4.447  1.00101.36           C  
ANISOU 1781  CE  MET A1036    17184  11461   9869  -1938   1695    128       C  
ATOM   1782  N   PHE A1037     -18.673 -27.606  -4.964  1.00 92.08           N  
ANISOU 1782  N   PHE A1037    15667  10244   9074  -1372   2074   -232       N  
ATOM   1783  CA  PHE A1037     -18.240 -28.113  -3.660  1.00 91.26           C  
ANISOU 1783  CA  PHE A1037    15390  10092   9193  -1259   1957   -129       C  
ATOM   1784  C   PHE A1037     -17.017 -27.336  -3.136  1.00 98.89           C  
ANISOU 1784  C   PHE A1037    16095  11191  10289  -1308   1886      8       C  
ATOM   1785  O   PHE A1037     -16.107 -27.042  -3.900  1.00100.47           O  
ANISOU 1785  O   PHE A1037    16147  11507  10519  -1377   2065     -2       O  
ATOM   1786  CB  PHE A1037     -17.885 -29.609  -3.768  1.00 94.03           C  
ANISOU 1786  CB  PHE A1037    15711  10313   9704  -1063   2140   -195       C  
ATOM   1787  CG  PHE A1037     -17.344 -30.250  -2.508  1.00 95.82           C  
ANISOU 1787  CG  PHE A1037    15812  10465  10129   -869   2026    -65       C  
ATOM   1788  CD1 PHE A1037     -15.988 -30.193  -2.203  1.00100.82           C  
ANISOU 1788  CD1 PHE A1037    16121  11238  10947   -718   2023     32       C  
ATOM   1789  CD2 PHE A1037     -18.185 -30.931  -1.638  1.00 96.19           C  
ANISOU 1789  CD2 PHE A1037    16061  10332  10153   -839   1925    -42       C  
ATOM   1790  CE1 PHE A1037     -15.493 -30.768  -1.027  1.00102.62           C  
ANISOU 1790  CE1 PHE A1037    16244  11430  11317   -484   1866    163       C  
ATOM   1791  CE2 PHE A1037     -17.686 -31.521  -0.472  1.00 99.50           C  
ANISOU 1791  CE2 PHE A1037    16443  10661  10703   -637   1811    106       C  
ATOM   1792  CZ  PHE A1037     -16.346 -31.433  -0.173  1.00 99.84           C  
ANISOU 1792  CZ  PHE A1037    16178  10845  10912   -430   1759    213       C  
ATOM   1793  N   ILE A1038     -16.985 -27.054  -1.822  1.00 96.96           N  
ANISOU 1793  N   ILE A1038    15784  10954  10105  -1298   1638    120       N  
ATOM   1794  CA  ILE A1038     -15.860 -26.441  -1.101  1.00 99.26           C  
ANISOU 1794  CA  ILE A1038    15800  11400  10515  -1365   1509    226       C  
ATOM   1795  C   ILE A1038     -15.662 -27.189   0.226  1.00105.24           C  
ANISOU 1795  C   ILE A1038    16445  12143  11399  -1156   1317    318       C  
ATOM   1796  O   ILE A1038     -16.502 -28.011   0.603  1.00104.59           O  
ANISOU 1796  O   ILE A1038    16570  11887  11284  -1019   1302    314       O  
ATOM   1797  CB  ILE A1038     -15.938 -24.902  -0.894  1.00102.26           C  
ANISOU 1797  CB  ILE A1038    16299  11811  10744  -1649   1360    266       C  
ATOM   1798  CG1 ILE A1038     -17.260 -24.456  -0.263  1.00100.99           C  
ANISOU 1798  CG1 ILE A1038    16464  11510  10397  -1637   1164    265       C  
ATOM   1799  CG2 ILE A1038     -15.630 -24.122  -2.146  1.00103.93           C  
ANISOU 1799  CG2 ILE A1038    16591  12053  10846  -1866   1567    229       C  
ATOM   1800  CD1 ILE A1038     -17.017 -23.593   0.979  1.00115.68           C  
ANISOU 1800  CD1 ILE A1038    18331  13393  12231  -1750    902    338       C  
ATOM   1801  N   GLY A1039     -14.575 -26.893   0.929  1.00104.01           N  
ANISOU 1801  N   GLY A1039    15979  12181  11358  -1159   1169    398       N  
ATOM   1802  CA  GLY A1039     -14.282 -27.539   2.203  1.00104.71           C  
ANISOU 1802  CA  GLY A1039    15973  12290  11524   -927    947    507       C  
ATOM   1803  C   GLY A1039     -13.302 -28.684   2.075  1.00110.50           C  
ANISOU 1803  C   GLY A1039    16424  13105  12456   -572   1044    530       C  
ATOM   1804  O   GLY A1039     -12.951 -29.089   0.961  1.00111.43           O  
ANISOU 1804  O   GLY A1039    16440  13241  12657   -498   1326    436       O  
ATOM   1805  N   ARG A1040     -12.856 -29.208   3.227  1.00107.69           N  
ANISOU 1805  N   ARG A1040    15968  12801  12148   -312    806    654       N  
ATOM   1806  CA  ARG A1040     -11.878 -30.288   3.327  1.00111.04           C  
ANISOU 1806  CA  ARG A1040    16137  13313  12742    141    826    704       C  
ATOM   1807  C   ARG A1040     -12.262 -31.535   2.545  1.00114.60           C  
ANISOU 1807  C   ARG A1040    16864  13438  13242    419   1130    648       C  
ATOM   1808  O   ARG A1040     -13.440 -31.892   2.464  1.00110.91           O  
ANISOU 1808  O   ARG A1040    16858  12628  12654    314   1221    627       O  
ATOM   1809  CB  ARG A1040     -11.613 -30.641   4.799  1.00111.87           C  
ANISOU 1809  CB  ARG A1040    16246  13456  12804    399    471    876       C  
ATOM   1810  CG  ARG A1040     -10.167 -31.020   5.085  1.00123.44           C  
ANISOU 1810  CG  ARG A1040    17184  15291  14425    783    328    923       C  
ATOM   1811  CD  ARG A1040      -9.911 -31.223   6.568  1.00134.94           C  
ANISOU 1811  CD  ARG A1040    18659  16832  15778   1023    -85   1100       C  
ATOM   1812  NE  ARG A1040     -10.058 -29.983   7.336  1.00141.13           N  
ANISOU 1812  NE  ARG A1040    19395  17814  16415    581   -366   1097       N  
ATOM   1813  CZ  ARG A1040      -9.082 -29.104   7.547  1.00155.76           C  
ANISOU 1813  CZ  ARG A1040    20727  20146  18309    373   -574   1033       C  
ATOM   1814  NH1 ARG A1040      -7.868 -29.314   7.051  1.00148.71           N  
ANISOU 1814  NH1 ARG A1040    19228  19661  17613    568   -529    968       N  
ATOM   1815  NH2 ARG A1040      -9.313 -28.006   8.254  1.00137.17           N1+
ANISOU 1815  NH2 ARG A1040    18449  17880  15789    -48   -812   1011       N1+
ATOM   1816  N   PHE A1041     -11.258 -32.176   1.949  1.00115.37           N  
ANISOU 1816  N   PHE A1041    16661  13668  13506    757   1299    598       N  
ATOM   1817  CA  PHE A1041     -11.441 -33.419   1.221  1.00117.03           C  
ANISOU 1817  CA  PHE A1041    17151  13551  13763   1076   1596    524       C  
ATOM   1818  C   PHE A1041     -11.282 -34.553   2.240  1.00124.60           C  
ANISOU 1818  C   PHE A1041    18333  14271  14739   1574   1434    690       C  
ATOM   1819  O   PHE A1041     -10.153 -34.918   2.566  1.00129.08           O  
ANISOU 1819  O   PHE A1041    18542  15072  15430   2027   1329    754       O  
ATOM   1820  CB  PHE A1041     -10.409 -33.530   0.082  1.00122.17           C  
ANISOU 1820  CB  PHE A1041    17392  14466  14562   1243   1886    375       C  
ATOM   1821  CG  PHE A1041     -10.809 -32.999  -1.277  1.00121.53           C  
ANISOU 1821  CG  PHE A1041    17380  14390  14405    862   2202    194       C  
ATOM   1822  CD1 PHE A1041     -11.795 -32.028  -1.404  1.00120.05           C  
ANISOU 1822  CD1 PHE A1041    17427  14141  14047    358   2136    184       C  
ATOM   1823  CD2 PHE A1041     -10.169 -33.444  -2.428  1.00127.02           C  
ANISOU 1823  CD2 PHE A1041    17913  15176  15174   1047   2560     35       C  
ATOM   1824  CE1 PHE A1041     -12.152 -31.533  -2.662  1.00119.82           C  
ANISOU 1824  CE1 PHE A1041    17500  14121  13903     59   2393     40       C  
ATOM   1825  CE2 PHE A1041     -10.525 -32.947  -3.685  1.00128.40           C  
ANISOU 1825  CE2 PHE A1041    18197  15364  15227    698   2844   -119       C  
ATOM   1826  CZ  PHE A1041     -11.509 -31.991  -3.793  1.00122.10           C  
ANISOU 1826  CZ  PHE A1041    17656  14493  14243    210   2742   -104       C  
ATOM   1827  N   ASP A1042     -12.404 -35.047   2.814  1.00119.07           N  
ANISOU 1827  N   ASP A1042    18211  13141  13889   1483   1395    769       N  
ATOM   1828  CA  ASP A1042     -12.360 -36.108   3.830  1.00121.92           C  
ANISOU 1828  CA  ASP A1042    18924  13196  14205   1903   1259    961       C  
ATOM   1829  C   ASP A1042     -13.560 -37.058   3.793  1.00124.89           C  
ANISOU 1829  C   ASP A1042    20019  12985  14450   1789   1465    951       C  
ATOM   1830  O   ASP A1042     -14.677 -36.641   3.480  1.00120.75           O  
ANISOU 1830  O   ASP A1042    19683  12382  13815   1290   1566    840       O  
ATOM   1831  CB  ASP A1042     -12.156 -35.532   5.257  1.00123.69           C  
ANISOU 1831  CB  ASP A1042    19017  13651  14329   1903    836   1165       C  
ATOM   1832  CG  ASP A1042     -13.114 -34.439   5.721  1.00125.14           C  
ANISOU 1832  CG  ASP A1042    19284  13915  14347   1337    704   1157       C  
ATOM   1833  OD1 ASP A1042     -14.269 -34.422   5.255  1.00122.03           O1-
ANISOU 1833  OD1 ASP A1042    19226  13275  13866    990    910   1053       O1-
ATOM   1834  OD2 ASP A1042     -12.709 -33.617   6.575  1.00128.62           O  
ANISOU 1834  OD2 ASP A1042    19457  14680  14732   1260    385   1241       O  
ATOM   1835  N   ARG A1043     -13.324 -38.335   4.129  1.00125.42           N  
ANISOU 1835  N   ARG A1043    20494  12648  14513   2253   1522   1062       N  
ATOM   1836  CA  ARG A1043     -14.384 -39.343   4.167  1.00125.52           C  
ANISOU 1836  CA  ARG A1043    21252  12052  14386   2109   1738   1058       C  
ATOM   1837  C   ARG A1043     -15.136 -39.296   5.498  1.00127.66           C  
ANISOU 1837  C   ARG A1043    21874  12183  14446   1898   1535   1270       C  
ATOM   1838  O   ARG A1043     -16.314 -39.653   5.552  1.00125.42           O  
ANISOU 1838  O   ARG A1043    22067  11570  14015   1488   1707   1222       O  
ATOM   1839  CB  ARG A1043     -13.815 -40.747   3.913  1.00131.76           C  
ANISOU 1839  CB  ARG A1043    22451  12377  15236   2691   1928   1082       C  
ATOM   1840  N   GLY A1044     -14.449 -38.842   6.546  1.00125.51           N  
ANISOU 1840  N   GLY A1044    21339  12205  14143   2151   1178   1480       N  
ATOM   1841  CA  GLY A1044     -14.981 -38.738   7.901  1.00125.24           C  
ANISOU 1841  CA  GLY A1044    21610  12099  13874   2018    956   1698       C  
ATOM   1842  C   GLY A1044     -16.060 -37.695   8.149  1.00123.43           C  
ANISOU 1842  C   GLY A1044    21303  12081  13512   1381    926   1611       C  
ATOM   1843  O   GLY A1044     -16.978 -37.948   8.939  1.00122.23           O  
ANISOU 1843  O   GLY A1044    21601  11699  13140   1136    955   1709       O  
ATOM   1844  N   GLN A1045     -15.947 -36.500   7.516  1.00116.43           N  
ANISOU 1844  N   GLN A1045    19868  11635  12737   1126    877   1434       N  
ATOM   1845  CA  GLN A1045     -16.918 -35.424   7.733  1.00111.77           C  
ANISOU 1845  CA  GLN A1045    19204  11250  12014    616    829   1345       C  
ATOM   1846  C   GLN A1045     -17.543 -34.821   6.453  1.00111.37           C  
ANISOU 1846  C   GLN A1045    18966  11313  12035    254   1045   1079       C  
ATOM   1847  O   GLN A1045     -18.612 -35.275   6.046  1.00109.92           O  
ANISOU 1847  O   GLN A1045    19084  10908  11775    -11   1278    962       O  
ATOM   1848  CB  GLN A1045     -16.333 -34.312   8.620  1.00112.61           C  
ANISOU 1848  CB  GLN A1045    18960  11763  12063    626    461   1438       C  
ATOM   1849  CG  GLN A1045     -16.717 -34.451  10.095  1.00123.69           C  
ANISOU 1849  CG  GLN A1045    20711  13080  13206    634    268   1639       C  
ATOM   1850  CD  GLN A1045     -15.687 -35.166  10.938  1.00136.48           C  
ANISOU 1850  CD  GLN A1045    22409  14657  14791   1147     25   1883       C  
ATOM   1851  OE1 GLN A1045     -14.794 -35.860  10.442  1.00133.23           O  
ANISOU 1851  OE1 GLN A1045    21881  14187  14555   1566     52   1914       O  
ATOM   1852  NE2 GLN A1045     -15.790 -35.007  12.245  1.00127.81           N  
ANISOU 1852  NE2 GLN A1045    21519  13606  13438   1163   -225   2059       N  
ATOM   1853  N   LYS A1046     -16.899 -33.799   5.843  1.00105.95           N  
ANISOU 1853  N   LYS A1046    17808  10982  11468    216    963    986       N  
ATOM   1854  CA  LYS A1046     -17.382 -33.009   4.689  1.00102.28           C  
ANISOU 1854  CA  LYS A1046    17177  10663  11020    -95   1111    773       C  
ATOM   1855  C   LYS A1046     -17.869 -33.827   3.474  1.00107.59           C  
ANISOU 1855  C   LYS A1046    18043  11105  11730   -146   1437    598       C  
ATOM   1856  O   LYS A1046     -18.532 -33.257   2.605  1.00105.10           O  
ANISOU 1856  O   LYS A1046    17682  10894  11358   -418   1538    427       O  
ATOM   1857  CB  LYS A1046     -16.350 -31.951   4.247  1.00103.22           C  
ANISOU 1857  CB  LYS A1046    16825  11139  11254    -94   1005    741       C  
ATOM   1858  CG  LYS A1046     -15.747 -31.108   5.390  1.00109.92           C  
ANISOU 1858  CG  LYS A1046    17460  12243  12062    -94    666    871       C  
ATOM   1859  CD  LYS A1046     -16.783 -30.370   6.258  1.00110.33           C  
ANISOU 1859  CD  LYS A1046    17738  12286  11895   -359    517    888       C  
ATOM   1860  CE  LYS A1046     -16.458 -30.490   7.729  1.00115.76           C  
ANISOU 1860  CE  LYS A1046    18494  13011  12477   -213    235   1066       C  
ATOM   1861  NZ  LYS A1046     -17.646 -30.237   8.590  1.00118.95           N1+
ANISOU 1861  NZ  LYS A1046    19234  13322  12641   -405    194   1081       N1+
ATOM   1862  N   GLY A1047     -17.589 -35.137   3.471  1.00107.70           N  
ANISOU 1862  N   GLY A1047    18325  10791  11804    120   1580    641       N  
ATOM   1863  CA  GLY A1047     -18.032 -36.121   2.482  1.00108.55           C  
ANISOU 1863  CA  GLY A1047    18733  10589  11920     76   1893    469       C  
ATOM   1864  C   GLY A1047     -17.867 -35.810   1.005  1.00110.51           C  
ANISOU 1864  C   GLY A1047    18777  10984  12229     -4   2081    246       C  
ATOM   1865  O   GLY A1047     -18.847 -35.840   0.250  1.00108.50           O  
ANISOU 1865  O   GLY A1047    18679  10684  11861   -323   2226     53       O  
ATOM   1866  N   VAL A1048     -16.617 -35.557   0.574  1.00107.54           N  
ANISOU 1866  N   VAL A1048    18042  10810  12007    284   2087    262       N  
ATOM   1867  CA  VAL A1048     -16.280 -35.307  -0.826  1.00106.90           C  
ANISOU 1867  CA  VAL A1048    17779  10874  11962    242   2306     69       C  
ATOM   1868  C   VAL A1048     -16.438 -36.611  -1.632  1.00113.51           C  
ANISOU 1868  C   VAL A1048    18996  11335  12799    375   2615    -97       C  
ATOM   1869  O   VAL A1048     -16.858 -36.567  -2.791  1.00112.71           O  
ANISOU 1869  O   VAL A1048    18970  11245  12609    167   2811   -313       O  
ATOM   1870  CB  VAL A1048     -14.879 -34.651  -0.978  1.00112.02           C  
ANISOU 1870  CB  VAL A1048    17900  11896  12764    457   2260    126       C  
ATOM   1871  CG1 VAL A1048     -13.749 -35.589  -0.556  1.00116.45           C  
ANISOU 1871  CG1 VAL A1048    18357  12392  13495   1004   2270    221       C  
ATOM   1872  CG2 VAL A1048     -14.660 -34.125  -2.391  1.00111.48           C  
ANISOU 1872  CG2 VAL A1048    17662  12026  12671    294   2496    -56       C  
ATOM   1873  N   ASP A1049     -16.138 -37.765  -0.979  1.00113.29           N  
ANISOU 1873  N   ASP A1049    19267  10944  12835    721   2643      6       N  
ATOM   1874  CA  ASP A1049     -16.221 -39.128  -1.516  1.00116.50           C  
ANISOU 1874  CA  ASP A1049    20159  10871  13234    901   2929   -127       C  
ATOM   1875  C   ASP A1049     -17.611 -39.467  -2.029  1.00119.41           C  
ANISOU 1875  C   ASP A1049    20950  11000  13419    392   3076   -335       C  
ATOM   1876  O   ASP A1049     -17.729 -40.132  -3.059  1.00121.39           O  
ANISOU 1876  O   ASP A1049    21460  11034  13627    363   3344   -570       O  
ATOM   1877  CB  ASP A1049     -15.718 -40.180  -0.494  1.00122.00           C  
ANISOU 1877  CB  ASP A1049    21183  11181  13991   1375   2874     83       C  
ATOM   1878  CG  ASP A1049     -16.356 -40.194   0.893  1.00126.95           C  
ANISOU 1878  CG  ASP A1049    22057  11669  14510   1221   2641    316       C  
ATOM   1879  OD1 ASP A1049     -16.866 -39.135   1.332  1.00121.58           O1-
ANISOU 1879  OD1 ASP A1049    21095  11335  13763    863   2436    366       O1-
ATOM   1880  OD2 ASP A1049     -16.310 -41.254   1.555  1.00137.23           O  
ANISOU 1880  OD2 ASP A1049    23866  12502  15774   1487   2674    455       O  
ATOM   1881  N   VAL A1050     -18.657 -38.972  -1.333  1.00112.77           N  
ANISOU 1881  N   VAL A1050    20140  10252  12455    -17   2901   -273       N  
ATOM   1882  CA  VAL A1050     -20.067 -39.152  -1.691  1.00111.39           C  
ANISOU 1882  CA  VAL A1050    20232   9995  12095   -549   2992   -477       C  
ATOM   1883  C   VAL A1050     -20.342 -38.449  -3.037  1.00113.25           C  
ANISOU 1883  C   VAL A1050    20219  10562  12248   -765   3053   -724       C  
ATOM   1884  O   VAL A1050     -21.006 -39.033  -3.897  1.00114.52           O  
ANISOU 1884  O   VAL A1050    20649  10580  12285  -1022   3234   -984       O  
ATOM   1885  CB  VAL A1050     -21.038 -38.702  -0.558  1.00112.87           C  
ANISOU 1885  CB  VAL A1050    20413  10302  12171   -870   2797   -351       C  
ATOM   1886  CG1 VAL A1050     -22.476 -39.114  -0.862  1.00113.05           C  
ANISOU 1886  CG1 VAL A1050    20692  10254  12009  -1412   2925   -584       C  
ATOM   1887  CG2 VAL A1050     -20.613 -39.269   0.794  1.00114.70           C  
ANISOU 1887  CG2 VAL A1050    20890  10246  12444   -611   2714    -65       C  
ATOM   1888  N   LEU A1051     -19.768 -37.241  -3.240  1.00106.59           N  
ANISOU 1888  N   LEU A1051    18913  10135  11452   -662   2909   -645       N  
ATOM   1889  CA  LEU A1051     -19.913 -36.485  -4.486  1.00104.57           C  
ANISOU 1889  CA  LEU A1051    18471  10178  11083   -821   2960   -824       C  
ATOM   1890  C   LEU A1051     -19.106 -37.090  -5.645  1.00110.59           C  
ANISOU 1890  C   LEU A1051    19316  10825  11879   -606   3247   -986       C  
ATOM   1891  O   LEU A1051     -19.660 -37.221  -6.738  1.00111.51           O  
ANISOU 1891  O   LEU A1051    19589  10960  11819   -820   3381  -1231       O  
ATOM   1892  CB  LEU A1051     -19.610 -34.985  -4.289  1.00101.53           C  
ANISOU 1892  CB  LEU A1051    17675  10202  10701   -834   2742   -675       C  
ATOM   1893  CG  LEU A1051     -19.732 -34.034  -5.505  1.00104.98           C  
ANISOU 1893  CG  LEU A1051    17982  10930  10978   -984   2773   -799       C  
ATOM   1894  CD1 LEU A1051     -21.053 -34.205  -6.259  1.00104.71           C  
ANISOU 1894  CD1 LEU A1051    18164  10924  10696  -1283   2790  -1037       C  
ATOM   1895  CD2 LEU A1051     -19.600 -32.598  -5.070  1.00105.54           C  
ANISOU 1895  CD2 LEU A1051    17786  11287  11028  -1039   2544   -631       C  
ATOM   1896  N   LEU A1052     -17.822 -37.463  -5.418  1.00107.63           N  
ANISOU 1896  N   LEU A1052    18823  10366  11705   -166   3337   -870       N  
ATOM   1897  CA  LEU A1052     -16.978 -38.076  -6.456  1.00110.16           C  
ANISOU 1897  CA  LEU A1052    19195  10597  12064    114   3647  -1034       C  
ATOM   1898  C   LEU A1052     -17.576 -39.395  -6.966  1.00115.48           C  
ANISOU 1898  C   LEU A1052    20445  10797  12634     54   3881  -1274       C  
ATOM   1899  O   LEU A1052     -17.536 -39.652  -8.171  1.00116.66           O  
ANISOU 1899  O   LEU A1052    20732  10931  12664     17   4121  -1524       O  
ATOM   1900  CB  LEU A1052     -15.537 -38.297  -5.964  1.00113.00           C  
ANISOU 1900  CB  LEU A1052    19269  11002  12666    656   3676   -871       C  
ATOM   1901  CG  LEU A1052     -14.660 -37.061  -5.766  1.00115.73           C  
ANISOU 1901  CG  LEU A1052    19001  11859  13113    695   3532   -713       C  
ATOM   1902  CD1 LEU A1052     -13.338 -37.435  -5.115  1.00119.52           C  
ANISOU 1902  CD1 LEU A1052    19165  12421  13826   1234   3509   -569       C  
ATOM   1903  CD2 LEU A1052     -14.399 -36.352  -7.077  1.00117.01           C  
ANISOU 1903  CD2 LEU A1052    18969  12326  13165    515   3740   -872       C  
ATOM   1904  N   LYS A1053     -18.156 -40.207  -6.049  1.00111.70           N  
ANISOU 1904  N   LYS A1053    20347   9926  12170     -3   3820  -1204       N  
ATOM   1905  CA  LYS A1053     -18.826 -41.467  -6.370  1.00114.32           C  
ANISOU 1905  CA  LYS A1053    21304   9744  12387   -169   4034  -1424       C  
ATOM   1906  C   LYS A1053     -20.120 -41.185  -7.139  1.00115.51           C  
ANISOU 1906  C   LYS A1053    21533  10066  12290   -778   4021  -1690       C  
ATOM   1907  O   LYS A1053     -20.429 -41.914  -8.073  1.00118.04           O  
ANISOU 1907  O   LYS A1053    22220  10161  12469   -935   4241  -1988       O  
ATOM   1908  CB  LYS A1053     -19.101 -42.301  -5.102  1.00118.48           C  
ANISOU 1908  CB  LYS A1053    22235   9816  12967   -128   3978  -1238       C  
ATOM   1909  CG  LYS A1053     -19.455 -43.766  -5.383  1.00139.21           C  
ANISOU 1909  CG  LYS A1053    25616  11773  15504   -199   4261  -1436       C  
ATOM   1910  CD  LYS A1053     -19.310 -44.656  -4.143  1.00151.55           C  
ANISOU 1910  CD  LYS A1053    27652  12802  17129     36   4250  -1184       C  
ATOM   1911  CE  LYS A1053     -19.705 -46.097  -4.388  1.00165.92           C  
ANISOU 1911  CE  LYS A1053    30334  13873  18837    -90   4550  -1373       C  
ATOM   1912  NZ  LYS A1053     -21.180 -46.282  -4.410  1.00173.01           N1+
ANISOU 1912  NZ  LYS A1053    31508  14699  19528   -925   4588  -1568       N1+
ATOM   1913  N   ALA A1054     -20.852 -40.117  -6.769  1.00107.74           N  
ANISOU 1913  N   ALA A1054    20199   9502  11234  -1089   3752  -1600       N  
ATOM   1914  CA  ALA A1054     -22.091 -39.713  -7.439  1.00106.07           C  
ANISOU 1914  CA  ALA A1054    19958   9568  10776  -1591   3673  -1835       C  
ATOM   1915  C   ALA A1054     -21.817 -39.227  -8.867  1.00110.34           C  
ANISOU 1915  C   ALA A1054    20378  10379  11168  -1562   3761  -2027       C  
ATOM   1916  O   ALA A1054     -22.635 -39.476  -9.751  1.00111.23           O  
ANISOU 1916  O   ALA A1054    20671  10549  11043  -1893   3805  -2321       O  
ATOM   1917  CB  ALA A1054     -22.802 -38.632  -6.638  1.00102.56           C  
ANISOU 1917  CB  ALA A1054    19153   9514  10301  -1783   3367  -1668       C  
ATOM   1918  N   ILE A1055     -20.662 -38.552  -9.091  1.00106.20           N  
ANISOU 1918  N   ILE A1055    19554  10039  10759  -1195   3793  -1870       N  
ATOM   1919  CA  ILE A1055     -20.231 -38.069 -10.414  1.00106.70           C  
ANISOU 1919  CA  ILE A1055    19528  10345  10668  -1148   3930  -2012       C  
ATOM   1920  C   ILE A1055     -19.898 -39.286 -11.301  1.00115.94           C  
ANISOU 1920  C   ILE A1055    21108  11166  11777  -1040   4275  -2292       C  
ATOM   1921  O   ILE A1055     -20.263 -39.294 -12.473  1.00117.22           O  
ANISOU 1921  O   ILE A1055    21429  11436  11674  -1230   4376  -2552       O  
ATOM   1922  CB  ILE A1055     -19.074 -37.025 -10.312  1.00107.89           C  
ANISOU 1922  CB  ILE A1055    19241  10792  10959   -866   3909  -1766       C  
ATOM   1923  CG1 ILE A1055     -19.567 -35.711  -9.650  1.00103.89           C  
ANISOU 1923  CG1 ILE A1055    18437  10610  10427  -1044   3572  -1553       C  
ATOM   1924  CG2 ILE A1055     -18.442 -36.731 -11.683  1.00109.42           C  
ANISOU 1924  CG2 ILE A1055    19408  11171  10994   -801   4157  -1909       C  
ATOM   1925  CD1 ILE A1055     -18.470 -34.845  -9.022  1.00106.53           C  
ANISOU 1925  CD1 ILE A1055    18379  11132  10965   -830   3499  -1278       C  
ATOM   1926  N   GLU A1056     -19.270 -40.335 -10.715  1.00115.42           N  
ANISOU 1926  N   GLU A1056    21270  10660  11925   -723   4440  -2247       N  
ATOM   1927  CA  GLU A1056     -18.931 -41.594 -11.392  1.00120.25           C  
ANISOU 1927  CA  GLU A1056    22364  10830  12497   -549   4781  -2508       C  
ATOM   1928  C   GLU A1056     -20.203 -42.330 -11.856  1.00125.27           C  
ANISOU 1928  C   GLU A1056    23500  11220  12878  -1066   4810  -2832       C  
ATOM   1929  O   GLU A1056     -20.178 -43.045 -12.861  1.00128.83           O  
ANISOU 1929  O   GLU A1056    24338  11453  13157  -1097   5067  -3150       O  
ATOM   1930  CB  GLU A1056     -18.079 -42.496 -10.481  1.00124.63           C  
ANISOU 1930  CB  GLU A1056    23090  10939  13323    -46   4888  -2340       C  
ATOM   1931  CG  GLU A1056     -16.628 -42.058 -10.354  1.00135.66           C  
ANISOU 1931  CG  GLU A1056    24010  12592  14943    532   4949  -2143       C  
ATOM   1932  CD  GLU A1056     -15.652 -43.187 -10.078  1.00161.81           C  
ANISOU 1932  CD  GLU A1056    27574  15472  18433   1165   5174  -2131       C  
ATOM   1933  OE1 GLU A1056     -15.619 -43.681  -8.927  1.00162.45           O1-
ANISOU 1933  OE1 GLU A1056    27821  15243  18658   1370   5033  -1913       O1-
ATOM   1934  OE2 GLU A1056     -14.918 -43.577 -11.015  1.00154.63           O  
ANISOU 1934  OE2 GLU A1056    26718  14538  17495   1492   5496  -2338       O  
ATOM   1935  N   ILE A1057     -21.310 -42.129 -11.124  1.00118.83           N  
ANISOU 1935  N   ILE A1057    22649  10480  12023  -1492   4554  -2771       N  
ATOM   1936  CA  ILE A1057     -22.637 -42.664 -11.422  1.00120.16           C  
ANISOU 1936  CA  ILE A1057    23141  10563  11952  -2086   4526  -3071       C  
ATOM   1937  C   ILE A1057     -23.262 -41.798 -12.546  1.00123.15           C  
ANISOU 1937  C   ILE A1057    23264  11500  12028  -2369   4383  -3276       C  
ATOM   1938  O   ILE A1057     -23.908 -42.344 -13.448  1.00126.45           O  
ANISOU 1938  O   ILE A1057    23988  11878  12180  -2716   4463  -3643       O  
ATOM   1939  CB  ILE A1057     -23.499 -42.714 -10.118  1.00121.46           C  
ANISOU 1939  CB  ILE A1057    23274  10678  12199  -2397   4330  -2903       C  
ATOM   1940  CG1 ILE A1057     -22.934 -43.751  -9.117  1.00124.21           C  
ANISOU 1940  CG1 ILE A1057    24047  10383  12762  -2132   4495  -2722       C  
ATOM   1941  CG2 ILE A1057     -24.995 -42.970 -10.401  1.00123.70           C  
ANISOU 1941  CG2 ILE A1057    23673  11104  12222  -3099   4248  -3216       C  
ATOM   1942  CD1 ILE A1057     -23.224 -43.452  -7.652  1.00127.57           C  
ANISOU 1942  CD1 ILE A1057    24305  10841  13324  -2177   4292  -2392       C  
ATOM   1943  N   LEU A1058     -23.031 -40.458 -12.498  1.00115.06           N  
ANISOU 1943  N   LEU A1058    21726  10970  11020  -2206   4170  -3040       N  
ATOM   1944  CA  LEU A1058     -23.521 -39.469 -13.473  1.00113.44           C  
ANISOU 1944  CA  LEU A1058    21299  11287  10516  -2364   4002  -3145       C  
ATOM   1945  C   LEU A1058     -22.813 -39.535 -14.850  1.00121.37           C  
ANISOU 1945  C   LEU A1058    22479  12314  11324  -2197   4251  -3330       C  
ATOM   1946  O   LEU A1058     -23.456 -39.264 -15.870  1.00122.74           O  
ANISOU 1946  O   LEU A1058    22722  12774  11141  -2433   4169  -3560       O  
ATOM   1947  CB  LEU A1058     -23.441 -38.035 -12.897  1.00108.38           C  
ANISOU 1947  CB  LEU A1058    20173  11054   9953  -2222   3726  -2808       C  
ATOM   1948  CG  LEU A1058     -24.511 -37.640 -11.877  1.00109.74           C  
ANISOU 1948  CG  LEU A1058    20127  11415  10153  -2462   3422  -2709       C  
ATOM   1949  CD1 LEU A1058     -23.968 -36.641 -10.882  1.00105.92           C  
ANISOU 1949  CD1 LEU A1058    19303  11052   9891  -2197   3266  -2331       C  
ATOM   1950  CD2 LEU A1058     -25.760 -37.097 -12.557  1.00111.05           C  
ANISOU 1950  CD2 LEU A1058    20181  12040   9973  -2766   3176  -2919       C  
ATOM   1951  N   SER A1059     -21.497 -39.871 -14.876  1.00118.98           N  
ANISOU 1951  N   SER A1059    22225  11756  11226  -1770   4549  -3235       N  
ATOM   1952  CA  SER A1059     -20.673 -39.983 -16.090  1.00121.70           C  
ANISOU 1952  CA  SER A1059    22711  12119  11410  -1560   4862  -3402       C  
ATOM   1953  C   SER A1059     -21.235 -41.038 -17.054  1.00130.17           C  
ANISOU 1953  C   SER A1059    24322  12947  12189  -1811   5038  -3847       C  
ATOM   1954  O   SER A1059     -21.272 -40.815 -18.266  1.00130.95           O  
ANISOU 1954  O   SER A1059    24544  13265  11946  -1892   5127  -4058       O  
ATOM   1955  CB  SER A1059     -19.226 -40.296 -15.725  1.00126.25           C  
ANISOU 1955  CB  SER A1059    23177  12484  12307  -1034   5146  -3238       C  
ATOM   1956  OG  SER A1059     -19.112 -41.524 -15.026  1.00136.52           O  
ANISOU 1956  OG  SER A1059    24800  13248  13823   -875   5267  -3284       O  
ATOM   1957  N   SER A1060     -21.739 -42.151 -16.491  1.00129.72           N  
ANISOU 1957  N   SER A1060    24622  12435  12230  -1986   5071  -3990       N  
ATOM   1958  CA  SER A1060     -22.374 -43.254 -17.210  1.00134.88           C  
ANISOU 1958  CA  SER A1060    25849  12774  12626  -2326   5221  -4433       C  
ATOM   1959  C   SER A1060     -23.719 -42.831 -17.833  1.00139.55           C  
ANISOU 1959  C   SER A1060    26378  13813  12833  -2899   4919  -4673       C  
ATOM   1960  O   SER A1060     -24.258 -43.566 -18.665  1.00143.64           O  
ANISOU 1960  O   SER A1060    27316  14212  13049  -3237   5006  -5088       O  
ATOM   1961  CB  SER A1060     -22.576 -44.444 -16.275  1.00140.48           C  
ANISOU 1961  CB  SER A1060    26968  12857  13553  -2413   5322  -4461       C  
ATOM   1962  OG  SER A1060     -23.026 -45.582 -16.989  1.00154.38           O  
ANISOU 1962  OG  SER A1060    29373  14213  15072  -2735   5530  -4907       O  
ATOM   1963  N   LYS A1061     -24.254 -41.656 -17.427  1.00131.98           N  
ANISOU 1963  N   LYS A1061    24901  13376  11868  -2984   4554  -4428       N  
ATOM   1964  CA  LYS A1061     -25.514 -41.109 -17.931  1.00131.72           C  
ANISOU 1964  CA  LYS A1061    24703  13865  11480  -3407   4209  -4610       C  
ATOM   1965  C   LYS A1061     -25.302 -40.090 -19.063  1.00136.17           C  
ANISOU 1965  C   LYS A1061    25139  14895  11704  -3240   4125  -4595       C  
ATOM   1966  O   LYS A1061     -24.232 -39.478 -19.166  1.00133.90           O  
ANISOU 1966  O   LYS A1061    24732  14617  11527  -2833   4280  -4333       O  
ATOM   1967  CB  LYS A1061     -26.361 -40.516 -16.792  1.00129.78           C  
ANISOU 1967  CB  LYS A1061    24028  13892  11392  -3578   3866  -4390       C  
ATOM   1968  N   LYS A1062     -26.337 -39.938 -19.922  1.00135.39           N  
ANISOU 1968  N   LYS A1062    25080  15197  11164  -3580   3881  -4887       N  
ATOM   1969  CA  LYS A1062     -26.380 -39.031 -21.074  1.00135.63           C  
ANISOU 1969  CA  LYS A1062    25087  15688  10760  -3477   3744  -4906       C  
ATOM   1970  C   LYS A1062     -26.583 -37.554 -20.680  1.00134.43           C  
ANISOU 1970  C   LYS A1062    24490  15974  10612  -3263   3406  -4521       C  
ATOM   1971  O   LYS A1062     -26.352 -36.672 -21.510  1.00133.62           O  
ANISOU 1971  O   LYS A1062    24421  16151  10196  -3078   3347  -4419       O  
ATOM   1972  CB  LYS A1062     -27.471 -39.482 -22.063  1.00142.76           C  
ANISOU 1972  CB  LYS A1062    26202  16875  11165  -3906   3552  -5376       C  
ATOM   1973  N   GLU A1063     -27.009 -37.290 -19.419  1.00127.48           N  
ANISOU 1973  N   GLU A1063    23255  15121  10060  -3288   3206  -4309       N  
ATOM   1974  CA  GLU A1063     -27.254 -35.940 -18.882  1.00123.16           C  
ANISOU 1974  CA  GLU A1063    22324  14923   9547  -3077   2892  -3963       C  
ATOM   1975  C   GLU A1063     -26.007 -35.277 -18.290  1.00124.61           C  
ANISOU 1975  C   GLU A1063    22403  14880  10063  -2707   3077  -3546       C  
ATOM   1976  O   GLU A1063     -26.101 -34.153 -17.807  1.00121.29           O  
ANISOU 1976  O   GLU A1063    21735  14667   9683  -2541   2852  -3257       O  
ATOM   1977  CB  GLU A1063     -28.388 -35.954 -17.844  1.00122.78           C  
ANISOU 1977  CB  GLU A1063    21938  15073   9639  -3297   2596  -3981       C  
ATOM   1978  CG  GLU A1063     -29.759 -36.243 -18.431  1.00133.33           C  
ANISOU 1978  CG  GLU A1063    23210  16854  10597  -3663   2312  -4370       C  
ATOM   1979  CD  GLU A1063     -30.339 -37.611 -18.122  1.00144.29           C  
ANISOU 1979  CD  GLU A1063    24708  18040  12077  -4170   2436  -4722       C  
ATOM   1980  OE1 GLU A1063     -29.563 -38.591 -18.032  1.00141.64           O  
ANISOU 1980  OE1 GLU A1063    24741  17126  11949  -4222   2810  -4776       O  
ATOM   1981  OE2 GLU A1063     -31.579 -37.703 -17.981  1.00127.20           O1-
ANISOU 1981  OE2 GLU A1063    22269  16299   9761  -4517   2165  -4955       O1-
ATOM   1982  N   PHE A1064     -24.848 -35.964 -18.330  1.00123.33           N  
ANISOU 1982  N   PHE A1064    22422  14312  10125  -2574   3479  -3536       N  
ATOM   1983  CA  PHE A1064     -23.563 -35.478 -17.810  1.00121.37           C  
ANISOU 1983  CA  PHE A1064    22020  13896  10198  -2251   3682  -3194       C  
ATOM   1984  C   PHE A1064     -23.020 -34.261 -18.582  1.00125.55           C  
ANISOU 1984  C   PHE A1064    22537  14682  10482  -2094   3699  -3002       C  
ATOM   1985  O   PHE A1064     -22.361 -33.399 -17.985  1.00122.25           O  
ANISOU 1985  O   PHE A1064    21893  14282  10273  -1933   3692  -2676       O  
ATOM   1986  CB  PHE A1064     -22.530 -36.621 -17.786  1.00125.70           C  
ANISOU 1986  CB  PHE A1064    22751  14013  10998  -2105   4104  -3294       C  
ATOM   1987  CG  PHE A1064     -21.294 -36.315 -16.978  1.00125.73           C  
ANISOU 1987  CG  PHE A1064    22487  13885  11400  -1782   4261  -2970       C  
ATOM   1988  CD1 PHE A1064     -21.310 -36.402 -15.592  1.00126.15           C  
ANISOU 1988  CD1 PHE A1064    22321  13788  11820  -1723   4117  -2762       C  
ATOM   1989  CD2 PHE A1064     -20.116 -35.923 -17.601  1.00129.73           C  
ANISOU 1989  CD2 PHE A1064    22939  14464  11889  -1560   4553  -2884       C  
ATOM   1990  CE1 PHE A1064     -20.169 -36.097 -14.843  1.00125.85           C  
ANISOU 1990  CE1 PHE A1064    22007  13692  12120  -1429   4213  -2480       C  
ATOM   1991  CE2 PHE A1064     -18.976 -35.615 -16.850  1.00131.46           C  
ANISOU 1991  CE2 PHE A1064    22829  14651  12469  -1299   4673  -2613       C  
ATOM   1992  CZ  PHE A1064     -19.009 -35.708 -15.476  1.00126.67           C  
ANISOU 1992  CZ  PHE A1064    21999  13910  12219  -1226   4480  -2417       C  
ATOM   1993  N   GLN A1065     -23.301 -34.206 -19.905  1.00125.87           N  
ANISOU 1993  N   GLN A1065    22864  14910  10052  -2176   3727  -3210       N  
ATOM   1994  CA  GLN A1065     -22.898 -33.149 -20.847  1.00126.85           C  
ANISOU 1994  CA  GLN A1065    23121  15257   9820  -2077   3772  -3061       C  
ATOM   1995  C   GLN A1065     -23.558 -31.806 -20.501  1.00128.49           C  
ANISOU 1995  C   GLN A1065    23192  15730   9900  -2026   3363  -2790       C  
ATOM   1996  O   GLN A1065     -22.941 -30.756 -20.680  1.00127.93           O  
ANISOU 1996  O   GLN A1065    23162  15699   9746  -1914   3427  -2511       O  
ATOM   1997  CB  GLN A1065     -23.256 -33.545 -22.289  1.00132.84           C  
ANISOU 1997  CB  GLN A1065    24274  16157  10044  -2192   3841  -3386       C  
ATOM   1998  CG  GLN A1065     -22.814 -34.950 -22.693  1.00155.79           C  
ANISOU 1998  CG  GLN A1065    27406  18775  13010  -2250   4220  -3731       C  
ATOM   1999  CD  GLN A1065     -23.599 -35.461 -23.878  1.00184.86           C  
ANISOU 1999  CD  GLN A1065    31462  22617  16158  -2461   4142  -4129       C  
ATOM   2000  OE1 GLN A1065     -23.345 -35.102 -25.033  1.00183.58           O  
ANISOU 2000  OE1 GLN A1065    31585  22623  15543  -2427   4265  -4181       O  
ATOM   2001  NE2 GLN A1065     -24.571 -36.318 -23.620  1.00180.55           N  
ANISOU 2001  NE2 GLN A1065    30938  22034  15627  -2722   3942  -4428       N  
ATOM   2002  N   GLU A1066     -24.811 -31.847 -20.009  1.00123.72           N  
ANISOU 2002  N   GLU A1066    22440  15302   9267  -2114   2967  -2886       N  
ATOM   2003  CA  GLU A1066     -25.593 -30.681 -19.582  1.00121.25           C  
ANISOU 2003  CA  GLU A1066    21977  15249   8843  -2000   2554  -2677       C  
ATOM   2004  C   GLU A1066     -25.052 -30.115 -18.268  1.00119.46           C  
ANISOU 2004  C   GLU A1066    21484  14836   9070  -1886   2560  -2351       C  
ATOM   2005  O   GLU A1066     -25.309 -28.950 -17.952  1.00118.13           O  
ANISOU 2005  O   GLU A1066    21280  14780   8822  -1738   2321  -2113       O  
ATOM   2006  CB  GLU A1066     -27.056 -31.089 -19.351  1.00123.52           C  
ANISOU 2006  CB  GLU A1066    22084  15828   9020  -2140   2184  -2935       C  
ATOM   2007  CG  GLU A1066     -27.947 -31.083 -20.578  1.00140.33           C  
ANISOU 2007  CG  GLU A1066    24399  18342  10577  -2195   1948  -3200       C  
ATOM   2008  CD  GLU A1066     -29.330 -31.645 -20.306  1.00161.87           C  
ANISOU 2008  CD  GLU A1066    26850  21413  13239  -2412   1621  -3514       C  
ATOM   2009  OE1 GLU A1066     -29.588 -32.800 -20.719  1.00156.85           O1-
ANISOU 2009  OE1 GLU A1066    26304  20755  12537  -2735   1730  -3882       O1-
ATOM   2010  OE2 GLU A1066     -30.150 -30.942 -19.669  1.00152.27           O  
ANISOU 2010  OE2 GLU A1066    25330  20493  12035  -2276   1276  -3411       O  
ATOM   2011  N   MET A1067     -24.341 -30.951 -17.488  1.00113.03           N  
ANISOU 2011  N   MET A1067    20516  13727   8702  -1934   2812  -2352       N  
ATOM   2012  CA  MET A1067     -23.815 -30.593 -16.172  1.00108.88           C  
ANISOU 2012  CA  MET A1067    19725  13040   8606  -1845   2803  -2081       C  
ATOM   2013  C   MET A1067     -22.362 -30.141 -16.155  1.00110.84           C  
ANISOU 2013  C   MET A1067    19948  13133   9034  -1743   3096  -1848       C  
ATOM   2014  O   MET A1067     -21.522 -30.701 -16.863  1.00112.18           O  
ANISOU 2014  O   MET A1067    20221  13211   9192  -1736   3442  -1946       O  
ATOM   2015  CB  MET A1067     -23.986 -31.754 -15.181  1.00110.19           C  
ANISOU 2015  CB  MET A1067    19734  13003   9132  -1934   2846  -2194       C  
ATOM   2016  CG  MET A1067     -25.412 -32.106 -14.888  1.00113.85           C  
ANISOU 2016  CG  MET A1067    20123  13648   9487  -2111   2567  -2393       C  
ATOM   2017  SD  MET A1067     -25.536 -33.793 -14.266  1.00119.08           S  
ANISOU 2017  SD  MET A1067    20833  13982  10428  -2331   2761  -2618       S  
ATOM   2018  CE  MET A1067     -27.291 -33.985 -14.258  1.00117.40           C  
ANISOU 2018  CE  MET A1067    20506  14135   9965  -2647   2443  -2898       C  
ATOM   2019  N   ARG A1068     -22.072 -29.158 -15.277  1.00103.46           N  
ANISOU 2019  N   ARG A1068    18848  12187   8275  -1679   2963  -1563       N  
ATOM   2020  CA  ARG A1068     -20.742 -28.609 -15.004  1.00102.13           C  
ANISOU 2020  CA  ARG A1068    18561  11925   8317  -1653   3182  -1334       C  
ATOM   2021  C   ARG A1068     -20.500 -28.785 -13.500  1.00102.57           C  
ANISOU 2021  C   ARG A1068    18301  11864   8807  -1604   3073  -1207       C  
ATOM   2022  O   ARG A1068     -21.423 -28.568 -12.716  1.00100.45           O  
ANISOU 2022  O   ARG A1068    17981  11623   8562  -1598   2770  -1179       O  
ATOM   2023  CB  ARG A1068     -20.647 -27.117 -15.395  1.00101.29           C  
ANISOU 2023  CB  ARG A1068    18649  11900   7938  -1684   3099  -1112       C  
ATOM   2024  CG  ARG A1068     -21.465 -26.677 -16.611  1.00104.26           C  
ANISOU 2024  CG  ARG A1068    19410  12420   7783  -1669   2987  -1186       C  
ATOM   2025  CD  ARG A1068     -20.903 -27.172 -17.921  1.00101.30           C  
ANISOU 2025  CD  ARG A1068    19247  12080   7162  -1734   3336  -1331       C  
ATOM   2026  NE  ARG A1068     -21.970 -27.289 -18.910  1.00103.35           N  
ANISOU 2026  NE  ARG A1068    19806  12511   6950  -1702   3149  -1515       N  
ATOM   2027  CZ  ARG A1068     -21.778 -27.531 -20.202  1.00113.00           C  
ANISOU 2027  CZ  ARG A1068    21333  13808   7796  -1747   3365  -1650       C  
ATOM   2028  NH1 ARG A1068     -20.549 -27.674 -20.683  1.00 99.42           N1+
ANISOU 2028  NH1 ARG A1068    19648  12006   6122  -1822   3822  -1623       N1+
ATOM   2029  NH2 ARG A1068     -22.814 -27.626 -21.025  1.00 96.90           N  
ANISOU 2029  NH2 ARG A1068    19543  11968   5307  -1713   3125  -1828       N  
ATOM   2030  N   PHE A1069     -19.281 -29.207 -13.098  1.00 98.85           N  
ANISOU 2030  N   PHE A1069    17605  11298   8657  -1546   3315  -1144       N  
ATOM   2031  CA  PHE A1069     -18.918 -29.467 -11.691  1.00 96.04           C  
ANISOU 2031  CA  PHE A1069    16961  10842   8685  -1463   3210  -1021       C  
ATOM   2032  C   PHE A1069     -17.619 -28.739 -11.256  1.00100.34           C  
ANISOU 2032  C   PHE A1069    17237  11459   9431  -1470   3304   -815       C  
ATOM   2033  O   PHE A1069     -16.581 -28.913 -11.898  1.00103.22           O  
ANISOU 2033  O   PHE A1069    17492  11895   9832  -1451   3619   -847       O  
ATOM   2034  CB  PHE A1069     -18.805 -30.988 -11.442  1.00 98.23           C  
ANISOU 2034  CB  PHE A1069    17215  10935   9174  -1330   3355  -1179       C  
ATOM   2035  CG  PHE A1069     -20.096 -31.769 -11.575  1.00 98.92           C  
ANISOU 2035  CG  PHE A1069    17534  10934   9116  -1419   3244  -1389       C  
ATOM   2036  CD1 PHE A1069     -20.469 -32.325 -12.792  1.00104.02           C  
ANISOU 2036  CD1 PHE A1069    18438  11584   9502  -1493   3399  -1644       C  
ATOM   2037  CD2 PHE A1069     -20.913 -31.985 -10.473  1.00 98.56           C  
ANISOU 2037  CD2 PHE A1069    17445  10822   9180  -1468   3004  -1353       C  
ATOM   2038  CE1 PHE A1069     -21.650 -33.065 -12.907  1.00105.17           C  
ANISOU 2038  CE1 PHE A1069    18766  11687   9508  -1650   3291  -1873       C  
ATOM   2039  CE2 PHE A1069     -22.098 -32.720 -10.592  1.00101.72           C  
ANISOU 2039  CE2 PHE A1069    18016  11189   9446  -1631   2933  -1570       C  
ATOM   2040  CZ  PHE A1069     -22.456 -33.257 -11.807  1.00102.37           C  
ANISOU 2040  CZ  PHE A1069    18325  11291   9281  -1737   3067  -1836       C  
ATOM   2041  N   ILE A1070     -17.684 -27.922 -10.176  1.00 93.28           N  
ANISOU 2041  N   ILE A1070    16222  10573   8646  -1520   3042   -630       N  
ATOM   2042  CA  ILE A1070     -16.532 -27.170  -9.646  1.00 93.27           C  
ANISOU 2042  CA  ILE A1070    15955  10662   8819  -1604   3075   -459       C  
ATOM   2043  C   ILE A1070     -16.212 -27.619  -8.209  1.00 95.97           C  
ANISOU 2043  C   ILE A1070    16003  10972   9488  -1472   2898   -378       C  
ATOM   2044  O   ILE A1070     -16.735 -27.046  -7.253  1.00 93.06           O  
ANISOU 2044  O   ILE A1070    15669  10564   9127  -1519   2609   -275       O  
ATOM   2045  CB  ILE A1070     -16.717 -25.623  -9.742  1.00 95.64           C  
ANISOU 2045  CB  ILE A1070    16461  10982   8895  -1829   2944   -312       C  
ATOM   2046  CG1 ILE A1070     -17.320 -25.184 -11.099  1.00 96.83           C  
ANISOU 2046  CG1 ILE A1070    17018  11128   8642  -1893   3037   -366       C  
ATOM   2047  CG2 ILE A1070     -15.402 -24.882  -9.420  1.00 98.13           C  
ANISOU 2047  CG2 ILE A1070    16517  11407   9359  -2032   3054   -182       C  
ATOM   2048  CD1 ILE A1070     -17.757 -23.722 -11.156  1.00105.31           C  
ANISOU 2048  CD1 ILE A1070    18434  12134   9445  -2021   2859   -212       C  
ATOM   2049  N   ILE A1071     -15.351 -28.632  -8.063  1.00 94.87           N  
ANISOU 2049  N   ILE A1071    15605  10852   9590  -1270   3068   -424       N  
ATOM   2050  CA  ILE A1071     -14.959 -29.176  -6.756  1.00 94.59           C  
ANISOU 2050  CA  ILE A1071    15322  10786   9830  -1076   2900   -335       C  
ATOM   2051  C   ILE A1071     -13.726 -28.427  -6.195  1.00103.83           C  
ANISOU 2051  C   ILE A1071    16079  12209  11164  -1153   2855   -206       C  
ATOM   2052  O   ILE A1071     -12.812 -28.103  -6.952  1.00106.15           O  
ANISOU 2052  O   ILE A1071    16164  12708  11459  -1253   3106   -240       O  
ATOM   2053  CB  ILE A1071     -14.776 -30.718  -6.836  1.00 98.55           C  
ANISOU 2053  CB  ILE A1071    15840  11129  10476   -747   3069   -447       C  
ATOM   2054  CG1 ILE A1071     -15.999 -31.390  -7.490  1.00 96.93           C  
ANISOU 2054  CG1 ILE A1071    16060  10694  10077   -792   3130   -617       C  
ATOM   2055  CG2 ILE A1071     -14.520 -31.322  -5.468  1.00 98.91           C  
ANISOU 2055  CG2 ILE A1071    15749  11089  10745   -505   2865   -325       C  
ATOM   2056  CD1 ILE A1071     -15.685 -32.170  -8.690  1.00103.77           C  
ANISOU 2056  CD1 ILE A1071    17041  11508  10881   -685   3473   -814       C  
ATOM   2057  N   ILE A1072     -13.727 -28.117  -4.878  1.00102.11           N  
ANISOU 2057  N   ILE A1072    15744  12001  11051  -1153   2542    -75       N  
ATOM   2058  CA  ILE A1072     -12.644 -27.388  -4.194  1.00105.13           C  
ANISOU 2058  CA  ILE A1072    15733  12646  11566  -1278   2427     24       C  
ATOM   2059  C   ILE A1072     -12.281 -28.049  -2.841  1.00111.96           C  
ANISOU 2059  C   ILE A1072    16365  13545  12630   -995   2172    112       C  
ATOM   2060  O   ILE A1072     -13.177 -28.433  -2.086  1.00109.39           O  
ANISOU 2060  O   ILE A1072    16310  12991  12262   -883   1974    162       O  
ATOM   2061  CB  ILE A1072     -12.970 -25.861  -4.051  1.00106.94           C  
ANISOU 2061  CB  ILE A1072    16148  12871  11613  -1686   2274     95       C  
ATOM   2062  CG1 ILE A1072     -13.114 -25.151  -5.415  1.00107.55           C  
ANISOU 2062  CG1 ILE A1072    16475  12925  11463  -1942   2534     46       C  
ATOM   2063  CG2 ILE A1072     -11.961 -25.117  -3.165  1.00110.61           C  
ANISOU 2063  CG2 ILE A1072    16253  13577  12196  -1888   2104    172       C  
ATOM   2064  CD1 ILE A1072     -14.499 -24.613  -5.691  1.00108.29           C  
ANISOU 2064  CD1 ILE A1072    17092  12772  11282  -1995   2410     51       C  
ATOM   2065  N   GLY A1073     -10.974 -28.157  -2.565  1.00113.46           N  
ANISOU 2065  N   GLY A1073    16047  14055  13009   -887   2183    128       N  
ATOM   2066  CA  GLY A1073     -10.425 -28.724  -1.335  1.00115.50           C  
ANISOU 2066  CA  GLY A1073    16032  14424  13428   -574   1916    222       C  
ATOM   2067  C   GLY A1073      -9.056 -29.365  -1.482  1.00125.96           C  
ANISOU 2067  C   GLY A1073    16794  16100  14965   -242   2041    180       C  
ATOM   2068  O   GLY A1073      -8.693 -29.834  -2.564  1.00128.21           O  
ANISOU 2068  O   GLY A1073    16988  16434  15291   -113   2397     59       O  
ATOM   2069  N   LYS A1074      -8.288 -29.396  -0.379  1.00125.33           N  
ANISOU 2069  N   LYS A1074    16322  16299  14998    -71   1738    266       N  
ATOM   2070  CA  LYS A1074      -6.945 -29.979  -0.326  1.00131.04           C  
ANISOU 2070  CA  LYS A1074    16413  17453  15921    323   1773    230       C  
ATOM   2071  C   LYS A1074      -6.776 -30.810   0.964  1.00136.84           C  
ANISOU 2071  C   LYS A1074    17120  18158  16713    848   1405    374       C  
ATOM   2072  O   LYS A1074      -5.748 -30.713   1.643  1.00141.25           O  
ANISOU 2072  O   LYS A1074    17112  19187  17368   1010   1162    401       O  
ATOM   2073  CB  LYS A1074      -5.889 -28.862  -0.411  1.00136.78           C  
ANISOU 2073  CB  LYS A1074    16516  18756  16698   -116   1766    161       C  
ATOM   2074  N   GLY A1075      -7.783 -31.629   1.272  1.00129.97           N  
ANISOU 2074  N   GLY A1075    16868  16754  15760   1094   1370    462       N  
ATOM   2075  CA  GLY A1075      -7.825 -32.430   2.491  1.00130.94           C  
ANISOU 2075  CA  GLY A1075    17160  16724  15866   1551   1050    635       C  
ATOM   2076  C   GLY A1075      -7.074 -33.745   2.513  1.00138.64           C  
ANISOU 2076  C   GLY A1075    18013  17692  16972   2305   1104    664       C  
ATOM   2077  O   GLY A1075      -6.256 -33.967   3.414  1.00142.88           O  
ANISOU 2077  O   GLY A1075    18202  18535  17553   2698    786    772       O  
ATOM   2078  N   ASP A1076      -7.383 -34.647   1.563  1.00133.51           N  
ANISOU 2078  N   ASP A1076    17700  16672  16356   2545   1482    566       N  
ATOM   2079  CA  ASP A1076      -6.799 -35.994   1.502  1.00137.94           C  
ANISOU 2079  CA  ASP A1076    18314  17081  17015   3316   1587    579       C  
ATOM   2080  C   ASP A1076      -6.048 -36.241   0.185  1.00143.22           C  
ANISOU 2080  C   ASP A1076    18618  17976  17824   3512   2014    351       C  
ATOM   2081  O   ASP A1076      -6.648 -36.082  -0.882  1.00139.42           O  
ANISOU 2081  O   ASP A1076    18403  17287  17285   3144   2359    195       O  
ATOM   2082  CB  ASP A1076      -7.919 -37.046   1.682  1.00137.65           C  
ANISOU 2082  CB  ASP A1076    19176  16273  16852   3461   1670    659       C  
ATOM   2083  CG  ASP A1076      -7.543 -38.432   2.175  1.00148.28           C  
ANISOU 2083  CG  ASP A1076    20842  17280  18217   4256   1630    781       C  
ATOM   2084  OD1 ASP A1076      -6.342 -38.681   2.401  1.00154.06           O  
ANISOU 2084  OD1 ASP A1076    21054  18409  19073   4847   1507    810       O  
ATOM   2085  OD2 ASP A1076      -8.455 -39.265   2.340  1.00151.67           O1-
ANISOU 2085  OD2 ASP A1076    22052  17051  18525   4285   1722    846       O1-
ATOM   2086  N   PRO A1077      -4.757 -36.664   0.231  1.00145.39           N  
ANISOU 2086  N   PRO A1077    18290  18695  18257   4122   2002    319       N  
ATOM   2087  CA  PRO A1077      -4.026 -36.934  -1.021  1.00148.84           C  
ANISOU 2087  CA  PRO A1077    18362  19378  18812   4342   2457     81       C  
ATOM   2088  C   PRO A1077      -4.694 -37.968  -1.934  1.00151.31           C  
ANISOU 2088  C   PRO A1077    19400  19028  19064   4563   2865    -42       C  
ATOM   2089  O   PRO A1077      -4.700 -37.766  -3.148  1.00150.27           O  
ANISOU 2089  O   PRO A1077    19219  18961  18915   4309   3275   -256       O  
ATOM   2090  CB  PRO A1077      -2.652 -37.409  -0.536  1.00158.69           C  
ANISOU 2090  CB  PRO A1077    18905  21169  20221   5111   2295     97       C  
ATOM   2091  CG  PRO A1077      -2.517 -36.851   0.834  1.00162.78           C  
ANISOU 2091  CG  PRO A1077    19180  21966  20702   5003   1729    308       C  
ATOM   2092  CD  PRO A1077      -3.895 -36.891   1.408  1.00151.81           C  
ANISOU 2092  CD  PRO A1077    18689  19866  19126   4658   1570    482       C  
ATOM   2093  N   GLU A1078      -5.277 -39.049  -1.356  1.00147.69           N  
ANISOU 2093  N   GLU A1078    19659  17917  18539   4981   2761     87       N  
ATOM   2094  CA  GLU A1078      -5.968 -40.108  -2.109  1.00147.19           C  
ANISOU 2094  CA  GLU A1078    20380  17149  18395   5144   3122    -39       C  
ATOM   2095  C   GLU A1078      -7.261 -39.608  -2.787  1.00142.49           C  
ANISOU 2095  C   GLU A1078    20263  16240  17636   4325   3290   -145       C  
ATOM   2096  O   GLU A1078      -7.583 -40.051  -3.894  1.00141.66           O  
ANISOU 2096  O   GLU A1078    20496  15862  17468   4267   3678   -366       O  
ATOM   2097  CB  GLU A1078      -6.219 -41.377  -1.251  1.00151.77           C  
ANISOU 2097  CB  GLU A1078    21654  17086  18926   5752   2972    141       C  
ATOM   2098  CG  GLU A1078      -7.126 -41.189  -0.038  1.00159.41           C  
ANISOU 2098  CG  GLU A1078    23059  17755  19755   5411   2588    405       C  
ATOM   2099  CD  GLU A1078      -7.798 -42.415   0.561  1.00182.39           C  
ANISOU 2099  CD  GLU A1078    26920  19848  22534   5717   2573    555       C  
ATOM   2100  OE1 GLU A1078      -7.541 -43.544   0.083  1.00187.68           O1-
ANISOU 2100  OE1 GLU A1078    28011  20079  23222   6281   2844    463       O1-
ATOM   2101  OE2 GLU A1078      -8.590 -42.240   1.517  1.00167.50           O  
ANISOU 2101  OE2 GLU A1078    25394  17740  20507   5374   2312    759       O  
ATOM   2102  N   LEU A1079      -7.982 -38.680  -2.127  1.00132.94           N  
ANISOU 2102  N   LEU A1079    19070  15102  16340   3731   2989     -1       N  
ATOM   2103  CA  LEU A1079      -9.219 -38.109  -2.656  1.00126.39           C  
ANISOU 2103  CA  LEU A1079    18620  14060  15344   3012   3079    -85       C  
ATOM   2104  C   LEU A1079      -8.950 -37.030  -3.698  1.00128.43           C  
ANISOU 2104  C   LEU A1079    18435  14778  15586   2575   3277   -243       C  
ATOM   2105  O   LEU A1079      -9.735 -36.895  -4.639  1.00124.96           O  
ANISOU 2105  O   LEU A1079    18330  14151  14998   2196   3502   -396       O  
ATOM   2106  CB  LEU A1079     -10.136 -37.608  -1.532  1.00121.75           C  
ANISOU 2106  CB  LEU A1079    18270  13341  14649   2631   2709    117       C  
ATOM   2107  CG  LEU A1079     -10.975 -38.687  -0.834  1.00126.40           C  
ANISOU 2107  CG  LEU A1079    19586  13299  15142   2784   2649    224       C  
ATOM   2108  CD1 LEU A1079     -11.282 -38.304   0.602  1.00124.73           C  
ANISOU 2108  CD1 LEU A1079    19409  13119  14865   2681   2243    480       C  
ATOM   2109  CD2 LEU A1079     -12.261 -38.979  -1.601  1.00125.07           C  
ANISOU 2109  CD2 LEU A1079    19994  12711  14816   2332   2893     48       C  
ATOM   2110  N   GLU A1080      -7.821 -36.292  -3.547  1.00127.70           N  
ANISOU 2110  N   GLU A1080    17601  15296  15622   2620   3200   -211       N  
ATOM   2111  CA  GLU A1080      -7.344 -35.255  -4.475  1.00127.54           C  
ANISOU 2111  CA  GLU A1080    17124  15749  15585   2204   3420   -339       C  
ATOM   2112  C   GLU A1080      -7.035 -35.886  -5.836  1.00136.00           C  
ANISOU 2112  C   GLU A1080    18262  16777  16635   2416   3919   -581       C  
ATOM   2113  O   GLU A1080      -7.342 -35.296  -6.873  1.00133.80           O  
ANISOU 2113  O   GLU A1080    18075  16557  16206   1974   4174   -707       O  
ATOM   2114  CB  GLU A1080      -6.071 -34.588  -3.931  1.00132.40           C  
ANISOU 2114  CB  GLU A1080    16910  17035  16363   2261   3255   -279       C  
ATOM   2115  CG  GLU A1080      -6.311 -33.464  -2.941  1.00137.90           C  
ANISOU 2115  CG  GLU A1080    17475  17903  17017   1783   2841   -111       C  
ATOM   2116  CD  GLU A1080      -5.080 -33.111  -2.130  1.00159.99           C  
ANISOU 2116  CD  GLU A1080    19505  21314  19970   1939   2583    -52       C  
ATOM   2117  OE1 GLU A1080      -4.100 -32.596  -2.717  1.00150.51           O  
ANISOU 2117  OE1 GLU A1080    17673  20665  18851   1787   2792   -179       O  
ATOM   2118  OE2 GLU A1080      -5.093 -33.361  -0.904  1.00155.83           O1-
ANISOU 2118  OE2 GLU A1080    19000  20745  19463   2196   2174    113       O1-
ATOM   2119  N   GLY A1081      -6.431 -37.078  -5.798  1.00138.94           N  
ANISOU 2119  N   GLY A1081    18631  17030  17128   3124   4046   -639       N  
ATOM   2120  CA  GLY A1081      -6.079 -37.880  -6.963  1.00143.44           C  
ANISOU 2120  CA  GLY A1081    19319  17503  17679   3470   4523   -887       C  
ATOM   2121  C   GLY A1081      -7.303 -38.389  -7.695  1.00145.38           C  
ANISOU 2121  C   GLY A1081    20399  17128  17712   3223   4710  -1021       C  
ATOM   2122  O   GLY A1081      -7.344 -38.342  -8.924  1.00145.87           O  
ANISOU 2122  O   GLY A1081    20564  17224  17637   3052   5087  -1240       O  
ATOM   2123  N   TRP A1082      -8.317 -38.854  -6.936  1.00139.75           N  
ANISOU 2123  N   TRP A1082    20275  15880  16942   3160   4446   -897       N  
ATOM   2124  CA  TRP A1082      -9.605 -39.330  -7.451  1.00137.13           C  
ANISOU 2124  CA  TRP A1082    20710  14990  16404   2838   4552  -1024       C  
ATOM   2125  C   TRP A1082     -10.335 -38.160  -8.138  1.00135.22           C  
ANISOU 2125  C   TRP A1082    20438  14972  15967   2115   4552  -1078       C  
ATOM   2126  O   TRP A1082     -10.917 -38.348  -9.209  1.00134.22           O  
ANISOU 2126  O   TRP A1082    20683  14675  15642   1888   4801  -1294       O  
ATOM   2127  CB  TRP A1082     -10.446 -39.902  -6.291  1.00134.49           C  
ANISOU 2127  CB  TRP A1082    20875  14163  16063   2850   4244   -843       C  
ATOM   2128  CG  TRP A1082     -11.767 -40.528  -6.655  1.00134.09           C  
ANISOU 2128  CG  TRP A1082    21585  13548  15814   2505   4339   -982       C  
ATOM   2129  CD1 TRP A1082     -12.350 -40.580  -7.888  1.00136.46           C  
ANISOU 2129  CD1 TRP A1082    22167  13756  15924   2173   4609  -1254       C  
ATOM   2130  CD2 TRP A1082     -12.672 -41.187  -5.757  1.00133.36           C  
ANISOU 2130  CD2 TRP A1082    22052  12948  15669   2414   4162   -868       C  
ATOM   2131  NE1 TRP A1082     -13.572 -41.203  -7.811  1.00135.01           N  
ANISOU 2131  NE1 TRP A1082    22627  13082  15588   1854   4584  -1335       N  
ATOM   2132  CE2 TRP A1082     -13.787 -41.607  -6.518  1.00136.47           C  
ANISOU 2132  CE2 TRP A1082    23002  12991  15861   1981   4340  -1103       C  
ATOM   2133  CE3 TRP A1082     -12.651 -41.465  -4.378  1.00135.16           C  
ANISOU 2133  CE3 TRP A1082    22377  13002  15974   2632   3874   -591       C  
ATOM   2134  CZ2 TRP A1082     -14.864 -42.301  -5.950  1.00135.46           C  
ANISOU 2134  CZ2 TRP A1082    23481  12360  15627   1716   4271  -1085       C  
ATOM   2135  CZ3 TRP A1082     -13.718 -42.150  -3.816  1.00136.24           C  
ANISOU 2135  CZ3 TRP A1082    23175  12602  15988   2393   3824   -547       C  
ATOM   2136  CH2 TRP A1082     -14.809 -42.559  -4.597  1.00136.09           C  
ANISOU 2136  CH2 TRP A1082    23661  12256  15789   1916   4034   -798       C  
ATOM   2137  N   ALA A1083     -10.262 -36.954  -7.534  1.00128.11           N  
ANISOU 2137  N   ALA A1083    19121  14453  15101   1786   4268   -888       N  
ATOM   2138  CA  ALA A1083     -10.874 -35.724  -8.039  1.00123.31           C  
ANISOU 2138  CA  ALA A1083    18497  14049  14307   1169   4222   -890       C  
ATOM   2139  C   ALA A1083     -10.254 -35.276  -9.363  1.00129.00           C  
ANISOU 2139  C   ALA A1083    19002  15088  14922   1048   4600  -1056       C  
ATOM   2140  O   ALA A1083     -10.973 -35.147 -10.359  1.00127.10           O  
ANISOU 2140  O   ALA A1083    19132  14730  14432    758   4760  -1200       O  
ATOM   2141  CB  ALA A1083     -10.764 -34.621  -6.998  1.00121.23           C  
ANISOU 2141  CB  ALA A1083    17877  14066  14117    929   3853   -657       C  
ATOM   2142  N   ARG A1084      -8.917 -35.084  -9.382  1.00129.29           N  
ANISOU 2142  N   ARG A1084    18435  15559  15129   1276   4751  -1048       N  
ATOM   2143  CA  ARG A1084      -8.168 -34.653 -10.564  1.00131.94           C  
ANISOU 2143  CA  ARG A1084    18493  16267  15372   1152   5163  -1198       C  
ATOM   2144  C   ARG A1084      -8.172 -35.696 -11.687  1.00140.15           C  
ANISOU 2144  C   ARG A1084    19877  17082  16291   1450   5588  -1467       C  
ATOM   2145  O   ARG A1084      -8.045 -35.317 -12.851  1.00141.66           O  
ANISOU 2145  O   ARG A1084    20107  17448  16271   1211   5928  -1609       O  
ATOM   2146  CB  ARG A1084      -6.747 -34.208 -10.198  1.00134.31           C  
ANISOU 2146  CB  ARG A1084    17982  17155  15895   1283   5213  -1141       C  
ATOM   2147  CG  ARG A1084      -6.543 -32.706 -10.349  1.00137.68           C  
ANISOU 2147  CG  ARG A1084    18124  17964  16223    639   5188  -1044       C  
ATOM   2148  CD  ARG A1084      -5.920 -32.086  -9.112  1.00143.16           C  
ANISOU 2148  CD  ARG A1084    18263  18997  17133    569   4829   -866       C  
ATOM   2149  NE  ARG A1084      -5.244 -30.821  -9.411  1.00150.57           N  
ANISOU 2149  NE  ARG A1084    18783  20406  18021     13   4955   -844       N  
ATOM   2150  CZ  ARG A1084      -5.796 -29.618  -9.277  1.00160.18           C  
ANISOU 2150  CZ  ARG A1084    20244  21543  19076   -590   4774   -715       C  
ATOM   2151  NH1 ARG A1084      -7.044 -29.496  -8.847  1.00145.70           N  
ANISOU 2151  NH1 ARG A1084    18994  19241  17123   -677   4451   -607       N  
ATOM   2152  NH2 ARG A1084      -5.101 -28.527  -9.572  1.00146.58           N1+
ANISOU 2152  NH2 ARG A1084    18193  20203  17296  -1112   4934   -703       N1+
ATOM   2153  N   SER A1085      -8.355 -36.994 -11.352  1.00138.43           N  
ANISOU 2153  N   SER A1085    19988  16440  16170   1946   5578  -1539       N  
ATOM   2154  CA  SER A1085      -8.460 -38.060 -12.350  1.00141.76           C  
ANISOU 2154  CA  SER A1085    20862  16542  16458   2222   5963  -1821       C  
ATOM   2155  C   SER A1085      -9.774 -37.885 -13.108  1.00143.23           C  
ANISOU 2155  C   SER A1085    21673  16436  16314   1698   5956  -1935       C  
ATOM   2156  O   SER A1085      -9.818 -38.143 -14.308  1.00145.35           O  
ANISOU 2156  O   SER A1085    22203  16672  16350   1652   6309  -2181       O  
ATOM   2157  CB  SER A1085      -8.407 -39.439 -11.699  1.00147.15           C  
ANISOU 2157  CB  SER A1085    21853  16752  17305   2838   5920  -1844       C  
ATOM   2158  OG  SER A1085      -7.095 -39.733 -11.249  1.00158.85           O  
ANISOU 2158  OG  SER A1085    22757  18550  19047   3461   5986  -1797       O  
ATOM   2159  N   LEU A1086     -10.829 -37.405 -12.413  1.00135.14           N  
ANISOU 2159  N   LEU A1086    20850  15254  15244   1312   5549  -1767       N  
ATOM   2160  CA  LEU A1086     -12.137 -37.138 -13.011  1.00131.62           C  
ANISOU 2160  CA  LEU A1086    20895  14629  14486    826   5461  -1861       C  
ATOM   2161  C   LEU A1086     -12.089 -35.856 -13.843  1.00135.09           C  
ANISOU 2161  C   LEU A1086    21163  15470  14694    418   5533  -1834       C  
ATOM   2162  O   LEU A1086     -12.828 -35.735 -14.818  1.00134.23           O  
ANISOU 2162  O   LEU A1086    21437  15308  14257    143   5613  -1988       O  
ATOM   2163  CB  LEU A1086     -13.251 -37.096 -11.948  1.00126.86           C  
ANISOU 2163  CB  LEU A1086    20508  13775  13919    609   5029  -1708       C  
ATOM   2164  CG  LEU A1086     -13.916 -38.444 -11.637  1.00132.24           C  
ANISOU 2164  CG  LEU A1086    21716  13915  14616    755   5027  -1833       C  
ATOM   2165  CD1 LEU A1086     -14.199 -38.590 -10.169  1.00130.24           C  
ANISOU 2165  CD1 LEU A1086    21442  13485  14559    820   4691  -1593       C  
ATOM   2166  CD2 LEU A1086     -15.203 -38.624 -12.421  1.00132.60           C  
ANISOU 2166  CD2 LEU A1086    22256  13781  14344    328   5027  -2061       C  
ATOM   2167  N   GLU A1087     -11.190 -34.922 -13.481  1.00132.35           N  
ANISOU 2167  N   GLU A1087    20272  15524  14492    372   5513  -1646       N  
ATOM   2168  CA  GLU A1087     -10.959 -33.671 -14.208  1.00132.30           C  
ANISOU 2168  CA  GLU A1087    20126  15870  14274    -26   5630  -1588       C  
ATOM   2169  C   GLU A1087     -10.228 -34.012 -15.524  1.00140.93           C  
ANISOU 2169  C   GLU A1087    21221  17127  15199     83   6161  -1817       C  
ATOM   2170  O   GLU A1087     -10.464 -33.376 -16.551  1.00140.66           O  
ANISOU 2170  O   GLU A1087    21417  17205  14821   -243   6330  -1864       O  
ATOM   2171  CB  GLU A1087     -10.121 -32.715 -13.334  1.00133.61           C  
ANISOU 2171  CB  GLU A1087    19712  16383  14669   -134   5478  -1352       C  
ATOM   2172  CG  GLU A1087      -9.800 -31.366 -13.956  1.00145.82           C  
ANISOU 2172  CG  GLU A1087    21151  18244  16009   -602   5610  -1264       C  
ATOM   2173  CD  GLU A1087      -8.495 -30.776 -13.460  1.00171.67           C  
ANISOU 2173  CD  GLU A1087    23750  21956  19522   -664   5692  -1160       C  
ATOM   2174  OE1 GLU A1087      -8.512 -30.089 -12.413  1.00166.07           O1-
ANISOU 2174  OE1 GLU A1087    22844  21299  18957   -835   5337   -970       O1-
ATOM   2175  OE2 GLU A1087      -7.452 -31.009 -14.114  1.00168.83           O  
ANISOU 2175  OE2 GLU A1087    23037  21917  19192   -552   6119  -1291       O  
ATOM   2176  N   GLU A1088      -9.352 -35.031 -15.471  1.00142.09           N  
ANISOU 2176  N   GLU A1088    21141  17282  15565    584   6423  -1955       N  
ATOM   2177  CA  GLU A1088      -8.561 -35.559 -16.585  1.00147.71           C  
ANISOU 2177  CA  GLU A1088    21812  18147  16163    820   6964  -2209       C  
ATOM   2178  C   GLU A1088      -9.444 -36.408 -17.512  1.00152.17           C  
ANISOU 2178  C   GLU A1088    23096  18303  16420    841   7108  -2480       C  
ATOM   2179  O   GLU A1088      -9.250 -36.380 -18.728  1.00155.05           O  
ANISOU 2179  O   GLU A1088    23635  18795  16482    754   7498  -2674       O  
ATOM   2180  CB  GLU A1088      -7.409 -36.415 -16.029  1.00153.90           C  
ANISOU 2180  CB  GLU A1088    22114  19052  17310   1458   7122  -2261       C  
ATOM   2181  CG  GLU A1088      -6.200 -36.536 -16.939  1.00172.31           C  
ANISOU 2181  CG  GLU A1088    24051  21812  19609   1687   7689  -2458       C  
ATOM   2182  CD  GLU A1088      -5.100 -37.443 -16.418  1.00202.37           C  
ANISOU 2182  CD  GLU A1088    27366  25765  23760   2429   7829  -2536       C  
ATOM   2183  OE1 GLU A1088      -4.645 -37.238 -15.269  1.00197.14           O  
ANISOU 2183  OE1 GLU A1088    26191  25304  23410   2587   7505  -2329       O  
ATOM   2184  OE2 GLU A1088      -4.683 -38.355 -17.168  1.00204.28           O1-
ANISOU 2184  OE2 GLU A1088    27747  25935  23936   2885   8258  -2813       O1-
ATOM   2185  N   LYS A1089     -10.403 -37.168 -16.926  1.00146.17           N  
ANISOU 2185  N   LYS A1089    22759  17064  15716    920   6804  -2504       N  
ATOM   2186  CA  LYS A1089     -11.340 -38.053 -17.629  1.00146.65           C  
ANISOU 2186  CA  LYS A1089    23510  16703  15508    874   6873  -2782       C  
ATOM   2187  C   LYS A1089     -12.569 -37.321 -18.174  1.00147.48           C  
ANISOU 2187  C   LYS A1089    23975  16827  15235    311   6637  -2782       C  
ATOM   2188  O   LYS A1089     -13.198 -37.818 -19.113  1.00149.03           O  
ANISOU 2188  O   LYS A1089    24673  16850  15100    188   6759  -3054       O  
ATOM   2189  CB  LYS A1089     -11.787 -39.213 -16.720  1.00148.45           C  
ANISOU 2189  CB  LYS A1089    24035  16411  15959   1152   6681  -2811       C  
ATOM   2190  CG  LYS A1089     -10.761 -40.327 -16.592  1.00161.27           C  
ANISOU 2190  CG  LYS A1089    25604  17856  17813   1821   6996  -2935       C  
ATOM   2191  CD  LYS A1089     -10.994 -41.149 -15.336  1.00166.55           C  
ANISOU 2191  CD  LYS A1089    26443  18078  18759   2114   6724  -2805       C  
ATOM   2192  CE  LYS A1089      -9.852 -42.095 -15.060  1.00178.55           C  
ANISOU 2192  CE  LYS A1089    27833  19478  20529   2887   6973  -2856       C  
ATOM   2193  NZ  LYS A1089     -10.035 -42.816 -13.774  1.00184.99           N1+
ANISOU 2193  NZ  LYS A1089    28851  19856  21581   3194   6681  -2670       N1+
ATOM   2194  N   HIS A1090     -12.935 -36.171 -17.576  1.00139.71           N  
ANISOU 2194  N   HIS A1090    22757  16046  14281      0   6280  -2497       N  
ATOM   2195  CA  HIS A1090     -14.109 -35.398 -17.988  1.00136.54           C  
ANISOU 2195  CA  HIS A1090    22657  15692  13529   -441   6004  -2467       C  
ATOM   2196  C   HIS A1090     -13.823 -33.911 -18.020  1.00138.06           C  
ANISOU 2196  C   HIS A1090    22586  16236  13634   -699   5922  -2202       C  
ATOM   2197  O   HIS A1090     -13.255 -33.367 -17.070  1.00135.76           O  
ANISOU 2197  O   HIS A1090    21869  16069  13645   -669   5796  -1965       O  
ATOM   2198  CB  HIS A1090     -15.312 -35.681 -17.071  1.00133.81           C  
ANISOU 2198  CB  HIS A1090    22484  15085  13271   -560   5560  -2424       C  
ATOM   2199  CG  HIS A1090     -15.669 -37.131 -16.976  1.00139.63           C  
ANISOU 2199  CG  HIS A1090    23567  15408  14076   -399   5639  -2673       C  
ATOM   2200  ND1 HIS A1090     -16.387 -37.764 -17.975  1.00143.83           N  
ANISOU 2200  ND1 HIS A1090    24588  15792  14268   -561   5744  -2998       N  
ATOM   2201  CD2 HIS A1090     -15.365 -38.034 -16.014  1.00142.14           C  
ANISOU 2201  CD2 HIS A1090    23855  15416  14735   -100   5633  -2637       C  
ATOM   2202  CE1 HIS A1090     -16.507 -39.022 -17.585  1.00145.29           C  
ANISOU 2202  CE1 HIS A1090    25044  15548  14609   -401   5818  -3160       C  
ATOM   2203  NE2 HIS A1090     -15.914 -39.230 -16.408  1.00144.70           N  
ANISOU 2203  NE2 HIS A1090    24698  15344  14938   -101   5757  -2936       N  
ATOM   2204  N   GLY A1091     -14.249 -33.268 -19.105  1.00135.10           N  
ANISOU 2204  N   GLY A1091    22521  15996  12815   -963   5980  -2248       N  
ATOM   2205  CA  GLY A1091     -14.083 -31.833 -19.320  1.00133.74           C  
ANISOU 2205  CA  GLY A1091    22281  16076  12456  -1242   5932  -2002       C  
ATOM   2206  C   GLY A1091     -15.140 -30.981 -18.649  1.00131.49           C  
ANISOU 2206  C   GLY A1091    22095  15743  12123  -1429   5420  -1799       C  
ATOM   2207  O   GLY A1091     -15.030 -29.753 -18.657  1.00130.05           O  
ANISOU 2207  O   GLY A1091    21910  15690  11814  -1633   5341  -1570       O  
ATOM   2208  N   ASN A1092     -16.182 -31.644 -18.082  1.00124.80           N  
ANISOU 2208  N   ASN A1092    21364  14698  11357  -1366   5095  -1896       N  
ATOM   2209  CA  ASN A1092     -17.318 -31.066 -17.350  1.00120.05           C  
ANISOU 2209  CA  ASN A1092    20812  14068  10733  -1480   4612  -1764       C  
ATOM   2210  C   ASN A1092     -16.961 -30.862 -15.880  1.00118.74           C  
ANISOU 2210  C   ASN A1092    20261  13847  11007  -1406   4427  -1547       C  
ATOM   2211  O   ASN A1092     -17.779 -30.342 -15.126  1.00114.91           O  
ANISOU 2211  O   ASN A1092    19772  13347  10541  -1476   4059  -1426       O  
ATOM   2212  CB  ASN A1092     -18.536 -32.007 -17.429  1.00122.58           C  
ANISOU 2212  CB  ASN A1092    21378  14256  10941  -1498   4417  -2015       C  
ATOM   2213  CG  ASN A1092     -19.280 -31.989 -18.740  1.00161.67           C  
ANISOU 2213  CG  ASN A1092    26723  19324  15382  -1625   4411  -2223       C  
ATOM   2214  OD1 ASN A1092     -19.375 -33.004 -19.444  1.00163.79           O  
ANISOU 2214  OD1 ASN A1092    27217  19500  15515  -1623   4605  -2521       O  
ATOM   2215  ND2 ASN A1092     -19.841 -30.840 -19.093  1.00154.83           N  
ANISOU 2215  ND2 ASN A1092    25987  18651  14191  -1721   4172  -2078       N  
ATOM   2216  N   VAL A1093     -15.749 -31.289 -15.478  1.00115.63           N  
ANISOU 2216  N   VAL A1093    19536  13456  10943  -1235   4676  -1515       N  
ATOM   2217  CA  VAL A1093     -15.240 -31.229 -14.110  1.00113.37           C  
ANISOU 2217  CA  VAL A1093    18863  13154  11060  -1124   4514  -1330       C  
ATOM   2218  C   VAL A1093     -14.057 -30.250 -13.994  1.00118.96           C  
ANISOU 2218  C   VAL A1093    19211  14116  11871  -1223   4649  -1146       C  
ATOM   2219  O   VAL A1093     -13.117 -30.320 -14.792  1.00122.04           O  
ANISOU 2219  O   VAL A1093    19476  14676  12217  -1206   5035  -1222       O  
ATOM   2220  CB  VAL A1093     -14.901 -32.660 -13.597  1.00118.42           C  
ANISOU 2220  CB  VAL A1093    19415  13585  11993   -794   4619  -1453       C  
ATOM   2221  CG1 VAL A1093     -14.248 -32.634 -12.218  1.00117.44           C  
ANISOU 2221  CG1 VAL A1093    18890  13483  12248   -622   4449  -1252       C  
ATOM   2222  CG2 VAL A1093     -16.144 -33.545 -13.576  1.00116.92           C  
ANISOU 2222  CG2 VAL A1093    19615  13113  11698   -820   4470  -1626       C  
ATOM   2223  N   LYS A1094     -14.132 -29.328 -13.007  1.00113.34           N  
ANISOU 2223  N   LYS A1094    18344  13444  11274  -1363   4345   -926       N  
ATOM   2224  CA  LYS A1094     -13.116 -28.323 -12.697  1.00114.77           C  
ANISOU 2224  CA  LYS A1094    18200  13848  11560  -1554   4403   -756       C  
ATOM   2225  C   LYS A1094     -12.714 -28.464 -11.235  1.00118.78           C  
ANISOU 2225  C   LYS A1094    18316  14380  12437  -1423   4149   -641       C  
ATOM   2226  O   LYS A1094     -13.357 -27.888 -10.357  1.00115.21           O  
ANISOU 2226  O   LYS A1094    17954  13827  11995  -1520   3795   -512       O  
ATOM   2227  CB  LYS A1094     -13.625 -26.899 -12.993  1.00115.78           C  
ANISOU 2227  CB  LYS A1094    18648  13962  11382  -1898   4268   -608       C  
ATOM   2228  N   VAL A1095     -11.680 -29.270 -10.966  1.00119.45           N  
ANISOU 2228  N   VAL A1095    17981  14605  12800  -1155   4320   -698       N  
ATOM   2229  CA  VAL A1095     -11.196 -29.477  -9.603  1.00119.51           C  
ANISOU 2229  CA  VAL A1095    17605  14677  13128   -973   4067   -587       C  
ATOM   2230  C   VAL A1095     -10.143 -28.417  -9.296  1.00127.06           C  
ANISOU 2230  C   VAL A1095    18115  15990  14172  -1255   4076   -478       C  
ATOM   2231  O   VAL A1095      -9.208 -28.228 -10.083  1.00130.78           O  
ANISOU 2231  O   VAL A1095    18318  16748  14625  -1364   4432   -549       O  
ATOM   2232  CB  VAL A1095     -10.712 -30.931  -9.335  1.00125.78           C  
ANISOU 2232  CB  VAL A1095    18221  15411  14160   -458   4170   -686       C  
ATOM   2233  CG1 VAL A1095     -10.062 -31.066  -7.958  1.00126.22           C  
ANISOU 2233  CG1 VAL A1095    17856  15598  14504   -236   3894   -547       C  
ATOM   2234  CG2 VAL A1095     -11.863 -31.921  -9.472  1.00123.49           C  
ANISOU 2234  CG2 VAL A1095    18450  14701  13771   -294   4123   -790       C  
ATOM   2235  N   ILE A1096     -10.338 -27.690  -8.179  1.00122.08           N  
ANISOU 2235  N   ILE A1096    17434  15346  13605  -1422   3704   -324       N  
ATOM   2236  CA  ILE A1096      -9.434 -26.641  -7.706  1.00124.36           C  
ANISOU 2236  CA  ILE A1096    17345  15938  13968  -1764   3644   -235       C  
ATOM   2237  C   ILE A1096      -8.942 -27.014  -6.298  1.00129.72           C  
ANISOU 2237  C   ILE A1096    17604  16761  14923  -1527   3319   -168       C  
ATOM   2238  O   ILE A1096      -9.656 -26.804  -5.315  1.00125.73           O  
ANISOU 2238  O   ILE A1096    17317  16051  14404  -1529   2954    -67       O  
ATOM   2239  CB  ILE A1096     -10.046 -25.196  -7.777  1.00125.19           C  
ANISOU 2239  CB  ILE A1096    17867  15885  13815  -2257   3516   -127       C  
ATOM   2240  CG1 ILE A1096     -10.908 -24.946  -9.061  1.00124.48           C  
ANISOU 2240  CG1 ILE A1096    18351  15562  13383  -2360   3717   -161       C  
ATOM   2241  CG2 ILE A1096      -8.963 -24.123  -7.608  1.00129.32           C  
ANISOU 2241  CG2 ILE A1096    18053  16711  14374  -2723   3585    -81       C  
ATOM   2242  CD1 ILE A1096     -10.174 -24.983 -10.496  1.00139.22           C  
ANISOU 2242  CD1 ILE A1096    20167  17624  15106  -2499   4228   -259       C  
ATOM   2243  N   THR A1097      -7.723 -27.585  -6.213  1.00131.86           N  
ANISOU 2243  N   THR A1097    17269  17411  15419  -1287   3455   -232       N  
ATOM   2244  CA  THR A1097      -7.084 -27.996  -4.955  1.00133.83           C  
ANISOU 2244  CA  THR A1097    17059  17882  15907   -991   3143   -173       C  
ATOM   2245  C   THR A1097      -6.546 -26.761  -4.184  1.00140.35           C  
ANISOU 2245  C   THR A1097    17578  19006  16744  -1474   2895   -101       C  
ATOM   2246  O   THR A1097      -6.240 -26.864  -2.994  1.00140.62           O  
ANISOU 2246  O   THR A1097    17342  19187  16900  -1323   2533    -33       O  
ATOM   2247  CB  THR A1097      -6.031 -29.097  -5.230  1.00144.59           C  
ANISOU 2247  CB  THR A1097    17901  19557  17480   -464   3373   -284       C  
ATOM   2248  OG1 THR A1097      -6.575 -30.048  -6.143  1.00142.23           O  
ANISOU 2248  OG1 THR A1097    18009  18923  17110   -149   3667   -386       O  
ATOM   2249  CG2 THR A1097      -5.592 -29.831  -3.974  1.00144.48           C  
ANISOU 2249  CG2 THR A1097    17566  19661  17669     42   3019   -204       C  
ATOM   2250  N   GLU A1098      -6.477 -25.592  -4.863  1.00138.51           N  
ANISOU 2250  N   GLU A1098    17465  18819  16344  -2071   3086   -117       N  
ATOM   2251  CA  GLU A1098      -6.005 -24.306  -4.334  1.00140.47           C  
ANISOU 2251  CA  GLU A1098    17552  19269  16551  -2657   2929    -79       C  
ATOM   2252  C   GLU A1098      -6.848 -23.753  -3.181  1.00141.87           C  
ANISOU 2252  C   GLU A1098    18131  19131  16643  -2753   2467     36       C  
ATOM   2253  O   GLU A1098      -8.031 -24.088  -3.050  1.00136.58           O  
ANISOU 2253  O   GLU A1098    17990  18031  15873  -2499   2338     97       O  
ATOM   2254  CB  GLU A1098      -5.973 -23.253  -5.451  1.00142.92           C  
ANISOU 2254  CB  GLU A1098    18146  19522  16634  -3250   3287    -99       C  
ATOM   2255  CG  GLU A1098      -4.857 -23.427  -6.460  1.00158.11           C  
ANISOU 2255  CG  GLU A1098    19563  21898  18614  -3373   3771   -224       C  
ATOM   2256  CD  GLU A1098      -4.857 -22.369  -7.543  1.00178.33           C  
ANISOU 2256  CD  GLU A1098    22503  24359  20895  -3995   4142   -213       C  
ATOM   2257  OE1 GLU A1098      -5.853 -22.289  -8.298  1.00166.45           O  
ANISOU 2257  OE1 GLU A1098    21695  22408  19140  -3943   4243   -158       O  
ATOM   2258  OE2 GLU A1098      -3.858 -21.620  -7.640  1.00177.51           O1-
ANISOU 2258  OE2 GLU A1098    22008  24636  20802  -4550   4330   -260       O1-
ATOM   2259  N   MET A1099      -6.231 -22.870  -2.368  1.00142.02           N  
ANISOU 2259  N   MET A1099    17888  19392  16682  -3162   2237     42       N  
ATOM   2260  CA  MET A1099      -6.896 -22.165  -1.276  1.00139.52           C  
ANISOU 2260  CA  MET A1099    17951  18811  16249  -3329   1830    120       C  
ATOM   2261  C   MET A1099      -7.428 -20.862  -1.884  1.00142.40           C  
ANISOU 2261  C   MET A1099    18917  18834  16353  -3877   1972    141       C  
ATOM   2262  O   MET A1099      -6.657 -19.932  -2.151  1.00146.16           O  
ANISOU 2262  O   MET A1099    19261  19493  16780  -4455   2115     95       O  
ATOM   2263  CB  MET A1099      -5.933 -21.910  -0.089  1.00145.93           C  
ANISOU 2263  CB  MET A1099    18207  20058  17182  -3486   1492     89       C  
ATOM   2264  CG  MET A1099      -6.528 -21.061   1.047  1.00147.56           C  
ANISOU 2264  CG  MET A1099    18831  20006  17228  -3728   1090    138       C  
ATOM   2265  SD  MET A1099      -7.900 -21.821   1.957  1.00145.86           S  
ANISOU 2265  SD  MET A1099    19123  19352  16943  -3133    777    259       S  
ATOM   2266  CE  MET A1099      -7.002 -22.920   3.046  1.00145.85           C  
ANISOU 2266  CE  MET A1099    18456  19813  17145  -2656    461    283       C  
ATOM   2267  N   LEU A1100      -8.739 -20.844  -2.178  1.00133.60           N  
ANISOU 2267  N   LEU A1100    18468  17236  15058  -3681   1958    206       N  
ATOM   2268  CA  LEU A1100      -9.426 -19.698  -2.770  1.00131.56           C  
ANISOU 2268  CA  LEU A1100    18878  16595  14513  -4032   2055    249       C  
ATOM   2269  C   LEU A1100      -9.834 -18.734  -1.672  1.00132.82           C  
ANISOU 2269  C   LEU A1100    19379  16532  14557  -4245   1703    282       C  
ATOM   2270  O   LEU A1100     -10.441 -19.150  -0.678  1.00128.90           O  
ANISOU 2270  O   LEU A1100    18921  15956  14100  -3911   1391    302       O  
ATOM   2271  CB  LEU A1100     -10.669 -20.146  -3.560  1.00127.23           C  
ANISOU 2271  CB  LEU A1100    18823  15711  13809  -3662   2154    280       C  
ATOM   2272  CG  LEU A1100     -10.427 -20.732  -4.936  1.00132.46           C  
ANISOU 2272  CG  LEU A1100    19405  16473  14450  -3580   2559    234       C  
ATOM   2273  CD1 LEU A1100     -10.323 -22.232  -4.870  1.00131.36           C  
ANISOU 2273  CD1 LEU A1100    18867  16506  14540  -3076   2589    169       C  
ATOM   2274  CD2 LEU A1100     -11.548 -20.362  -5.870  1.00132.62           C  
ANISOU 2274  CD2 LEU A1100    20091  16137  14161  -3530   2649    271       C  
ATOM   2275  N   SER A1101      -9.492 -17.444  -1.852  1.00131.43           N  
ANISOU 2275  N   SER A1101    19495  16231  14213  -4822   1779    281       N  
ATOM   2276  CA  SER A1101      -9.828 -16.380  -0.906  1.00130.90           C  
ANISOU 2276  CA  SER A1101    19856  15889  13992  -5081   1489    285       C  
ATOM   2277  C   SER A1101     -11.342 -16.172  -0.887  1.00128.76           C  
ANISOU 2277  C   SER A1101    20281  15137  13503  -4699   1360    351       C  
ATOM   2278  O   SER A1101     -12.016 -16.491  -1.868  1.00126.38           O  
ANISOU 2278  O   SER A1101    20220  14691  13106  -4432   1546    395       O  
ATOM   2279  CB  SER A1101      -9.129 -15.077  -1.282  1.00139.57           C  
ANISOU 2279  CB  SER A1101    21211  16887  14932  -5816   1669    264       C  
ATOM   2280  OG  SER A1101      -7.795 -15.286  -1.717  1.00153.79           O  
ANISOU 2280  OG  SER A1101    22350  19181  16903  -6198   1922    194       O  
ATOM   2281  N   ARG A1102     -11.870 -15.643   0.235  1.00122.71           N  
ANISOU 2281  N   ARG A1102    19812  14168  12644  -4666   1039    336       N  
ATOM   2282  CA  ARG A1102     -13.294 -15.346   0.472  1.00118.05           C  
ANISOU 2282  CA  ARG A1102    19822  13190  11844  -4294    885    365       C  
ATOM   2283  C   ARG A1102     -13.913 -14.551  -0.690  1.00120.27           C  
ANISOU 2283  C   ARG A1102    20751  13095  11850  -4321   1092    427       C  
ATOM   2284  O   ARG A1102     -15.102 -14.696  -0.976  1.00116.77           O  
ANISOU 2284  O   ARG A1102    20626  12475  11266  -3879   1048    452       O  
ATOM   2285  CB  ARG A1102     -13.456 -14.558   1.786  1.00118.28           C  
ANISOU 2285  CB  ARG A1102    20121  13054  11766  -4421    577    311       C  
ATOM   2286  CG  ARG A1102     -12.794 -15.215   2.992  1.00128.16           C  
ANISOU 2286  CG  ARG A1102    20797  14679  13219  -4421    330    260       C  
ATOM   2287  CD  ARG A1102     -12.334 -14.196   4.016  1.00135.32           C  
ANISOU 2287  CD  ARG A1102    21898  15508  14010  -4850    101    171       C  
ATOM   2288  NE  ARG A1102     -11.382 -14.776   4.964  1.00132.92           N  
ANISOU 2288  NE  ARG A1102    20951  15665  13886  -4947   -126    120       N  
ATOM   2289  CZ  ARG A1102     -10.913 -14.151   6.038  1.00139.38           C  
ANISOU 2289  CZ  ARG A1102    21798  16544  14618  -5281   -398     19       C  
ATOM   2290  NH1 ARG A1102     -11.313 -12.917   6.324  1.00118.93           N  
ANISOU 2290  NH1 ARG A1102    19894  13526  11770  -5566   -451    -53       N  
ATOM   2291  NH2 ARG A1102     -10.047 -14.755   6.839  1.00127.77           N1+
ANISOU 2291  NH2 ARG A1102    19699  15554  13291  -5307   -633    -19       N1+
ATOM   2292  N   GLU A1103     -13.080 -13.738  -1.364  1.00119.22           N  
ANISOU 2292  N   GLU A1103    20796  12877  11626  -4852   1321    451       N  
ATOM   2293  CA  GLU A1103     -13.422 -12.892  -2.505  1.00120.37           C  
ANISOU 2293  CA  GLU A1103    21617  12649  11470  -4969   1546    541       C  
ATOM   2294  C   GLU A1103     -13.758 -13.726  -3.741  1.00120.31           C  
ANISOU 2294  C   GLU A1103    21487  12777  11447  -4648   1775    589       C  
ATOM   2295  O   GLU A1103     -14.572 -13.295  -4.558  1.00119.43           O  
ANISOU 2295  O   GLU A1103    21961  12371  11047  -4441   1834    667       O  
ATOM   2296  CB  GLU A1103     -12.260 -11.930  -2.826  1.00127.82           C  
ANISOU 2296  CB  GLU A1103    22714  13514  12338  -5733   1777    549       C  
ATOM   2297  CG  GLU A1103     -11.801 -11.062  -1.659  1.00144.03           C  
ANISOU 2297  CG  GLU A1103    24901  15440  14384  -6174   1566    464       C  
ATOM   2298  CD  GLU A1103     -10.674 -11.636  -0.818  1.00166.53           C  
ANISOU 2298  CD  GLU A1103    26881  18840  17553  -6469   1459    341       C  
ATOM   2299  OE1 GLU A1103     -10.965 -12.416   0.119  1.00150.40           O1-
ANISOU 2299  OE1 GLU A1103    24433  17028  15683  -6051   1169    293       O1-
ATOM   2300  OE2 GLU A1103      -9.498 -11.302  -1.094  1.00166.01           O  
ANISOU 2300  OE2 GLU A1103    26535  18998  17544  -7119   1667    292       O  
ATOM   2301  N   PHE A1104     -13.114 -14.905  -3.882  1.00115.00           N  
ANISOU 2301  N   PHE A1104    20082  12551  11060  -4588   1893    535       N  
ATOM   2302  CA  PHE A1104     -13.301 -15.834  -5.001  1.00113.16           C  
ANISOU 2302  CA  PHE A1104    19680  12480  10835  -4311   2126    537       C  
ATOM   2303  C   PHE A1104     -14.541 -16.722  -4.831  1.00110.51           C  
ANISOU 2303  C   PHE A1104    19336  12136  10516  -3700   1927    504       C  
ATOM   2304  O   PHE A1104     -15.251 -16.948  -5.806  1.00109.43           O  
ANISOU 2304  O   PHE A1104    19457  11928  10195  -3460   2027    515       O  
ATOM   2305  CB  PHE A1104     -12.045 -16.709  -5.226  1.00117.14           C  
ANISOU 2305  CB  PHE A1104    19435  13444  11627  -4476   2365    469       C  
ATOM   2306  CG  PHE A1104     -10.757 -15.988  -5.572  1.00124.31           C  
ANISOU 2306  CG  PHE A1104    20207  14496  12531  -5124   2641    468       C  
ATOM   2307  CD1 PHE A1104     -10.484 -15.603  -6.880  1.00130.52           C  
ANISOU 2307  CD1 PHE A1104    21283  15216  13093  -5397   3034    518       C  
ATOM   2308  CD2 PHE A1104      -9.791 -15.753  -4.604  1.00128.82           C  
ANISOU 2308  CD2 PHE A1104    20320  15321  13305  -5485   2521    403       C  
ATOM   2309  CE1 PHE A1104      -9.285 -14.947  -7.201  1.00136.73           C  
ANISOU 2309  CE1 PHE A1104    21924  16163  13863  -6070   3339    508       C  
ATOM   2310  CE2 PHE A1104      -8.593 -15.100  -4.925  1.00137.08           C  
ANISOU 2310  CE2 PHE A1104    21170  16567  14347  -6157   2791    370       C  
ATOM   2311  CZ  PHE A1104      -8.349 -14.704  -6.220  1.00138.12           C  
ANISOU 2311  CZ  PHE A1104    21601  16615  14264  -6464   3219    423       C  
ATOM   2312  N   VAL A1105     -14.785 -17.237  -3.607  1.00103.19           N  
ANISOU 2312  N   VAL A1105    18114  11308   9786  -3485   1653    456       N  
ATOM   2313  CA  VAL A1105     -15.913 -18.127  -3.272  1.00 98.60           C  
ANISOU 2313  CA  VAL A1105    17478  10747   9237  -2994   1483    412       C  
ATOM   2314  C   VAL A1105     -17.273 -17.412  -3.416  1.00103.14           C  
ANISOU 2314  C   VAL A1105    18630  11051   9509  -2752   1335    426       C  
ATOM   2315  O   VAL A1105     -18.253 -18.040  -3.820  1.00101.05           O  
ANISOU 2315  O   VAL A1105    18384  10836   9174  -2413   1311    377       O  
ATOM   2316  CB  VAL A1105     -15.748 -18.814  -1.890  1.00 99.64           C  
ANISOU 2316  CB  VAL A1105    17202  11040   9616  -2872   1259    382       C  
ATOM   2317  CG1 VAL A1105     -16.623 -20.052  -1.789  1.00 95.97           C  
ANISOU 2317  CG1 VAL A1105    16592  10647   9227  -2463   1217    335       C  
ATOM   2318  CG2 VAL A1105     -14.292 -19.191  -1.631  1.00101.90           C  
ANISOU 2318  CG2 VAL A1105    16949  11611  10159  -3108   1339    377       C  
ATOM   2319  N   ARG A1106     -17.316 -16.099  -3.119  1.00102.47           N  
ANISOU 2319  N   ARG A1106    19016  10689   9230  -2924   1240    476       N  
ATOM   2320  CA  ARG A1106     -18.502 -15.249  -3.257  1.00102.32           C  
ANISOU 2320  CA  ARG A1106    19592  10389   8894  -2643   1099    495       C  
ATOM   2321  C   ARG A1106     -18.828 -15.088  -4.749  1.00108.51           C  
ANISOU 2321  C   ARG A1106    20710  11098   9422  -2550   1273    552       C  
ATOM   2322  O   ARG A1106     -20.006 -15.075  -5.109  1.00107.79           O  
ANISOU 2322  O   ARG A1106    20847  10988   9122  -2135   1151    529       O  
ATOM   2323  CB  ARG A1106     -18.283 -13.876  -2.575  1.00103.88           C  
ANISOU 2323  CB  ARG A1106    20281  10243   8944  -2874    989    530       C  
ATOM   2324  CG  ARG A1106     -19.435 -12.885  -2.769  1.00109.91           C  
ANISOU 2324  CG  ARG A1106    21743  10666   9352  -2518    858    556       C  
ATOM   2325  CD  ARG A1106     -19.286 -11.600  -1.991  1.00117.75           C  
ANISOU 2325  CD  ARG A1106    23283  11262  10195  -2697    748    562       C  
ATOM   2326  NE  ARG A1106     -18.085 -10.857  -2.366  1.00124.19           N  
ANISOU 2326  NE  ARG A1106    24361  11853  10973  -3319    945    636       N  
ATOM   2327  CZ  ARG A1106     -17.510  -9.943  -1.597  1.00139.66           C  
ANISOU 2327  CZ  ARG A1106    26632  13540  12894  -3720    893    606       C  
ATOM   2328  NH1 ARG A1106     -18.021  -9.645  -0.411  1.00128.60           N1+
ANISOU 2328  NH1 ARG A1106    25351  12036  11474  -3517    645    507       N1+
ATOM   2329  NH2 ARG A1106     -16.412  -9.322  -2.005  1.00128.94           N  
ANISOU 2329  NH2 ARG A1106    25469  12022  11499  -4365   1105    657       N  
ATOM   2330  N   GLU A1107     -17.782 -14.990  -5.609  1.00107.96           N  
ANISOU 2330  N   GLU A1107    20635  11035   9349  -2936   1559    615       N  
ATOM   2331  CA  GLU A1107     -17.904 -14.888  -7.074  1.00109.73           C  
ANISOU 2331  CA  GLU A1107    21182  11208   9302  -2912   1772    678       C  
ATOM   2332  C   GLU A1107     -18.530 -16.178  -7.610  1.00109.52           C  
ANISOU 2332  C   GLU A1107    20789  11485   9338  -2559   1779    573       C  
ATOM   2333  O   GLU A1107     -19.402 -16.130  -8.478  1.00109.07           O  
ANISOU 2333  O   GLU A1107    21046  11406   8991  -2274   1740    576       O  
ATOM   2334  CB  GLU A1107     -16.521 -14.690  -7.725  1.00114.89           C  
ANISOU 2334  CB  GLU A1107    21770  11893   9989  -3460   2131    738       C  
ATOM   2335  CG  GLU A1107     -15.965 -13.284  -7.631  1.00132.20           C  
ANISOU 2335  CG  GLU A1107    24515  13722  11993  -3910   2204    851       C  
ATOM   2336  CD  GLU A1107     -16.398 -12.396  -8.776  1.00162.64           C  
ANISOU 2336  CD  GLU A1107    29193  17223  15381  -3877   2322    998       C  
ATOM   2337  OE1 GLU A1107     -15.935 -12.622  -9.919  1.00159.83           O  
ANISOU 2337  OE1 GLU A1107    28866  16968  14894  -4056   2636   1046       O  
ATOM   2338  OE2 GLU A1107     -17.210 -11.476  -8.528  1.00160.06           O1-
ANISOU 2338  OE2 GLU A1107    29510  16513  14794  -3633   2102   1066       O1-
ATOM   2339  N   LEU A1108     -18.089 -17.326  -7.053  1.00103.07           N  
ANISOU 2339  N   LEU A1108    19336  10943   8883  -2575   1810    475       N  
ATOM   2340  CA  LEU A1108     -18.545 -18.667  -7.388  1.00100.20           C  
ANISOU 2340  CA  LEU A1108    18621  10820   8629  -2314   1840    352       C  
ATOM   2341  C   LEU A1108     -20.005 -18.875  -7.012  1.00100.66           C  
ANISOU 2341  C   LEU A1108    18758  10902   8585  -1924   1561    274       C  
ATOM   2342  O   LEU A1108     -20.750 -19.424  -7.821  1.00100.20           O  
ANISOU 2342  O   LEU A1108    18732  10963   8377  -1724   1570    187       O  
ATOM   2343  CB  LEU A1108     -17.674 -19.723  -6.675  1.00 99.27           C  
ANISOU 2343  CB  LEU A1108    17898  10907   8914  -2396   1915    293       C  
ATOM   2344  CG  LEU A1108     -16.266 -19.981  -7.219  1.00106.66           C  
ANISOU 2344  CG  LEU A1108    18543  11988   9996  -2681   2238    301       C  
ATOM   2345  CD1 LEU A1108     -15.370 -20.591  -6.152  1.00105.87           C  
ANISOU 2345  CD1 LEU A1108    17891  12070  10266  -2727   2194    280       C  
ATOM   2346  CD2 LEU A1108     -16.300 -20.889  -8.443  1.00111.15           C  
ANISOU 2346  CD2 LEU A1108    19060  12674  10496  -2560   2497    209       C  
ATOM   2347  N   TYR A1109     -20.412 -18.454  -5.793  1.00 95.30           N  
ANISOU 2347  N   TYR A1109    18088  10149   7971  -1836   1323    283       N  
ATOM   2348  CA  TYR A1109     -21.776 -18.647  -5.282  1.00 93.67           C  
ANISOU 2348  CA  TYR A1109    17874  10030   7687  -1486   1086    190       C  
ATOM   2349  C   TYR A1109     -22.868 -17.921  -6.076  1.00 98.33           C  
ANISOU 2349  C   TYR A1109    18884  10585   7893  -1188    962    183       C  
ATOM   2350  O   TYR A1109     -23.972 -18.451  -6.222  1.00 97.12           O  
ANISOU 2350  O   TYR A1109    18591  10657   7654   -916    843     55       O  
ATOM   2351  CB  TYR A1109     -21.892 -18.267  -3.796  1.00 94.37           C  
ANISOU 2351  CB  TYR A1109    17916  10051   7891  -1464    896    198       C  
ATOM   2352  CG  TYR A1109     -21.153 -19.110  -2.775  1.00 94.70           C  
ANISOU 2352  CG  TYR A1109    17522  10191   8267  -1626    915    192       C  
ATOM   2353  CD1 TYR A1109     -21.157 -20.501  -2.852  1.00 95.13           C  
ANISOU 2353  CD1 TYR A1109    17201  10430   8515  -1583   1010    122       C  
ATOM   2354  CD2 TYR A1109     -20.585 -18.527  -1.645  1.00 95.98           C  
ANISOU 2354  CD2 TYR A1109    17699  10252   8516  -1778    801    244       C  
ATOM   2355  CE1 TYR A1109     -20.541 -21.283  -1.871  1.00 95.06           C  
ANISOU 2355  CE1 TYR A1109    16862  10482   8773  -1648    999    140       C  
ATOM   2356  CE2 TYR A1109     -19.983 -19.298  -0.652  1.00 95.83           C  
ANISOU 2356  CE2 TYR A1109    17301  10355   8756  -1861    763    247       C  
ATOM   2357  CZ  TYR A1109     -19.965 -20.675  -0.766  1.00100.02           C  
ANISOU 2357  CZ  TYR A1109    17482  11051   9469  -1768    859    210       C  
ATOM   2358  OH  TYR A1109     -19.344 -21.413   0.210  1.00 98.27           O  
ANISOU 2358  OH  TYR A1109    16956  10915   9468  -1792    807    242       O  
ATOM   2359  N   GLY A1110     -22.561 -16.717  -6.548  1.00 97.29           N  
ANISOU 2359  N   GLY A1110    19266  10181   7520  -1243    984    316       N  
ATOM   2360  CA  GLY A1110     -23.486 -15.909  -7.337  1.00 99.73           C  
ANISOU 2360  CA  GLY A1110    20070  10405   7417   -903    852    351       C  
ATOM   2361  C   GLY A1110     -23.475 -16.235  -8.822  1.00106.09           C  
ANISOU 2361  C   GLY A1110    21001  11312   7995   -899    988    361       C  
ATOM   2362  O   GLY A1110     -24.022 -15.475  -9.627  1.00109.03           O  
ANISOU 2362  O   GLY A1110    21874  11581   7973   -646    895    435       O  
ATOM   2363  N   SER A1111     -22.854 -17.367  -9.200  1.00100.76           N  
ANISOU 2363  N   SER A1111    19915  10831   7537  -1144   1206    284       N  
ATOM   2364  CA  SER A1111     -22.757 -17.821 -10.585  1.00102.07           C  
ANISOU 2364  CA  SER A1111    20170  11114   7496  -1177   1376    256       C  
ATOM   2365  C   SER A1111     -23.326 -19.237 -10.732  1.00106.03           C  
ANISOU 2365  C   SER A1111    20201  11953   8132  -1083   1358     34       C  
ATOM   2366  O   SER A1111     -24.080 -19.499 -11.681  1.00107.38           O  
ANISOU 2366  O   SER A1111    20478  12306   8015   -901   1285    -64       O  
ATOM   2367  CB  SER A1111     -21.305 -17.811 -11.046  1.00105.06           C  
ANISOU 2367  CB  SER A1111    20567  11374   7975  -1607   1739    353       C  
ATOM   2368  OG  SER A1111     -20.690 -16.551 -10.855  1.00113.81           O  
ANISOU 2368  OG  SER A1111    22100  12162   8982  -1821   1793    540       O  
ATOM   2369  N   VAL A1112     -22.948 -20.153  -9.797  1.00 99.43           N  
ANISOU 2369  N   VAL A1112    18885  11186   7707  -1222   1422    -47       N  
ATOM   2370  CA  VAL A1112     -23.371 -21.557  -9.811  1.00 97.23           C  
ANISOU 2370  CA  VAL A1112    18224  11134   7586  -1202   1450   -250       C  
ATOM   2371  C   VAL A1112     -24.857 -21.684  -9.457  1.00 98.59           C  
ANISOU 2371  C   VAL A1112    18300  11523   7637   -945   1161   -391       C  
ATOM   2372  O   VAL A1112     -25.347 -20.951  -8.598  1.00 97.81           O  
ANISOU 2372  O   VAL A1112    18242  11394   7527   -788    962   -335       O  
ATOM   2373  CB  VAL A1112     -22.459 -22.513  -8.973  1.00 99.52           C  
ANISOU 2373  CB  VAL A1112    18119  11384   8311  -1389   1620   -266       C  
ATOM   2374  CG1 VAL A1112     -21.022 -22.518  -9.496  1.00100.69           C  
ANISOU 2374  CG1 VAL A1112    18252  11443   8562  -1611   1927   -180       C  
ATOM   2375  CG2 VAL A1112     -22.497 -22.196  -7.474  1.00 97.39           C  
ANISOU 2375  CG2 VAL A1112    17702  11045   8256  -1370   1447   -190       C  
ATOM   2376  N   ASP A1113     -25.569 -22.589 -10.149  1.00 94.40           N  
ANISOU 2376  N   ASP A1113    17640  11233   6994   -919   1150   -596       N  
ATOM   2377  CA  ASP A1113     -26.994 -22.859  -9.934  1.00 93.88           C  
ANISOU 2377  CA  ASP A1113    17384  11480   6806   -747    904   -784       C  
ATOM   2378  C   ASP A1113     -27.195 -23.549  -8.583  1.00 95.22           C  
ANISOU 2378  C   ASP A1113    17199  11670   7312   -851    907   -843       C  
ATOM   2379  O   ASP A1113     -28.123 -23.214  -7.843  1.00 94.72           O  
ANISOU 2379  O   ASP A1113    17004  11778   7206   -691    711   -892       O  
ATOM   2380  CB  ASP A1113     -27.545 -23.775 -11.039  1.00 97.21           C  
ANISOU 2380  CB  ASP A1113    17743  12156   7035   -814    925  -1020       C  
ATOM   2381  CG  ASP A1113     -27.320 -23.285 -12.444  1.00109.01           C  
ANISOU 2381  CG  ASP A1113    19609  13650   8158   -736    948   -976       C  
ATOM   2382  OD1 ASP A1113     -28.167 -22.523 -12.944  1.00113.31           O  
ANISOU 2382  OD1 ASP A1113    20329  14391   8334   -451    685   -978       O  
ATOM   2383  OD2 ASP A1113     -26.303 -23.674 -13.049  1.00111.61           O1-
ANISOU 2383  OD2 ASP A1113    20061  13802   8544   -933   1234   -942       O1-
ATOM   2384  N   PHE A1114     -26.331 -24.539  -8.284  1.00 89.72           N  
ANISOU 2384  N   PHE A1114    16365  10803   6920  -1092   1141   -842       N  
ATOM   2385  CA  PHE A1114     -26.407 -25.350  -7.078  1.00 87.24           C  
ANISOU 2385  CA  PHE A1114    15797  10455   6896  -1204   1176   -874       C  
ATOM   2386  C   PHE A1114     -25.073 -25.506  -6.384  1.00 87.90           C  
ANISOU 2386  C   PHE A1114    15853  10259   7286  -1297   1330   -696       C  
ATOM   2387  O   PHE A1114     -24.019 -25.544  -7.034  1.00 87.97           O  
ANISOU 2387  O   PHE A1114    15937  10139   7350  -1356   1508   -629       O  
ATOM   2388  CB  PHE A1114     -26.988 -26.744  -7.389  1.00 90.07           C  
ANISOU 2388  CB  PHE A1114    16013  10930   7280  -1383   1276  -1113       C  
ATOM   2389  CG  PHE A1114     -28.372 -26.747  -7.997  1.00 93.92           C  
ANISOU 2389  CG  PHE A1114    16419  11795   7472  -1352   1102  -1343       C  
ATOM   2390  CD1 PHE A1114     -28.545 -26.668  -9.377  1.00 98.78           C  
ANISOU 2390  CD1 PHE A1114    17178  12550   7803  -1316   1075  -1456       C  
ATOM   2391  CD2 PHE A1114     -29.500 -26.878  -7.197  1.00 96.76           C  
ANISOU 2391  CD2 PHE A1114    16528  12417   7817  -1371    969  -1465       C  
ATOM   2392  CE1 PHE A1114     -29.821 -26.647  -9.941  1.00102.04           C  
ANISOU 2392  CE1 PHE A1114    17472  13384   7917  -1264    862  -1681       C  
ATOM   2393  CE2 PHE A1114     -30.780 -26.880  -7.764  1.00102.43           C  
ANISOU 2393  CE2 PHE A1114    17075  13582   8261  -1342    792  -1707       C  
ATOM   2394  CZ  PHE A1114     -30.931 -26.752  -9.133  1.00102.40           C  
ANISOU 2394  CZ  PHE A1114    17200  13736   7973  -1275    714  -1813       C  
ATOM   2395  N   VAL A1115     -25.137 -25.606  -5.045  1.00 80.96           N  
ANISOU 2395  N   VAL A1115    14842   9333   6587  -1302   1259   -631       N  
ATOM   2396  CA  VAL A1115     -23.997 -25.845  -4.174  1.00 79.11           C  
ANISOU 2396  CA  VAL A1115    14528   8899   6629  -1358   1337   -476       C  
ATOM   2397  C   VAL A1115     -24.249 -27.184  -3.503  1.00 81.30           C  
ANISOU 2397  C   VAL A1115    14688   9131   7071  -1432   1418   -545       C  
ATOM   2398  O   VAL A1115     -25.329 -27.404  -2.961  1.00 80.59           O  
ANISOU 2398  O   VAL A1115    14553   9163   6905  -1463   1338   -637       O  
ATOM   2399  CB  VAL A1115     -23.667 -24.666  -3.194  1.00 82.08           C  
ANISOU 2399  CB  VAL A1115    14952   9216   7020  -1308   1172   -312       C  
ATOM   2400  CG1 VAL A1115     -24.793 -24.392  -2.205  1.00 81.20           C  
ANISOU 2400  CG1 VAL A1115    14820   9216   6814  -1219    996   -358       C  
ATOM   2401  CG2 VAL A1115     -22.342 -24.886  -2.466  1.00 81.69           C  
ANISOU 2401  CG2 VAL A1115    14779   9030   7229  -1383   1227   -168       C  
ATOM   2402  N   ILE A1116     -23.303 -28.110  -3.635  1.00 78.57           N  
ANISOU 2402  N   ILE A1116    14314   8616   6922  -1455   1600   -518       N  
ATOM   2403  CA  ILE A1116     -23.420 -29.437  -3.033  1.00 78.93           C  
ANISOU 2403  CA  ILE A1116    14364   8518   7109  -1500   1701   -555       C  
ATOM   2404  C   ILE A1116     -22.653 -29.434  -1.722  1.00 83.19           C  
ANISOU 2404  C   ILE A1116    14835   8940   7831  -1410   1623   -350       C  
ATOM   2405  O   ILE A1116     -21.455 -29.138  -1.713  1.00 83.23           O  
ANISOU 2405  O   ILE A1116    14742   8911   7970  -1314   1632   -227       O  
ATOM   2406  CB  ILE A1116     -23.053 -30.606  -3.998  1.00 83.68           C  
ANISOU 2406  CB  ILE A1116    15060   8969   7766  -1523   1948   -687       C  
ATOM   2407  CG1 ILE A1116     -23.972 -30.583  -5.249  1.00 84.99           C  
ANISOU 2407  CG1 ILE A1116    15306   9301   7685  -1647   1976   -919       C  
ATOM   2408  CG2 ILE A1116     -23.169 -31.954  -3.283  1.00 85.22           C  
ANISOU 2408  CG2 ILE A1116    15371   8920   8088  -1561   2056   -702       C  
ATOM   2409  CD1 ILE A1116     -23.423 -31.269  -6.518  1.00 93.35           C  
ANISOU 2409  CD1 ILE A1116    16488  10258   8721  -1647   2212  -1058       C  
ATOM   2410  N   ILE A1117     -23.383 -29.667  -0.606  1.00 80.04           N  
ANISOU 2410  N   ILE A1117    14470   8536   7404  -1461   1535   -323       N  
ATOM   2411  CA  ILE A1117     -22.861 -29.726   0.770  1.00 79.82           C  
ANISOU 2411  CA  ILE A1117    14433   8416   7480  -1381   1431   -135       C  
ATOM   2412  C   ILE A1117     -23.142 -31.164   1.260  1.00 89.21           C  
ANISOU 2412  C   ILE A1117    15791   9387   8719  -1428   1571   -138       C  
ATOM   2413  O   ILE A1117     -24.142 -31.398   1.950  1.00 89.55           O  
ANISOU 2413  O   ILE A1117    15920   9459   8645  -1576   1569   -173       O  
ATOM   2414  CB  ILE A1117     -23.466 -28.623   1.702  1.00 80.20           C  
ANISOU 2414  CB  ILE A1117    14459   8626   7388  -1400   1225    -90       C  
ATOM   2415  CG1 ILE A1117     -23.562 -27.254   1.000  1.00 78.57           C  
ANISOU 2415  CG1 ILE A1117    14220   8570   7063  -1375   1124   -136       C  
ATOM   2416  CG2 ILE A1117     -22.667 -28.502   3.000  1.00 79.61           C  
ANISOU 2416  CG2 ILE A1117    14378   8479   7391  -1313   1085    105       C  
ATOM   2417  CD1 ILE A1117     -24.913 -26.785   0.813  1.00 77.67           C  
ANISOU 2417  CD1 ILE A1117    14127   8646   6737  -1388   1072   -281       C  
ATOM   2418  N   PRO A1118     -22.313 -32.160   0.855  1.00 89.03           N  
ANISOU 2418  N   PRO A1118    15850   9132   8845  -1308   1725   -117       N  
ATOM   2419  CA  PRO A1118     -22.610 -33.550   1.222  1.00 91.46           C  
ANISOU 2419  CA  PRO A1118    16441   9141   9170  -1354   1883   -123       C  
ATOM   2420  C   PRO A1118     -21.923 -34.016   2.511  1.00 97.57           C  
ANISOU 2420  C   PRO A1118    17334   9719  10018  -1148   1799    123       C  
ATOM   2421  O   PRO A1118     -21.194 -35.013   2.498  1.00100.77           O  
ANISOU 2421  O   PRO A1118    17915   9838  10536   -930   1904    194       O  
ATOM   2422  CB  PRO A1118     -22.154 -34.322  -0.025  1.00 94.93           C  
ANISOU 2422  CB  PRO A1118    16969   9410   9688  -1289   2102   -264       C  
ATOM   2423  CG  PRO A1118     -21.036 -33.472  -0.619  1.00 98.06           C  
ANISOU 2423  CG  PRO A1118    17079   9992  10186  -1080   2045   -213       C  
ATOM   2424  CD  PRO A1118     -21.104 -32.096   0.008  1.00 90.98           C  
ANISOU 2424  CD  PRO A1118    15965   9370   9233  -1124   1797   -103       C  
ATOM   2425  N   SER A1119     -22.175 -33.311   3.630  1.00 92.32           N  
ANISOU 2425  N   SER A1119    16609   9205   9262  -1181   1603    248       N  
ATOM   2426  CA  SER A1119     -21.580 -33.645   4.927  1.00 93.43           C  
ANISOU 2426  CA  SER A1119    16877   9212   9409   -989   1474    488       C  
ATOM   2427  C   SER A1119     -22.194 -34.877   5.605  1.00 99.57           C  
ANISOU 2427  C   SER A1119    18086   9660  10085  -1088   1630    552       C  
ATOM   2428  O   SER A1119     -23.378 -35.165   5.427  1.00 98.37           O  
ANISOU 2428  O   SER A1119    18069   9496   9812  -1430   1799    399       O  
ATOM   2429  CB  SER A1119     -21.650 -32.449   5.869  1.00 94.27           C  
ANISOU 2429  CB  SER A1119    16823   9585   9408  -1018   1222    573       C  
ATOM   2430  OG  SER A1119     -20.990 -31.324   5.316  1.00101.12           O  
ANISOU 2430  OG  SER A1119    17376  10687  10357   -962   1090    534       O  
ATOM   2431  N   TYR A1120     -21.361 -35.610   6.370  1.00 99.53           N  
ANISOU 2431  N   TYR A1120    18303   9400  10114   -789   1571    779       N  
ATOM   2432  CA  TYR A1120     -21.753 -36.748   7.209  1.00102.91           C  
ANISOU 2432  CA  TYR A1120    19249   9445  10407   -832   1695    918       C  
ATOM   2433  C   TYR A1120     -22.189 -36.135   8.549  1.00108.66           C  
ANISOU 2433  C   TYR A1120    20003  10357  10927   -944   1525   1059       C  
ATOM   2434  O   TYR A1120     -23.175 -36.564   9.142  1.00109.06           O  
ANISOU 2434  O   TYR A1120    20364  10291  10783  -1248   1682   1066       O  
ATOM   2435  CB  TYR A1120     -20.561 -37.698   7.438  1.00107.54           C  
ANISOU 2435  CB  TYR A1120    20078   9692  11092   -342   1658   1125       C  
ATOM   2436  CG  TYR A1120     -20.370 -38.726   6.347  1.00111.08           C  
ANISOU 2436  CG  TYR A1120    20751   9785  11670   -248   1926    993       C  
ATOM   2437  CD1 TYR A1120     -19.615 -38.436   5.213  1.00112.15           C  
ANISOU 2437  CD1 TYR A1120    20517  10086  12008    -41   1944    849       C  
ATOM   2438  CD2 TYR A1120     -20.929 -39.995   6.453  1.00115.22           C  
ANISOU 2438  CD2 TYR A1120    21904   9786  12089   -387   2186   1004       C  
ATOM   2439  CE1 TYR A1120     -19.434 -39.381   4.204  1.00115.64           C  
ANISOU 2439  CE1 TYR A1120    21196  10201  12541     64   2208    702       C  
ATOM   2440  CE2 TYR A1120     -20.757 -40.948   5.451  1.00118.67           C  
ANISOU 2440  CE2 TYR A1120    22619   9849  12623   -308   2441    854       C  
ATOM   2441  CZ  TYR A1120     -20.009 -40.638   4.327  1.00123.93           C  
ANISOU 2441  CZ  TYR A1120    22896  10706  13487    -59   2447    696       C  
ATOM   2442  OH  TYR A1120     -19.838 -41.585   3.345  1.00124.26           O  
ANISOU 2442  OH  TYR A1120    23244  10373  13595     37   2717    525       O  
ATOM   2443  N   PHE A1121     -21.437 -35.112   9.006  1.00106.31           N  
ANISOU 2443  N   PHE A1121    19378  10361  10655   -729   1221   1150       N  
ATOM   2444  CA  PHE A1121     -21.661 -34.334  10.219  1.00106.55           C  
ANISOU 2444  CA  PHE A1121    19394  10606  10484   -787   1015   1254       C  
ATOM   2445  C   PHE A1121     -21.374 -32.858   9.897  1.00109.71           C  
ANISOU 2445  C   PHE A1121    19333  11400  10953   -801    808   1133       C  
ATOM   2446  O   PHE A1121     -20.296 -32.535   9.383  1.00109.31           O  
ANISOU 2446  O   PHE A1121    18999  11447  11088   -592    674   1142       O  
ATOM   2447  CB  PHE A1121     -20.790 -34.853  11.379  1.00111.99           C  
ANISOU 2447  CB  PHE A1121    20334  11143  11075   -452    811   1549       C  
ATOM   2448  CG  PHE A1121     -21.166 -36.240  11.861  1.00117.80           C  
ANISOU 2448  CG  PHE A1121    21668  11423  11668   -453   1020   1708       C  
ATOM   2449  CD1 PHE A1121     -20.592 -37.376  11.292  1.00123.98           C  
ANISOU 2449  CD1 PHE A1121    22691  11823  12593   -186   1146   1770       C  
ATOM   2450  CD2 PHE A1121     -22.084 -36.411  12.895  1.00121.45           C  
ANISOU 2450  CD2 PHE A1121    22501  11815  11829   -724   1118   1794       C  
ATOM   2451  CE1 PHE A1121     -20.952 -38.659  11.727  1.00128.95           C  
ANISOU 2451  CE1 PHE A1121    23986  11944  13066   -207   1361   1921       C  
ATOM   2452  CE2 PHE A1121     -22.433 -37.695  13.338  1.00128.37           C  
ANISOU 2452  CE2 PHE A1121    24007  12223  12544   -788   1348   1955       C  
ATOM   2453  CZ  PHE A1121     -21.865 -38.809  12.751  1.00129.30           C  
ANISOU 2453  CZ  PHE A1121    24421  11903  12805   -534   1462   2023       C  
ATOM   2454  N   GLU A1122     -22.386 -31.987  10.119  1.00105.63           N  
ANISOU 2454  N   GLU A1122    18756  11100  10281  -1060    821   1000       N  
ATOM   2455  CA  GLU A1122     -22.346 -30.531   9.894  1.00103.25           C  
ANISOU 2455  CA  GLU A1122    18156  11094   9979  -1098    654    879       C  
ATOM   2456  C   GLU A1122     -23.238 -29.819  10.929  1.00105.80           C  
ANISOU 2456  C   GLU A1122    18585  11578  10036  -1231    602    846       C  
ATOM   2457  O   GLU A1122     -24.446 -29.670  10.716  1.00104.57           O  
ANISOU 2457  O   GLU A1122    18425  11530   9776  -1415    777    682       O  
ATOM   2458  CB  GLU A1122     -22.733 -30.159   8.447  1.00102.67           C  
ANISOU 2458  CB  GLU A1122    17873  11106  10030  -1201    792    666       C  
ATOM   2459  CG  GLU A1122     -22.386 -28.734   8.049  1.00111.72           C  
ANISOU 2459  CG  GLU A1122    18794  12458  11198  -1188    623    588       C  
ATOM   2460  CD  GLU A1122     -20.919 -28.381   8.195  1.00138.64           C  
ANISOU 2460  CD  GLU A1122    22045  15894  14739  -1048    419    709       C  
ATOM   2461  OE1 GLU A1122     -20.131 -28.763   7.300  1.00140.64           O1-
ANISOU 2461  OE1 GLU A1122    22138  16111  15189   -963    491    709       O1-
ATOM   2462  OE2 GLU A1122     -20.554 -27.748   9.213  1.00132.23           O  
ANISOU 2462  OE2 GLU A1122    21250  15170  13820  -1034    193    784       O  
ATOM   2463  N   PRO A1123     -22.660 -29.402  12.071  1.00102.63           N  
ANISOU 2463  N   PRO A1123    18265  11228   9503  -1128    362    983       N  
ATOM   2464  CA  PRO A1123     -23.487 -28.811  13.136  1.00102.78           C  
ANISOU 2464  CA  PRO A1123    18442  11380   9231  -1233    343    946       C  
ATOM   2465  C   PRO A1123     -24.070 -27.431  12.859  1.00104.22           C  
ANISOU 2465  C   PRO A1123    18475  11776   9349  -1292    303    733       C  
ATOM   2466  O   PRO A1123     -25.082 -27.078  13.468  1.00104.12           O  
ANISOU 2466  O   PRO A1123    18561  11890   9108  -1366    396    637       O  
ATOM   2467  CB  PRO A1123     -22.552 -28.786  14.352  1.00106.80           C  
ANISOU 2467  CB  PRO A1123    19101  11877   9603  -1086     62   1147       C  
ATOM   2468  CG  PRO A1123     -21.376 -29.639  13.982  1.00112.67           C  
ANISOU 2468  CG  PRO A1123    19774  12473  10563   -875    -31   1312       C  
ATOM   2469  CD  PRO A1123     -21.256 -29.546  12.501  1.00105.92           C  
ANISOU 2469  CD  PRO A1123    18634  11614   9997   -902    101   1167       C  
ATOM   2470  N   PHE A1124     -23.437 -26.651  11.973  1.00 99.30           N  
ANISOU 2470  N   PHE A1124    17646  11183   8901  -1245    184    663       N  
ATOM   2471  CA  PHE A1124     -23.875 -25.287  11.677  1.00 97.85           C  
ANISOU 2471  CA  PHE A1124    17420  11119   8638  -1257    127    489       C  
ATOM   2472  C   PHE A1124     -24.319 -25.093  10.232  1.00 96.41           C  
ANISOU 2472  C   PHE A1124    17078  10963   8590  -1265    266    349       C  
ATOM   2473  O   PHE A1124     -25.407 -24.567  10.002  1.00 94.60           O  
ANISOU 2473  O   PHE A1124    16849  10862   8232  -1242    350    189       O  
ATOM   2474  CB  PHE A1124     -22.790 -24.264  12.084  1.00100.97           C  
ANISOU 2474  CB  PHE A1124    17833  11510   9022  -1249   -158    525       C  
ATOM   2475  CG  PHE A1124     -23.210 -22.812  12.036  1.00102.69           C  
ANISOU 2475  CG  PHE A1124    18166  11756   9096  -1258   -225    361       C  
ATOM   2476  CD1 PHE A1124     -24.077 -22.290  12.989  1.00106.93           C  
ANISOU 2476  CD1 PHE A1124    18915  12358   9355  -1210   -223    268       C  
ATOM   2477  CD2 PHE A1124     -22.724 -21.963  11.049  1.00104.43           C  
ANISOU 2477  CD2 PHE A1124    18333  11913   9433  -1301   -272    302       C  
ATOM   2478  CE1 PHE A1124     -24.462 -20.945  12.946  1.00108.17           C  
ANISOU 2478  CE1 PHE A1124    19243  12491   9365  -1150   -279    109       C  
ATOM   2479  CE2 PHE A1124     -23.116 -20.624  11.003  1.00107.60           C  
ANISOU 2479  CE2 PHE A1124    18949  12259   9675  -1280   -327    168       C  
ATOM   2480  CZ  PHE A1124     -23.976 -20.120  11.955  1.00106.63           C  
ANISOU 2480  CZ  PHE A1124    19052  12175   9287  -1178   -340     68       C  
ATOM   2481  N   GLY A1125     -23.483 -25.509   9.286  1.00 91.40           N  
ANISOU 2481  N   GLY A1125    16303  10239   8185  -1264    284    402       N  
ATOM   2482  CA  GLY A1125     -23.776 -25.384   7.863  1.00 89.65           C  
ANISOU 2482  CA  GLY A1125    15965  10037   8062  -1275    408    283       C  
ATOM   2483  C   GLY A1125     -23.706 -23.952   7.379  1.00 90.93           C  
ANISOU 2483  C   GLY A1125    16163  10228   8159  -1250    298    204       C  
ATOM   2484  O   GLY A1125     -24.646 -23.464   6.743  1.00 89.86           O  
ANISOU 2484  O   GLY A1125    16052  10175   7917  -1191    358     68       O  
ATOM   2485  N   LEU A1126     -22.593 -23.271   7.704  1.00 86.14           N  
ANISOU 2485  N   LEU A1126    15577   9556   7594  -1297    129    285       N  
ATOM   2486  CA  LEU A1126     -22.337 -21.892   7.307  1.00 85.54           C  
ANISOU 2486  CA  LEU A1126    15628   9425   7448  -1343     35    231       C  
ATOM   2487  C   LEU A1126     -22.271 -21.756   5.763  1.00 86.18           C  
ANISOU 2487  C   LEU A1126    15658   9474   7611  -1356    170    192       C  
ATOM   2488  O   LEU A1126     -22.820 -20.793   5.218  1.00 85.56           O  
ANISOU 2488  O   LEU A1126    15774   9348   7384  -1299    165    115       O  
ATOM   2489  CB  LEU A1126     -21.052 -21.379   7.990  1.00 87.39           C  
ANISOU 2489  CB  LEU A1126    15854   9627   7724  -1494   -158    311       C  
ATOM   2490  CG  LEU A1126     -20.659 -19.917   7.744  1.00 92.98           C  
ANISOU 2490  CG  LEU A1126    16771  10218   8340  -1644   -250    255       C  
ATOM   2491  CD1 LEU A1126     -21.485 -18.980   8.563  1.00 93.05           C  
ANISOU 2491  CD1 LEU A1126    17124  10145   8085  -1562   -347    158       C  
ATOM   2492  CD2 LEU A1126     -19.190 -19.691   8.027  1.00 98.27           C  
ANISOU 2492  CD2 LEU A1126    17282  10931   9126  -1893   -388    316       C  
ATOM   2493  N   VAL A1127     -21.645 -22.753   5.076  1.00 80.59           N  
ANISOU 2493  N   VAL A1127    14731   8783   7106  -1392    295    244       N  
ATOM   2494  CA  VAL A1127     -21.500 -22.872   3.612  1.00 78.96           C  
ANISOU 2494  CA  VAL A1127    14468   8567   6968  -1412    457    206       C  
ATOM   2495  C   VAL A1127     -22.876 -22.786   2.948  1.00 80.83           C  
ANISOU 2495  C   VAL A1127    14816   8860   7036  -1297    525     77       C  
ATOM   2496  O   VAL A1127     -23.012 -22.095   1.949  1.00 81.69           O  
ANISOU 2496  O   VAL A1127    15046   8947   7045  -1279    553     38       O  
ATOM   2497  CB  VAL A1127     -20.731 -24.169   3.201  1.00 82.94           C  
ANISOU 2497  CB  VAL A1127    14735   9081   7698  -1407    600    254       C  
ATOM   2498  CG1 VAL A1127     -20.731 -24.392   1.689  1.00 81.88           C  
ANISOU 2498  CG1 VAL A1127    14578   8946   7588  -1418    798    181       C  
ATOM   2499  CG2 VAL A1127     -19.304 -24.164   3.747  1.00 84.81           C  
ANISOU 2499  CG2 VAL A1127    14780   9351   8093  -1463    506    366       C  
ATOM   2500  N   ALA A1128     -23.891 -23.464   3.512  1.00 75.66           N  
ANISOU 2500  N   ALA A1128    14119   8305   6324  -1230    548     11       N  
ATOM   2501  CA  ALA A1128     -25.266 -23.424   3.016  1.00 74.74           C  
ANISOU 2501  CA  ALA A1128    14008   8351   6040  -1132    589   -146       C  
ATOM   2502  C   ALA A1128     -25.835 -21.996   3.145  1.00 78.42           C  
ANISOU 2502  C   ALA A1128    14668   8843   6287   -960    447   -194       C  
ATOM   2503  O   ALA A1128     -26.396 -21.466   2.189  1.00 78.06           O  
ANISOU 2503  O   ALA A1128    14695   8863   6100   -823    432   -272       O  
ATOM   2504  CB  ALA A1128     -26.128 -24.403   3.797  1.00 75.49           C  
ANISOU 2504  CB  ALA A1128    13994   8571   6118  -1176    666   -208       C  
ATOM   2505  N   LEU A1129     -25.640 -21.360   4.309  1.00 74.62           N  
ANISOU 2505  N   LEU A1129    14316   8286   5751   -941    333   -147       N  
ATOM   2506  CA  LEU A1129     -26.161 -20.024   4.563  1.00 74.69           C  
ANISOU 2506  CA  LEU A1129    14584   8257   5539   -747    212   -206       C  
ATOM   2507  C   LEU A1129     -25.527 -18.973   3.680  1.00 80.30           C  
ANISOU 2507  C   LEU A1129    15568   8744   6199   -751    163   -150       C  
ATOM   2508  O   LEU A1129     -26.254 -18.267   2.979  1.00 81.82           O  
ANISOU 2508  O   LEU A1129    15941   8945   6201   -515    131   -215       O  
ATOM   2509  CB  LEU A1129     -26.073 -19.650   6.048  1.00 74.51           C  
ANISOU 2509  CB  LEU A1129    14681   8186   5445   -754    118   -194       C  
ATOM   2510  CG  LEU A1129     -26.990 -20.435   6.984  1.00 77.78           C  
ANISOU 2510  CG  LEU A1129    14922   8832   5800   -713    192   -265       C  
ATOM   2511  CD1 LEU A1129     -26.426 -20.477   8.389  1.00 77.55           C  
ANISOU 2511  CD1 LEU A1129    14993   8723   5750   -824    117   -185       C  
ATOM   2512  CD2 LEU A1129     -28.409 -19.884   6.969  1.00 80.86           C  
ANISOU 2512  CD2 LEU A1129    15310   9448   5964   -424    211   -448       C  
ATOM   2513  N   GLU A1130     -24.185 -18.897   3.665  1.00 75.73           N  
ANISOU 2513  N   GLU A1130    15013   7990   5772  -1015    164    -29       N  
ATOM   2514  CA  GLU A1130     -23.458 -17.916   2.859  1.00 75.88           C  
ANISOU 2514  CA  GLU A1130    15307   7785   5738  -1131    166     34       C  
ATOM   2515  C   GLU A1130     -23.670 -18.126   1.324  1.00 78.00           C  
ANISOU 2515  C   GLU A1130    15573   8095   5970  -1069    292     33       C  
ATOM   2516  O   GLU A1130     -23.657 -17.141   0.580  1.00 79.15           O  
ANISOU 2516  O   GLU A1130    16077   8060   5936  -1028    288     65       O  
ATOM   2517  CB  GLU A1130     -21.969 -17.839   3.274  1.00 77.71           C  
ANISOU 2517  CB  GLU A1130    15463   7919   6143  -1485    151    131       C  
ATOM   2518  CG  GLU A1130     -21.126 -19.068   2.976  1.00 86.70           C  
ANISOU 2518  CG  GLU A1130    16178   9215   7548  -1626    265    190       C  
ATOM   2519  CD  GLU A1130     -19.860 -19.240   3.794  1.00108.48           C  
ANISOU 2519  CD  GLU A1130    18719  12020  10478  -1859    184    257       C  
ATOM   2520  OE1 GLU A1130     -19.726 -18.572   4.844  1.00 89.50           O1-
ANISOU 2520  OE1 GLU A1130    16464   9557   7986  -1938     10    247       O1-
ATOM   2521  OE2 GLU A1130     -19.005 -20.063   3.389  1.00111.60           O  
ANISOU 2521  OE2 GLU A1130    18786  12536  11082  -1936    286    306       O  
ATOM   2522  N   ALA A1131     -23.941 -19.384   0.883  1.00 72.04           N  
ANISOU 2522  N   ALA A1131    14482   7552   5339  -1053    400    -12       N  
ATOM   2523  CA  ALA A1131     -24.213 -19.745  -0.518  1.00 71.83           C  
ANISOU 2523  CA  ALA A1131    14433   7608   5252  -1002    511    -50       C  
ATOM   2524  C   ALA A1131     -25.610 -19.317  -0.925  1.00 77.07           C  
ANISOU 2524  C   ALA A1131    15222   8412   5648   -681    410   -163       C  
ATOM   2525  O   ALA A1131     -25.781 -18.778  -2.010  1.00 77.45           O  
ANISOU 2525  O   ALA A1131    15499   8422   5504   -568    405   -152       O  
ATOM   2526  CB  ALA A1131     -24.060 -21.242  -0.723  1.00 71.23           C  
ANISOU 2526  CB  ALA A1131    14007   7676   5380  -1105    653    -94       C  
ATOM   2527  N   MET A1132     -26.604 -19.559  -0.046  1.00 75.69           N  
ANISOU 2527  N   MET A1132    14886   8433   5441   -521    333   -272       N  
ATOM   2528  CA  MET A1132     -28.021 -19.212  -0.210  1.00 77.55           C  
ANISOU 2528  CA  MET A1132    15108   8920   5435   -177    225   -419       C  
ATOM   2529  C   MET A1132     -28.234 -17.703  -0.279  1.00 86.01           C  
ANISOU 2529  C   MET A1132    16622   9802   6255    130     82   -378       C  
ATOM   2530  O   MET A1132     -29.194 -17.263  -0.905  1.00 88.01           O  
ANISOU 2530  O   MET A1132    16948  10226   6267    488    -23   -462       O  
ATOM   2531  CB  MET A1132     -28.847 -19.791   0.951  1.00 79.25           C  
ANISOU 2531  CB  MET A1132    15029   9391   5693   -151    230   -539       C  
ATOM   2532  CG  MET A1132     -29.262 -21.229   0.743  1.00 81.78           C  
ANISOU 2532  CG  MET A1132    14969   9970   6133   -355    358   -646       C  
ATOM   2533  SD  MET A1132     -29.737 -22.071   2.277  1.00 84.87           S  
ANISOU 2533  SD  MET A1132    15117  10512   6619   -511    451   -702       S  
ATOM   2534  CE  MET A1132     -31.374 -21.411   2.517  1.00 83.83           C  
ANISOU 2534  CE  MET A1132    14822  10817   6212   -162    365   -921       C  
ATOM   2535  N   CYS A1133     -27.352 -16.917   0.370  1.00 84.95           N  
ANISOU 2535  N   CYS A1133    16802   9317   6159      0     65   -260       N  
ATOM   2536  CA  CYS A1133     -27.404 -15.453   0.397  1.00 88.82           C  
ANISOU 2536  CA  CYS A1133    17838   9500   6409    228    -43   -215       C  
ATOM   2537  C   CYS A1133     -27.141 -14.868  -0.989  1.00 95.98           C  
ANISOU 2537  C   CYS A1133    19116  10213   7141    276    -28   -111       C  
ATOM   2538  O   CYS A1133     -27.749 -13.862  -1.356  1.00 97.94           O  
ANISOU 2538  O   CYS A1133    19794  10323   7095    660   -141   -105       O  
ATOM   2539  CB  CYS A1133     -26.428 -14.894   1.429  1.00 89.80           C  
ANISOU 2539  CB  CYS A1133    18192   9301   6625    -51    -50   -142       C  
ATOM   2540  SG  CYS A1133     -26.965 -15.079   3.151  1.00 93.35           S  
ANISOU 2540  SG  CYS A1133    18457   9906   7104     43   -116   -264       S  
ATOM   2541  N   LEU A1134     -26.249 -15.528  -1.755  1.00 93.16           N  
ANISOU 2541  N   LEU A1134    18609   9848   6939    -83    122    -29       N  
ATOM   2542  CA  LEU A1134     -25.820 -15.145  -3.104  1.00 95.15           C  
ANISOU 2542  CA  LEU A1134    19186   9936   7030   -143    201     81       C  
ATOM   2543  C   LEU A1134     -26.657 -15.769  -4.252  1.00100.59           C  
ANISOU 2543  C   LEU A1134    19702  10949   7567     97    180      0       C  
ATOM   2544  O   LEU A1134     -26.520 -15.347  -5.411  1.00103.62           O  
ANISOU 2544  O   LEU A1134    20432  11219   7720    144    211     88       O  
ATOM   2545  CB  LEU A1134     -24.326 -15.440  -3.267  1.00 94.37           C  
ANISOU 2545  CB  LEU A1134    19012   9685   7161   -671    406    192       C  
ATOM   2546  CG  LEU A1134     -23.452 -14.596  -2.344  1.00100.29           C  
ANISOU 2546  CG  LEU A1134    20008  10118   7981   -950    397    266       C  
ATOM   2547  CD1 LEU A1134     -22.224 -15.326  -1.944  1.00 99.22           C  
ANISOU 2547  CD1 LEU A1134    19454  10070   8173  -1392    525    291       C  
ATOM   2548  CD2 LEU A1134     -23.131 -13.239  -2.956  1.00106.34           C  
ANISOU 2548  CD2 LEU A1134    21476  10461   8467  -1014    428    389       C  
ATOM   2549  N   GLY A1135     -27.531 -16.724  -3.919  1.00 94.52           N  
ANISOU 2549  N   GLY A1135    18439  10582   6892    219    126   -172       N  
ATOM   2550  CA  GLY A1135     -28.440 -17.332  -4.883  1.00 94.85           C  
ANISOU 2550  CA  GLY A1135    18267  10995   6777    411     69   -305       C  
ATOM   2551  C   GLY A1135     -28.257 -18.791  -5.242  1.00 96.33           C  
ANISOU 2551  C   GLY A1135    18013  11414   7173    100    222   -409       C  
ATOM   2552  O   GLY A1135     -29.076 -19.318  -5.996  1.00 97.89           O  
ANISOU 2552  O   GLY A1135    18028  11942   7223    214    160   -560       O  
ATOM   2553  N   ALA A1136     -27.195 -19.463  -4.743  1.00 88.81           N  
ANISOU 2553  N   ALA A1136    16903  10299   6541   -276    409   -345       N  
ATOM   2554  CA  ALA A1136     -26.969 -20.883  -5.048  1.00 86.44           C  
ANISOU 2554  CA  ALA A1136    16264  10142   6439   -529    574   -443       C  
ATOM   2555  C   ALA A1136     -27.961 -21.769  -4.278  1.00 88.33           C  
ANISOU 2555  C   ALA A1136    16126  10668   6767   -522    531   -619       C  
ATOM   2556  O   ALA A1136     -28.149 -21.580  -3.081  1.00 87.91           O  
ANISOU 2556  O   ALA A1136    15996  10603   6802   -487    478   -600       O  
ATOM   2557  CB  ALA A1136     -25.530 -21.279  -4.747  1.00 85.76           C  
ANISOU 2557  CB  ALA A1136    16133   9809   6644   -836    770   -315       C  
ATOM   2558  N   ILE A1137     -28.644 -22.677  -4.983  1.00 85.01           N  
ANISOU 2558  N   ILE A1137    15502  10517   6281   -580    559   -804       N  
ATOM   2559  CA  ILE A1137     -29.634 -23.578  -4.398  1.00 84.49           C  
ANISOU 2559  CA  ILE A1137    15086  10746   6268   -671    559   -998       C  
ATOM   2560  C   ILE A1137     -28.907 -24.781  -3.778  1.00 86.20           C  
ANISOU 2560  C   ILE A1137    15201  10756   6796   -999    775   -964       C  
ATOM   2561  O   ILE A1137     -28.292 -25.565  -4.499  1.00 86.51           O  
ANISOU 2561  O   ILE A1137    15282  10666   6922  -1170    930   -983       O  
ATOM   2562  CB  ILE A1137     -30.749 -23.973  -5.413  1.00 89.80           C  
ANISOU 2562  CB  ILE A1137    15587  11833   6701   -634    469  -1245       C  
ATOM   2563  CG1 ILE A1137     -31.587 -22.742  -5.813  1.00 91.79           C  
ANISOU 2563  CG1 ILE A1137    15919  12336   6622   -192    202  -1267       C  
ATOM   2564  CG2 ILE A1137     -31.653 -25.072  -4.831  1.00 91.80           C  
ANISOU 2564  CG2 ILE A1137    15465  12380   7036   -884    536  -1467       C  
ATOM   2565  CD1 ILE A1137     -31.834 -22.614  -7.228  1.00 96.89           C  
ANISOU 2565  CD1 ILE A1137    16685  13145   6982    -71     96  -1338       C  
ATOM   2566  N   PRO A1138     -28.956 -24.947  -2.444  1.00 80.84           N  
ANISOU 2566  N   PRO A1138    14425  10029   6260  -1054    791   -912       N  
ATOM   2567  CA  PRO A1138     -28.220 -26.056  -1.833  1.00 79.52           C  
ANISOU 2567  CA  PRO A1138    14233   9628   6352  -1295    970   -842       C  
ATOM   2568  C   PRO A1138     -28.761 -27.460  -2.094  1.00 85.08           C  
ANISOU 2568  C   PRO A1138    14826  10408   7093  -1555   1127  -1022       C  
ATOM   2569  O   PRO A1138     -29.972 -27.680  -2.170  1.00 87.08           O  
ANISOU 2569  O   PRO A1138    14903  10986   7199  -1636   1096  -1226       O  
ATOM   2570  CB  PRO A1138     -28.254 -25.712  -0.349  1.00 80.09           C  
ANISOU 2570  CB  PRO A1138    14291   9661   6480  -1253    911   -735       C  
ATOM   2571  CG  PRO A1138     -29.483 -24.915  -0.184  1.00 85.34           C  
ANISOU 2571  CG  PRO A1138    14858  10648   6917  -1067    770   -863       C  
ATOM   2572  CD  PRO A1138     -29.608 -24.107  -1.419  1.00 81.88           C  
ANISOU 2572  CD  PRO A1138    14519  10292   6300   -861    654   -902       C  
ATOM   2573  N   ILE A1139     -27.829 -28.403  -2.247  1.00 80.09           N  
ANISOU 2573  N   ILE A1139    14302   9478   6652  -1686   1302   -959       N  
ATOM   2574  CA  ILE A1139     -28.078 -29.829  -2.323  1.00 81.24           C  
ANISOU 2574  CA  ILE A1139    14475   9526   6867  -1946   1492  -1090       C  
ATOM   2575  C   ILE A1139     -27.253 -30.312  -1.130  1.00 84.59           C  
ANISOU 2575  C   ILE A1139    15003   9635   7502  -1936   1566   -877       C  
ATOM   2576  O   ILE A1139     -26.026 -30.388  -1.218  1.00 84.50           O  
ANISOU 2576  O   ILE A1139    15075   9379   7651  -1804   1610   -724       O  
ATOM   2577  CB  ILE A1139     -27.666 -30.517  -3.657  1.00 85.74           C  
ANISOU 2577  CB  ILE A1139    15164   9980   7433  -2020   1633  -1216       C  
ATOM   2578  CG1 ILE A1139     -28.160 -29.735  -4.901  1.00 86.78           C  
ANISOU 2578  CG1 ILE A1139    15247  10411   7315  -1932   1504  -1353       C  
ATOM   2579  CG2 ILE A1139     -28.179 -31.974  -3.664  1.00 88.95           C  
ANISOU 2579  CG2 ILE A1139    15662  10271   7863  -2339   1825  -1402       C  
ATOM   2580  CD1 ILE A1139     -27.664 -30.283  -6.275  1.00 90.44           C  
ANISOU 2580  CD1 ILE A1139    15868  10771   7722  -1985   1648  -1473       C  
ATOM   2581  N   ALA A1140     -27.900 -30.509   0.019  1.00 80.41           N  
ANISOU 2581  N   ALA A1140    14446   9161   6947  -2042   1562   -856       N  
ATOM   2582  CA  ALA A1140     -27.164 -30.905   1.211  1.00 80.24           C  
ANISOU 2582  CA  ALA A1140    14562   8862   7065  -1999   1593   -634       C  
ATOM   2583  C   ALA A1140     -27.705 -32.166   1.850  1.00 87.86           C  
ANISOU 2583  C   ALA A1140    15686   9674   8023  -2267   1779   -669       C  
ATOM   2584  O   ALA A1140     -28.824 -32.579   1.548  1.00 89.31           O  
ANISOU 2584  O   ALA A1140    15805  10046   8082  -2548   1877   -890       O  
ATOM   2585  CB  ALA A1140     -27.142 -29.766   2.219  1.00 79.31           C  
ANISOU 2585  CB  ALA A1140    14369   8875   6891  -1838   1404   -500       C  
ATOM   2586  N   SER A1141     -26.902 -32.791   2.722  1.00 85.47           N  
ANISOU 2586  N   SER A1141    15606   9036   7833  -2190   1826   -453       N  
ATOM   2587  CA  SER A1141     -27.330 -33.968   3.470  1.00 88.32           C  
ANISOU 2587  CA  SER A1141    16239   9163   8154  -2432   2014   -426       C  
ATOM   2588  C   SER A1141     -28.216 -33.477   4.636  1.00 92.02           C  
ANISOU 2588  C   SER A1141    16624   9887   8453  -2561   1973   -401       C  
ATOM   2589  O   SER A1141     -27.924 -32.425   5.212  1.00 89.66           O  
ANISOU 2589  O   SER A1141    16191   9746   8130  -2331   1775   -288       O  
ATOM   2590  CB  SER A1141     -26.125 -34.741   3.997  1.00 93.34           C  
ANISOU 2590  CB  SER A1141    17180   9354   8930  -2207   2044   -176       C  
ATOM   2591  OG  SER A1141     -25.271 -35.187   2.954  1.00102.72           O  
ANISOU 2591  OG  SER A1141    18421  10336  10273  -2035   2110   -214       O  
ATOM   2592  N   ALA A1142     -29.320 -34.199   4.946  1.00 90.47           N  
ANISOU 2592  N   ALA A1142    16502   9752   8121  -2958   2179   -536       N  
ATOM   2593  CA  ALA A1142     -30.241 -33.848   6.035  1.00 90.68           C  
ANISOU 2593  CA  ALA A1142    16433  10059   7962  -3119   2213   -544       C  
ATOM   2594  C   ALA A1142     -29.538 -34.225   7.348  1.00 96.09           C  
ANISOU 2594  C   ALA A1142    17485  10397   8626  -3013   2221   -232       C  
ATOM   2595  O   ALA A1142     -29.824 -35.259   7.960  1.00 98.85           O  
ANISOU 2595  O   ALA A1142    18177  10494   8887  -3295   2445   -163       O  
ATOM   2596  CB  ALA A1142     -31.561 -34.595   5.869  1.00 94.49           C  
ANISOU 2596  CB  ALA A1142    16853  10740   8308  -3641   2469   -802       C  
ATOM   2597  N   VAL A1143     -28.548 -33.393   7.724  1.00 90.34           N  
ANISOU 2597  N   VAL A1143    16719   9641   7967  -2610   1965    -40       N  
ATOM   2598  CA  VAL A1143     -27.640 -33.577   8.851  1.00 90.53           C  
ANISOU 2598  CA  VAL A1143    17031   9393   7973  -2402   1866    261       C  
ATOM   2599  C   VAL A1143     -27.432 -32.257   9.583  1.00 93.12           C  
ANISOU 2599  C   VAL A1143    17181   9986   8216  -2178   1615    324       C  
ATOM   2600  O   VAL A1143     -27.194 -31.233   8.941  1.00 90.29           O  
ANISOU 2600  O   VAL A1143    16548   9820   7939  -2009   1445    232       O  
ATOM   2601  CB  VAL A1143     -26.304 -34.176   8.316  1.00 94.24           C  
ANISOU 2601  CB  VAL A1143    17652   9492   8664  -2124   1800    409       C  
ATOM   2602  CG1 VAL A1143     -25.108 -33.805   9.180  1.00 94.05           C  
ANISOU 2602  CG1 VAL A1143    17680   9388   8665  -1760   1539    675       C  
ATOM   2603  CG2 VAL A1143     -26.402 -35.684   8.153  1.00 97.24           C  
ANISOU 2603  CG2 VAL A1143    18443   9447   9055  -2300   2063    433       C  
ATOM   2604  N   GLY A1144     -27.503 -32.322  10.917  1.00 92.06           N  
ANISOU 2604  N   GLY A1144    17270   9818   7889  -2194   1607    482       N  
ATOM   2605  CA  GLY A1144     -27.292 -31.216  11.845  1.00 90.94           C  
ANISOU 2605  CA  GLY A1144    17076   9868   7609  -2013   1384    547       C  
ATOM   2606  C   GLY A1144     -27.938 -29.907  11.454  1.00 93.58           C  
ANISOU 2606  C   GLY A1144    17080  10573   7903  -1966   1307    319       C  
ATOM   2607  O   GLY A1144     -29.163 -29.833  11.310  1.00 94.60           O  
ANISOU 2607  O   GLY A1144    17056  10972   7917  -2147   1487    115       O  
ATOM   2608  N   GLY A1145     -27.087 -28.899  11.256  1.00 87.85           N  
ANISOU 2608  N   GLY A1145    16253   9861   7266  -1721   1040    351       N  
ATOM   2609  CA  GLY A1145     -27.453 -27.534  10.884  1.00 85.72           C  
ANISOU 2609  CA  GLY A1145    15789   9831   6951  -1602    922    180       C  
ATOM   2610  C   GLY A1145     -28.118 -27.363   9.533  1.00 86.98           C  
ANISOU 2610  C   GLY A1145    15708  10147   7194  -1622   1007    -27       C  
ATOM   2611  O   GLY A1145     -28.889 -26.421   9.351  1.00 85.36           O  
ANISOU 2611  O   GLY A1145    15373  10191   6867  -1519    973   -195       O  
ATOM   2612  N   LEU A1146     -27.833 -28.273   8.579  1.00 83.57           N  
ANISOU 2612  N   LEU A1146    15240   9571   6940  -1719   1110    -23       N  
ATOM   2613  CA  LEU A1146     -28.391 -28.268   7.212  1.00 82.27           C  
ANISOU 2613  CA  LEU A1146    14876   9550   6831  -1762   1180   -220       C  
ATOM   2614  C   LEU A1146     -29.880 -28.644   7.220  1.00 87.67           C  
ANISOU 2614  C   LEU A1146    15406  10543   7361  -1974   1366   -437       C  
ATOM   2615  O   LEU A1146     -30.647 -28.152   6.391  1.00 85.76           O  
ANISOU 2615  O   LEU A1146    14931  10597   7059  -1927   1342   -642       O  
ATOM   2616  CB  LEU A1146     -27.599 -29.222   6.295  1.00 81.71           C  
ANISOU 2616  CB  LEU A1146    14863   9215   6969  -1817   1258   -168       C  
ATOM   2617  CG  LEU A1146     -26.078 -29.050   6.279  1.00 84.85           C  
ANISOU 2617  CG  LEU A1146    15330   9373   7537  -1625   1116     30       C  
ATOM   2618  CD1 LEU A1146     -25.387 -30.342   5.913  1.00 85.60           C  
ANISOU 2618  CD1 LEU A1146    15544   9182   7797  -1646   1251    110       C  
ATOM   2619  CD2 LEU A1146     -25.659 -27.914   5.365  1.00 86.71           C  
ANISOU 2619  CD2 LEU A1146    15433   9701   7812  -1492    983    -21       C  
ATOM   2620  N   ARG A1147     -30.280 -29.491   8.187  1.00 87.77           N  
ANISOU 2620  N   ARG A1147    15548  10514   7285  -2210   1548   -389       N  
ATOM   2621  CA  ARG A1147     -31.651 -29.948   8.391  1.00 90.91           C  
ANISOU 2621  CA  ARG A1147    15788  11230   7523  -2510   1776   -590       C  
ATOM   2622  C   ARG A1147     -32.525 -28.809   8.954  1.00 96.84           C  
ANISOU 2622  C   ARG A1147    16307  12415   8072  -2335   1720   -729       C  
ATOM   2623  O   ARG A1147     -33.737 -28.789   8.731  1.00 99.27           O  
ANISOU 2623  O   ARG A1147    16297  13161   8260  -2461   1842   -978       O  
ATOM   2624  CB  ARG A1147     -31.651 -31.147   9.349  1.00 93.98           C  
ANISOU 2624  CB  ARG A1147    16491  11366   7850  -2826   2009   -446       C  
ATOM   2625  CG  ARG A1147     -32.804 -32.104   9.114  1.00111.76           C  
ANISOU 2625  CG  ARG A1147    18646  13799  10019  -3308   2314   -656       C  
ATOM   2626  CD  ARG A1147     -32.712 -33.317  10.013  1.00131.02           C  
ANISOU 2626  CD  ARG A1147    21527  15875  12378  -3643   2568   -478       C  
ATOM   2627  NE  ARG A1147     -33.739 -34.309   9.688  1.00149.88           N  
ANISOU 2627  NE  ARG A1147    23877  18373  14696  -4205   2888   -691       N  
ATOM   2628  CZ  ARG A1147     -34.899 -34.432  10.328  1.00173.11           C  
ANISOU 2628  CZ  ARG A1147    26659  21693  17424  -4587   3142   -842       C  
ATOM   2629  NH1 ARG A1147     -35.196 -33.627  11.343  1.00159.66           N1+
ANISOU 2629  NH1 ARG A1147    24840  20280  15543  -4414   3124   -800       N1+
ATOM   2630  NH2 ARG A1147     -35.768 -35.366   9.964  1.00166.96           N  
ANISOU 2630  NH2 ARG A1147    25832  21015  16589  -5174   3436  -1056       N  
ATOM   2631  N   ASP A1148     -31.897 -27.865   9.673  1.00 92.07           N  
ANISOU 2631  N   ASP A1148    15856  11705   7421  -2037   1533   -589       N  
ATOM   2632  CA  ASP A1148     -32.527 -26.712  10.316  1.00 92.74           C  
ANISOU 2632  CA  ASP A1148    15841  12092   7303  -1796   1470   -701       C  
ATOM   2633  C   ASP A1148     -32.792 -25.564   9.346  1.00 94.74           C  
ANISOU 2633  C   ASP A1148    15901  12538   7558  -1456   1282   -858       C  
ATOM   2634  O   ASP A1148     -33.889 -25.007   9.342  1.00 95.46           O  
ANISOU 2634  O   ASP A1148    15738  13047   7486  -1302   1318  -1077       O  
ATOM   2635  CB  ASP A1148     -31.624 -26.236  11.468  1.00 94.68           C  
ANISOU 2635  CB  ASP A1148    16423  12071   7481  -1657   1333   -491       C  
ATOM   2636  CG  ASP A1148     -32.248 -25.281  12.464  1.00110.45           C  
ANISOU 2636  CG  ASP A1148    18441  14309   9216  -1471   1334   -595       C  
ATOM   2637  OD1 ASP A1148     -33.499 -25.226  12.537  1.00114.73           O  
ANISOU 2637  OD1 ASP A1148    18716  15269   9608  -1490   1520   -816       O  
ATOM   2638  OD2 ASP A1148     -31.486 -24.606  13.188  1.00115.39           O1-
ANISOU 2638  OD2 ASP A1148    19337  14731   9774  -1314   1155   -476       O1-
ATOM   2639  N   ILE A1149     -31.779 -25.209   8.539  1.00 89.92           N  
ANISOU 2639  N   ILE A1149    15422  11631   7111  -1320   1092   -743       N  
ATOM   2640  CA  ILE A1149     -31.801 -24.130   7.548  1.00 89.83           C  
ANISOU 2640  CA  ILE A1149    15366  11677   7088  -1011    908   -825       C  
ATOM   2641  C   ILE A1149     -32.750 -24.417   6.363  1.00 97.25           C  
ANISOU 2641  C   ILE A1149    15987  12960   8003  -1021    953  -1039       C  
ATOM   2642  O   ILE A1149     -33.765 -23.737   6.200  1.00 99.02           O  
ANISOU 2642  O   ILE A1149    16005  13563   8054   -770    906  -1230       O  
ATOM   2643  CB  ILE A1149     -30.349 -23.845   7.049  1.00 90.40           C  
ANISOU 2643  CB  ILE A1149    15680  11331   7337   -979    754   -625       C  
ATOM   2644  CG1 ILE A1149     -29.416 -23.415   8.191  1.00 90.24           C  
ANISOU 2644  CG1 ILE A1149    15924  11053   7312   -964    649   -452       C  
ATOM   2645  CG2 ILE A1149     -30.327 -22.828   5.899  1.00 90.64           C  
ANISOU 2645  CG2 ILE A1149    15745  11362   7331   -725    606   -681       C  
ATOM   2646  CD1 ILE A1149     -27.988 -23.870   7.999  1.00 96.25           C  
ANISOU 2646  CD1 ILE A1149    16784  11496   8289  -1095    587   -250       C  
ATOM   2647  N   ILE A1150     -32.373 -25.396   5.526  1.00 94.48           N  
ANISOU 2647  N   ILE A1150    15609  12479   7810  -1277   1024  -1014       N  
ATOM   2648  CA  ILE A1150     -33.024 -25.779   4.277  1.00 96.24           C  
ANISOU 2648  CA  ILE A1150    15590  12961   8014  -1348   1038  -1207       C  
ATOM   2649  C   ILE A1150     -34.461 -26.278   4.480  1.00107.59           C  
ANISOU 2649  C   ILE A1150    16649  14920   9310  -1535   1181  -1468       C  
ATOM   2650  O   ILE A1150     -34.719 -27.102   5.364  1.00109.30           O  
ANISOU 2650  O   ILE A1150    16854  15143   9531  -1865   1394  -1465       O  
ATOM   2651  CB  ILE A1150     -32.124 -26.799   3.502  1.00 97.45           C  
ANISOU 2651  CB  ILE A1150    15888  12771   8365  -1604   1118  -1115       C  
ATOM   2652  CG1 ILE A1150     -30.765 -26.157   3.124  1.00 94.48           C  
ANISOU 2652  CG1 ILE A1150    15775  12013   8111  -1400    981   -902       C  
ATOM   2653  CG2 ILE A1150     -32.820 -27.353   2.252  1.00100.20           C  
ANISOU 2653  CG2 ILE A1150    16024  13383   8664  -1755   1151  -1345       C  
ATOM   2654  CD1 ILE A1150     -29.619 -27.103   2.970  1.00 95.65           C  
ANISOU 2654  CD1 ILE A1150    16087  11781   8474  -1579   1084   -749       C  
ATOM   2655  N   THR A1151     -35.390 -25.737   3.657  1.00108.03           N  
ANISOU 2655  N   THR A1151    16397  15434   9214  -1315   1056  -1694       N  
ATOM   2656  CA  THR A1151     -36.806 -26.109   3.585  1.00112.51           C  
ANISOU 2656  CA  THR A1151    16477  16639   9634  -1467   1144  -2001       C  
ATOM   2657  C   THR A1151     -37.109 -26.646   2.183  1.00117.51           C  
ANISOU 2657  C   THR A1151    16922  17472  10253  -1629   1076  -2181       C  
ATOM   2658  O   THR A1151     -36.197 -26.744   1.358  1.00114.50           O  
ANISOU 2658  O   THR A1151    16833  16697   9974  -1612    998  -2048       O  
ATOM   2659  CB  THR A1151     -37.753 -24.968   4.052  1.00128.51           C  
ANISOU 2659  CB  THR A1151    18233  19148  11447   -997   1041  -2146       C  
ATOM   2660  OG1 THR A1151     -39.071 -25.504   4.188  1.00136.92           O  
ANISOU 2660  OG1 THR A1151    18749  20883  12391  -1237   1188  -2451       O  
ATOM   2661  CG2 THR A1151     -37.808 -23.787   3.086  1.00126.41           C  
ANISOU 2661  CG2 THR A1151    18003  18969  11057   -411    730  -2168       C  
ATOM   2662  N   ASN A1152     -38.380 -26.995   1.917  1.00118.75           N  
ANISOU 2662  N   ASN A1152    16576  18277  10266  -1805   1111  -2500       N  
ATOM   2663  CA  ASN A1152     -38.813 -27.495   0.612  1.00120.94           C  
ANISOU 2663  CA  ASN A1152    16630  18847  10476  -1986   1016  -2727       C  
ATOM   2664  C   ASN A1152     -38.624 -26.398  -0.443  1.00123.09           C  
ANISOU 2664  C   ASN A1152    16985  19162  10619  -1393    677  -2687       C  
ATOM   2665  O   ASN A1152     -38.135 -26.684  -1.537  1.00122.10           O  
ANISOU 2665  O   ASN A1152    17048  18841  10502  -1466    595  -2672       O  
ATOM   2666  CB  ASN A1152     -40.279 -27.960   0.659  1.00129.48           C  
ANISOU 2666  CB  ASN A1152    17072  20724  11401  -2292   1095  -3108       C  
ATOM   2667  CG  ASN A1152     -40.564 -29.068   1.651  1.00155.26           C  
ANISOU 2667  CG  ASN A1152    20288  23959  14744  -2959   1473  -3161       C  
ATOM   2668  OD1 ASN A1152     -40.897 -28.823   2.822  1.00149.66           O  
ANISOU 2668  OD1 ASN A1152    19478  23384  14001  -2928   1631  -3126       O  
ATOM   2669  ND2 ASN A1152     -40.457 -30.312   1.197  1.00146.25           N  
ANISOU 2669  ND2 ASN A1152    19271  22622  13677  -3584   1642  -3251       N  
ATOM   2670  N   GLU A1153     -38.957 -25.137  -0.081  1.00119.15           N  
ANISOU 2670  N   GLU A1153    16427  18859   9983   -797    503  -2652       N  
ATOM   2671  CA  GLU A1153     -38.847 -23.961  -0.947  1.00118.68           C  
ANISOU 2671  CA  GLU A1153    16542  18799   9754   -172    188  -2585       C  
ATOM   2672  C   GLU A1153     -37.412 -23.417  -1.118  1.00117.44           C  
ANISOU 2672  C   GLU A1153    17036  17870   9715    -23    154  -2236       C  
ATOM   2673  O   GLU A1153     -37.175 -22.639  -2.051  1.00117.09           O  
ANISOU 2673  O   GLU A1153    17235  17729   9524    354    -61  -2158       O  
ATOM   2674  CB  GLU A1153     -39.796 -22.840  -0.468  1.00123.29           C  
ANISOU 2674  CB  GLU A1153    16867  19854  10125    442     34  -2698       C  
ATOM   2675  CG  GLU A1153     -41.232 -23.000  -0.948  1.00139.66           C  
ANISOU 2675  CG  GLU A1153    18246  22838  11982    538    -92  -3069       C  
ATOM   2676  CD  GLU A1153     -42.047 -21.725  -1.076  1.00159.48           C  
ANISOU 2676  CD  GLU A1153    20577  25803  14217   1376   -374  -3166       C  
ATOM   2677  OE1 GLU A1153     -41.676 -20.854  -1.896  1.00149.24           O1-
ANISOU 2677  OE1 GLU A1153    19685  24247  12772   1893   -643  -3012       O1-
ATOM   2678  OE2 GLU A1153     -43.078 -21.609  -0.374  1.00155.02           O  
ANISOU 2678  OE2 GLU A1153    19474  25862  13563   1528   -312  -3401       O  
ATOM   2679  N   THR A1154     -36.460 -23.823  -0.234  1.00110.38           N  
ANISOU 2679  N   THR A1154    16421  16458   9061   -326    362  -2029       N  
ATOM   2680  CA  THR A1154     -35.073 -23.316  -0.251  1.00106.24           C  
ANISOU 2680  CA  THR A1154    16422  15280   8663   -236    342  -1724       C  
ATOM   2681  C   THR A1154     -33.977 -24.361  -0.538  1.00105.38           C  
ANISOU 2681  C   THR A1154    16507  14741   8791   -680    513  -1594       C  
ATOM   2682  O   THR A1154     -32.799 -24.072  -0.311  1.00101.91           O  
ANISOU 2682  O   THR A1154    16404  13825   8491   -668    535  -1356       O  
ATOM   2683  CB  THR A1154     -34.743 -22.565   1.061  1.00115.43           C  
ANISOU 2683  CB  THR A1154    17789  16204   9864    -56    363  -1575       C  
ATOM   2684  OG1 THR A1154     -34.737 -23.484   2.154  1.00114.76           O  
ANISOU 2684  OG1 THR A1154    17583  16100   9921   -442    582  -1573       O  
ATOM   2685  CG2 THR A1154     -35.680 -21.399   1.335  1.00116.80           C  
ANISOU 2685  CG2 THR A1154    17879  16704   9795    481    204  -1689       C  
ATOM   2686  N   GLY A1155     -34.344 -25.534  -1.046  1.00102.11           N  
ANISOU 2686  N   GLY A1155    15887  14498   8410  -1054    631  -1765       N  
ATOM   2687  CA  GLY A1155     -33.337 -26.537  -1.362  1.00 99.56           C  
ANISOU 2687  CA  GLY A1155    15787  13750   8293  -1396    803  -1664       C  
ATOM   2688  C   GLY A1155     -33.750 -27.988  -1.303  1.00103.36           C  
ANISOU 2688  C   GLY A1155    16130  14295   8847  -1891   1015  -1834       C  
ATOM   2689  O   GLY A1155     -34.898 -28.315  -0.985  1.00105.80           O  
ANISOU 2689  O   GLY A1155    16110  15037   9050  -2077   1055  -2055       O  
ATOM   2690  N   ILE A1156     -32.771 -28.862  -1.605  1.00 97.32           N  
ANISOU 2690  N   ILE A1156    15636  13083   8260  -2110   1172  -1735       N  
ATOM   2691  CA  ILE A1156     -32.886 -30.320  -1.705  1.00 97.99           C  
ANISOU 2691  CA  ILE A1156    15774  13033   8423  -2574   1402  -1866       C  
ATOM   2692  C   ILE A1156     -32.084 -30.991  -0.582  1.00 98.89           C  
ANISOU 2692  C   ILE A1156    16153  12671   8748  -2697   1590  -1637       C  
ATOM   2693  O   ILE A1156     -30.877 -30.762  -0.465  1.00 95.64           O  
ANISOU 2693  O   ILE A1156    15967  11886   8488  -2475   1571  -1396       O  
ATOM   2694  CB  ILE A1156     -32.408 -30.771  -3.126  1.00101.28           C  
ANISOU 2694  CB  ILE A1156    16352  13307   8824  -2629   1421  -1962       C  
ATOM   2695  CG1 ILE A1156     -33.102 -29.975  -4.250  1.00102.94           C  
ANISOU 2695  CG1 ILE A1156    16359  13981   8772  -2428   1184  -2142       C  
ATOM   2696  CG2 ILE A1156     -32.570 -32.273  -3.352  1.00104.55           C  
ANISOU 2696  CG2 ILE A1156    16896  13540   9287  -3109   1661  -2143       C  
ATOM   2697  CD1 ILE A1156     -32.224 -28.913  -4.904  1.00109.81           C  
ANISOU 2697  CD1 ILE A1156    17434  14684   9604  -2013   1044  -1941       C  
ATOM   2698  N   LEU A1157     -32.753 -31.810   0.243  1.00 97.17           N  
ANISOU 2698  N   LEU A1157    15908  12494   8518  -3056   1768  -1712       N  
ATOM   2699  CA  LEU A1157     -32.077 -32.513   1.339  1.00 96.78           C  
ANISOU 2699  CA  LEU A1157    16174  11988   8611  -3158   1938  -1480       C  
ATOM   2700  C   LEU A1157     -31.942 -34.007   1.059  1.00104.32           C  
ANISOU 2700  C   LEU A1157    17434  12571   9632  -3547   2190  -1550       C  
ATOM   2701  O   LEU A1157     -32.922 -34.752   1.126  1.00107.61           O  
ANISOU 2701  O   LEU A1157    17802  13141   9943  -4007   2358  -1764       O  
ATOM   2702  CB  LEU A1157     -32.703 -32.239   2.727  1.00 97.17           C  
ANISOU 2702  CB  LEU A1157    16123  12227   8571  -3218   1978  -1418       C  
ATOM   2703  CG  LEU A1157     -32.398 -30.878   3.389  1.00 99.03           C  
ANISOU 2703  CG  LEU A1157    16273  12576   8779  -2780   1765  -1251       C  
ATOM   2704  CD1 LEU A1157     -33.230 -30.688   4.640  1.00100.89           C  
ANISOU 2704  CD1 LEU A1157    16387  13074   8870  -2876   1847  -1270       C  
ATOM   2705  CD2 LEU A1157     -30.910 -30.716   3.743  1.00 97.77           C  
ANISOU 2705  CD2 LEU A1157    16419  11940   8790  -2519   1683   -942       C  
ATOM   2706  N   VAL A1158     -30.724 -34.429   0.705  1.00100.34           N  
ANISOU 2706  N   VAL A1158    17244  11587   9293  -3363   2226  -1391       N  
ATOM   2707  CA  VAL A1158     -30.394 -35.823   0.395  1.00103.03           C  
ANISOU 2707  CA  VAL A1158    17978  11463   9705  -3610   2466  -1436       C  
ATOM   2708  C   VAL A1158     -30.043 -36.572   1.691  1.00110.26           C  
ANISOU 2708  C   VAL A1158    19261  11955  10680  -3670   2617  -1191       C  
ATOM   2709  O   VAL A1158     -29.871 -35.934   2.732  1.00108.87           O  
ANISOU 2709  O   VAL A1158    19007  11860  10499  -3472   2505   -977       O  
ATOM   2710  CB  VAL A1158     -29.267 -35.927  -0.675  1.00105.26           C  
ANISOU 2710  CB  VAL A1158    18410  11471  10114  -3319   2454  -1410       C  
ATOM   2711  CG1 VAL A1158     -29.579 -35.056  -1.876  1.00103.61           C  
ANISOU 2711  CG1 VAL A1158    17893  11680   9793  -3227   2289  -1600       C  
ATOM   2712  CG2 VAL A1158     -27.900 -35.564  -0.101  1.00102.92           C  
ANISOU 2712  CG2 VAL A1158    18203  10901  10000  -2864   2372  -1077       C  
ATOM   2713  N   LYS A1159     -29.936 -37.910   1.639  1.00110.45           N  
ANISOU 2713  N   LYS A1159    19738  11503  10724  -3929   2865  -1221       N  
ATOM   2714  CA  LYS A1159     -29.533 -38.653   2.827  1.00111.84           C  
ANISOU 2714  CA  LYS A1159    20362  11213  10920  -3924   2999   -951       C  
ATOM   2715  C   LYS A1159     -28.015 -38.814   2.813  1.00115.14           C  
ANISOU 2715  C   LYS A1159    21021  11202  11526  -3373   2922   -690       C  
ATOM   2716  O   LYS A1159     -27.439 -39.092   1.752  1.00115.71           O  
ANISOU 2716  O   LYS A1159    21149  11115  11699  -3217   2957   -797       O  
ATOM   2717  CB  LYS A1159     -30.263 -39.996   2.954  1.00118.76           C  
ANISOU 2717  CB  LYS A1159    21688  11754  11682  -4502   3324  -1087       C  
ATOM   2718  CG  LYS A1159     -30.343 -40.503   4.395  1.00130.26           C  
ANISOU 2718  CG  LYS A1159    23539  12912  13043  -4629   3464   -822       C  
ATOM   2719  CD  LYS A1159     -31.328 -39.700   5.266  1.00135.87           C  
ANISOU 2719  CD  LYS A1159    23844  14189  13593  -4853   3424   -842       C  
ATOM   2720  CE  LYS A1159     -30.671 -39.019   6.448  1.00134.75           C  
ANISOU 2720  CE  LYS A1159    23709  14043  13446  -4408   3242   -493       C  
ATOM   2721  NZ  LYS A1159     -30.018 -37.743   6.065  1.00131.04           N1+
ANISOU 2721  NZ  LYS A1159    22782  13898  13108  -3880   2904   -455       N1+
ATOM   2722  N   ALA A1160     -27.369 -38.581   3.977  1.00109.85           N  
ANISOU 2722  N   ALA A1160    20444  10412  10883  -3065   2806   -367       N  
ATOM   2723  CA  ALA A1160     -25.916 -38.643   4.151  1.00108.79           C  
ANISOU 2723  CA  ALA A1160    20433   9989  10913  -2510   2683   -108       C  
ATOM   2724  C   ALA A1160     -25.331 -40.033   3.911  1.00117.35           C  
ANISOU 2724  C   ALA A1160    22077  10450  12060  -2398   2894    -62       C  
ATOM   2725  O   ALA A1160     -25.860 -41.022   4.426  1.00120.80           O  
ANISOU 2725  O   ALA A1160    23016  10509  12373  -2695   3107    -33       O  
ATOM   2726  CB  ALA A1160     -25.532 -38.145   5.535  1.00108.49           C  
ANISOU 2726  CB  ALA A1160    20384  10012  10827  -2280   2492    194       C  
ATOM   2727  N   GLY A1161     -24.262 -40.086   3.112  1.00114.55           N  
ANISOU 2727  N   GLY A1161    21654   9988  11881  -1978   2860    -66       N  
ATOM   2728  CA  GLY A1161     -23.527 -41.313   2.808  1.00119.04           C  
ANISOU 2728  CA  GLY A1161    22727   9976  12528  -1712   3045    -30       C  
ATOM   2729  C   GLY A1161     -23.817 -42.040   1.507  1.00125.70           C  
ANISOU 2729  C   GLY A1161    23791  10596  13372  -1932   3301   -353       C  
ATOM   2730  O   GLY A1161     -22.915 -42.699   0.974  1.00127.87           O  
ANISOU 2730  O   GLY A1161    24309  10520  13757  -1540   3410   -357       O  
ATOM   2731  N   ASP A1162     -25.076 -41.988   1.008  1.00122.12           N  
ANISOU 2731  N   ASP A1162    23272  10352  12777  -2546   3402   -642       N  
ATOM   2732  CA  ASP A1162     -25.434 -42.693  -0.229  1.00124.55           C  
ANISOU 2732  CA  ASP A1162    23811  10476  13038  -2828   3625   -988       C  
ATOM   2733  C   ASP A1162     -25.249 -41.809  -1.469  1.00123.53           C  
ANISOU 2733  C   ASP A1162    23171  10820  12945  -2715   3512  -1193       C  
ATOM   2734  O   ASP A1162     -25.876 -40.747  -1.568  1.00120.03           O  
ANISOU 2734  O   ASP A1162    22229  10945  12434  -2890   3325  -1258       O  
ATOM   2735  CB  ASP A1162     -26.843 -43.338  -0.173  1.00129.78           C  
ANISOU 2735  CB  ASP A1162    24741  11069  13498  -3596   3818  -1229       C  
ATOM   2736  CG  ASP A1162     -27.114 -44.386  -1.259  1.00147.25           C  
ANISOU 2736  CG  ASP A1162    27403  12907  15637  -3922   4082  -1576       C  
ATOM   2737  OD1 ASP A1162     -26.300 -45.338  -1.395  1.00150.87           O  
ANISOU 2737  OD1 ASP A1162    28441  12719  16163  -3607   4261  -1516       O  
ATOM   2738  OD2 ASP A1162     -28.149 -44.269  -1.954  1.00155.00           O1-
ANISOU 2738  OD2 ASP A1162    28171  14246  16476  -4476   4103  -1920       O1-
ATOM   2739  N   PRO A1163     -24.364 -42.224  -2.409  1.00119.67           N  
ANISOU 2739  N   PRO A1163    22833  10093  12544  -2381   3634  -1286       N  
ATOM   2740  CA  PRO A1163     -24.125 -41.411  -3.612  1.00116.57           C  
ANISOU 2740  CA  PRO A1163    22022  10124  12146  -2279   3563  -1461       C  
ATOM   2741  C   PRO A1163     -25.260 -41.510  -4.629  1.00120.40           C  
ANISOU 2741  C   PRO A1163    22515  10816  12417  -2821   3625  -1847       C  
ATOM   2742  O   PRO A1163     -25.427 -40.594  -5.433  1.00117.99           O  
ANISOU 2742  O   PRO A1163    21813  10987  12029  -2831   3488  -1964       O  
ATOM   2743  CB  PRO A1163     -22.797 -41.955  -4.156  1.00120.68           C  
ANISOU 2743  CB  PRO A1163    22736  10308  12810  -1744   3725  -1432       C  
ATOM   2744  CG  PRO A1163     -22.305 -42.939  -3.121  1.00128.61           C  
ANISOU 2744  CG  PRO A1163    24211  10745  13910  -1472   3813  -1201       C  
ATOM   2745  CD  PRO A1163     -23.516 -43.427  -2.420  1.00125.47           C  
ANISOU 2745  CD  PRO A1163    24145  10165  13362  -2036   3855  -1231       C  
ATOM   2746  N   GLY A1164     -26.032 -42.600  -4.566  1.00119.50           N  
ANISOU 2746  N   GLY A1164    22865  10349  12191  -3281   3818  -2039       N  
ATOM   2747  CA  GLY A1164     -27.207 -42.826  -5.401  1.00120.72           C  
ANISOU 2747  CA  GLY A1164    23027  10720  12121  -3891   3864  -2438       C  
ATOM   2748  C   GLY A1164     -28.302 -41.834  -5.064  1.00121.22           C  
ANISOU 2748  C   GLY A1164    22530  11458  12070  -4206   3620  -2468       C  
ATOM   2749  O   GLY A1164     -29.029 -41.379  -5.949  1.00119.58           O  
ANISOU 2749  O   GLY A1164    22019  11729  11686  -4452   3503  -2744       O  
ATOM   2750  N   GLU A1165     -28.393 -41.471  -3.763  1.00117.00           N  
ANISOU 2750  N   GLU A1165    21860  10978  11617  -4143   3531  -2178       N  
ATOM   2751  CA  GLU A1165     -29.299 -40.461  -3.203  1.00114.44           C  
ANISOU 2751  CA  GLU A1165    21009  11265  11208  -4310   3314  -2150       C  
ATOM   2752  C   GLU A1165     -28.898 -39.067  -3.721  1.00112.91           C  
ANISOU 2752  C   GLU A1165    20320  11546  11033  -3877   3041  -2073       C  
ATOM   2753  O   GLU A1165     -29.772 -38.244  -4.012  1.00111.46           O  
ANISOU 2753  O   GLU A1165    19719  11928  10701  -4011   2856  -2217       O  
ATOM   2754  CB  GLU A1165     -29.224 -40.476  -1.666  1.00115.46           C  
ANISOU 2754  CB  GLU A1165    21228  11229  11414  -4251   3323  -1829       C  
ATOM   2755  CG  GLU A1165     -30.105 -41.522  -1.011  1.00132.76           C  
ANISOU 2755  CG  GLU A1165    23786  13167  13491  -4846   3566  -1920       C  
ATOM   2756  CD  GLU A1165     -31.540 -41.086  -0.790  1.00161.93           C  
ANISOU 2756  CD  GLU A1165    27035  17485  17008  -5367   3518  -2136       C  
ATOM   2757  OE1 GLU A1165     -31.756 -40.038  -0.136  1.00153.04           O1-
ANISOU 2757  OE1 GLU A1165    25465  16806  15875  -5164   3325  -1991       O1-
ATOM   2758  OE2 GLU A1165     -32.452 -41.803  -1.262  1.00164.54           O  
ANISOU 2758  OE2 GLU A1165    27454  17870  17195  -5984   3680  -2470       O  
ATOM   2759  N   LEU A1166     -27.574 -38.816  -3.843  1.00106.42           N  
ANISOU 2759  N   LEU A1166    19558  10496  10381  -3358   3026  -1851       N  
ATOM   2760  CA  LEU A1166     -27.040 -37.552  -4.336  1.00102.61           C  
ANISOU 2760  CA  LEU A1166    18704  10368   9915  -2995   2823  -1756       C  
ATOM   2761  C   LEU A1166     -27.208 -37.427  -5.847  1.00108.11           C  
ANISOU 2761  C   LEU A1166    19362  11266  10449  -3061   2833  -2032       C  
ATOM   2762  O   LEU A1166     -27.730 -36.413  -6.305  1.00106.64           O  
ANISOU 2762  O   LEU A1166    18859  11550  10110  -3054   2628  -2094       O  
ATOM   2763  CB  LEU A1166     -25.568 -37.379  -3.927  1.00101.13           C  
ANISOU 2763  CB  LEU A1166    18550   9921   9953  -2500   2830  -1451       C  
ATOM   2764  CG  LEU A1166     -24.981 -35.964  -4.038  1.00101.80           C  
ANISOU 2764  CG  LEU A1166    18258  10349  10072  -2199   2621  -1288       C  
ATOM   2765  CD1 LEU A1166     -25.503 -35.053  -2.938  1.00100.00           C  
ANISOU 2765  CD1 LEU A1166    17794  10384   9818  -2222   2397  -1128       C  
ATOM   2766  CD2 LEU A1166     -23.487 -36.004  -3.942  1.00102.81           C  
ANISOU 2766  CD2 LEU A1166    18391  10264  10408  -1794   2681  -1084       C  
ATOM   2767  N   ALA A1167     -26.775 -38.454  -6.613  1.00107.52           N  
ANISOU 2767  N   ALA A1167    19653  10823  10376  -3097   3069  -2199       N  
ATOM   2768  CA  ALA A1167     -26.862 -38.504  -8.074  1.00109.04           C  
ANISOU 2768  CA  ALA A1167    19902  11150  10379  -3171   3117  -2485       C  
ATOM   2769  C   ALA A1167     -28.292 -38.244  -8.571  1.00115.17           C  
ANISOU 2769  C   ALA A1167    20473  12411  10873  -3598   2946  -2777       C  
ATOM   2770  O   ALA A1167     -28.479 -37.480  -9.522  1.00114.14           O  
ANISOU 2770  O   ALA A1167    20153  12672  10545  -3519   2792  -2880       O  
ATOM   2771  CB  ALA A1167     -26.355 -39.846  -8.584  1.00113.62           C  
ANISOU 2771  CB  ALA A1167    20991  11190  10990  -3206   3428  -2657       C  
ATOM   2772  N   ASN A1168     -29.294 -38.835  -7.886  1.00114.40           N  
ANISOU 2772  N   ASN A1168    20396  12326  10743  -4038   2968  -2898       N  
ATOM   2773  CA  ASN A1168     -30.720 -38.694  -8.197  1.00116.18           C  
ANISOU 2773  CA  ASN A1168    20339  13085  10718  -4486   2812  -3203       C  
ATOM   2774  C   ASN A1168     -31.227 -37.264  -7.967  1.00116.94           C  
ANISOU 2774  C   ASN A1168    19899  13799  10733  -4250   2488  -3082       C  
ATOM   2775  O   ASN A1168     -32.144 -36.831  -8.670  1.00118.10           O  
ANISOU 2775  O   ASN A1168    19759  14489  10626  -4383   2285  -3324       O  
ATOM   2776  CB  ASN A1168     -31.541 -39.697  -7.390  1.00120.15           C  
ANISOU 2776  CB  ASN A1168    20992  13428  11232  -5044   2977  -3334       C  
ATOM   2777  CG  ASN A1168     -32.478 -40.514  -8.234  1.00143.49           C  
ANISOU 2777  CG  ASN A1168    24049  16521  13949  -5650   3042  -3796       C  
ATOM   2778  OD1 ASN A1168     -32.069 -41.434  -8.964  1.00134.99           O  
ANISOU 2778  OD1 ASN A1168    23452  15003  12834  -5783   3244  -3982       O  
ATOM   2779  ND2 ASN A1168     -33.761 -40.193  -8.147  1.00138.19           N  
ANISOU 2779  ND2 ASN A1168    22915  16490  13100  -6031   2872  -4016       N  
ATOM   2780  N   ALA A1169     -30.623 -36.540  -6.986  1.00109.04           N  
ANISOU 2780  N   ALA A1169    18792  12711   9929  -3880   2428  -2718       N  
ATOM   2781  CA  ALA A1169     -30.932 -35.147  -6.637  1.00105.05           C  
ANISOU 2781  CA  ALA A1169    17889  12657   9368  -3588   2152  -2564       C  
ATOM   2782  C   ALA A1169     -30.357 -34.171  -7.666  1.00105.62           C  
ANISOU 2782  C   ALA A1169    17930  12869   9331  -3207   2004  -2498       C  
ATOM   2783  O   ALA A1169     -31.017 -33.189  -7.995  1.00104.34           O  
ANISOU 2783  O   ALA A1169    17507  13170   8968  -3069   1753  -2542       O  
ATOM   2784  CB  ALA A1169     -30.390 -34.820  -5.259  1.00102.82           C  
ANISOU 2784  CB  ALA A1169    17601  12156   9309  -3377   2166  -2226       C  
ATOM   2785  N   ILE A1170     -29.129 -34.444  -8.167  1.00101.14           N  
ANISOU 2785  N   ILE A1170    17644  11905   8880  -3023   2174  -2392       N  
ATOM   2786  CA  ILE A1170     -28.432 -33.663  -9.198  1.00 99.98           C  
ANISOU 2786  CA  ILE A1170    17541  11826   8622  -2731   2126  -2326       C  
ATOM   2787  C   ILE A1170     -29.242 -33.744 -10.523  1.00107.64           C  
ANISOU 2787  C   ILE A1170    18527  13133   9240  -2899   2032  -2650       C  
ATOM   2788  O   ILE A1170     -29.314 -32.762 -11.262  1.00106.62           O  
ANISOU 2788  O   ILE A1170    18341  13285   8883  -2685   1853  -2616       O  
ATOM   2789  CB  ILE A1170     -26.942 -34.130  -9.311  1.00102.49           C  
ANISOU 2789  CB  ILE A1170    18100  11677   9164  -2540   2391  -2173       C  
ATOM   2790  CG1 ILE A1170     -26.145 -33.757  -8.031  1.00 99.87           C  
ANISOU 2790  CG1 ILE A1170    17669  11153   9125  -2315   2380  -1837       C  
ATOM   2791  CG2 ILE A1170     -26.236 -33.591 -10.571  1.00103.28           C  
ANISOU 2791  CG2 ILE A1170    18291  11841   9108  -2351   2445  -2176       C  
ATOM   2792  CD1 ILE A1170     -24.840 -34.575  -7.797  1.00106.75           C  
ANISOU 2792  CD1 ILE A1170    18718  11583  10260  -2141   2632  -1718       C  
ATOM   2793  N   LEU A1171     -29.900 -34.896 -10.770  1.00108.94           N  
ANISOU 2793  N   LEU A1171    18790  13269   9331  -3302   2136  -2964       N  
ATOM   2794  CA  LEU A1171     -30.774 -35.111 -11.925  1.00113.23           C  
ANISOU 2794  CA  LEU A1171    19322  14178   9523  -3543   2020  -3326       C  
ATOM   2795  C   LEU A1171     -32.058 -34.281 -11.754  1.00119.57           C  
ANISOU 2795  C   LEU A1171    19684  15629  10116  -3552   1668  -3408       C  
ATOM   2796  O   LEU A1171     -32.497 -33.636 -12.707  1.00120.87           O  
ANISOU 2796  O   LEU A1171    19759  16210   9958  -3411   1430  -3518       O  
ATOM   2797  CB  LEU A1171     -31.104 -36.604 -12.088  1.00117.14           C  
ANISOU 2797  CB  LEU A1171    20069  14422  10016  -4042   2244  -3654       C  
ATOM   2798  N   LYS A1172     -32.625 -34.267 -10.522  1.00116.86           N  
ANISOU 2798  N   LYS A1172    19079  15382   9941  -3665   1640  -3341       N  
ATOM   2799  CA  LYS A1172     -33.824 -33.506 -10.130  1.00117.79           C  
ANISOU 2799  CA  LYS A1172    18723  16123   9908  -3623   1352  -3413       C  
ATOM   2800  C   LYS A1172     -33.557 -31.998 -10.244  1.00120.50           C  
ANISOU 2800  C   LYS A1172    18985  16639  10159  -3038   1105  -3145       C  
ATOM   2801  O   LYS A1172     -34.448 -31.237 -10.637  1.00121.47           O  
ANISOU 2801  O   LYS A1172    18830  17316  10008  -2849    803  -3254       O  
ATOM   2802  CB  LYS A1172     -34.250 -33.867  -8.686  1.00118.82           C  
ANISOU 2802  CB  LYS A1172    18673  16211  10261  -3857   1472  -3356       C  
ATOM   2803  CG  LYS A1172     -35.760 -33.921  -8.469  1.00131.31           C  
ANISOU 2803  CG  LYS A1172    19765  18464  11662  -4168   1327  -3662       C  
ATOM   2804  CD  LYS A1172     -36.373 -35.241  -8.968  1.00145.46           C  
ANISOU 2804  CD  LYS A1172    21608  20309  13350  -4846   1475  -4064       C  
ATOM   2805  CE  LYS A1172     -37.878 -35.260  -8.875  1.00158.04           C  
ANISOU 2805  CE  LYS A1172    22622  22689  14739  -5199   1317  -4413       C  
ATOM   2806  NZ  LYS A1172     -38.454 -36.453  -9.549  1.00173.23           N1+
ANISOU 2806  NZ  LYS A1172    24604  24704  16511  -5904   1422  -4846       N1+
ATOM   2807  N   ALA A1173     -32.310 -31.589  -9.912  1.00114.83           N  
ANISOU 2807  N   ALA A1173    18531  15441   9659  -2757   1235  -2804       N  
ATOM   2808  CA  ALA A1173     -31.795 -30.223  -9.965  1.00113.08           C  
ANISOU 2808  CA  ALA A1173    18367  15212   9387  -2284   1081  -2518       C  
ATOM   2809  C   ALA A1173     -31.786 -29.725 -11.410  1.00121.55           C  
ANISOU 2809  C   ALA A1173    19602  16469  10111  -2107    942  -2588       C  
ATOM   2810  O   ALA A1173     -32.197 -28.591 -11.670  1.00122.10           O  
ANISOU 2810  O   ALA A1173    19627  16820   9945  -1761    677  -2504       O  
ATOM   2811  CB  ALA A1173     -30.386 -30.189  -9.392  1.00110.54           C  
ANISOU 2811  CB  ALA A1173    18278  14345   9379  -2177   1301  -2209       C  
ATOM   2812  N   LEU A1174     -31.346 -30.597 -12.347  1.00120.82           N  
ANISOU 2812  N   LEU A1174    19746  16204   9954  -2327   1127  -2748       N  
ATOM   2813  CA  LEU A1174     -31.287 -30.350 -13.786  1.00123.67           C  
ANISOU 2813  CA  LEU A1174    20327  16715   9948  -2230   1049  -2848       C  
ATOM   2814  C   LEU A1174     -32.704 -30.180 -14.358  1.00133.19           C  
ANISOU 2814  C   LEU A1174    21279  18560  10767  -2246    696  -3133       C  
ATOM   2815  O   LEU A1174     -32.920 -29.307 -15.201  1.00134.42           O  
ANISOU 2815  O   LEU A1174    21534  18977  10561  -1934    457  -3090       O  
ATOM   2816  CB  LEU A1174     -30.566 -31.524 -14.478  1.00125.01           C  
ANISOU 2816  CB  LEU A1174    20791  16546  10162  -2506   1371  -3012       C  
ATOM   2817  CG  LEU A1174     -30.226 -31.353 -15.958  1.00131.76           C  
ANISOU 2817  CG  LEU A1174    21957  17459  10645  -2419   1388  -3093       C  
ATOM   2818  CD1 LEU A1174     -28.793 -30.934 -16.129  1.00129.87           C  
ANISOU 2818  CD1 LEU A1174    21988  16819  10539  -2207   1659  -2799       C  
ATOM   2819  CD2 LEU A1174     -30.487 -32.632 -16.723  1.00136.70           C  
ANISOU 2819  CD2 LEU A1174    22734  18075  11129  -2794   1523  -3487       C  
ATOM   2820  N   GLU A1175     -33.660 -31.011 -13.890  1.00133.16           N  
ANISOU 2820  N   GLU A1175    20950  18822  10821  -2614    666  -3423       N  
ATOM   2821  CA  GLU A1175     -35.062 -30.982 -14.312  1.00138.23           C  
ANISOU 2821  CA  GLU A1175    21219  20172  11131  -2702    335  -3750       C  
ATOM   2822  C   GLU A1175     -35.738 -29.667 -13.905  1.00144.12           C  
ANISOU 2822  C   GLU A1175    21660  21350  11748  -2201     -6  -3597       C  
ATOM   2823  O   GLU A1175     -36.604 -29.179 -14.632  1.00147.24           O  
ANISOU 2823  O   GLU A1175    21867  22324  11756  -1984   -357  -3758       O  
ATOM   2824  CB  GLU A1175     -35.820 -32.183 -13.732  1.00141.86           C  
ANISOU 2824  CB  GLU A1175    21394  20770  11737  -3297    458  -4076       C  
ATOM   2825  CG  GLU A1175     -37.035 -32.587 -14.546  1.00157.78           C  
ANISOU 2825  CG  GLU A1175    23102  23466  13381  -3599    202  -4530       C  
ATOM   2826  CD  GLU A1175     -38.228 -32.983 -13.702  1.00180.61           C  
ANISOU 2826  CD  GLU A1175    25428  26854  16344  -3978    148  -4784       C  
ATOM   2827  OE1 GLU A1175     -38.959 -32.076 -13.242  1.00168.40           O  
ANISOU 2827  OE1 GLU A1175    23427  25831  14726  -3623   -114  -4729       O  
ATOM   2828  OE2 GLU A1175     -38.433 -34.201 -13.498  1.00180.73           O1-
ANISOU 2828  OE2 GLU A1175    25474  26722  16471  -4634    392  -5045       O1-
ATOM   2829  N   LEU A1176     -35.333 -29.100 -12.752  1.00138.68           N  
ANISOU 2829  N   LEU A1176    20950  20379  11362  -1988     88  -3296       N  
ATOM   2830  CA  LEU A1176     -35.850 -27.828 -12.242  1.00139.14           C  
ANISOU 2830  CA  LEU A1176    20813  20724  11329  -1476   -182  -3133       C  
ATOM   2831  C   LEU A1176     -35.210 -26.642 -12.953  1.00144.58           C  
ANISOU 2831  C   LEU A1176    21932  21206  11794   -965   -315  -2844       C  
ATOM   2832  O   LEU A1176     -35.864 -25.611 -13.116  1.00146.80           O  
ANISOU 2832  O   LEU A1176    22145  21833  11800   -483   -634  -2798       O  
ATOM   2833  CB  LEU A1176     -35.603 -27.699 -10.728  1.00135.57           C  
ANISOU 2833  CB  LEU A1176    20252  20001  11257  -1483     -9  -2938       C  
ATOM   2834  CG  LEU A1176     -36.520 -28.497  -9.807  1.00141.72           C  
ANISOU 2834  CG  LEU A1176    20563  21101  12181  -1873     70  -3181       C  
ATOM   2835  CD1 LEU A1176     -35.921 -28.612  -8.420  1.00138.13           C  
ANISOU 2835  CD1 LEU A1176    20185  20198  12099  -1962    324  -2947       C  
ATOM   2836  CD2 LEU A1176     -37.916 -27.878  -9.729  1.00147.99           C  
ANISOU 2836  CD2 LEU A1176    20830  22679  12720  -1609   -251  -3388       C  
ATOM   2837  N   SER A1177     -33.933 -26.793 -13.361  1.00139.80           N  
ANISOU 2837  N   SER A1177    21782  20038  11296  -1066    -51  -2651       N  
ATOM   2838  CA  SER A1177     -33.097 -25.770 -13.999  1.00139.61           C  
ANISOU 2838  CA  SER A1177    22237  19713  11097   -722    -61  -2351       C  
ATOM   2839  C   SER A1177     -33.662 -25.157 -15.290  1.00146.52           C  
ANISOU 2839  C   SER A1177    23297  20949  11427   -405   -369  -2412       C  
ATOM   2840  O   SER A1177     -33.531 -23.945 -15.486  1.00145.91           O  
ANISOU 2840  O   SER A1177    23530  20776  11133     36   -521  -2156       O  
ATOM   2841  CB  SER A1177     -31.694 -26.312 -14.251  1.00142.55           C  
ANISOU 2841  CB  SER A1177    22939  19536  11687   -991    329  -2224       C  
ATOM   2842  OG  SER A1177     -30.784 -25.263 -14.537  1.00154.32           O  
ANISOU 2842  OG  SER A1177    24837  20700  13096   -742    389  -1899       O  
ATOM   2843  N   ARG A1178     -34.270 -25.983 -16.164  1.00146.83           N  
ANISOU 2843  N   ARG A1178    23199  21374  11218   -633   -465  -2747       N  
ATOM   2844  CA  ARG A1178     -34.839 -25.550 -17.452  1.00151.66           C  
ANISOU 2844  CA  ARG A1178    23975  22390  11258   -357   -790  -2842       C  
ATOM   2845  C   ARG A1178     -35.945 -24.480 -17.307  1.00158.54           C  
ANISOU 2845  C   ARG A1178    24631  23767  11842    220  -1252  -2814       C  
ATOM   2846  O   ARG A1178     -36.115 -23.654 -18.211  1.00161.74           O  
ANISOU 2846  O   ARG A1178    25371  24308  11776    661  -1519  -2701       O  
ATOM   2847  CB  ARG A1178     -35.320 -26.751 -18.293  1.00154.83           C  
ANISOU 2847  CB  ARG A1178    24221  23141  11465   -788   -814  -3266       C  
ATOM   2848  CG  ARG A1178     -36.277 -27.685 -17.561  1.00167.30           C  
ANISOU 2848  CG  ARG A1178    25184  25119  13265  -1183   -855  -3623       C  
ATOM   2849  CD  ARG A1178     -36.734 -28.841 -18.425  1.00186.40           C  
ANISOU 2849  CD  ARG A1178    27517  27844  15463  -1673   -875  -4064       C  
ATOM   2850  NE  ARG A1178     -37.475 -29.837 -17.649  1.00200.70           N  
ANISOU 2850  NE  ARG A1178    28823  29900  17535  -2193   -804  -4388       N  
ATOM   2851  CZ  ARG A1178     -38.793 -29.825 -17.466  1.00221.27           C  
ANISOU 2851  CZ  ARG A1178    30826  33261  19983  -2233  -1129  -4676       C  
ATOM   2852  NH1 ARG A1178     -39.540 -28.874 -18.014  1.00213.09           N  
ANISOU 2852  NH1 ARG A1178    29601  32834  18528  -1700  -1593  -4684       N  
ATOM   2853  NH2 ARG A1178     -39.377 -30.775 -16.747  1.00209.85           N1+
ANISOU 2853  NH2 ARG A1178    28970  31984  18780  -2804   -987  -4962       N1+
ATOM   2854  N   SER A1179     -36.663 -24.486 -16.162  1.00153.21           N  
ANISOU 2854  N   SER A1179    23432  23350  11430    251  -1327  -2905       N  
ATOM   2855  CA  SER A1179     -37.741 -23.547 -15.840  1.00155.43           C  
ANISOU 2855  CA  SER A1179    23416  24141  11501    830  -1722  -2916       C  
ATOM   2856  C   SER A1179     -37.217 -22.304 -15.079  1.00155.12           C  
ANISOU 2856  C   SER A1179    23734  23616  11589   1300  -1677  -2517       C  
ATOM   2857  O   SER A1179     -36.001 -22.163 -14.902  1.00150.68           O  
ANISOU 2857  O   SER A1179    23633  22368  11250   1129  -1362  -2239       O  
ATOM   2858  CB  SER A1179     -38.841 -24.261 -15.056  1.00160.28           C  
ANISOU 2858  CB  SER A1179    23244  25361  12294    570  -1787  -3276       C  
ATOM   2859  OG  SER A1179     -39.368 -25.356 -15.788  1.00171.64           O  
ANISOU 2859  OG  SER A1179    24387  27251  13578     90  -1846  -3671       O  
ATOM   2860  N   ASP A1180     -38.132 -21.398 -14.654  1.00153.08           N  
ANISOU 2860  N   ASP A1180    23262  23731  11169   1897  -1994  -2513       N  
ATOM   2861  CA  ASP A1180     -37.804 -20.160 -13.944  1.00150.64           C  
ANISOU 2861  CA  ASP A1180    23328  22991  10918   2390  -1993  -2185       C  
ATOM   2862  C   ASP A1180     -37.244 -20.405 -12.543  1.00148.14           C  
ANISOU 2862  C   ASP A1180    22881  22271  11135   2047  -1648  -2103       C  
ATOM   2863  O   ASP A1180     -37.995 -20.579 -11.575  1.00147.90           O  
ANISOU 2863  O   ASP A1180    22318  22599  11279   2066  -1671  -2277       O  
ATOM   2864  CB  ASP A1180     -39.001 -19.196 -13.921  1.00157.54           C  
ANISOU 2864  CB  ASP A1180    24013  24403  11441   3186  -2430  -2246       C  
ATOM   2865  N   LEU A1181     -35.907 -20.416 -12.449  1.00139.65           N  
ANISOU 2865  N   LEU A1181    22285  20483  10291   1730  -1326  -1841       N  
ATOM   2866  CA  LEU A1181     -35.173 -20.618 -11.201  1.00134.40           C  
ANISOU 2866  CA  LEU A1181    21584  19383  10098   1410  -1018  -1722       C  
ATOM   2867  C   LEU A1181     -35.082 -19.308 -10.395  1.00136.20           C  
ANISOU 2867  C   LEU A1181    22119  19309  10322   1872  -1090  -1490       C  
ATOM   2868  O   LEU A1181     -34.741 -19.333  -9.211  1.00132.20           O  
ANISOU 2868  O   LEU A1181    21520  18564  10144   1708   -917  -1431       O  
ATOM   2869  CB  LEU A1181     -33.771 -21.175 -11.519  1.00131.26           C  
ANISOU 2869  CB  LEU A1181    21517  18435   9921    919   -673  -1567       C  
ATOM   2870  CG  LEU A1181     -33.302 -22.409 -10.730  1.00132.51           C  
ANISOU 2870  CG  LEU A1181    21357  18461  10531    356   -366  -1664       C  
ATOM   2871  CD1 LEU A1181     -34.135 -23.646 -11.054  1.00134.20           C  
ANISOU 2871  CD1 LEU A1181    21115  19153  10722     42   -386  -2019       C  
ATOM   2872  CD2 LEU A1181     -31.846 -22.712 -11.019  1.00132.83           C  
ANISOU 2872  CD2 LEU A1181    21744  17961  10764     38    -53  -1477       C  
ATOM   2873  N   SER A1182     -35.430 -18.179 -11.048  1.00135.45           N  
ANISOU 2873  N   SER A1182    22427  19222   9816   2466  -1360  -1369       N  
ATOM   2874  CA  SER A1182     -35.435 -16.804 -10.546  1.00136.22           C  
ANISOU 2874  CA  SER A1182    22979  18990   9788   3003  -1470  -1156       C  
ATOM   2875  C   SER A1182     -36.129 -16.606  -9.182  1.00138.51           C  
ANISOU 2875  C   SER A1182    22869  19490  10270   3219  -1503  -1283       C  
ATOM   2876  O   SER A1182     -35.591 -15.889  -8.331  1.00136.16           O  
ANISOU 2876  O   SER A1182    22924  18702  10110   3281  -1390  -1108       O  
ATOM   2877  CB  SER A1182     -36.043 -15.877 -11.594  1.00145.98           C  
ANISOU 2877  CB  SER A1182    24615  20370  10479   3676  -1815  -1083       C  
ATOM   2878  OG  SER A1182     -35.902 -14.505 -11.262  1.00158.72           O  
ANISOU 2878  OG  SER A1182    26868  21510  11929   4189  -1891   -839       O  
ATOM   2879  N   LYS A1183     -37.318 -17.220  -8.981  1.00136.00           N  
ANISOU 2879  N   LYS A1183    21823  19917   9935   3307  -1644  -1604       N  
ATOM   2880  CA  LYS A1183     -38.078 -17.097  -7.728  1.00135.38           C  
ANISOU 2880  CA  LYS A1183    21297  20142   9999   3503  -1641  -1761       C  
ATOM   2881  C   LYS A1183     -37.615 -18.068  -6.644  1.00133.71           C  
ANISOU 2881  C   LYS A1183    20762  19801  10238   2826  -1302  -1815       C  
ATOM   2882  O   LYS A1183     -37.721 -17.739  -5.458  1.00132.76           O  
ANISOU 2882  O   LYS A1183    20578  19600  10263   2921  -1209  -1811       O  
ATOM   2883  CB  LYS A1183     -39.591 -17.205  -7.963  1.00142.65           C  
ANISOU 2883  CB  LYS A1183    21554  21979  10667   3929  -1932  -2087       C  
ATOM   2884  CG  LYS A1183     -40.294 -15.852  -8.010  1.00157.75           C  
ANISOU 2884  CG  LYS A1183    23707  24011  12221   4890  -2243  -2040       C  
ATOM   2885  CD  LYS A1183     -41.771 -15.989  -8.378  1.00172.27           C  
ANISOU 2885  CD  LYS A1183    24805  26866  13784   5352  -2570  -2381       C  
ATOM   2886  CE  LYS A1183     -42.518 -14.678  -8.297  1.00183.69           C  
ANISOU 2886  CE  LYS A1183    26440  28466  14887   6408  -2873  -2355       C  
ATOM   2887  NZ  LYS A1183     -43.937 -14.820  -8.721  1.00196.44           N1+
ANISOU 2887  NZ  LYS A1183    27254  31166  16217   6900  -3224  -2701       N1+
ATOM   2888  N   PHE A1184     -37.089 -19.251  -7.046  1.00126.41           N  
ANISOU 2888  N   PHE A1184    19694  18830   9506   2176  -1116  -1860       N  
ATOM   2889  CA  PHE A1184     -36.568 -20.280  -6.132  1.00121.62           C  
ANISOU 2889  CA  PHE A1184    18867  18042   9299   1544   -798  -1882       C  
ATOM   2890  C   PHE A1184     -35.292 -19.791  -5.443  1.00119.91           C  
ANISOU 2890  C   PHE A1184    19157  17096   9305   1437   -617  -1577       C  
ATOM   2891  O   PHE A1184     -35.061 -20.121  -4.281  1.00116.77           O  
ANISOU 2891  O   PHE A1184    18631  16570   9166   1192   -442  -1561       O  
ATOM   2892  CB  PHE A1184     -36.302 -21.598  -6.886  1.00122.51           C  
ANISOU 2892  CB  PHE A1184    18816  18222   9508    971   -663  -2004       C  
ATOM   2893  CG  PHE A1184     -36.291 -22.858  -6.047  1.00122.06           C  
ANISOU 2893  CG  PHE A1184    18406  18200   9770    383   -393  -2133       C  
ATOM   2894  CD1 PHE A1184     -37.465 -23.354  -5.490  1.00128.08           C  
ANISOU 2894  CD1 PHE A1184    18594  19551  10519    271   -399  -2413       C  
ATOM   2895  CD2 PHE A1184     -35.124 -23.590  -5.879  1.00120.13           C  
ANISOU 2895  CD2 PHE A1184    18410  17422   9813    -61   -125  -1982       C  
ATOM   2896  CE1 PHE A1184     -37.460 -24.536  -4.741  1.00127.62           C  
ANISOU 2896  CE1 PHE A1184    18307  19470  10715   -315   -122  -2512       C  
ATOM   2897  CE2 PHE A1184     -35.123 -24.774  -5.135  1.00121.83           C  
ANISOU 2897  CE2 PHE A1184    18395  17615  10281   -558    115  -2078       C  
ATOM   2898  CZ  PHE A1184     -36.289 -25.238  -4.570  1.00122.61           C  
ANISOU 2898  CZ  PHE A1184    18012  18227  10346   -705    124  -2331       C  
ATOM   2899  N   ARG A1185     -34.483 -18.988  -6.165  1.00115.57           N  
ANISOU 2899  N   ARG A1185    19189  16099   8625   1602   -664  -1343       N  
ATOM   2900  CA  ARG A1185     -33.237 -18.384  -5.691  1.00112.31           C  
ANISOU 2900  CA  ARG A1185    19273  15029   8371   1477   -519  -1068       C  
ATOM   2901  C   ARG A1185     -33.521 -17.276  -4.670  1.00115.97           C  
ANISOU 2901  C   ARG A1185    19936  15350   8776   1872   -610  -1013       C  
ATOM   2902  O   ARG A1185     -32.717 -17.075  -3.754  1.00113.31           O  
ANISOU 2902  O   ARG A1185    19785  14617   8650   1655   -473   -885       O  
ATOM   2903  CB  ARG A1185     -32.424 -17.832  -6.873  1.00114.31           C  
ANISOU 2903  CB  ARG A1185    20079  14916   8439   1499   -520   -865       C  
ATOM   2904  CG  ARG A1185     -31.798 -18.919  -7.749  1.00127.30           C  
ANISOU 2904  CG  ARG A1185    21615  16567  10188   1043   -344   -893       C  
ATOM   2905  CD  ARG A1185     -31.134 -18.357  -8.991  1.00139.79           C  
ANISOU 2905  CD  ARG A1185    23728  17872  11516   1086   -328   -717       C  
ATOM   2906  NE  ARG A1185     -29.980 -19.153  -9.414  1.00144.97           N  
ANISOU 2906  NE  ARG A1185    24398  18302  12382    589    -38   -661       N  
ATOM   2907  CZ  ARG A1185     -28.715 -18.854  -9.130  1.00159.62           C  
ANISOU 2907  CZ  ARG A1185    26506  19712  14431    324    178   -458       C  
ATOM   2908  NH1 ARG A1185     -28.423 -17.773  -8.415  1.00145.55           N  
ANISOU 2908  NH1 ARG A1185    25033  17616  12654    442    134   -294       N  
ATOM   2909  NH2 ARG A1185     -27.732 -19.625  -9.568  1.00148.96           N1+
ANISOU 2909  NH2 ARG A1185    25095  18247  13257    -59    441   -440       N1+
ATOM   2910  N   GLU A1186     -34.667 -16.571  -4.814  1.00115.22           N  
ANISOU 2910  N   GLU A1186    19796  15601   8380   2474   -849  -1129       N  
ATOM   2911  CA  GLU A1186     -35.063 -15.497  -3.896  1.00116.43           C  
ANISOU 2911  CA  GLU A1186    20163  15640   8433   2949   -935  -1118       C  
ATOM   2912  C   GLU A1186     -35.532 -16.024  -2.527  1.00117.39           C  
ANISOU 2912  C   GLU A1186    19784  16047   8772   2801   -808  -1291       C  
ATOM   2913  O   GLU A1186     -35.380 -15.319  -1.526  1.00116.76           O  
ANISOU 2913  O   GLU A1186    19959  15693   8712   2957   -772  -1243       O  
ATOM   2914  CB  GLU A1186     -36.098 -14.555  -4.535  1.00123.28           C  
ANISOU 2914  CB  GLU A1186    21178  16775   8886   3736  -1233  -1179       C  
ATOM   2915  CG  GLU A1186     -36.120 -13.152  -3.937  1.00136.49           C  
ANISOU 2915  CG  GLU A1186    23447  18026  10387   4282  -1312  -1072       C  
ATOM   2916  CD  GLU A1186     -34.805 -12.395  -3.961  1.00154.17           C  
ANISOU 2916  CD  GLU A1186    26510  19413  12654   4036  -1195   -776       C  
ATOM   2917  OE1 GLU A1186     -34.390 -11.952  -5.057  1.00153.09           O  
ANISOU 2917  OE1 GLU A1186    26888  18979  12301   4102  -1259   -593       O  
ATOM   2918  OE2 GLU A1186     -34.187 -12.248  -2.882  1.00143.17           O1-
ANISOU 2918  OE2 GLU A1186    25247  17672  11478   3745  -1036   -736       O1-
ATOM   2919  N   ASN A1187     -36.087 -17.260  -2.486  1.00111.57           N  
ANISOU 2919  N   ASN A1187    18389  15833   8168   2464   -725  -1496       N  
ATOM   2920  CA  ASN A1187     -36.522 -17.923  -1.254  1.00109.42           C  
ANISOU 2920  CA  ASN A1187    17654  15840   8080   2218   -554  -1650       C  
ATOM   2921  C   ASN A1187     -35.282 -18.310  -0.439  1.00108.51           C  
ANISOU 2921  C   ASN A1187    17789  15176   8265   1705   -334  -1455       C  
ATOM   2922  O   ASN A1187     -35.309 -18.213   0.789  1.00107.95           O  
ANISOU 2922  O   ASN A1187    17691  15054   8270   1670   -234  -1465       O  
ATOM   2923  CB  ASN A1187     -37.378 -19.153  -1.556  1.00108.71           C  
ANISOU 2923  CB  ASN A1187    16886  16391   8025   1907   -502  -1909       C  
ATOM   2924  CG  ASN A1187     -38.546 -18.903  -2.481  1.00135.14           C  
ANISOU 2924  CG  ASN A1187    19898  20377  11072   2351   -757  -2126       C  
ATOM   2925  OD1 ASN A1187     -39.260 -17.897  -2.382  1.00130.02           O  
ANISOU 2925  OD1 ASN A1187    19260  19955  10185   3015   -945  -2187       O  
ATOM   2926  ND2 ASN A1187     -38.773 -19.829  -3.404  1.00128.99           N  
ANISOU 2926  ND2 ASN A1187    18816  19914  10279   2017   -782  -2264       N  
ATOM   2927  N   CYS A1188     -34.185 -18.702  -1.137  1.00101.79           N  
ANISOU 2927  N   CYS A1188    17183  13940   7553   1347   -270  -1283       N  
ATOM   2928  CA  CYS A1188     -32.876 -19.051  -0.572  1.00 97.57           C  
ANISOU 2928  CA  CYS A1188    16864  12917   7292    910   -101  -1089       C  
ATOM   2929  C   CYS A1188     -32.240 -17.820   0.078  1.00 99.12           C  
ANISOU 2929  C   CYS A1188    17555  12663   7442   1099   -157   -927       C  
ATOM   2930  O   CYS A1188     -31.744 -17.920   1.192  1.00 96.06           O  
ANISOU 2930  O   CYS A1188    17198  12094   7206    893    -71   -871       O  
ATOM   2931  CB  CYS A1188     -31.959 -19.641  -1.643  1.00 96.54           C  
ANISOU 2931  CB  CYS A1188    16839  12572   7270    592    -25   -982       C  
ATOM   2932  SG  CYS A1188     -32.417 -21.307  -2.187  1.00100.42           S  
ANISOU 2932  SG  CYS A1188    16845  13437   7873    208    104  -1177       S  
ATOM   2933  N   LYS A1189     -32.246 -16.668  -0.629  1.00 97.90           N  
ANISOU 2933  N   LYS A1189    17837  12309   7052   1474   -305   -853       N  
ATOM   2934  CA  LYS A1189     -31.697 -15.401  -0.147  1.00 98.34           C  
ANISOU 2934  CA  LYS A1189    18471  11880   7014   1640   -358   -719       C  
ATOM   2935  C   LYS A1189     -32.441 -14.927   1.109  1.00103.22           C  
ANISOU 2935  C   LYS A1189    19046  12621   7553   1946   -391   -852       C  
ATOM   2936  O   LYS A1189     -31.799 -14.604   2.113  1.00102.23           O  
ANISOU 2936  O   LYS A1189    19149  12179   7513   1765   -338   -790       O  
ATOM   2937  CB  LYS A1189     -31.710 -14.333  -1.259  1.00103.14           C  
ANISOU 2937  CB  LYS A1189    19617  12241   7331   2002   -493   -614       C  
ATOM   2938  N   LYS A1190     -33.792 -14.961   1.071  1.00101.14           N  
ANISOU 2938  N   LYS A1190    18433  12878   7119   2385   -471  -1058       N  
ATOM   2939  CA  LYS A1190     -34.668 -14.557   2.173  1.00102.22           C  
ANISOU 2939  CA  LYS A1190    18444  13250   7145   2742   -470  -1230       C  
ATOM   2940  C   LYS A1190     -34.516 -15.452   3.410  1.00101.86           C  
ANISOU 2940  C   LYS A1190    18051  13334   7316   2292   -276  -1282       C  
ATOM   2941  O   LYS A1190     -34.472 -14.919   4.519  1.00102.50           O  
ANISOU 2941  O   LYS A1190    18343  13257   7346   2388   -237  -1306       O  
ATOM   2942  CB  LYS A1190     -36.135 -14.473   1.714  1.00108.59           C  
ANISOU 2942  CB  LYS A1190    18841  14697   7723   3306   -593  -1458       C  
ATOM   2943  CG  LYS A1190     -37.004 -13.600   2.615  1.00126.76           C  
ANISOU 2943  CG  LYS A1190    21187  17157   9818   3902   -622  -1623       C  
ATOM   2944  CD  LYS A1190     -38.460 -13.600   2.186  1.00138.22           C  
ANISOU 2944  CD  LYS A1190    22094  19364  11058   4469   -745  -1877       C  
ATOM   2945  CE  LYS A1190     -39.308 -12.758   3.109  1.00145.56           C  
ANISOU 2945  CE  LYS A1190    23032  20487  11786   5108   -739  -2062       C  
ATOM   2946  NZ  LYS A1190     -40.703 -12.644   2.614  1.00155.89           N1+
ANISOU 2946  NZ  LYS A1190    23783  22583  12867   5759   -892  -2316       N1+
ATOM   2947  N   ARG A1191     -34.437 -16.795   3.229  1.00 94.05           N  
ANISOU 2947  N   ARG A1191    16601  12598   6534   1813   -151  -1297       N  
ATOM   2948  CA  ARG A1191     -34.271 -17.746   4.338  1.00 91.09           C  
ANISOU 2948  CA  ARG A1191    15969  12302   6338   1376     40  -1310       C  
ATOM   2949  C   ARG A1191     -32.922 -17.559   5.021  1.00 90.91           C  
ANISOU 2949  C   ARG A1191    16361  11724   6458   1080     60  -1096       C  
ATOM   2950  O   ARG A1191     -32.871 -17.514   6.249  1.00 90.44           O  
ANISOU 2950  O   ARG A1191    16355  11624   6383   1014    126  -1108       O  
ATOM   2951  CB  ARG A1191     -34.441 -19.206   3.871  1.00 88.71           C  
ANISOU 2951  CB  ARG A1191    15208  12295   6204    938    170  -1362       C  
ATOM   2952  CG  ARG A1191     -34.283 -20.281   4.960  1.00 92.74           C  
ANISOU 2952  CG  ARG A1191    15535  12833   6869    482    383  -1345       C  
ATOM   2953  CD  ARG A1191     -35.514 -20.397   5.829  1.00106.48           C  
ANISOU 2953  CD  ARG A1191    16924  15074   8461    578    506  -1561       C  
ATOM   2954  NE  ARG A1191     -35.353 -21.371   6.910  1.00113.93           N  
ANISOU 2954  NE  ARG A1191    17798  15993   9497    135    728  -1513       N  
ATOM   2955  CZ  ARG A1191     -35.425 -21.075   8.205  1.00122.59           C  
ANISOU 2955  CZ  ARG A1191    19020  17069  10492    178    815  -1505       C  
ATOM   2956  NH1 ARG A1191     -35.635 -19.825   8.597  1.00107.53           N1+
ANISOU 2956  NH1 ARG A1191    17314  15139   8404    642    706  -1565       N1+
ATOM   2957  NH2 ARG A1191     -35.289 -22.027   9.117  1.00109.26           N  
ANISOU 2957  NH2 ARG A1191    17312  15352   8848   -230   1016  -1438       N  
ATOM   2958  N   ALA A1192     -31.842 -17.447   4.232  1.00 84.50           N  
ANISOU 2958  N   ALA A1192    15815  10531   5760    895      6   -918       N  
ATOM   2959  CA  ALA A1192     -30.492 -17.263   4.745  1.00 82.70           C  
ANISOU 2959  CA  ALA A1192    15899   9850   5672    586      5   -734       C  
ATOM   2960  C   ALA A1192     -30.386 -16.031   5.626  1.00 89.76           C  
ANISOU 2960  C   ALA A1192    17229  10477   6398    794    -84   -744       C  
ATOM   2961  O   ALA A1192     -29.782 -16.118   6.689  1.00 89.98           O  
ANISOU 2961  O   ALA A1192    17338  10363   6488    560    -71   -697       O  
ATOM   2962  CB  ALA A1192     -29.507 -17.178   3.606  1.00 82.50           C  
ANISOU 2962  CB  ALA A1192    16054   9544   5747    407    -16   -583       C  
ATOM   2963  N   MET A1193     -31.014 -14.906   5.224  1.00 88.42           N  
ANISOU 2963  N   MET A1193    17367  10241   5986   1260   -184   -818       N  
ATOM   2964  CA  MET A1193     -31.010 -13.671   6.015  1.00 89.96           C  
ANISOU 2964  CA  MET A1193    18069  10129   5983   1512   -255   -860       C  
ATOM   2965  C   MET A1193     -31.823 -13.856   7.279  1.00 92.24           C  
ANISOU 2965  C   MET A1193    18140  10726   6179   1670   -182  -1032       C  
ATOM   2966  O   MET A1193     -31.301 -13.589   8.354  1.00 92.38           O  
ANISOU 2966  O   MET A1193    18399  10524   6175   1498   -179  -1024       O  
ATOM   2967  CB  MET A1193     -31.563 -12.481   5.216  1.00 96.07           C  
ANISOU 2967  CB  MET A1193    19278  10731   6493   2058   -371   -892       C  
ATOM   2968  CG  MET A1193     -30.702 -12.080   4.051  1.00 99.92           C  
ANISOU 2968  CG  MET A1193    20145  10823   6996   1888   -418   -703       C  
ATOM   2969  SD  MET A1193     -31.624 -11.039   2.908  1.00108.56           S  
ANISOU 2969  SD  MET A1193    21648  11857   7743   2607   -559   -721       S  
ATOM   2970  CE  MET A1193     -30.789 -11.437   1.380  1.00103.69           C  
ANISOU 2970  CE  MET A1193    21074  11107   7216   2238   -535   -512       C  
ATOM   2971  N   SER A1194     -33.085 -14.336   7.156  1.00 88.17           N  
ANISOU 2971  N   SER A1194    17150  10757   5594   1959   -116  -1201       N  
ATOM   2972  CA  SER A1194     -34.006 -14.558   8.278  1.00 89.18           C  
ANISOU 2972  CA  SER A1194    16998  11280   5608   2107     11  -1391       C  
ATOM   2973  C   SER A1194     -33.446 -15.468   9.374  1.00 88.18           C  
ANISOU 2973  C   SER A1194    16737  11151   5617   1586    142  -1320       C  
ATOM   2974  O   SER A1194     -33.596 -15.140  10.548  1.00 89.83           O  
ANISOU 2974  O   SER A1194    17104  11351   5677   1653    200  -1400       O  
ATOM   2975  CB  SER A1194     -35.360 -15.066   7.792  1.00 96.01           C  
ANISOU 2975  CB  SER A1194    17265  12806   6408   2378     74  -1587       C  
ATOM   2976  OG  SER A1194     -35.315 -16.424   7.382  1.00107.30           O  
ANISOU 2976  OG  SER A1194    18217  14502   8049   1901    176  -1548       O  
ATOM   2977  N   PHE A1195     -32.784 -16.580   8.983  1.00 79.06           N  
ANISOU 2977  N   PHE A1195    15347   9980   4713   1109    183  -1168       N  
ATOM   2978  CA  PHE A1195     -32.153 -17.558   9.868  1.00 76.22           C  
ANISOU 2978  CA  PHE A1195    14898   9577   4485    648    280  -1053       C  
ATOM   2979  C   PHE A1195     -30.946 -16.951  10.597  1.00 78.71           C  
ANISOU 2979  C   PHE A1195    15671   9439   4798    492    150   -920       C  
ATOM   2980  O   PHE A1195     -30.780 -17.185  11.799  1.00 80.22           O  
ANISOU 2980  O   PHE A1195    15932   9637   4912    346    189   -908       O  
ATOM   2981  CB  PHE A1195     -31.710 -18.792   9.069  1.00 75.56           C  
ANISOU 2981  CB  PHE A1195    14526   9525   4660    282    337   -931       C  
ATOM   2982  CG  PHE A1195     -31.283 -19.977   9.902  1.00 76.44           C  
ANISOU 2982  CG  PHE A1195    14528   9632   4882   -114    458   -818       C  
ATOM   2983  CD1 PHE A1195     -29.976 -20.091  10.363  1.00 78.31           C  
ANISOU 2983  CD1 PHE A1195    14997   9523   5233   -340    358   -620       C  
ATOM   2984  CD2 PHE A1195     -32.181 -20.992  10.208  1.00 79.73           C  
ANISOU 2984  CD2 PHE A1195    14621  10402   5272   -267    670   -907       C  
ATOM   2985  CE1 PHE A1195     -29.581 -21.191  11.130  1.00 78.70           C  
ANISOU 2985  CE1 PHE A1195    14995   9557   5351   -622    441   -493       C  
ATOM   2986  CE2 PHE A1195     -31.786 -22.092  10.980  1.00 81.96           C  
ANISOU 2986  CE2 PHE A1195    14915  10608   5618   -618    792   -773       C  
ATOM   2987  CZ  PHE A1195     -30.486 -22.185  11.431  1.00 78.48           C  
ANISOU 2987  CZ  PHE A1195    14744   9798   5276   -750    663   -555       C  
ATOM   2988  N   SER A1196     -30.096 -16.208   9.861  1.00 71.57           N  
ANISOU 2988  N   SER A1196    15073   8163   3956    480      0   -825       N  
ATOM   2989  CA  SER A1196     -28.893 -15.549  10.366  1.00 70.09           C  
ANISOU 2989  CA  SER A1196    15292   7568   3773    262   -139   -726       C  
ATOM   2990  C   SER A1196     -29.202 -14.473  11.400  1.00 74.95           C  
ANISOU 2990  C   SER A1196    16326   8044   4108    486   -190   -868       C  
ATOM   2991  O   SER A1196     -28.488 -14.381  12.405  1.00 74.56           O  
ANISOU 2991  O   SER A1196    16467   7851   4013    242   -265   -838       O  
ATOM   2992  CB  SER A1196     -28.114 -14.931   9.215  1.00 73.12           C  
ANISOU 2992  CB  SER A1196    15905   7629   4248    185   -229   -626       C  
ATOM   2993  OG  SER A1196     -27.625 -15.955   8.370  1.00 82.19           O  
ANISOU 2993  OG  SER A1196    16697   8881   5651    -62   -172   -500       O  
ATOM   2994  N   VAL A 372     -30.247 -13.646  11.137  1.00 83.24           N  
ANISOU 2994  N   VAL A 372    14864   9977   6788  -1620    382    -68       N  
ATOM   2995  CA  VAL A 372     -30.676 -12.558  12.025  1.00 81.92           C  
ANISOU 2995  CA  VAL A 372    14658   9732   6735  -1608    258     30       C  
ATOM   2996  C   VAL A 372     -31.372 -13.130  13.254  1.00 82.04           C  
ANISOU 2996  C   VAL A 372    14441   9733   6996  -1453    156      0       C  
ATOM   2997  O   VAL A 372     -31.228 -12.571  14.340  1.00 81.75           O  
ANISOU 2997  O   VAL A 372    14267   9692   7102  -1428    151     38       O  
ATOM   2998  CB  VAL A 372     -31.482 -11.414  11.339  1.00 87.17           C  
ANISOU 2998  CB  VAL A 372    15600  10267   7254  -1657     71    139       C  
ATOM   2999  CG1 VAL A 372     -30.782 -10.921  10.072  1.00 88.74           C  
ANISOU 2999  CG1 VAL A 372    16061  10475   7182  -1836    180    172       C  
ATOM   3000  CG2 VAL A 372     -32.926 -11.816  11.046  1.00 87.14           C  
ANISOU 3000  CG2 VAL A 372    15652  10191   7266  -1535   -165    131       C  
ATOM   3001  N   ALA A 373     -32.076 -14.270  13.087  1.00 75.54           N  
ANISOU 3001  N   ALA A 373    13585   8908   6210  -1367     84    -70       N  
ATOM   3002  CA  ALA A 373     -32.757 -14.993  14.161  1.00 72.18           C  
ANISOU 3002  CA  ALA A 373    12956   8478   5991  -1250     -2   -106       C  
ATOM   3003  C   ALA A 373     -31.716 -15.531  15.127  1.00 73.28           C  
ANISOU 3003  C   ALA A 373    12886   8691   6265  -1218    171   -161       C  
ATOM   3004  O   ALA A 373     -31.875 -15.391  16.339  1.00 71.64           O  
ANISOU 3004  O   ALA A 373    12506   8482   6231  -1159    137   -141       O  
ATOM   3005  CB  ALA A 373     -33.562 -16.152  13.583  1.00 72.92           C  
ANISOU 3005  CB  ALA A 373    13103   8554   6049  -1215    -93   -174       C  
ATOM   3006  N   GLN A 374     -30.644 -16.135  14.580  1.00 69.66           N  
ANISOU 3006  N   GLN A 374    12442   8306   5718  -1246    352   -235       N  
ATOM   3007  CA  GLN A 374     -29.561 -16.726  15.358  1.00 68.72           C  
ANISOU 3007  CA  GLN A 374    12129   8275   5705  -1193    515   -305       C  
ATOM   3008  C   GLN A 374     -28.678 -15.679  16.027  1.00 70.63           C  
ANISOU 3008  C   GLN A 374    12260   8581   5996  -1255    611   -251       C  
ATOM   3009  O   GLN A 374     -28.256 -15.912  17.157  1.00 68.48           O  
ANISOU 3009  O   GLN A 374    11790   8347   5883  -1187    652   -273       O  
ATOM   3010  CB  GLN A 374     -28.747 -17.729  14.531  1.00 71.58           C  
ANISOU 3010  CB  GLN A 374    12537   8711   5949  -1172    667   -419       C  
ATOM   3011  CG  GLN A 374     -29.531 -19.013  14.271  1.00 90.99           C  
ANISOU 3011  CG  GLN A 374    15069  11091   8412  -1087    569   -491       C  
ATOM   3012  CD  GLN A 374     -28.680 -20.252  14.220  1.00112.96           C  
ANISOU 3012  CD  GLN A 374    17809  13923  11185   -984    701   -624       C  
ATOM   3013  OE1 GLN A 374     -27.631 -20.301  13.561  1.00107.51           O  
ANISOU 3013  OE1 GLN A 374    17134  13342  10372   -992    873   -690       O  
ATOM   3014  NE2 GLN A 374     -29.146 -21.304  14.889  1.00107.22           N  
ANISOU 3014  NE2 GLN A 374    17043  13119  10577   -885    618   -670       N  
ATOM   3015  N   ALA A 375     -28.439 -14.522  15.371  1.00 67.51           N  
ANISOU 3015  N   ALA A 375    12007   8186   5460  -1392    634   -177       N  
ATOM   3016  CA  ALA A 375     -27.649 -13.437  15.952  1.00 67.29           C  
ANISOU 3016  CA  ALA A 375    11908   8202   5456  -1488    710   -117       C  
ATOM   3017  C   ALA A 375     -28.342 -12.871  17.186  1.00 71.19           C  
ANISOU 3017  C   ALA A 375    12313   8608   6128  -1421    564    -51       C  
ATOM   3018  O   ALA A 375     -27.691 -12.694  18.225  1.00 69.93           O  
ANISOU 3018  O   ALA A 375    11975   8502   6093  -1412    629    -56       O  
ATOM   3019  CB  ALA A 375     -27.439 -12.335  14.936  1.00 69.58           C  
ANISOU 3019  CB  ALA A 375    12430   8473   5536  -1666    733    -40       C  
ATOM   3020  N   ARG A 376     -29.668 -12.610  17.077  1.00 68.74           N  
ANISOU 3020  N   ARG A 376    12117   8177   5824  -1367    364      0       N  
ATOM   3021  CA  ARG A 376     -30.465 -12.061  18.172  1.00 67.89           C  
ANISOU 3021  CA  ARG A 376    11932   7997   5867  -1285    217     52       C  
ATOM   3022  C   ARG A 376     -30.678 -13.099  19.297  1.00 71.25           C  
ANISOU 3022  C   ARG A 376    12125   8459   6486  -1161    214    -11       C  
ATOM   3023  O   ARG A 376     -30.690 -12.731  20.469  1.00 70.33           O  
ANISOU 3023  O   ARG A 376    11876   8338   6507  -1117    190     11       O  
ATOM   3024  CB  ARG A 376     -31.776 -11.402  17.682  1.00 68.93           C  
ANISOU 3024  CB  ARG A 376    12240   8017   5932  -1251      4    115       C  
ATOM   3025  CG  ARG A 376     -32.843 -12.325  17.120  1.00 89.33           C  
ANISOU 3025  CG  ARG A 376    14851  10592   8500  -1176   -111     71       C  
ATOM   3026  CD  ARG A 376     -34.131 -11.583  16.810  1.00111.22           C  
ANISOU 3026  CD  ARG A 376    17750  13282  11227  -1119   -337    126       C  
ATOM   3027  NE  ARG A 376     -34.964 -11.408  18.005  1.00124.23           N  
ANISOU 3027  NE  ARG A 376    19225  14930  13046   -998   -454    130       N  
ATOM   3028  CZ  ARG A 376     -35.247 -10.235  18.568  1.00138.66           C  
ANISOU 3028  CZ  ARG A 376    21080  16699  14904   -947   -548    188       C  
ATOM   3029  NH1 ARG A 376     -34.780  -9.106  18.043  1.00120.17           N1+
ANISOU 3029  NH1 ARG A 376    18957  14272  12431  -1018   -553    258       N1+
ATOM   3030  NH2 ARG A 376     -36.006 -10.181  19.655  1.00128.24           N  
ANISOU 3030  NH2 ARG A 376    19586  15404  13735   -829   -639    175       N  
ATOM   3031  N   GLU A 377     -30.763 -14.386  18.956  1.00 68.76           N  
ANISOU 3031  N   GLU A 377    11781   8174   6170  -1114    246    -90       N  
ATOM   3032  CA  GLU A 377     -30.899 -15.415  19.986  1.00 67.41           C  
ANISOU 3032  CA  GLU A 377    11432   8020   6160  -1015    244   -145       C  
ATOM   3033  C   GLU A 377     -29.581 -15.618  20.723  1.00 70.12           C  
ANISOU 3033  C   GLU A 377    11621   8444   6578  -1001    403   -185       C  
ATOM   3034  O   GLU A 377     -29.606 -15.825  21.932  1.00 69.03           O  
ANISOU 3034  O   GLU A 377    11333   8307   6588   -935    385   -187       O  
ATOM   3035  CB  GLU A 377     -31.481 -16.721  19.430  1.00 69.10           C  
ANISOU 3035  CB  GLU A 377    11701   8213   6342   -976    203   -213       C  
ATOM   3036  CG  GLU A 377     -32.986 -16.651  19.197  1.00 83.82           C  
ANISOU 3036  CG  GLU A 377    13630  10020   8198   -970     10   -180       C  
ATOM   3037  CD  GLU A 377     -33.853 -16.359  20.412  1.00117.42           C  
ANISOU 3037  CD  GLU A 377    17740  14269  12605   -917   -102   -143       C  
ATOM   3038  OE1 GLU A 377     -33.730 -17.080  21.429  1.00115.19           O  
ANISOU 3038  OE1 GLU A 377    17319  14001  12447   -876    -68   -175       O  
ATOM   3039  OE2 GLU A 377     -34.662 -15.407  20.340  1.00119.70           O1-
ANISOU 3039  OE2 GLU A 377    18064  14540  12878   -909   -228    -87       O1-
ATOM   3040  N   LYS A 378     -28.434 -15.466  20.010  1.00 66.85           N  
ANISOU 3040  N   LYS A 378    11238   8113   6051  -1070    556   -214       N  
ATOM   3041  CA  LYS A 378     -27.068 -15.563  20.549  1.00 65.68           C  
ANISOU 3041  CA  LYS A 378    10926   8082   5948  -1067    715   -262       C  
ATOM   3042  C   LYS A 378     -26.859 -14.431  21.534  1.00 67.35           C  
ANISOU 3042  C   LYS A 378    11051   8292   6247  -1118    694   -188       C  
ATOM   3043  O   LYS A 378     -26.195 -14.618  22.555  1.00 66.62           O  
ANISOU 3043  O   LYS A 378    10781   8260   6272  -1069    744   -216       O  
ATOM   3044  CB  LYS A 378     -26.013 -15.506  19.421  1.00 68.94           C  
ANISOU 3044  CB  LYS A 378    11391   8611   6191  -1156    882   -309       C  
ATOM   3045  CG  LYS A 378     -24.619 -15.975  19.832  1.00 71.42           C  
ANISOU 3045  CG  LYS A 378    11506   9089   6544  -1113   1050   -400       C  
ATOM   3046  CD  LYS A 378     -23.712 -16.263  18.636  1.00 78.78           C  
ANISOU 3046  CD  LYS A 378    12473  10161   7299  -1163   1221   -482       C  
ATOM   3047  CE  LYS A 378     -23.505 -17.747  18.386  1.00 90.39           C  
ANISOU 3047  CE  LYS A 378    13917  11660   8768   -988   1264   -614       C  
ATOM   3048  NZ  LYS A 378     -23.060 -18.016  16.995  1.00 95.06           N1+
ANISOU 3048  NZ  LYS A 378    14621  12342   9155  -1032   1391   -686       N1+
ATOM   3049  N   ARG A 379     -27.462 -13.264  21.231  1.00 62.89           N  
ANISOU 3049  N   ARG A 379    10631   7645   5618  -1206    602    -95       N  
ATOM   3050  CA  ARG A 379     -27.439 -12.055  22.055  1.00 60.75           C  
ANISOU 3050  CA  ARG A 379    10344   7334   5404  -1257    552    -18       C  
ATOM   3051  C   ARG A 379     -28.270 -12.263  23.318  1.00 62.55           C  
ANISOU 3051  C   ARG A 379    10457   7502   5806  -1127    431    -10       C  
ATOM   3052  O   ARG A 379     -27.795 -11.937  24.399  1.00 63.20           O  
ANISOU 3052  O   ARG A 379    10412   7608   5991  -1118    453     -3       O  
ATOM   3053  CB  ARG A 379     -27.998 -10.858  21.271  1.00 58.33           C  
ANISOU 3053  CB  ARG A 379    10276   6925   4961  -1355    459     72       C  
ATOM   3054  CG  ARG A 379     -26.940  -9.917  20.750  1.00 69.01           C  
ANISOU 3054  CG  ARG A 379    11723   8322   6177  -1546    574    110       C  
ATOM   3055  CD  ARG A 379     -27.566  -8.826  19.892  1.00 81.69           C  
ANISOU 3055  CD  ARG A 379    13620   9793   7624  -1635    462    202       C  
ATOM   3056  NE  ARG A 379     -27.735  -9.217  18.485  1.00 83.82           N  
ANISOU 3056  NE  ARG A 379    14055  10071   7723  -1680    485    190       N  
ATOM   3057  CZ  ARG A 379     -28.806  -8.938  17.746  1.00 81.17           C  
ANISOU 3057  CZ  ARG A 379    13934   9614   7294  -1644    327    235       C  
ATOM   3058  NH1 ARG A 379     -29.842  -8.298  18.279  1.00 59.21           N  
ANISOU 3058  NH1 ARG A 379    11210   6707   4582  -1542    133    288       N  
ATOM   3059  NH2 ARG A 379     -28.860  -9.319  16.479  1.00 61.94           N1+
ANISOU 3059  NH2 ARG A 379    11649   7192   4692  -1695    356    219       N1+
ATOM   3060  N   PHE A 380     -29.503 -12.795  23.190  1.00 57.02           N  
ANISOU 3060  N   PHE A 380     9798   6737   5129  -1039    306    -14       N  
ATOM   3061  CA  PHE A 380     -30.383 -12.996  24.332  1.00 55.81           C  
ANISOU 3061  CA  PHE A 380     9535   6550   5120   -936    199     -9       C  
ATOM   3062  C   PHE A 380     -29.781 -13.939  25.352  1.00 59.10           C  
ANISOU 3062  C   PHE A 380     9772   7022   5661   -875    276    -65       C  
ATOM   3063  O   PHE A 380     -29.948 -13.728  26.547  1.00 58.40           O  
ANISOU 3063  O   PHE A 380     9577   6926   5687   -829    238    -49       O  
ATOM   3064  CB  PHE A 380     -31.802 -13.429  23.913  1.00 58.17           C  
ANISOU 3064  CB  PHE A 380     9895   6804   5404   -882     59    -12       C  
ATOM   3065  CG  PHE A 380     -32.851 -12.996  24.915  1.00 59.53           C  
ANISOU 3065  CG  PHE A 380     9988   6953   5679   -805    -70     17       C  
ATOM   3066  CD1 PHE A 380     -33.407 -11.726  24.858  1.00 63.93           C  
ANISOU 3066  CD1 PHE A 380    10634   7457   6199   -789   -178     73       C  
ATOM   3067  CD2 PHE A 380     -33.229 -13.831  25.954  1.00 61.01           C  
ANISOU 3067  CD2 PHE A 380    10021   7170   5989   -747    -80    -17       C  
ATOM   3068  CE1 PHE A 380     -34.323 -11.301  25.818  1.00 64.49           C  
ANISOU 3068  CE1 PHE A 380    10619   7525   6359   -695   -286     83       C  
ATOM   3069  CE2 PHE A 380     -34.155 -13.409  26.906  1.00 63.83           C  
ANISOU 3069  CE2 PHE A 380    10291   7533   6429   -683   -179      1       C  
ATOM   3070  CZ  PHE A 380     -34.697 -12.148  26.831  1.00 62.62           C  
ANISOU 3070  CZ  PHE A 380    10205   7346   6242   -647   -278     44       C  
ATOM   3071  N   THR A 381     -29.023 -14.931  24.883  1.00 55.54           N  
ANISOU 3071  N   THR A 381     9300   6627   5177   -866    382   -134       N  
ATOM   3072  CA  THR A 381     -28.316 -15.902  25.710  1.00 53.93           C  
ANISOU 3072  CA  THR A 381     8954   6469   5068   -787    450   -197       C  
ATOM   3073  C   THR A 381     -27.239 -15.214  26.538  1.00 54.93           C  
ANISOU 3073  C   THR A 381     8952   6665   5252   -810    525   -186       C  
ATOM   3074  O   THR A 381     -27.038 -15.610  27.684  1.00 55.27           O  
ANISOU 3074  O   THR A 381     8873   6716   5409   -737    515   -203       O  
ATOM   3075  CB  THR A 381     -27.780 -17.024  24.822  1.00 62.28           C  
ANISOU 3075  CB  THR A 381    10054   7563   6048   -753    535   -282       C  
ATOM   3076  OG1 THR A 381     -28.909 -17.685  24.248  1.00 60.28           O  
ANISOU 3076  OG1 THR A 381     9920   7229   5755   -741    439   -288       O  
ATOM   3077  CG2 THR A 381     -26.924 -18.031  25.585  1.00 62.26           C  
ANISOU 3077  CG2 THR A 381     9926   7604   6126   -643    599   -358       C  
ATOM   3078  N   PHE A 382     -26.547 -14.201  25.971  1.00 49.18           N  
ANISOU 3078  N   PHE A 382     8262   5986   4436   -925    594   -157       N  
ATOM   3079  CA  PHE A 382     -25.499 -13.468  26.675  1.00 48.36           C  
ANISOU 3079  CA  PHE A 382     8043   5960   4371   -985    662   -147       C  
ATOM   3080  C   PHE A 382     -26.086 -12.674  27.844  1.00 54.79           C  
ANISOU 3080  C   PHE A 382     8839   6694   5285   -972    554    -82       C  
ATOM   3081  O   PHE A 382     -25.521 -12.660  28.942  1.00 54.97           O  
ANISOU 3081  O   PHE A 382     8724   6759   5404   -943    569    -95       O  
ATOM   3082  CB  PHE A 382     -24.707 -12.551  25.730  1.00 50.71           C  
ANISOU 3082  CB  PHE A 382     8414   6326   4528  -1153    759   -125       C  
ATOM   3083  CG  PHE A 382     -23.928 -11.490  26.467  1.00 53.16           C  
ANISOU 3083  CG  PHE A 382     8652   6681   4866  -1262    788    -88       C  
ATOM   3084  CD1 PHE A 382     -22.825 -11.824  27.243  1.00 57.61           C  
ANISOU 3084  CD1 PHE A 382     9004   7380   5506  -1239    871   -147       C  
ATOM   3085  CD2 PHE A 382     -24.357 -10.169  26.474  1.00 56.54           C  
ANISOU 3085  CD2 PHE A 382     9233   7003   5246  -1372    709      4       C  
ATOM   3086  CE1 PHE A 382     -22.153 -10.847  27.993  1.00 58.49           C  
ANISOU 3086  CE1 PHE A 382     9047   7531   5644  -1351    881   -113       C  
ATOM   3087  CE2 PHE A 382     -23.672  -9.193  27.211  1.00 59.16           C  
ANISOU 3087  CE2 PHE A 382     9523   7355   5599  -1483    722     38       C  
ATOM   3088  CZ  PHE A 382     -22.561  -9.536  27.941  1.00 57.13           C  
ANISOU 3088  CZ  PHE A 382     9044   7246   5415  -1486    812    -20       C  
ATOM   3089  N   VAL A 383     -27.208 -11.988  27.583  1.00 51.54           N  
ANISOU 3089  N   VAL A 383     8569   6174   4839   -986    439    -20       N  
ATOM   3090  CA  VAL A 383     -27.936 -11.153  28.534  1.00 49.84           C  
ANISOU 3090  CA  VAL A 383     8364   5878   4694   -954    326     34       C  
ATOM   3091  C   VAL A 383     -28.342 -12.027  29.723  1.00 53.49           C  
ANISOU 3091  C   VAL A 383     8682   6348   5292   -832    290      1       C  
ATOM   3092  O   VAL A 383     -28.156 -11.631  30.879  1.00 55.08           O  
ANISOU 3092  O   VAL A 383     8803   6548   5575   -811    272     12       O  
ATOM   3093  CB  VAL A 383     -29.133 -10.499  27.810  1.00 53.28           C  
ANISOU 3093  CB  VAL A 383     8977   6215   5051   -949    204     83       C  
ATOM   3094  CG1 VAL A 383     -30.029  -9.729  28.768  1.00 52.47           C  
ANISOU 3094  CG1 VAL A 383     8878   6041   5017   -873     77    118       C  
ATOM   3095  CG2 VAL A 383     -28.648  -9.605  26.677  1.00 54.37           C  
ANISOU 3095  CG2 VAL A 383     9293   6329   5037  -1085    236    126       C  
ATOM   3096  N   LEU A 384     -28.797 -13.251  29.427  1.00 47.09           N  
ANISOU 3096  N   LEU A 384     7856   5545   4493   -768    287    -42       N  
ATOM   3097  CA  LEU A 384     -29.205 -14.238  30.413  1.00 44.87           C  
ANISOU 3097  CA  LEU A 384     7477   5260   4313   -679    256    -71       C  
ATOM   3098  C   LEU A 384     -28.025 -14.775  31.223  1.00 49.69           C  
ANISOU 3098  C   LEU A 384     7963   5928   4989   -643    336   -112       C  
ATOM   3099  O   LEU A 384     -28.232 -15.241  32.347  1.00 50.67           O  
ANISOU 3099  O   LEU A 384     8015   6037   5199   -581    301   -117       O  
ATOM   3100  CB  LEU A 384     -29.968 -15.378  29.733  1.00 44.29           C  
ANISOU 3100  CB  LEU A 384     7460   5164   4206   -652    225   -104       C  
ATOM   3101  CG  LEU A 384     -31.297 -15.025  29.075  1.00 47.13           C  
ANISOU 3101  CG  LEU A 384     7910   5484   4512   -670    119    -74       C  
ATOM   3102  CD1 LEU A 384     -31.898 -16.224  28.470  1.00 45.80           C  
ANISOU 3102  CD1 LEU A 384     7789   5302   4310   -666     93   -113       C  
ATOM   3103  CD2 LEU A 384     -32.272 -14.318  30.049  1.00 48.03           C  
ANISOU 3103  CD2 LEU A 384     7968   5588   4693   -634     21    -36       C  
ATOM   3104  N   ALA A 385     -26.798 -14.717  30.668  1.00 44.70           N  
ANISOU 3104  N   ALA A 385     7304   5373   4309   -681    440   -145       N  
ATOM   3105  CA  ALA A 385     -25.603 -15.120  31.402  1.00 44.44           C  
ANISOU 3105  CA  ALA A 385     7130   5421   4333   -635    507   -193       C  
ATOM   3106  C   ALA A 385     -25.329 -14.013  32.417  1.00 49.74           C  
ANISOU 3106  C   ALA A 385     7739   6101   5060   -684    481   -147       C  
ATOM   3107  O   ALA A 385     -25.041 -14.319  33.576  1.00 50.01           O  
ANISOU 3107  O   ALA A 385     7675   6147   5181   -618    460   -161       O  
ATOM   3108  CB  ALA A 385     -24.420 -15.257  30.462  1.00 46.36           C  
ANISOU 3108  CB  ALA A 385     7337   5782   4498   -669    630   -251       C  
ATOM   3109  N   VAL A 386     -25.470 -12.722  31.990  1.00 45.06           N  
ANISOU 3109  N   VAL A 386     7231   5484   4407   -800    470    -90       N  
ATOM   3110  CA  VAL A 386     -25.285 -11.546  32.838  1.00 43.72           C  
ANISOU 3110  CA  VAL A 386     7051   5293   4267   -861    433    -45       C  
ATOM   3111  C   VAL A 386     -26.239 -11.668  34.026  1.00 48.49           C  
ANISOU 3111  C   VAL A 386     7638   5823   4963   -760    333    -27       C  
ATOM   3112  O   VAL A 386     -25.772 -11.601  35.153  1.00 49.13           O  
ANISOU 3112  O   VAL A 386     7626   5927   5114   -736    326    -35       O  
ATOM   3113  CB  VAL A 386     -25.427 -10.199  32.057  1.00 46.86           C  
ANISOU 3113  CB  VAL A 386     7608   5637   4561   -995    417     16       C  
ATOM   3114  CG1 VAL A 386     -25.343  -8.988  32.990  1.00 46.09           C  
ANISOU 3114  CG1 VAL A 386     7540   5484   4489  -1048    357     61       C  
ATOM   3115  CG2 VAL A 386     -24.378 -10.091  30.957  1.00 47.49           C  
ANISOU 3115  CG2 VAL A 386     7696   5813   4534  -1126    536     -2       C  
ATOM   3116  N   VAL A 387     -27.545 -11.962  33.773  1.00 44.51           N  
ANISOU 3116  N   VAL A 387     7208   5251   4454   -702    261    -12       N  
ATOM   3117  CA  VAL A 387     -28.582 -12.196  34.799  1.00 42.44           C  
ANISOU 3117  CA  VAL A 387     6915   4948   4262   -617    180     -5       C  
ATOM   3118  C   VAL A 387     -28.111 -13.244  35.816  1.00 47.83           C  
ANISOU 3118  C   VAL A 387     7485   5665   5022   -556    206    -40       C  
ATOM   3119  O   VAL A 387     -28.236 -13.004  37.007  1.00 48.25           O  
ANISOU 3119  O   VAL A 387     7491   5709   5131   -525    171    -29       O  
ATOM   3120  CB  VAL A 387     -29.975 -12.548  34.177  1.00 44.29           C  
ANISOU 3120  CB  VAL A 387     7215   5148   4466   -584    113      1       C  
ATOM   3121  CG1 VAL A 387     -30.938 -13.117  35.217  1.00 42.68           C  
ANISOU 3121  CG1 VAL A 387     6944   4947   4327   -519     59     -7       C  
ATOM   3122  CG2 VAL A 387     -30.600 -11.348  33.470  1.00 43.91           C  
ANISOU 3122  CG2 VAL A 387     7285   5051   4347   -607     47     40       C  
ATOM   3123  N   MET A 388     -27.517 -14.358  35.338  1.00 48.69           N  
ANISOU 3123  N   MET A 388     7569   5808   5123   -531    263    -85       N  
ATOM   3124  CA  MET A 388     -26.978 -15.483  36.132  1.00 50.16           C  
ANISOU 3124  CA  MET A 388     7685   6011   5364   -452    276   -125       C  
ATOM   3125  C   MET A 388     -25.729 -15.097  36.930  1.00 51.12           C  
ANISOU 3125  C   MET A 388     7698   6197   5526   -444    306   -141       C  
ATOM   3126  O   MET A 388     -25.652 -15.438  38.101  1.00 51.18           O  
ANISOU 3126  O   MET A 388     7662   6193   5591   -387    269   -142       O  
ATOM   3127  CB  MET A 388     -26.737 -16.751  35.268  1.00 54.54           C  
ANISOU 3127  CB  MET A 388     8277   6565   5881   -405    314   -180       C  
ATOM   3128  CG  MET A 388     -28.038 -17.459  34.871  1.00 61.13           C  
ANISOU 3128  CG  MET A 388     9212   7326   6689   -410    260   -170       C  
ATOM   3129  SD  MET A 388     -28.055 -18.602  33.418  1.00 69.66           S  
ANISOU 3129  SD  MET A 388    10401   8382   7685   -395    291   -226       S  
ATOM   3130  CE  MET A 388     -29.679 -18.261  32.749  1.00 65.90           C  
ANISOU 3130  CE  MET A 388    10012   7864   7164   -478    215   -181       C  
ATOM   3131  N   GLY A 389     -24.782 -14.396  36.313  1.00 45.37           N  
ANISOU 3131  N   GLY A 389     6933   5546   4761   -514    370   -151       N  
ATOM   3132  CA  GLY A 389     -23.554 -13.975  36.978  1.00 45.47           C  
ANISOU 3132  CA  GLY A 389     6824   5649   4805   -533    398   -172       C  
ATOM   3133  C   GLY A 389     -23.811 -13.005  38.113  1.00 50.38           C  
ANISOU 3133  C   GLY A 389     7448   6227   5467   -571    333   -124       C  
ATOM   3134  O   GLY A 389     -23.301 -13.188  39.226  1.00 51.42           O  
ANISOU 3134  O   GLY A 389     7497   6385   5655   -522    305   -140       O  
ATOM   3135  N   VAL A 390     -24.656 -11.985  37.849  1.00 45.27           N  
ANISOU 3135  N   VAL A 390     6912   5503   4785   -640    296    -70       N  
ATOM   3136  CA  VAL A 390     -25.052 -10.963  38.821  1.00 43.32           C  
ANISOU 3136  CA  VAL A 390     6703   5196   4560   -662    228    -32       C  
ATOM   3137  C   VAL A 390     -25.764 -11.603  40.027  1.00 46.99           C  
ANISOU 3137  C   VAL A 390     7142   5624   5089   -554    170    -34       C  
ATOM   3138  O   VAL A 390     -25.518 -11.172  41.144  1.00 46.84           O  
ANISOU 3138  O   VAL A 390     7093   5601   5102   -548    135    -29       O  
ATOM   3139  CB  VAL A 390     -25.851  -9.808  38.164  1.00 46.59           C  
ANISOU 3139  CB  VAL A 390     7266   5527   4911   -724    188     16       C  
ATOM   3140  CG1 VAL A 390     -26.304  -8.787  39.196  1.00 45.99           C  
ANISOU 3140  CG1 VAL A 390     7245   5378   4850   -713    110     41       C  
ATOM   3141  CG2 VAL A 390     -25.022  -9.109  37.092  1.00 47.57           C  
ANISOU 3141  CG2 VAL A 390     7440   5681   4953   -864    246     27       C  
ATOM   3142  N   TRP A 391     -26.573 -12.673  39.817  1.00 43.61           N  
ANISOU 3142  N   TRP A 391     6729   5174   4667   -485    164    -43       N  
ATOM   3143  CA  TRP A 391     -27.262 -13.396  40.895  1.00 42.81           C  
ANISOU 3143  CA  TRP A 391     6615   5045   4604   -415    121    -42       C  
ATOM   3144  C   TRP A 391     -26.274 -14.148  41.795  1.00 44.66           C  
ANISOU 3144  C   TRP A 391     6779   5310   4881   -363    125    -69       C  
ATOM   3145  O   TRP A 391     -26.381 -14.118  43.033  1.00 43.33           O  
ANISOU 3145  O   TRP A 391     6598   5127   4739   -335     85    -60       O  
ATOM   3146  CB  TRP A 391     -28.298 -14.358  40.311  1.00 41.91           C  
ANISOU 3146  CB  TRP A 391     6549   4904   4471   -394    115    -45       C  
ATOM   3147  CG  TRP A 391     -29.116 -15.099  41.336  1.00 42.72           C  
ANISOU 3147  CG  TRP A 391     6653   4986   4592   -363     79    -39       C  
ATOM   3148  CD1 TRP A 391     -30.329 -14.730  41.833  1.00 45.22           C  
ANISOU 3148  CD1 TRP A 391     6975   5305   4903   -370     43    -21       C  
ATOM   3149  CD2 TRP A 391     -28.793 -16.358  41.953  1.00 43.05           C  
ANISOU 3149  CD2 TRP A 391     6702   5005   4648   -325     76    -53       C  
ATOM   3150  NE1 TRP A 391     -30.785 -15.676  42.723  1.00 44.96           N  
ANISOU 3150  NE1 TRP A 391     6943   5267   4873   -367     32    -19       N  
ATOM   3151  CE2 TRP A 391     -29.856 -16.680  42.828  1.00 46.80           C  
ANISOU 3151  CE2 TRP A 391     7198   5468   5117   -342     45    -33       C  
ATOM   3152  CE3 TRP A 391     -27.705 -17.250  41.853  1.00 45.45           C  
ANISOU 3152  CE3 TRP A 391     7005   5303   4960   -270     92    -86       C  
ATOM   3153  CZ2 TRP A 391     -29.864 -17.854  43.605  1.00 46.77           C  
ANISOU 3153  CZ2 TRP A 391     7242   5422   5105   -332     27    -31       C  
ATOM   3154  CZ3 TRP A 391     -27.701 -18.401  42.638  1.00 47.49           C  
ANISOU 3154  CZ3 TRP A 391     7315   5510   5219   -225     59    -91       C  
ATOM   3155  CH2 TRP A 391     -28.763 -18.686  43.512  1.00 47.85           C  
ANISOU 3155  CH2 TRP A 391     7409   5521   5250   -268     27    -56       C  
ATOM   3156  N   VAL A 392     -25.326 -14.826  41.160  1.00 41.06           N  
ANISOU 3156  N   VAL A 392     6280   4900   4419   -338    169   -109       N  
ATOM   3157  CA  VAL A 392     -24.298 -15.605  41.833  1.00 42.47           C  
ANISOU 3157  CA  VAL A 392     6389   5118   4630   -257    162   -149       C  
ATOM   3158  C   VAL A 392     -23.407 -14.688  42.671  1.00 46.43           C  
ANISOU 3158  C   VAL A 392     6801   5681   5158   -289    145   -149       C  
ATOM   3159  O   VAL A 392     -23.106 -15.038  43.815  1.00 42.92           O  
ANISOU 3159  O   VAL A 392     6331   5232   4744   -227     94   -155       O  
ATOM   3160  CB  VAL A 392     -23.510 -16.492  40.825  1.00 47.96           C  
ANISOU 3160  CB  VAL A 392     7052   5866   5304   -198    215   -209       C  
ATOM   3161  CG1 VAL A 392     -22.289 -17.146  41.476  1.00 48.76           C  
ANISOU 3161  CG1 VAL A 392     7057   6033   5435    -87    198   -265       C  
ATOM   3162  CG2 VAL A 392     -24.421 -17.545  40.198  1.00 47.21           C  
ANISOU 3162  CG2 VAL A 392     7074   5686   5179   -163    210   -212       C  
ATOM   3163  N   LEU A 393     -23.032 -13.497  42.118  1.00 45.88           N  
ANISOU 3163  N   LEU A 393     6707   5658   5066   -400    180   -138       N  
ATOM   3164  CA  LEU A 393     -22.200 -12.532  42.850  1.00 47.36           C  
ANISOU 3164  CA  LEU A 393     6827   5899   5267   -467    160   -137       C  
ATOM   3165  C   LEU A 393     -22.951 -11.854  43.976  1.00 51.03           C  
ANISOU 3165  C   LEU A 393     7367   6278   5745   -474     90    -97       C  
ATOM   3166  O   LEU A 393     -22.342 -11.539  44.992  1.00 51.06           O  
ANISOU 3166  O   LEU A 393     7322   6308   5769   -479     48   -104       O  
ATOM   3167  CB  LEU A 393     -21.524 -11.511  41.936  1.00 48.85           C  
ANISOU 3167  CB  LEU A 393     6993   6157   5410   -612    218   -137       C  
ATOM   3168  CG  LEU A 393     -20.795 -12.117  40.741  1.00 56.50           C  
ANISOU 3168  CG  LEU A 393     7884   7236   6348   -615    307   -185       C  
ATOM   3169  CD1 LEU A 393     -20.622 -11.101  39.623  1.00 58.37           C  
ANISOU 3169  CD1 LEU A 393     8169   7499   6509   -783    370   -162       C  
ATOM   3170  CD2 LEU A 393     -19.490 -12.819  41.143  1.00 59.84           C  
ANISOU 3170  CD2 LEU A 393     8125   7808   6805   -539    321   -259       C  
ATOM   3171  N   CYS A 394     -24.272 -11.669  43.820  1.00 47.52           N  
ANISOU 3171  N   CYS A 394     7031   5744   5282   -465     74    -62       N  
ATOM   3172  CA  CYS A 394     -25.143 -11.066  44.833  1.00 47.30           C  
ANISOU 3172  CA  CYS A 394     7068   5648   5254   -449     17    -37       C  
ATOM   3173  C   CYS A 394     -25.392 -12.004  46.044  1.00 49.68           C  
ANISOU 3173  C   CYS A 394     7353   5941   5582   -363    -16    -42       C  
ATOM   3174  O   CYS A 394     -25.543 -11.518  47.167  1.00 50.95           O  
ANISOU 3174  O   CYS A 394     7534   6082   5742   -355    -59    -35       O  
ATOM   3175  CB  CYS A 394     -26.458 -10.587  44.211  1.00 47.82           C  
ANISOU 3175  CB  CYS A 394     7229   5655   5287   -449     10    -13       C  
ATOM   3176  SG  CYS A 394     -26.351  -8.989  43.346  1.00 52.48           S  
ANISOU 3176  SG  CYS A 394     7917   6199   5823   -546      1     10       S  
ATOM   3177  N   TRP A 395     -25.462 -13.323  45.815  1.00 43.52           N  
ANISOU 3177  N   TRP A 395     6561   5164   4810   -306      0    -54       N  
ATOM   3178  CA  TRP A 395     -25.721 -14.286  46.877  1.00 42.79           C  
ANISOU 3178  CA  TRP A 395     6493   5043   4721   -243    -36    -50       C  
ATOM   3179  C   TRP A 395     -24.497 -15.023  47.382  1.00 47.78           C  
ANISOU 3179  C   TRP A 395     7076   5704   5375   -177    -65    -79       C  
ATOM   3180  O   TRP A 395     -24.596 -15.683  48.413  1.00 48.84           O  
ANISOU 3180  O   TRP A 395     7254   5801   5501   -128   -112    -70       O  
ATOM   3181  CB  TRP A 395     -26.771 -15.303  46.441  1.00 41.57           C  
ANISOU 3181  CB  TRP A 395     6403   4846   4545   -233    -21    -39       C  
ATOM   3182  CG  TRP A 395     -28.149 -14.743  46.395  1.00 42.16           C  
ANISOU 3182  CG  TRP A 395     6511   4914   4596   -275    -15    -17       C  
ATOM   3183  CD1 TRP A 395     -28.873 -14.421  45.283  1.00 44.63           C  
ANISOU 3183  CD1 TRP A 395     6834   5232   4893   -305      6    -15       C  
ATOM   3184  CD2 TRP A 395     -28.975 -14.421  47.524  1.00 42.03           C  
ANISOU 3184  CD2 TRP A 395     6511   4899   4559   -279    -35     -4       C  
ATOM   3185  NE1 TRP A 395     -30.115 -13.951  45.645  1.00 44.00           N  
ANISOU 3185  NE1 TRP A 395     6763   5165   4791   -313     -7     -5       N  
ATOM   3186  CE2 TRP A 395     -30.202 -13.933  47.020  1.00 45.90           C  
ANISOU 3186  CE2 TRP A 395     7002   5411   5027   -298    -24     -2       C  
ATOM   3187  CE3 TRP A 395     -28.799 -14.501  48.920  1.00 42.76           C  
ANISOU 3187  CE3 TRP A 395     6619   4987   4642   -261    -63      2       C  
ATOM   3188  CZ2 TRP A 395     -31.253 -13.547  47.867  1.00 44.64           C  
ANISOU 3188  CZ2 TRP A 395     6836   5287   4838   -293    -30     -4       C  
ATOM   3189  CZ3 TRP A 395     -29.832 -14.103  49.749  1.00 43.38           C  
ANISOU 3189  CZ3 TRP A 395     6710   5088   4684   -272    -62      7       C  
ATOM   3190  CH2 TRP A 395     -31.037 -13.629  49.223  1.00 43.84           C  
ANISOU 3190  CH2 TRP A 395     6748   5186   4724   -283    -41     -1       C  
ATOM   3191  N   PHE A 396     -23.360 -14.967  46.662  1.00 44.90           N  
ANISOU 3191  N   PHE A 396     6620   5414   5027   -170    -40   -117       N  
ATOM   3192  CA  PHE A 396     -22.152 -15.663  47.093  1.00 44.70           C  
ANISOU 3192  CA  PHE A 396     6518   5443   5021    -78    -76   -160       C  
ATOM   3193  C   PHE A 396     -21.683 -15.226  48.456  1.00 49.98           C  
ANISOU 3193  C   PHE A 396     7162   6128   5702    -72   -147   -155       C  
ATOM   3194  O   PHE A 396     -21.446 -16.132  49.249  1.00 50.07           O  
ANISOU 3194  O   PHE A 396     7205   6109   5709     28   -211   -163       O  
ATOM   3195  CB  PHE A 396     -21.000 -15.611  46.086  1.00 47.12           C  
ANISOU 3195  CB  PHE A 396     6695   5871   5337    -74    -25   -217       C  
ATOM   3196  CG  PHE A 396     -19.842 -16.465  46.552  1.00 50.31           C  
ANISOU 3196  CG  PHE A 396     7009   6348   5760     62    -74   -277       C  
ATOM   3197  CD1 PHE A 396     -19.917 -17.861  46.503  1.00 52.78           C  
ANISOU 3197  CD1 PHE A 396     7396   6595   6062    210   -105   -302       C  
ATOM   3198  CD2 PHE A 396     -18.702 -15.880  47.108  1.00 53.91           C  
ANISOU 3198  CD2 PHE A 396     7319   6929   6237     49   -107   -310       C  
ATOM   3199  CE1 PHE A 396     -18.860 -18.654  46.969  1.00 54.99           C  
ANISOU 3199  CE1 PHE A 396     7611   6929   6352    371   -172   -364       C  
ATOM   3200  CE2 PHE A 396     -17.642 -16.676  47.572  1.00 58.25           C  
ANISOU 3200  CE2 PHE A 396     7770   7560   6802    201   -170   -375       C  
ATOM   3201  CZ  PHE A 396     -17.727 -18.057  47.494  1.00 56.47           C  
ANISOU 3201  CZ  PHE A 396     7626   7263   6566    376   -206   -403       C  
ATOM   3202  N   PRO A 397     -21.574 -13.899  48.795  1.00 47.06           N  
ANISOU 3202  N   PRO A 397     6764   5784   5331   -174   -152   -140       N  
ATOM   3203  CA  PRO A 397     -21.129 -13.531  50.152  1.00 47.29           C  
ANISOU 3203  CA  PRO A 397     6784   5821   5361   -168   -230   -140       C  
ATOM   3204  C   PRO A 397     -21.983 -14.144  51.262  1.00 53.06           C  
ANISOU 3204  C   PRO A 397     7638   6457   6066   -108   -278   -108       C  
ATOM   3205  O   PRO A 397     -21.430 -14.680  52.230  1.00 55.14           O  
ANISOU 3205  O   PRO A 397     7905   6722   6324    -36   -353   -117       O  
ATOM   3206  CB  PRO A 397     -21.191 -12.005  50.134  1.00 48.69           C  
ANISOU 3206  CB  PRO A 397     6970   6003   5528   -300   -220   -125       C  
ATOM   3207  CG  PRO A 397     -21.059 -11.639  48.670  1.00 52.46           C  
ANISOU 3207  CG  PRO A 397     7407   6521   6003   -376   -141   -131       C  
ATOM   3208  CD  PRO A 397     -21.862 -12.683  47.999  1.00 47.28           C  
ANISOU 3208  CD  PRO A 397     6801   5817   5347   -298   -100   -123       C  
ATOM   3209  N   PHE A 398     -23.317 -14.146  51.097  1.00 47.67           N  
ANISOU 3209  N   PHE A 398     7053   5701   5358   -137   -237    -72       N  
ATOM   3210  CA  PHE A 398     -24.173 -14.757  52.106  1.00 46.47           C  
ANISOU 3210  CA  PHE A 398     7009   5483   5165   -110   -264    -43       C  
ATOM   3211  C   PHE A 398     -23.962 -16.257  52.173  1.00 52.08           C  
ANISOU 3211  C   PHE A 398     7772   6152   5863    -29   -294    -43       C  
ATOM   3212  O   PHE A 398     -23.764 -16.782  53.262  1.00 52.13           O  
ANISOU 3212  O   PHE A 398     7846   6122   5838     16   -360    -32       O  
ATOM   3213  CB  PHE A 398     -25.667 -14.459  51.855  1.00 46.85           C  
ANISOU 3213  CB  PHE A 398     7117   5501   5184   -165   -208    -17       C  
ATOM   3214  CG  PHE A 398     -26.572 -15.256  52.765  1.00 47.45           C  
ANISOU 3214  CG  PHE A 398     7289   5536   5204   -164   -215     10       C  
ATOM   3215  CD1 PHE A 398     -26.746 -14.889  54.097  1.00 49.67           C  
ANISOU 3215  CD1 PHE A 398     7617   5815   5442   -169   -246     19       C  
ATOM   3216  CD2 PHE A 398     -27.186 -16.419  52.318  1.00 48.78           C  
ANISOU 3216  CD2 PHE A 398     7515   5668   5351   -173   -193     26       C  
ATOM   3217  CE1 PHE A 398     -27.551 -15.646  54.948  1.00 49.87           C  
ANISOU 3217  CE1 PHE A 398     7737   5816   5397   -192   -241     46       C  
ATOM   3218  CE2 PHE A 398     -27.969 -17.187  53.181  1.00 51.13           C  
ANISOU 3218  CE2 PHE A 398     7915   5931   5581   -207   -197     56       C  
ATOM   3219  CZ  PHE A 398     -28.164 -16.782  54.482  1.00 48.69           C  
ANISOU 3219  CZ  PHE A 398     7642   5634   5224   -221   -215     67       C  
ATOM   3220  N   PHE A 399     -24.073 -16.958  51.024  1.00 48.56           N  
ANISOU 3220  N   PHE A 399     7326   5695   5430     -9   -253    -54       N  
ATOM   3221  CA  PHE A 399     -23.996 -18.404  51.025  1.00 48.28           C  
ANISOU 3221  CA  PHE A 399     7383   5589   5370     70   -288    -57       C  
ATOM   3222  C   PHE A 399     -22.644 -18.882  51.423  1.00 55.89           C  
ANISOU 3222  C   PHE A 399     8307   6579   6350    197   -366    -97       C  
ATOM   3223  O   PHE A 399     -22.571 -19.857  52.162  1.00 58.86           O  
ANISOU 3223  O   PHE A 399     8806   6874   6687    271   -441    -85       O  
ATOM   3224  CB  PHE A 399     -24.496 -19.026  49.725  1.00 49.38           C  
ANISOU 3224  CB  PHE A 399     7554   5701   5508     59   -232    -65       C  
ATOM   3225  CG  PHE A 399     -26.008 -19.117  49.714  1.00 49.59           C  
ANISOU 3225  CG  PHE A 399     7670   5680   5494    -47   -193    -20       C  
ATOM   3226  CD1 PHE A 399     -26.672 -20.064  50.490  1.00 52.57           C  
ANISOU 3226  CD1 PHE A 399     8192   5974   5809    -73   -226     15       C  
ATOM   3227  CD2 PHE A 399     -26.769 -18.230  48.966  1.00 49.80           C  
ANISOU 3227  CD2 PHE A 399     7634   5755   5532   -127   -131    -15       C  
ATOM   3228  CE1 PHE A 399     -28.063 -20.130  50.499  1.00 52.65           C  
ANISOU 3228  CE1 PHE A 399     8251   5980   5775   -191   -183     48       C  
ATOM   3229  CE2 PHE A 399     -28.165 -18.302  48.972  1.00 52.10           C  
ANISOU 3229  CE2 PHE A 399     7974   6036   5785   -212   -102     14       C  
ATOM   3230  CZ  PHE A 399     -28.802 -19.256  49.730  1.00 50.38           C  
ANISOU 3230  CZ  PHE A 399     7868   5765   5510   -251   -122     42       C  
ATOM   3231  N   PHE A 400     -21.590 -18.140  51.089  1.00 51.92           N  
ANISOU 3231  N   PHE A 400     7640   6192   5895    213   -360   -142       N  
ATOM   3232  CA  PHE A 400     -20.265 -18.511  51.546  1.00 53.30           C  
ANISOU 3232  CA  PHE A 400     7735   6430   6085    339   -444   -193       C  
ATOM   3233  C   PHE A 400     -20.215 -18.434  53.080  1.00 56.30           C  
ANISOU 3233  C   PHE A 400     8188   6770   6435    353   -541   -163       C  
ATOM   3234  O   PHE A 400     -19.768 -19.396  53.717  1.00 57.33           O  
ANISOU 3234  O   PHE A 400     8396   6850   6538    482   -639   -173       O  
ATOM   3235  CB  PHE A 400     -19.182 -17.644  50.887  1.00 56.77           C  
ANISOU 3235  CB  PHE A 400     7960   7037   6572    312   -406   -249       C  
ATOM   3236  CG  PHE A 400     -17.784 -18.015  51.307  1.00 61.61           C  
ANISOU 3236  CG  PHE A 400     8445   7760   7203    448   -493   -317       C  
ATOM   3237  CD1 PHE A 400     -17.215 -19.220  50.906  1.00 67.41           C  
ANISOU 3237  CD1 PHE A 400     9176   8502   7935    631   -527   -376       C  
ATOM   3238  CD2 PHE A 400     -17.042 -17.175  52.127  1.00 65.97           C  
ANISOU 3238  CD2 PHE A 400     8886   8411   7770    403   -552   -330       C  
ATOM   3239  CE1 PHE A 400     -15.931 -19.584  51.332  1.00 70.90           C  
ANISOU 3239  CE1 PHE A 400     9487   9062   8391    790   -622   -451       C  
ATOM   3240  CE2 PHE A 400     -15.750 -17.533  52.539  1.00 71.22           C  
ANISOU 3240  CE2 PHE A 400     9410   9201   8449    535   -645   -400       C  
ATOM   3241  CZ  PHE A 400     -15.204 -18.735  52.140  1.00 70.45           C  
ANISOU 3241  CZ  PHE A 400     9293   9124   8353    738   -681   -463       C  
ATOM   3242  N   SER A 401     -20.753 -17.328  53.672  1.00 49.96           N  
ANISOU 3242  N   SER A 401     7389   5971   5622    227   -520   -126       N  
ATOM   3243  CA  SER A 401     -20.785 -17.092  55.130  1.00 47.96           C  
ANISOU 3243  CA  SER A 401     7211   5684   5326    221   -600   -100       C  
ATOM   3244  C   SER A 401     -21.688 -18.002  55.908  1.00 50.41           C  
ANISOU 3244  C   SER A 401     7722   5868   5562    233   -626    -48       C  
ATOM   3245  O   SER A 401     -21.347 -18.384  57.017  1.00 52.47           O  
ANISOU 3245  O   SER A 401     8068   6091   5775    289   -723    -37       O  
ATOM   3246  CB  SER A 401     -21.140 -15.652  55.434  1.00 48.95           C  
ANISOU 3246  CB  SER A 401     7301   5844   5453     95   -564    -87       C  
ATOM   3247  OG  SER A 401     -20.149 -14.853  54.819  1.00 60.63           O  
ANISOU 3247  OG  SER A 401     8616   7435   6985     61   -556   -132       O  
ATOM   3248  N   TYR A 402     -22.837 -18.330  55.358  1.00 45.37           N  
ANISOU 3248  N   TYR A 402     7163   5171   4902    167   -545    -16       N  
ATOM   3249  CA  TYR A 402     -23.798 -19.214  55.983  1.00 45.93           C  
ANISOU 3249  CA  TYR A 402     7424   5137   4891    133   -551     35       C  
ATOM   3250  C   TYR A 402     -23.215 -20.642  55.996  1.00 54.00           C  
ANISOU 3250  C   TYR A 402     8568   6066   5885    255   -639     31       C  
ATOM   3251  O   TYR A 402     -23.300 -21.297  57.039  1.00 55.36           O  
ANISOU 3251  O   TYR A 402     8908   6149   5975    271   -715     68       O  
ATOM   3252  CB  TYR A 402     -25.140 -19.078  55.243  1.00 45.93           C  
ANISOU 3252  CB  TYR A 402     7433   5135   4882     17   -439     58       C  
ATOM   3253  CG  TYR A 402     -26.344 -19.841  55.758  1.00 47.12           C  
ANISOU 3253  CG  TYR A 402     7745   5217   4941    -75   -415    109       C  
ATOM   3254  CD1 TYR A 402     -26.646 -19.878  57.115  1.00 49.39           C  
ANISOU 3254  CD1 TYR A 402     8140   5483   5144   -116   -444    142       C  
ATOM   3255  CD2 TYR A 402     -27.271 -20.378  54.877  1.00 48.13           C  
ANISOU 3255  CD2 TYR A 402     7904   5324   5058   -149   -351    121       C  
ATOM   3256  CE1 TYR A 402     -27.787 -20.535  57.584  1.00 51.26           C  
ANISOU 3256  CE1 TYR A 402     8515   5681   5281   -235   -404    189       C  
ATOM   3257  CE2 TYR A 402     -28.391 -21.058  55.330  1.00 50.24           C  
ANISOU 3257  CE2 TYR A 402     8304   5552   5233   -268   -322    165       C  
ATOM   3258  CZ  TYR A 402     -28.673 -21.101  56.681  1.00 62.98           C  
ANISOU 3258  CZ  TYR A 402    10016   7155   6758   -320   -340    199       C  
ATOM   3259  OH  TYR A 402     -29.828 -21.731  57.084  1.00 72.00           O  
ANISOU 3259  OH  TYR A 402    11275   8286   7797   -470   -294    241       O  
ATOM   3260  N   SER A 403     -22.524 -21.074  54.893  1.00 50.68           N  
ANISOU 3260  N   SER A 403     8070   5665   5520    354   -639    -19       N  
ATOM   3261  CA  SER A 403     -21.835 -22.379  54.782  1.00 51.58           C  
ANISOU 3261  CA  SER A 403     8293   5695   5612    516   -733    -45       C  
ATOM   3262  C   SER A 403     -20.719 -22.531  55.813  1.00 59.54           C  
ANISOU 3262  C   SER A 403     9302   6715   6606    658   -872    -68       C  
ATOM   3263  O   SER A 403     -20.616 -23.585  56.437  1.00 61.02           O  
ANISOU 3263  O   SER A 403     9693   6772   6721    751   -979    -48       O  
ATOM   3264  CB  SER A 403     -21.227 -22.549  53.400  1.00 53.52           C  
ANISOU 3264  CB  SER A 403     8409   6004   5921    604   -691   -115       C  
ATOM   3265  OG  SER A 403     -22.270 -22.522  52.451  1.00 63.27           O  
ANISOU 3265  OG  SER A 403     9670   7213   7156    481   -582    -92       O  
ATOM   3266  N   LEU A 404     -19.864 -21.493  55.968  1.00 58.08           N  
ANISOU 3266  N   LEU A 404     8902   6682   6484    672   -882   -110       N  
ATOM   3267  CA  LEU A 404     -18.789 -21.488  56.950  1.00 60.53           C  
ANISOU 3267  CA  LEU A 404     9177   7037   6785    793  -1020   -138       C  
ATOM   3268  C   LEU A 404     -19.314 -21.727  58.359  1.00 63.34           C  
ANISOU 3268  C   LEU A 404     9750   7272   7043    752  -1098    -68       C  
ATOM   3269  O   LEU A 404     -18.870 -22.678  58.981  1.00 65.96           O  
ANISOU 3269  O   LEU A 404    10233   7512   7315    891  -1231    -66       O  
ATOM   3270  CB  LEU A 404     -17.943 -20.215  56.882  1.00 61.48           C  
ANISOU 3270  CB  LEU A 404     9034   7347   6978    752  -1004   -188       C  
ATOM   3271  CG  LEU A 404     -16.751 -20.266  55.934  1.00 68.67           C  
ANISOU 3271  CG  LEU A 404     9716   8415   7960    869  -1005   -282       C  
ATOM   3272  CD1 LEU A 404     -16.003 -18.956  55.951  1.00 69.22           C  
ANISOU 3272  CD1 LEU A 404     9547   8671   8082    770   -986   -320       C  
ATOM   3273  CD2 LEU A 404     -15.777 -21.373  56.327  1.00 74.71           C  
ANISOU 3273  CD2 LEU A 404    10508   9173   8703   1115  -1159   -337       C  
ATOM   3274  N   TYR A 405     -20.324 -20.964  58.809  1.00 57.51           N  
ANISOU 3274  N   TYR A 405     9053   6525   6273    571  -1013    -13       N  
ATOM   3275  CA  TYR A 405     -20.991 -21.126  60.109  1.00 58.32           C  
ANISOU 3275  CA  TYR A 405     9362   6533   6266    500  -1052     53       C  
ATOM   3276  C   TYR A 405     -21.598 -22.538  60.280  1.00 66.17           C  
ANISOU 3276  C   TYR A 405    10629   7352   7160    511  -1087    107       C  
ATOM   3277  O   TYR A 405     -21.637 -23.071  61.393  1.00 68.25           O  
ANISOU 3277  O   TYR A 405    11099   7517   7317    522  -1181    152       O  
ATOM   3278  CB  TYR A 405     -22.074 -20.057  60.289  1.00 58.35           C  
ANISOU 3278  CB  TYR A 405     9330   6582   6257    316   -925     83       C  
ATOM   3279  CG  TYR A 405     -22.819 -20.166  61.597  1.00 61.46           C  
ANISOU 3279  CG  TYR A 405     9917   6909   6526    231   -939    141       C  
ATOM   3280  CD1 TYR A 405     -22.234 -19.763  62.790  1.00 63.63           C  
ANISOU 3280  CD1 TYR A 405    10227   7198   6752    263  -1038    139       C  
ATOM   3281  CD2 TYR A 405     -24.109 -20.687  61.644  1.00 63.13           C  
ANISOU 3281  CD2 TYR A 405    10275   7057   6656    106   -850    194       C  
ATOM   3282  CE1 TYR A 405     -22.916 -19.867  64.000  1.00 65.18           C  
ANISOU 3282  CE1 TYR A 405    10611   7339   6815    179  -1042    190       C  
ATOM   3283  CE2 TYR A 405     -24.800 -20.800  62.849  1.00 64.95           C  
ANISOU 3283  CE2 TYR A 405    10675   7249   6753     10   -847    244       C  
ATOM   3284  CZ  TYR A 405     -24.202 -20.382  64.025  1.00 74.18           C  
ANISOU 3284  CZ  TYR A 405    11889   8426   7870     50   -939    243       C  
ATOM   3285  OH  TYR A 405     -24.887 -20.478  65.213  1.00 80.30           O  
ANISOU 3285  OH  TYR A 405    12840   9171   8499    -51   -925    289       O  
ATOM   3286  N   GLY A 406     -22.061 -23.129  59.180  1.00 62.11           N  
ANISOU 3286  N   GLY A 406    10135   6794   6671    497  -1016    104       N  
ATOM   3287  CA  GLY A 406     -22.572 -24.489  59.187  1.00 62.56           C  
ANISOU 3287  CA  GLY A 406    10463   6674   6634    495  -1055    148       C  
ATOM   3288  C   GLY A 406     -21.442 -25.436  59.521  1.00 68.06           C  
ANISOU 3288  C   GLY A 406    11283   7277   7301    720  -1233    120       C  
ATOM   3289  O   GLY A 406     -21.622 -26.363  60.317  1.00 68.89           O  
ANISOU 3289  O   GLY A 406    11675   7216   7285    731  -1332    174       O  
ATOM   3290  N   ILE A 407     -20.238 -25.134  58.979  1.00 64.35           N  
ANISOU 3290  N   ILE A 407    10589   6926   6934    901  -1279     32       N  
ATOM   3291  CA  ILE A 407     -19.034 -25.934  59.190  1.00 65.84           C  
ANISOU 3291  CA  ILE A 407    10829   7074   7112   1162  -1453    -22       C  
ATOM   3292  C   ILE A 407     -18.336 -25.612  60.540  1.00 72.38           C  
ANISOU 3292  C   ILE A 407    11667   7934   7899   1231  -1595    -15       C  
ATOM   3293  O   ILE A 407     -18.431 -26.434  61.445  1.00 75.02           O  
ANISOU 3293  O   ILE A 407    12287   8102   8115   1278  -1721     37       O  
ATOM   3294  CB  ILE A 407     -18.075 -25.871  57.971  1.00 68.03           C  
ANISOU 3294  CB  ILE A 407    10853   7492   7503   1329  -1433   -132       C  
ATOM   3295  CG1 ILE A 407     -18.733 -26.562  56.749  1.00 67.47           C  
ANISOU 3295  CG1 ILE A 407    10872   7329   7433   1301  -1338   -137       C  
ATOM   3296  CG2 ILE A 407     -16.721 -26.527  58.290  1.00 69.93           C  
ANISOU 3296  CG2 ILE A 407    11082   7750   7740   1628  -1622   -211       C  
ATOM   3297  CD1 ILE A 407     -18.356 -26.006  55.394  1.00 65.05           C  
ANISOU 3297  CD1 ILE A 407    10284   7197   7237   1318  -1218   -217       C  
ATOM   3298  N   CYS A 408     -17.626 -24.472  60.675  1.00 66.91           N  
ANISOU 3298  N   CYS A 408    10690   7442   7291   1231  -1587    -65       N  
ATOM   3299  CA  CYS A 408     -16.849 -24.181  61.877  1.00 66.62           C  
ANISOU 3299  CA  CYS A 408    10645   7450   7218   1309  -1738    -73       C  
ATOM   3300  C   CYS A 408     -17.569 -23.304  62.884  1.00 69.19           C  
ANISOU 3300  C   CYS A 408    11030   7774   7486   1101  -1690     -4       C  
ATOM   3301  O   CYS A 408     -16.977 -22.941  63.902  1.00 70.38           O  
ANISOU 3301  O   CYS A 408    11174   7966   7601   1140  -1808     -9       O  
ATOM   3302  CB  CYS A 408     -15.472 -23.629  61.528  1.00 67.47           C  
ANISOU 3302  CB  CYS A 408    10426   7778   7433   1453  -1798   -181       C  
ATOM   3303  SG  CYS A 408     -15.367 -22.876  59.888  1.00 70.42           S  
ANISOU 3303  SG  CYS A 408    10471   8338   7945   1376  -1604   -250       S  
ATOM   3304  N   ARG A 409     -18.854 -23.029  62.663  1.00 64.21           N  
ANISOU 3304  N   ARG A 409    10470   7096   6831    894  -1528     57       N  
ATOM   3305  CA  ARG A 409     -19.681 -22.268  63.606  1.00 64.03           C  
ANISOU 3305  CA  ARG A 409    10519   7073   6736    708  -1466    114       C  
ATOM   3306  C   ARG A 409     -19.028 -21.000  64.179  1.00 69.24           C  
ANISOU 3306  C   ARG A 409    10992   7878   7437    689  -1498     73       C  
ATOM   3307  O   ARG A 409     -18.783 -20.058  63.434  1.00 69.82           O  
ANISOU 3307  O   ARG A 409    10824   8086   7620    647  -1418     24       O  
ATOM   3308  CB  ARG A 409     -20.162 -23.191  64.733  1.00 64.85           C  
ANISOU 3308  CB  ARG A 409    10962   7004   6675    687  -1550    193       C  
ATOM   3309  CG  ARG A 409     -21.648 -23.403  64.697  1.00 71.18           C  
ANISOU 3309  CG  ARG A 409    11916   7732   7396    479  -1401    263       C  
ATOM   3310  CD  ARG A 409     -21.992 -24.869  64.786  1.00 69.36           C  
ANISOU 3310  CD  ARG A 409    11998   7304   7050    491  -1464    322       C  
ATOM   3311  NE  ARG A 409     -22.885 -25.303  63.713  1.00 67.06           N  
ANISOU 3311  NE  ARG A 409    11717   6979   6785    385  -1334    336       N  
ATOM   3312  CZ  ARG A 409     -24.185 -25.030  63.641  1.00 80.41           C  
ANISOU 3312  CZ  ARG A 409    13415   8704   8434    161  -1173    377       C  
ATOM   3313  NH1 ARG A 409     -24.764 -24.263  64.556  1.00 65.45           N  
ANISOU 3313  NH1 ARG A 409    11508   6888   6473     28  -1107    402       N  
ATOM   3314  NH2 ARG A 409     -24.909 -25.494  62.637  1.00 78.02           N1+
ANISOU 3314  NH2 ARG A 409    13118   8372   8153     76  -1079    383       N1+
ATOM   3315  N   GLU A 410     -18.737 -20.996  65.482  1.00 66.66           N  
ANISOU 3315  N   GLU A 410    10798   7515   7014    712  -1623     96       N  
ATOM   3316  CA  GLU A 410     -18.135 -19.886  66.225  1.00 67.19           C  
ANISOU 3316  CA  GLU A 410    10743   7696   7091    685  -1681     62       C  
ATOM   3317  C   GLU A 410     -16.729 -19.506  65.736  1.00 69.61           C  
ANISOU 3317  C   GLU A 410    10776   8159   7515    807  -1774    -28       C  
ATOM   3318  O   GLU A 410     -16.471 -18.324  65.506  1.00 69.49           O  
ANISOU 3318  O   GLU A 410    10559   8273   7569    712  -1719    -68       O  
ATOM   3319  CB  GLU A 410     -18.122 -20.200  67.741  1.00 70.01           C  
ANISOU 3319  CB  GLU A 410    11345   7960   7294    698  -1815    108       C  
ATOM   3320  N   ALA A 411     -15.836 -20.500  65.571  1.00 64.52           N  
ANISOU 3320  N   ALA A 411    10127   7505   6882   1015  -1913    -62       N  
ATOM   3321  CA  ALA A 411     -14.461 -20.318  65.109  1.00 64.90           C  
ANISOU 3321  CA  ALA A 411     9897   7732   7031   1156  -2005   -160       C  
ATOM   3322  C   ALA A 411     -14.346 -19.570  63.759  1.00 69.20           C  
ANISOU 3322  C   ALA A 411    10158   8430   7707   1069  -1845   -214       C  
ATOM   3323  O   ALA A 411     -13.283 -19.024  63.453  1.00 69.84           O  
ANISOU 3323  O   ALA A 411     9970   8703   7863   1099  -1885   -294       O  
ATOM   3324  CB  ALA A 411     -13.773 -21.664  65.016  1.00 67.23           C  
ANISOU 3324  CB  ALA A 411    10267   7971   7305   1419  -2158   -192       C  
ATOM   3325  N   CYS A 412     -15.443 -19.538  62.970  1.00 64.05           N  
ANISOU 3325  N   CYS A 412     9567   7701   7070    949  -1667   -170       N  
ATOM   3326  CA  CYS A 412     -15.505 -18.885  61.672  1.00 62.59           C  
ANISOU 3326  CA  CYS A 412     9170   7626   6987    857  -1512   -206       C  
ATOM   3327  C   CYS A 412     -16.888 -18.279  61.426  1.00 63.25           C  
ANISOU 3327  C   CYS A 412     9350   7628   7056    661  -1346   -141       C  
ATOM   3328  O   CYS A 412     -17.497 -18.494  60.381  1.00 63.21           O  
ANISOU 3328  O   CYS A 412     9336   7596   7085    627  -1224   -133       O  
ATOM   3329  CB  CYS A 412     -15.091 -19.849  60.564  1.00 64.51           C  
ANISOU 3329  CB  CYS A 412     9342   7889   7281   1014  -1500   -255       C  
ATOM   3330  SG  CYS A 412     -16.338 -21.108  60.166  1.00 68.45           S  
ANISOU 3330  SG  CYS A 412    10134   8157   7717   1035  -1436   -185       S  
ATOM   3331  N   GLN A 413     -17.358 -17.468  62.372  1.00 58.04           N  
ANISOU 3331  N   GLN A 413     8770   6942   6339    541  -1345   -107       N  
ATOM   3332  CA  GLN A 413     -18.649 -16.790  62.284  1.00 55.77           C  
ANISOU 3332  CA  GLN A 413     8560   6602   6028    381  -1202    -62       C  
ATOM   3333  C   GLN A 413     -18.447 -15.402  61.756  1.00 61.09           C  
ANISOU 3333  C   GLN A 413     9060   7381   6770    266  -1134    -98       C  
ATOM   3334  O   GLN A 413     -17.756 -14.612  62.386  1.00 63.36           O  
ANISOU 3334  O   GLN A 413     9288   7734   7054    232  -1211   -127       O  
ATOM   3335  CB  GLN A 413     -19.276 -16.724  63.673  1.00 57.21           C  
ANISOU 3335  CB  GLN A 413     8947   6700   6092    333  -1241    -14       C  
ATOM   3336  CG  GLN A 413     -20.602 -15.985  63.798  1.00 58.61           C  
ANISOU 3336  CG  GLN A 413     9196   6847   6226    191  -1104     16       C  
ATOM   3337  CD  GLN A 413     -21.248 -16.443  65.080  1.00 73.74           C  
ANISOU 3337  CD  GLN A 413    11338   8678   8002    170  -1134     65       C  
ATOM   3338  OE1 GLN A 413     -22.405 -16.870  65.115  1.00 59.96           O  
ANISOU 3338  OE1 GLN A 413     9711   6879   6192    103  -1036    109       O  
ATOM   3339  NE2 GLN A 413     -20.488 -16.421  66.163  1.00 78.45           N  
ANISOU 3339  NE2 GLN A 413    11997   9270   8539    219  -1273     60       N  
ATOM   3340  N   VAL A 414     -19.034 -15.094  60.600  1.00 57.50           N  
ANISOU 3340  N   VAL A 414     8542   6936   6369    199  -1001    -97       N  
ATOM   3341  CA  VAL A 414     -18.970 -13.760  60.007  1.00 56.41           C  
ANISOU 3341  CA  VAL A 414     8286   6867   6280     78   -933   -121       C  
ATOM   3342  C   VAL A 414     -19.764 -12.847  60.953  1.00 57.78           C  
ANISOU 3342  C   VAL A 414     8588   6981   6383     -8   -922    -99       C  
ATOM   3343  O   VAL A 414     -20.817 -13.276  61.438  1.00 57.50           O  
ANISOU 3343  O   VAL A 414     8700   6866   6283      0   -883    -60       O  
ATOM   3344  CB  VAL A 414     -19.521 -13.800  58.556  1.00 60.16           C  
ANISOU 3344  CB  VAL A 414     8704   7344   6809     45   -803   -117       C  
ATOM   3345  CG1 VAL A 414     -20.183 -12.487  58.149  1.00 59.44           C  
ANISOU 3345  CG1 VAL A 414     8617   7245   6722    -84   -719   -111       C  
ATOM   3346  CG2 VAL A 414     -18.418 -14.174  57.572  1.00 60.73           C  
ANISOU 3346  CG2 VAL A 414     8600   7525   6951     99   -809   -165       C  
ATOM   3347  N   PRO A 415     -19.260 -11.643  61.318  1.00 53.31           N  
ANISOU 3347  N   PRO A 415     7983   6457   5817    -91   -963   -128       N  
ATOM   3348  CA  PRO A 415     -20.009 -10.808  62.274  1.00 51.87           C  
ANISOU 3348  CA  PRO A 415     7945   6208   5554   -147   -961   -120       C  
ATOM   3349  C   PRO A 415     -21.437 -10.496  61.830  1.00 55.63           C  
ANISOU 3349  C   PRO A 415     8499   6625   6012   -174   -832    -99       C  
ATOM   3350  O   PRO A 415     -21.716 -10.367  60.630  1.00 53.87           O  
ANISOU 3350  O   PRO A 415     8206   6414   5849   -197   -751    -97       O  
ATOM   3351  CB  PRO A 415     -19.148  -9.551  62.415  1.00 53.47           C  
ANISOU 3351  CB  PRO A 415     8088   6458   5769   -245  -1024   -160       C  
ATOM   3352  CG  PRO A 415     -17.805  -9.922  61.928  1.00 59.04           C  
ANISOU 3352  CG  PRO A 415     8608   7281   6544   -234  -1088   -190       C  
ATOM   3353  CD  PRO A 415     -18.011 -10.977  60.888  1.00 55.47           C  
ANISOU 3353  CD  PRO A 415     8087   6843   6148   -151  -1012   -175       C  
ATOM   3354  N   GLY A 416     -22.329 -10.413  62.814  1.00 53.43           N  
ANISOU 3354  N   GLY A 416     8362   6298   5642   -166   -816    -88       N  
ATOM   3355  CA  GLY A 416     -23.743 -10.097  62.623  1.00 52.29           C  
ANISOU 3355  CA  GLY A 416     8280   6128   5461   -176   -703    -83       C  
ATOM   3356  C   GLY A 416     -23.987  -9.003  61.603  1.00 55.32           C  
ANISOU 3356  C   GLY A 416     8611   6508   5898   -215   -651   -107       C  
ATOM   3357  O   GLY A 416     -24.660  -9.275  60.604  1.00 55.61           O  
ANISOU 3357  O   GLY A 416     8603   6553   5974   -207   -569    -94       O  
ATOM   3358  N   PRO A 417     -23.372  -7.792  61.760  1.00 49.21           N  
ANISOU 3358  N   PRO A 417     7857   5718   5124   -267   -710   -141       N  
ATOM   3359  CA  PRO A 417     -23.585  -6.717  60.770  1.00 48.24           C  
ANISOU 3359  CA  PRO A 417     7728   5566   5034   -314   -674   -157       C  
ATOM   3360  C   PRO A 417     -23.190  -7.015  59.332  1.00 50.89           C  
ANISOU 3360  C   PRO A 417     7942   5935   5458   -349   -633   -138       C  
ATOM   3361  O   PRO A 417     -23.851  -6.526  58.434  1.00 50.57           O  
ANISOU 3361  O   PRO A 417     7918   5865   5430   -355   -574   -136       O  
ATOM   3362  CB  PRO A 417     -22.768  -5.559  61.324  1.00 50.87           C  
ANISOU 3362  CB  PRO A 417     8125   5865   5338   -391   -767   -189       C  
ATOM   3363  CG  PRO A 417     -22.612  -5.861  62.749  1.00 54.95           C  
ANISOU 3363  CG  PRO A 417     8708   6386   5784   -357   -832   -199       C  
ATOM   3364  CD  PRO A 417     -22.532  -7.316  62.872  1.00 50.12           C  
ANISOU 3364  CD  PRO A 417     8025   5826   5190   -297   -820   -164       C  
ATOM   3365  N   LEU A 418     -22.137  -7.807  59.105  1.00 48.28           N  
ANISOU 3365  N   LEU A 418     7493   5671   5179   -358   -665   -130       N  
ATOM   3366  CA  LEU A 418     -21.680  -8.182  57.758  1.00 47.22           C  
ANISOU 3366  CA  LEU A 418     7234   5589   5118   -383   -618   -122       C  
ATOM   3367  C   LEU A 418     -22.623  -9.223  57.149  1.00 53.13           C  
ANISOU 3367  C   LEU A 418     7978   6326   5881   -307   -537    -96       C  
ATOM   3368  O   LEU A 418     -22.985  -9.105  55.975  1.00 55.08           O  
ANISOU 3368  O   LEU A 418     8196   6572   6159   -328   -471    -89       O  
ATOM   3369  CB  LEU A 418     -20.286  -8.778  57.843  1.00 47.46           C  
ANISOU 3369  CB  LEU A 418     7130   5715   5188   -383   -683   -140       C  
ATOM   3370  CG  LEU A 418     -19.241  -8.145  57.002  1.00 52.17           C  
ANISOU 3370  CG  LEU A 418     7605   6392   5823   -494   -683   -163       C  
ATOM   3371  CD1 LEU A 418     -18.434  -7.222  57.838  1.00 55.05           C  
ANISOU 3371  CD1 LEU A 418     7978   6779   6158   -591   -778   -189       C  
ATOM   3372  CD2 LEU A 418     -18.308  -9.180  56.505  1.00 52.22           C  
ANISOU 3372  CD2 LEU A 418     7441   6517   5883   -437   -687   -184       C  
ATOM   3373  N   PHE A 419     -23.018 -10.229  57.946  1.00 47.69           N  
ANISOU 3373  N   PHE A 419     7336   5626   5160   -234   -548    -80       N  
ATOM   3374  CA  PHE A 419     -23.935 -11.286  57.563  1.00 47.32           C  
ANISOU 3374  CA  PHE A 419     7310   5561   5107   -188   -483    -53       C  
ATOM   3375  C   PHE A 419     -25.252 -10.682  57.098  1.00 49.73           C  
ANISOU 3375  C   PHE A 419     7655   5848   5394   -207   -404    -51       C  
ATOM   3376  O   PHE A 419     -25.726 -11.032  56.023  1.00 46.81           O  
ANISOU 3376  O   PHE A 419     7247   5484   5056   -209   -345    -41       O  
ATOM   3377  CB  PHE A 419     -24.161 -12.188  58.773  1.00 51.03           C  
ANISOU 3377  CB  PHE A 419     7872   6007   5512   -145   -521    -32       C  
ATOM   3378  CG  PHE A 419     -24.636 -13.566  58.421  1.00 54.76           C  
ANISOU 3378  CG  PHE A 419     8375   6455   5977   -114   -488     -1       C  
ATOM   3379  CD1 PHE A 419     -23.766 -14.495  57.849  1.00 59.94           C  
ANISOU 3379  CD1 PHE A 419     8983   7111   6680    -58   -526     -3       C  
ATOM   3380  CD2 PHE A 419     -25.950 -13.949  58.668  1.00 58.55           C  
ANISOU 3380  CD2 PHE A 419     8935   6919   6395   -143   -421     23       C  
ATOM   3381  CE1 PHE A 419     -24.204 -15.780  57.521  1.00 61.13           C  
ANISOU 3381  CE1 PHE A 419     9201   7213   6812    -30   -507     23       C  
ATOM   3382  CE2 PHE A 419     -26.397 -15.233  58.326  1.00 62.29           C  
ANISOU 3382  CE2 PHE A 419     9457   7359   6850   -146   -396     54       C  
ATOM   3383  CZ  PHE A 419     -25.515 -16.143  57.771  1.00 60.81           C  
ANISOU 3383  CZ  PHE A 419     9258   7139   6706    -88   -445     56       C  
ATOM   3384  N   LYS A 420     -25.813  -9.716  57.881  1.00 49.22           N  
ANISOU 3384  N   LYS A 420     7665   5764   5274   -210   -411    -70       N  
ATOM   3385  CA  LYS A 420     -27.045  -8.952  57.575  1.00 48.16           C  
ANISOU 3385  CA  LYS A 420     7565   5622   5112   -193   -354    -87       C  
ATOM   3386  C   LYS A 420     -26.885  -8.205  56.252  1.00 51.54           C  
ANISOU 3386  C   LYS A 420     7962   6029   5591   -221   -344    -91       C  
ATOM   3387  O   LYS A 420     -27.724  -8.380  55.374  1.00 52.52           O  
ANISOU 3387  O   LYS A 420     8062   6166   5728   -202   -290    -85       O  
ATOM   3388  CB  LYS A 420     -27.399  -7.977  58.708  1.00 50.76           C  
ANISOU 3388  CB  LYS A 420     7990   5932   5366   -169   -381   -123       C  
ATOM   3389  CG  LYS A 420     -27.758  -8.656  60.041  1.00 60.59           C  
ANISOU 3389  CG  LYS A 420     9286   7205   6533   -149   -376   -119       C  
ATOM   3390  CD  LYS A 420     -27.749  -7.630  61.152  1.00 68.10           C  
ANISOU 3390  CD  LYS A 420    10336   8130   7408   -129   -419   -162       C  
ATOM   3391  CE  LYS A 420     -27.759  -8.188  62.553  1.00 75.71           C  
ANISOU 3391  CE  LYS A 420    11371   9113   8283   -127   -434   -157       C  
ATOM   3392  NZ  LYS A 420     -27.315  -7.155  63.547  1.00 76.80           N1+
ANISOU 3392  NZ  LYS A 420    11612   9209   8359   -120   -506   -200       N1+
ATOM   3393  N   PHE A 421     -25.771  -7.460  56.062  1.00 46.72           N  
ANISOU 3393  N   PHE A 421     7352   5396   5005   -282   -396    -98       N  
ATOM   3394  CA  PHE A 421     -25.512  -6.758  54.809  1.00 47.09           C  
ANISOU 3394  CA  PHE A 421     7391   5419   5082   -340   -385    -94       C  
ATOM   3395  C   PHE A 421     -25.484  -7.707  53.609  1.00 54.44           C  
ANISOU 3395  C   PHE A 421     8227   6394   6064   -343   -327    -71       C  
ATOM   3396  O   PHE A 421     -26.040  -7.362  52.561  1.00 57.14           O  
ANISOU 3396  O   PHE A 421     8587   6715   6408   -349   -293    -64       O  
ATOM   3397  CB  PHE A 421     -24.216  -5.954  54.886  1.00 49.57           C  
ANISOU 3397  CB  PHE A 421     7709   5724   5401   -445   -445   -103       C  
ATOM   3398  CG  PHE A 421     -23.806  -5.230  53.618  1.00 51.37           C  
ANISOU 3398  CG  PHE A 421     7944   5932   5641   -544   -430    -93       C  
ATOM   3399  CD1 PHE A 421     -24.410  -4.028  53.256  1.00 55.36           C  
ANISOU 3399  CD1 PHE A 421     8597   6338   6100   -560   -447    -95       C  
ATOM   3400  CD2 PHE A 421     -22.751  -5.699  52.840  1.00 53.47           C  
ANISOU 3400  CD2 PHE A 421     8083   6281   5950   -623   -405    -85       C  
ATOM   3401  CE1 PHE A 421     -24.007  -3.337  52.103  1.00 56.85           C  
ANISOU 3401  CE1 PHE A 421     8828   6492   6280   -672   -440    -76       C  
ATOM   3402  CE2 PHE A 421     -22.338  -5.005  51.695  1.00 57.27           C  
ANISOU 3402  CE2 PHE A 421     8580   6756   6424   -742   -380    -74       C  
ATOM   3403  CZ  PHE A 421     -22.977  -3.831  51.326  1.00 56.07           C  
ANISOU 3403  CZ  PHE A 421     8599   6487   6219   -777   -399    -63       C  
ATOM   3404  N   PHE A 422     -24.850  -8.899  53.771  1.00 48.03           N  
ANISOU 3404  N   PHE A 422     7332   5635   5284   -326   -325    -64       N  
ATOM   3405  CA  PHE A 422     -24.714  -9.951  52.762  1.00 45.28           C  
ANISOU 3405  CA  PHE A 422     6908   5322   4975   -312   -279    -53       C  
ATOM   3406  C   PHE A 422     -26.025 -10.495  52.229  1.00 51.04           C  
ANISOU 3406  C   PHE A 422     7666   6035   5693   -275   -224    -38       C  
ATOM   3407  O   PHE A 422     -26.091 -10.835  51.048  1.00 53.13           O  
ANISOU 3407  O   PHE A 422     7897   6309   5980   -286   -183    -33       O  
ATOM   3408  CB  PHE A 422     -23.846 -11.101  53.290  1.00 46.07           C  
ANISOU 3408  CB  PHE A 422     6950   5459   5093   -265   -313    -58       C  
ATOM   3409  CG  PHE A 422     -22.360 -10.808  53.360  1.00 47.09           C  
ANISOU 3409  CG  PHE A 422     6987   5655   5251   -299   -360    -85       C  
ATOM   3410  CD1 PHE A 422     -21.823  -9.669  52.759  1.00 49.56           C  
ANISOU 3410  CD1 PHE A 422     7267   5993   5569   -404   -351    -96       C  
ATOM   3411  CD2 PHE A 422     -21.493 -11.684  54.002  1.00 47.44           C  
ANISOU 3411  CD2 PHE A 422     6976   5742   5306   -231   -420   -101       C  
ATOM   3412  CE1 PHE A 422     -20.450  -9.411  52.813  1.00 50.70           C  
ANISOU 3412  CE1 PHE A 422     7301   6230   5732   -463   -389   -125       C  
ATOM   3413  CE2 PHE A 422     -20.119 -11.424  54.050  1.00 50.35           C  
ANISOU 3413  CE2 PHE A 422     7223   6207   5700   -257   -468   -137       C  
ATOM   3414  CZ  PHE A 422     -19.606 -10.300  53.440  1.00 48.88           C  
ANISOU 3414  CZ  PHE A 422     6979   6072   5522   -384   -445   -151       C  
ATOM   3415  N   PHE A 423     -27.060 -10.622  53.068  1.00 47.62           N  
ANISOU 3415  N   PHE A 423     7285   5591   5217   -240   -219    -35       N  
ATOM   3416  CA  PHE A 423     -28.327 -11.126  52.522  1.00 46.38           C  
ANISOU 3416  CA  PHE A 423     7128   5448   5045   -226   -167    -27       C  
ATOM   3417  C   PHE A 423     -29.181  -9.975  51.983  1.00 50.92           C  
ANISOU 3417  C   PHE A 423     7724   6018   5604   -212   -158    -44       C  
ATOM   3418  O   PHE A 423     -30.154 -10.228  51.262  1.00 50.71           O  
ANISOU 3418  O   PHE A 423     7678   6018   5573   -200   -126    -43       O  
ATOM   3419  CB  PHE A 423     -29.097 -12.077  53.474  1.00 47.15           C  
ANISOU 3419  CB  PHE A 423     7254   5567   5096   -218   -150    -16       C  
ATOM   3420  CG  PHE A 423     -29.519 -11.581  54.836  1.00 47.25           C  
ANISOU 3420  CG  PHE A 423     7311   5594   5047   -201   -161    -30       C  
ATOM   3421  CD1 PHE A 423     -30.549 -10.653  54.969  1.00 49.35           C  
ANISOU 3421  CD1 PHE A 423     7579   5895   5277   -170   -138    -62       C  
ATOM   3422  CD2 PHE A 423     -28.980 -12.133  55.989  1.00 48.60           C  
ANISOU 3422  CD2 PHE A 423     7531   5750   5185   -205   -195    -17       C  
ATOM   3423  CE1 PHE A 423     -30.960 -10.215  56.225  1.00 49.57           C  
ANISOU 3423  CE1 PHE A 423     7649   5948   5236   -144   -138    -87       C  
ATOM   3424  CE2 PHE A 423     -29.407 -11.711  57.251  1.00 51.11           C  
ANISOU 3424  CE2 PHE A 423     7903   6086   5430   -195   -198    -32       C  
ATOM   3425  CZ  PHE A 423     -30.380 -10.743  57.359  1.00 48.51           C  
ANISOU 3425  CZ  PHE A 423     7568   5799   5066   -166   -163    -70       C  
ATOM   3426  N   TRP A 424     -28.793  -8.705  52.304  1.00 46.93           N  
ANISOU 3426  N   TRP A 424     7272   5473   5087   -211   -200    -61       N  
ATOM   3427  CA  TRP A 424     -29.436  -7.517  51.758  1.00 44.96           C  
ANISOU 3427  CA  TRP A 424     7083   5187   4814   -181   -216    -78       C  
ATOM   3428  C   TRP A 424     -28.934  -7.327  50.346  1.00 49.10           C  
ANISOU 3428  C   TRP A 424     7608   5683   5366   -238   -210    -57       C  
ATOM   3429  O   TRP A 424     -29.774  -7.179  49.473  1.00 49.89           O  
ANISOU 3429  O   TRP A 424     7720   5780   5455   -206   -201    -57       O  
ATOM   3430  CB  TRP A 424     -29.305  -6.294  52.662  1.00 43.84           C  
ANISOU 3430  CB  TRP A 424     7038   4990   4630   -157   -270   -107       C  
ATOM   3431  CG  TRP A 424     -30.386  -6.289  53.706  1.00 44.56           C  
ANISOU 3431  CG  TRP A 424     7136   5125   4669    -67   -257   -143       C  
ATOM   3432  CD1 TRP A 424     -30.263  -6.687  55.000  1.00 47.38           C  
ANISOU 3432  CD1 TRP A 424     7493   5514   4996    -64   -253   -152       C  
ATOM   3433  CD2 TRP A 424     -31.792  -6.035  53.495  1.00 44.44           C  
ANISOU 3433  CD2 TRP A 424     7108   5157   4619     31   -236   -178       C  
ATOM   3434  NE1 TRP A 424     -31.490  -6.679  55.619  1.00 47.20           N  
ANISOU 3434  NE1 TRP A 424     7460   5559   4916     14   -217   -189       N  
ATOM   3435  CE2 TRP A 424     -32.445  -6.256  54.725  1.00 48.28           C  
ANISOU 3435  CE2 TRP A 424     7574   5717   5052     80   -208   -212       C  
ATOM   3436  CE3 TRP A 424     -32.558  -5.606  52.392  1.00 45.86           C  
ANISOU 3436  CE3 TRP A 424     7289   5335   4800     87   -246   -189       C  
ATOM   3437  CZ2 TRP A 424     -33.834  -6.090  54.883  1.00 47.50           C  
ANISOU 3437  CZ2 TRP A 424     7428   5716   4905    180   -175   -265       C  
ATOM   3438  CZ3 TRP A 424     -33.930  -5.434  52.551  1.00 47.63           C  
ANISOU 3438  CZ3 TRP A 424     7470   5645   4983    202   -232   -241       C  
ATOM   3439  CH2 TRP A 424     -34.556  -5.698  53.781  1.00 48.40           C  
ANISOU 3439  CH2 TRP A 424     7518   5841   5031    246   -191   -281       C  
ATOM   3440  N   ILE A 425     -27.604  -7.528  50.068  1.00 46.11           N  
ANISOU 3440  N   ILE A 425     7194   5308   5019   -320   -209    -42       N  
ATOM   3441  CA  ILE A 425     -27.057  -7.553  48.686  1.00 45.66           C  
ANISOU 3441  CA  ILE A 425     7118   5254   4978   -388   -181    -25       C  
ATOM   3442  C   ILE A 425     -27.869  -8.612  47.909  1.00 47.07           C  
ANISOU 3442  C   ILE A 425     7249   5466   5168   -345   -135    -18       C  
ATOM   3443  O   ILE A 425     -28.173  -8.418  46.741  1.00 48.98           O  
ANISOU 3443  O   ILE A 425     7518   5694   5398   -363   -120     -8       O  
ATOM   3444  CB  ILE A 425     -25.545  -7.932  48.580  1.00 49.31           C  
ANISOU 3444  CB  ILE A 425     7494   5769   5471   -466   -167    -26       C  
ATOM   3445  CG1 ILE A 425     -24.628  -7.066  49.438  1.00 50.32           C  
ANISOU 3445  CG1 ILE A 425     7643   5889   5589   -532   -219    -37       C  
ATOM   3446  CG2 ILE A 425     -25.052  -7.944  47.111  1.00 50.77           C  
ANISOU 3446  CG2 ILE A 425     7656   5980   5654   -540   -119    -17       C  
ATOM   3447  CD1 ILE A 425     -23.247  -7.937  49.811  1.00 59.20           C  
ANISOU 3447  CD1 ILE A 425     8620   7116   6755   -552   -219    -56       C  
ATOM   3448  N   GLY A 426     -28.195  -9.715  48.576  1.00 40.49           N  
ANISOU 3448  N   GLY A 426     6367   4670   4349   -302   -120    -21       N  
ATOM   3449  CA  GLY A 426     -29.006 -10.782  48.020  1.00 39.21           C  
ANISOU 3449  CA  GLY A 426     6177   4533   4188   -282    -86    -15       C  
ATOM   3450  C   GLY A 426     -30.386 -10.290  47.656  1.00 42.38           C  
ANISOU 3450  C   GLY A 426     6601   4942   4559   -248    -90    -22       C  
ATOM   3451  O   GLY A 426     -30.854 -10.550  46.547  1.00 41.96           O  
ANISOU 3451  O   GLY A 426     6544   4897   4501   -257    -77    -17       O  
ATOM   3452  N   TYR A 427     -31.033  -9.535  48.570  1.00 39.46           N  
ANISOU 3452  N   TYR A 427     6255   4579   4161   -198   -115    -41       N  
ATOM   3453  CA  TYR A 427     -32.361  -8.962  48.317  1.00 39.98           C  
ANISOU 3453  CA  TYR A 427     6324   4674   4193   -131   -130    -65       C  
ATOM   3454  C   TYR A 427     -32.336  -7.916  47.224  1.00 48.22           C  
ANISOU 3454  C   TYR A 427     7443   5655   5224   -115   -171    -62       C  
ATOM   3455  O   TYR A 427     -33.326  -7.753  46.513  1.00 49.54           O  
ANISOU 3455  O   TYR A 427     7605   5848   5370    -63   -190    -75       O  
ATOM   3456  CB  TYR A 427     -32.981  -8.356  49.572  1.00 40.20           C  
ANISOU 3456  CB  TYR A 427     6359   4731   4183    -59   -144   -101       C  
ATOM   3457  CG  TYR A 427     -33.464  -9.357  50.600  1.00 40.00           C  
ANISOU 3457  CG  TYR A 427     6268   4791   4139    -77    -98   -107       C  
ATOM   3458  CD1 TYR A 427     -33.884 -10.634  50.221  1.00 41.16           C  
ANISOU 3458  CD1 TYR A 427     6355   4993   4292   -139    -58    -87       C  
ATOM   3459  CD2 TYR A 427     -33.550  -9.012  51.947  1.00 39.08           C  
ANISOU 3459  CD2 TYR A 427     6170   4694   3983    -43    -98   -131       C  
ATOM   3460  CE1 TYR A 427     -34.330 -11.554  51.171  1.00 43.62           C  
ANISOU 3460  CE1 TYR A 427     6637   5369   4568   -185    -17    -84       C  
ATOM   3461  CE2 TYR A 427     -34.026  -9.909  52.896  1.00 38.92           C  
ANISOU 3461  CE2 TYR A 427     6109   4754   3926    -78    -51   -131       C  
ATOM   3462  CZ  TYR A 427     -34.393 -11.184  52.509  1.00 48.43           C  
ANISOU 3462  CZ  TYR A 427     7265   6004   5134   -158    -11   -103       C  
ATOM   3463  OH  TYR A 427     -34.804 -12.059  53.473  1.00 49.78           O  
ANISOU 3463  OH  TYR A 427     7429   6236   5250   -220     32    -94       O  
ATOM   3464  N   CYS A 428     -31.211  -7.211  47.088  1.00 46.44           N  
ANISOU 3464  N   CYS A 428     7292   5350   5002   -168   -191    -45       N  
ATOM   3465  CA  CYS A 428     -31.019  -6.182  46.077  1.00 47.64           C  
ANISOU 3465  CA  CYS A 428     7555   5421   5123   -189   -230    -32       C  
ATOM   3466  C   CYS A 428     -31.013  -6.775  44.721  1.00 52.40           C  
ANISOU 3466  C   CYS A 428     8138   6041   5729   -236   -201     -9       C  
ATOM   3467  O   CYS A 428     -31.327  -6.062  43.769  1.00 54.89           O  
ANISOU 3467  O   CYS A 428     8550   6302   6003   -228   -239      2       O  
ATOM   3468  CB  CYS A 428     -29.738  -5.404  46.330  1.00 48.49           C  
ANISOU 3468  CB  CYS A 428     7740   5461   5225   -282   -247    -17       C  
ATOM   3469  SG  CYS A 428     -29.849  -4.279  47.726  1.00 53.57           S  
ANISOU 3469  SG  CYS A 428     8481   6039   5834   -223   -313    -49       S  
ATOM   3470  N   ASN A 429     -30.645  -8.065  44.610  1.00 46.85           N  
ANISOU 3470  N   ASN A 429     7333   5401   5065   -278   -141     -2       N  
ATOM   3471  CA  ASN A 429     -30.584  -8.731  43.316  1.00 47.58           C  
ANISOU 3471  CA  ASN A 429     7415   5510   5155   -320   -108     11       C  
ATOM   3472  C   ASN A 429     -31.943  -8.760  42.589  1.00 54.14           C  
ANISOU 3472  C   ASN A 429     8258   6356   5955   -262   -140      4       C  
ATOM   3473  O   ASN A 429     -31.987  -8.772  41.350  1.00 55.51           O  
ANISOU 3473  O   ASN A 429     8478   6513   6100   -292   -142     17       O  
ATOM   3474  CB  ASN A 429     -29.998 -10.137  43.433  1.00 44.80           C  
ANISOU 3474  CB  ASN A 429     6974   5207   4841   -348    -52      7       C  
ATOM   3475  CG  ASN A 429     -30.011 -10.829  42.112  1.00 56.08           C  
ANISOU 3475  CG  ASN A 429     8407   6646   6255   -378    -20     10       C  
ATOM   3476  OD1 ASN A 429     -31.018 -11.393  41.710  1.00 47.17           O  
ANISOU 3476  OD1 ASN A 429     7273   5535   5114   -356    -29      6       O  
ATOM   3477  ND2 ASN A 429     -28.935 -10.713  41.366  1.00 54.11           N  
ANISOU 3477  ND2 ASN A 429     8169   6396   5995   -438     17     13       N  
ATOM   3478  N   SER A 430     -33.043  -8.755  43.371  1.00 50.14           N  
ANISOU 3478  N   SER A 430     7705   5899   5448   -181   -166    -22       N  
ATOM   3479  CA  SER A 430     -34.416  -8.809  42.869  1.00 49.29           C  
ANISOU 3479  CA  SER A 430     7565   5849   5314   -117   -203    -43       C  
ATOM   3480  C   SER A 430     -34.782  -7.576  42.015  1.00 52.51           C  
ANISOU 3480  C   SER A 430     8087   6193   5673    -52   -282    -43       C  
ATOM   3481  O   SER A 430     -35.588  -7.692  41.100  1.00 52.67           O  
ANISOU 3481  O   SER A 430     8103   6244   5666    -21   -320    -50       O  
ATOM   3482  CB  SER A 430     -35.395  -9.051  44.015  1.00 50.83           C  
ANISOU 3482  CB  SER A 430     7659   6142   5510    -57   -199    -80       C  
ATOM   3483  OG  SER A 430     -35.083 -10.245  44.728  1.00 54.28           O  
ANISOU 3483  OG  SER A 430     8031   6618   5974   -133   -135    -70       O  
ATOM   3484  N   SER A 431     -34.109  -6.443  42.249  1.00 47.50           N  
ANISOU 3484  N   SER A 431     7573   5457   5019    -46   -314    -32       N  
ATOM   3485  CA  SER A 431     -34.323  -5.192  41.530  1.00 48.02           C  
ANISOU 3485  CA  SER A 431     7803   5421   5021      7   -402    -24       C  
ATOM   3486  C   SER A 431     -33.486  -5.067  40.275  1.00 51.60           C  
ANISOU 3486  C   SER A 431     8369   5798   5439   -113   -389     26       C  
ATOM   3487  O   SER A 431     -33.771  -4.205  39.453  1.00 51.03           O  
ANISOU 3487  O   SER A 431     8452   5639   5298    -83   -466     41       O  
ATOM   3488  CB  SER A 431     -34.020  -4.003  42.450  1.00 51.18           C  
ANISOU 3488  CB  SER A 431     8316   5729   5400     54   -450    -37       C  
ATOM   3489  OG  SER A 431     -32.667  -3.867  42.871  1.00 52.67           O  
ANISOU 3489  OG  SER A 431     8543   5864   5605    -78   -404     -8       O  
ATOM   3490  N   LEU A 432     -32.449  -5.917  40.139  1.00 49.34           N  
ANISOU 3490  N   LEU A 432     8013   5547   5188   -242   -295     47       N  
ATOM   3491  CA  LEU A 432     -31.405  -5.863  39.097  1.00 48.85           C  
ANISOU 3491  CA  LEU A 432     8027   5446   5089   -378   -251     84       C  
ATOM   3492  C   LEU A 432     -31.773  -6.399  37.720  1.00 51.09           C  
ANISOU 3492  C   LEU A 432     8333   5748   5332   -398   -244     95       C  
ATOM   3493  O   LEU A 432     -31.453  -5.729  36.737  1.00 51.32           O  
ANISOU 3493  O   LEU A 432     8509   5707   5283   -465   -261    128       O  
ATOM   3494  CB  LEU A 432     -30.109  -6.529  39.590  1.00 47.72           C  
ANISOU 3494  CB  LEU A 432     7777   5358   4997   -478   -157     82       C  
ATOM   3495  CG  LEU A 432     -29.441  -5.764  40.765  1.00 51.24           C  
ANISOU 3495  CG  LEU A 432     8240   5769   5459   -502   -173     80       C  
ATOM   3496  CD1 LEU A 432     -28.039  -6.203  40.970  1.00 51.49           C  
ANISOU 3496  CD1 LEU A 432     8181   5862   5522   -614    -97     79       C  
ATOM   3497  CD2 LEU A 432     -29.447  -4.261  40.542  1.00 50.05           C  
ANISOU 3497  CD2 LEU A 432     8289   5493   5233   -531   -248    103       C  
ATOM   3498  N   ASN A 433     -32.433  -7.562  37.628  1.00 46.47           N  
ANISOU 3498  N   ASN A 433     7626   5248   4783   -355   -222     71       N  
ATOM   3499  CA  ASN A 433     -32.830  -8.134  36.331  1.00 46.02           C  
ANISOU 3499  CA  ASN A 433     7595   5208   4681   -376   -224     75       C  
ATOM   3500  C   ASN A 433     -33.514  -7.089  35.438  1.00 50.07           C  
ANISOU 3500  C   ASN A 433     8267   5648   5109   -332   -326     94       C  
ATOM   3501  O   ASN A 433     -33.040  -6.920  34.318  1.00 50.99           O  
ANISOU 3501  O   ASN A 433     8500   5720   5153   -415   -312    124       O  
ATOM   3502  CB  ASN A 433     -33.670  -9.419  36.480  1.00 44.70           C  
ANISOU 3502  CB  ASN A 433     7295   5131   4556   -339   -214     43       C  
ATOM   3503  CG  ASN A 433     -32.955 -10.603  37.066  1.00 66.66           C  
ANISOU 3503  CG  ASN A 433     9975   7956   7397   -387   -125     29       C  
ATOM   3504  OD1 ASN A 433     -31.780 -10.558  37.461  1.00 61.85           O  
ANISOU 3504  OD1 ASN A 433     9356   7333   6811   -430    -67     35       O  
ATOM   3505  ND2 ASN A 433     -33.660 -11.712  37.130  1.00 63.07           N  
ANISOU 3505  ND2 ASN A 433     9449   7555   6960   -381   -123      8       N  
ATOM   3506  N   PRO A 434     -34.517  -6.293  35.904  1.00 46.55           N  
ANISOU 3506  N   PRO A 434     7849   5182   4655   -200   -431     78       N  
ATOM   3507  CA  PRO A 434     -35.091  -5.252  35.017  1.00 47.61           C  
ANISOU 3507  CA  PRO A 434     8167   5226   4696   -135   -549     95       C  
ATOM   3508  C   PRO A 434     -34.077  -4.219  34.494  1.00 52.13           C  
ANISOU 3508  C   PRO A 434     8964   5656   5188   -243   -552    150       C  
ATOM   3509  O   PRO A 434     -34.240  -3.739  33.378  1.00 52.65           O  
ANISOU 3509  O   PRO A 434     9203   5645   5155   -260   -615    182       O  
ATOM   3510  CB  PRO A 434     -36.187  -4.608  35.874  1.00 49.58           C  
ANISOU 3510  CB  PRO A 434     8382   5493   4962     50   -651     50       C  
ATOM   3511  CG  PRO A 434     -36.528  -5.659  36.884  1.00 53.00           C  
ANISOU 3511  CG  PRO A 434     8577   6072   5487     64   -578      7       C  
ATOM   3512  CD  PRO A 434     -35.234  -6.328  37.199  1.00 47.48           C  
ANISOU 3512  CD  PRO A 434     7839   5367   4835    -89   -452     34       C  
ATOM   3513  N   VAL A 435     -33.006  -3.918  35.258  1.00 48.35           N  
ANISOU 3513  N   VAL A 435     8487   5147   4738   -338   -483    163       N  
ATOM   3514  CA  VAL A 435     -31.951  -2.989  34.806  1.00 48.39           C  
ANISOU 3514  CA  VAL A 435     8688   5038   4658   -490   -471    215       C  
ATOM   3515  C   VAL A 435     -31.121  -3.688  33.703  1.00 53.08           C  
ANISOU 3515  C   VAL A 435     9267   5689   5213   -653   -361    239       C  
ATOM   3516  O   VAL A 435     -30.937  -3.120  32.633  1.00 55.25           O  
ANISOU 3516  O   VAL A 435     9734   5886   5372   -741   -383    283       O  
ATOM   3517  CB  VAL A 435     -31.095  -2.424  35.981  1.00 50.29           C  
ANISOU 3517  CB  VAL A 435     8925   5246   4936   -552   -443    214       C  
ATOM   3518  CG1 VAL A 435     -30.046  -1.433  35.486  1.00 50.18           C  
ANISOU 3518  CG1 VAL A 435     9121   5123   4822   -744   -434    268       C  
ATOM   3519  CG2 VAL A 435     -31.989  -1.770  37.030  1.00 49.95           C  
ANISOU 3519  CG2 VAL A 435     8909   5152   4920   -371   -549    178       C  
ATOM   3520  N   ILE A 436     -30.696  -4.940  33.940  1.00 47.15           N  
ANISOU 3520  N   ILE A 436     8301   5070   4543   -679   -250    207       N  
ATOM   3521  CA  ILE A 436     -29.954  -5.768  32.975  1.00 45.44           C  
ANISOU 3521  CA  ILE A 436     8042   4928   4295   -794   -139    207       C  
ATOM   3522  C   ILE A 436     -30.692  -5.850  31.638  1.00 49.80           C  
ANISOU 3522  C   ILE A 436     8719   5449   4755   -777   -189    223       C  
ATOM   3523  O   ILE A 436     -30.088  -5.600  30.598  1.00 51.77           O  
ANISOU 3523  O   ILE A 436     9092   5679   4900   -905   -144    253       O  
ATOM   3524  CB  ILE A 436     -29.664  -7.177  33.555  1.00 46.31           C  
ANISOU 3524  CB  ILE A 436     7922   5162   4511   -759    -49    157       C  
ATOM   3525  CG1 ILE A 436     -28.769  -7.092  34.814  1.00 44.89           C  
ANISOU 3525  CG1 ILE A 436     7630   5018   4409   -785     -4    143       C  
ATOM   3526  CG2 ILE A 436     -29.054  -8.090  32.488  1.00 48.56           C  
ANISOU 3526  CG2 ILE A 436     8177   5520   4755   -833     51    140       C  
ATOM   3527  CD1 ILE A 436     -29.062  -8.116  35.889  1.00 42.56           C  
ANISOU 3527  CD1 ILE A 436     7162   4787   4222   -682      6    103       C  
ATOM   3528  N   TYR A 437     -31.987  -6.188  31.663  1.00 45.20           N  
ANISOU 3528  N   TYR A 437     8099   4874   4200   -631   -282    200       N  
ATOM   3529  CA  TYR A 437     -32.779  -6.285  30.438  1.00 45.62           C  
ANISOU 3529  CA  TYR A 437     8260   4907   4167   -602   -353    210       C  
ATOM   3530  C   TYR A 437     -32.762  -4.966  29.687  1.00 50.25           C  
ANISOU 3530  C   TYR A 437     9113   5357   4622   -640   -439    265       C  
ATOM   3531  O   TYR A 437     -32.310  -4.960  28.561  1.00 48.64           O  
ANISOU 3531  O   TYR A 437     9037   5132   4311   -755   -401    295       O  
ATOM   3532  CB  TYR A 437     -34.220  -6.770  30.713  1.00 46.46           C  
ANISOU 3532  CB  TYR A 437     8257   5069   4327   -443   -452    169       C  
ATOM   3533  CG  TYR A 437     -34.339  -8.121  31.398  1.00 45.83           C  
ANISOU 3533  CG  TYR A 437     7952   5106   4354   -431   -377    122       C  
ATOM   3534  CD1 TYR A 437     -33.578  -9.210  30.979  1.00 46.22           C  
ANISOU 3534  CD1 TYR A 437     7948   5202   4410   -526   -263    109       C  
ATOM   3535  CD2 TYR A 437     -35.270  -8.331  32.409  1.00 46.27           C  
ANISOU 3535  CD2 TYR A 437     7865   5226   4489   -323   -427     87       C  
ATOM   3536  CE1 TYR A 437     -33.712 -10.458  31.580  1.00 45.81           C  
ANISOU 3536  CE1 TYR A 437     7737   5227   4440   -512   -213     69       C  
ATOM   3537  CE2 TYR A 437     -35.406  -9.570  33.022  1.00 46.19           C  
ANISOU 3537  CE2 TYR A 437     7685   5307   4556   -337   -364     53       C  
ATOM   3538  CZ  TYR A 437     -34.633 -10.635  32.597  1.00 53.65           C  
ANISOU 3538  CZ  TYR A 437     8612   6268   5506   -430   -265     48       C  
ATOM   3539  OH  TYR A 437     -34.772 -11.857  33.206  1.00 57.86           O  
ANISOU 3539  OH  TYR A 437     9020   6862   6102   -441   -220     17       O  
ATOM   3540  N   THR A 438     -33.153  -3.839  30.337  1.00 49.57           N  
ANISOU 3540  N   THR A 438     9132   5171   4531   -553   -549    279       N  
ATOM   3541  CA  THR A 438     -33.132  -2.472  29.763  1.00 51.29           C  
ANISOU 3541  CA  THR A 438     9655   5220   4614   -581   -654    335       C  
ATOM   3542  C   THR A 438     -31.798  -2.181  29.065  1.00 54.09           C  
ANISOU 3542  C   THR A 438    10148   5535   4867   -829   -542    390       C  
ATOM   3543  O   THR A 438     -31.787  -1.940  27.864  1.00 54.79           O  
ANISOU 3543  O   THR A 438    10430   5567   4822   -907   -566    432       O  
ATOM   3544  CB  THR A 438     -33.338  -1.424  30.878  1.00 64.42           C  
ANISOU 3544  CB  THR A 438    11386   6783   6306   -480   -745    329       C  
ATOM   3545  OG1 THR A 438     -34.498  -1.764  31.618  1.00 68.68           O  
ANISOU 3545  OG1 THR A 438    11753   7402   6941   -261   -819    266       O  
ATOM   3546  CG2 THR A 438     -33.465   0.003  30.347  1.00 66.49           C  
ANISOU 3546  CG2 THR A 438    12004   6838   6422   -476   -887    383       C  
ATOM   3547  N   VAL A 439     -30.688  -2.233  29.836  1.00 49.20           N  
ANISOU 3547  N   VAL A 439     9418   4968   4308   -955   -421    385       N  
ATOM   3548  CA  VAL A 439     -29.310  -1.966  29.419  1.00 49.61           C  
ANISOU 3548  CA  VAL A 439     9535   5035   4280  -1205   -295    421       C  
ATOM   3549  C   VAL A 439     -28.845  -2.825  28.251  1.00 55.19           C  
ANISOU 3549  C   VAL A 439    10196   5851   4923  -1315   -174    417       C  
ATOM   3550  O   VAL A 439     -28.386  -2.260  27.266  1.00 57.19           O  
ANISOU 3550  O   VAL A 439    10656   6051   5022  -1481   -151    468       O  
ATOM   3551  CB  VAL A 439     -28.308  -2.056  30.604  1.00 51.71           C  
ANISOU 3551  CB  VAL A 439     9617   5382   4648  -1283   -198    395       C  
ATOM   3552  CG1 VAL A 439     -26.867  -1.887  30.122  1.00 52.27           C  
ANISOU 3552  CG1 VAL A 439     9701   5521   4636  -1551    -57    418       C  
ATOM   3553  CG2 VAL A 439     -28.636  -1.029  31.689  1.00 51.21           C  
ANISOU 3553  CG2 VAL A 439     9655   5189   4614  -1208   -317    403       C  
ATOM   3554  N   PHE A 440     -28.954  -4.164  28.363  1.00 51.68           N  
ANISOU 3554  N   PHE A 440     9506   5549   4581  -1229    -99    355       N  
ATOM   3555  CA  PHE A 440     -28.448  -5.137  27.386  1.00 52.69           C  
ANISOU 3555  CA  PHE A 440     9566   5793   4662  -1306     27    329       C  
ATOM   3556  C   PHE A 440     -29.425  -5.590  26.264  1.00 59.26           C  
ANISOU 3556  C   PHE A 440    10499   6598   5419  -1230    -42    329       C  
ATOM   3557  O   PHE A 440     -28.955  -6.188  25.292  1.00 61.68           O  
ANISOU 3557  O   PHE A 440    10814   6976   5646  -1317     58    313       O  
ATOM   3558  CB  PHE A 440     -27.905  -6.374  28.118  1.00 53.30           C  
ANISOU 3558  CB  PHE A 440     9352   6023   4877  -1257    142    257       C  
ATOM   3559  CG  PHE A 440     -26.678  -6.099  28.949  1.00 55.67           C  
ANISOU 3559  CG  PHE A 440     9534   6394   5224  -1363    235    247       C  
ATOM   3560  CD1 PHE A 440     -25.413  -6.078  28.368  1.00 61.59           C  
ANISOU 3560  CD1 PHE A 440    10258   7251   5893  -1544    378    239       C  
ATOM   3561  CD2 PHE A 440     -26.784  -5.829  30.308  1.00 56.10           C  
ANISOU 3561  CD2 PHE A 440     9499   6422   5393  -1288    180    241       C  
ATOM   3562  CE1 PHE A 440     -24.276  -5.786  29.138  1.00 62.66           C  
ANISOU 3562  CE1 PHE A 440    10264   7475   6069  -1653    454    224       C  
ATOM   3563  CE2 PHE A 440     -25.650  -5.536  31.072  1.00 58.86           C  
ANISOU 3563  CE2 PHE A 440     9746   6839   5780  -1393    251    231       C  
ATOM   3564  CZ  PHE A 440     -24.407  -5.518  30.484  1.00 58.87           C  
ANISOU 3564  CZ  PHE A 440     9707   6955   5707  -1576    382    223       C  
ATOM   3565  N   ASN A 441     -30.743  -5.327  26.381  1.00 54.25           N  
ANISOU 3565  N   ASN A 441     9930   5878   4804  -1068   -209    337       N  
ATOM   3566  CA  ASN A 441     -31.743  -5.760  25.405  1.00 54.16           C  
ANISOU 3566  CA  ASN A 441     9992   5857   4731   -988   -297    330       C  
ATOM   3567  C   ASN A 441     -32.590  -4.615  24.890  1.00 61.80           C  
ANISOU 3567  C   ASN A 441    11217   6676   5587   -927   -477    383       C  
ATOM   3568  O   ASN A 441     -33.217  -3.901  25.677  1.00 62.12           O  
ANISOU 3568  O   ASN A 441    11276   6648   5679   -799   -598    387       O  
ATOM   3569  CB  ASN A 441     -32.617  -6.892  25.975  1.00 51.38           C  
ANISOU 3569  CB  ASN A 441     9413   5596   4514   -837   -326    265       C  
ATOM   3570  CG  ASN A 441     -33.558  -7.509  24.965  1.00 76.14           C  
ANISOU 3570  CG  ASN A 441    12592   8748   7588   -784   -405    248       C  
ATOM   3571  OD1 ASN A 441     -34.716  -7.107  24.839  1.00 72.70           O  
ANISOU 3571  OD1 ASN A 441    12214   8274   7135   -665   -567    253       O  
ATOM   3572  ND2 ASN A 441     -33.081  -8.484  24.207  1.00 64.72           N  
ANISOU 3572  ND2 ASN A 441    11124   7366   6101   -864   -299    220       N  
ATOM   3573  N   GLN A 442     -32.627  -4.464  23.557  1.00 61.39           N  
ANISOU 3573  N   GLN A 442    11375   6576   5373  -1004   -502    419       N  
ATOM   3574  CA  GLN A 442     -33.378  -3.412  22.875  1.00 63.93           C  
ANISOU 3574  CA  GLN A 442    11989   6743   5558   -948   -687    474       C  
ATOM   3575  C   GLN A 442     -34.885  -3.570  22.969  1.00 68.65           C  
ANISOU 3575  C   GLN A 442    12528   7348   6209   -710   -875    436       C  
ATOM   3576  O   GLN A 442     -35.583  -2.566  23.069  1.00 71.17           O  
ANISOU 3576  O   GLN A 442    13010   7548   6483   -581  -1051    460       O  
ATOM   3577  CB  GLN A 442     -32.944  -3.242  21.402  1.00 67.85           C  
ANISOU 3577  CB  GLN A 442    12742   7191   5849  -1113   -656    526       C  
ATOM   3578  CG  GLN A 442     -33.051  -4.516  20.519  1.00 95.67           C  
ANISOU 3578  CG  GLN A 442    16163  10839   9349  -1132   -580    479       C  
ATOM   3579  CD  GLN A 442     -33.510  -4.259  19.093  1.00108.70           C  
ANISOU 3579  CD  GLN A 442    18092  12409  10800  -1161   -683    520       C  
ATOM   3580  OE1 GLN A 442     -34.345  -3.390  18.819  1.00101.90           O  
ANISOU 3580  OE1 GLN A 442    17444  11415   9860  -1057   -885    563       O  
ATOM   3581  NE2 GLN A 442     -32.996  -5.040  18.151  1.00100.85           N  
ANISOU 3581  NE2 GLN A 442    17108  11497   9715  -1285   -554    501       N  
ATOM   3582  N   ASP A 443     -35.383  -4.809  22.941  1.00 63.26           N  
ANISOU 3582  N   ASP A 443    11618   6806   5612   -653   -845    373       N  
ATOM   3583  CA  ASP A 443     -36.814  -5.114  22.969  1.00 62.74           C  
ANISOU 3583  CA  ASP A 443    11453   6793   5591   -462  -1009    327       C  
ATOM   3584  C   ASP A 443     -37.475  -4.822  24.302  1.00 61.12           C  
ANISOU 3584  C   ASP A 443    11073   6624   5526   -294  -1078    288       C  
ATOM   3585  O   ASP A 443     -38.613  -4.347  24.314  1.00 61.81           O  
ANISOU 3585  O   ASP A 443    11177   6706   5601   -113  -1259    267       O  
ATOM   3586  CB  ASP A 443     -37.059  -6.546  22.512  1.00 64.76           C  
ANISOU 3586  CB  ASP A 443    11544   7182   5879   -499   -946    275       C  
ATOM   3587  CG  ASP A 443     -36.553  -6.740  21.098  1.00 81.99           C  
ANISOU 3587  CG  ASP A 443    13929   9325   7898   -637   -901    306       C  
ATOM   3588  OD1 ASP A 443     -36.958  -5.945  20.204  1.00 86.19           O  
ANISOU 3588  OD1 ASP A 443    14710   9755   8282   -614  -1040    351       O  
ATOM   3589  OD2 ASP A 443     -35.737  -7.666  20.882  1.00 88.03           O1-
ANISOU 3589  OD2 ASP A 443    14618  10158   8671   -759   -731    281       O1-
ATOM   3590  N   PHE A 444     -36.756  -5.055  25.410  1.00 52.41           N  
ANISOU 3590  N   PHE A 444     9809   5563   4542   -344   -940    274       N  
ATOM   3591  CA  PHE A 444     -37.216  -4.719  26.751  1.00 49.27           C  
ANISOU 3591  CA  PHE A 444     9265   5194   4263   -206   -982    239       C  
ATOM   3592  C   PHE A 444     -37.069  -3.204  26.912  1.00 56.17           C  
ANISOU 3592  C   PHE A 444    10382   5898   5061   -154  -1082    283       C  
ATOM   3593  O   PHE A 444     -37.992  -2.579  27.428  1.00 58.91           O  
ANISOU 3593  O   PHE A 444    10726   6230   5428     43  -1225    252       O  
ATOM   3594  CB  PHE A 444     -36.399  -5.439  27.816  1.00 48.07           C  
ANISOU 3594  CB  PHE A 444     8902   5123   4240   -289   -809    216       C  
ATOM   3595  CG  PHE A 444     -36.797  -6.857  28.152  1.00 47.23           C  
ANISOU 3595  CG  PHE A 444     8541   5169   4234   -285   -745    160       C  
ATOM   3596  CD1 PHE A 444     -37.849  -7.114  29.027  1.00 49.43           C  
ANISOU 3596  CD1 PHE A 444     8632   5547   4603   -154   -808    108       C  
ATOM   3597  CD2 PHE A 444     -36.036  -7.932  27.712  1.00 46.65           C  
ANISOU 3597  CD2 PHE A 444     8420   5142   4165   -419   -609    154       C  
ATOM   3598  CE1 PHE A 444     -38.166  -8.425  29.403  1.00 48.00           C  
ANISOU 3598  CE1 PHE A 444     8241   5494   4501   -187   -743     64       C  
ATOM   3599  CE2 PHE A 444     -36.355  -9.241  28.094  1.00 47.63           C  
ANISOU 3599  CE2 PHE A 444     8349   5374   4373   -421   -558    105       C  
ATOM   3600  CZ  PHE A 444     -37.420  -9.477  28.930  1.00 44.97           C  
ANISOU 3600  CZ  PHE A 444     7850   5122   4116   -321   -626     66       C  
ATOM   3601  N   ARG A 445     -35.953  -2.600  26.429  1.00 51.51           N  
ANISOU 3601  N   ARG A 445    10016   5186   4371   -329  -1016    351       N  
ATOM   3602  CA  ARG A 445     -35.760  -1.145  26.470  1.00 52.84           C  
ANISOU 3602  CA  ARG A 445    10477   5162   4439   -319  -1119    404       C  
ATOM   3603  C   ARG A 445     -36.916  -0.415  25.776  1.00 59.03           C  
ANISOU 3603  C   ARG A 445    11470   5842   5114   -130  -1350    410       C  
ATOM   3604  O   ARG A 445     -37.467   0.531  26.321  1.00 60.04           O  
ANISOU 3604  O   ARG A 445    11706   5871   5236     45  -1495    397       O  
ATOM   3605  CB  ARG A 445     -34.439  -0.742  25.785  1.00 54.32           C  
ANISOU 3605  CB  ARG A 445    10882   5256   4502   -586  -1007    480       C  
ATOM   3606  CG  ARG A 445     -33.879   0.634  26.243  1.00 58.04           C  
ANISOU 3606  CG  ARG A 445    11609   5542   4903   -652  -1057    533       C  
ATOM   3607  CD  ARG A 445     -32.541   0.985  25.604  1.00 57.94           C  
ANISOU 3607  CD  ARG A 445    11780   5473   4761   -960   -928    605       C  
ATOM   3608  NE  ARG A 445     -31.613  -0.148  25.578  1.00 75.47           N  
ANISOU 3608  NE  ARG A 445    13733   7890   7053  -1121   -705    577       N  
ATOM   3609  CZ  ARG A 445     -31.251  -0.806  24.482  1.00103.21           C  
ANISOU 3609  CZ  ARG A 445    17249  11484  10484  -1247   -606    586       C  
ATOM   3610  NH1 ARG A 445     -31.703  -0.429  23.293  1.00103.63           N1+
ANISOU 3610  NH1 ARG A 445    17569  11435  10370  -1259   -704    634       N1+
ATOM   3611  NH2 ARG A 445     -30.420  -1.837  24.565  1.00 97.71           N  
ANISOU 3611  NH2 ARG A 445    16300  10967   9860  -1352   -413    544       N  
ATOM   3612  N   ARG A 446     -37.270  -0.851  24.572  1.00 57.43           N  
ANISOU 3612  N   ARG A 446    11336   5664   4821   -153  -1392    424       N  
ATOM   3613  CA  ARG A 446     -38.338  -0.253  23.785  1.00 59.06           C  
ANISOU 3613  CA  ARG A 446    11741   5786   4912     24  -1621    429       C  
ATOM   3614  C   ARG A 446     -39.688  -0.439  24.485  1.00 65.94           C  
ANISOU 3614  C   ARG A 446    12372   6786   5898    306  -1755    337       C  
ATOM   3615  O   ARG A 446     -40.458   0.511  24.556  1.00 68.31           O  
ANISOU 3615  O   ARG A 446    12817   6992   6145    524  -1954    322       O  
ATOM   3616  CB  ARG A 446     -38.307  -0.806  22.358  1.00 55.75           C  
ANISOU 3616  CB  ARG A 446    11430   5383   4369    -93  -1615    461       C  
ATOM   3617  CG  ARG A 446     -39.272  -0.162  21.390  1.00 74.24           C  
ANISOU 3617  CG  ARG A 446    14025   7622   6562     64  -1860    480       C  
ATOM   3618  CD  ARG A 446     -39.056  -0.647  19.957  1.00 99.30           C  
ANISOU 3618  CD  ARG A 446    17351  10792   9588    -92  -1837    522       C  
ATOM   3619  NE  ARG A 446     -37.784  -0.177  19.394  1.00115.23           N  
ANISOU 3619  NE  ARG A 446    19647  12673  11462   -356  -1709    613       N  
ATOM   3620  CZ  ARG A 446     -36.769  -0.969  19.062  1.00126.24           C  
ANISOU 3620  CZ  ARG A 446    20956  14160  12851   -597  -1479    622       C  
ATOM   3621  NH1 ARG A 446     -36.872  -2.288  19.203  1.00112.38           N  
ANISOU 3621  NH1 ARG A 446    18879  12598  11220   -598  -1365    551       N  
ATOM   3622  NH2 ARG A 446     -35.649  -0.452  18.570  1.00106.35           N1+
ANISOU 3622  NH2 ARG A 446    18677  11542  10189   -840  -1365    698       N1+
ATOM   3623  N   SER A 447     -39.936  -1.625  25.067  1.00 62.62           N  
ANISOU 3623  N   SER A 447    11589   6578   5627    300  -1642    271       N  
ATOM   3624  CA  SER A 447     -41.169  -1.928  25.797  1.00 63.07           C  
ANISOU 3624  CA  SER A 447    11370   6801   5791    520  -1732    179       C  
ATOM   3625  C   SER A 447     -41.316  -1.033  27.032  1.00 69.06           C  
ANISOU 3625  C   SER A 447    12116   7515   6610    682  -1775    146       C  
ATOM   3626  O   SER A 447     -42.388  -0.479  27.270  1.00 69.41           O  
ANISOU 3626  O   SER A 447    12133   7591   6647    936  -1947     86       O  
ATOM   3627  CB  SER A 447     -41.212  -3.400  26.191  1.00 64.13           C  
ANISOU 3627  CB  SER A 447    11166   7145   6054    417  -1578    131       C  
ATOM   3628  OG  SER A 447     -42.416  -4.001  25.742  1.00 75.04           O  
ANISOU 3628  OG  SER A 447    12392   8683   7438    518  -1690     73       O  
ATOM   3629  N   PHE A 448     -40.218  -0.857  27.784  1.00 66.54           N  
ANISOU 3629  N   PHE A 448    11824   7121   6337    542  -1627    180       N  
ATOM   3630  CA  PHE A 448     -40.182  -0.029  28.981  1.00 66.66           C  
ANISOU 3630  CA  PHE A 448    11852   7076   6400    661  -1650    153       C  
ATOM   3631  C   PHE A 448     -40.424   1.415  28.616  1.00 70.67           C  
ANISOU 3631  C   PHE A 448    12717   7362   6772    808  -1848    179       C  
ATOM   3632  O   PHE A 448     -41.297   2.029  29.214  1.00 71.01           O  
ANISOU 3632  O   PHE A 448    12740   7412   6828   1069  -1985    111       O  
ATOM   3633  CB  PHE A 448     -38.869  -0.228  29.755  1.00 67.95           C  
ANISOU 3633  CB  PHE A 448    11974   7213   6631    448  -1453    187       C  
ATOM   3634  CG  PHE A 448     -38.613  -1.616  30.321  1.00 69.54           C  
ANISOU 3634  CG  PHE A 448    11840   7613   6968    337  -1272    155       C  
ATOM   3635  CD1 PHE A 448     -39.668  -2.440  30.703  1.00 73.73           C  
ANISOU 3635  CD1 PHE A 448    12090   8339   7584    458  -1288     80       C  
ATOM   3636  CD2 PHE A 448     -37.319  -2.067  30.541  1.00 72.17           C  
ANISOU 3636  CD2 PHE A 448    12144   7940   7339    115  -1094    194       C  
ATOM   3637  CE1 PHE A 448     -39.426  -3.705  31.256  1.00 73.75           C  
ANISOU 3637  CE1 PHE A 448    11831   8495   7696    346  -1132     57       C  
ATOM   3638  CE2 PHE A 448     -37.080  -3.330  31.096  1.00 74.21           C  
ANISOU 3638  CE2 PHE A 448    12127   8357   7713     40   -949    162       C  
ATOM   3639  CZ  PHE A 448     -38.134  -4.137  31.461  1.00 72.21           C  
ANISOU 3639  CZ  PHE A 448    11638   8264   7534    151   -971     99       C  
ATOM   3640  N   LYS A 449     -39.728   1.927  27.576  1.00 68.43           N  
ANISOU 3640  N   LYS A 449    12767   6889   6345    651  -1872    272       N  
ATOM   3641  CA  LYS A 449     -39.890   3.298  27.073  1.00 70.71           C  
ANISOU 3641  CA  LYS A 449    13470   6925   6471    758  -2073    315       C  
ATOM   3642  C   LYS A 449     -41.329   3.582  26.659  1.00 76.50           C  
ANISOU 3642  C   LYS A 449    14216   7691   7160   1080  -2312    252       C  
ATOM   3643  O   LYS A 449     -41.844   4.614  27.049  1.00 76.34           O  
ANISOU 3643  O   LYS A 449    14368   7545   7093   1319  -2485    219       O  
ATOM   3644  CB  LYS A 449     -38.928   3.607  25.920  1.00 74.21           C  
ANISOU 3644  CB  LYS A 449    14250   7194   6752    491  -2037    430       C  
ATOM   3645  CG  LYS A 449     -37.670   4.353  26.348  1.00 92.97           C  
ANISOU 3645  CG  LYS A 449    16847   9397   9082    267  -1941    499       C  
ATOM   3646  CD  LYS A 449     -36.972   5.042  25.155  1.00110.76           C  
ANISOU 3646  CD  LYS A 449    19527  11437  11120     46  -1973    612       C  
ATOM   3647  CE  LYS A 449     -35.671   4.382  24.734  1.00127.88           C  
ANISOU 3647  CE  LYS A 449    21624  13690  13275   -320  -1726    669       C  
ATOM   3648  NZ  LYS A 449     -34.588   4.537  25.752  1.00138.26           N1+
ANISOU 3648  NZ  LYS A 449    22852  15013  14668   -502  -1568    674       N1+
ATOM   3649  N   HIS A 450     -41.992   2.641  25.941  1.00 75.51           N  
ANISOU 3649  N   HIS A 450    13890   7748   7052   1100  -2326    224       N  
ATOM   3650  CA  HIS A 450     -43.395   2.718  25.497  1.00 78.39           C  
ANISOU 3650  CA  HIS A 450    14194   8207   7385   1390  -2548    153       C  
ATOM   3651  C   HIS A 450     -44.371   2.812  26.671  1.00 79.89           C  
ANISOU 3651  C   HIS A 450    14096   8566   7694   1675  -2608     29       C  
ATOM   3652  O   HIS A 450     -45.388   3.497  26.557  1.00 82.60           O  
ANISOU 3652  O   HIS A 450    14501   8904   7981   1984  -2834    -35       O  
ATOM   3653  CB  HIS A 450     -43.767   1.515  24.612  1.00 80.56           C  
ANISOU 3653  CB  HIS A 450    14266   8671   7671   1288  -2511    145       C  
ATOM   3654  CG  HIS A 450     -45.087   1.658  23.904  1.00 88.13           C  
ANISOU 3654  CG  HIS A 450    15216   9708   8562   1544  -2758     88       C  
ATOM   3655  ND1 HIS A 450     -46.233   1.019  24.367  1.00 90.97           N  
ANISOU 3655  ND1 HIS A 450    15180  10353   9032   1718  -2803    -28       N  
ATOM   3656  CD2 HIS A 450     -45.402   2.356  22.781  1.00 93.22           C  
ANISOU 3656  CD2 HIS A 450    16196  10191   9034   1642  -2973    131       C  
ATOM   3657  CE1 HIS A 450     -47.198   1.348  23.513  1.00 93.04           C  
ANISOU 3657  CE1 HIS A 450    15526  10632   9192   1923  -3046    -58       C  
ATOM   3658  NE2 HIS A 450     -46.748   2.149  22.543  1.00 94.58           N  
ANISOU 3658  NE2 HIS A 450    16166  10554   9215   1897  -3162     36       N  
ATOM   3659  N   ILE A 451     -44.074   2.131  27.794  1.00 71.15           N  
ANISOU 3659  N   ILE A 451    12678   7617   6740   1583  -2410    -11       N  
ATOM   3660  CA  ILE A 451     -44.935   2.195  28.968  1.00 69.51           C  
ANISOU 3660  CA  ILE A 451    12193   7584   6633   1824  -2437   -129       C  
ATOM   3661  C   ILE A 451     -44.682   3.507  29.733  1.00 72.75           C  
ANISOU 3661  C   ILE A 451    12856   7785   7002   1982  -2515   -138       C  
ATOM   3662  O   ILE A 451     -45.599   4.322  29.901  1.00 75.16           O  
ANISOU 3662  O   ILE A 451    13221   8077   7260   2310  -2712   -218       O  
ATOM   3663  CB  ILE A 451     -44.743   0.949  29.859  1.00 69.82           C  
ANISOU 3663  CB  ILE A 451    11838   7861   6832   1656  -2205   -162       C  
ATOM   3664  CG1 ILE A 451     -45.113  -0.344  29.101  1.00 68.33           C  
ANISOU 3664  CG1 ILE A 451    11423   7867   6671   1517  -2154   -164       C  
ATOM   3665  CG2 ILE A 451     -45.527   1.091  31.190  1.00 70.75           C  
ANISOU 3665  CG2 ILE A 451    11690   8155   7037   1877  -2208   -280       C  
ATOM   3666  CD1 ILE A 451     -44.356  -1.594  29.594  1.00 67.73           C  
ANISOU 3666  CD1 ILE A 451    11131   7897   6707   1239  -1906   -139       C  
ATOM   3667  N   LEU A 452     -43.427   3.705  30.174  1.00 65.54           N  
ANISOU 3667  N   LEU A 452    12094   6709   6099   1752  -2367    -63       N  
ATOM   3668  CA  LEU A 452     -42.977   4.844  30.971  1.00 64.21           C  
ANISOU 3668  CA  LEU A 452    12173   6329   5894   1826  -2408    -62       C  
ATOM   3669  C   LEU A 452     -43.092   6.211  30.307  1.00 70.67           C  
ANISOU 3669  C   LEU A 452    13465   6847   6538   1979  -2644    -26       C  
ATOM   3670  O   LEU A 452     -43.435   7.166  31.002  1.00 72.69           O  
ANISOU 3670  O   LEU A 452    13862   6993   6764   2220  -2767    -87       O  
ATOM   3671  CB  LEU A 452     -41.537   4.629  31.460  1.00 61.20           C  
ANISOU 3671  CB  LEU A 452    11828   5866   5558   1495  -2194     18       C  
ATOM   3672  CG  LEU A 452     -41.284   3.400  32.332  1.00 61.02           C  
ANISOU 3672  CG  LEU A 452    11392   6093   5700   1357  -1971    -17       C  
ATOM   3673  CD1 LEU A 452     -39.819   3.275  32.678  1.00 58.94           C  
ANISOU 3673  CD1 LEU A 452    11194   5737   5462   1051  -1792     62       C  
ATOM   3674  CD2 LEU A 452     -42.139   3.408  33.587  1.00 61.39           C  
ANISOU 3674  CD2 LEU A 452    11186   6303   5835   1600  -1984   -136       C  
ATOM   3675  N   PHE A 453     -42.783   6.321  28.998  1.00 66.66           N  
ANISOU 3675  N   PHE A 453    13228   6196   5904   1840  -2707     72       N  
ATOM   3676  CA  PHE A 453     -42.779   7.600  28.272  1.00 68.57           C  
ANISOU 3676  CA  PHE A 453    13983   6117   5954   1937  -2931    129       C  
ATOM   3677  C   PHE A 453     -43.680   7.624  27.034  1.00 73.89           C  
ANISOU 3677  C   PHE A 453    14762   6794   6518   2106  -3138    130       C  
ATOM   3678  O   PHE A 453     -43.525   6.812  26.126  1.00 72.97           O  
ANISOU 3678  O   PHE A 453    14562   6774   6390   1915  -3064    183       O  
ATOM   3679  CB  PHE A 453     -41.329   8.016  27.911  1.00 70.20           C  
ANISOU 3679  CB  PHE A 453    14541   6073   6059   1561  -2824    269       C  
ATOM   3680  CG  PHE A 453     -40.340   7.873  29.051  1.00 70.17           C  
ANISOU 3680  CG  PHE A 453    14403   6093   6164   1354  -2613    273       C  
ATOM   3681  CD1 PHE A 453     -40.341   8.773  30.115  1.00 74.53           C  
ANISOU 3681  CD1 PHE A 453    15085   6511   6720   1501  -2680    225       C  
ATOM   3682  CD2 PHE A 453     -39.441   6.814  29.083  1.00 69.51           C  
ANISOU 3682  CD2 PHE A 453    14058   6175   6178   1035  -2357    315       C  
ATOM   3683  CE1 PHE A 453     -39.460   8.611  31.192  1.00 73.53           C  
ANISOU 3683  CE1 PHE A 453    14823   6421   6694   1315  -2496    223       C  
ATOM   3684  CE2 PHE A 453     -38.570   6.647  30.163  1.00 71.09           C  
ANISOU 3684  CE2 PHE A 453    14114   6415   6481    870  -2180    310       C  
ATOM   3685  CZ  PHE A 453     -38.588   7.544  31.214  1.00 70.00           C  
ANISOU 3685  CZ  PHE A 453    14101   6149   6346   1004  -2251    267       C  
ATOM   3686  N   ARG A 454     -44.619   8.573  26.993  1.00 72.97           N  
ANISOU 3686  N   ARG A 454    14843   6569   6314   2480  -3408     65       N  
ATOM   3687  CA  ARG A 454     -45.568   8.735  25.887  1.00 94.33           C  
ANISOU 3687  CA  ARG A 454    17667   9269   8904   2702  -3652     51       C  
ATOM   3688  C   ARG A 454     -45.722  10.207  25.473  1.00115.91           C  
ANISOU 3688  C   ARG A 454    20971  11636  11435   2922  -3939     83       C  
ATOM   3689  O   ARG A 454     -44.844  11.035  25.733  1.00 79.83           O  
ANISOU 3689  O   ARG A 454    16779   6772   6781   2778  -3922    159       O  
ATOM   3690  CB  ARG A 454     -46.933   8.124  26.262  1.00 94.90           C  
ANISOU 3690  CB  ARG A 454    17260   9698   9099   3023  -3719   -106       C  
ATOM   3691  CG  ARG A 454     -46.874   6.637  26.613  1.00101.61           C  
ANISOU 3691  CG  ARG A 454    17582  10896  10130   2800  -3459   -134       C  
ATOM   3692  CD  ARG A 454     -48.091   6.162  27.372  1.00113.31           C  
ANISOU 3692  CD  ARG A 454    18586  12727  11738   3078  -3484   -296       C  
ATOM   3693  NE  ARG A 454     -48.200   4.703  27.342  1.00127.06           N  
ANISOU 3693  NE  ARG A 454    19891  14780  13607   2858  -3293   -309       N  
ATOM   3694  CZ  ARG A 454     -48.783   4.011  26.364  1.00144.97           C  
ANISOU 3694  CZ  ARG A 454    22032  17199  15850   2832  -3362   -313       C  
ATOM   3695  NH1 ARG A 454     -49.316   4.640  25.319  1.00132.83           N  
ANISOU 3695  NH1 ARG A 454    20759  15544  14167   3020  -3621   -302       N  
ATOM   3696  NH2 ARG A 454     -48.835   2.686  26.421  1.00129.29           N  
ANISOU 3696  NH2 ARG A 454    19677  15472  13975   2616  -3184   -326       N  
TER    3697      ARG A 454                                                      
ATOM   3698  N   PRO B  41      -1.085  -6.719  75.223  1.00115.02           N  
ANISOU 3698  N   PRO B  41    13765  18947  10992   3193  -1090   -331       N  
ATOM   3699  CA  PRO B  41      -2.172  -6.791  76.214  1.00114.32           C  
ANISOU 3699  CA  PRO B  41    13978  18633  10828   3267  -1018   -218       C  
ATOM   3700  C   PRO B  41      -3.549  -7.159  75.624  1.00114.34           C  
ANISOU 3700  C   PRO B  41    14240  18154  11050   3202   -802    -80       C  
ATOM   3701  O   PRO B  41      -4.135  -8.077  76.194  1.00114.50           O  
ANISOU 3701  O   PRO B  41    14480  18013  11012   3444   -713    102       O  
ATOM   3702  CB  PRO B  41      -2.146  -5.418  76.907  1.00116.73           C  
ANISOU 3702  CB  PRO B  41    14242  19085  11024   3004  -1123   -405       C  
ATOM   3703  CG  PRO B  41      -1.009  -4.637  76.252  1.00122.06           C  
ANISOU 3703  CG  PRO B  41    14594  20061  11724   2771  -1251   -616       C  
ATOM   3704  CD  PRO B  41      -0.155  -5.611  75.502  1.00118.20           C  
ANISOU 3704  CD  PRO B  41    13913  19722  11277   2978  -1264   -555       C  
ATOM   3705  N   PRO B  42      -4.095  -6.558  74.512  1.00106.96           N  
ANISOU 3705  N   PRO B  42    13297  16989  10355   2899   -710   -146       N  
ATOM   3706  CA  PRO B  42      -5.415  -7.003  74.017  1.00103.98           C  
ANISOU 3706  CA  PRO B  42    13151  16191  10165   2865   -516    -12       C  
ATOM   3707  C   PRO B  42      -5.321  -8.103  72.950  1.00106.28           C  
ANISOU 3707  C   PRO B  42    13434  16342  10606   2984   -424     91       C  
ATOM   3708  O   PRO B  42      -4.448  -8.035  72.072  1.00106.90           O  
ANISOU 3708  O   PRO B  42    13299  16573  10744   2929   -480      3       O  
ATOM   3709  CB  PRO B  42      -6.020  -5.718  73.434  1.00103.64           C  
ANISOU 3709  CB  PRO B  42    13103  16004  10274   2497   -487   -145       C  
ATOM   3710  CG  PRO B  42      -4.841  -4.825  73.119  1.00108.78           C  
ANISOU 3710  CG  PRO B  42    13493  16957  10881   2319   -637   -338       C  
ATOM   3711  CD  PRO B  42      -3.585  -5.447  73.676  1.00107.23           C  
ANISOU 3711  CD  PRO B  42    13124  17129  10489   2571   -773   -341       C  
ATOM   3712  N   ARG B  43      -6.227  -9.105  72.996  1.00100.58           N  
ANISOU 3712  N   ARG B  43    12945  15326   9946   3131   -273    269       N  
ATOM   3713  CA  ARG B  43      -6.204 -10.181  71.984  1.00 99.17           C  
ANISOU 3713  CA  ARG B  43    12792  14978   9908   3235   -174    358       C  
ATOM   3714  C   ARG B  43      -7.427 -10.097  71.053  1.00 97.09           C  
ANISOU 3714  C   ARG B  43    12650  14357   9882   3003    -18    379       C  
ATOM   3715  O   ARG B  43      -8.547  -9.865  71.509  1.00 95.65           O  
ANISOU 3715  O   ARG B  43    12635  13980   9728   2914     70    429       O  
ATOM   3716  CB  ARG B  43      -5.992 -11.598  72.595  1.00101.48           C  
ANISOU 3716  CB  ARG B  43    13238  15241  10077   3618   -134    538       C  
ATOM   3717  CG  ARG B  43      -5.975 -12.793  71.602  1.00110.51           C  
ANISOU 3717  CG  ARG B  43    14452  16180  11358   3747    -21    629       C  
ATOM   3718  CD  ARG B  43      -4.913 -12.745  70.496  1.00118.02           C  
ANISOU 3718  CD  ARG B  43    15147  17317  12379   3729    -92    509       C  
ATOM   3719  NE  ARG B  43      -5.223 -13.681  69.407  1.00122.00           N  
ANISOU 3719  NE  ARG B  43    15751  17551  13051   3761     46    569       N  
ATOM   3720  CZ  ARG B  43      -5.073 -13.423  68.108  1.00132.56           C  
ANISOU 3720  CZ  ARG B  43    16953  18864  14551   3572     68    464       C  
ATOM   3721  NH1 ARG B  43      -4.599 -12.249  67.706  1.00119.43           N  
ANISOU 3721  NH1 ARG B  43    15049  17421  12908   3330    -31    303       N  
ATOM   3722  NH2 ARG B  43      -5.398 -14.337  67.202  1.00114.30           N  
ANISOU 3722  NH2 ARG B  43    14760  16299  12371   3614    195    519       N  
ATOM   3723  N   GLY B  44      -7.150 -10.254  69.755  1.00 90.18           N  
ANISOU 3723  N   GLY B  44    11669  13434   9162   2912      7    330       N  
ATOM   3724  CA  GLY B  44      -8.082 -10.169  68.637  1.00 86.63           C  
ANISOU 3724  CA  GLY B  44    11280  12703   8931   2691    124    324       C  
ATOM   3725  C   GLY B  44      -9.333 -11.015  68.682  1.00 87.05           C  
ANISOU 3725  C   GLY B  44    11579  12420   9074   2728    290    467       C  
ATOM   3726  O   GLY B  44      -9.439 -11.987  69.432  1.00 87.02           O  
ANISOU 3726  O   GLY B  44    11736  12350   8980   2959    347    602       O  
ATOM   3727  N   GLN B  45     -10.294 -10.608  67.857  1.00 81.18           N  
ANISOU 3727  N   GLN B  45    10864  11472   8507   2486    368    435       N  
ATOM   3728  CA  GLN B  45     -11.598 -11.235  67.649  1.00 79.76           C  
ANISOU 3728  CA  GLN B  45    10872  10982   8451   2434    527    534       C  
ATOM   3729  C   GLN B  45     -11.382 -12.493  66.824  1.00 81.19           C  
ANISOU 3729  C   GLN B  45    11113  11028   8709   2545    605    592       C  
ATOM   3730  O   GLN B  45     -12.142 -13.446  66.941  1.00 82.09           O  
ANISOU 3730  O   GLN B  45    11416  10908   8865   2600    737    704       O  
ATOM   3731  CB  GLN B  45     -12.506 -10.253  66.847  1.00 79.43           C  
ANISOU 3731  CB  GLN B  45    10783  10830   8568   2139    549    448       C  
ATOM   3732  CG  GLN B  45     -13.963 -10.712  66.604  1.00 99.26           C  
ANISOU 3732  CG  GLN B  45    13441  13061  11213   2043    701    524       C  
ATOM   3733  CD  GLN B  45     -14.475 -10.446  65.195  1.00109.88           C  
ANISOU 3733  CD  GLN B  45    14723  14288  12738   1832    724    456       C  
ATOM   3734  OE1 GLN B  45     -14.489  -9.305  64.699  1.00100.81           O  
ANISOU 3734  OE1 GLN B  45    13463  13207  11632   1665    651    356       O  
ATOM   3735  NE2 GLN B  45     -14.931 -11.504  64.529  1.00 96.63           N  
ANISOU 3735  NE2 GLN B  45    13132  12423  11159   1833    829    511       N  
ATOM   3736  N   TYR B  46     -10.350 -12.476  65.978  1.00 74.89           N  
ANISOU 3736  N   TYR B  46    10155  10375   7926   2564    530    507       N  
ATOM   3737  CA  TYR B  46     -10.053 -13.501  65.003  1.00 73.58           C  
ANISOU 3737  CA  TYR B  46    10017  10100   7838   2647    594    524       C  
ATOM   3738  C   TYR B  46      -9.307 -14.673  65.588  1.00 77.79           C  
ANISOU 3738  C   TYR B  46    10642  10665   8248   2986    606    623       C  
ATOM   3739  O   TYR B  46      -8.208 -14.527  66.138  1.00 79.18           O  
ANISOU 3739  O   TYR B  46    10691  11117   8277   3165    490    601       O  
ATOM   3740  CB  TYR B  46      -9.328 -12.885  63.793  1.00 73.47           C  
ANISOU 3740  CB  TYR B  46     9788  10236   7892   2505    522    383       C  
ATOM   3741  CG  TYR B  46      -9.980 -11.599  63.339  1.00 73.29           C  
ANISOU 3741  CG  TYR B  46     9689  10197   7959   2194    494    295       C  
ATOM   3742  CD1 TYR B  46      -9.684 -10.388  63.960  1.00 74.98           C  
ANISOU 3742  CD1 TYR B  46     9791  10604   8092   2100    386    225       C  
ATOM   3743  CD2 TYR B  46     -10.963 -11.603  62.356  1.00 73.39           C  
ANISOU 3743  CD2 TYR B  46     9765   9989   8130   2003    577    285       C  
ATOM   3744  CE1 TYR B  46     -10.336  -9.212  63.604  1.00 73.94           C  
ANISOU 3744  CE1 TYR B  46     9631  10423   8038   1838    370    155       C  
ATOM   3745  CE2 TYR B  46     -11.615 -10.428  61.981  1.00 73.32           C  
ANISOU 3745  CE2 TYR B  46     9706   9959   8194   1752    549    219       C  
ATOM   3746  CZ  TYR B  46     -11.292  -9.233  62.606  1.00 82.46           C  
ANISOU 3746  CZ  TYR B  46    10772  11288   9273   1678    449    158       C  
ATOM   3747  OH  TYR B  46     -11.920  -8.066  62.259  1.00 87.36           O  
ANISOU 3747  OH  TYR B  46    11371  11863   9958   1454    426     98       O  
ATOM   3748  N   SER B  47      -9.940 -15.853  65.468  1.00 72.55           N  
ANISOU 3748  N   SER B  47    10209   9712   7642   3071    749    732       N  
ATOM   3749  CA  SER B  47      -9.398 -17.134  65.904  1.00 73.54           C  
ANISOU 3749  CA  SER B  47    10494   9779   7671   3402    795    848       C  
ATOM   3750  C   SER B  47      -8.289 -17.532  64.948  1.00 78.35           C  
ANISOU 3750  C   SER B  47    10971  10505   8294   3534    752    770       C  
ATOM   3751  O   SER B  47      -8.284 -17.085  63.794  1.00 76.88           O  
ANISOU 3751  O   SER B  47    10647  10333   8230   3327    745    650       O  
ATOM   3752  CB  SER B  47     -10.491 -18.203  65.891  1.00 75.54           C  
ANISOU 3752  CB  SER B  47    11048   9648   8007   3387    979    969       C  
ATOM   3753  OG  SER B  47     -10.878 -18.561  64.575  1.00 78.44           O  
ANISOU 3753  OG  SER B  47    11434   9825   8546   3224   1060    902       O  
ATOM   3754  N   ALA B  48      -7.379 -18.405  65.410  1.00 76.82           N  
ANISOU 3754  N   ALA B  48    10829  10390   7967   3891    732    842       N  
ATOM   3755  CA  ALA B  48      -6.252 -18.950  64.648  1.00 77.47           C  
ANISOU 3755  CA  ALA B  48    10800  10599   8037   4096    702    782       C  
ATOM   3756  C   ALA B  48      -6.634 -19.286  63.180  1.00 79.48           C  
ANISOU 3756  C   ALA B  48    11087  10636   8474   3918    807    703       C  
ATOM   3757  O   ALA B  48      -5.905 -18.908  62.256  1.00 78.38           O  
ANISOU 3757  O   ALA B  48    10724  10688   8369   3864    753    572       O  
ATOM   3758  CB  ALA B  48      -5.710 -20.180  65.360  1.00 81.10           C  
ANISOU 3758  CB  ALA B  48    11450  11007   8358   4521    732    922       C  
ATOM   3759  N   GLY B  49      -7.800 -19.923  62.999  1.00 74.72           N  
ANISOU 3759  N   GLY B  49    10752   9657   7981   3801    956    774       N  
ATOM   3760  CA  GLY B  49      -8.359 -20.270  61.697  1.00 73.04           C  
ANISOU 3760  CA  GLY B  49    10605   9214   7935   3605   1059    701       C  
ATOM   3761  C   GLY B  49      -8.674 -19.040  60.869  1.00 74.48           C  
ANISOU 3761  C   GLY B  49    10561   9519   8219   3255    996    565       C  
ATOM   3762  O   GLY B  49      -8.157 -18.900  59.758  1.00 73.21           O  
ANISOU 3762  O   GLY B  49    10259   9449   8108   3195    977    449       O  
ATOM   3763  N   ALA B  50      -9.486 -18.110  61.429  1.00 70.29           N  
ANISOU 3763  N   ALA B  50     9997   9002   7706   3037    964    579       N  
ATOM   3764  CA  ALA B  50      -9.869 -16.858  60.758  1.00 68.09           C  
ANISOU 3764  CA  ALA B  50     9535   8821   7515   2717    903    466       C  
ATOM   3765  C   ALA B  50      -8.625 -16.103  60.272  1.00 73.21           C  
ANISOU 3765  C   ALA B  50     9909   9797   8109   2727    780    348       C  
ATOM   3766  O   ALA B  50      -8.517 -15.837  59.077  1.00 72.62           O  
ANISOU 3766  O   ALA B  50     9737   9741   8115   2571    783    249       O  
ATOM   3767  CB  ALA B  50     -10.711 -15.981  61.681  1.00 67.44           C  
ANISOU 3767  CB  ALA B  50     9460   8744   7420   2569    876    506       C  
ATOM   3768  N   VAL B  51      -7.648 -15.861  61.169  1.00 70.35           N  
ANISOU 3768  N   VAL B  51     9427   9701   7600   2918    679    359       N  
ATOM   3769  CA  VAL B  51      -6.383 -15.190  60.853  1.00 69.75           C  
ANISOU 3769  CA  VAL B  51     9071   9975   7455   2932    563    246       C  
ATOM   3770  C   VAL B  51      -5.760 -15.809  59.585  1.00 73.86           C  
ANISOU 3770  C   VAL B  51     9533  10505   8027   2991    613    175       C  
ATOM   3771  O   VAL B  51      -5.447 -15.080  58.644  1.00 72.84           O  
ANISOU 3771  O   VAL B  51     9227  10505   7943   2790    584     61       O  
ATOM   3772  CB  VAL B  51      -5.401 -15.227  62.061  1.00 74.83           C  
ANISOU 3772  CB  VAL B  51     9620  10894   7916   3202    457    281       C  
ATOM   3773  CG1 VAL B  51      -4.054 -14.599  61.703  1.00 75.38           C  
ANISOU 3773  CG1 VAL B  51     9373  11354   7915   3206    343    150       C  
ATOM   3774  CG2 VAL B  51      -6.001 -14.557  63.299  1.00 73.65           C  
ANISOU 3774  CG2 VAL B  51     9532  10750   7700   3133    408    336       C  
ATOM   3775  N   ALA B  52      -5.646 -17.151  59.550  1.00 71.22           N  
ANISOU 3775  N   ALA B  52     9371  10007   7683   3258    701    244       N  
ATOM   3776  CA  ALA B  52      -5.079 -17.900  58.428  1.00 71.31           C  
ANISOU 3776  CA  ALA B  52     9367   9997   7731   3363    766    180       C  
ATOM   3777  C   ALA B  52      -5.880 -17.734  57.135  1.00 73.01           C  
ANISOU 3777  C   ALA B  52     9633  10013   8094   3064    843    106       C  
ATOM   3778  O   ALA B  52      -5.291 -17.432  56.100  1.00 73.01           O  
ANISOU 3778  O   ALA B  52     9467  10162   8111   2982    833     -6       O  
ATOM   3779  CB  ALA B  52      -4.943 -19.370  58.792  1.00 74.23           C  
ANISOU 3779  CB  ALA B  52     9973  10174   8058   3715    853    282       C  
ATOM   3780  N   GLY B  53      -7.203 -17.887  57.215  1.00 67.51           N  
ANISOU 3780  N   GLY B  53     9147   9010   7491   2899    915    167       N  
ATOM   3781  CA  GLY B  53      -8.109 -17.743  56.079  1.00 65.14           C  
ANISOU 3781  CA  GLY B  53     8903   8522   7323   2615    976    104       C  
ATOM   3782  C   GLY B  53      -8.101 -16.343  55.498  1.00 66.92           C  
ANISOU 3782  C   GLY B  53     8912   8938   7574   2333    890     12       C  
ATOM   3783  O   GLY B  53      -8.006 -16.176  54.277  1.00 65.73           O  
ANISOU 3783  O   GLY B  53     8696   8806   7471   2195    907    -81       O  
ATOM   3784  N   LEU B  54      -8.166 -15.324  56.388  1.00 62.29           N  
ANISOU 3784  N   LEU B  54     8229   8493   6945   2255    799     37       N  
ATOM   3785  CA  LEU B  54      -8.142 -13.905  56.028  1.00 59.91           C  
ANISOU 3785  CA  LEU B  54     7752   8356   6655   1995    715    -40       C  
ATOM   3786  C   LEU B  54      -6.801 -13.493  55.447  1.00 62.58           C  
ANISOU 3786  C   LEU B  54     7858   8993   6925   2011    659   -140       C  
ATOM   3787  O   LEU B  54      -6.762 -12.748  54.471  1.00 61.06           O  
ANISOU 3787  O   LEU B  54     7569   8861   6769   1790    647   -218       O  
ATOM   3788  CB  LEU B  54      -8.534 -13.001  57.211  1.00 59.41           C  
ANISOU 3788  CB  LEU B  54     7674   8345   6552   1930    642      5       C  
ATOM   3789  CG  LEU B  54      -9.992 -13.050  57.686  1.00 63.00           C  
ANISOU 3789  CG  LEU B  54     8315   8540   7082   1836    697     86       C  
ATOM   3790  CD1 LEU B  54     -10.202 -12.104  58.825  1.00 62.02           C  
ANISOU 3790  CD1 LEU B  54     8158   8506   6899   1794    625    111       C  
ATOM   3791  CD2 LEU B  54     -10.975 -12.716  56.557  1.00 66.01           C  
ANISOU 3791  CD2 LEU B  54     8731   8762   7588   1584    735     44       C  
ATOM   3792  N   ALA B  55      -5.706 -14.000  56.015  1.00 60.80           N  
ANISOU 3792  N   ALA B  55     7542   8963   6596   2277    630   -135       N  
ATOM   3793  CA  ALA B  55      -4.378 -13.697  55.495  1.00 62.50           C  
ANISOU 3793  CA  ALA B  55     7508   9499   6741   2308    586   -236       C  
ATOM   3794  C   ALA B  55      -4.202 -14.277  54.095  1.00 66.54           C  
ANISOU 3794  C   ALA B  55     8028   9950   7305   2297    677   -301       C  
ATOM   3795  O   ALA B  55      -3.536 -13.647  53.279  1.00 67.21           O  
ANISOU 3795  O   ALA B  55     7924  10240   7372   2157    662   -398       O  
ATOM   3796  CB  ALA B  55      -3.301 -14.234  56.427  1.00 65.81           C  
ANISOU 3796  CB  ALA B  55     7823  10149   7032   2635    533   -213       C  
ATOM   3797  N   ALA B  56      -4.816 -15.461  53.815  1.00 61.36           N  
ANISOU 3797  N   ALA B  56     7601   9006   6708   2427    778   -253       N  
ATOM   3798  CA  ALA B  56      -4.764 -16.146  52.519  1.00 60.03           C  
ANISOU 3798  CA  ALA B  56     7488   8737   6585   2429    874   -320       C  
ATOM   3799  C   ALA B  56      -5.566 -15.412  51.450  1.00 62.10           C  
ANISOU 3799  C   ALA B  56     7766   8899   6930   2085    887   -374       C  
ATOM   3800  O   ALA B  56      -5.083 -15.309  50.329  1.00 62.48           O  
ANISOU 3800  O   ALA B  56     7721   9051   6969   2010    918   -465       O  
ATOM   3801  CB  ALA B  56      -5.257 -17.573  52.654  1.00 61.41           C  
ANISOU 3801  CB  ALA B  56     7932   8608   6795   2644    974   -256       C  
ATOM   3802  N   VAL B  57      -6.780 -14.903  51.784  1.00 57.15           N  
ANISOU 3802  N   VAL B  57     7255   8084   6375   1888    866   -316       N  
ATOM   3803  CA  VAL B  57      -7.631 -14.149  50.846  1.00 55.37           C  
ANISOU 3803  CA  VAL B  57     7050   7769   6221   1582    863   -354       C  
ATOM   3804  C   VAL B  57      -7.057 -12.743  50.580  1.00 59.54           C  
ANISOU 3804  C   VAL B  57     7372   8547   6702   1388    783   -408       C  
ATOM   3805  O   VAL B  57      -7.108 -12.282  49.436  1.00 58.72           O  
ANISOU 3805  O   VAL B  57     7235   8467   6611   1203    796   -468       O  
ATOM   3806  CB  VAL B  57      -9.142 -14.110  51.200  1.00 57.42           C  
ANISOU 3806  CB  VAL B  57     7484   7760   6571   1452    873   -284       C  
ATOM   3807  CG1 VAL B  57      -9.778 -15.485  51.067  1.00 58.14           C  
ANISOU 3807  CG1 VAL B  57     7788   7583   6718   1557    975   -258       C  
ATOM   3808  CG2 VAL B  57      -9.396 -13.528  52.577  1.00 56.37           C  
ANISOU 3808  CG2 VAL B  57     7341   7658   6419   1473    811   -205       C  
ATOM   3809  N   VAL B  58      -6.483 -12.084  51.617  1.00 56.09           N  
ANISOU 3809  N   VAL B  58     6811   8297   6204   1426    705   -389       N  
ATOM   3810  CA  VAL B  58      -5.832 -10.777  51.447  1.00 56.23           C  
ANISOU 3810  CA  VAL B  58     6642   8552   6170   1232    637   -448       C  
ATOM   3811  C   VAL B  58      -4.499 -10.990  50.725  1.00 61.86           C  
ANISOU 3811  C   VAL B  58     7167   9526   6812   1297    664   -537       C  
ATOM   3812  O   VAL B  58      -4.123 -10.188  49.864  1.00 61.49           O  
ANISOU 3812  O   VAL B  58     7013   9606   6745   1087    666   -602       O  
ATOM   3813  CB  VAL B  58      -5.701  -9.951  52.763  1.00 60.12           C  
ANISOU 3813  CB  VAL B  58     7071   9155   6615   1217    543   -420       C  
ATOM   3814  CG1 VAL B  58      -4.894  -8.666  52.547  1.00 59.87           C  
ANISOU 3814  CG1 VAL B  58     6851   9370   6525   1004    483   -499       C  
ATOM   3815  CG2 VAL B  58      -7.078  -9.622  53.348  1.00 58.09           C  
ANISOU 3815  CG2 VAL B  58     6993   8649   6429   1131    530   -343       C  
ATOM   3816  N   GLY B  59      -3.845 -12.106  51.045  1.00 60.05           N  
ANISOU 3816  N   GLY B  59     6914   9360   6541   1594    696   -534       N  
ATOM   3817  CA  GLY B  59      -2.601 -12.539  50.424  1.00 62.02           C  
ANISOU 3817  CA  GLY B  59     6987   9857   6722   1727    736   -617       C  
ATOM   3818  C   GLY B  59      -2.792 -12.737  48.940  1.00 67.09           C  
ANISOU 3818  C   GLY B  59     7680  10412   7398   1605    826   -677       C  
ATOM   3819  O   GLY B  59      -2.060 -12.140  48.142  1.00 66.47           O  
ANISOU 3819  O   GLY B  59     7431  10554   7271   1464    841   -757       O  
ATOM   3820  N   PHE B  60      -3.836 -13.527  48.565  1.00 65.40           N  
ANISOU 3820  N   PHE B  60     7711   9876   7263   1632    887   -640       N  
ATOM   3821  CA  PHE B  60      -4.206 -13.774  47.165  1.00 66.61           C  
ANISOU 3821  CA  PHE B  60     7951   9913   7445   1510    964   -699       C  
ATOM   3822  C   PHE B  60      -4.515 -12.443  46.468  1.00 68.61           C  
ANISOU 3822  C   PHE B  60     8147  10221   7699   1169    926   -720       C  
ATOM   3823  O   PHE B  60      -3.899 -12.146  45.448  1.00 68.27           O  
ANISOU 3823  O   PHE B  60     8000  10338   7603   1069    967   -794       O  
ATOM   3824  CB  PHE B  60      -5.383 -14.780  47.026  1.00 68.76           C  
ANISOU 3824  CB  PHE B  60     8497   9827   7803   1560   1021   -661       C  
ATOM   3825  CG  PHE B  60      -5.886 -14.943  45.604  1.00 70.97           C  
ANISOU 3825  CG  PHE B  60     8870   9991   8103   1402   1081   -730       C  
ATOM   3826  CD1 PHE B  60      -5.291 -15.860  44.739  1.00 76.49           C  
ANISOU 3826  CD1 PHE B  60     9589  10710   8762   1543   1174   -816       C  
ATOM   3827  CD2 PHE B  60      -6.918 -14.140  45.114  1.00 71.93           C  
ANISOU 3827  CD2 PHE B  60     9055  10004   8272   1122   1041   -714       C  
ATOM   3828  CE1 PHE B  60      -5.718 -15.974  43.411  1.00 77.34           C  
ANISOU 3828  CE1 PHE B  60     9782  10734   8869   1390   1225   -891       C  
ATOM   3829  CE2 PHE B  60      -7.338 -14.247  43.786  1.00 75.09           C  
ANISOU 3829  CE2 PHE B  60     9530  10331   8668    980   1082   -780       C  
ATOM   3830  CZ  PHE B  60      -6.738 -15.166  42.944  1.00 75.22           C  
ANISOU 3830  CZ  PHE B  60     9569  10371   8638   1106   1173   -871       C  
ATOM   3831  N   LEU B  61      -5.441 -11.642  47.051  1.00 63.93           N  
ANISOU 3831  N   LEU B  61     7630   9501   7160   1008    855   -650       N  
ATOM   3832  CA  LEU B  61      -5.841 -10.324  46.561  1.00 62.98           C  
ANISOU 3832  CA  LEU B  61     7494   9393   7041    711    810   -649       C  
ATOM   3833  C   LEU B  61      -4.634  -9.409  46.300  1.00 66.11           C  
ANISOU 3833  C   LEU B  61     7676  10092   7349    591    798   -709       C  
ATOM   3834  O   LEU B  61      -4.591  -8.790  45.241  1.00 66.53           O  
ANISOU 3834  O   LEU B  61     7720  10184   7374    389    824   -741       O  
ATOM   3835  CB  LEU B  61      -6.858  -9.664  47.519  1.00 62.21           C  
ANISOU 3835  CB  LEU B  61     7492   9140   7004    630    734   -567       C  
ATOM   3836  CG  LEU B  61      -7.278  -8.189  47.275  1.00 66.70           C  
ANISOU 3836  CG  LEU B  61     8064   9706   7573    358    676   -553       C  
ATOM   3837  CD1 LEU B  61      -7.849  -7.971  45.854  1.00 66.83           C  
ANISOU 3837  CD1 LEU B  61     8166   9629   7596    190    706   -570       C  
ATOM   3838  CD2 LEU B  61      -8.267  -7.714  48.351  1.00 66.97           C  
ANISOU 3838  CD2 LEU B  61     8195   9586   7664    342    613   -480       C  
ATOM   3839  N   ILE B  62      -3.655  -9.346  47.228  1.00 61.26           N  
ANISOU 3839  N   ILE B  62     6891   9702   6684    708    763   -725       N  
ATOM   3840  CA  ILE B  62      -2.452  -8.524  47.036  1.00 60.92           C  
ANISOU 3840  CA  ILE B  62     6617   9977   6555    578    756   -796       C  
ATOM   3841  C   ILE B  62      -1.679  -8.993  45.786  1.00 65.88           C  
ANISOU 3841  C   ILE B  62     7147  10757   7128    596    857   -876       C  
ATOM   3842  O   ILE B  62      -1.283  -8.159  44.968  1.00 65.46           O  
ANISOU 3842  O   ILE B  62     7014  10832   7026    359    887   -919       O  
ATOM   3843  CB  ILE B  62      -1.556  -8.463  48.308  1.00 63.99           C  
ANISOU 3843  CB  ILE B  62     6821  10604   6888    717    687   -811       C  
ATOM   3844  CG1 ILE B  62      -2.272  -7.738  49.464  1.00 62.54           C  
ANISOU 3844  CG1 ILE B  62     6730  10295   6737    641    591   -747       C  
ATOM   3845  CG2 ILE B  62      -0.217  -7.788  47.993  1.00 65.51           C  
ANISOU 3845  CG2 ILE B  62     6739  11164   6987    584    696   -907       C  
ATOM   3846  CD1 ILE B  62      -1.559  -7.752  50.840  1.00 65.99           C  
ANISOU 3846  CD1 ILE B  62     7023  10941   7110    796    508   -755       C  
ATOM   3847  N   VAL B  63      -1.488 -10.325  45.644  1.00 63.73           N  
ANISOU 3847  N   VAL B  63     6900  10457   6858    878    916   -896       N  
ATOM   3848  CA  VAL B  63      -0.763 -10.927  44.518  1.00 65.27           C  
ANISOU 3848  CA  VAL B  63     7016  10789   6997    948   1022   -981       C  
ATOM   3849  C   VAL B  63      -1.539 -10.682  43.209  1.00 70.32           C  
ANISOU 3849  C   VAL B  63     7817  11251   7651    730   1075   -988       C  
ATOM   3850  O   VAL B  63      -0.923 -10.294  42.213  1.00 73.49           O  
ANISOU 3850  O   VAL B  63     8115  11829   7979    591   1140  -1052       O  
ATOM   3851  CB  VAL B  63      -0.354 -12.422  44.738  1.00 69.62           C  
ANISOU 3851  CB  VAL B  63     7579  11332   7541   1332   1076  -1004       C  
ATOM   3852  CG1 VAL B  63       0.437 -12.980  43.556  1.00 70.62           C  
ANISOU 3852  CG1 VAL B  63     7617  11616   7600   1410   1193  -1107       C  
ATOM   3853  CG2 VAL B  63       0.451 -12.591  46.017  1.00 70.74           C  
ANISOU 3853  CG2 VAL B  63     7551  11681   7645   1559   1010   -989       C  
ATOM   3854  N   PHE B  64      -2.873 -10.845  43.230  1.00 63.31           N  
ANISOU 3854  N   PHE B  64     7169  10040   6847    687   1044   -923       N  
ATOM   3855  CA  PHE B  64      -3.718 -10.618  42.072  1.00 62.14           C  
ANISOU 3855  CA  PHE B  64     7176   9727   6706    495   1070   -925       C  
ATOM   3856  C   PHE B  64      -3.588  -9.163  41.598  1.00 64.00           C  
ANISOU 3856  C   PHE B  64     7349  10076   6891    190   1044   -913       C  
ATOM   3857  O   PHE B  64      -3.346  -8.927  40.413  1.00 63.41           O  
ANISOU 3857  O   PHE B  64     7270  10077   6745     57   1107   -955       O  
ATOM   3858  CB  PHE B  64      -5.171 -10.977  42.406  1.00 63.24           C  
ANISOU 3858  CB  PHE B  64     7542   9539   6947    505   1024   -856       C  
ATOM   3859  CG  PHE B  64      -6.104 -10.990  41.215  1.00 65.72           C  
ANISOU 3859  CG  PHE B  64     8015   9689   7266    354   1042   -870       C  
ATOM   3860  CD1 PHE B  64      -6.239 -12.127  40.428  1.00 69.90           C  
ANISOU 3860  CD1 PHE B  64     8645  10127   7788    460   1118   -938       C  
ATOM   3861  CD2 PHE B  64      -6.881  -9.879  40.907  1.00 67.97           C  
ANISOU 3861  CD2 PHE B  64     8362   9907   7557    117    977   -817       C  
ATOM   3862  CE1 PHE B  64      -7.110 -12.140  39.331  1.00 70.68           C  
ANISOU 3862  CE1 PHE B  64     8883  10095   7875    314   1122   -962       C  
ATOM   3863  CE2 PHE B  64      -7.734  -9.885  39.797  1.00 70.56           C  
ANISOU 3863  CE2 PHE B  64     8825  10112   7871     -6    979   -829       C  
ATOM   3864  CZ  PHE B  64      -7.845 -11.018  39.020  1.00 69.12           C  
ANISOU 3864  CZ  PHE B  64     8724   9864   7675     85   1047   -905       C  
ATOM   3865  N   THR B  65      -3.694  -8.203  42.545  1.00 59.72           N  
ANISOU 3865  N   THR B  65     6771   9545   6374     86    959   -856       N  
ATOM   3866  CA  THR B  65      -3.607  -6.755  42.316  1.00 58.93           C  
ANISOU 3866  CA  THR B  65     6647   9510   6234   -202    930   -835       C  
ATOM   3867  C   THR B  65      -2.254  -6.391  41.752  1.00 67.29           C  
ANISOU 3867  C   THR B  65     7500  10880   7189   -303   1003   -911       C  
ATOM   3868  O   THR B  65      -2.188  -5.603  40.814  1.00 69.17           O  
ANISOU 3868  O   THR B  65     7767  11148   7365   -536   1042   -910       O  
ATOM   3869  CB  THR B  65      -3.897  -5.966  43.609  1.00 56.31           C  
ANISOU 3869  CB  THR B  65     6318   9127   5949   -249    831   -780       C  
ATOM   3870  OG1 THR B  65      -5.169  -6.358  44.135  1.00 48.76           O  
ANISOU 3870  OG1 THR B  65     5541   7899   5088   -148    778   -711       O  
ATOM   3871  CG2 THR B  65      -3.840  -4.449  43.410  1.00 50.58           C  
ANISOU 3871  CG2 THR B  65     5606   8426   5184   -548    805   -760       C  
ATOM   3872  N   VAL B  66      -1.177  -6.953  42.314  1.00 65.04           N  
ANISOU 3872  N   VAL B  66     7003  10835   6874   -127   1023   -973       N  
ATOM   3873  CA  VAL B  66       0.177  -6.665  41.844  1.00 66.39           C  
ANISOU 3873  CA  VAL B  66     6930  11351   6945   -211   1098  -1058       C  
ATOM   3874  C   VAL B  66       0.400  -7.188  40.411  1.00 70.68           C  
ANISOU 3874  C   VAL B  66     7491  11942   7423   -210   1221  -1111       C  
ATOM   3875  O   VAL B  66       0.688  -6.376  39.542  1.00 72.12           O  
ANISOU 3875  O   VAL B  66     7653  12218   7531   -465   1279  -1123       O  
ATOM   3876  CB  VAL B  66       1.266  -7.132  42.843  1.00 70.89           C  
ANISOU 3876  CB  VAL B  66     7243  12200   7491      1   1076  -1115       C  
ATOM   3877  CG1 VAL B  66       2.662  -7.083  42.214  1.00 72.76           C  
ANISOU 3877  CG1 VAL B  66     7200  12822   7622    -42   1173  -1219       C  
ATOM   3878  CG2 VAL B  66       1.212  -6.310  44.135  1.00 69.67           C  
ANISOU 3878  CG2 VAL B  66     7048  12059   7363    -84    959  -1080       C  
ATOM   3879  N   VAL B  67       0.223  -8.500  40.153  1.00 65.96           N  
ANISOU 3879  N   VAL B  67     6957  11259   6846     61   1264  -1141       N  
ATOM   3880  CA  VAL B  67       0.473  -9.060  38.821  1.00 66.50           C  
ANISOU 3880  CA  VAL B  67     7045  11380   6840     82   1384  -1210       C  
ATOM   3881  C   VAL B  67      -0.433  -8.412  37.767  1.00 68.65           C  
ANISOU 3881  C   VAL B  67     7528  11466   7090   -176   1391  -1166       C  
ATOM   3882  O   VAL B  67       0.073  -7.995  36.731  1.00 71.02           O  
ANISOU 3882  O   VAL B  67     7778  11920   7285   -339   1479  -1204       O  
ATOM   3883  CB  VAL B  67       0.487 -10.618  38.730  1.00 71.24           C  
ANISOU 3883  CB  VAL B  67     7700  11907   7462    427   1438  -1266       C  
ATOM   3884  CG1 VAL B  67       1.512 -11.219  39.688  1.00 72.64           C  
ANISOU 3884  CG1 VAL B  67     7658  12306   7635    708   1435  -1305       C  
ATOM   3885  CG2 VAL B  67      -0.887 -11.233  38.966  1.00 69.43           C  
ANISOU 3885  CG2 VAL B  67     7750  11295   7335    509   1378  -1204       C  
ATOM   3886  N   GLY B  68      -1.721  -8.274  38.064  1.00 60.81           N  
ANISOU 3886  N   GLY B  68     6752  10169   6183   -212   1297  -1083       N  
ATOM   3887  CA  GLY B  68      -2.681  -7.668  37.151  1.00 58.87           C  
ANISOU 3887  CA  GLY B  68     6706   9746   5915   -422   1280  -1032       C  
ATOM   3888  C   GLY B  68      -2.304  -6.259  36.732  1.00 63.60           C  
ANISOU 3888  C   GLY B  68     7268  10464   6432   -721   1292   -995       C  
ATOM   3889  O   GLY B  68      -2.263  -5.955  35.539  1.00 64.80           O  
ANISOU 3889  O   GLY B  68     7484  10655   6483   -868   1359  -1003       O  
ATOM   3890  N   ASN B  69      -2.031  -5.383  37.708  1.00 59.98           N  
ANISOU 3890  N   ASN B  69     6725  10055   6008   -820   1232   -956       N  
ATOM   3891  CA  ASN B  69      -1.672  -3.993  37.434  1.00 59.98           C  
ANISOU 3891  CA  ASN B  69     6715  10137   5939  -1123   1247   -920       C  
ATOM   3892  C   ASN B  69      -0.272  -3.873  36.849  1.00 65.55           C  
ANISOU 3892  C   ASN B  69     7202  11176   6528  -1225   1374  -1003       C  
ATOM   3893  O   ASN B  69      -0.024  -2.946  36.075  1.00 66.87           O  
ANISOU 3893  O   ASN B  69     7408  11398   6602  -1490   1436   -979       O  
ATOM   3894  CB  ASN B  69      -1.877  -3.103  38.656  1.00 58.93           C  
ANISOU 3894  CB  ASN B  69     6586   9929   5876  -1207   1145   -867       C  
ATOM   3895  CG  ASN B  69      -3.331  -2.839  38.964  1.00 67.33           C  
ANISOU 3895  CG  ASN B  69     7889  10666   7025  -1190   1039   -772       C  
ATOM   3896  OD1 ASN B  69      -4.009  -2.021  38.319  1.00 65.95           O  
ANISOU 3896  OD1 ASN B  69     7898  10341   6820  -1358   1022   -702       O  
ATOM   3897  ND2 ASN B  69      -3.838  -3.519  39.964  1.00 46.19           N  
ANISOU 3897  ND2 ASN B  69     5216   7883   4450   -979    968   -764       N  
ATOM   3898  N   VAL B  70       0.629  -4.836  37.168  1.00 61.85           N  
ANISOU 3898  N   VAL B  70     6509  10932   6057  -1006   1422  -1097       N  
ATOM   3899  CA  VAL B  70       1.974  -4.873  36.588  1.00 63.62           C  
ANISOU 3899  CA  VAL B  70     6490  11512   6170  -1061   1554  -1191       C  
ATOM   3900  C   VAL B  70       1.819  -5.191  35.096  1.00 69.29           C  
ANISOU 3900  C   VAL B  70     7326  12212   6791  -1100   1665  -1210       C  
ATOM   3901  O   VAL B  70       2.525  -4.609  34.262  1.00 70.75           O  
ANISOU 3901  O   VAL B  70     7431  12594   6855  -1315   1778  -1235       O  
ATOM   3902  CB  VAL B  70       2.952  -5.807  37.345  1.00 67.27           C  
ANISOU 3902  CB  VAL B  70     6678  12233   6650   -780   1566  -1285       C  
ATOM   3903  CG1 VAL B  70       3.895  -6.552  36.402  1.00 69.11           C  
ANISOU 3903  CG1 VAL B  70     6744  12734   6782   -668   1717  -1392       C  
ATOM   3904  CG2 VAL B  70       3.736  -5.022  38.384  1.00 67.49           C  
ANISOU 3904  CG2 VAL B  70     6481  12480   6683   -900   1514  -1303       C  
ATOM   3905  N   LEU B  71       0.815  -6.031  34.773  1.00 65.09           N  
ANISOU 3905  N   LEU B  71     7002  11426   6303   -923   1629  -1194       N  
ATOM   3906  CA  LEU B  71       0.470  -6.396  33.404  1.00 66.10           C  
ANISOU 3906  CA  LEU B  71     7279  11498   6338   -945   1708  -1215       C  
ATOM   3907  C   LEU B  71      -0.076  -5.222  32.609  1.00 69.47           C  
ANISOU 3907  C   LEU B  71     7889  11820   6687  -1251   1702  -1123       C  
ATOM   3908  O   LEU B  71       0.167  -5.160  31.403  1.00 69.22           O  
ANISOU 3908  O   LEU B  71     7900  11882   6519  -1354   1807  -1147       O  
ATOM   3909  CB  LEU B  71      -0.479  -7.592  33.364  1.00 65.19           C  
ANISOU 3909  CB  LEU B  71     7335  11138   6295   -697   1660  -1234       C  
ATOM   3910  CG  LEU B  71       0.207  -8.951  33.477  1.00 71.30           C  
ANISOU 3910  CG  LEU B  71     7983  12031   7077   -388   1736  -1349       C  
ATOM   3911  CD1 LEU B  71      -0.743  -9.988  34.038  1.00 70.08           C  
ANISOU 3911  CD1 LEU B  71     7992  11591   7043   -154   1658  -1342       C  
ATOM   3912  CD2 LEU B  71       0.759  -9.403  32.132  1.00 74.82           C  
ANISOU 3912  CD2 LEU B  71     8414  12635   7380   -380   1884  -1447       C  
ATOM   3913  N   VAL B  72      -0.773  -4.275  33.288  1.00 65.46           N  
ANISOU 3913  N   VAL B  72     7495  11125   6253  -1385   1585  -1017       N  
ATOM   3914  CA  VAL B  72      -1.301  -3.045  32.670  1.00 65.34           C  
ANISOU 3914  CA  VAL B  72     7675  10985   6167  -1659   1569   -912       C  
ATOM   3915  C   VAL B  72      -0.114  -2.152  32.288  1.00 71.49           C  
ANISOU 3915  C   VAL B  72     8319  12018   6827  -1920   1693   -926       C  
ATOM   3916  O   VAL B  72      -0.064  -1.650  31.165  1.00 71.00           O  
ANISOU 3916  O   VAL B  72     8368  11980   6627  -2102   1776   -890       O  
ATOM   3917  CB  VAL B  72      -2.333  -2.308  33.571  1.00 66.81           C  
ANISOU 3917  CB  VAL B  72     8016  10903   6467  -1698   1418   -806       C  
ATOM   3918  CG1 VAL B  72      -2.602  -0.887  33.082  1.00 67.15           C  
ANISOU 3918  CG1 VAL B  72     8236  10848   6429  -1980   1414   -698       C  
ATOM   3919  CG2 VAL B  72      -3.634  -3.091  33.673  1.00 64.50           C  
ANISOU 3919  CG2 VAL B  72     7879  10363   6265  -1495   1313   -784       C  
ATOM   3920  N   VAL B  73       0.853  -2.000  33.218  1.00 70.27           N  
ANISOU 3920  N   VAL B  73     7916  12067   6716  -1937   1708   -981       N  
ATOM   3921  CA  VAL B  73       2.076  -1.210  33.031  1.00 73.31           C  
ANISOU 3921  CA  VAL B  73     8119  12733   7004  -2197   1828  -1017       C  
ATOM   3922  C   VAL B  73       2.790  -1.640  31.735  1.00 79.28           C  
ANISOU 3922  C   VAL B  73     8795  13722   7608  -2225   2000  -1083       C  
ATOM   3923  O   VAL B  73       2.985  -0.813  30.844  1.00 81.38           O  
ANISOU 3923  O   VAL B  73     9154  14021   7745  -2498   2097  -1035       O  
ATOM   3924  CB  VAL B  73       3.002  -1.294  34.281  1.00 78.28           C  
ANISOU 3924  CB  VAL B  73     8447  13591   7706  -2141   1800  -1098       C  
ATOM   3925  CG1 VAL B  73       4.376  -0.680  34.009  1.00 81.21           C  
ANISOU 3925  CG1 VAL B  73     8568  14320   7969  -2399   1940  -1168       C  
ATOM   3926  CG2 VAL B  73       2.354  -0.648  35.499  1.00 76.09           C  
ANISOU 3926  CG2 VAL B  73     8268  13094   7547  -2173   1646  -1032       C  
ATOM   3927  N   ILE B  74       3.118  -2.944  31.628  1.00 74.72           N  
ANISOU 3927  N   ILE B  74     8072  13279   7038  -1933   2040  -1188       N  
ATOM   3928  CA  ILE B  74       3.782  -3.593  30.489  1.00 75.43           C  
ANISOU 3928  CA  ILE B  74     8073  13595   6993  -1880   2203  -1278       C  
ATOM   3929  C   ILE B  74       2.961  -3.423  29.205  1.00 79.57           C  
ANISOU 3929  C   ILE B  74     8895  13932   7405  -1982   2233  -1212       C  
ATOM   3930  O   ILE B  74       3.552  -3.186  28.160  1.00 82.53           O  
ANISOU 3930  O   ILE B  74     9246  14491   7619  -2136   2385  -1234       O  
ATOM   3931  CB  ILE B  74       4.065  -5.094  30.816  1.00 77.89           C  
ANISOU 3931  CB  ILE B  74     8233  13999   7365  -1487   2208  -1396       C  
ATOM   3932  CG1 ILE B  74       5.071  -5.239  31.977  1.00 78.82           C  
ANISOU 3932  CG1 ILE B  74     8020  14377   7552  -1378   2193  -1465       C  
ATOM   3933  CG2 ILE B  74       4.526  -5.892  29.591  1.00 79.81           C  
ANISOU 3933  CG2 ILE B  74     8445  14408   7471  -1383   2367  -1495       C  
ATOM   3934  CD1 ILE B  74       4.956  -6.554  32.779  1.00 80.10           C  
ANISOU 3934  CD1 ILE B  74     8123  14486   7824   -964   2120  -1522       C  
ATOM   3935  N   ALA B  75       1.614  -3.536  29.279  1.00 73.12           N  
ANISOU 3935  N   ALA B  75     8348  12772   6662  -1897   2090  -1132       N  
ATOM   3936  CA  ALA B  75       0.724  -3.407  28.118  1.00 72.31           C  
ANISOU 3936  CA  ALA B  75     8528  12496   6452  -1967   2085  -1070       C  
ATOM   3937  C   ALA B  75       0.815  -2.038  27.434  1.00 78.10           C  
ANISOU 3937  C   ALA B  75     9395  13233   7049  -2308   2143   -959       C  
ATOM   3938  O   ALA B  75       1.066  -1.994  26.232  1.00 80.14           O  
ANISOU 3938  O   ALA B  75     9720  13598   7131  -2406   2264   -965       O  
ATOM   3939  CB  ALA B  75      -0.708  -3.725  28.502  1.00 70.42           C  
ANISOU 3939  CB  ALA B  75     8501  11922   6331  -1820   1908  -1012       C  
ATOM   3940  N   VAL B  76       0.687  -0.935  28.198  1.00 74.14           N  
ANISOU 3940  N   VAL B  76     8934  12619   6615  -2488   2072   -862       N  
ATOM   3941  CA  VAL B  76       0.784   0.444  27.693  1.00 75.33           C  
ANISOU 3941  CA  VAL B  76     9241  12731   6649  -2820   2128   -745       C  
ATOM   3942  C   VAL B  76       2.218   0.785  27.217  1.00 85.70           C  
ANISOU 3942  C   VAL B  76    10348  14385   7830  -3046   2335   -806       C  
ATOM   3943  O   VAL B  76       2.390   1.532  26.237  1.00 88.20           O  
ANISOU 3943  O   VAL B  76    10811  14724   7978  -3291   2446   -732       O  
ATOM   3944  CB  VAL B  76       0.243   1.459  28.738  1.00 76.63           C  
ANISOU 3944  CB  VAL B  76     9518  12661   6937  -2925   1995   -644       C  
ATOM   3945  CG1 VAL B  76       0.581   2.901  28.372  1.00 77.90           C  
ANISOU 3945  CG1 VAL B  76     9820  12792   6985  -3284   2076   -540       C  
ATOM   3946  CG2 VAL B  76      -1.257   1.296  28.936  1.00 73.73           C  
ANISOU 3946  CG2 VAL B  76     9387  11967   6659  -2743   1814   -564       C  
ATOM   3947  N   LEU B  77       3.237   0.213  27.893  1.00 84.16           N  
ANISOU 3947  N   LEU B  77     9812  14464   7701  -2956   2388   -937       N  
ATOM   3948  CA  LEU B  77       4.647   0.467  27.568  1.00 87.61           C  
ANISOU 3948  CA  LEU B  77     9987  15274   8028  -3156   2582  -1016       C  
ATOM   3949  C   LEU B  77       5.259  -0.525  26.529  1.00 95.06           C  
ANISOU 3949  C   LEU B  77    10797  16485   8838  -3017   2742  -1128       C  
ATOM   3950  O   LEU B  77       6.486  -0.659  26.466  1.00 97.43           O  
ANISOU 3950  O   LEU B  77    10791  17149   9079  -3076   2892  -1233       O  
ATOM   3951  CB  LEU B  77       5.492   0.523  28.867  1.00 87.70           C  
ANISOU 3951  CB  LEU B  77     9675  15484   8162  -3156   2551  -1101       C  
ATOM   3952  CG  LEU B  77       5.162   1.641  29.882  1.00 90.42           C  
ANISOU 3952  CG  LEU B  77    10117  15629   8609  -3355   2431  -1017       C  
ATOM   3953  CD1 LEU B  77       5.824   1.373  31.192  1.00 90.30           C  
ANISOU 3953  CD1 LEU B  77     9790  15803   8718  -3256   2365  -1120       C  
ATOM   3954  CD2 LEU B  77       5.582   3.017  29.382  1.00 93.78           C  
ANISOU 3954  CD2 LEU B  77    10650  16068   8914  -3796   2550   -942       C  
ATOM   3955  N   THR B  78       4.414  -1.205  25.711  1.00 91.23           N  
ANISOU 3955  N   THR B  78    10532  15833   8297  -2836   2712  -1115       N  
ATOM   3956  CA  THR B  78       4.865  -2.175  24.703  1.00 93.13           C  
ANISOU 3956  CA  THR B  78    10696  16284   8406  -2686   2855  -1229       C  
ATOM   3957  C   THR B  78       3.952  -2.201  23.470  1.00 97.85           C  
ANISOU 3957  C   THR B  78    11627  16693   8857  -2704   2852  -1161       C  
ATOM   3958  O   THR B  78       4.459  -2.169  22.345  1.00100.25           O  
ANISOU 3958  O   THR B  78    11943  17185   8962  -2813   3023  -1187       O  
ATOM   3959  CB  THR B  78       5.063  -3.585  25.325  1.00102.43           C  
ANISOU 3959  CB  THR B  78    11670  17542   9709  -2296   2815  -1374       C  
ATOM   3960  OG1 THR B  78       6.028  -3.508  26.377  1.00100.30           O  
ANISOU 3960  OG1 THR B  78    11069  17504   9536  -2285   2826  -1436       O  
ATOM   3961  CG2 THR B  78       5.522  -4.636  24.304  1.00105.40           C  
ANISOU 3961  CG2 THR B  78    11984  18114   9950  -2113   2967  -1507       C  
ATOM   3962  N   SER B  79       2.622  -2.297  23.678  1.00 91.44           N  
ANISOU 3962  N   SER B  79    11072  15538   8135  -2588   2661  -1083       N  
ATOM   3963  CA  SER B  79       1.636  -2.363  22.597  1.00 90.50           C  
ANISOU 3963  CA  SER B  79    11260  15240   7884  -2579   2619  -1025       C  
ATOM   3964  C   SER B  79       1.494  -1.057  21.844  1.00 95.23           C  
ANISOU 3964  C   SER B  79    12083  15785   8316  -2892   2665   -867       C  
ATOM   3965  O   SER B  79       1.402   0.013  22.463  1.00 94.72           O  
ANISOU 3965  O   SER B  79    12074  15599   8317  -3078   2611   -750       O  
ATOM   3966  CB  SER B  79       0.286  -2.803  23.137  1.00 91.25           C  
ANISOU 3966  CB  SER B  79    11521  15015   8133  -2379   2398   -993       C  
ATOM   3967  OG  SER B  79       0.427  -4.065  23.763  1.00 99.06           O  
ANISOU 3967  OG  SER B  79    12339  16039   9260  -2092   2374  -1134       O  
ATOM   3968  N   ARG B  80       1.485  -1.152  20.496  1.00 92.70           N  
ANISOU 3968  N   ARG B  80    11907  15547   7767  -2946   2770   -866       N  
ATOM   3969  CA  ARG B  80       1.357  -0.011  19.585  1.00 93.71           C  
ANISOU 3969  CA  ARG B  80    12284  15631   7689  -3222   2833   -710       C  
ATOM   3970  C   ARG B  80      -0.068   0.544  19.608  1.00 95.00           C  
ANISOU 3970  C   ARG B  80    12771  15445   7879  -3200   2621   -554       C  
ATOM   3971  O   ARG B  80      -0.279   1.725  19.311  1.00 94.98           O  
ANISOU 3971  O   ARG B  80    12988  15325   7777  -3418   2624   -387       O  
ATOM   3972  CB  ARG B  80       1.775  -0.403  18.165  1.00 96.56           C  
ANISOU 3972  CB  ARG B  80    12696  16206   7788  -3250   3008   -767       C  
ATOM   3973  N   ALA B  81      -1.036  -0.312  19.991  1.00 89.31           N  
ANISOU 3973  N   ALA B  81    12076  14562   7296  -2933   2441   -611       N  
ATOM   3974  CA  ALA B  81      -2.454   0.019  20.139  1.00 87.23           C  
ANISOU 3974  CA  ALA B  81    12058  13996   7088  -2860   2221   -495       C  
ATOM   3975  C   ALA B  81      -2.679   0.901  21.379  1.00 89.71           C  
ANISOU 3975  C   ALA B  81    12368  14124   7595  -2928   2118   -391       C  
ATOM   3976  O   ALA B  81      -3.656   1.655  21.436  1.00 88.30           O  
ANISOU 3976  O   ALA B  81    12419  13710   7422  -2949   1978   -249       O  
ATOM   3977  CB  ALA B  81      -3.254  -1.258  20.263  1.00 86.12           C  
ANISOU 3977  CB  ALA B  81    11890  13782   7050  -2579   2092   -618       C  
ATOM   3978  N   LEU B  82      -1.755   0.809  22.360  1.00 86.28           N  
ANISOU 3978  N   LEU B  82    11668  13809   7305  -2954   2187   -469       N  
ATOM   3979  CA  LEU B  82      -1.783   1.575  23.612  1.00 85.12           C  
ANISOU 3979  CA  LEU B  82    11481  13527   7336  -3027   2107   -404       C  
ATOM   3980  C   LEU B  82      -0.623   2.618  23.703  1.00 93.76           C  
ANISOU 3980  C   LEU B  82    12500  14761   8363  -3340   2269   -364       C  
ATOM   3981  O   LEU B  82      -0.452   3.277  24.742  1.00 93.45           O  
ANISOU 3981  O   LEU B  82    12406  14644   8457  -3436   2227   -334       O  
ATOM   3982  CB  LEU B  82      -1.798   0.617  24.828  1.00 82.33           C  
ANISOU 3982  CB  LEU B  82    10891  13176   7213  -2790   2019   -526       C  
ATOM   3983  CG  LEU B  82      -2.809  -0.539  24.786  1.00 83.98           C  
ANISOU 3983  CG  LEU B  82    11147  13266   7497  -2505   1889   -589       C  
ATOM   3984  CD1 LEU B  82      -2.358  -1.680  25.650  1.00 83.31           C  
ANISOU 3984  CD1 LEU B  82    10806  13279   7570  -2292   1894   -735       C  
ATOM   3985  CD2 LEU B  82      -4.210  -0.087  25.156  1.00 82.31           C  
ANISOU 3985  CD2 LEU B  82    11149  12755   7371  -2449   1692   -473       C  
ATOM   3986  N   ARG B  83       0.130   2.803  22.588  1.00 92.74           N  
ANISOU 3986  N   ARG B  83    12386  14832   8018  -3517   2458   -363       N  
ATOM   3987  CA  ARG B  83       1.238   3.758  22.492  1.00 95.01           C  
ANISOU 3987  CA  ARG B  83    12611  15274   8213  -3852   2641   -329       C  
ATOM   3988  C   ARG B  83       0.774   5.229  22.445  1.00 97.69           C  
ANISOU 3988  C   ARG B  83    13274  15346   8498  -4098   2609   -133       C  
ATOM   3989  O   ARG B  83       1.615   6.127  22.378  1.00 99.27           O  
ANISOU 3989  O   ARG B  83    13469  15627   8621  -4414   2761    -91       O  
ATOM   3990  CB  ARG B  83       2.174   3.415  21.314  1.00101.23           C  
ANISOU 3990  CB  ARG B  83    13304  16376   8783  -3953   2868   -396       C  
ATOM   3991  CG  ARG B  83       3.654   3.761  21.563  1.00122.85           C  
ANISOU 3991  CG  ARG B  83    15751  19426  11501  -4205   3072   -472       C  
ATOM   3992  CD  ARG B  83       4.341   2.815  22.546  1.00142.37           C  
ANISOU 3992  CD  ARG B  83    17818  22125  14152  -4010   3058   -657       C  
ATOM   3993  NE  ARG B  83       5.242   3.524  23.460  1.00156.46           N  
ANISOU 3993  NE  ARG B  83    19383  24040  16023  -4244   3112   -683       N  
ATOM   3994  CZ  ARG B  83       4.905   3.944  24.677  1.00169.20           C  
ANISOU 3994  CZ  ARG B  83    20994  25472  17823  -4241   2956   -657       C  
ATOM   3995  NH1 ARG B  83       3.678   3.735  25.145  1.00152.59           N1+
ANISOU 3995  NH1 ARG B  83    19087  23046  15843  -4011   2745   -595       N1+
ATOM   3996  NH2 ARG B  83       5.789   4.578  25.435  1.00154.46           N  
ANISOU 3996  NH2 ARG B  83    18921  23755  16011  -4475   3013   -699       N  
ATOM   3997  N   ALA B  84      -0.552   5.478  22.510  1.00 92.14           N  
ANISOU 3997  N   ALA B  84    12848  14327   7835  -3955   2417    -17       N  
ATOM   3998  CA  ALA B  84      -1.116   6.828  22.581  1.00 92.77           C  
ANISOU 3998  CA  ALA B  84    13253  14114   7883  -4121   2362    169       C  
ATOM   3999  C   ALA B  84      -0.741   7.401  23.979  1.00 97.30           C  
ANISOU 3999  C   ALA B  84    13699  14615   8655  -4230   2329    141       C  
ATOM   4000  O   ALA B  84      -0.746   6.636  24.958  1.00 94.86           O  
ANISOU 4000  O   ALA B  84    13140  14365   8538  -4039   2237     17       O  
ATOM   4001  CB  ALA B  84      -2.625   6.784  22.400  1.00 91.73           C  
ANISOU 4001  CB  ALA B  84    13382  13709   7763  -3881   2151    270       C  
ATOM   4002  N   PRO B  85      -0.333   8.700  24.068  1.00 95.81           N  
ANISOU 4002  N   PRO B  85    13677  14315   8411  -4548   2418    244       N  
ATOM   4003  CA  PRO B  85       0.157   9.256  25.355  1.00 95.11           C  
ANISOU 4003  CA  PRO B  85    13456  14191   8490  -4693   2405    192       C  
ATOM   4004  C   PRO B  85      -0.789   9.178  26.555  1.00 95.97           C  
ANISOU 4004  C   PRO B  85    13585  14065   8815  -4455   2183    186       C  
ATOM   4005  O   PRO B  85      -0.342   8.888  27.668  1.00 94.01           O  
ANISOU 4005  O   PRO B  85    13074  13919   8727  -4427   2148     65       O  
ATOM   4006  CB  PRO B  85       0.488  10.707  25.007  1.00 99.87           C  
ANISOU 4006  CB  PRO B  85    14345  14638   8962  -5067   2530    330       C  
ATOM   4007  CG  PRO B  85       0.754  10.693  23.530  1.00106.70           C  
ANISOU 4007  CG  PRO B  85    15340  15623   9578  -5176   2689    403       C  
ATOM   4008  CD  PRO B  85      -0.217   9.694  22.981  1.00100.16           C  
ANISOU 4008  CD  PRO B  85    14545  14781   8729  -4808   2552    403       C  
ATOM   4009  N   GLN B  86      -2.090   9.419  26.323  1.00 91.25           N  
ANISOU 4009  N   GLN B  86    13287  13174   8210  -4276   2035    316       N  
ATOM   4010  CA  GLN B  86      -3.171   9.371  27.316  1.00 87.64           C  
ANISOU 4010  CA  GLN B  86    12884  12480   7935  -4031   1827    330       C  
ATOM   4011  C   GLN B  86      -3.205   8.078  28.147  1.00 86.37           C  
ANISOU 4011  C   GLN B  86    12389  12476   7953  -3770   1737    170       C  
ATOM   4012  O   GLN B  86      -3.713   8.087  29.264  1.00 84.63           O  
ANISOU 4012  O   GLN B  86    12134  12121   7902  -3639   1608    149       O  
ATOM   4013  CB  GLN B  86      -4.525   9.578  26.619  1.00 88.98           C  
ANISOU 4013  CB  GLN B  86    13374  12406   8028  -3847   1698    479       C  
ATOM   4014  CG  GLN B  86      -4.661   8.833  25.277  1.00114.01           C  
ANISOU 4014  CG  GLN B  86    16561  15732  11026  -3758   1737    485       C  
ATOM   4015  CD  GLN B  86      -6.082   8.729  24.779  1.00142.35           C  
ANISOU 4015  CD  GLN B  86    20371  19140  14574  -3510   1564    584       C  
ATOM   4016  OE1 GLN B  86      -6.900   9.658  24.902  1.00139.22           O  
ANISOU 4016  OE1 GLN B  86    20250  18475  14171  -3479   1467    726       O  
ATOM   4017  NE2 GLN B  86      -6.406   7.584  24.192  1.00137.58           N  
ANISOU 4017  NE2 GLN B  86    19649  18689  13936  -3322   1523    504       N  
ATOM   4018  N   ASN B  87      -2.684   6.970  27.600  1.00 81.24           N  
ANISOU 4018  N   ASN B  87    11513  12098   7256  -3684   1812     62       N  
ATOM   4019  CA  ASN B  87      -2.651   5.673  28.284  1.00 78.12           C  
ANISOU 4019  CA  ASN B  87    10826  11846   7010  -3428   1747    -85       C  
ATOM   4020  C   ASN B  87      -1.656   5.626  29.465  1.00 79.89           C  
ANISOU 4020  C   ASN B  87    10761  12234   7360  -3499   1783   -200       C  
ATOM   4021  O   ASN B  87      -1.835   4.816  30.368  1.00 76.02           O  
ANISOU 4021  O   ASN B  87    10094  11770   7022  -3275   1690   -285       O  
ATOM   4022  CB  ASN B  87      -2.390   4.544  27.291  1.00 75.64           C  
ANISOU 4022  CB  ASN B  87    10395  11749   6594  -3310   1824   -167       C  
ATOM   4023  CG  ASN B  87      -3.555   4.231  26.400  1.00 86.14           C  
ANISOU 4023  CG  ASN B  87    11952  12933   7845  -3150   1731    -97       C  
ATOM   4024  OD1 ASN B  87      -4.554   3.647  26.839  1.00 77.69           O  
ANISOU 4024  OD1 ASN B  87    10897  11726   6896  -2914   1576   -110       O  
ATOM   4025  ND2 ASN B  87      -3.441   4.592  25.122  1.00 72.36           N  
ANISOU 4025  ND2 ASN B  87    10377  11232   5885  -3282   1826    -26       N  
ATOM   4026  N   LEU B  88      -0.631   6.509  29.468  1.00 78.40           N  
ANISOU 4026  N   LEU B  88    10532  12156   7101  -3816   1917   -202       N  
ATOM   4027  CA  LEU B  88       0.369   6.600  30.542  1.00 78.26           C  
ANISOU 4027  CA  LEU B  88    10234  12323   7177  -3926   1949   -316       C  
ATOM   4028  C   LEU B  88      -0.293   6.824  31.907  1.00 78.19           C  
ANISOU 4028  C   LEU B  88    10258  12103   7345  -3804   1778   -312       C  
ATOM   4029  O   LEU B  88       0.277   6.429  32.931  1.00 77.80           O  
ANISOU 4029  O   LEU B  88     9942  12217   7401  -3746   1749   -427       O  
ATOM   4030  CB  LEU B  88       1.392   7.726  30.267  1.00 81.37           C  
ANISOU 4030  CB  LEU B  88    10643  12816   7457  -4342   2113   -300       C  
ATOM   4031  CG  LEU B  88       2.390   7.539  29.113  1.00 87.68           C  
ANISOU 4031  CG  LEU B  88    11320  13914   8081  -4517   2322   -336       C  
ATOM   4032  CD1 LEU B  88       2.909   8.883  28.632  1.00 90.58           C  
ANISOU 4032  CD1 LEU B  88    11874  14227   8314  -4944   2469   -249       C  
ATOM   4033  CD2 LEU B  88       3.567   6.664  29.526  1.00 89.52           C  
ANISOU 4033  CD2 LEU B  88    11100  14560   8353  -4465   2396   -519       C  
ATOM   4034  N   PHE B  89      -1.508   7.443  31.916  1.00 71.77           N  
ANISOU 4034  N   PHE B  89     9771  10942   6555  -3746   1665   -182       N  
ATOM   4035  CA  PHE B  89      -2.299   7.684  33.133  1.00 68.76           C  
ANISOU 4035  CA  PHE B  89     9458  10337   6330  -3609   1506   -168       C  
ATOM   4036  C   PHE B  89      -2.617   6.372  33.828  1.00 69.86           C  
ANISOU 4036  C   PHE B  89     9375  10566   6605  -3281   1406   -259       C  
ATOM   4037  O   PHE B  89      -2.454   6.280  35.037  1.00 69.31           O  
ANISOU 4037  O   PHE B  89     9163  10520   6652  -3221   1342   -326       O  
ATOM   4038  CB  PHE B  89      -3.593   8.451  32.831  1.00 69.55           C  
ANISOU 4038  CB  PHE B  89     9933  10080   6414  -3558   1412    -12       C  
ATOM   4039  CG  PHE B  89      -3.416   9.916  32.501  1.00 72.80           C  
ANISOU 4039  CG  PHE B  89    10626  10312   6722  -3860   1485     94       C  
ATOM   4040  CD1 PHE B  89      -2.999  10.822  33.476  1.00 76.47           C  
ANISOU 4040  CD1 PHE B  89    11117  10692   7246  -4053   1491     64       C  
ATOM   4041  CD2 PHE B  89      -3.738  10.404  31.240  1.00 75.10           C  
ANISOU 4041  CD2 PHE B  89    11189  10494   6852  -3941   1542    227       C  
ATOM   4042  CE1 PHE B  89      -2.840  12.176  33.171  1.00 79.74           C  
ANISOU 4042  CE1 PHE B  89    11825  10907   7565  -4344   1569    159       C  
ATOM   4043  CE2 PHE B  89      -3.591  11.758  30.937  1.00 80.41           C  
ANISOU 4043  CE2 PHE B  89    12159  10969   7423  -4213   1617    338       C  
ATOM   4044  CZ  PHE B  89      -3.141  12.636  31.903  1.00 80.01           C  
ANISOU 4044  CZ  PHE B  89    12139  10822   7441  -4419   1635    303       C  
ATOM   4045  N   LEU B  90      -2.998   5.342  33.046  1.00 65.77           N  
ANISOU 4045  N   LEU B  90     8828  10105   6055  -3083   1405   -268       N  
ATOM   4046  CA  LEU B  90      -3.305   3.982  33.510  1.00 63.40           C  
ANISOU 4046  CA  LEU B  90     8350   9874   5865  -2777   1334   -351       C  
ATOM   4047  C   LEU B  90      -2.063   3.241  34.036  1.00 69.84           C  
ANISOU 4047  C   LEU B  90     8825  11002   6710  -2745   1407   -492       C  
ATOM   4048  O   LEU B  90      -2.230   2.254  34.749  1.00 69.16           O  
ANISOU 4048  O   LEU B  90     8599  10948   6732  -2497   1341   -556       O  
ATOM   4049  CB  LEU B  90      -4.030   3.138  32.433  1.00 62.08           C  
ANISOU 4049  CB  LEU B  90     8273   9673   5640  -2610   1322   -333       C  
ATOM   4050  CG  LEU B  90      -4.931   3.859  31.427  1.00 65.60           C  
ANISOU 4050  CG  LEU B  90     9027   9921   5977  -2680   1292   -200       C  
ATOM   4051  CD1 LEU B  90      -5.238   2.962  30.257  1.00 65.43           C  
ANISOU 4051  CD1 LEU B  90     9031   9972   5859  -2566   1315   -223       C  
ATOM   4052  CD2 LEU B  90      -6.208   4.378  32.068  1.00 64.56           C  
ANISOU 4052  CD2 LEU B  90     9083   9502   5946  -2577   1135   -108       C  
ATOM   4053  N   VAL B  91      -0.833   3.714  33.704  1.00 69.45           N  
ANISOU 4053  N   VAL B  91     8642  11185   6561  -2991   1544   -538       N  
ATOM   4054  CA  VAL B  91       0.433   3.152  34.222  1.00 71.41           C  
ANISOU 4054  CA  VAL B  91     8537  11771   6823  -2976   1613   -675       C  
ATOM   4055  C   VAL B  91       0.658   3.743  35.616  1.00 75.56           C  
ANISOU 4055  C   VAL B  91     8980  12281   7447  -3044   1531   -703       C  
ATOM   4056  O   VAL B  91       1.025   3.013  36.541  1.00 74.72           O  
ANISOU 4056  O   VAL B  91     8643  12324   7422  -2857   1479   -791       O  
ATOM   4057  CB  VAL B  91       1.670   3.357  33.297  1.00 78.62           C  
ANISOU 4057  CB  VAL B  91     9300  12985   7586  -3211   1801   -728       C  
ATOM   4058  CG1 VAL B  91       2.952   2.831  33.952  1.00 79.49           C  
ANISOU 4058  CG1 VAL B  91     9017  13469   7718  -3176   1853   -875       C  
ATOM   4059  CG2 VAL B  91       1.460   2.698  31.937  1.00 78.67           C  
ANISOU 4059  CG2 VAL B  91     9388  13022   7481  -3122   1884   -714       C  
ATOM   4060  N   SER B  92       0.397   5.057  35.767  1.00 72.51           N  
ANISOU 4060  N   SER B  92     8806  11699   7046  -3296   1515   -626       N  
ATOM   4061  CA  SER B  92       0.477   5.750  37.047  1.00 72.29           C  
ANISOU 4061  CA  SER B  92     8761  11608   7100  -3382   1432   -652       C  
ATOM   4062  C   SER B  92      -0.639   5.294  38.019  1.00 75.13           C  
ANISOU 4062  C   SER B  92     9204  11746   7598  -3083   1268   -623       C  
ATOM   4063  O   SER B  92      -0.406   5.205  39.227  1.00 75.99           O  
ANISOU 4063  O   SER B  92     9170  11918   7782  -3016   1194   -689       O  
ATOM   4064  CB  SER B  92       0.391   7.244  36.822  1.00 77.85           C  
ANISOU 4064  CB  SER B  92     9726  12111   7742  -3717   1471   -572       C  
ATOM   4065  OG  SER B  92       0.503   7.887  38.077  1.00 90.32           O  
ANISOU 4065  OG  SER B  92    11288  13634   9394  -3803   1394   -618       O  
ATOM   4066  N   LEU B  93      -1.846   5.017  37.483  1.00 68.99           N  
ANISOU 4066  N   LEU B  93     8649  10724   6841  -2913   1213   -526       N  
ATOM   4067  CA  LEU B  93      -2.997   4.505  38.215  1.00 65.62           C  
ANISOU 4067  CA  LEU B  93     8302  10095   6535  -2636   1077   -493       C  
ATOM   4068  C   LEU B  93      -2.748   3.021  38.567  1.00 70.27           C  
ANISOU 4068  C   LEU B  93     8648  10867   7184  -2359   1065   -579       C  
ATOM   4069  O   LEU B  93      -3.223   2.570  39.605  1.00 69.18           O  
ANISOU 4069  O   LEU B  93     8477  10658   7151  -2163    970   -590       O  
ATOM   4070  CB  LEU B  93      -4.278   4.688  37.371  1.00 64.32           C  
ANISOU 4070  CB  LEU B  93     8423   9663   6354  -2572   1034   -373       C  
ATOM   4071  CG  LEU B  93      -5.647   4.400  38.025  1.00 66.34           C  
ANISOU 4071  CG  LEU B  93     8797   9682   6727  -2331    898   -322       C  
ATOM   4072  CD1 LEU B  93      -5.978   5.411  39.117  1.00 66.74           C  
ANISOU 4072  CD1 LEU B  93     8958   9560   6839  -2392    827   -295       C  
ATOM   4073  CD2 LEU B  93      -6.756   4.427  36.993  1.00 67.08           C  
ANISOU 4073  CD2 LEU B  93     9109   9598   6779  -2267    864   -225       C  
ATOM   4074  N   ALA B  94      -2.001   2.266  37.720  1.00 69.41           N  
ANISOU 4074  N   ALA B  94     8384  10986   7002  -2335   1167   -638       N  
ATOM   4075  CA  ALA B  94      -1.629   0.863  37.992  1.00 69.47           C  
ANISOU 4075  CA  ALA B  94     8174  11170   7052  -2067   1174   -726       C  
ATOM   4076  C   ALA B  94      -0.632   0.850  39.150  1.00 77.79           C  
ANISOU 4076  C   ALA B  94     8971  12450   8136  -2058   1159   -813       C  
ATOM   4077  O   ALA B  94      -0.757   0.018  40.052  1.00 77.79           O  
ANISOU 4077  O   ALA B  94     8876  12464   8217  -1807   1090   -843       O  
ATOM   4078  CB  ALA B  94      -0.987   0.232  36.772  1.00 71.10           C  
ANISOU 4078  CB  ALA B  94     8288  11572   7155  -2065   1302   -776       C  
ATOM   4079  N   SER B  95       0.328   1.820  39.132  1.00 76.20           N  
ANISOU 4079  N   SER B  95     8671  12420   7861  -2347   1222   -849       N  
ATOM   4080  CA  SER B  95       1.360   2.067  40.142  1.00 76.62           C  
ANISOU 4080  CA  SER B  95     8472  12723   7916  -2419   1207   -943       C  
ATOM   4081  C   SER B  95       0.719   2.413  41.484  1.00 78.40           C  
ANISOU 4081  C   SER B  95     8786  12766   8236  -2350   1066   -919       C  
ATOM   4082  O   SER B  95       1.190   1.944  42.520  1.00 77.89           O  
ANISOU 4082  O   SER B  95     8522  12870   8204  -2202   1007   -988       O  
ATOM   4083  CB  SER B  95       2.273   3.207  39.703  1.00 80.97           C  
ANISOU 4083  CB  SER B  95     8970  13428   8368  -2809   1307   -974       C  
ATOM   4084  OG  SER B  95       2.916   2.889  38.481  1.00 88.50           O  
ANISOU 4084  OG  SER B  95     9828  14579   9221  -2878   1451   -999       O  
ATOM   4085  N   ALA B  96      -0.369   3.214  41.458  1.00 72.69           N  
ANISOU 4085  N   ALA B  96     8366  11705   7547  -2435   1014   -819       N  
ATOM   4086  CA  ALA B  96      -1.110   3.597  42.655  1.00 70.49           C  
ANISOU 4086  CA  ALA B  96     8205  11225   7352  -2365    893   -792       C  
ATOM   4087  C   ALA B  96      -1.670   2.349  43.331  1.00 70.99           C  
ANISOU 4087  C   ALA B  96     8212  11260   7503  -2002    817   -789       C  
ATOM   4088  O   ALA B  96      -1.383   2.119  44.498  1.00 71.11           O  
ANISOU 4088  O   ALA B  96     8097  11374   7549  -1892    751   -839       O  
ATOM   4089  CB  ALA B  96      -2.232   4.556  42.293  1.00 70.35           C  
ANISOU 4089  CB  ALA B  96     8525  10858   7348  -2474    866   -681       C  
ATOM   4090  N   ASP B  97      -2.369   1.506  42.562  1.00 65.35           N  
ANISOU 4090  N   ASP B  97     7584  10434   6812  -1828    837   -738       N  
ATOM   4091  CA  ASP B  97      -2.993   0.266  42.997  1.00 63.96           C  
ANISOU 4091  CA  ASP B  97     7397  10190   6716  -1509    789   -727       C  
ATOM   4092  C   ASP B  97      -1.981  -0.828  43.416  1.00 68.77           C  
ANISOU 4092  C   ASP B  97     7737  11078   7313  -1314    814   -815       C  
ATOM   4093  O   ASP B  97      -2.325  -1.678  44.245  1.00 67.27           O  
ANISOU 4093  O   ASP B  97     7530  10843   7187  -1061    760   -808       O  
ATOM   4094  CB  ASP B  97      -3.973  -0.230  41.923  1.00 65.56           C  
ANISOU 4094  CB  ASP B  97     7773  10203   6932  -1433    810   -665       C  
ATOM   4095  CG  ASP B  97      -5.210   0.648  41.694  1.00 80.83           C  
ANISOU 4095  CG  ASP B  97     9972  11847   8893  -1527    754   -566       C  
ATOM   4096  OD1 ASP B  97      -5.732   1.228  42.685  1.00 80.55           O  
ANISOU 4096  OD1 ASP B  97    10013  11677   8915  -1523    677   -536       O  
ATOM   4097  OD2 ASP B  97      -5.680   0.723  40.530  1.00 90.45           O1-
ANISOU 4097  OD2 ASP B  97    11321  12979  10067  -1584    785   -522       O1-
ATOM   4098  N   ILE B  98      -0.737  -0.805  42.871  1.00 67.31           N  
ANISOU 4098  N   ILE B  98     7348  11188   7041  -1421    901   -893       N  
ATOM   4099  CA  ILE B  98       0.334  -1.749  43.272  1.00 67.83           C  
ANISOU 4099  CA  ILE B  98     7132  11559   7081  -1224    923   -983       C  
ATOM   4100  C   ILE B  98       0.811  -1.354  44.694  1.00 74.72           C  
ANISOU 4100  C   ILE B  98     7865  12564   7960  -1222    830  -1023       C  
ATOM   4101  O   ILE B  98       0.904  -2.211  45.578  1.00 75.72           O  
ANISOU 4101  O   ILE B  98     7900  12754   8115   -947    774  -1036       O  
ATOM   4102  CB  ILE B  98       1.520  -1.818  42.256  1.00 71.69           C  
ANISOU 4102  CB  ILE B  98     7417  12355   7468  -1335   1050  -1064       C  
ATOM   4103  CG1 ILE B  98       1.099  -2.492  40.932  1.00 71.32           C  
ANISOU 4103  CG1 ILE B  98     7492  12206   7401  -1264   1139  -1041       C  
ATOM   4104  CG2 ILE B  98       2.714  -2.556  42.860  1.00 72.08           C  
ANISOU 4104  CG2 ILE B  98     7141  12762   7483  -1144   1056  -1164       C  
ATOM   4105  CD1 ILE B  98       1.842  -1.972  39.682  1.00 72.60           C  
ANISOU 4105  CD1 ILE B  98     7588  12549   7448  -1514   1272  -1077       C  
ATOM   4106  N   LEU B  99       1.078  -0.043  44.901  1.00 71.37           N  
ANISOU 4106  N   LEU B  99     7451  12164   7502  -1533    815  -1040       N  
ATOM   4107  CA  LEU B  99       1.513   0.546  46.162  1.00 71.00           C  
ANISOU 4107  CA  LEU B  99     7297  12235   7446  -1601    727  -1093       C  
ATOM   4108  C   LEU B  99       0.482   0.317  47.261  1.00 73.98           C  
ANISOU 4108  C   LEU B  99     7838  12369   7901  -1396    616  -1029       C  
ATOM   4109  O   LEU B  99       0.874   0.063  48.395  1.00 74.02           O  
ANISOU 4109  O   LEU B  99     7706  12523   7895  -1263    538  -1073       O  
ATOM   4110  CB  LEU B  99       1.807   2.032  45.979  1.00 71.79           C  
ANISOU 4110  CB  LEU B  99     7454  12325   7498  -2006    750  -1118       C  
ATOM   4111  CG  LEU B  99       2.962   2.377  45.042  1.00 78.39           C  
ANISOU 4111  CG  LEU B  99     8100  13443   8242  -2259    871  -1191       C  
ATOM   4112  CD1 LEU B  99       2.923   3.835  44.620  1.00 79.16           C  
ANISOU 4112  CD1 LEU B  99     8371  13403   8302  -2670    918  -1174       C  
ATOM   4113  CD2 LEU B  99       4.286   2.013  45.643  1.00 82.77           C  
ANISOU 4113  CD2 LEU B  99     8275  14435   8739  -2216    859  -1319       C  
ATOM   4114  N   VAL B 100      -0.832   0.337  46.910  1.00 69.27           N  
ANISOU 4114  N   VAL B 100     7522  11421   7376  -1356    610   -927       N  
ATOM   4115  CA  VAL B 100      -1.952   0.061  47.831  1.00 67.30           C  
ANISOU 4115  CA  VAL B 100     7437  10927   7206  -1162    526   -858       C  
ATOM   4116  C   VAL B 100      -1.793  -1.380  48.326  1.00 68.84           C  
ANISOU 4116  C   VAL B 100     7512  11223   7420   -820    514   -862       C  
ATOM   4117  O   VAL B 100      -1.751  -1.622  49.530  1.00 69.07           O  
ANISOU 4117  O   VAL B 100     7494  11299   7452   -669    441   -868       O  
ATOM   4118  CB  VAL B 100      -3.361   0.252  47.179  1.00 69.96           C  
ANISOU 4118  CB  VAL B 100     8056  10914   7610  -1176    533   -756       C  
ATOM   4119  CG1 VAL B 100      -4.484   0.042  48.188  1.00 68.01           C  
ANISOU 4119  CG1 VAL B 100     7952  10449   7442   -999    457   -695       C  
ATOM   4120  CG2 VAL B 100      -3.508   1.608  46.516  1.00 70.67           C  
ANISOU 4120  CG2 VAL B 100     8293  10889   7669  -1482    556   -736       C  
ATOM   4121  N   ALA B 101      -1.699  -2.319  47.385  1.00 63.60           N  
ANISOU 4121  N   ALA B 101     6821  10585   6761   -697    589   -859       N  
ATOM   4122  CA  ALA B 101      -1.579  -3.735  47.672  1.00 63.43           C  
ANISOU 4122  CA  ALA B 101     6729  10614   6756   -369    599   -858       C  
ATOM   4123  C   ALA B 101      -0.355  -4.067  48.512  1.00 69.17           C  
ANISOU 4123  C   ALA B 101     7194  11672   7415   -234    566   -931       C  
ATOM   4124  O   ALA B 101      -0.439  -4.863  49.452  1.00 68.06           O  
ANISOU 4124  O   ALA B 101     7044  11529   7286     35    518   -906       O  
ATOM   4125  CB  ALA B 101      -1.562  -4.525  46.373  1.00 64.31           C  
ANISOU 4125  CB  ALA B 101     6859  10709   6866   -309    698   -866       C  
ATOM   4126  N   THR B 102       0.760  -3.405  48.215  1.00 68.31           N  
ANISOU 4126  N   THR B 102     6874  11853   7229   -429    589  -1019       N  
ATOM   4127  CA  THR B 102       2.042  -3.676  48.856  1.00 70.27           C  
ANISOU 4127  CA  THR B 102     6821  12482   7397   -319    559  -1107       C  
ATOM   4128  C   THR B 102       2.264  -2.930  50.188  1.00 75.14           C  
ANISOU 4128  C   THR B 102     7370  13201   7980   -395    441  -1138       C  
ATOM   4129  O   THR B 102       2.609  -3.588  51.169  1.00 74.52           O  
ANISOU 4129  O   THR B 102     7179  13267   7868   -134    371  -1146       O  
ATOM   4130  CB  THR B 102       3.202  -3.435  47.853  1.00 71.16           C  
ANISOU 4130  CB  THR B 102     6697  12906   7434   -489    653  -1202       C  
ATOM   4131  OG1 THR B 102       3.068  -2.148  47.235  1.00 67.61           O  
ANISOU 4131  OG1 THR B 102     6335  12379   6975   -886    690  -1207       O  
ATOM   4132  CG2 THR B 102       3.262  -4.502  46.771  1.00 65.04           C  
ANISOU 4132  CG2 THR B 102     5924  12124   6663   -302    762  -1199       C  
ATOM   4133  N   LEU B 103       2.079  -1.581  50.220  1.00 72.65           N  
ANISOU 4133  N   LEU B 103     7136  12808   7661   -740    421  -1155       N  
ATOM   4134  CA  LEU B 103       2.393  -0.710  51.371  1.00 73.38           C  
ANISOU 4134  CA  LEU B 103     7163  13011   7705   -876    319  -1215       C  
ATOM   4135  C   LEU B 103       1.270  -0.431  52.349  1.00 75.12           C  
ANISOU 4135  C   LEU B 103     7632  12936   7976   -817    237  -1144       C  
ATOM   4136  O   LEU B 103       1.579  -0.007  53.463  1.00 75.72           O  
ANISOU 4136  O   LEU B 103     7637  13135   7996   -839    144  -1198       O  
ATOM   4137  CB  LEU B 103       2.997   0.647  50.925  1.00 75.13           C  
ANISOU 4137  CB  LEU B 103     7326  13342   7880  -1308    353  -1298       C  
ATOM   4138  CG  LEU B 103       4.104   0.635  49.837  1.00 82.31           C  
ANISOU 4138  CG  LEU B 103     7995  14546   8731  -1462    460  -1374       C  
ATOM   4139  CD1 LEU B 103       4.400   2.033  49.364  1.00 83.97           C  
ANISOU 4139  CD1 LEU B 103     8246  14752   8908  -1917    511  -1424       C  
ATOM   4140  CD2 LEU B 103       5.396  -0.028  50.328  1.00 86.75           C  
ANISOU 4140  CD2 LEU B 103     8174  15576   9211  -1293    427  -1480       C  
ATOM   4141  N   VAL B 104      -0.014  -0.608  51.975  1.00 69.87           N  
ANISOU 4141  N   VAL B 104     7243  11903   7403   -754    269  -1034       N  
ATOM   4142  CA  VAL B 104      -1.072  -0.303  52.952  1.00 68.27           C  
ANISOU 4142  CA  VAL B 104     7252  11446   7242   -699    199   -974       C  
ATOM   4143  C   VAL B 104      -1.895  -1.546  53.298  1.00 69.80           C  
ANISOU 4143  C   VAL B 104     7551  11476   7493   -359    200   -877       C  
ATOM   4144  O   VAL B 104      -2.120  -1.804  54.474  1.00 68.93           O  
ANISOU 4144  O   VAL B 104     7464  11361   7365   -193    133   -857       O  
ATOM   4145  CB  VAL B 104      -1.974   0.940  52.632  1.00 71.18           C  
ANISOU 4145  CB  VAL B 104     7870  11520   7657   -962    209   -942       C  
ATOM   4146  CG1 VAL B 104      -1.142   2.190  52.381  1.00 72.87           C  
ANISOU 4146  CG1 VAL B 104     8014  11868   7807  -1315    217  -1037       C  
ATOM   4147  CG2 VAL B 104      -2.920   0.704  51.470  1.00 69.52           C  
ANISOU 4147  CG2 VAL B 104     7842  11048   7526   -955    282   -850       C  
ATOM   4148  N   MET B 105      -2.294  -2.322  52.299  1.00 66.04           N  
ANISOU 4148  N   MET B 105     7139  10878   7077   -267    279   -824       N  
ATOM   4149  CA  MET B 105      -3.137  -3.494  52.475  1.00 65.99           C  
ANISOU 4149  CA  MET B 105     7259  10681   7135      9    298   -736       C  
ATOM   4150  C   MET B 105      -2.622  -4.570  53.460  1.00 72.46           C  
ANISOU 4150  C   MET B 105     7971  11653   7906    323    265   -729       C  
ATOM   4151  O   MET B 105      -3.478  -5.105  54.170  1.00 72.38           O  
ANISOU 4151  O   MET B 105     8114  11453   7935    493    253   -649       O  
ATOM   4152  CB  MET B 105      -3.467  -4.126  51.131  1.00 68.25           C  
ANISOU 4152  CB  MET B 105     7610  10850   7474     22    390   -710       C  
ATOM   4153  CG  MET B 105      -4.605  -3.429  50.427  1.00 70.84           C  
ANISOU 4153  CG  MET B 105     8143  10903   7868   -166    408   -659       C  
ATOM   4154  SD  MET B 105      -5.094  -4.229  48.889  1.00 74.73           S  
ANISOU 4154  SD  MET B 105     8724  11263   8408   -141    500   -634       S  
ATOM   4155  CE  MET B 105      -5.476  -5.821  49.477  1.00 71.25           C  
ANISOU 4155  CE  MET B 105     8326  10731   8013    192    518   -593       C  
ATOM   4156  N   PRO B 106      -1.313  -4.935  53.571  1.00 71.08           N  
ANISOU 4156  N   PRO B 106     7551  11812   7645    424    250   -801       N  
ATOM   4157  CA  PRO B 106      -0.942  -5.953  54.572  1.00 71.25           C  
ANISOU 4157  CA  PRO B 106     7508  11951   7613    760    208   -774       C  
ATOM   4158  C   PRO B 106      -1.060  -5.393  55.996  1.00 75.59           C  
ANISOU 4158  C   PRO B 106     8074  12543   8104    765    101   -770       C  
ATOM   4159  O   PRO B 106      -1.447  -6.126  56.915  1.00 76.33           O  
ANISOU 4159  O   PRO B 106     8263  12557   8181   1017     76   -694       O  
ATOM   4160  CB  PRO B 106       0.514  -6.304  54.227  1.00 75.17           C  
ANISOU 4160  CB  PRO B 106     7712  12827   8024    845    214   -866       C  
ATOM   4161  CG  PRO B 106       0.827  -5.620  52.959  1.00 80.48           C  
ANISOU 4161  CG  PRO B 106     8311  13553   8715    557    283   -933       C  
ATOM   4162  CD  PRO B 106      -0.120  -4.467  52.833  1.00 74.85           C  
ANISOU 4162  CD  PRO B 106     7793  12586   8061    252    274   -906       C  
ATOM   4163  N   PHE B 107      -0.773  -4.081  56.163  1.00 69.99           N  
ANISOU 4163  N   PHE B 107     7297  11938   7359    474     48   -851       N  
ATOM   4164  CA  PHE B 107      -0.834  -3.390  57.442  1.00 68.93           C  
ANISOU 4164  CA  PHE B 107     7180  11854   7158    432    -53   -875       C  
ATOM   4165  C   PHE B 107      -2.243  -3.224  57.936  1.00 71.09           C  
ANISOU 4165  C   PHE B 107     7734  11777   7500    444    -45   -782       C  
ATOM   4166  O   PHE B 107      -2.464  -3.467  59.114  1.00 71.56           O  
ANISOU 4166  O   PHE B 107     7844  11841   7504    611   -102   -748       O  
ATOM   4167  CB  PHE B 107      -0.074  -2.068  57.394  1.00 71.46           C  
ANISOU 4167  CB  PHE B 107     7358  12375   7420     98    -99  -1004       C  
ATOM   4168  CG  PHE B 107       1.388  -2.303  57.110  1.00 74.88           C  
ANISOU 4168  CG  PHE B 107     7465  13220   7767    109   -113  -1105       C  
ATOM   4169  CD1 PHE B 107       2.239  -2.774  58.106  1.00 78.71           C  
ANISOU 4169  CD1 PHE B 107     7746  14026   8135    324   -210  -1149       C  
ATOM   4170  CD2 PHE B 107       1.901  -2.127  55.830  1.00 76.69           C  
ANISOU 4170  CD2 PHE B 107     7586  13530   8025    -70    -27  -1151       C  
ATOM   4171  CE1 PHE B 107       3.576  -3.050  57.831  1.00 81.50           C  
ANISOU 4171  CE1 PHE B 107     7772  14788   8408    365   -224  -1244       C  
ATOM   4172  CE2 PHE B 107       3.244  -2.395  55.557  1.00 81.49           C  
ANISOU 4172  CE2 PHE B 107     7870  14541   8552    -46    -27  -1248       C  
ATOM   4173  CZ  PHE B 107       4.072  -2.854  56.560  1.00 81.44           C  
ANISOU 4173  CZ  PHE B 107     7643  14863   8436    175   -127  -1296       C  
ATOM   4174  N   SER B 108      -3.214  -2.895  57.041  1.00 66.27           N  
ANISOU 4174  N   SER B 108     7302  10875   7001    293     27   -736       N  
ATOM   4175  CA  SER B 108      -4.652  -2.778  57.375  1.00 64.07           C  
ANISOU 4175  CA  SER B 108     7275  10268   6800    312     47   -647       C  
ATOM   4176  C   SER B 108      -5.144  -4.075  57.992  1.00 66.37           C  
ANISOU 4176  C   SER B 108     7644  10471   7103    623     70   -549       C  
ATOM   4177  O   SER B 108      -5.831  -4.034  59.009  1.00 64.53           O  
ANISOU 4177  O   SER B 108     7531  10131   6856    704     47   -500       O  
ATOM   4178  CB  SER B 108      -5.502  -2.468  56.140  1.00 65.86           C  
ANISOU 4178  CB  SER B 108     7639  10250   7137    152    119   -611       C  
ATOM   4179  OG  SER B 108      -5.362  -1.141  55.661  1.00 75.83           O  
ANISOU 4179  OG  SER B 108     8915  11503   8393   -142    106   -672       O  
ATOM   4180  N   LEU B 109      -4.777  -5.226  57.377  1.00 63.41           N  
ANISOU 4180  N   LEU B 109     7213  10135   6746    795    125   -521       N  
ATOM   4181  CA  LEU B 109      -5.166  -6.544  57.860  1.00 62.84           C  
ANISOU 4181  CA  LEU B 109     7238   9957   6683   1088    164   -426       C  
ATOM   4182  C   LEU B 109      -4.386  -6.952  59.106  1.00 68.97           C  
ANISOU 4182  C   LEU B 109     7920  10956   7330   1318     91   -422       C  
ATOM   4183  O   LEU B 109      -4.984  -7.476  60.050  1.00 70.04           O  
ANISOU 4183  O   LEU B 109     8195  10972   7445   1492     95   -334       O  
ATOM   4184  CB  LEU B 109      -5.040  -7.598  56.761  1.00 62.58           C  
ANISOU 4184  CB  LEU B 109     7205   9865   6707   1192    251   -409       C  
ATOM   4185  CG  LEU B 109      -5.417  -9.004  57.201  1.00 67.49           C  
ANISOU 4185  CG  LEU B 109     7959  10344   7340   1485    306   -311       C  
ATOM   4186  CD1 LEU B 109      -6.918  -9.154  57.406  1.00 65.84           C  
ANISOU 4186  CD1 LEU B 109     7983   9808   7224   1443    360   -223       C  
ATOM   4187  CD2 LEU B 109      -4.842 -10.037  56.283  1.00 71.91           C  
ANISOU 4187  CD2 LEU B 109     8475  10933   7913   1629    375   -328       C  
ATOM   4188  N   ALA B 110      -3.060  -6.734  59.108  1.00 65.65           N  
ANISOU 4188  N   ALA B 110     7260  10871   6814   1322     27   -515       N  
ATOM   4189  CA  ALA B 110      -2.207  -7.068  60.242  1.00 67.01           C  
ANISOU 4189  CA  ALA B 110     7305  11311   6843   1545    -63   -525       C  
ATOM   4190  C   ALA B 110      -2.717  -6.367  61.490  1.00 72.07           C  
ANISOU 4190  C   ALA B 110     8044  11916   7422   1494   -136   -514       C  
ATOM   4191  O   ALA B 110      -2.925  -7.020  62.506  1.00 72.43           O  
ANISOU 4191  O   ALA B 110     8179  11943   7397   1738   -156   -432       O  
ATOM   4192  CB  ALA B 110      -0.776  -6.649  59.960  1.00 69.45           C  
ANISOU 4192  CB  ALA B 110     7310  12013   7067   1472   -128   -655       C  
ATOM   4193  N   ASN B 111      -2.979  -5.050  61.385  1.00 69.24           N  
ANISOU 4193  N   ASN B 111     7696  11522   7089   1182   -163   -591       N  
ATOM   4194  CA  ASN B 111      -3.469  -4.200  62.470  1.00 69.73           C  
ANISOU 4194  CA  ASN B 111     7858  11541   7095   1095   -226   -608       C  
ATOM   4195  C   ASN B 111      -4.822  -4.686  63.019  1.00 74.47           C  
ANISOU 4195  C   ASN B 111     8716  11831   7747   1230   -162   -477       C  
ATOM   4196  O   ASN B 111      -5.004  -4.744  64.246  1.00 76.50           O  
ANISOU 4196  O   ASN B 111     9040  12121   7905   1360   -207   -446       O  
ATOM   4197  CB  ASN B 111      -3.509  -2.734  62.022  1.00 66.42           C  
ANISOU 4197  CB  ASN B 111     7432  11094   6711    731   -243   -715       C  
ATOM   4198  CG  ASN B 111      -4.073  -1.789  63.035  1.00 85.38           C  
ANISOU 4198  CG  ASN B 111     9963  13415   9063    629   -294   -746       C  
ATOM   4199  OD1 ASN B 111      -3.464  -1.491  64.075  1.00 76.40           O  
ANISOU 4199  OD1 ASN B 111     8742  12499   7787    658   -393   -816       O  
ATOM   4200  ND2 ASN B 111      -5.257  -1.292  62.735  1.00 79.44           N  
ANISOU 4200  ND2 ASN B 111     9416  12352   8417    516   -230   -701       N  
ATOM   4201  N   GLU B 112      -5.729  -5.093  62.105  1.00 68.15           N  
ANISOU 4201  N   GLU B 112     8048  10754   7092   1202    -55   -404       N  
ATOM   4202  CA  GLU B 112      -7.060  -5.618  62.403  1.00 66.18           C  
ANISOU 4202  CA  GLU B 112     8020  10211   6914   1295     27   -286       C  
ATOM   4203  C   GLU B 112      -6.982  -6.888  63.255  1.00 70.07           C  
ANISOU 4203  C   GLU B 112     8571  10720   7332   1611     46   -183       C  
ATOM   4204  O   GLU B 112      -7.457  -6.872  64.397  1.00 69.89           O  
ANISOU 4204  O   GLU B 112     8656  10660   7237   1701     36   -131       O  
ATOM   4205  CB  GLU B 112      -7.839  -5.890  61.095  1.00 65.92           C  
ANISOU 4205  CB  GLU B 112     8067   9938   7039   1194    126   -251       C  
ATOM   4206  CG  GLU B 112      -9.316  -6.197  61.284  1.00 73.98           C  
ANISOU 4206  CG  GLU B 112     9291  10669   8150   1215    208   -155       C  
ATOM   4207  CD  GLU B 112     -10.055  -5.178  62.126  1.00106.81           C  
ANISOU 4207  CD  GLU B 112    13534  14763  12286   1118    181   -166       C  
ATOM   4208  OE1 GLU B 112     -10.005  -3.971  61.787  1.00103.72           O  
ANISOU 4208  OE1 GLU B 112    13112  14389  11908    911    136   -248       O  
ATOM   4209  OE2 GLU B 112     -10.665  -5.586  63.141  1.00111.41           O1-
ANISOU 4209  OE2 GLU B 112    14226  15274  12831   1255    212    -92       O1-
ATOM   4210  N   LEU B 113      -6.375  -7.970  62.697  1.00 66.12           N  
ANISOU 4210  N   LEU B 113     8014  10269   6840   1784     81   -153       N  
ATOM   4211  CA  LEU B 113      -6.226  -9.281  63.343  1.00 67.03           C  
ANISOU 4211  CA  LEU B 113     8210  10372   6886   2107    111    -45       C  
ATOM   4212  C   LEU B 113      -5.536  -9.206  64.705  1.00 74.78           C  
ANISOU 4212  C   LEU B 113     9131  11600   7683   2285      5    -41       C  
ATOM   4213  O   LEU B 113      -5.982  -9.867  65.646  1.00 75.23           O  
ANISOU 4213  O   LEU B 113     9349  11561   7673   2483     34     72       O  
ATOM   4214  CB  LEU B 113      -5.489 -10.294  62.434  1.00 67.37           C  
ANISOU 4214  CB  LEU B 113     8180  10460   6956   2262    153    -43       C  
ATOM   4215  CG  LEU B 113      -6.025 -10.540  61.024  1.00 69.36           C  
ANISOU 4215  CG  LEU B 113     8487  10499   7368   2119    255    -55       C  
ATOM   4216  CD1 LEU B 113      -4.990 -11.209  60.198  1.00 70.84           C  
ANISOU 4216  CD1 LEU B 113     8542  10831   7543   2248    268   -101       C  
ATOM   4217  CD2 LEU B 113      -7.268 -11.397  61.029  1.00 68.49           C  
ANISOU 4217  CD2 LEU B 113     8630  10044   7350   2171    372     59       C  
ATOM   4218  N   MET B 114      -4.465  -8.388  64.804  1.00 74.06           N  
ANISOU 4218  N   MET B 114     8810  11829   7499   2198   -116   -168       N  
ATOM   4219  CA  MET B 114      -3.651  -8.192  66.009  1.00 76.73           C  
ANISOU 4219  CA  MET B 114     9040  12468   7645   2336   -244   -200       C  
ATOM   4220  C   MET B 114      -4.341  -7.428  67.132  1.00 81.70           C  
ANISOU 4220  C   MET B 114     9795  13043   8203   2251   -281   -199       C  
ATOM   4221  O   MET B 114      -3.938  -7.572  68.288  1.00 83.52           O  
ANISOU 4221  O   MET B 114    10013  13458   8261   2432   -365   -181       O  
ATOM   4222  CB  MET B 114      -2.311  -7.525  65.671  1.00 80.49           C  
ANISOU 4222  CB  MET B 114     9211  13318   8055   2223   -356   -358       C  
ATOM   4223  CG  MET B 114      -1.345  -8.446  64.987  1.00 85.41           C  
ANISOU 4223  CG  MET B 114     9671  14111   8672   2425   -345   -358       C  
ATOM   4224  SD  MET B 114       0.268  -7.673  64.858  1.00 91.94           S  
ANISOU 4224  SD  MET B 114    10103  15445   9385   2308   -483   -545       S  
ATOM   4225  CE  MET B 114       1.075  -8.382  66.273  1.00 91.34           C  
ANISOU 4225  CE  MET B 114     9938  15689   9079   2707   -616   -503       C  
ATOM   4226  N   ALA B 115      -5.355  -6.611  66.797  1.00 77.73           N  
ANISOU 4226  N   ALA B 115     9409  12303   7821   1993   -222   -220       N  
ATOM   4227  CA  ALA B 115      -6.132  -5.779  67.728  1.00 78.11           C  
ANISOU 4227  CA  ALA B 115     9588  12266   7822   1891   -237   -232       C  
ATOM   4228  C   ALA B 115      -5.367  -4.543  68.254  1.00 85.33           C  
ANISOU 4228  C   ALA B 115    10362  13444   8618   1720   -373   -393       C  
ATOM   4229  O   ALA B 115      -5.795  -3.932  69.241  1.00 85.97           O  
ANISOU 4229  O   ALA B 115    10543  13511   8610   1688   -405   -417       O  
ATOM   4230  CB  ALA B 115      -6.691  -6.615  68.885  1.00 79.48           C  
ANISOU 4230  CB  ALA B 115     9941  12361   7897   2152   -198    -94       C  
ATOM   4231  N   TYR B 116      -4.252  -4.160  67.575  1.00 82.81           N  
ANISOU 4231  N   TYR B 116     9813  13359   8293   1593   -444   -512       N  
ATOM   4232  CA  TYR B 116      -3.404  -2.999  67.912  1.00 83.21           C  
ANISOU 4232  CA  TYR B 116     9703  13673   8239   1382   -567   -685       C  
ATOM   4233  C   TYR B 116      -2.329  -2.739  66.834  1.00 85.68           C  
ANISOU 4233  C   TYR B 116     9769  14190   8594   1216   -594   -792       C  
ATOM   4234  O   TYR B 116      -2.205  -3.522  65.883  1.00 84.52           O  
ANISOU 4234  O   TYR B 116     9574  13998   8543   1304   -522   -730       O  
ATOM   4235  CB  TYR B 116      -2.800  -3.098  69.353  1.00 86.05           C  
ANISOU 4235  CB  TYR B 116    10004  14317   8373   1563   -695   -714       C  
ATOM   4236  CG  TYR B 116      -1.661  -4.080  69.543  1.00 89.09           C  
ANISOU 4236  CG  TYR B 116    10186  15027   8638   1840   -772   -692       C  
ATOM   4237  CD1 TYR B 116      -1.900  -5.450  69.625  1.00 90.82           C  
ANISOU 4237  CD1 TYR B 116    10502  15148   8859   2180   -708   -521       C  
ATOM   4238  CD2 TYR B 116      -0.356  -3.635  69.729  1.00 92.25           C  
ANISOU 4238  CD2 TYR B 116    10304  15838   8908   1772   -913   -843       C  
ATOM   4239  CE1 TYR B 116      -0.856  -6.359  69.804  1.00 93.84           C  
ANISOU 4239  CE1 TYR B 116    10714  15817   9124   2473   -778   -494       C  
ATOM   4240  CE2 TYR B 116       0.696  -4.532  69.924  1.00 95.44           C  
ANISOU 4240  CE2 TYR B 116    10501  16569   9193   2058   -992   -825       C  
ATOM   4241  CZ  TYR B 116       0.443  -5.896  69.961  1.00102.61           C  
ANISOU 4241  CZ  TYR B 116    11521  17359  10107   2426   -925   -646       C  
ATOM   4242  OH  TYR B 116       1.485  -6.781  70.153  1.00104.12           O  
ANISOU 4242  OH  TYR B 116    11523  17865  10173   2742  -1003   -623       O  
ATOM   4243  N   TRP B 117      -1.584  -1.624  66.969  1.00 82.07           N  
ANISOU 4243  N   TRP B 117     9167  13949   8065    960   -686   -958       N  
ATOM   4244  CA  TRP B 117      -0.508  -1.265  66.051  1.00 82.56           C  
ANISOU 4244  CA  TRP B 117     8980  14242   8146    763   -707  -1074       C  
ATOM   4245  C   TRP B 117       0.874  -1.700  66.569  1.00 90.53           C  
ANISOU 4245  C   TRP B 117     9688  15718   8990    918   -830  -1150       C  
ATOM   4246  O   TRP B 117       1.506  -1.009  67.385  1.00 92.94           O  
ANISOU 4246  O   TRP B 117     9874  16287   9152    808   -953  -1282       O  
ATOM   4247  CB  TRP B 117      -0.526   0.221  65.695  1.00 80.40           C  
ANISOU 4247  CB  TRP B 117     8734  13903   7912    348   -710  -1210       C  
ATOM   4248  CG  TRP B 117       0.429   0.550  64.585  1.00 81.52           C  
ANISOU 4248  CG  TRP B 117     8654  14226   8094    121   -692  -1305       C  
ATOM   4249  CD1 TRP B 117       1.692   1.046  64.713  1.00 86.86           C  
ANISOU 4249  CD1 TRP B 117     9058  15284   8662    -47   -781  -1463       C  
ATOM   4250  CD2 TRP B 117       0.223   0.331  63.183  1.00 79.46           C  
ANISOU 4250  CD2 TRP B 117     8410  13800   7981     45   -573  -1246       C  
ATOM   4251  NE1 TRP B 117       2.272   1.190  63.477  1.00 86.43           N  
ANISOU 4251  NE1 TRP B 117     8854  15305   8683   -237   -712  -1505       N  
ATOM   4252  CE2 TRP B 117       1.394   0.755  62.517  1.00 85.25           C  
ANISOU 4252  CE2 TRP B 117     8886  14820   8685   -176   -585  -1371       C  
ATOM   4253  CE3 TRP B 117      -0.844  -0.173  62.418  1.00 77.68           C  
ANISOU 4253  CE3 TRP B 117     8388  13224   7901    132   -457  -1108       C  
ATOM   4254  CZ2 TRP B 117       1.520   0.710  61.122  1.00 83.36           C  
ANISOU 4254  CZ2 TRP B 117     8604  14516   8550   -306   -478  -1354       C  
ATOM   4255  CZ3 TRP B 117      -0.716  -0.217  61.039  1.00 77.94           C  
ANISOU 4255  CZ3 TRP B 117     8378  13198   8036      6   -366  -1099       C  
ATOM   4256  CH2 TRP B 117       0.453   0.224  60.406  1.00 80.34           C  
ANISOU 4256  CH2 TRP B 117     8442  13782   8301   -206   -374  -1217       C  
ATOM   4257  N   TYR B 118       1.340  -2.840  66.059  1.00 86.40           N  
ANISOU 4257  N   TYR B 118     9042  15301   8484   1174   -797  -1075       N  
ATOM   4258  CA  TYR B 118       2.614  -3.421  66.428  1.00 88.87           C  
ANISOU 4258  CA  TYR B 118     9063  16054   8650   1387   -903  -1125       C  
ATOM   4259  C   TYR B 118       3.817  -2.668  65.825  1.00 95.40           C  
ANISOU 4259  C   TYR B 118     9562  17235   9451   1105   -951  -1309       C  
ATOM   4260  O   TYR B 118       4.856  -2.578  66.481  1.00 99.04           O  
ANISOU 4260  O   TYR B 118     9761  18119   9751   1152  -1085  -1417       O  
ATOM   4261  CB  TYR B 118       2.628  -4.918  66.024  1.00 90.07           C  
ANISOU 4261  CB  TYR B 118     9230  16152   8839   1775   -831   -977       C  
ATOM   4262  CG  TYR B 118       3.909  -5.649  66.359  1.00 95.43           C  
ANISOU 4262  CG  TYR B 118     9618  17273   9367   2069   -933  -1010       C  
ATOM   4263  CD1 TYR B 118       4.183  -6.056  67.661  1.00 99.91           C  
ANISOU 4263  CD1 TYR B 118    10173  18042   9748   2356  -1057   -974       C  
ATOM   4264  CD2 TYR B 118       4.860  -5.916  65.379  1.00 97.43           C  
ANISOU 4264  CD2 TYR B 118     9602  17765   9651   2070   -905  -1078       C  
ATOM   4265  CE1 TYR B 118       5.389  -6.681  67.988  1.00104.72           C  
ANISOU 4265  CE1 TYR B 118    10497  19090  10203   2646  -1167  -1007       C  
ATOM   4266  CE2 TYR B 118       6.071  -6.535  65.694  1.00101.55           C  
ANISOU 4266  CE2 TYR B 118     9825  18732  10028   2353  -1004  -1120       C  
ATOM   4267  CZ  TYR B 118       6.330  -6.921  67.000  1.00112.10           C  
ANISOU 4267  CZ  TYR B 118    11146  20269  11179   2649  -1141  -1083       C  
ATOM   4268  OH  TYR B 118       7.515  -7.549  67.321  1.00117.76           O  
ANISOU 4268  OH  TYR B 118    11563  21438  11740   2962  -1250  -1118       O  
ATOM   4269  N   PHE B 119       3.661  -2.107  64.603  1.00 89.30           N  
ANISOU 4269  N   PHE B 119     8805  16301   8826    803   -843  -1345       N  
ATOM   4270  CA  PHE B 119       4.701  -1.521  63.725  1.00 89.65           C  
ANISOU 4270  CA  PHE B 119     8566  16620   8877    520   -833  -1490       C  
ATOM   4271  C   PHE B 119       5.311  -0.130  64.098  1.00 95.92           C  
ANISOU 4271  C   PHE B 119     9227  17631   9588    114   -920  -1683       C  
ATOM   4272  O   PHE B 119       6.209   0.343  63.384  1.00 96.46           O  
ANISOU 4272  O   PHE B 119     9051  17942   9656   -142   -901  -1805       O  
ATOM   4273  CB  PHE B 119       4.175  -1.484  62.280  1.00 88.36           C  
ANISOU 4273  CB  PHE B 119     8525  16156   8891    362   -671  -1432       C  
ATOM   4274  CG  PHE B 119       3.572  -2.814  61.887  1.00 86.98           C  
ANISOU 4274  CG  PHE B 119     8490  15761   8797    720   -585  -1265       C  
ATOM   4275  CD1 PHE B 119       4.379  -3.927  61.671  1.00 90.72           C  
ANISOU 4275  CD1 PHE B 119     8759  16487   9225   1031   -584  -1245       C  
ATOM   4276  CD2 PHE B 119       2.195  -2.976  61.815  1.00 84.48           C  
ANISOU 4276  CD2 PHE B 119     8513  14993   8594    760   -507  -1133       C  
ATOM   4277  CE1 PHE B 119       3.821  -5.163  61.360  1.00 89.90           C  
ANISOU 4277  CE1 PHE B 119     8815  16152   9189   1356   -500  -1099       C  
ATOM   4278  CE2 PHE B 119       1.639  -4.212  61.505  1.00 85.60           C  
ANISOU 4278  CE2 PHE B 119     8789  14930   8804   1065   -427   -992       C  
ATOM   4279  CZ  PHE B 119       2.455  -5.296  61.276  1.00 85.50           C  
ANISOU 4279  CZ  PHE B 119     8600  15140   8747   1354   -421   -976       C  
ATOM   4280  N   GLY B 120       4.889   0.455  65.217  1.00 93.67           N  
ANISOU 4280  N   GLY B 120     9089  17280   9222     64  -1009  -1717       N  
ATOM   4281  CA  GLY B 120       5.440   1.717  65.707  1.00 95.63           C  
ANISOU 4281  CA  GLY B 120     9241  17719   9376   -304  -1099  -1911       C  
ATOM   4282  C   GLY B 120       4.864   2.997  65.135  1.00 98.33           C  
ANISOU 4282  C   GLY B 120     9801  17733   9826   -737  -1013  -1966       C  
ATOM   4283  O   GLY B 120       4.325   3.017  64.023  1.00 95.69           O  
ANISOU 4283  O   GLY B 120     9604  17108   9644   -824   -877  -1880       O  
ATOM   4284  N   GLN B 121       5.032   4.086  65.907  1.00 96.60           N  
ANISOU 4284  N   GLN B 121     9615  17576   9512  -1009  -1099  -2119       N  
ATOM   4285  CA  GLN B 121       4.571   5.462  65.666  1.00 96.01           C  
ANISOU 4285  CA  GLN B 121     9772  17209   9497  -1427  -1044  -2202       C  
ATOM   4286  C   GLN B 121       4.937   6.064  64.293  1.00 98.87           C  
ANISOU 4286  C   GLN B 121    10084  17513   9969  -1783   -924  -2240       C  
ATOM   4287  O   GLN B 121       4.130   6.829  63.749  1.00 96.46           O  
ANISOU 4287  O   GLN B 121    10073  16806   9771  -1991   -827  -2201       O  
ATOM   4288  CB  GLN B 121       5.048   6.403  66.793  1.00100.26           C  
ANISOU 4288  CB  GLN B 121    10275  17944   9877  -1651  -1177  -2400       C  
ATOM   4289  CG  GLN B 121       6.539   6.276  67.156  1.00122.64           C  
ANISOU 4289  CG  GLN B 121    12674  21370  12553  -1713  -1307  -2568       C  
ATOM   4290  CD  GLN B 121       7.047   7.409  68.014  1.00148.48           C  
ANISOU 4290  CD  GLN B 121    15914  24815  15685  -2055  -1420  -2797       C  
ATOM   4291  OE1 GLN B 121       6.497   7.725  69.076  1.00143.96           O  
ANISOU 4291  OE1 GLN B 121    15549  24124  15027  -1994  -1495  -2828       O  
ATOM   4292  NE2 GLN B 121       8.128   8.037  67.580  1.00145.85           N  
ANISOU 4292  NE2 GLN B 121    15316  24782  15319  -2432  -1430  -2974       N  
ATOM   4293  N   TRP B 122       6.146   5.766  63.757  1.00 97.17           N  
ANISOU 4293  N   TRP B 122     9502  17704   9714  -1854   -930  -2317       N  
ATOM   4294  CA  TRP B 122       6.574   6.315  62.466  1.00 97.21           C  
ANISOU 4294  CA  TRP B 122     9442  17692   9802  -2201   -806  -2356       C  
ATOM   4295  C   TRP B 122       5.850   5.638  61.333  1.00 98.27           C  
ANISOU 4295  C   TRP B 122     9723  17530  10086  -2024   -666  -2168       C  
ATOM   4296  O   TRP B 122       5.320   6.337  60.467  1.00 97.23           O  
ANISOU 4296  O   TRP B 122     9817  17073  10054  -2273   -552  -2129       O  
ATOM   4297  CB  TRP B 122       8.095   6.254  62.256  1.00 99.27           C  
ANISOU 4297  CB  TRP B 122     9247  18504   9967  -2352   -843  -2510       C  
ATOM   4298  CG  TRP B 122       8.545   6.795  60.920  1.00101.09           C  
ANISOU 4298  CG  TRP B 122     9410  18728  10271  -2717   -696  -2543       C  
ATOM   4299  CD1 TRP B 122       8.794   8.099  60.604  1.00105.64           C  
ANISOU 4299  CD1 TRP B 122    10066  19225  10847  -3227   -642  -2665       C  
ATOM   4300  CD2 TRP B 122       8.802   6.036  59.725  1.00100.13           C  
ANISOU 4300  CD2 TRP B 122     9147  18676  10223  -2598   -576  -2453       C  
ATOM   4301  NE1 TRP B 122       9.193   8.202  59.288  1.00105.42           N  
ANISOU 4301  NE1 TRP B 122     9952  19220  10883  -3438   -493  -2645       N  
ATOM   4302  CE2 TRP B 122       9.212   6.951  58.727  1.00105.29           C  
ANISOU 4302  CE2 TRP B 122     9790  19305  10908  -3057   -452  -2521       C  
ATOM   4303  CE3 TRP B 122       8.733   4.667  59.402  1.00 99.90           C  
ANISOU 4303  CE3 TRP B 122     9014  18717  10226  -2151   -555  -2324       C  
ATOM   4304  CZ2 TRP B 122       9.550   6.544  57.433  1.00104.35           C  
ANISOU 4304  CZ2 TRP B 122     9550  19253  10847  -3076   -310  -2465       C  
ATOM   4305  CZ3 TRP B 122       9.065   4.266  58.119  1.00101.33           C  
ANISOU 4305  CZ3 TRP B 122     9079  18952  10470  -2168   -418  -2280       C  
ATOM   4306  CH2 TRP B 122       9.452   5.199  57.146  1.00103.16           C  
ANISOU 4306  CH2 TRP B 122     9295  19174  10726  -2623   -297  -2348       C  
ATOM   4307  N   TRP B 123       5.811   4.285  61.333  1.00 93.11           N  
ANISOU 4307  N   TRP B 123     8960  16976   9440  -1592   -675  -2053       N  
ATOM   4308  CA  TRP B 123       5.112   3.565  60.279  1.00 89.99           C  
ANISOU 4308  CA  TRP B 123     8708  16304   9181  -1417   -547  -1887       C  
ATOM   4309  C   TRP B 123       3.600   3.750  60.379  1.00 89.35           C  
ANISOU 4309  C   TRP B 123     9038  15710   9200  -1352   -505  -1755       C  
ATOM   4310  O   TRP B 123       2.906   3.596  59.377  1.00 87.75           O  
ANISOU 4310  O   TRP B 123     9004  15220   9116  -1350   -393  -1645       O  
ATOM   4311  CB  TRP B 123       5.520   2.085  60.177  1.00 89.09           C  
ANISOU 4311  CB  TRP B 123     8384  16416   9049   -996   -553  -1812       C  
ATOM   4312  CG  TRP B 123       4.990   1.431  58.927  1.00 87.85           C  
ANISOU 4312  CG  TRP B 123     8341  16017   9022   -890   -411  -1681       C  
ATOM   4313  CD1 TRP B 123       4.004   0.489  58.850  1.00 88.33           C  
ANISOU 4313  CD1 TRP B 123     8615  15783   9163   -570   -370  -1522       C  
ATOM   4314  CD2 TRP B 123       5.286   1.810  57.574  1.00 87.64           C  
ANISOU 4314  CD2 TRP B 123     8268  15974   9055  -1155   -287  -1703       C  
ATOM   4315  NE1 TRP B 123       3.696   0.229  57.535  1.00 86.16           N  
ANISOU 4315  NE1 TRP B 123     8414  15329   8993   -611   -239  -1454       N  
ATOM   4316  CE2 TRP B 123       4.477   1.015  56.729  1.00 88.83           C  
ANISOU 4316  CE2 TRP B 123     8598  15837   9315   -954   -187  -1558       C  
ATOM   4317  CE3 TRP B 123       6.173   2.731  56.991  1.00 90.85           C  
ANISOU 4317  CE3 TRP B 123     8501  16592   9427  -1552   -245  -1833       C  
ATOM   4318  CZ2 TRP B 123       4.537   1.104  55.339  1.00 87.53           C  
ANISOU 4318  CZ2 TRP B 123     8443  15602   9214  -1116    -56  -1540       C  
ATOM   4319  CZ3 TRP B 123       6.240   2.808  55.611  1.00 91.95           C  
ANISOU 4319  CZ3 TRP B 123     8652  16655   9629  -1713   -103  -1802       C  
ATOM   4320  CH2 TRP B 123       5.424   2.008  54.801  1.00 90.02           C  
ANISOU 4320  CH2 TRP B 123     8590  16131   9483  -1488    -15  -1657       C  
ATOM   4321  N   CYS B 124       3.097   4.151  61.559  1.00 83.99           N  
ANISOU 4321  N   CYS B 124     8515  14932   8467  -1317   -594  -1777       N  
ATOM   4322  CA  CYS B 124       1.671   4.418  61.734  1.00 80.55           C  
ANISOU 4322  CA  CYS B 124     8449  14038   8116  -1263   -553  -1669       C  
ATOM   4323  C   CYS B 124       1.259   5.657  60.922  1.00 81.28           C  
ANISOU 4323  C   CYS B 124     8753  13840   8289  -1636   -469  -1694       C  
ATOM   4324  O   CYS B 124       0.258   5.621  60.202  1.00 77.74           O  
ANISOU 4324  O   CYS B 124     8532  13046   7959  -1595   -380  -1570       O  
ATOM   4325  CB  CYS B 124       1.315   4.558  63.210  1.00 81.25           C  
ANISOU 4325  CB  CYS B 124     8637  14126   8108  -1134   -660  -1699       C  
ATOM   4326  SG  CYS B 124      -0.389   5.090  63.509  1.00 82.90           S  
ANISOU 4326  SG  CYS B 124     9279  13811   8409  -1106   -606  -1599       S  
ATOM   4327  N   GLY B 125       2.073   6.706  61.019  1.00 79.21           N  
ANISOU 4327  N   GLY B 125     8407  13734   7956  -1993   -498  -1854       N  
ATOM   4328  CA  GLY B 125       1.895   7.962  60.306  1.00 79.07           C  
ANISOU 4328  CA  GLY B 125     8586  13470   7988  -2380   -419  -1894       C  
ATOM   4329  C   GLY B 125       2.085   7.819  58.810  1.00 82.33           C  
ANISOU 4329  C   GLY B 125     8956  13845   8482  -2493   -296  -1825       C  
ATOM   4330  O   GLY B 125       1.369   8.464  58.047  1.00 82.15           O  
ANISOU 4330  O   GLY B 125     9199  13476   8539  -2641   -209  -1755       O  
ATOM   4331  N   VAL B 126       3.042   6.974  58.368  1.00 78.18           N  
ANISOU 4331  N   VAL B 126     8099  13677   7927  -2408   -286  -1842       N  
ATOM   4332  CA  VAL B 126       3.281   6.743  56.934  1.00 76.91           C  
ANISOU 4332  CA  VAL B 126     7879  13517   7828  -2495   -161  -1783       C  
ATOM   4333  C   VAL B 126       2.147   5.880  56.364  1.00 77.64           C  
ANISOU 4333  C   VAL B 126     8161  13309   8030  -2183   -104  -1601       C  
ATOM   4334  O   VAL B 126       1.586   6.241  55.334  1.00 76.01           O  
ANISOU 4334  O   VAL B 126     8149  12837   7896  -2307     -8  -1523       O  
ATOM   4335  CB  VAL B 126       4.695   6.188  56.596  1.00 81.82           C  
ANISOU 4335  CB  VAL B 126     8081  14630   8377  -2517   -154  -1877       C  
ATOM   4336  CG1 VAL B 126       4.872   6.023  55.090  1.00 80.87           C  
ANISOU 4336  CG1 VAL B 126     7932  14484   8311  -2620     -9  -1818       C  
ATOM   4337  CG2 VAL B 126       5.789   7.090  57.155  1.00 84.69           C  
ANISOU 4337  CG2 VAL B 126     8240  15307   8630  -2862   -212  -2071       C  
ATOM   4338  N   TYR B 127       1.784   4.779  57.059  1.00 73.01           N  
ANISOU 4338  N   TYR B 127     7535  12757   7447  -1793   -165  -1535       N  
ATOM   4339  CA  TYR B 127       0.693   3.899  56.656  1.00 70.66           C  
ANISOU 4339  CA  TYR B 127     7412  12185   7250  -1505   -116  -1375       C  
ATOM   4340  C   TYR B 127      -0.610   4.678  56.443  1.00 73.11           C  
ANISOU 4340  C   TYR B 127     8078  12057   7644  -1604    -80  -1296       C  
ATOM   4341  O   TYR B 127      -1.243   4.511  55.400  1.00 71.61           O  
ANISOU 4341  O   TYR B 127     8018  11655   7537  -1594      2  -1200       O  
ATOM   4342  CB  TYR B 127       0.508   2.744  57.651  1.00 71.96           C  
ANISOU 4342  CB  TYR B 127     7515  12437   7390  -1109   -187  -1325       C  
ATOM   4343  CG  TYR B 127      -0.873   2.120  57.646  1.00 72.48           C  
ANISOU 4343  CG  TYR B 127     7832  12152   7554   -867   -152  -1175       C  
ATOM   4344  CD1 TYR B 127      -1.241   1.195  56.672  1.00 72.56           C  
ANISOU 4344  CD1 TYR B 127     7866  12057   7646   -714    -68  -1078       C  
ATOM   4345  CD2 TYR B 127      -1.793   2.414  58.645  1.00 73.58           C  
ANISOU 4345  CD2 TYR B 127     8173  12088   7697   -791   -199  -1142       C  
ATOM   4346  CE1 TYR B 127      -2.493   0.585  56.690  1.00 70.35           C  
ANISOU 4346  CE1 TYR B 127     7797  11480   7454   -512    -37   -953       C  
ATOM   4347  CE2 TYR B 127      -3.055   1.828  58.659  1.00 72.86           C  
ANISOU 4347  CE2 TYR B 127     8285  11705   7693   -584   -159  -1011       C  
ATOM   4348  CZ  TYR B 127      -3.399   0.913  57.681  1.00 79.07           C  
ANISOU 4348  CZ  TYR B 127     9082  12395   8564   -454    -80   -918       C  
ATOM   4349  OH  TYR B 127      -4.651   0.365  57.700  1.00 82.10           O  
ANISOU 4349  OH  TYR B 127     9655  12504   9034   -284    -40   -803       O  
ATOM   4350  N   LEU B 128      -0.985   5.544  57.410  1.00 69.74           N  
ANISOU 4350  N   LEU B 128     7802  11509   7186  -1695   -142  -1345       N  
ATOM   4351  CA  LEU B 128      -2.188   6.376  57.330  1.00 68.05           C  
ANISOU 4351  CA  LEU B 128     7922  10896   7039  -1771   -115  -1284       C  
ATOM   4352  C   LEU B 128      -2.092   7.454  56.263  1.00 72.08           C  
ANISOU 4352  C   LEU B 128     8561  11255   7570  -2108    -39  -1297       C  
ATOM   4353  O   LEU B 128      -3.074   7.673  55.554  1.00 71.50           O  
ANISOU 4353  O   LEU B 128     8716  10876   7576  -2090     16  -1192       O  
ATOM   4354  CB  LEU B 128      -2.556   6.998  58.682  1.00 68.69           C  
ANISOU 4354  CB  LEU B 128     8131  10902   7068  -1761   -194  -1347       C  
ATOM   4355  CG  LEU B 128      -3.061   6.047  59.761  1.00 72.46           C  
ANISOU 4355  CG  LEU B 128     8588  11414   7528  -1410   -252  -1294       C  
ATOM   4356  CD1 LEU B 128      -3.328   6.797  61.007  1.00 73.64           C  
ANISOU 4356  CD1 LEU B 128     8866  11506   7606  -1444   -321  -1373       C  
ATOM   4357  CD2 LEU B 128      -4.330   5.320  59.336  1.00 72.09           C  
ANISOU 4357  CD2 LEU B 128     8698  11098   7596  -1168   -191  -1133       C  
ATOM   4358  N   ALA B 129      -0.914   8.099  56.122  1.00 69.41           N  
ANISOU 4358  N   ALA B 129     8075  11142   7157  -2413    -34  -1423       N  
ATOM   4359  CA  ALA B 129      -0.662   9.139  55.116  1.00 69.88           C  
ANISOU 4359  CA  ALA B 129     8253  11080   7217  -2771     53  -1438       C  
ATOM   4360  C   ALA B 129      -0.795   8.595  53.688  1.00 71.97           C  
ANISOU 4360  C   ALA B 129     8506  11303   7536  -2731    152  -1326       C  
ATOM   4361  O   ALA B 129      -1.463   9.203  52.859  1.00 70.47           O  
ANISOU 4361  O   ALA B 129     8567  10820   7387  -2839    216  -1243       O  
ATOM   4362  CB  ALA B 129       0.719   9.735  55.320  1.00 73.50           C  
ANISOU 4362  CB  ALA B 129     8498  11851   7577  -3098     44  -1605       C  
ATOM   4363  N   LEU B 130      -0.188   7.427  53.431  1.00 69.08           N  
ANISOU 4363  N   LEU B 130     7859  11227   7162  -2552    159  -1324       N  
ATOM   4364  CA  LEU B 130      -0.192   6.731  52.147  1.00 68.29           C  
ANISOU 4364  CA  LEU B 130     7708  11142   7098  -2483    250  -1241       C  
ATOM   4365  C   LEU B 130      -1.581   6.190  51.791  1.00 71.48           C  
ANISOU 4365  C   LEU B 130     8337  11227   7596  -2225    258  -1094       C  
ATOM   4366  O   LEU B 130      -1.995   6.274  50.627  1.00 69.20           O  
ANISOU 4366  O   LEU B 130     8175  10782   7337  -2283    333  -1014       O  
ATOM   4367  CB  LEU B 130       0.812   5.555  52.168  1.00 68.54           C  
ANISOU 4367  CB  LEU B 130     7382  11569   7090  -2307    246  -1293       C  
ATOM   4368  CG  LEU B 130       2.304   5.847  52.097  1.00 75.34           C  
ANISOU 4368  CG  LEU B 130     7940  12827   7858  -2547    266  -1433       C  
ATOM   4369  CD1 LEU B 130       3.069   4.553  51.909  1.00 75.72           C  
ANISOU 4369  CD1 LEU B 130     7670  13217   7882  -2292    276  -1453       C  
ATOM   4370  CD2 LEU B 130       2.644   6.828  50.963  1.00 78.03           C  
ANISOU 4370  CD2 LEU B 130     8361  13109   8177  -2938    382  -1444       C  
ATOM   4371  N   ASP B 131      -2.276   5.592  52.791  1.00 67.83           N  
ANISOU 4371  N   ASP B 131     7910  10694   7171  -1943    183  -1061       N  
ATOM   4372  CA  ASP B 131      -3.593   4.985  52.610  1.00 65.20           C  
ANISOU 4372  CA  ASP B 131     7753  10095   6927  -1695    188   -936       C  
ATOM   4373  C   ASP B 131      -4.621   6.004  52.107  1.00 68.13           C  
ANISOU 4373  C   ASP B 131     8427  10121   7340  -1825    211   -867       C  
ATOM   4374  O   ASP B 131      -5.407   5.694  51.200  1.00 67.40           O  
ANISOU 4374  O   ASP B 131     8446   9860   7302  -1746    251   -770       O  
ATOM   4375  CB  ASP B 131      -4.016   4.264  53.891  1.00 65.50           C  
ANISOU 4375  CB  ASP B 131     7762  10148   6977  -1413    115   -926       C  
ATOM   4376  CG  ASP B 131      -5.469   4.383  54.238  1.00 68.11           C  
ANISOU 4376  CG  ASP B 131     8337  10163   7381  -1280    101   -836       C  
ATOM   4377  OD1 ASP B 131      -6.272   3.625  53.669  1.00 63.94           O  
ANISOU 4377  OD1 ASP B 131     7868   9504   6925  -1116    136   -742       O  
ATOM   4378  OD2 ASP B 131      -5.799   5.233  55.081  1.00 79.51           O1-
ANISOU 4378  OD2 ASP B 131     9907  11499   8804  -1342     57   -870       O1-
ATOM   4379  N   VAL B 132      -4.543   7.235  52.641  1.00 63.06           N  
ANISOU 4379  N   VAL B 132     7913   9385   6661  -2033    186   -925       N  
ATOM   4380  CA  VAL B 132      -5.359   8.367  52.222  1.00 61.59           C  
ANISOU 4380  CA  VAL B 132     8030   8875   6497  -2169    209   -872       C  
ATOM   4381  C   VAL B 132      -4.872   8.859  50.823  1.00 66.64           C  
ANISOU 4381  C   VAL B 132     8711   9504   7105  -2420    296   -846       C  
ATOM   4382  O   VAL B 132      -5.710   9.050  49.934  1.00 65.68           O  
ANISOU 4382  O   VAL B 132     8782   9156   7016  -2391    328   -739       O  
ATOM   4383  CB  VAL B 132      -5.346   9.492  53.291  1.00 65.64           C  
ANISOU 4383  CB  VAL B 132     8681   9287   6971  -2306    162   -957       C  
ATOM   4384  CG1 VAL B 132      -6.042  10.744  52.790  1.00 66.02           C  
ANISOU 4384  CG1 VAL B 132     9059   8995   7030  -2459    196   -907       C  
ATOM   4385  CG2 VAL B 132      -5.972   9.025  54.596  1.00 63.94           C  
ANISOU 4385  CG2 VAL B 132     8459   9059   6776  -2044     88   -966       C  
ATOM   4386  N   LEU B 133      -3.529   9.020  50.620  1.00 64.64           N  
ANISOU 4386  N   LEU B 133     8264   9516   6778  -2658    334   -943       N  
ATOM   4387  CA  LEU B 133      -2.937   9.492  49.356  1.00 65.49           C  
ANISOU 4387  CA  LEU B 133     8393   9651   6838  -2925    434   -927       C  
ATOM   4388  C   LEU B 133      -3.252   8.606  48.158  1.00 69.20           C  
ANISOU 4388  C   LEU B 133     8829  10132   7333  -2777    489   -828       C  
ATOM   4389  O   LEU B 133      -3.580   9.142  47.105  1.00 70.73           O  
ANISOU 4389  O   LEU B 133     9214  10153   7508  -2902    551   -748       O  
ATOM   4390  CB  LEU B 133      -1.418   9.736  49.471  1.00 67.85           C  
ANISOU 4390  CB  LEU B 133     8442  10283   7055  -3201    469  -1064       C  
ATOM   4391  CG  LEU B 133      -0.666  10.211  48.196  1.00 73.29           C  
ANISOU 4391  CG  LEU B 133     9121  11045   7680  -3511    594  -1059       C  
ATOM   4392  CD1 LEU B 133      -0.717  11.722  48.038  1.00 74.47           C  
ANISOU 4392  CD1 LEU B 133     9564  10941   7791  -3856    640  -1059       C  
ATOM   4393  CD2 LEU B 133       0.768   9.719  48.200  1.00 76.11           C  
ANISOU 4393  CD2 LEU B 133     9094  11849   7975  -3621    628  -1181       C  
ATOM   4394  N   PHE B 134      -3.161   7.279  48.297  1.00 64.35           N  
ANISOU 4394  N   PHE B 134     7996   9706   6749  -2514    467   -833       N  
ATOM   4395  CA  PHE B 134      -3.456   6.384  47.180  1.00 63.45           C  
ANISOU 4395  CA  PHE B 134     7856   9598   6653  -2375    520   -758       C  
ATOM   4396  C   PHE B 134      -4.947   6.379  46.805  1.00 67.51           C  
ANISOU 4396  C   PHE B 134     8629   9788   7232  -2218    493   -635       C  
ATOM   4397  O   PHE B 134      -5.282   6.153  45.635  1.00 67.22           O  
ANISOU 4397  O   PHE B 134     8666   9689   7186  -2212    541   -567       O  
ATOM   4398  CB  PHE B 134      -2.907   4.966  47.416  1.00 64.75           C  
ANISOU 4398  CB  PHE B 134     7739  10036   6828  -2138    514   -804       C  
ATOM   4399  CG  PHE B 134      -1.409   4.869  47.631  1.00 68.51           C  
ANISOU 4399  CG  PHE B 134     7919  10881   7231  -2259    541   -925       C  
ATOM   4400  CD1 PHE B 134      -0.525   5.629  46.867  1.00 73.94           C  
ANISOU 4400  CD1 PHE B 134     8557  11695   7842  -2579    628   -970       C  
ATOM   4401  CD2 PHE B 134      -0.881   4.005  48.584  1.00 70.80           C  
ANISOU 4401  CD2 PHE B 134     7975  11407   7520  -2048    484   -990       C  
ATOM   4402  CE1 PHE B 134       0.855   5.559  47.088  1.00 76.87           C  
ANISOU 4402  CE1 PHE B 134     8623  12442   8144  -2702    653  -1093       C  
ATOM   4403  CE2 PHE B 134       0.501   3.944  48.812  1.00 75.65           C  
ANISOU 4403  CE2 PHE B 134     8291  12396   8059  -2145    496  -1108       C  
ATOM   4404  CZ  PHE B 134       1.357   4.729  48.071  1.00 75.75           C  
ANISOU 4404  CZ  PHE B 134     8231  12549   8003  -2478    580  -1165       C  
ATOM   4405  N   CYS B 135      -5.833   6.676  47.776  1.00 64.62           N  
ANISOU 4405  N   CYS B 135     8398   9231   6922  -2099    417   -614       N  
ATOM   4406  CA  CYS B 135      -7.280   6.764  47.536  1.00 63.62           C  
ANISOU 4406  CA  CYS B 135     8496   8820   6857  -1949    385   -508       C  
ATOM   4407  C   CYS B 135      -7.635   8.077  46.818  1.00 68.48           C  
ANISOU 4407  C   CYS B 135     9379   9207   7433  -2147    410   -447       C  
ATOM   4408  O   CYS B 135      -8.527   8.097  45.965  1.00 67.64           O  
ANISOU 4408  O   CYS B 135     9424   8938   7338  -2074    411   -350       O  
ATOM   4409  CB  CYS B 135      -8.071   6.598  48.833  1.00 62.80           C  
ANISOU 4409  CB  CYS B 135     8425   8618   6819  -1747    310   -510       C  
ATOM   4410  SG  CYS B 135      -9.868   6.755  48.629  1.00 65.36           S  
ANISOU 4410  SG  CYS B 135     8986   8630   7219  -1562    273   -393       S  
ATOM   4411  N   THR B 136      -6.941   9.171  47.185  1.00 66.00           N  
ANISOU 4411  N   THR B 136     9132   8879   7065  -2396    428   -506       N  
ATOM   4412  CA  THR B 136      -7.144  10.501  46.604  1.00 66.53           C  
ANISOU 4412  CA  THR B 136     9485   8709   7084  -2606    463   -453       C  
ATOM   4413  C   THR B 136      -6.526  10.579  45.228  1.00 70.74           C  
ANISOU 4413  C   THR B 136    10018   9320   7540  -2797    556   -413       C  
ATOM   4414  O   THR B 136      -7.169  11.118  44.324  1.00 70.74           O  
ANISOU 4414  O   THR B 136    10256   9111   7509  -2819    577   -305       O  
ATOM   4415  CB  THR B 136      -6.625  11.591  47.540  1.00 69.24           C  
ANISOU 4415  CB  THR B 136     9916   8996   7397  -2817    457   -543       C  
ATOM   4416  OG1 THR B 136      -7.070  11.294  48.867  1.00 68.19           O  
ANISOU 4416  OG1 THR B 136     9728   8861   7321  -2617    374   -595       O  
ATOM   4417  CG2 THR B 136      -7.068  12.978  47.116  1.00 61.72           C  
ANISOU 4417  CG2 THR B 136     9322   7720   6406  -2980    487   -478       C  
ATOM   4418  N   SER B 137      -5.296  10.021  45.055  1.00 67.57           N  
ANISOU 4418  N   SER B 137     9346   9231   7097  -2917    613   -498       N  
ATOM   4419  CA  SER B 137      -4.624  10.006  43.761  1.00 68.92           C  
ANISOU 4419  CA  SER B 137     9483   9519   7184  -3098    718   -473       C  
ATOM   4420  C   SER B 137      -5.440   9.251  42.708  1.00 72.74           C  
ANISOU 4420  C   SER B 137    10019   9942   7674  -2894    719   -369       C  
ATOM   4421  O   SER B 137      -5.399   9.649  41.546  1.00 73.70           O  
ANISOU 4421  O   SER B 137    10278  10009   7716  -3030    789   -298       O  
ATOM   4422  CB  SER B 137      -3.188   9.506  43.863  1.00 73.65           C  
ANISOU 4422  CB  SER B 137     9752  10492   7741  -3231    777   -595       C  
ATOM   4423  OG  SER B 137      -3.112   8.097  43.984  1.00 84.90           O  
ANISOU 4423  OG  SER B 137    10922  12127   9208  -2960    750   -627       O  
ATOM   4424  N   SER B 138      -6.231   8.219  43.128  1.00 67.35           N  
ANISOU 4424  N   SER B 138     9253   9257   7081  -2580    641   -360       N  
ATOM   4425  CA  SER B 138      -7.146   7.458  42.258  1.00 66.09           C  
ANISOU 4425  CA  SER B 138     9144   9029   6939  -2380    624   -279       C  
ATOM   4426  C   SER B 138      -8.305   8.373  41.812  1.00 67.55           C  
ANISOU 4426  C   SER B 138     9645   8909   7113  -2367    583   -159       C  
ATOM   4427  O   SER B 138      -8.639   8.409  40.628  1.00 67.53           O  
ANISOU 4427  O   SER B 138     9757   8856   7045  -2382    608    -81       O  
ATOM   4428  CB  SER B 138      -7.697   6.225  42.976  1.00 68.62           C  
ANISOU 4428  CB  SER B 138     9313   9400   7360  -2086    557   -307       C  
ATOM   4429  OG  SER B 138      -6.688   5.286  43.316  1.00 80.91           O  
ANISOU 4429  OG  SER B 138    10595  11228   8918  -2046    590   -403       O  
ATOM   4430  N   ALA B 139      -8.882   9.130  42.749  1.00 61.39           N  
ANISOU 4430  N   ALA B 139     9006   7937   6382  -2333    522   -149       N  
ATOM   4431  CA  ALA B 139      -9.964  10.055  42.463  1.00 61.30           C  
ANISOU 4431  CA  ALA B 139     9293   7637   6362  -2288    480    -42       C  
ATOM   4432  C   ALA B 139      -9.477  11.170  41.558  1.00 70.50           C  
ANISOU 4432  C   ALA B 139    10676   8700   7411  -2550    556     18       C  
ATOM   4433  O   ALA B 139     -10.190  11.512  40.607  1.00 73.21           O  
ANISOU 4433  O   ALA B 139    11222   8895   7700  -2503    546    133       O  
ATOM   4434  CB  ALA B 139     -10.489  10.640  43.754  1.00 61.72           C  
ANISOU 4434  CB  ALA B 139     9435   7530   6485  -2207    418    -67       C  
ATOM   4435  N   VAL B 140      -8.256  11.730  41.836  1.00 66.29           N  
ANISOU 4435  N   VAL B 140    10101   8256   6830  -2833    634    -59       N  
ATOM   4436  CA  VAL B 140      -7.668  12.832  41.064  1.00 67.27           C  
ANISOU 4436  CA  VAL B 140    10438   8282   6841  -3135    729    -11       C  
ATOM   4437  C   VAL B 140      -7.232  12.346  39.652  1.00 71.98           C  
ANISOU 4437  C   VAL B 140    10975   9037   7338  -3215    813     39       C  
ATOM   4438  O   VAL B 140      -7.463  13.060  38.675  1.00 72.54           O  
ANISOU 4438  O   VAL B 140    11305   8947   7310  -3313    858    153       O  
ATOM   4439  CB  VAL B 140      -6.567  13.602  41.846  1.00 71.75           C  
ANISOU 4439  CB  VAL B 140    10978   8894   7390  -3437    786   -121       C  
ATOM   4440  CG1 VAL B 140      -5.901  14.669  40.981  1.00 73.84           C  
ANISOU 4440  CG1 VAL B 140    11458   9065   7532  -3786    908    -72       C  
ATOM   4441  CG2 VAL B 140      -7.158  14.255  43.093  1.00 71.30           C  
ANISOU 4441  CG2 VAL B 140    11065   8622   7405  -3356    705   -155       C  
ATOM   4442  N   HIS B 141      -6.675  11.121  39.540  1.00 68.10           N  
ANISOU 4442  N   HIS B 141    10164   8845   6866  -3144    832    -40       N  
ATOM   4443  CA  HIS B 141      -6.301  10.504  38.262  1.00 69.13           C  
ANISOU 4443  CA  HIS B 141    10216   9146   6906  -3177    911    -14       C  
ATOM   4444  C   HIS B 141      -7.542  10.401  37.374  1.00 72.46           C  
ANISOU 4444  C   HIS B 141    10843   9391   7298  -2983    850    115       C  
ATOM   4445  O   HIS B 141      -7.466  10.648  36.171  1.00 73.39           O  
ANISOU 4445  O   HIS B 141    11094   9499   7290  -3083    914    194       O  
ATOM   4446  CB  HIS B 141      -5.762   9.081  38.490  1.00 69.43           C  
ANISOU 4446  CB  HIS B 141     9894   9489   6995  -3036    914   -126       C  
ATOM   4447  CG  HIS B 141      -4.276   8.965  38.446  1.00 74.90           C  
ANISOU 4447  CG  HIS B 141    10351  10476   7632  -3258   1027   -231       C  
ATOM   4448  ND1 HIS B 141      -3.493   9.297  39.537  1.00 77.45           N  
ANISOU 4448  ND1 HIS B 141    10529  10906   7994  -3386   1026   -334       N  
ATOM   4449  CD2 HIS B 141      -3.474   8.543  37.441  1.00 77.84           C  
ANISOU 4449  CD2 HIS B 141    10596  11072   7907  -3363   1142   -253       C  
ATOM   4450  CE1 HIS B 141      -2.244   9.081  39.156  1.00 78.51           C  
ANISOU 4450  CE1 HIS B 141    10439  11335   8057  -3568   1136   -415       C  
ATOM   4451  NE2 HIS B 141      -2.185   8.639  37.898  1.00 79.12           N  
ANISOU 4451  NE2 HIS B 141    10522  11488   8051  -3560   1216   -368       N  
ATOM   4452  N   LEU B 142      -8.695  10.057  37.984  1.00 66.74           N  
ANISOU 4452  N   LEU B 142    10139   8539   6679  -2709    725    133       N  
ATOM   4453  CA  LEU B 142      -9.961   9.912  37.274  1.00 65.45           C  
ANISOU 4453  CA  LEU B 142    10130   8238   6500  -2504    646    238       C  
ATOM   4454  C   LEU B 142     -10.591  11.284  36.944  1.00 71.97           C  
ANISOU 4454  C   LEU B 142    11314   8774   7255  -2552    625    371       C  
ATOM   4455  O   LEU B 142     -11.524  11.355  36.154  1.00 70.98           O  
ANISOU 4455  O   LEU B 142    11344   8549   7077  -2413    566    474       O  
ATOM   4456  CB  LEU B 142     -10.918   8.948  38.018  1.00 62.58           C  
ANISOU 4456  CB  LEU B 142     9621   7883   6274  -2209    535    199       C  
ATOM   4457  CG  LEU B 142     -10.389   7.505  38.233  1.00 63.94           C  
ANISOU 4457  CG  LEU B 142     9482   8307   6504  -2128    558     86       C  
ATOM   4458  CD1 LEU B 142     -11.219   6.755  39.232  1.00 61.36           C  
ANISOU 4458  CD1 LEU B 142     9045   7951   6317  -1886    469     49       C  
ATOM   4459  CD2 LEU B 142     -10.244   6.742  36.934  1.00 64.06           C  
ANISOU 4459  CD2 LEU B 142     9447   8461   6431  -2125    603     91       C  
ATOM   4460  N   CYS B 143     -10.023  12.376  37.495  1.00 71.97           N  
ANISOU 4460  N   CYS B 143    11455   8648   7244  -2759    677    364       N  
ATOM   4461  CA  CYS B 143     -10.398  13.760  37.168  1.00 73.39           C  
ANISOU 4461  CA  CYS B 143    12012   8533   7343  -2845    687    486       C  
ATOM   4462  C   CYS B 143      -9.516  14.215  36.000  1.00 80.11           C  
ANISOU 4462  C   CYS B 143    12982   9425   8031  -3128    820    545       C  
ATOM   4463  O   CYS B 143     -10.014  14.882  35.093  1.00 82.39           O  
ANISOU 4463  O   CYS B 143    13564   9536   8205  -3121    823    689       O  
ATOM   4464  CB  CYS B 143     -10.256  14.679  38.374  1.00 73.68           C  
ANISOU 4464  CB  CYS B 143    12160   8390   7446  -2933    683    436       C  
ATOM   4465  SG  CYS B 143     -11.520  14.419  39.637  1.00 75.25           S  
ANISOU 4465  SG  CYS B 143    12314   8476   7802  -2583    536    404       S  
ATOM   4466  N   ALA B 144      -8.218  13.800  36.001  1.00 75.30           N  
ANISOU 4466  N   ALA B 144    12133   9073   7403  -3360    930    437       N  
ATOM   4467  CA  ALA B 144      -7.240  14.079  34.945  1.00 76.21           C  
ANISOU 4467  CA  ALA B 144    12292   9297   7367  -3649   1080    468       C  
ATOM   4468  C   ALA B 144      -7.604  13.352  33.637  1.00 77.85           C  
ANISOU 4468  C   ALA B 144    12489   9618   7472  -3520   1081    542       C  
ATOM   4469  O   ALA B 144      -7.498  13.947  32.560  1.00 79.35           O  
ANISOU 4469  O   ALA B 144    12912   9734   7503  -3659   1160    657       O  
ATOM   4470  CB  ALA B 144      -5.856  13.662  35.399  1.00 77.13           C  
ANISOU 4470  CB  ALA B 144    12087   9711   7509  -3872   1179    312       C  
ATOM   4471  N   ILE B 145      -8.020  12.068  33.738  1.00 70.78           N  
ANISOU 4471  N   ILE B 145    11338   8897   6659  -3263    999    472       N  
ATOM   4472  CA  ILE B 145      -8.452  11.256  32.600  1.00 69.55           C  
ANISOU 4472  CA  ILE B 145    11155   8854   6418  -3119    981    513       C  
ATOM   4473  C   ILE B 145      -9.756  11.830  32.074  1.00 75.48           C  
ANISOU 4473  C   ILE B 145    12212   9356   7112  -2947    874    666       C  
ATOM   4474  O   ILE B 145      -9.845  12.110  30.890  1.00 76.72           O  
ANISOU 4474  O   ILE B 145    12552   9495   7103  -2996    911    771       O  
ATOM   4475  CB  ILE B 145      -8.598   9.751  32.931  1.00 69.41           C  
ANISOU 4475  CB  ILE B 145    10811   9050   6512  -2897    922    389       C  
ATOM   4476  CG1 ILE B 145      -7.237   9.123  33.236  1.00 69.84           C  
ANISOU 4476  CG1 ILE B 145    10562   9385   6588  -3040   1037    248       C  
ATOM   4477  CG2 ILE B 145      -9.243   9.037  31.754  1.00 69.80           C  
ANISOU 4477  CG2 ILE B 145    10890   9163   6468  -2748    886    432       C  
ATOM   4478  CD1 ILE B 145      -7.241   7.916  34.180  1.00 74.33           C  
ANISOU 4478  CD1 ILE B 145    10832  10098   7311  -2834    975    118       C  
ATOM   4479  N   SER B 146     -10.767  12.006  32.950  1.00 72.65           N  
ANISOU 4479  N   SER B 146    11903   8822   6880  -2733    741    680       N  
ATOM   4480  CA  SER B 146     -12.064  12.559  32.560  1.00 72.55           C  
ANISOU 4480  CA  SER B 146    12152   8591   6823  -2531    625    817       C  
ATOM   4481  C   SER B 146     -11.864  13.848  31.804  1.00 78.01           C  
ANISOU 4481  C   SER B 146    13209   9085   7348  -2702    696    966       C  
ATOM   4482  O   SER B 146     -12.368  13.953  30.691  1.00 78.58           O  
ANISOU 4482  O   SER B 146    13449   9135   7274  -2627    668   1082       O  
ATOM   4483  CB  SER B 146     -12.963  12.784  33.772  1.00 74.26           C  
ANISOU 4483  CB  SER B 146    12374   8643   7198  -2326    508    800       C  
ATOM   4484  OG  SER B 146     -12.427  13.784  34.620  1.00 83.05           O  
ANISOU 4484  OG  SER B 146    13616   9590   8349  -2493    567    788       O  
ATOM   4485  N   LEU B 147     -11.056  14.787  32.360  1.00 75.54           N  
ANISOU 4485  N   LEU B 147    13016   8644   7041  -2953    798    957       N  
ATOM   4486  CA  LEU B 147     -10.764  16.078  31.728  1.00 77.71           C  
ANISOU 4486  CA  LEU B 147    13670   8696   7161  -3161    893   1096       C  
ATOM   4487  C   LEU B 147      -9.947  15.969  30.459  1.00 84.71           C  
ANISOU 4487  C   LEU B 147    14585   9739   7862  -3384   1029   1144       C  
ATOM   4488  O   LEU B 147     -10.131  16.806  29.587  1.00 86.84           O  
ANISOU 4488  O   LEU B 147    15197   9832   7965  -3442   1068   1306       O  
ATOM   4489  CB  LEU B 147     -10.138  17.063  32.698  1.00 78.38           C  
ANISOU 4489  CB  LEU B 147    13874   8599   7307  -3391    967   1053       C  
ATOM   4490  CG  LEU B 147     -11.160  17.772  33.567  1.00 82.40           C  
ANISOU 4490  CG  LEU B 147    14590   8808   7911  -3175    851   1093       C  
ATOM   4491  CD1 LEU B 147     -10.528  18.295  34.800  1.00 82.50           C  
ANISOU 4491  CD1 LEU B 147    14579   8736   8029  -3362    899    975       C  
ATOM   4492  CD2 LEU B 147     -11.884  18.884  32.799  1.00 88.13           C  
ANISOU 4492  CD2 LEU B 147    15776   9214   8494  -3098    835   1296       C  
ATOM   4493  N   ASP B 148      -9.114  14.918  30.314  1.00 82.04           N  
ANISOU 4493  N   ASP B 148    13901   9729   7540  -3476   1100   1013       N  
ATOM   4494  CA  ASP B 148      -8.350  14.660  29.090  1.00 84.30           C  
ANISOU 4494  CA  ASP B 148    14171  10210   7648  -3660   1236   1039       C  
ATOM   4495  C   ASP B 148      -9.295  14.293  27.942  1.00 89.06           C  
ANISOU 4495  C   ASP B 148    14900  10821   8118  -3429   1147   1150       C  
ATOM   4496  O   ASP B 148      -9.171  14.873  26.864  1.00 92.33           O  
ANISOU 4496  O   ASP B 148    15576  11178   8329  -3546   1225   1285       O  
ATOM   4497  CB  ASP B 148      -7.283  13.561  29.289  1.00 85.37           C  
ANISOU 4497  CB  ASP B 148    13888  10706   7844  -3762   1324    856       C  
ATOM   4498  CG  ASP B 148      -6.552  13.180  28.009  1.00 98.76           C  
ANISOU 4498  CG  ASP B 148    15540  12629   9354  -3913   1467    867       C  
ATOM   4499  OD1 ASP B 148      -5.866  14.065  27.423  1.00102.75           O  
ANISOU 4499  OD1 ASP B 148    16246  13084   9709  -4208   1619    950       O  
ATOM   4500  OD2 ASP B 148      -6.675  12.011  27.583  1.00101.01           O1-
ANISOU 4500  OD2 ASP B 148    15609  13135   9636  -3743   1434    793       O1-
ATOM   4501  N   ARG B 149     -10.244  13.358  28.181  1.00 82.92           N  
ANISOU 4501  N   ARG B 149    13946  10115   7446  -3114    985   1093       N  
ATOM   4502  CA  ARG B 149     -11.255  12.916  27.210  1.00 83.34           C  
ANISOU 4502  CA  ARG B 149    14074  10200   7390  -2876    869   1170       C  
ATOM   4503  C   ARG B 149     -12.134  14.093  26.795  1.00 94.24           C  
ANISOU 4503  C   ARG B 149    15858  11293   8654  -2781    794   1370       C  
ATOM   4504  O   ARG B 149     -12.559  14.145  25.643  1.00 96.01           O  
ANISOU 4504  O   ARG B 149    16252  11538   8689  -2708    764   1481       O  
ATOM   4505  CB  ARG B 149     -12.147  11.795  27.775  1.00 78.25           C  
ANISOU 4505  CB  ARG B 149    13165   9655   6912  -2585    710   1059       C  
ATOM   4506  CG  ARG B 149     -11.411  10.563  28.285  1.00 88.10           C  
ANISOU 4506  CG  ARG B 149    14033  11153   8287  -2620    766    868       C  
ATOM   4507  CD  ARG B 149     -10.906   9.673  27.172  1.00103.11           C  
ANISOU 4507  CD  ARG B 149    15820  13304  10052  -2671    844    814       C  
ATOM   4508  NE  ARG B 149     -10.039   8.609  27.683  1.00110.89           N  
ANISOU 4508  NE  ARG B 149    16468  14514  11150  -2710    921    636       N  
ATOM   4509  CZ  ARG B 149      -9.217   7.892  26.923  1.00122.92           C  
ANISOU 4509  CZ  ARG B 149    17857  16274  12573  -2801   1039    558       C  
ATOM   4510  NH1 ARG B 149      -9.141   8.119  25.617  1.00113.80           N1+
ANISOU 4510  NH1 ARG B 149    16874  15167  11198  -2881   1098    639       N1+
ATOM   4511  NH2 ARG B 149      -8.456   6.948  27.465  1.00 96.76           N  
ANISOU 4511  NH2 ARG B 149    14242  13152   9368  -2800   1102    401       N  
ATOM   4512  N   TYR B 150     -12.389  15.042  27.725  1.00 94.32           N  
ANISOU 4512  N   TYR B 150    16034  11038   8766  -2770    766   1413       N  
ATOM   4513  CA  TYR B 150     -13.179  16.252  27.475  1.00 98.10           C  
ANISOU 4513  CA  TYR B 150    16921  11206   9148  -2662    704   1602       C  
ATOM   4514  C   TYR B 150     -12.488  17.171  26.463  1.00105.73           C  
ANISOU 4514  C   TYR B 150    18227  12064   9883  -2918    857   1752       C  
ATOM   4515  O   TYR B 150     -13.151  17.606  25.523  1.00107.12           O  
ANISOU 4515  O   TYR B 150    18682  12140   9878  -2782    799   1920       O  
ATOM   4516  CB  TYR B 150     -13.510  16.996  28.783  1.00100.49           C  
ANISOU 4516  CB  TYR B 150    17310  11251   9619  -2601    659   1585       C  
ATOM   4517  CG  TYR B 150     -14.198  18.328  28.575  1.00107.10           C  
ANISOU 4517  CG  TYR B 150    18600  11738  10356  -2498    620   1775       C  
ATOM   4518  CD1 TYR B 150     -15.514  18.394  28.128  1.00110.03           C  
ANISOU 4518  CD1 TYR B 150    19094  12046  10668  -2144    450   1889       C  
ATOM   4519  CD2 TYR B 150     -13.536  19.523  28.835  1.00110.88           C  
ANISOU 4519  CD2 TYR B 150    19387  11947  10796  -2749    752   1837       C  
ATOM   4520  CE1 TYR B 150     -16.152  19.621  27.936  1.00114.72           C  
ANISOU 4520  CE1 TYR B 150    20112  12314  11160  -2010    410   2071       C  
ATOM   4521  CE2 TYR B 150     -14.162  20.755  28.644  1.00114.74           C  
ANISOU 4521  CE2 TYR B 150    20329  12080  11188  -2638    724   2016       C  
ATOM   4522  CZ  TYR B 150     -15.470  20.801  28.194  1.00124.86           C  
ANISOU 4522  CZ  TYR B 150    21732  13302  12407  -2251    552   2138       C  
ATOM   4523  OH  TYR B 150     -16.080  22.020  28.011  1.00131.18           O  
ANISOU 4523  OH  TYR B 150    22987  13749  13105  -2109    523   2320       O  
ATOM   4524  N   TRP B 151     -11.163  17.440  26.632  1.00103.35           N  
ANISOU 4524  N   TRP B 151    17893  11801   9575  -3289   1052   1693       N  
ATOM   4525  CA  TRP B 151     -10.403  18.258  25.678  1.00106.62           C  
ANISOU 4525  CA  TRP B 151    18608  12134   9768  -3583   1228   1826       C  
ATOM   4526  C   TRP B 151     -10.272  17.518  24.343  1.00109.14           C  
ANISOU 4526  C   TRP B 151    18857  12717   9893  -3573   1262   1857       C  
ATOM   4527  O   TRP B 151     -10.166  18.176  23.310  1.00112.05           O  
ANISOU 4527  O   TRP B 151    19550  12993  10031  -3676   1345   2026       O  
ATOM   4528  CB  TRP B 151      -8.999  18.642  26.187  1.00107.00           C  
ANISOU 4528  CB  TRP B 151    18583  12210   9860  -4004   1433   1731       C  
ATOM   4529  CG  TRP B 151      -8.905  19.098  27.613  1.00107.74           C  
ANISOU 4529  CG  TRP B 151    18636  12139  10160  -4054   1408   1632       C  
ATOM   4530  CD1 TRP B 151      -8.064  18.604  28.569  1.00109.41           C  
ANISOU 4530  CD1 TRP B 151    18493  12543  10534  -4214   1458   1433       C  
ATOM   4531  CD2 TRP B 151      -9.597  20.201  28.219  1.00108.81           C  
ANISOU 4531  CD2 TRP B 151    19118  11884  10340  -3959   1341   1726       C  
ATOM   4532  NE1 TRP B 151      -8.235  19.289  29.751  1.00108.85           N  
ANISOU 4532  NE1 TRP B 151    18515  12237  10606  -4222   1414   1391       N  
ATOM   4533  CE2 TRP B 151      -9.163  20.281  29.562  1.00111.94           C  
ANISOU 4533  CE2 TRP B 151    19339  12261  10931  -4072   1349   1564       C  
ATOM   4534  CE3 TRP B 151     -10.569  21.111  27.769  1.00112.00           C  
ANISOU 4534  CE3 TRP B 151    19964  11958  10633  -3763   1267   1929       C  
ATOM   4535  CZ2 TRP B 151      -9.671  21.231  30.458  1.00112.07           C  
ANISOU 4535  CZ2 TRP B 151    19613  11933  11035  -4005   1294   1588       C  
ATOM   4536  CZ3 TRP B 151     -11.056  22.064  28.652  1.00114.27           C  
ANISOU 4536  CZ3 TRP B 151    20509  11897  11012  -3686   1218   1959       C  
ATOM   4537  CH2 TRP B 151     -10.617  22.111  29.981  1.00113.79           C  
ANISOU 4537  CH2 TRP B 151    20270  11819  11147  -3810   1233   1784       C  
ATOM   4538  N   SER B 152     -10.265  16.154  24.370  1.00101.25           N  
ANISOU 4538  N   SER B 152    17454  12038   8980  -3452   1206   1694       N  
ATOM   4539  CA  SER B 152     -10.190  15.287  23.182  1.00100.83           C  
ANISOU 4539  CA  SER B 152    17297  12254   8759  -3414   1225   1684       C  
ATOM   4540  C   SER B 152     -11.451  15.492  22.325  1.00106.00           C  
ANISOU 4540  C   SER B 152    18213  12807   9256  -3128   1060   1846       C  
ATOM   4541  O   SER B 152     -11.358  15.666  21.105  1.00106.73           O  
ANISOU 4541  O   SER B 152    18506  12950   9097  -3182   1117   1963       O  
ATOM   4542  CB  SER B 152     -10.077  13.816  23.585  1.00 99.28           C  
ANISOU 4542  CB  SER B 152    16645  12356   8720  -3301   1176   1467       C  
ATOM   4543  OG  SER B 152      -8.984  13.573  24.455  1.00102.56           O  
ANISOU 4543  OG  SER B 152    16795  12886   9287  -3511   1300   1314       O  
ATOM   4544  N   VAL B 153     -12.620  15.515  23.006  1.00101.91           N  
ANISOU 4544  N   VAL B 153    17690  12153   8881  -2826    858   1853       N  
ATOM   4545  CA  VAL B 153     -13.971  15.690  22.472  1.00102.05           C  
ANISOU 4545  CA  VAL B 153    17890  12085   8798  -2500    662   1982       C  
ATOM   4546  C   VAL B 153     -14.225  17.154  22.024  1.00109.63           C  
ANISOU 4546  C   VAL B 153    19349  12727   9580  -2505    681   2226       C  
ATOM   4547  O   VAL B 153     -14.609  17.367  20.871  1.00110.69           O  
ANISOU 4547  O   VAL B 153    19712  12876   9468  -2417    643   2373       O  
ATOM   4548  CB  VAL B 153     -15.005  15.149  23.504  1.00102.33           C  
ANISOU 4548  CB  VAL B 153    17687  12120   9075  -2206    467   1875       C  
ATOM   4549  CG1 VAL B 153     -16.397  15.712  23.276  1.00103.10           C  
ANISOU 4549  CG1 VAL B 153    18006  12062   9106  -1877    271   2023       C  
ATOM   4550  CG2 VAL B 153     -15.036  13.624  23.502  1.00 99.33           C  
ANISOU 4550  CG2 VAL B 153    16897  12056   8789  -2141    420   1680       C  
ATOM   4551  N   THR B 154     -13.990  18.143  22.924  1.00107.96           N  
ANISOU 4551  N   THR B 154    19316  12225   9479  -2608    742   2265       N  
ATOM   4552  CA  THR B 154     -14.157  19.585  22.673  1.00111.62           C  
ANISOU 4552  CA  THR B 154    20281  12328   9801  -2629    782   2485       C  
ATOM   4553  C   THR B 154     -13.234  20.062  21.522  1.00119.70           C  
ANISOU 4553  C   THR B 154    21573  13350  10557  -2934    981   2616       C  
ATOM   4554  O   THR B 154     -13.692  20.166  20.382  1.00120.40           O  
ANISOU 4554  O   THR B 154    21876  13465  10404  -2805    932   2770       O  
ATOM   4555  CB  THR B 154     -13.981  20.381  23.989  1.00119.54           C  
ANISOU 4555  CB  THR B 154    21370  13045  11005  -2712    822   2445       C  
ATOM   4556  OG1 THR B 154     -14.832  19.820  24.982  1.00117.74           O  
ANISOU 4556  OG1 THR B 154    20867  12865  11004  -2425    647   2320       O  
ATOM   4557  CG2 THR B 154     -14.288  21.866  23.835  1.00122.87           C  
ANISOU 4557  CG2 THR B 154    22335  13047  11301  -2688    848   2664       C  
ATOM   4558  N   GLN B 155     -11.945  20.323  21.827  1.00118.43           N  
ANISOU 4558  N   GLN B 155    21384  13182  10432  -3340   1205   2549       N  
ATOM   4559  CA  GLN B 155     -10.966  20.757  20.842  1.00122.09           C  
ANISOU 4559  CA  GLN B 155    22065  13664  10661  -3679   1426   2653       C  
ATOM   4560  C   GLN B 155     -10.317  19.520  20.239  1.00126.82           C  
ANISOU 4560  C   GLN B 155    22283  14693  11211  -3782   1495   2508       C  
ATOM   4561  O   GLN B 155      -9.275  19.035  20.699  1.00125.09           O  
ANISOU 4561  O   GLN B 155    21751  14669  11109  -4042   1634   2334       O  
ATOM   4562  CB  GLN B 155      -9.964  21.746  21.450  1.00125.32           C  
ANISOU 4562  CB  GLN B 155    22653  13842  11122  -4074   1632   2657       C  
ATOM   4563  CG  GLN B 155      -9.016  22.397  20.444  1.00144.93           C  
ANISOU 4563  CG  GLN B 155    25430  16288  13349  -4449   1879   2795       C  
ATOM   4564  CD  GLN B 155      -9.674  23.368  19.496  1.00165.88           C  
ANISOU 4564  CD  GLN B 155    28642  18644  15740  -4323   1861   3083       C  
ATOM   4565  OE1 GLN B 155     -10.181  22.986  18.430  1.00162.10           O  
ANISOU 4565  OE1 GLN B 155    28226  18308  15056  -4120   1785   3187       O  
ATOM   4566  NE2 GLN B 155      -9.645  24.652  19.846  1.00156.92           N  
ANISOU 4566  NE2 GLN B 155    27943  17088  14593  -4448   1936   3216       N  
ATOM   4567  N   ALA B 156     -11.001  18.999  19.213  1.00125.42           N  
ANISOU 4567  N   ALA B 156    22132  14668  10856  -3545   1383   2576       N  
ATOM   4568  CA  ALA B 156     -10.695  17.786  18.473  1.00124.90           C  
ANISOU 4568  CA  ALA B 156    21760  14989  10707  -3547   1404   2454       C  
ATOM   4569  C   ALA B 156      -9.246  17.662  17.974  1.00131.81           C  
ANISOU 4569  C   ALA B 156    22552  16059  11470  -3950   1680   2400       C  
ATOM   4570  O   ALA B 156      -8.551  16.756  18.432  1.00129.14           O  
ANISOU 4570  O   ALA B 156    21804  15979  11283  -4050   1744   2186       O  
ATOM   4571  CB  ALA B 156     -11.677  17.622  17.322  1.00126.79           C  
ANISOU 4571  CB  ALA B 156    22182  15287  10708  -3266   1251   2586       C  
ATOM   4572  N   VAL B 157      -8.785  18.561  17.073  1.00133.47           N  
ANISOU 4572  N   VAL B 157    23143  16152  11417  -4174   1848   2591       N  
ATOM   4573  CA  VAL B 157      -7.451  18.464  16.462  1.00135.91           C  
ANISOU 4573  CA  VAL B 157    23382  16673  11585  -4559   2124   2553       C  
ATOM   4574  C   VAL B 157      -6.371  19.339  17.159  1.00142.95           C  
ANISOU 4574  C   VAL B 157    24334  17412  12568  -4973   2343   2543       C  
ATOM   4575  O   VAL B 157      -5.265  18.838  17.387  1.00142.44           O  
ANISOU 4575  O   VAL B 157    23933  17612  12576  -5236   2509   2371       O  
ATOM   4576  CB  VAL B 157      -7.507  18.697  14.919  1.00143.00           C  
ANISOU 4576  CB  VAL B 157    24604  17622  12108  -4580   2201   2743       C  
ATOM   4577  CG1 VAL B 157      -7.949  20.114  14.547  1.00146.14           C  
ANISOU 4577  CG1 VAL B 157    25587  17619  12322  -4593   2212   3036       C  
ATOM   4578  CG2 VAL B 157      -6.198  18.316  14.229  1.00144.47           C  
ANISOU 4578  CG2 VAL B 157    24633  18114  12146  -4929   2477   2666       C  
ATOM   4579  N   GLU B 158      -6.679  20.609  17.488  1.00142.08           N  
ANISOU 4579  N   GLU B 158    24640  16892  12451  -5028   2342   2715       N  
ATOM   4580  CA  GLU B 158      -5.726  21.527  18.120  1.00144.09           C  
ANISOU 4580  CA  GLU B 158    25004  16966  12778  -5440   2544   2708       C  
ATOM   4581  C   GLU B 158      -5.193  21.018  19.464  1.00144.72           C  
ANISOU 4581  C   GLU B 158    24629  17185  13173  -5528   2530   2449       C  
ATOM   4582  O   GLU B 158      -4.016  21.220  19.761  1.00145.08           O  
ANISOU 4582  O   GLU B 158    24537  17333  13255  -5926   2736   2352       O  
ATOM   4583  CB  GLU B 158      -6.331  22.936  18.245  1.00148.22           C  
ANISOU 4583  CB  GLU B 158    26094  16984  13241  -5417   2516   2937       C  
ATOM   4584  CG  GLU B 158      -5.330  24.057  18.479  1.00162.84           C  
ANISOU 4584  CG  GLU B 158    28205  18606  15062  -5904   2771   2989       C  
ATOM   4585  CD  GLU B 158      -5.939  25.446  18.501  1.00178.73           C  
ANISOU 4585  CD  GLU B 158    30834  20085  16990  -5869   2756   3226       C  
ATOM   4586  OE1 GLU B 158      -6.663  25.763  19.473  1.00170.29           O1-
ANISOU 4586  OE1 GLU B 158    29824  18763  16115  -5641   2586   3199       O1-
ATOM   4587  OE2 GLU B 158      -5.690  26.218  17.547  1.00166.61           O  
ANISOU 4587  OE2 GLU B 158    29736  18380  15187  -6062   2922   3443       O  
ATOM   4588  N   TYR B 159      -6.036  20.356  20.268  1.00138.42           N  
ANISOU 4588  N   TYR B 159    23591  16409  12592  -5167   2292   2336       N  
ATOM   4589  CA  TYR B 159      -5.567  19.860  21.563  1.00136.22           C  
ANISOU 4589  CA  TYR B 159    22900  16261  12598  -5226   2269   2101       C  
ATOM   4590  C   TYR B 159      -5.293  18.334  21.528  1.00134.68           C  
ANISOU 4590  C   TYR B 159    22182  16507  12483  -5096   2232   1896       C  
ATOM   4591  O   TYR B 159      -5.179  17.695  22.575  1.00130.71           O  
ANISOU 4591  O   TYR B 159    21321  16127  12215  -5018   2155   1709       O  
ATOM   4592  CB  TYR B 159      -6.495  20.307  22.725  1.00137.19           C  
ANISOU 4592  CB  TYR B 159    23124  16074  12930  -4987   2075   2101       C  
ATOM   4593  CG  TYR B 159      -6.582  21.816  22.933  1.00143.96           C  
ANISOU 4593  CG  TYR B 159    24477  16484  13735  -5150   2139   2264       C  
ATOM   4594  CD1 TYR B 159      -5.798  22.698  22.186  1.00150.10           C  
ANISOU 4594  CD1 TYR B 159    25579  17147  14306  -5529   2369   2398       C  
ATOM   4595  CD2 TYR B 159      -7.448  22.362  23.882  1.00144.34           C  
ANISOU 4595  CD2 TYR B 159    24688  16217  13938  -4927   1980   2283       C  
ATOM   4596  CE1 TYR B 159      -5.907  24.079  22.340  1.00154.33           C  
ANISOU 4596  CE1 TYR B 159    26615  17238  14786  -5677   2435   2555       C  
ATOM   4597  CE2 TYR B 159      -7.560  23.745  24.050  1.00148.48           C  
ANISOU 4597  CE2 TYR B 159    25702  16305  14409  -5053   2041   2431       C  
ATOM   4598  CZ  TYR B 159      -6.781  24.600  23.281  1.00160.31           C  
ANISOU 4598  CZ  TYR B 159    27541  17670  15701  -5432   2269   2567       C  
ATOM   4599  OH  TYR B 159      -6.862  25.965  23.442  1.00163.99           O  
ANISOU 4599  OH  TYR B 159    28523  17676  16111  -5574   2343   2713       O  
ATOM   4600  N   ASN B 160      -5.116  17.785  20.301  1.00131.27           N  
ANISOU 4600  N   ASN B 160    21730  16308  11839  -5091   2305   1932       N  
ATOM   4601  CA  ASN B 160      -4.743  16.389  20.026  1.00128.47           C  
ANISOU 4601  CA  ASN B 160    20944  16364  11506  -5001   2313   1750       C  
ATOM   4602  C   ASN B 160      -3.226  16.345  19.801  1.00131.94           C  
ANISOU 4602  C   ASN B 160    21185  17068  11879  -5401   2587   1655       C  
ATOM   4603  O   ASN B 160      -2.566  15.390  20.219  1.00129.98           O  
ANISOU 4603  O   ASN B 160    20501  17130  11757  -5407   2623   1448       O  
ATOM   4604  CB  ASN B 160      -5.472  15.844  18.796  1.00129.03           C  
ANISOU 4604  CB  ASN B 160    21126  16532  11366  -4757   2231   1834       C  
ATOM   4605  CG  ASN B 160      -5.147  14.403  18.488  1.00150.66           C  
ANISOU 4605  CG  ASN B 160    23462  19661  14123  -4651   2240   1640       C  
ATOM   4606  OD1 ASN B 160      -5.649  13.477  19.133  1.00149.31           O  
ANISOU 4606  OD1 ASN B 160    23013  19571  14146  -4393   2077   1495       O  
ATOM   4607  ND2 ASN B 160      -4.291  14.182  17.502  1.00141.09           N  
ANISOU 4607  ND2 ASN B 160    22217  18689  12701  -4851   2441   1630       N  
ATOM   4608  N   LEU B 161      -2.682  17.388  19.135  1.00129.92           N  
ANISOU 4608  N   LEU B 161    21256  16689  11418  -5731   2784   1812       N  
ATOM   4609  CA  LEU B 161      -1.252  17.569  18.893  1.00131.47           C  
ANISOU 4609  CA  LEU B 161    21311  17110  11531  -6165   3067   1747       C  
ATOM   4610  C   LEU B 161      -0.555  17.840  20.235  1.00132.83           C  
ANISOU 4610  C   LEU B 161    21243  17278  11946  -6379   3100   1594       C  
ATOM   4611  O   LEU B 161       0.577  17.396  20.439  1.00133.24           O  
ANISOU 4611  O   LEU B 161    20920  17662  12042  -6602   3251   1424       O  
ATOM   4612  CB  LEU B 161      -1.034  18.751  17.936  1.00135.87           C  
ANISOU 4612  CB  LEU B 161    22351  17458  11815  -6458   3254   1981       C  
ATOM   4613  CG  LEU B 161      -0.904  18.424  16.445  1.00142.75           C  
ANISOU 4613  CG  LEU B 161    23331  18528  12381  -6465   3375   2076       C  
ATOM   4614  CD1 LEU B 161      -2.257  18.106  15.809  1.00141.42           C  
ANISOU 4614  CD1 LEU B 161    23385  18242  12106  -6029   3143   2200       C  
ATOM   4615  CD2 LEU B 161      -0.286  19.577  15.710  1.00150.64           C  
ANISOU 4615  CD2 LEU B 161    24721  19379  13136  -6872   3630   2266       C  
ATOM   4616  N   LYS B 162      -1.264  18.544  21.157  1.00125.99           N  
ANISOU 4616  N   LYS B 162    20585  16050  11233  -6287   2948   1646       N  
ATOM   4617  CA  LYS B 162      -0.830  18.887  22.513  1.00123.52           C  
ANISOU 4617  CA  LYS B 162    20110  15674  11150  -6444   2934   1511       C  
ATOM   4618  C   LYS B 162      -0.597  17.648  23.381  1.00120.66           C  
ANISOU 4618  C   LYS B 162    19200  15639  11006  -6251   2829   1268       C  
ATOM   4619  O   LYS B 162       0.335  17.654  24.186  1.00121.07           O  
ANISOU 4619  O   LYS B 162    18969  15854  11177  -6484   2908   1110       O  
ATOM   4620  CB  LYS B 162      -1.838  19.830  23.189  1.00125.44           C  
ANISOU 4620  CB  LYS B 162    20734  15445  11482  -6306   2776   1631       C  
ATOM   4621  CG  LYS B 162      -1.476  21.303  23.057  1.00145.19           C  
ANISOU 4621  CG  LYS B 162    23684  17611  13869  -6685   2940   1778       C  
ATOM   4622  CD  LYS B 162      -2.159  22.136  24.132  1.00155.40           C  
ANISOU 4622  CD  LYS B 162    25228  18495  15321  -6596   2803   1804       C  
ATOM   4623  CE  LYS B 162      -1.493  23.475  24.338  1.00169.88           C  
ANISOU 4623  CE  LYS B 162    27396  20047  17103  -7053   2988   1861       C  
ATOM   4624  NZ  LYS B 162      -2.052  24.188  25.518  1.00177.53           N1+
ANISOU 4624  NZ  LYS B 162    28554  20653  18247  -6971   2858   1837       N1+
ATOM   4625  N   ARG B 163      -1.434  16.594  23.224  1.00110.83           N  
ANISOU 4625  N   ARG B 163    17815  14490   9808  -5832   2651   1237       N  
ATOM   4626  CA  ARG B 163      -1.307  15.340  23.978  1.00105.80           C  
ANISOU 4626  CA  ARG B 163    16701  14134   9366  -5612   2549   1024       C  
ATOM   4627  C   ARG B 163       0.005  14.639  23.578  1.00108.82           C  
ANISOU 4627  C   ARG B 163    16710  14954   9683  -5811   2746    877       C  
ATOM   4628  O   ARG B 163       0.052  13.896  22.596  1.00109.76           O  
ANISOU 4628  O   ARG B 163    16756  15283   9667  -5707   2797    873       O  
ATOM   4629  CB  ARG B 163      -2.534  14.433  23.761  1.00101.49           C  
ANISOU 4629  CB  ARG B 163    16144  13561   8856  -5157   2336   1040       C  
ATOM   4630  CG  ARG B 163      -2.566  13.232  24.697  1.00108.47           C  
ANISOU 4630  CG  ARG B 163    16606  14647   9962  -4913   2215    841       C  
ATOM   4631  CD  ARG B 163      -3.299  12.049  24.113  1.00119.53           C  
ANISOU 4631  CD  ARG B 163    17905  16171  11341  -4572   2100    809       C  
ATOM   4632  NE  ARG B 163      -4.747  12.253  24.104  1.00129.79           N  
ANISOU 4632  NE  ARG B 163    19464  17188  12661  -4294   1895    930       N  
ATOM   4633  CZ  ARG B 163      -5.486  12.327  23.001  1.00147.07           C  
ANISOU 4633  CZ  ARG B 163    21906  19306  14668  -4177   1849   1063       C  
ATOM   4634  NH1 ARG B 163      -4.924  12.191  21.804  1.00129.91           N1+
ANISOU 4634  NH1 ARG B 163    19778  17311  12272  -4314   1998   1093       N1+
ATOM   4635  NH2 ARG B 163      -6.794  12.519  23.086  1.00137.29           N  
ANISOU 4635  NH2 ARG B 163    20864  17840  13460  -3915   1652   1160       N  
ATOM   4636  N   THR B 164       1.074  14.922  24.327  1.00103.72           N  
ANISOU 4636  N   THR B 164    15834  14451   9124  -6103   2859    754       N  
ATOM   4637  CA  THR B 164       2.427  14.416  24.090  1.00104.11           C  
ANISOU 4637  CA  THR B 164    15502  14932   9122  -6327   3057    605       C  
ATOM   4638  C   THR B 164       2.860  13.558  25.293  1.00104.14           C  
ANISOU 4638  C   THR B 164    15035  15183   9349  -6185   2966    385       C  
ATOM   4639  O   THR B 164       2.410  13.851  26.404  1.00101.66           O  
ANISOU 4639  O   THR B 164    14751  14667   9207  -6105   2813    363       O  
ATOM   4640  CB  THR B 164       3.348  15.638  23.849  1.00113.38           C  
ANISOU 4640  CB  THR B 164    16838  16070  10173  -6843   3286    665       C  
ATOM   4641  OG1 THR B 164       2.761  16.458  22.839  1.00113.60           O  
ANISOU 4641  OG1 THR B 164    17366  15797  10001  -6917   3339    896       O  
ATOM   4642  CG2 THR B 164       4.766  15.267  23.435  1.00113.25           C  
ANISOU 4642  CG2 THR B 164    16452  16513  10064  -7124   3524    531       C  
ATOM   4643  N   PRO B 165       3.715  12.509  25.128  1.00100.21           N  
ANISOU 4643  N   PRO B 165    14113  15116   8848  -6133   3053    223       N  
ATOM   4644  CA  PRO B 165       4.138  11.723  26.305  1.00 97.76           C  
ANISOU 4644  CA  PRO B 165    13375  15032   8738  -5979   2960     27       C  
ATOM   4645  C   PRO B 165       4.792  12.579  27.396  1.00100.23           C  
ANISOU 4645  C   PRO B 165    13598  15333   9151  -6281   2978    -41       C  
ATOM   4646  O   PRO B 165       4.484  12.387  28.568  1.00 96.59           O  
ANISOU 4646  O   PRO B 165    13024  14803   8871  -6111   2810   -116       O  
ATOM   4647  CB  PRO B 165       5.109  10.685  25.725  1.00100.83           C  
ANISOU 4647  CB  PRO B 165    13376  15884   9050  -5939   3106   -112       C  
ATOM   4648  CG  PRO B 165       4.794  10.621  24.277  1.00106.68           C  
ANISOU 4648  CG  PRO B 165    14360  16593   9579  -5929   3207      7       C  
ATOM   4649  CD  PRO B 165       4.339  11.991  23.891  1.00103.90           C  
ANISOU 4649  CD  PRO B 165    14476  15883   9120  -6194   3242    208       C  
ATOM   4650  N   ARG B 166       5.638  13.559  27.009  1.00 99.58           N  
ANISOU 4650  N   ARG B 166    13594  15298   8944  -6740   3180    -12       N  
ATOM   4651  CA  ARG B 166       6.294  14.473  27.951  1.00100.65           C  
ANISOU 4651  CA  ARG B 166    13674  15415   9153  -7093   3214    -84       C  
ATOM   4652  C   ARG B 166       5.298  15.428  28.617  1.00103.27           C  
ANISOU 4652  C   ARG B 166    14421  15247   9570  -7081   3064     30       C  
ATOM   4653  O   ARG B 166       5.499  15.792  29.779  1.00101.95           O  
ANISOU 4653  O   ARG B 166    14157  15043   9535  -7174   2986    -70       O  
ATOM   4654  CB  ARG B 166       7.449  15.231  27.284  1.00103.91           C  
ANISOU 4654  CB  ARG B 166    14067  16014   9401  -7610   3488    -86       C  
ATOM   4655  CG  ARG B 166       8.812  14.599  27.556  1.00113.62           C  
ANISOU 4655  CG  ARG B 166    14723  17801  10646  -7739   3603   -304       C  
ATOM   4656  CD  ARG B 166       9.795  14.787  26.408  1.00126.65           C  
ANISOU 4656  CD  ARG B 166    16292  19739  12090  -8086   3892   -295       C  
ATOM   4657  NE  ARG B 166      10.251  16.173  26.253  1.00134.47           N  
ANISOU 4657  NE  ARG B 166    17540  20568  12985  -8637   4065   -223       N  
ATOM   4658  CZ  ARG B 166      11.313  16.693  26.863  1.00145.73           C  
ANISOU 4658  CZ  ARG B 166    18706  22224  14439  -9046   4169   -366       C  
ATOM   4659  NH1 ARG B 166      12.040  15.954  27.692  1.00136.15           N1+
ANISOU 4659  NH1 ARG B 166    16951  21435  13344  -8946   4106   -586       N1+
ATOM   4660  NH2 ARG B 166      11.653  17.959  26.651  1.00124.22           N  
ANISOU 4660  NH2 ARG B 166    16270  19308  11621  -9561   4336   -290       N  
ATOM   4661  N   ARG B 167       4.207  15.791  27.892  1.00 99.75           N  
ANISOU 4661  N   ARG B 167    14426  14432   9044  -6938   3015    232       N  
ATOM   4662  CA  ARG B 167       3.123  16.660  28.371  1.00 98.74           C  
ANISOU 4662  CA  ARG B 167    14725  13814   8978  -6858   2872    361       C  
ATOM   4663  C   ARG B 167       2.225  15.906  29.347  1.00 98.29           C  
ANISOU 4663  C   ARG B 167    14540  13690   9118  -6415   2621    298       C  
ATOM   4664  O   ARG B 167       1.792  16.485  30.342  1.00 98.03           O  
ANISOU 4664  O   ARG B 167    14638  13404   9204  -6399   2506    289       O  
ATOM   4665  CB  ARG B 167       2.292  17.219  27.199  1.00100.50           C  
ANISOU 4665  CB  ARG B 167    15437  13719   9028  -6817   2902    598       C  
ATOM   4666  CG  ARG B 167       1.573  18.532  27.524  1.00113.10           C  
ANISOU 4666  CG  ARG B 167    17531  14812  10630  -6906   2849    746       C  
ATOM   4667  CD  ARG B 167       2.047  19.672  26.629  1.00127.16           C  
ANISOU 4667  CD  ARG B 167    19682  16427  12204  -7325   3071    894       C  
ATOM   4668  NE  ARG B 167       1.532  20.978  27.056  1.00136.92           N  
ANISOU 4668  NE  ARG B 167    21392  17177  13454  -7450   3043   1011       N  
ATOM   4669  CZ  ARG B 167       1.594  22.091  26.326  1.00153.94           C  
ANISOU 4669  CZ  ARG B 167    24011  19044  15436  -7735   3197   1190       C  
ATOM   4670  NH1 ARG B 167       2.137  22.072  25.114  1.00142.57           N  
ANISOU 4670  NH1 ARG B 167    22622  17764  13786  -7937   3393   1279       N  
ATOM   4671  NH2 ARG B 167       1.101  23.228  26.799  1.00140.91           N1+
ANISOU 4671  NH2 ARG B 167    22795  16934  13812  -7811   3163   1284       N1+
ATOM   4672  N   VAL B 168       1.947  14.622  29.053  1.00 91.73           N  
ANISOU 4672  N   VAL B 168    13465  13075   8311  -6065   2547    251       N  
ATOM   4673  CA  VAL B 168       1.122  13.724  29.867  1.00 87.61           C  
ANISOU 4673  CA  VAL B 168    12796  12527   7964  -5641   2330    189       C  
ATOM   4674  C   VAL B 168       1.888  13.336  31.145  1.00 90.28           C  
ANISOU 4674  C   VAL B 168    12740  13109   8456  -5665   2292     -7       C  
ATOM   4675  O   VAL B 168       1.276  13.241  32.209  1.00 87.51           O  
ANISOU 4675  O   VAL B 168    12380  12613   8256  -5463   2125    -41       O  
ATOM   4676  CB  VAL B 168       0.639  12.493  29.032  1.00 89.67           C  
ANISOU 4676  CB  VAL B 168    12955  12933   8182  -5305   2289    199       C  
ATOM   4677  CG1 VAL B 168       0.139  11.343  29.911  1.00 85.71           C  
ANISOU 4677  CG1 VAL B 168    12195  12508   7862  -4920   2112     90       C  
ATOM   4678  CG2 VAL B 168      -0.429  12.899  28.016  1.00 89.56           C  
ANISOU 4678  CG2 VAL B 168    13359  12629   8041  -5202   2252    396       C  
ATOM   4679  N   LYS B 169       3.225  13.132  31.042  1.00 89.53           N  
ANISOU 4679  N   LYS B 169    12313  13395   8309  -5911   2448   -134       N  
ATOM   4680  CA  LYS B 169       4.085  12.770  32.183  1.00 89.57           C  
ANISOU 4680  CA  LYS B 169    11911  13692   8430  -5947   2418   -326       C  
ATOM   4681  C   LYS B 169       4.142  13.886  33.245  1.00 94.13           C  
ANISOU 4681  C   LYS B 169    12622  14063   9081  -6192   2369   -352       C  
ATOM   4682  O   LYS B 169       4.301  13.593  34.435  1.00 92.27           O  
ANISOU 4682  O   LYS B 169    12155  13931   8972  -6089   2252   -479       O  
ATOM   4683  CB  LYS B 169       5.488  12.323  31.724  1.00 94.48           C  
ANISOU 4683  CB  LYS B 169    12139  14795   8962  -6145   2600   -453       C  
ATOM   4684  CG  LYS B 169       5.544  10.846  31.327  1.00105.51           C  
ANISOU 4684  CG  LYS B 169    13246  16477  10366  -5778   2584   -519       C  
ATOM   4685  CD  LYS B 169       6.886  10.451  30.712  1.00118.26           C  
ANISOU 4685  CD  LYS B 169    14502  18562  11869  -5956   2786   -633       C  
ATOM   4686  CE  LYS B 169       6.955   8.982  30.350  1.00123.92           C  
ANISOU 4686  CE  LYS B 169    14952  19541  12592  -5573   2774   -709       C  
ATOM   4687  NZ  LYS B 169       6.312   8.690  29.041  1.00128.08           N1+
ANISOU 4687  NZ  LYS B 169    15735  19936  12995  -5456   2831   -590       N1+
ATOM   4688  N   ALA B 170       3.957  15.154  32.796  1.00 92.15           N  
ANISOU 4688  N   ALA B 170    12777  13498   8739  -6497   2456   -226       N  
ATOM   4689  CA  ALA B 170       3.880  16.362  33.610  1.00 92.74           C  
ANISOU 4689  CA  ALA B 170    13095  13284   8857  -6748   2429   -226       C  
ATOM   4690  C   ALA B 170       2.530  16.405  34.335  1.00 94.06           C  
ANISOU 4690  C   ALA B 170    13506  13083   9148  -6393   2217   -157       C  
ATOM   4691  O   ALA B 170       2.487  16.818  35.497  1.00 94.47           O  
ANISOU 4691  O   ALA B 170    13558  13035   9303  -6428   2125   -242       O  
ATOM   4692  CB  ALA B 170       4.032  17.587  32.730  1.00 96.73           C  
ANISOU 4692  CB  ALA B 170    13998  13545   9210  -7140   2604    -89       C  
ATOM   4693  N   THR B 171       1.430  15.980  33.660  1.00 87.56           N  
ANISOU 4693  N   THR B 171    12882  12077   8308  -6054   2140    -13       N  
ATOM   4694  CA  THR B 171       0.089  15.909  34.267  1.00 84.44           C  
ANISOU 4694  CA  THR B 171    12681  11375   8028  -5688   1942     52       C  
ATOM   4695  C   THR B 171       0.076  14.815  35.353  1.00 86.51           C  
ANISOU 4695  C   THR B 171    12558  11865   8446  -5400   1803    -98       C  
ATOM   4696  O   THR B 171      -0.532  15.028  36.399  1.00 84.52           O  
ANISOU 4696  O   THR B 171    12379  11428   8308  -5259   1669   -122       O  
ATOM   4697  CB  THR B 171      -1.022  15.731  33.213  1.00 87.79           C  
ANISOU 4697  CB  THR B 171    13382  11595   8380  -5428   1899    233       C  
ATOM   4698  OG1 THR B 171      -0.760  16.579  32.095  1.00 93.99           O  
ANISOU 4698  OG1 THR B 171    14465  12260   8988  -5709   2056    365       O  
ATOM   4699  CG2 THR B 171      -2.407  16.042  33.763  1.00 79.44           C  
ANISOU 4699  CG2 THR B 171    12598  10172   7415  -5132   1723    321       C  
ATOM   4700  N   ILE B 172       0.783  13.670  35.118  1.00 83.19           N  
ANISOU 4700  N   ILE B 172    11741  11845   8021  -5315   1843   -200       N  
ATOM   4701  CA  ILE B 172       0.927  12.567  36.083  1.00 81.28           C  
ANISOU 4701  CA  ILE B 172    11128  11848   7908  -5048   1732   -339       C  
ATOM   4702  C   ILE B 172       1.593  13.101  37.368  1.00 88.47           C  
ANISOU 4702  C   ILE B 172    11899  12831   8885  -5241   1701   -473       C  
ATOM   4703  O   ILE B 172       1.197  12.702  38.465  1.00 87.43           O  
ANISOU 4703  O   ILE B 172    11668  12681   8870  -5008   1558   -534       O  
ATOM   4704  CB  ILE B 172       1.659  11.321  35.486  1.00 84.07           C  
ANISOU 4704  CB  ILE B 172    11115  12606   8222  -4935   1806   -419       C  
ATOM   4705  CG1 ILE B 172       0.768  10.581  34.475  1.00 82.60           C  
ANISOU 4705  CG1 ILE B 172    11057  12327   8000  -4653   1782   -312       C  
ATOM   4706  CG2 ILE B 172       2.144  10.351  36.581  1.00 82.91           C  
ANISOU 4706  CG2 ILE B 172    10569  12747   8186  -4734   1720   -577       C  
ATOM   4707  CD1 ILE B 172       1.516   9.664  33.504  1.00 88.95           C  
ANISOU 4707  CD1 ILE B 172    11617  13470   8709  -4631   1908   -365       C  
ATOM   4708  N   VAL B 173       2.574  14.019  37.245  1.00 87.80           N  
ANISOU 4708  N   VAL B 173    11819  12824   8717  -5676   1836   -521       N  
ATOM   4709  CA  VAL B 173       3.174  14.585  38.451  1.00 88.76           C  
ANISOU 4709  CA  VAL B 173    11825  13009   8890  -5885   1798   -660       C  
ATOM   4710  C   VAL B 173       2.216  15.632  39.039  1.00 93.21           C  
ANISOU 4710  C   VAL B 173    12811  13104   9502  -5899   1711   -586       C  
ATOM   4711  O   VAL B 173       2.070  15.680  40.263  1.00 92.94           O  
ANISOU 4711  O   VAL B 173    12713  13042   9558  -5813   1589   -679       O  
ATOM   4712  CB  VAL B 173       4.653  15.072  38.343  1.00 95.71           C  
ANISOU 4712  CB  VAL B 173    12476  14207   9684  -6349   1956   -786       C  
ATOM   4713  CG1 VAL B 173       5.562  13.973  37.808  1.00 95.54           C  
ANISOU 4713  CG1 VAL B 173    12012  14670   9619  -6278   2037   -868       C  
ATOM   4714  CG2 VAL B 173       4.797  16.353  37.528  1.00 98.42           C  
ANISOU 4714  CG2 VAL B 173    13181  14300   9912  -6774   2118   -688       C  
ATOM   4715  N   ALA B 174       1.513  16.409  38.172  1.00 89.39           N  
ANISOU 4715  N   ALA B 174    12758  12255   8950  -5964   1767   -413       N  
ATOM   4716  CA  ALA B 174       0.555  17.426  38.605  1.00 88.83           C  
ANISOU 4716  CA  ALA B 174    13121  11719   8912  -5944   1696   -327       C  
ATOM   4717  C   ALA B 174      -0.525  16.811  39.464  1.00 90.50           C  
ANISOU 4717  C   ALA B 174    13310  11821   9253  -5500   1505   -327       C  
ATOM   4718  O   ALA B 174      -0.838  17.360  40.515  1.00 90.35           O  
ANISOU 4718  O   ALA B 174    13407  11620   9302  -5492   1421   -381       O  
ATOM   4719  CB  ALA B 174      -0.070  18.107  37.411  1.00 90.49           C  
ANISOU 4719  CB  ALA B 174    13760  11606   9017  -5989   1775   -125       C  
ATOM   4720  N   VAL B 175      -1.048  15.639  39.049  1.00 84.64           N  
ANISOU 4720  N   VAL B 175    12405  11209   8544  -5146   1443   -280       N  
ATOM   4721  CA  VAL B 175      -2.093  14.910  39.757  1.00 80.91           C  
ANISOU 4721  CA  VAL B 175    11890  10662   8192  -4725   1278   -273       C  
ATOM   4722  C   VAL B 175      -1.556  14.293  41.040  1.00 84.49           C  
ANISOU 4722  C   VAL B 175    11995  11373   8735  -4653   1201   -442       C  
ATOM   4723  O   VAL B 175      -2.241  14.381  42.052  1.00 83.23           O  
ANISOU 4723  O   VAL B 175    11906  11057   8662  -4473   1084   -462       O  
ATOM   4724  CB  VAL B 175      -2.872  13.902  38.874  1.00 82.56           C  
ANISOU 4724  CB  VAL B 175    12070  10898   8401  -4401   1241   -171       C  
ATOM   4725  CG1 VAL B 175      -3.445  14.592  37.647  1.00 83.56           C  
ANISOU 4725  CG1 VAL B 175    12560  10769   8419  -4461   1299      1       C  
ATOM   4726  CG2 VAL B 175      -2.038  12.690  38.473  1.00 81.85           C  
ANISOU 4726  CG2 VAL B 175    11594  11213   8294  -4356   1295   -255       C  
ATOM   4727  N   TRP B 176      -0.319  13.737  41.026  1.00 82.86           N  
ANISOU 4727  N   TRP B 176    11423  11565   8497  -4796   1270   -564       N  
ATOM   4728  CA  TRP B 176       0.314  13.166  42.220  1.00 83.00           C  
ANISOU 4728  CA  TRP B 176    11095  11867   8575  -4731   1195   -725       C  
ATOM   4729  C   TRP B 176       0.560  14.226  43.295  1.00 88.80           C  
ANISOU 4729  C   TRP B 176    11933  12487   9320  -4966   1160   -818       C  
ATOM   4730  O   TRP B 176       0.389  13.935  44.481  1.00 88.73           O  
ANISOU 4730  O   TRP B 176    11811  12521   9380  -4794   1041   -900       O  
ATOM   4731  CB  TRP B 176       1.607  12.418  41.879  1.00 83.46           C  
ANISOU 4731  CB  TRP B 176    10743  12388   8581  -4828   1281   -832       C  
ATOM   4732  CG  TRP B 176       1.387  10.968  41.559  1.00 82.62           C  
ANISOU 4732  CG  TRP B 176    10417  12463   8511  -4456   1248   -814       C  
ATOM   4733  CD1 TRP B 176       1.524  10.366  40.344  1.00 85.46           C  
ANISOU 4733  CD1 TRP B 176    10723  12937   8813  -4409   1343   -761       C  
ATOM   4734  CD2 TRP B 176       0.967   9.942  42.470  1.00 80.50           C  
ANISOU 4734  CD2 TRP B 176     9983  12262   8339  -4083   1116   -852       C  
ATOM   4735  NE1 TRP B 176       1.233   9.027  40.441  1.00 82.77           N  
ANISOU 4735  NE1 TRP B 176    10196  12723   8531  -4035   1279   -773       N  
ATOM   4736  CE2 TRP B 176       0.873   8.739  41.732  1.00 83.26           C  
ANISOU 4736  CE2 TRP B 176    10194  12750   8691  -3831   1142   -820       C  
ATOM   4737  CE3 TRP B 176       0.630   9.924  43.837  1.00 80.73           C  
ANISOU 4737  CE3 TRP B 176     9991  12236   8446  -3937    985   -906       C  
ATOM   4738  CZ2 TRP B 176       0.465   7.527  42.315  1.00 80.53           C  
ANISOU 4738  CZ2 TRP B 176     9701  12469   8428  -3451   1046   -837       C  
ATOM   4739  CZ3 TRP B 176       0.239   8.719  44.415  1.00 80.02           C  
ANISOU 4739  CZ3 TRP B 176     9743  12231   8430  -3557    891   -914       C  
ATOM   4740  CH2 TRP B 176       0.146   7.544  43.655  1.00 79.40           C  
ANISOU 4740  CH2 TRP B 176     9544  12265   8358  -3323    924   -876       C  
ATOM   4741  N   LEU B 177       0.916  15.467  42.875  1.00 85.89           N  
ANISOU 4741  N   LEU B 177    11810  11950   8876  -5359   1267   -801       N  
ATOM   4742  CA  LEU B 177       1.129  16.614  43.764  1.00 85.78           C  
ANISOU 4742  CA  LEU B 177    11963  11770   8857  -5633   1253   -890       C  
ATOM   4743  C   LEU B 177      -0.202  17.117  44.322  1.00 85.69           C  
ANISOU 4743  C   LEU B 177    12322  11325   8912  -5405   1148   -808       C  
ATOM   4744  O   LEU B 177      -0.294  17.348  45.522  1.00 85.88           O  
ANISOU 4744  O   LEU B 177    12337  11313   8982  -5371   1055   -912       O  
ATOM   4745  CB  LEU B 177       1.860  17.762  43.045  1.00 88.91           C  
ANISOU 4745  CB  LEU B 177    12552  12081   9150  -6129   1419   -884       C  
ATOM   4746  CG  LEU B 177       3.332  17.554  42.750  1.00 95.81           C  
ANISOU 4746  CG  LEU B 177    13051  13402   9952  -6456   1535  -1011       C  
ATOM   4747  CD1 LEU B 177       3.770  18.424  41.613  1.00 99.23           C  
ANISOU 4747  CD1 LEU B 177    13709  13719  10273  -6858   1725   -932       C  
ATOM   4748  CD2 LEU B 177       4.184  17.839  43.961  1.00100.01           C  
ANISOU 4748  CD2 LEU B 177    13349  14157  10494  -6676   1483  -1222       C  
ATOM   4749  N   ILE B 178      -1.234  17.277  43.463  1.00 78.99           N  
ANISOU 4749  N   ILE B 178    11785  10168   8060  -5235   1160   -626       N  
ATOM   4750  CA  ILE B 178      -2.556  17.765  43.869  1.00 76.62           C  
ANISOU 4750  CA  ILE B 178    11831   9465   7815  -4992   1068   -536       C  
ATOM   4751  C   ILE B 178      -3.120  16.848  44.935  1.00 76.66           C  
ANISOU 4751  C   ILE B 178    11622   9579   7925  -4621    922   -596       C  
ATOM   4752  O   ILE B 178      -3.588  17.333  45.969  1.00 76.54           O  
ANISOU 4752  O   ILE B 178    11744   9385   7954  -4553    847   -647       O  
ATOM   4753  CB  ILE B 178      -3.504  18.022  42.655  1.00 79.10           C  
ANISOU 4753  CB  ILE B 178    12474   9492   8090  -4862   1101   -329       C  
ATOM   4754  CG1 ILE B 178      -3.085  19.315  41.926  1.00 82.86           C  
ANISOU 4754  CG1 ILE B 178    13297   9732   8455  -5249   1240   -266       C  
ATOM   4755  CG2 ILE B 178      -4.982  18.122  43.078  1.00 76.95           C  
ANISOU 4755  CG2 ILE B 178    12438   8908   7892  -4488    978   -241       C  
ATOM   4756  CD1 ILE B 178      -3.536  19.403  40.477  1.00 92.90           C  
ANISOU 4756  CD1 ILE B 178    14794  10866   9637  -5205   1308    -72       C  
ATOM   4757  N   SER B 179      -2.965  15.527  44.725  1.00 70.19           N  
ANISOU 4757  N   SER B 179    10465   9069   7137  -4407    895   -603       N  
ATOM   4758  CA  SER B 179      -3.374  14.465  45.641  1.00 66.80           C  
ANISOU 4758  CA  SER B 179     9801   8785   6797  -4062    777   -652       C  
ATOM   4759  C   SER B 179      -2.826  14.692  47.050  1.00 72.91           C  
ANISOU 4759  C   SER B 179    10443   9675   7585  -4145    716   -813       C  
ATOM   4760  O   SER B 179      -3.571  14.525  48.010  1.00 71.42           O  
ANISOU 4760  O   SER B 179    10294   9384   7458  -3903    616   -826       O  
ATOM   4761  CB  SER B 179      -2.919  13.117  45.109  1.00 67.28           C  
ANISOU 4761  CB  SER B 179     9519   9183   6861  -3917    794   -659       C  
ATOM   4762  OG  SER B 179      -3.558  12.898  43.867  1.00 71.93           O  
ANISOU 4762  OG  SER B 179    10251   9648   7431  -3817    835   -517       O  
ATOM   4763  N   ALA B 180      -1.549  15.122  47.166  1.00 72.73           N  
ANISOU 4763  N   ALA B 180    10272   9867   7494  -4500    777   -939       N  
ATOM   4764  CA  ALA B 180      -0.887  15.459  48.430  1.00 73.96           C  
ANISOU 4764  CA  ALA B 180    10299  10164   7637  -4645    720  -1112       C  
ATOM   4765  C   ALA B 180      -1.531  16.696  49.081  1.00 77.95           C  
ANISOU 4765  C   ALA B 180    11189  10280   8147  -4739    693  -1123       C  
ATOM   4766  O   ALA B 180      -1.767  16.669  50.288  1.00 76.36           O  
ANISOU 4766  O   ALA B 180    10961  10081   7972  -4610    593  -1211       O  
ATOM   4767  CB  ALA B 180       0.607  15.694  48.208  1.00 77.59           C  
ANISOU 4767  CB  ALA B 180    10514  10952   8016  -5038    805  -1240       C  
ATOM   4768  N   VAL B 181      -1.875  17.743  48.284  1.00 75.83           N  
ANISOU 4768  N   VAL B 181    11297   9667   7846  -4930    781  -1027       N  
ATOM   4769  CA  VAL B 181      -2.509  18.971  48.799  1.00 77.30           C  
ANISOU 4769  CA  VAL B 181    11896   9441   8032  -5006    770  -1029       C  
ATOM   4770  C   VAL B 181      -3.932  18.687  49.308  1.00 79.84           C  
ANISOU 4770  C   VAL B 181    12369   9534   8434  -4564    666   -944       C  
ATOM   4771  O   VAL B 181      -4.492  19.471  50.067  1.00 80.59           O  
ANISOU 4771  O   VAL B 181    12727   9355   8539  -4534    629   -980       O  
ATOM   4772  CB  VAL B 181      -2.452  20.176  47.817  1.00 83.98           C  
ANISOU 4772  CB  VAL B 181    13130   9967   8812  -5321    899   -941       C  
ATOM   4773  CG1 VAL B 181      -2.745  21.489  48.542  1.00 85.97           C  
ANISOU 4773  CG1 VAL B 181    13772   9845   9049  -5477    898  -1003       C  
ATOM   4774  CG2 VAL B 181      -1.097  20.269  47.125  1.00 86.17           C  
ANISOU 4774  CG2 VAL B 181    13218  10513   9009  -5740   1023  -1001       C  
ATOM   4775  N   ILE B 182      -4.489  17.548  48.926  1.00 75.11           N  
ANISOU 4775  N   ILE B 182    11589   9061   7889  -4230    625   -846       N  
ATOM   4776  CA  ILE B 182      -5.804  17.120  49.374  1.00 73.27           C  
ANISOU 4776  CA  ILE B 182    11433   8673   7734  -3819    534   -770       C  
ATOM   4777  C   ILE B 182      -5.636  16.173  50.572  1.00 79.14           C  
ANISOU 4777  C   ILE B 182    11859   9693   8518  -3628    442   -881       C  
ATOM   4778  O   ILE B 182      -6.205  16.437  51.630  1.00 78.53           O  
ANISOU 4778  O   ILE B 182    11882   9490   8464  -3492    377   -930       O  
ATOM   4779  CB  ILE B 182      -6.633  16.497  48.223  1.00 74.07           C  
ANISOU 4779  CB  ILE B 182    11566   8713   7866  -3580    544   -595       C  
ATOM   4780  CG1 ILE B 182      -6.819  17.503  47.062  1.00 75.74           C  
ANISOU 4780  CG1 ILE B 182    12124   8641   8014  -3755    629   -474       C  
ATOM   4781  CG2 ILE B 182      -7.988  16.012  48.755  1.00 72.88           C  
ANISOU 4781  CG2 ILE B 182    11453   8437   7799  -3173    451   -534       C  
ATOM   4782  CD1 ILE B 182      -7.352  16.926  45.777  1.00 81.05           C  
ANISOU 4782  CD1 ILE B 182    12800   9317   8679  -3596    646   -318       C  
ATOM   4783  N   SER B 183      -4.861  15.075  50.395  1.00 77.02           N  
ANISOU 4783  N   SER B 183    11221   9795   8246  -3605    442   -916       N  
ATOM   4784  CA  SER B 183      -4.578  14.061  51.412  1.00 76.49           C  
ANISOU 4784  CA  SER B 183    10840  10020   8201  -3414    361  -1003       C  
ATOM   4785  C   SER B 183      -4.028  14.679  52.670  1.00 85.38           C  
ANISOU 4785  C   SER B 183    11953  11208   9281  -3569    311  -1165       C  
ATOM   4786  O   SER B 183      -4.593  14.453  53.738  1.00 83.92           O  
ANISOU 4786  O   SER B 183    11774  10991   9119  -3346    232  -1195       O  
ATOM   4787  CB  SER B 183      -3.597  13.019  50.885  1.00 78.84           C  
ANISOU 4787  CB  SER B 183    10778  10698   8479  -3431    390  -1027       C  
ATOM   4788  OG  SER B 183      -4.115  12.398  49.724  1.00 84.22           O  
ANISOU 4788  OG  SER B 183    11478  11327   9195  -3284    435   -890       O  
ATOM   4789  N   PHE B 184      -2.957  15.490  52.540  1.00 87.80           N  
ANISOU 4789  N   PHE B 184    12251  11595   9513  -3964    363  -1272       N  
ATOM   4790  CA  PHE B 184      -2.304  16.188  53.654  1.00 91.67           C  
ANISOU 4790  CA  PHE B 184    12730  12159   9943  -4185    319  -1452       C  
ATOM   4791  C   PHE B 184      -2.759  17.651  53.682  1.00103.67           C  
ANISOU 4791  C   PHE B 184    14683  13260  11445  -4396    362  -1460       C  
ATOM   4792  O   PHE B 184      -2.377  18.453  52.824  1.00104.23           O  
ANISOU 4792  O   PHE B 184    14924  13196  11482  -4709    461  -1439       O  
ATOM   4793  CB  PHE B 184      -0.772  16.009  53.629  1.00 94.94           C  
ANISOU 4793  CB  PHE B 184    12796  12994  10284  -4478    337  -1592       C  
ATOM   4794  CG  PHE B 184      -0.348  14.652  53.115  1.00 94.38           C  
ANISOU 4794  CG  PHE B 184    12358  13272  10231  -4278    338  -1542       C  
ATOM   4795  CD1 PHE B 184      -0.834  13.485  53.695  1.00 94.22           C  
ANISOU 4795  CD1 PHE B 184    12175  13370  10255  -3869    252  -1501       C  
ATOM   4796  CD2 PHE B 184       0.506  14.541  52.026  1.00 97.41           C  
ANISOU 4796  CD2 PHE B 184    12582  13846  10582  -4496    438  -1533       C  
ATOM   4797  CE1 PHE B 184      -0.496  12.237  53.181  1.00 93.69           C  
ANISOU 4797  CE1 PHE B 184    11816  13576  10205  -3672    262  -1450       C  
ATOM   4798  CE2 PHE B 184       0.869  13.286  51.529  1.00 98.80           C  
ANISOU 4798  CE2 PHE B 184    12441  14326  10772  -4289    447  -1492       C  
ATOM   4799  CZ  PHE B 184       0.366  12.141  52.114  1.00 94.26           C  
ANISOU 4799  CZ  PHE B 184    11729  13840  10246  -3875    357  -1453       C  
ATOM   4800  N   PRO B 185      -3.671  17.968  54.626  1.00105.30           N  
ANISOU 4800  N   PRO B 185    15097  13238  11674  -4194    296  -1476       N  
ATOM   4801  CA  PRO B 185      -4.262  19.309  54.678  1.00108.65           C  
ANISOU 4801  CA  PRO B 185    15969  13226  12088  -4318    335  -1473       C  
ATOM   4802  C   PRO B 185      -3.293  20.479  54.567  1.00121.11           C  
ANISOU 4802  C   PRO B 185    17693  14735  13587  -4810    406  -1598       C  
ATOM   4803  O   PRO B 185      -2.274  20.515  55.270  1.00122.39           O  
ANISOU 4803  O   PRO B 185    17639  15175  13689  -5046    372  -1779       O  
ATOM   4804  CB  PRO B 185      -5.011  19.325  56.016  1.00109.50           C  
ANISOU 4804  CB  PRO B 185    16155  13244  12206  -4060    244  -1541       C  
ATOM   4805  CG  PRO B 185      -4.572  18.083  56.738  1.00111.95           C  
ANISOU 4805  CG  PRO B 185    16048  13977  12510  -3882    158  -1600       C  
ATOM   4806  CD  PRO B 185      -4.243  17.111  55.679  1.00105.56           C  
ANISOU 4806  CD  PRO B 185    14983  13387  11738  -3826    193  -1489       C  
ATOM   4807  N   PRO B 186      -3.637  21.468  53.703  1.00122.74           N  
ANISOU 4807  N   PRO B 186    18285  14562  13790  -4968    504  -1502       N  
ATOM   4808  CA  PRO B 186      -2.786  22.669  53.567  1.00127.05           C  
ANISOU 4808  CA  PRO B 186    19035  14978  14260  -5464    593  -1612       C  
ATOM   4809  C   PRO B 186      -2.716  23.467  54.863  1.00133.16           C  
ANISOU 4809  C   PRO B 186    19972  15630  14993  -5589    541  -1805       C  
ATOM   4810  O   PRO B 186      -1.743  24.188  55.086  1.00135.62           O  
ANISOU 4810  O   PRO B 186    20305  15990  15235  -6026    582  -1967       O  
ATOM   4811  CB  PRO B 186      -3.465  23.470  52.444  1.00129.74           C  
ANISOU 4811  CB  PRO B 186    19813  14877  14607  -5489    697  -1429       C  
ATOM   4812  CG  PRO B 186      -4.877  23.007  52.441  1.00131.43           C  
ANISOU 4812  CG  PRO B 186    20129  14912  14895  -4982    631  -1276       C  
ATOM   4813  CD  PRO B 186      -4.837  21.554  52.842  1.00123.53           C  
ANISOU 4813  CD  PRO B 186    18663  14330  13942  -4699    536  -1290       C  
ATOM   4814  N   LEU B 187      -3.739  23.298  55.735  1.00128.89           N  
ANISOU 4814  N   LEU B 187    19529  14954  14491  -5209    453  -1799       N  
ATOM   4815  CA  LEU B 187      -3.857  23.935  57.049  1.00130.60           C  
ANISOU 4815  CA  LEU B 187    19903  15055  14663  -5237    394  -1978       C  
ATOM   4816  C   LEU B 187      -2.893  23.316  58.079  1.00135.49           C  
ANISOU 4816  C   LEU B 187    20108  16148  15225  -5332    296  -2176       C  
ATOM   4817  O   LEU B 187      -3.031  23.579  59.277  1.00135.99           O  
ANISOU 4817  O   LEU B 187    20230  16197  15243  -5283    222  -2324       O  
ATOM   4818  CB  LEU B 187      -5.320  23.894  57.558  1.00128.51           C  
ANISOU 4818  CB  LEU B 187    19861  14512  14453  -4771    347  -1890       C  
ATOM   4819  CG  LEU B 187      -6.336  24.804  56.856  1.00133.46           C  
ANISOU 4819  CG  LEU B 187    20972  14623  15113  -4669    426  -1742       C  
ATOM   4820  CD1 LEU B 187      -7.742  24.411  57.219  1.00130.98           C  
ANISOU 4820  CD1 LEU B 187    20729  14173  14864  -4158    372  -1636       C  
ATOM   4821  CD2 LEU B 187      -6.099  26.288  57.175  1.00138.81           C  
ANISOU 4821  CD2 LEU B 187    22087  14929  15724  -4997    490  -1874       C  
ATOM   4822  N   VAL B 188      -1.896  22.522  57.592  1.00131.85           N  
ANISOU 4822  N   VAL B 188    19231  16112  14753  -5466    296  -2181       N  
ATOM   4823  CA  VAL B 188      -0.840  21.802  58.322  1.00132.24           C  
ANISOU 4823  CA  VAL B 188    18823  16681  14743  -5545    205  -2342       C  
ATOM   4824  C   VAL B 188      -1.484  21.053  59.523  1.00134.10           C  
ANISOU 4824  C   VAL B 188    18942  17032  14979  -5121     76  -2364       C  
ATOM   4825  O   VAL B 188      -0.975  21.016  60.646  1.00134.53           O  
ANISOU 4825  O   VAL B 188    18842  17323  14950  -5174    -19  -2544       O  
ATOM   4826  CB  VAL B 188       0.416  22.687  58.643  1.00140.55           C  
ANISOU 4826  CB  VAL B 188    19839  17869  15694  -6091    224  -2575       C  
ATOM   4827  CG1 VAL B 188       0.180  23.744  59.735  1.00142.38           C  
ANISOU 4827  CG1 VAL B 188    20395  17839  15864  -6225    186  -2751       C  
ATOM   4828  CG2 VAL B 188       1.649  21.833  58.937  1.00141.14           C  
ANISOU 4828  CG2 VAL B 188    19367  18549  15710  -6189    151  -2699       C  
ATOM   4829  N   SER B 189      -2.646  20.447  59.230  1.00128.42           N  
ANISOU 4829  N   SER B 189    18303  16141  14348  -4700     78  -2172       N  
ATOM   4830  CA  SER B 189      -3.451  19.704  60.181  1.00126.20           C  
ANISOU 4830  CA  SER B 189    17954  15914  14083  -4276    -12  -2145       C  
ATOM   4831  C   SER B 189      -2.905  18.294  60.397  1.00128.43           C  
ANISOU 4831  C   SER B 189    17774  16668  14358  -4085    -85  -2132       C  
ATOM   4832  O   SER B 189      -2.520  17.622  59.439  1.00126.54           O  
ANISOU 4832  O   SER B 189    17323  16597  14160  -4086    -46  -2035       O  
ATOM   4833  CB  SER B 189      -4.915  19.703  59.740  1.00127.76           C  
ANISOU 4833  CB  SER B 189    18428  15737  14377  -3942     31  -1955       C  
ATOM   4834  OG  SER B 189      -5.602  18.506  60.060  1.00133.38           O  
ANISOU 4834  OG  SER B 189    18947  16594  15139  -3524    -22  -1851       O  
ATOM   4835  N   LEU B 190      -2.854  17.871  61.670  1.00125.73           N  
ANISOU 4835  N   LEU B 190    17292  16531  13949  -3918   -190  -2233       N  
ATOM   4836  CA  LEU B 190      -2.362  16.566  62.093  1.00124.69           C  
ANISOU 4836  CA  LEU B 190    16758  16830  13788  -3700   -272  -2227       C  
ATOM   4837  C   LEU B 190      -3.369  15.456  61.758  1.00125.99           C  
ANISOU 4837  C   LEU B 190    16888  16930  14053  -3269   -255  -2018       C  
ATOM   4838  O   LEU B 190      -4.580  15.645  61.878  1.00124.21           O  
ANISOU 4838  O   LEU B 190    16922  16386  13885  -3059   -228  -1927       O  
ATOM   4839  CB  LEU B 190      -2.025  16.589  63.603  1.00126.18           C  
ANISOU 4839  CB  LEU B 190    16861  17232  13849  -3667   -389  -2400       C  
ATOM   4840  CG  LEU B 190      -1.232  15.411  64.186  1.00130.68           C  
ANISOU 4840  CG  LEU B 190    17011  18297  14345  -3501   -493  -2434       C  
ATOM   4841  CD1 LEU B 190       0.199  15.382  63.664  1.00132.99           C  
ANISOU 4841  CD1 LEU B 190    16987  18953  14590  -3813   -501  -2537       C  
ATOM   4842  CD2 LEU B 190      -1.211  15.476  65.697  1.00133.65           C  
ANISOU 4842  CD2 LEU B 190    17384  18807  14589  -3405   -607  -2573       C  
ATOM   4843  N   TYR B 191      -2.842  14.312  61.313  1.00122.02           N  
ANISOU 4843  N   TYR B 191    16059  16734  13569  -3149   -265  -1951       N  
ATOM   4844  CA  TYR B 191      -3.560  13.089  60.936  1.00118.97           C  
ANISOU 4844  CA  TYR B 191    15583  16351  13270  -2779   -249  -1772       C  
ATOM   4845  C   TYR B 191      -3.870  12.192  62.138  1.00120.09           C  
ANISOU 4845  C   TYR B 191    15611  16650  13368  -2445   -331  -1767       C  
ATOM   4846  O   TYR B 191      -4.532  11.170  61.953  1.00116.57           O  
ANISOU 4846  O   TYR B 191    15117  16185  12992  -2140   -313  -1623       O  
ATOM   4847  CB  TYR B 191      -2.623  12.267  60.056  1.00120.93           C  
ANISOU 4847  CB  TYR B 191    15518  16901  13529  -2823   -227  -1740       C  
ATOM   4848  CG  TYR B 191      -2.964  12.225  58.591  1.00122.71           C  
ANISOU 4848  CG  TYR B 191    15827  16947  13850  -2863   -124  -1604       C  
ATOM   4849  CD1 TYR B 191      -2.890  13.371  57.806  1.00126.28           C  
ANISOU 4849  CD1 TYR B 191    16494  17177  14311  -3182    -49  -1617       C  
ATOM   4850  CD2 TYR B 191      -3.233  11.017  57.957  1.00121.83           C  
ANISOU 4850  CD2 TYR B 191    15571  16913  13806  -2604    -99  -1471       C  
ATOM   4851  CE1 TYR B 191      -3.152  13.329  56.441  1.00127.46           C  
ANISOU 4851  CE1 TYR B 191    16719  17185  14525  -3219     42  -1488       C  
ATOM   4852  CE2 TYR B 191      -3.495  10.960  56.593  1.00122.33           C  
ANISOU 4852  CE2 TYR B 191    15701  16840  13940  -2649    -11  -1359       C  
ATOM   4853  CZ  TYR B 191      -3.443  12.117  55.834  1.00133.71           C  
ANISOU 4853  CZ  TYR B 191    17353  18072  15377  -2953     57  -1365       C  
ATOM   4854  OH  TYR B 191      -3.674  12.053  54.482  1.00135.90           O  
ANISOU 4854  OH  TYR B 191    17700  18234  15703  -2991    141  -1249       O  
ATOM   4855  N   ARG B 192      -3.317  12.525  63.341  1.00117.96           N  
ANISOU 4855  N   ARG B 192    15288  16560  12973  -2517   -421  -1927       N  
ATOM   4856  CA  ARG B 192      -3.353  11.764  64.604  1.00115.42           C  
ANISOU 4856  CA  ARG B 192    14842  16450  12562  -2244   -512  -1949       C  
ATOM   4857  C   ARG B 192      -2.548  10.473  64.401  1.00119.97           C  
ANISOU 4857  C   ARG B 192    15062  17401  13121  -2087   -548  -1900       C  
ATOM   4858  O   ARG B 192      -1.702  10.411  63.502  1.00 68.96           O  
ANISOU 4858  O   ARG B 192     8421  11100   6681  -2266   -522  -1918       O  
ATOM   4859  CB  ARG B 192      -4.790  11.481  65.105  1.00111.69           C  
ANISOU 4859  CB  ARG B 192    14590  15706  12141  -1924   -482  -1829       C  
ATOM   4860  CG  ARG B 192      -4.877  10.867  66.500  1.00115.43           C  
ANISOU 4860  CG  ARG B 192    14993  16364  12500  -1673   -562  -1856       C  
ATOM   4861  CD  ARG B 192      -6.303  10.841  67.031  1.00117.62           C  
ANISOU 4861  CD  ARG B 192    15515  16358  12818  -1422   -514  -1764       C  
ATOM   4862  NE  ARG B 192      -6.997   9.583  66.731  1.00115.91           N  
ANISOU 4862  NE  ARG B 192    15227  16124  12690  -1112   -465  -1575       N  
ATOM   4863  CZ  ARG B 192      -8.108   9.164  67.338  1.00120.75           C  
ANISOU 4863  CZ  ARG B 192    15960  16601  13319   -848   -427  -1482       C  
ATOM   4864  NH1 ARG B 192      -8.666   9.893  68.299  1.00105.05           N  
ANISOU 4864  NH1 ARG B 192    14166  14490  11258   -827   -433  -1559       N  
ATOM   4865  NH2 ARG B 192      -8.661   8.008  66.997  1.00 99.36           N  
ANISOU 4865  NH2 ARG B 192    13180  13880  10693   -611   -376  -1320       N  
ATOM   4866  N   PRO B 200      -0.884   0.390  71.970  1.00 82.41           N  
ANISOU 4866  N   PRO B 200     9267  14630   7414    967  -1124  -1287       N  
ATOM   4867  CA  PRO B 200      -0.703   1.390  70.907  1.00 81.22           C  
ANISOU 4867  CA  PRO B 200     9063  14395   7401    589  -1085  -1406       C  
ATOM   4868  C   PRO B 200      -1.663   1.183  69.742  1.00 82.31           C  
ANISOU 4868  C   PRO B 200     9361  14145   7769    554   -922  -1278       C  
ATOM   4869  O   PRO B 200      -1.673   0.122  69.115  1.00 81.40           O  
ANISOU 4869  O   PRO B 200     9196  14000   7733    753   -859  -1151       O  
ATOM   4870  CB  PRO B 200       0.762   1.210  70.485  1.00 84.97           C  
ANISOU 4870  CB  PRO B 200     9184  15285   7816    542  -1176  -1508       C  
ATOM   4871  CG  PRO B 200       1.112  -0.180  70.890  1.00 90.62           C  
ANISOU 4871  CG  PRO B 200     9797  16192   8441    963  -1213  -1379       C  
ATOM   4872  CD  PRO B 200       0.324  -0.436  72.154  1.00 86.41           C  
ANISOU 4872  CD  PRO B 200     9495  15545   7790   1186  -1232  -1292       C  
ATOM   4873  N   GLN B 201      -2.486   2.188  69.463  1.00 77.17           N  
ANISOU 4873  N   GLN B 201     8910  13195   7216    314   -856  -1314       N  
ATOM   4874  CA  GLN B 201      -3.417   2.104  68.346  1.00 74.88           C  
ANISOU 4874  CA  GLN B 201     8764  12555   7131    267   -716  -1205       C  
ATOM   4875  C   GLN B 201      -2.929   2.997  67.199  1.00 79.43           C  
ANISOU 4875  C   GLN B 201     9264  13117   7799    -74   -696  -1307       C  
ATOM   4876  O   GLN B 201      -1.976   3.758  67.389  1.00 81.19           O  
ANISOU 4876  O   GLN B 201     9349  13571   7929   -294   -780  -1468       O  
ATOM   4877  CB  GLN B 201      -4.858   2.438  68.785  1.00 74.72           C  
ANISOU 4877  CB  GLN B 201     9039  12189   7165    304   -640  -1136       C  
ATOM   4878  CG  GLN B 201      -5.547   1.350  69.618  1.00 86.82           C  
ANISOU 4878  CG  GLN B 201    10670  13668   8649    642   -606   -987       C  
ATOM   4879  CD  GLN B 201      -5.650  -0.010  68.951  1.00114.63           C  
ANISOU 4879  CD  GLN B 201    14143  17148  12264    859   -532   -830       C  
ATOM   4880  OE1 GLN B 201      -5.886  -0.145  67.738  1.00113.31           O  
ANISOU 4880  OE1 GLN B 201    13969  16828  12256    774   -455   -788       O  
ATOM   4881  NE2 GLN B 201      -5.495  -1.057  69.747  1.00105.89           N  
ANISOU 4881  NE2 GLN B 201    13024  16163  11048   1151   -552   -738       N  
ATOM   4882  N   CYS B 202      -3.555   2.886  66.015  1.00 74.22           N  
ANISOU 4882  N   CYS B 202     8691  12200   7309   -124   -584  -1216       N  
ATOM   4883  CA  CYS B 202      -3.173   3.663  64.835  1.00 74.58           C  
ANISOU 4883  CA  CYS B 202     8694  12204   7439   -431   -545  -1284       C  
ATOM   4884  C   CYS B 202      -4.403   4.279  64.173  1.00 78.68           C  
ANISOU 4884  C   CYS B 202     9476  12321   8097   -537   -449  -1218       C  
ATOM   4885  O   CYS B 202      -4.802   3.911  63.065  1.00 76.57           O  
ANISOU 4885  O   CYS B 202     9236  11904   7954   -527   -366  -1125       O  
ATOM   4886  CB  CYS B 202      -2.367   2.807  63.859  1.00 74.83           C  
ANISOU 4886  CB  CYS B 202     8499  12426   7509   -376   -518  -1251       C  
ATOM   4887  SG  CYS B 202      -1.566   3.742  62.529  1.00 79.65           S  
ANISOU 4887  SG  CYS B 202     8999  13093   8170   -771   -477  -1355       S  
ATOM   4888  N   GLY B 203      -5.013   5.211  64.876  1.00 77.34           N  
ANISOU 4888  N   GLY B 203     9501  11987   7898   -621   -464  -1270       N  
ATOM   4889  CA  GLY B 203      -6.213   5.861  64.369  1.00 76.01           C  
ANISOU 4889  CA  GLY B 203     9585  11449   7846   -687   -382  -1212       C  
ATOM   4890  C   GLY B 203      -5.951   7.071  63.500  1.00 78.92           C  
ANISOU 4890  C   GLY B 203    10029  11700   8255  -1017   -359  -1291       C  
ATOM   4891  O   GLY B 203      -4.868   7.663  63.551  1.00 81.10           O  
ANISOU 4891  O   GLY B 203    10193  12169   8451  -1249   -410  -1425       O  
ATOM   4892  N   LEU B 204      -6.973   7.466  62.733  1.00 71.61           N  
ANISOU 4892  N   LEU B 204     9303  10458   7446  -1041   -282  -1208       N  
ATOM   4893  CA  LEU B 204      -6.954   8.639  61.867  1.00 70.97           C  
ANISOU 4893  CA  LEU B 204     9364  10193   7406  -1322   -245  -1248       C  
ATOM   4894  C   LEU B 204      -7.658   9.785  62.592  1.00 74.18           C  
ANISOU 4894  C   LEU B 204    10035  10362   7786  -1378   -251  -1311       C  
ATOM   4895  O   LEU B 204      -8.519   9.537  63.434  1.00 72.60           O  
ANISOU 4895  O   LEU B 204     9923  10080   7580  -1158   -253  -1274       O  
ATOM   4896  CB  LEU B 204      -7.670   8.303  60.546  1.00 69.16           C  
ANISOU 4896  CB  LEU B 204     9196   9774   7309  -1273   -165  -1108       C  
ATOM   4897  CG  LEU B 204      -7.293   9.108  59.306  1.00 73.96           C  
ANISOU 4897  CG  LEU B 204     9867  10289   7947  -1549   -120  -1119       C  
ATOM   4898  CD1 LEU B 204      -5.869   8.814  58.864  1.00 75.23           C  
ANISOU 4898  CD1 LEU B 204     9773  10756   8054  -1717   -130  -1189       C  
ATOM   4899  CD2 LEU B 204      -8.239   8.792  58.173  1.00 74.17           C  
ANISOU 4899  CD2 LEU B 204     9989  10108   8085  -1451    -56   -976       C  
ATOM   4900  N   ASN B 205      -7.286  11.032  62.276  1.00 73.07           N  
ANISOU 4900  N   ASN B 205    10030  10109   7624  -1674   -244  -1406       N  
ATOM   4901  CA  ASN B 205      -7.841  12.247  62.882  1.00 74.34           C  
ANISOU 4901  CA  ASN B 205    10473  10020   7754  -1756   -242  -1485       C  
ATOM   4902  C   ASN B 205      -9.376  12.221  62.940  1.00 78.40           C  
ANISOU 4902  C   ASN B 205    11190  10247   8350  -1498   -193  -1368       C  
ATOM   4903  O   ASN B 205     -10.062  12.064  61.931  1.00 76.26           O  
ANISOU 4903  O   ASN B 205    10978   9811   8185  -1431   -137  -1241       O  
ATOM   4904  CB  ASN B 205      -7.293  13.503  62.203  1.00 76.38           C  
ANISOU 4904  CB  ASN B 205    10879  10141   8002  -2115   -214  -1568       C  
ATOM   4905  CG  ASN B 205      -7.632  14.776  62.929  1.00 86.05           C  
ANISOU 4905  CG  ASN B 205    12395  11128   9171  -2227   -218  -1683       C  
ATOM   4906  OD1 ASN B 205      -8.707  15.349  62.737  1.00 72.24           O  
ANISOU 4906  OD1 ASN B 205    10916   9051   7482  -2129   -168  -1618       O  
ATOM   4907  ND2 ASN B 205      -6.717  15.253  63.766  1.00 79.23           N  
ANISOU 4907  ND2 ASN B 205    11483  10431   8188  -2432   -279  -1864       N  
ATOM   4908  N   ASP B 206      -9.880  12.301  64.165  1.00 78.11           N  
ANISOU 4908  N   ASP B 206    11234  10193   8253  -1345   -216  -1417       N  
ATOM   4909  CA  ASP B 206     -11.279  12.203  64.560  1.00 77.79           C  
ANISOU 4909  CA  ASP B 206    11342   9952   8261  -1079   -172  -1333       C  
ATOM   4910  C   ASP B 206     -12.060  13.518  64.540  1.00 81.98           C  
ANISOU 4910  C   ASP B 206    12189  10151   8809  -1125   -133  -1372       C  
ATOM   4911  O   ASP B 206     -13.280  13.466  64.713  1.00 81.13           O  
ANISOU 4911  O   ASP B 206    12190   9881   8755   -896    -88  -1295       O  
ATOM   4912  CB  ASP B 206     -11.341  11.618  65.980  1.00 80.86           C  
ANISOU 4912  CB  ASP B 206    11655  10518   8550   -891   -209  -1375       C  
ATOM   4913  CG  ASP B 206     -12.181  10.372  66.108  1.00100.09           C  
ANISOU 4913  CG  ASP B 206    13990  12995  11044   -592   -168  -1225       C  
ATOM   4914  OD1 ASP B 206     -13.430  10.489  66.069  1.00101.09           O1-
ANISOU 4914  OD1 ASP B 206    14252  12915  11244   -436   -104  -1151       O1-
ATOM   4915  OD2 ASP B 206     -11.595   9.279  66.269  1.00112.27           O  
ANISOU 4915  OD2 ASP B 206    15320  14780  12558   -512   -197  -1186       O  
ATOM   4916  N   GLU B 207     -11.384  14.687  64.407  1.00 78.92           N  
ANISOU 4916  N   GLU B 207    11953   9664   8370  -1411   -146  -1495       N  
ATOM   4917  CA  GLU B 207     -12.053  16.000  64.411  1.00 79.25           C  
ANISOU 4917  CA  GLU B 207    12335   9360   8417  -1455   -105  -1539       C  
ATOM   4918  C   GLU B 207     -13.135  16.058  63.327  1.00 79.61           C  
ANISOU 4918  C   GLU B 207    12499   9161   8589  -1308    -43  -1375       C  
ATOM   4919  O   GLU B 207     -12.882  15.688  62.178  1.00 77.16           O  
ANISOU 4919  O   GLU B 207    12090   8883   8344  -1383    -30  -1276       O  
ATOM   4920  CB  GLU B 207     -11.050  17.163  64.254  1.00 83.41           C  
ANISOU 4920  CB  GLU B 207    13008   9809   8876  -1829   -117  -1686       C  
ATOM   4921  CG  GLU B 207     -10.143  17.402  65.452  1.00 97.61           C  
ANISOU 4921  CG  GLU B 207    14750  11806  10532  -1984   -185  -1885       C  
ATOM   4922  CD  GLU B 207     -10.570  18.509  66.400  1.00140.42           C  
ANISOU 4922  CD  GLU B 207    20480  16999  15875  -1997   -178  -2027       C  
ATOM   4923  OE1 GLU B 207     -10.912  19.612  65.915  1.00149.67           O  
ANISOU 4923  OE1 GLU B 207    21960  17829  17077  -2107   -122  -2041       O  
ATOM   4924  OE2 GLU B 207     -10.540  18.281  67.633  1.00142.48           O1-
ANISOU 4924  OE2 GLU B 207    20687  17417  16032  -1893   -226  -2127       O1-
ATOM   4925  N   THR B 208     -14.350  16.474  63.724  1.00 75.85           N  
ANISOU 4925  N   THR B 208    12217   8468   8136  -1082     -7  -1350       N  
ATOM   4926  CA  THR B 208     -15.551  16.581  62.891  1.00 74.88           C  
ANISOU 4926  CA  THR B 208    12205   8127   8117   -889     41  -1207       C  
ATOM   4927  C   THR B 208     -15.309  17.281  61.545  1.00 81.55           C  
ANISOU 4927  C   THR B 208    13200   8782   9003  -1074     59  -1147       C  
ATOM   4928  O   THR B 208     -15.899  16.884  60.541  1.00 79.98           O  
ANISOU 4928  O   THR B 208    12955   8546   8889   -962     74  -1003       O  
ATOM   4929  CB  THR B 208     -16.721  17.222  63.683  1.00 83.32           C  
ANISOU 4929  CB  THR B 208    13490   8993   9175   -652     77  -1237       C  
ATOM   4930  OG1 THR B 208     -17.847  17.394  62.822  1.00 77.64           O  
ANISOU 4930  OG1 THR B 208    12865   8083   8550   -464    113  -1104       O  
ATOM   4931  CG2 THR B 208     -16.358  18.576  64.345  1.00 90.81           C  
ANISOU 4931  CG2 THR B 208    14738   9740  10027   -807     80  -1405       C  
ATOM   4932  N   TRP B 209     -14.446  18.294  61.512  1.00 82.08           N  
ANISOU 4932  N   TRP B 209    13447   8736   9003  -1364     59  -1256       N  
ATOM   4933  CA  TRP B 209     -14.230  19.018  60.277  1.00 83.54           C  
ANISOU 4933  CA  TRP B 209    13812   8718   9212  -1548     91  -1192       C  
ATOM   4934  C   TRP B 209     -13.181  18.397  59.395  1.00 81.92           C  
ANISOU 4934  C   TRP B 209    13378   8734   9014  -1775     83  -1154       C  
ATOM   4935  O   TRP B 209     -13.303  18.551  58.182  1.00 82.62           O  
ANISOU 4935  O   TRP B 209    13540   8709   9142  -1823    114  -1038       O  
ATOM   4936  CB  TRP B 209     -13.986  20.501  60.534  1.00 87.23           C  
ANISOU 4936  CB  TRP B 209    14645   8888   9611  -1746    119  -1308       C  
ATOM   4937  CG  TRP B 209     -15.280  21.187  60.890  1.00 90.28           C  
ANISOU 4937  CG  TRP B 209    15309   8978  10014  -1462    147  -1286       C  
ATOM   4938  CD1 TRP B 209     -15.676  21.601  62.131  1.00 94.41           C  
ANISOU 4938  CD1 TRP B 209    15957   9431  10485  -1339    147  -1411       C  
ATOM   4939  CD2 TRP B 209     -16.421  21.355  60.028  1.00 90.00           C  
ANISOU 4939  CD2 TRP B 209    15407   8736  10052  -1214    172  -1123       C  
ATOM   4940  NE1 TRP B 209     -16.956  22.109  62.074  1.00 94.63           N  
ANISOU 4940  NE1 TRP B 209    16205   9199  10550  -1040    183  -1342       N  
ATOM   4941  CE2 TRP B 209     -17.441  21.957  60.797  1.00 95.21           C  
ANISOU 4941  CE2 TRP B 209    16278   9195  10702   -952    193  -1163       C  
ATOM   4942  CE3 TRP B 209     -16.671  21.074  58.670  1.00 90.54           C  
ANISOU 4942  CE3 TRP B 209    15438   8783  10181  -1183    177   -952       C  
ATOM   4943  CZ2 TRP B 209     -18.682  22.305  60.248  1.00 94.84           C  
ANISOU 4943  CZ2 TRP B 209    16391   8935  10708   -657    214  -1038       C  
ATOM   4944  CZ3 TRP B 209     -17.897  21.422  58.129  1.00 92.30           C  
ANISOU 4944  CZ3 TRP B 209    15828   8794  10450   -902    189   -828       C  
ATOM   4945  CH2 TRP B 209     -18.885  22.031  58.913  1.00 94.01           C  
ANISOU 4945  CH2 TRP B 209    16238   8823  10660   -637    205   -870       C  
ATOM   4946  N   TYR B 210     -12.210  17.641  59.952  1.00 74.00           N  
ANISOU 4946  N   TYR B 210    12091   8058   7969  -1881     43  -1241       N  
ATOM   4947  CA  TYR B 210     -11.243  16.947  59.105  1.00 72.14           C  
ANISOU 4947  CA  TYR B 210    11607   8061   7741  -2054     41  -1204       C  
ATOM   4948  C   TYR B 210     -11.977  15.799  58.377  1.00 73.62           C  
ANISOU 4948  C   TYR B 210    11623   8328   8022  -1793     47  -1037       C  
ATOM   4949  O   TYR B 210     -11.741  15.598  57.180  1.00 74.83           O  
ANISOU 4949  O   TYR B 210    11731   8494   8206  -1882     74   -948       O  
ATOM   4950  CB  TYR B 210     -10.021  16.411  59.881  1.00 73.68           C  
ANISOU 4950  CB  TYR B 210    11528   8606   7861  -2199    -10  -1338       C  
ATOM   4951  CG  TYR B 210      -9.364  15.248  59.159  1.00 75.15           C  
ANISOU 4951  CG  TYR B 210    11392   9087   8077  -2205    -14  -1270       C  
ATOM   4952  CD1 TYR B 210      -8.504  15.465  58.083  1.00 78.08           C  
ANISOU 4952  CD1 TYR B 210    11718   9508   8441  -2476     25  -1260       C  
ATOM   4953  CD2 TYR B 210      -9.712  13.933  59.455  1.00 73.76           C  
ANISOU 4953  CD2 TYR B 210    10983   9103   7938  -1925    -41  -1200       C  
ATOM   4954  CE1 TYR B 210      -7.952  14.404  57.372  1.00 77.26           C  
ANISOU 4954  CE1 TYR B 210    11330   9663   8361  -2458     31  -1200       C  
ATOM   4955  CE2 TYR B 210      -9.174  12.867  58.747  1.00 74.08           C  
ANISOU 4955  CE2 TYR B 210    10762   9377   8007  -1906    -37  -1136       C  
ATOM   4956  CZ  TYR B 210      -8.301  13.105  57.698  1.00 84.48           C  
ANISOU 4956  CZ  TYR B 210    12028  10756   9315  -2164     -2  -1140       C  
ATOM   4957  OH  TYR B 210      -7.795  12.045  56.983  1.00 86.15           O  
ANISOU 4957  OH  TYR B 210    11987  11196   9550  -2125     11  -1084       O  
ATOM   4958  N   ILE B 211     -12.843  15.042  59.109  1.00 64.89           N  
ANISOU 4958  N   ILE B 211    10423   7281   6951  -1489     27  -1002       N  
ATOM   4959  CA  ILE B 211     -13.637  13.938  58.570  1.00 61.51           C  
ANISOU 4959  CA  ILE B 211     9841   6918   6611  -1247     35   -862       C  
ATOM   4960  C   ILE B 211     -14.410  14.425  57.338  1.00 66.15           C  
ANISOU 4960  C   ILE B 211    10605   7273   7257  -1214     65   -742       C  
ATOM   4961  O   ILE B 211     -14.213  13.877  56.249  1.00 64.93           O  
ANISOU 4961  O   ILE B 211    10342   7193   7135  -1257     75   -658       O  
ATOM   4962  CB  ILE B 211     -14.586  13.310  59.657  1.00 63.36           C  
ANISOU 4962  CB  ILE B 211    10015   7194   6866   -951     28   -853       C  
ATOM   4963  CG1 ILE B 211     -13.790  12.510  60.733  1.00 63.33           C  
ANISOU 4963  CG1 ILE B 211     9796   7471   6796   -947     -7   -935       C  
ATOM   4964  CG2 ILE B 211     -15.704  12.442  59.029  1.00 61.44           C  
ANISOU 4964  CG2 ILE B 211     9685   6937   6723   -715     50   -709       C  
ATOM   4965  CD1 ILE B 211     -14.610  11.979  61.913  1.00 63.22           C  
ANISOU 4965  CD1 ILE B 211     9750   7497   6773   -688     -2   -932       C  
ATOM   4966  N   LEU B 212     -15.242  15.491  57.509  1.00 63.69           N  
ANISOU 4966  N   LEU B 212    10576   6680   6943  -1135     79   -740       N  
ATOM   4967  CA  LEU B 212     -16.127  16.047  56.475  1.00 63.51           C  
ANISOU 4967  CA  LEU B 212    10748   6421   6960  -1044     96   -621       C  
ATOM   4968  C   LEU B 212     -15.405  16.759  55.328  1.00 69.75           C  
ANISOU 4968  C   LEU B 212    11691   7099   7714  -1307    120   -588       C  
ATOM   4969  O   LEU B 212     -15.864  16.664  54.184  1.00 70.22           O  
ANISOU 4969  O   LEU B 212    11783   7095   7801  -1249    124   -462       O  
ATOM   4970  CB  LEU B 212     -17.211  16.954  57.074  1.00 64.36           C  
ANISOU 4970  CB  LEU B 212    11110   6276   7069   -844    105   -633       C  
ATOM   4971  CG  LEU B 212     -18.060  16.350  58.194  1.00 67.74           C  
ANISOU 4971  CG  LEU B 212    11411   6800   7525   -574    100   -659       C  
ATOM   4972  CD1 LEU B 212     -18.825  17.425  58.939  1.00 69.52           C  
ANISOU 4972  CD1 LEU B 212    11905   6785   7723   -430    120   -715       C  
ATOM   4973  CD2 LEU B 212     -18.966  15.211  57.692  1.00 65.93           C  
ANISOU 4973  CD2 LEU B 212    10961   6705   7383   -352     94   -536       C  
ATOM   4974  N   SER B 213     -14.295  17.461  55.600  1.00 66.89           N  
ANISOU 4974  N   SER B 213    11418   6718   7281  -1605    137   -699       N  
ATOM   4975  CA  SER B 213     -13.578  18.111  54.506  1.00 67.67           C  
ANISOU 4975  CA  SER B 213    11656   6717   7338  -1883    178   -664       C  
ATOM   4976  C   SER B 213     -12.852  17.057  53.656  1.00 70.71           C  
ANISOU 4976  C   SER B 213    11747   7384   7734  -1983    183   -616       C  
ATOM   4977  O   SER B 213     -12.876  17.153  52.432  1.00 68.51           O  
ANISOU 4977  O   SER B 213    11538   7043   7452  -2043    212   -508       O  
ATOM   4978  CB  SER B 213     -12.620  19.170  55.029  1.00 71.29           C  
ANISOU 4978  CB  SER B 213    12293   7077   7718  -2202    205   -805       C  
ATOM   4979  OG  SER B 213     -11.711  18.603  55.952  1.00 75.18           O  
ANISOU 4979  OG  SER B 213    12522   7862   8182  -2315    174   -945       O  
ATOM   4980  N   SER B 214     -12.289  16.008  54.313  1.00 69.00           N  
ANISOU 4980  N   SER B 214    11211   7479   7528  -1962    153   -688       N  
ATOM   4981  CA  SER B 214     -11.568  14.896  53.668  1.00 68.59           C  
ANISOU 4981  CA  SER B 214    10860   7715   7485  -2017    159   -662       C  
ATOM   4982  C   SER B 214     -12.458  14.006  52.760  1.00 70.45           C  
ANISOU 4982  C   SER B 214    11014   7964   7789  -1785    155   -519       C  
ATOM   4983  O   SER B 214     -11.978  13.497  51.746  1.00 68.84           O  
ANISOU 4983  O   SER B 214    10693   7883   7578  -1872    181   -470       O  
ATOM   4984  CB  SER B 214     -10.818  14.056  54.701  1.00 71.92           C  
ANISOU 4984  CB  SER B 214    10997   8439   7891  -2008    122   -772       C  
ATOM   4985  OG  SER B 214     -11.678  13.301  55.539  1.00 77.72           O  
ANISOU 4985  OG  SER B 214    11645   9212   8673  -1706     85   -753       O  
ATOM   4986  N   CYS B 215     -13.745  13.844  53.112  1.00 66.54           N  
ANISOU 4986  N   CYS B 215    10579   7352   7353  -1501    127   -462       N  
ATOM   4987  CA  CYS B 215     -14.685  13.068  52.312  1.00 65.38           C  
ANISOU 4987  CA  CYS B 215    10359   7215   7268  -1293    116   -342       C  
ATOM   4988  C   CYS B 215     -15.049  13.847  51.074  1.00 69.57           C  
ANISOU 4988  C   CYS B 215    11111   7547   7773  -1343    130   -241       C  
ATOM   4989  O   CYS B 215     -15.157  13.269  50.000  1.00 67.80           O  
ANISOU 4989  O   CYS B 215    10808   7395   7556  -1326    133   -160       O  
ATOM   4990  CB  CYS B 215     -15.919  12.695  53.127  1.00 65.46           C  
ANISOU 4990  CB  CYS B 215    10344   7188   7342   -999     88   -324       C  
ATOM   4991  SG  CYS B 215     -15.610  11.455  54.412  1.00 68.56           S  
ANISOU 4991  SG  CYS B 215    10457   7835   7756   -898     79   -402       S  
ATOM   4992  N   ILE B 216     -15.202  15.173  51.215  1.00 69.64           N  
ANISOU 4992  N   ILE B 216    11418   7300   7741  -1408    142   -247       N  
ATOM   4993  CA  ILE B 216     -15.503  16.062  50.085  1.00 70.90           C  
ANISOU 4993  CA  ILE B 216    11845   7236   7857  -1455    159   -141       C  
ATOM   4994  C   ILE B 216     -14.288  16.166  49.153  1.00 72.79           C  
ANISOU 4994  C   ILE B 216    12076   7553   8028  -1770    214   -136       C  
ATOM   4995  O   ILE B 216     -14.440  15.972  47.956  1.00 73.65           O  
ANISOU 4995  O   ILE B 216    12203   7669   8112  -1768    222    -31       O  
ATOM   4996  CB  ILE B 216     -16.078  17.444  50.513  1.00 75.87           C  
ANISOU 4996  CB  ILE B 216    12830   7537   8461  -1402    164   -142       C  
ATOM   4997  CG1 ILE B 216     -17.414  17.269  51.280  1.00 75.26           C  
ANISOU 4997  CG1 ILE B 216    12736   7411   8450  -1051    118   -133       C  
ATOM   4998  CG2 ILE B 216     -16.267  18.351  49.284  1.00 77.76           C  
ANISOU 4998  CG2 ILE B 216    13368   7540   8637  -1459    187    -17       C  
ATOM   4999  CD1 ILE B 216     -17.790  18.445  52.219  1.00 84.60           C  
ANISOU 4999  CD1 ILE B 216    14201   8332   9611   -987    130   -199       C  
ATOM   5000  N   GLY B 217     -13.108  16.399  49.715  1.00 66.82           N  
ANISOU 5000  N   GLY B 217    11267   6887   7235  -2032    249   -255       N  
ATOM   5001  CA  GLY B 217     -11.864  16.493  48.962  1.00 67.11           C  
ANISOU 5001  CA  GLY B 217    11256   7038   7204  -2355    313   -273       C  
ATOM   5002  C   GLY B 217     -11.458  15.237  48.203  1.00 68.70           C  
ANISOU 5002  C   GLY B 217    11156   7529   7416  -2340    320   -242       C  
ATOM   5003  O   GLY B 217     -11.128  15.312  47.014  1.00 68.24           O  
ANISOU 5003  O   GLY B 217    11144   7480   7305  -2471    370   -169       O  
ATOM   5004  N   SER B 218     -11.470  14.072  48.873  1.00 62.93           N  
ANISOU 5004  N   SER B 218    10132   7031   6747  -2176    278   -297       N  
ATOM   5005  CA  SER B 218     -11.054  12.815  48.237  1.00 60.65           C  
ANISOU 5005  CA  SER B 218     9565   7009   6470  -2143    290   -283       C  
ATOM   5006  C   SER B 218     -12.153  12.013  47.546  1.00 62.94           C  
ANISOU 5006  C   SER B 218     9822   7281   6811  -1885    257   -176       C  
ATOM   5007  O   SER B 218     -11.809  11.144  46.743  1.00 62.82           O  
ANISOU 5007  O   SER B 218     9645   7438   6787  -1893    280   -156       O  
ATOM   5008  CB  SER B 218     -10.332  11.918  49.226  1.00 61.01           C  
ANISOU 5008  CB  SER B 218     9317   7325   6540  -2117    271   -396       C  
ATOM   5009  OG  SER B 218      -9.192  12.600  49.704  1.00 70.28           O  
ANISOU 5009  OG  SER B 218    10479   8571   7651  -2388    297   -506       O  
ATOM   5010  N   PHE B 219     -13.446  12.261  47.843  1.00 57.49           N  
ANISOU 5010  N   PHE B 219     9270   6405   6170  -1660    206   -118       N  
ATOM   5011  CA  PHE B 219     -14.473  11.456  47.206  1.00 55.03           C  
ANISOU 5011  CA  PHE B 219     8894   6112   5905  -1437    170    -33       C  
ATOM   5012  C   PHE B 219     -15.544  12.255  46.492  1.00 62.01           C  
ANISOU 5012  C   PHE B 219    10025   6768   6768  -1332    140     78       C  
ATOM   5013  O   PHE B 219     -15.618  12.144  45.278  1.00 63.35           O  
ANISOU 5013  O   PHE B 219    10231   6950   6889  -1361    144    155       O  
ATOM   5014  CB  PHE B 219     -15.102  10.441  48.173  1.00 53.92           C  
ANISOU 5014  CB  PHE B 219     8560   6071   5855  -1210    133    -70       C  
ATOM   5015  CG  PHE B 219     -16.115   9.518  47.527  1.00 53.56           C  
ANISOU 5015  CG  PHE B 219     8424   6067   5861  -1018    103     -1       C  
ATOM   5016  CD1 PHE B 219     -15.704   8.402  46.800  1.00 54.72           C  
ANISOU 5016  CD1 PHE B 219     8392   6391   6008  -1043    122     -4       C  
ATOM   5017  CD2 PHE B 219     -17.480   9.765  47.640  1.00 54.84           C  
ANISOU 5017  CD2 PHE B 219     8674   6097   6066   -814     56     56       C  
ATOM   5018  CE1 PHE B 219     -16.644   7.551  46.198  1.00 53.85           C  
ANISOU 5018  CE1 PHE B 219     8208   6313   5940   -890     93     43       C  
ATOM   5019  CE2 PHE B 219     -18.418   8.913  47.036  1.00 55.90           C  
ANISOU 5019  CE2 PHE B 219     8704   6291   6243   -662     23    105       C  
ATOM   5020  CZ  PHE B 219     -17.992   7.817  46.316  1.00 52.49           C  
ANISOU 5020  CZ  PHE B 219     8111   6023   5810   -714     41     96       C  
ATOM   5021  N   PHE B 220     -16.391  13.007  47.210  1.00 59.33           N  
ANISOU 5021  N   PHE B 220     9849   6238   6455  -1190    107     87       N  
ATOM   5022  CA  PHE B 220     -17.539  13.714  46.626  1.00 59.87           C  
ANISOU 5022  CA  PHE B 220    10135   6104   6507  -1023     66    195       C  
ATOM   5023  C   PHE B 220     -17.199  14.787  45.570  1.00 65.08           C  
ANISOU 5023  C   PHE B 220    11080   6587   7061  -1179     95    280       C  
ATOM   5024  O   PHE B 220     -17.906  14.838  44.563  1.00 64.73           O  
ANISOU 5024  O   PHE B 220    11118   6497   6980  -1063     58    389       O  
ATOM   5025  CB  PHE B 220     -18.447  14.295  47.719  1.00 61.81           C  
ANISOU 5025  CB  PHE B 220    10488   6196   6802   -823     37    172       C  
ATOM   5026  CG  PHE B 220     -18.940  13.239  48.687  1.00 61.02           C  
ANISOU 5026  CG  PHE B 220    10127   6262   6794   -653     17    110       C  
ATOM   5027  CD1 PHE B 220     -19.839  12.255  48.275  1.00 62.33           C  
ANISOU 5027  CD1 PHE B 220    10114   6553   7016   -473    -21    158       C  
ATOM   5028  CD2 PHE B 220     -18.499  13.223  50.007  1.00 62.18           C  
ANISOU 5028  CD2 PHE B 220    10218   6444   6964   -686     40      4       C  
ATOM   5029  CE1 PHE B 220     -20.283  11.271  49.165  1.00 61.69           C  
ANISOU 5029  CE1 PHE B 220     9812   6610   7016   -341    -22    108       C  
ATOM   5030  CE2 PHE B 220     -18.962  12.253  50.903  1.00 63.16           C  
ANISOU 5030  CE2 PHE B 220    10126   6711   7159   -528     32    -37       C  
ATOM   5031  CZ  PHE B 220     -19.841  11.276  50.474  1.00 60.20           C  
ANISOU 5031  CZ  PHE B 220     9586   6443   6845   -363      8     18       C  
ATOM   5032  N   ALA B 221     -16.151  15.628  45.776  1.00 63.41           N  
ANISOU 5032  N   ALA B 221    11020   6281   6793  -1444    160    233       N  
ATOM   5033  CA  ALA B 221     -15.749  16.649  44.792  1.00 65.63           C  
ANISOU 5033  CA  ALA B 221    11593   6380   6965  -1630    210    318       C  
ATOM   5034  C   ALA B 221     -15.193  15.968  43.525  1.00 73.13           C  
ANISOU 5034  C   ALA B 221    12416   7517   7854  -1757    241    371       C  
ATOM   5035  O   ALA B 221     -15.721  16.261  42.443  1.00 74.24           O  
ANISOU 5035  O   ALA B 221    12723   7563   7923  -1687    224    498       O  
ATOM   5036  CB  ALA B 221     -14.748  17.628  45.380  1.00 67.71           C  
ANISOU 5036  CB  ALA B 221    12026   6514   7188  -1915    282    235       C  
ATOM   5037  N   PRO B 222     -14.251  14.977  43.610  1.00 69.65           N  
ANISOU 5037  N   PRO B 222    11674   7354   7434  -1895    276    281       N  
ATOM   5038  CA  PRO B 222     -13.822  14.278  42.389  1.00 69.71           C  
ANISOU 5038  CA  PRO B 222    11564   7541   7380  -1978    309    325       C  
ATOM   5039  C   PRO B 222     -14.952  13.492  41.715  1.00 74.81           C  
ANISOU 5039  C   PRO B 222    12135   8243   8048  -1710    231    402       C  
ATOM   5040  O   PRO B 222     -14.921  13.352  40.495  1.00 75.41           O  
ANISOU 5040  O   PRO B 222    12254   8362   8036  -1749    244    478       O  
ATOM   5041  CB  PRO B 222     -12.710  13.351  42.880  1.00 70.19           C  
ANISOU 5041  CB  PRO B 222    11307   7883   7478  -2111    353    196       C  
ATOM   5042  CG  PRO B 222     -12.261  13.926  44.148  1.00 74.90           C  
ANISOU 5042  CG  PRO B 222    11924   8424   8111  -2206    361     96       C  
ATOM   5043  CD  PRO B 222     -13.490  14.481  44.772  1.00 70.34           C  
ANISOU 5043  CD  PRO B 222    11529   7611   7584  -1975    291    136       C  
ATOM   5044  N   CYS B 223     -15.957  13.004  42.492  1.00 71.01           N  
ANISOU 5044  N   CYS B 223    11544   7766   7671  -1451    153    378       N  
ATOM   5045  CA  CYS B 223     -17.135  12.302  41.959  1.00 70.24           C  
ANISOU 5045  CA  CYS B 223    11365   7723   7601  -1206     72    436       C  
ATOM   5046  C   CYS B 223     -18.020  13.264  41.201  1.00 73.84           C  
ANISOU 5046  C   CYS B 223    12096   7979   7979  -1091     22    566       C  
ATOM   5047  O   CYS B 223     -18.693  12.848  40.260  1.00 73.02           O  
ANISOU 5047  O   CYS B 223    11965   7943   7836   -972    -35    633       O  
ATOM   5048  CB  CYS B 223     -17.914  11.581  43.054  1.00 69.67           C  
ANISOU 5048  CB  CYS B 223    11103   7713   7658   -995     22    373       C  
ATOM   5049  SG  CYS B 223     -17.219   9.973  43.513  1.00 72.39           S  
ANISOU 5049  SG  CYS B 223    11095   8333   8079  -1035     57    259       S  
ATOM   5050  N   LEU B 224     -18.027  14.542  41.618  1.00 71.55           N  
ANISOU 5050  N   LEU B 224    12080   7445   7662  -1117     39    598       N  
ATOM   5051  CA  LEU B 224     -18.786  15.597  40.970  1.00 73.92           C  
ANISOU 5051  CA  LEU B 224    12692   7517   7877   -995     -1    730       C  
ATOM   5052  C   LEU B 224     -18.102  15.953  39.665  1.00 80.09           C  
ANISOU 5052  C   LEU B 224    13641   8277   8513  -1195     52    822       C  
ATOM   5053  O   LEU B 224     -18.778  16.031  38.643  1.00 81.09           O  
ANISOU 5053  O   LEU B 224    13869   8388   8554  -1062     -6    936       O  
ATOM   5054  CB  LEU B 224     -18.912  16.835  41.872  1.00 75.92           C  
ANISOU 5054  CB  LEU B 224    13210   7492   8144   -970     17    724       C  
ATOM   5055  CG  LEU B 224     -19.544  18.074  41.224  1.00 83.55           C  
ANISOU 5055  CG  LEU B 224    14562   8175   9009   -852     -7    867       C  
ATOM   5056  CD1 LEU B 224     -21.074  17.966  41.170  1.00 83.92           C  
ANISOU 5056  CD1 LEU B 224    14576   8222   9087   -464   -125    931       C  
ATOM   5057  CD2 LEU B 224     -19.082  19.340  41.907  1.00 86.95           C  
ANISOU 5057  CD2 LEU B 224    15305   8310   9420   -981     63    845       C  
ATOM   5058  N   ILE B 225     -16.763  16.141  39.689  1.00 77.70           N  
ANISOU 5058  N   ILE B 225    13353   7997   8173  -1515    162    768       N  
ATOM   5059  CA  ILE B 225     -15.972  16.454  38.493  1.00 79.60           C  
ANISOU 5059  CA  ILE B 225    13736   8239   8269  -1749    242    845       C  
ATOM   5060  C   ILE B 225     -16.194  15.362  37.430  1.00 83.28           C  
ANISOU 5060  C   ILE B 225    14007   8947   8691  -1672    205    874       C  
ATOM   5061  O   ILE B 225     -16.692  15.682  36.358  1.00 85.09           O  
ANISOU 5061  O   ILE B 225    14418   9113   8800  -1596    172   1002       O  
ATOM   5062  CB  ILE B 225     -14.468  16.686  38.819  1.00 83.57           C  
ANISOU 5062  CB  ILE B 225    14206   8789   8756  -2117    372    752       C  
ATOM   5063  CG1 ILE B 225     -14.278  17.886  39.773  1.00 85.42           C  
ANISOU 5063  CG1 ILE B 225    14686   8757   9013  -2220    407    721       C  
ATOM   5064  CG2 ILE B 225     -13.641  16.863  37.533  1.00 86.29           C  
ANISOU 5064  CG2 ILE B 225    14653   9185   8948  -2367    472    826       C  
ATOM   5065  CD1 ILE B 225     -13.133  17.717  40.798  1.00 91.78           C  
ANISOU 5065  CD1 ILE B 225    15295   9692   9883  -2467    473    553       C  
ATOM   5066  N   MET B 226     -15.904  14.083  37.764  1.00 77.85           N  
ANISOU 5066  N   MET B 226    12965   8521   8093  -1668    203    755       N  
ATOM   5067  CA  MET B 226     -16.066  12.898  36.908  1.00 77.40           C  
ANISOU 5067  CA  MET B 226    12698   8698   8011  -1602    174    746       C  
ATOM   5068  C   MET B 226     -17.408  12.863  36.170  1.00 80.68           C  
ANISOU 5068  C   MET B 226    13196   9077   8380  -1345     55    847       C  
ATOM   5069  O   MET B 226     -17.422  12.684  34.950  1.00 80.81           O  
ANISOU 5069  O   MET B 226    13265   9170   8269  -1368     50    913       O  
ATOM   5070  CB  MET B 226     -15.924  11.606  37.740  1.00 77.89           C  
ANISOU 5070  CB  MET B 226    12411   8970   8216  -1543    166    605       C  
ATOM   5071  CG  MET B 226     -14.504  11.129  37.914  1.00 81.87           C  
ANISOU 5071  CG  MET B 226    12740   9645   8720  -1776    275    503       C  
ATOM   5072  SD  MET B 226     -14.288  10.275  39.498  1.00 84.90           S  
ANISOU 5072  SD  MET B 226    12837  10145   9275  -1701    265    357       S  
ATOM   5073  CE  MET B 226     -14.950   8.727  39.139  1.00 79.69           C  
ANISOU 5073  CE  MET B 226    11944   9662   8671  -1505    212    323       C  
ATOM   5074  N   GLY B 227     -18.498  13.023  36.931  1.00 75.91           N  
ANISOU 5074  N   GLY B 227    12590   8380   7874  -1106    -39    851       N  
ATOM   5075  CA  GLY B 227     -19.875  12.982  36.456  1.00 76.03           C  
ANISOU 5075  CA  GLY B 227    12633   8389   7868   -833   -167    927       C  
ATOM   5076  C   GLY B 227     -20.229  14.109  35.517  1.00 83.93           C  
ANISOU 5076  C   GLY B 227    13969   9211   8708   -779   -198   1087       C  
ATOM   5077  O   GLY B 227     -20.767  13.859  34.435  1.00 84.98           O  
ANISOU 5077  O   GLY B 227    14117   9437   8733   -683   -271   1158       O  
ATOM   5078  N   LEU B 228     -19.899  15.356  35.910  1.00 81.86           N  
ANISOU 5078  N   LEU B 228    13996   8690   8418   -848   -143   1144       N  
ATOM   5079  CA  LEU B 228     -20.175  16.555  35.109  1.00 83.94           C  
ANISOU 5079  CA  LEU B 228    14641   8728   8524   -797   -156   1310       C  
ATOM   5080  C   LEU B 228     -19.397  16.575  33.792  1.00 86.57           C  
ANISOU 5080  C   LEU B 228    15095   9119   8680  -1010    -87   1390       C  
ATOM   5081  O   LEU B 228     -19.941  17.012  32.774  1.00 87.27           O  
ANISOU 5081  O   LEU B 228    15393   9150   8615   -888   -147   1533       O  
ATOM   5082  CB  LEU B 228     -19.910  17.855  35.891  1.00 85.78           C  
ANISOU 5082  CB  LEU B 228    15178   8642   8773   -854    -91   1337       C  
ATOM   5083  CG  LEU B 228     -20.508  18.037  37.285  1.00 90.49           C  
ANISOU 5083  CG  LEU B 228    15711   9144   9527   -677   -129   1252       C  
ATOM   5084  CD1 LEU B 228     -20.437  19.488  37.708  1.00 93.21           C  
ANISOU 5084  CD1 LEU B 228    16452   9130   9834   -689    -80   1312       C  
ATOM   5085  CD2 LEU B 228     -21.930  17.474  37.401  1.00 92.86           C  
ANISOU 5085  CD2 LEU B 228    15819   9570   9893   -316   -272   1254       C  
ATOM   5086  N   VAL B 229     -18.121  16.128  33.825  1.00 81.43           N  
ANISOU 5086  N   VAL B 229    14312   8589   8039  -1318     40   1299       N  
ATOM   5087  CA  VAL B 229     -17.236  16.051  32.658  1.00 82.42           C  
ANISOU 5087  CA  VAL B 229    14507   8807   8002  -1553    135   1349       C  
ATOM   5088  C   VAL B 229     -17.766  14.987  31.688  1.00 85.73           C  
ANISOU 5088  C   VAL B 229    14738   9478   8357  -1418     50   1349       C  
ATOM   5089  O   VAL B 229     -17.875  15.269  30.492  1.00 87.99           O  
ANISOU 5089  O   VAL B 229    15213   9762   8457  -1417     41   1470       O  
ATOM   5090  CB  VAL B 229     -15.751  15.821  33.039  1.00 85.58           C  
ANISOU 5090  CB  VAL B 229    14770   9306   8440  -1898    292   1232       C  
ATOM   5091  CG1 VAL B 229     -14.929  15.447  31.821  1.00 86.06           C  
ANISOU 5091  CG1 VAL B 229    14812   9541   8344  -2103    388   1258       C  
ATOM   5092  CG2 VAL B 229     -15.158  17.054  33.712  1.00 87.09           C  
ANISOU 5092  CG2 VAL B 229    15215   9235   8639  -2090    385   1249       C  
ATOM   5093  N   TYR B 230     -18.143  13.794  32.211  1.00 78.35           N  
ANISOU 5093  N   TYR B 230    13457   8747   7568  -1300    -15   1215       N  
ATOM   5094  CA  TYR B 230     -18.708  12.715  31.403  1.00 76.97           C  
ANISOU 5094  CA  TYR B 230    13092   8802   7350  -1180   -100   1187       C  
ATOM   5095  C   TYR B 230     -20.121  13.011  30.929  1.00 84.37           C  
ANISOU 5095  C   TYR B 230    14135   9699   8225   -889   -263   1290       C  
ATOM   5096  O   TYR B 230     -20.578  12.380  29.977  1.00 85.06           O  
ANISOU 5096  O   TYR B 230    14147   9958   8214   -814   -339   1297       O  
ATOM   5097  CB  TYR B 230     -18.615  11.347  32.095  1.00 73.95           C  
ANISOU 5097  CB  TYR B 230    12336   8625   7136  -1170   -101   1013       C  
ATOM   5098  CG  TYR B 230     -17.468  10.525  31.554  1.00 72.19           C  
ANISOU 5098  CG  TYR B 230    11971   8596   6864  -1387     15    929       C  
ATOM   5099  CD1 TYR B 230     -16.199  10.623  32.107  1.00 72.52           C  
ANISOU 5099  CD1 TYR B 230    11961   8645   6949  -1613    153    863       C  
ATOM   5100  CD2 TYR B 230     -17.635   9.702  30.444  1.00 72.99           C  
ANISOU 5100  CD2 TYR B 230    11996   8880   6858  -1366    -14    912       C  
ATOM   5101  CE1 TYR B 230     -15.124   9.917  31.580  1.00 71.87           C  
ANISOU 5101  CE1 TYR B 230    11741   8756   6811  -1794    265    787       C  
ATOM   5102  CE2 TYR B 230     -16.567   8.979  29.912  1.00 73.80           C  
ANISOU 5102  CE2 TYR B 230    11982   9157   6902  -1548    103    832       C  
ATOM   5103  CZ  TYR B 230     -15.312   9.086  30.491  1.00 81.33           C  
ANISOU 5103  CZ  TYR B 230    12871  10123   7907  -1753    245    772       C  
ATOM   5104  OH  TYR B 230     -14.236   8.370  30.022  1.00 84.33           O  
ANISOU 5104  OH  TYR B 230    13111  10696   8235  -1913    365    685       O  
ATOM   5105  N   ALA B 231     -20.799  13.986  31.559  1.00 82.99           N  
ANISOU 5105  N   ALA B 231    14135   9306   8093   -722   -319   1365       N  
ATOM   5106  CA  ALA B 231     -22.117  14.443  31.125  1.00 84.82           C  
ANISOU 5106  CA  ALA B 231    14487   9490   8250   -420   -473   1478       C  
ATOM   5107  C   ALA B 231     -21.924  15.206  29.798  1.00 91.02           C  
ANISOU 5107  C   ALA B 231    15601  10195   8786   -458   -466   1648       C  
ATOM   5108  O   ALA B 231     -22.714  15.029  28.872  1.00 90.50           O  
ANISOU 5108  O   ALA B 231    15546  10247   8591   -283   -590   1716       O  
ATOM   5109  CB  ALA B 231     -22.737  15.354  32.178  1.00 86.08           C  
ANISOU 5109  CB  ALA B 231    14774   9420   8514   -236   -507   1510       C  
ATOM   5110  N   ARG B 232     -20.835  16.004  29.703  1.00 90.57           N  
ANISOU 5110  N   ARG B 232    15801   9956   8656   -707   -316   1710       N  
ATOM   5111  CA  ARG B 232     -20.453  16.771  28.507  1.00 94.54           C  
ANISOU 5111  CA  ARG B 232    16648  10357   8916   -803   -265   1877       C  
ATOM   5112  C   ARG B 232     -19.960  15.819  27.399  1.00101.94           C  
ANISOU 5112  C   ARG B 232    17436  11572   9725   -947   -235   1840       C  
ATOM   5113  O   ARG B 232     -20.275  16.027  26.224  1.00103.12           O  
ANISOU 5113  O   ARG B 232    17764  11758   9660   -874   -288   1966       O  
ATOM   5114  CB  ARG B 232     -19.365  17.823  28.833  1.00 93.76           C  
ANISOU 5114  CB  ARG B 232    16838   9992   8795  -1079    -89   1928       C  
ATOM   5115  CG  ARG B 232     -19.877  19.074  29.545  1.00102.19           C  
ANISOU 5115  CG  ARG B 232    18211  10715   9902   -929   -112   2019       C  
ATOM   5116  CD  ARG B 232     -19.638  20.335  28.729  1.00120.40           C  
ANISOU 5116  CD  ARG B 232    21010  12742  11993   -995    -44   2225       C  
ATOM   5117  NE  ARG B 232     -19.444  21.517  29.574  1.00132.05           N  
ANISOU 5117  NE  ARG B 232    22790  13855  13528  -1048     32   2258       N  
ATOM   5118  CZ  ARG B 232     -19.270  22.754  29.113  1.00150.91           C  
ANISOU 5118  CZ  ARG B 232    25659  15919  15760  -1103    105   2433       C  
ATOM   5119  NH1 ARG B 232     -19.274  22.990  27.806  1.00142.11           N  
ANISOU 5119  NH1 ARG B 232    24778  14807  14410  -1102    110   2605       N  
ATOM   5120  NH2 ARG B 232     -19.096  23.764  29.956  1.00137.58           N1+
ANISOU 5120  NH2 ARG B 232    24240  13895  14140  -1160    177   2436       N1+
ATOM   5121  N   ILE B 233     -19.200  14.772  27.788  1.00 99.21           N  
ANISOU 5121  N   ILE B 233    16770  11422   9501  -1134   -152   1665       N  
ATOM   5122  CA  ILE B 233     -18.656  13.754  26.891  1.00100.16           C  
ANISOU 5122  CA  ILE B 233    16718  11811   9529  -1270   -106   1593       C  
ATOM   5123  C   ILE B 233     -19.775  13.039  26.119  1.00109.54           C  
ANISOU 5123  C   ILE B 233    17793  13187  10638  -1030   -280   1591       C  
ATOM   5124  O   ILE B 233     -19.773  13.085  24.885  1.00111.67           O  
ANISOU 5124  O   ILE B 233    18205  13539  10686  -1043   -293   1676       O  
ATOM   5125  CB  ILE B 233     -17.700  12.780  27.642  1.00100.54           C  
ANISOU 5125  CB  ILE B 233    16441  12011   9748  -1462      7   1400       C  
ATOM   5126  CG1 ILE B 233     -16.361  13.473  27.986  1.00101.46           C  
ANISOU 5126  CG1 ILE B 233    16674  12014   9861  -1766    196   1405       C  
ATOM   5127  CG2 ILE B 233     -17.463  11.496  26.836  1.00100.60           C  
ANISOU 5127  CG2 ILE B 233    16221  12309   9695  -1505     16   1294       C  
ATOM   5128  CD1 ILE B 233     -15.517  12.773  29.049  1.00105.86           C  
ANISOU 5128  CD1 ILE B 233    16930  12682  10612  -1905    283   1227       C  
ATOM   5129  N   TYR B 234     -20.754  12.439  26.836  1.00107.79           N  
ANISOU 5129  N   TYR B 234    17332  13035  10586   -818   -412   1499       N  
ATOM   5130  CA  TYR B 234     -21.866  11.724  26.210  1.00109.89           C  
ANISOU 5130  CA  TYR B 234    17455  13500  10800   -610   -583   1472       C  
ATOM   5131  C   TYR B 234     -22.860  12.669  25.502  1.00117.91           C  
ANISOU 5131  C   TYR B 234    18731  14434  11637   -369   -729   1654       C  
ATOM   5132  O   TYR B 234     -23.710  12.193  24.755  1.00118.49           O  
ANISOU 5132  O   TYR B 234    18717  14695  11608   -214   -876   1649       O  
ATOM   5133  CB  TYR B 234     -22.554  10.756  27.199  1.00110.52           C  
ANISOU 5133  CB  TYR B 234    17188  13689  11114   -494   -659   1312       C  
ATOM   5134  CG  TYR B 234     -21.788   9.450  27.343  1.00113.01           C  
ANISOU 5134  CG  TYR B 234    17235  14178  11524   -680   -561   1133       C  
ATOM   5135  CD1 TYR B 234     -22.009   8.386  26.469  1.00115.93           C  
ANISOU 5135  CD1 TYR B 234    17459  14777  11813   -688   -612   1045       C  
ATOM   5136  CD2 TYR B 234     -20.783   9.308  28.301  1.00112.39           C  
ANISOU 5136  CD2 TYR B 234    17072  14036  11597   -848   -415   1054       C  
ATOM   5137  CE1 TYR B 234     -21.265   7.207  26.556  1.00116.04           C  
ANISOU 5137  CE1 TYR B 234    17263  14925  11902   -843   -511    884       C  
ATOM   5138  CE2 TYR B 234     -20.034   8.133  28.398  1.00111.85           C  
ANISOU 5138  CE2 TYR B 234    16775  14124  11600   -990   -323    901       C  
ATOM   5139  CZ  TYR B 234     -20.277   7.086  27.522  1.00121.02           C  
ANISOU 5139  CZ  TYR B 234    17811  15486  12684   -981   -367    819       C  
ATOM   5140  OH  TYR B 234     -19.536   5.931  27.606  1.00121.48           O  
ANISOU 5140  OH  TYR B 234    17671  15678  12809  -1099   -270    668       O  
ATOM   5141  N   ARG B 235     -22.694  13.999  25.672  1.00117.21           N  
ANISOU 5141  N   ARG B 235    18973  14069  11491   -349   -683   1812       N  
ATOM   5142  CA  ARG B 235     -23.503  15.040  25.025  1.00120.50           C  
ANISOU 5142  CA  ARG B 235    19701  14360  11725   -110   -800   2011       C  
ATOM   5143  C   ARG B 235     -22.990  15.296  23.580  1.00128.22           C  
ANISOU 5143  C   ARG B 235    20934  15377  12407   -226   -757   2140       C  
ATOM   5144  O   ARG B 235     -23.762  15.710  22.707  1.00129.94           O  
ANISOU 5144  O   ARG B 235    21328  15620  12423    -10   -893   2279       O  
ATOM   5145  CB  ARG B 235     -23.528  16.323  25.903  1.00121.75           C  
ANISOU 5145  CB  ARG B 235    20128  14172  11958    -38   -754   2114       C  
ATOM   5146  CG  ARG B 235     -24.193  17.598  25.329  1.00140.06           C  
ANISOU 5146  CG  ARG B 235    22852  16278  14085    207   -839   2343       C  
ATOM   5147  CD  ARG B 235     -25.641  17.453  24.861  1.00155.61           C  
ANISOU 5147  CD  ARG B 235    24732  18415  15976    591  -1075   2390       C  
ATOM   5148  NE  ARG B 235     -26.541  16.966  25.910  1.00162.75           N  
ANISOU 5148  NE  ARG B 235    25307  19417  17113    788  -1177   2254       N  
ATOM   5149  CZ  ARG B 235     -27.813  16.631  25.711  1.00176.35           C  
ANISOU 5149  CZ  ARG B 235    26837  21346  18821   1092  -1377   2241       C  
ATOM   5150  NH1 ARG B 235     -28.356  16.740  24.503  1.00166.06           N  
ANISOU 5150  NH1 ARG B 235    25640  20180  17277   1253  -1514   2354       N  
ATOM   5151  NH2 ARG B 235     -28.557  16.201  26.721  1.00159.73           N1+
ANISOU 5151  NH2 ARG B 235    24431  19326  16933   1235  -1440   2114       N1+
ATOM   5152  N   VAL B 236     -21.696  15.004  23.334  1.00125.08           N  
ANISOU 5152  N   VAL B 236    20537  15011  11977   -558   -569   2088       N  
ATOM   5153  CA  VAL B 236     -21.044  15.150  22.023  1.00127.08           C  
ANISOU 5153  CA  VAL B 236    21005  15323  11957   -718   -487   2189       C  
ATOM   5154  C   VAL B 236     -20.898  13.747  21.363  1.00130.05           C  
ANISOU 5154  C   VAL B 236    21076  16044  12292   -795   -504   2027       C  
ATOM   5155  O   VAL B 236     -20.545  13.643  20.187  1.00130.67           O  
ANISOU 5155  O   VAL B 236    21277  16240  12130   -885   -467   2082       O  
ATOM   5156  CB  VAL B 236     -19.707  15.950  22.123  1.00131.72           C  
ANISOU 5156  CB  VAL B 236    21842  15700  12507  -1039   -250   2259       C  
ATOM   5157  CG1 VAL B 236     -19.208  16.402  20.755  1.00134.35           C  
ANISOU 5157  CG1 VAL B 236    22484  16038  12525  -1165   -166   2418       C  
ATOM   5158  CG2 VAL B 236     -19.849  17.161  23.045  1.00132.30           C  
ANISOU 5158  CG2 VAL B 236    22161  15423  12683   -981   -229   2358       C  
ATOM   5159  N   ALA B 237     -21.231  12.675  22.121  1.00124.90           N  
ANISOU 5159  N   ALA B 237    20045  15545  11868   -748   -562   1830       N  
ATOM   5160  CA  ALA B 237     -21.218  11.289  21.642  1.00124.09           C  
ANISOU 5160  CA  ALA B 237    19653  15737  11759   -797   -589   1656       C  
ATOM   5161  C   ALA B 237     -22.381  11.050  20.660  1.00130.94           C  
ANISOU 5161  C   ALA B 237    20526  16780  12445   -570   -799   1693       C  
ATOM   5162  O   ALA B 237     -22.265  10.231  19.743  1.00130.84           O  
ANISOU 5162  O   ALA B 237    20431  16991  12293   -635   -811   1611       O  
ATOM   5163  CB  ALA B 237     -21.324  10.328  22.815  1.00121.77           C  
ANISOU 5163  CB  ALA B 237    19002  15505  11761   -796   -591   1458       C  
ATOM   5164  N   LYS B 238     -23.488  11.797  20.846  1.00129.45           N  
ANISOU 5164  N   LYS B 238    20441  16497  12248   -298   -965   1812       N  
ATOM   5165  CA  LYS B 238     -24.690  11.739  20.017  1.00131.43           C  
ANISOU 5165  CA  LYS B 238    20695  16918  12327    -44  -1189   1862       C  
ATOM   5166  C   LYS B 238     -24.497  12.348  18.608  1.00138.82           C  
ANISOU 5166  C   LYS B 238    21964  17873  12907    -41  -1199   2039       C  
ATOM   5167  O   LYS B 238     -25.424  12.280  17.795  1.00140.21           O  
ANISOU 5167  O   LYS B 238    22151  18222  12901    165  -1392   2082       O  
ATOM   5168  CB  LYS B 238     -25.874  12.394  20.752  1.00134.36           C  
ANISOU 5168  CB  LYS B 238    21057  17185  12809    264  -1350   1934       C  
ATOM   5169  N   LEU B 239     -23.301  12.921  18.315  1.00136.50           N  
ANISOU 5169  N   LEU B 239    21934  17422  12509   -274   -992   2138       N  
ATOM   5170  CA  LEU B 239     -22.981  13.519  17.011  1.00139.94           C  
ANISOU 5170  CA  LEU B 239    22713  17857  12600   -310   -961   2316       C  
ATOM   5171  C   LEU B 239     -22.941  12.498  15.872  1.00146.68           C  
ANISOU 5171  C   LEU B 239    23441  19034  13257   -374  -1002   2209       C  
ATOM   5172  O   LEU B 239     -23.206  12.865  14.723  1.00149.02           O  
ANISOU 5172  O   LEU B 239    23972  19406  13243   -285  -1077   2348       O  
ATOM   5173  CB  LEU B 239     -21.647  14.287  17.045  1.00140.40           C  
ANISOU 5173  CB  LEU B 239    23046  17684  12614   -595   -701   2422       C  
ATOM   5174  CG  LEU B 239     -21.624  15.706  17.626  1.00146.07           C  
ANISOU 5174  CG  LEU B 239    24101  18035  13365   -543   -651   2617       C  
ATOM   5175  CD1 LEU B 239     -20.309  16.373  17.306  1.00147.44           C  
ANISOU 5175  CD1 LEU B 239    24562  18040  13419   -867   -396   2722       C  
ATOM   5176  CD2 LEU B 239     -22.748  16.578  17.070  1.00151.59           C  
ANISOU 5176  CD2 LEU B 239    25085  18646  13864   -199   -846   2831       C  
ATOM   5177  N   ARG B 240     -22.588  11.227  16.195  1.00142.42           N  
ANISOU 5177  N   ARG B 240    22551  18674  12887   -525   -947   1963       N  
ATOM   5178  CA  ARG B 240     -22.457  10.089  15.269  1.00143.05           C  
ANISOU 5178  CA  ARG B 240    22478  19050  12826   -613   -960   1809       C  
ATOM   5179  C   ARG B 240     -21.455  10.378  14.132  1.00150.73           C  
ANISOU 5179  C   ARG B 240    23718  20054  13500   -805   -795   1906       C  
ATOM   5180  O   ARG B 240     -21.609   9.883  13.010  1.00152.41           O  
ANISOU 5180  O   ARG B 240    23954  20491  13464   -795   -855   1871       O  
ATOM   5181  CB  ARG B 240     -23.830   9.615  14.748  1.00144.49           C  
ANISOU 5181  CB  ARG B 240    22531  19458  12912   -365  -1235   1758       C  
ATOM   5182  N   THR B 241     -20.400  11.156  14.455  1.00147.97           N  
ANISOU 5182  N   THR B 241    23558  19487  13175   -999   -576   2015       N  
ATOM   5183  CA  THR B 241     -19.329  11.558  13.538  1.00150.09           C  
ANISOU 5183  CA  THR B 241    24085  19754  13188  -1222   -374   2120       C  
ATOM   5184  C   THR B 241     -18.401  10.394  13.157  1.00152.59           C  
ANISOU 5184  C   THR B 241    24178  20307  13491  -1444   -217   1910       C  
ATOM   5185  O   THR B 241     -17.429  10.601  12.429  1.00153.72           O  
ANISOU 5185  O   THR B 241    24484  20488  13435  -1650    -25   1966       O  
ATOM   5186  CB  THR B 241     -18.558  12.767  14.093  1.00161.27           C  
ANISOU 5186  CB  THR B 241    25756  20861  14657  -1376   -192   2288       C  
ATOM   5187  OG1 THR B 241     -18.383  12.624  15.508  1.00160.12           O  
ANISOU 5187  OG1 THR B 241    25378  20592  14867  -1417   -153   2169       O  
ATOM   5188  CG2 THR B 241     -19.244  14.084  13.773  1.00162.75           C  
ANISOU 5188  CG2 THR B 241    26343  20827  14669  -1186   -295   2562       C  
ATOM   5189  N   GLY B1001     -18.711   9.192  13.644  1.00147.30           N  
ANISOU 5189  N   GLY B1001    22174  22829  10966   2350   1886    545       N  
ATOM   5190  CA  GLY B1001     -17.957   7.984  13.340  1.00145.35           C  
ANISOU 5190  CA  GLY B1001    21869  22446  10910   2216   1805    984       C  
ATOM   5191  C   GLY B1001     -18.317   7.424  11.979  1.00143.96           C  
ANISOU 5191  C   GLY B1001    21430  21919  11348   2067   1895   1081       C  
ATOM   5192  O   GLY B1001     -19.494   7.421  11.600  1.00142.62           O  
ANISOU 5192  O   GLY B1001    21073  21741  11373   2046   2180    988       O  
ATOM   5193  N   ILE B1002     -17.297   6.961  11.226  1.00137.60           N  
ANISOU 5193  N   ILE B1002    20586  20856  10840   1977   1642   1237       N  
ATOM   5194  CA  ILE B1002     -17.470   6.342   9.904  1.00133.93           C  
ANISOU 5194  CA  ILE B1002    19917  20050  10919   1845   1693   1327       C  
ATOM   5195  C   ILE B1002     -17.888   4.894  10.147  1.00139.44           C  
ANISOU 5195  C   ILE B1002    20584  20715  11682   1747   2003   1747       C  
ATOM   5196  O   ILE B1002     -17.220   4.178  10.899  1.00141.06           O  
ANISOU 5196  O   ILE B1002    20958  20992  11647   1796   1985   2084       O  
ATOM   5197  CB  ILE B1002     -16.206   6.405   8.987  1.00133.78           C  
ANISOU 5197  CB  ILE B1002    19879  19772  11179   1803   1353   1320       C  
ATOM   5198  CG1 ILE B1002     -15.375   7.692   9.169  1.00134.52           C  
ANISOU 5198  CG1 ILE B1002    20080  19930  11101   1846   1030   1003       C  
ATOM   5199  CG2 ILE B1002     -16.581   6.195   7.524  1.00130.31           C  
ANISOU 5199  CG2 ILE B1002    19266  19011  11234   1711   1399   1254       C  
ATOM   5200  CD1 ILE B1002     -14.205   7.580  10.226  1.00147.03           C  
ANISOU 5200  CD1 ILE B1002    21778  21772  12314   1895    779   1124       C  
ATOM   5201  N   ASP B1003     -18.991   4.465   9.520  1.00135.44           N  
ANISOU 5201  N   ASP B1003    19871  20096  11495   1611   2281   1723       N  
ATOM   5202  CA  ASP B1003     -19.505   3.105   9.662  1.00137.09           C  
ANISOU 5202  CA  ASP B1003    20047  20202  11841   1436   2624   2079       C  
ATOM   5203  C   ASP B1003     -18.645   2.153   8.806  1.00138.28           C  
ANISOU 5203  C   ASP B1003    20235  19960  12345   1361   2481   2302       C  
ATOM   5204  O   ASP B1003     -19.080   1.722   7.739  1.00136.20           O  
ANISOU 5204  O   ASP B1003    19798  19440  12511   1203   2540   2215       O  
ATOM   5205  CB  ASP B1003     -21.005   3.065   9.269  1.00139.58           C  
ANISOU 5205  CB  ASP B1003    20056  20576  12401   1275   2947   1892       C  
ATOM   5206  CG  ASP B1003     -21.805   1.866   9.753  1.00149.56           C  
ANISOU 5206  CG  ASP B1003    21271  21829  13725   1032   3413   2208       C  
ATOM   5207  OD1 ASP B1003     -21.284   1.101  10.595  1.00151.77           O  
ANISOU 5207  OD1 ASP B1003    21837  22070  13761   1035   3539   2622       O  
ATOM   5208  OD2 ASP B1003     -22.961   1.701   9.299  1.00154.72           O1-
ANISOU 5208  OD2 ASP B1003    21600  22521  14667    838   3655   2042       O1-
ATOM   5209  N   CYS B1004     -17.406   1.842   9.274  1.00134.47           N  
ANISOU 5209  N   CYS B1004    19970  19458  11663   1506   2274   2562       N  
ATOM   5210  CA  CYS B1004     -16.461   0.953   8.577  1.00132.13           C  
ANISOU 5210  CA  CYS B1004    19721  18823  11658   1521   2139   2784       C  
ATOM   5211  C   CYS B1004     -17.010  -0.466   8.466  1.00135.66           C  
ANISOU 5211  C   CYS B1004    20235  18961  12347   1353   2492   3108       C  
ATOM   5212  O   CYS B1004     -16.630  -1.200   7.554  1.00133.58           O  
ANISOU 5212  O   CYS B1004    19967  18331  12456   1307   2457   3171       O  
ATOM   5213  CB  CYS B1004     -15.079   0.979   9.226  1.00133.67           C  
ANISOU 5213  CB  CYS B1004    20075  19159  11554   1761   1837   2976       C  
ATOM   5214  SG  CYS B1004     -13.706   0.951   8.040  1.00134.21           S  
ANISOU 5214  SG  CYS B1004    20023  18988  11982   1845   1484   2903       S  
ATOM   5215  N   SER B1005     -17.958  -0.818   9.365  1.00134.41           N  
ANISOU 5215  N   SER B1005    20143  18937  11989   1239   2867   3283       N  
ATOM   5216  CA  SER B1005     -18.696  -2.084   9.398  1.00136.72           C  
ANISOU 5216  CA  SER B1005    20503  18938  12506    988   3295   3573       C  
ATOM   5217  C   SER B1005     -19.649  -2.172   8.170  1.00136.52           C  
ANISOU 5217  C   SER B1005    20152  18711  13006    682   3397   3228       C  
ATOM   5218  O   SER B1005     -20.281  -3.211   7.948  1.00138.64           O  
ANISOU 5218  O   SER B1005    20419  18684  13576    392   3719   3365       O  
ATOM   5219  CB  SER B1005     -19.480  -2.192  10.707  1.00144.42           C  
ANISOU 5219  CB  SER B1005    21595  20195  13082    931   3689   3803       C  
ATOM   5220  OG  SER B1005     -20.171  -3.424  10.833  1.00155.36           O  
ANISOU 5220  OG  SER B1005    23076  21276  14678    639   4160   4124       O  
ATOM   5221  N   PHE B1006     -19.725  -1.069   7.376  1.00127.21           N  
ANISOU 5221  N   PHE B1006    18722  17688  11923    753   3107   2775       N  
ATOM   5222  CA  PHE B1006     -20.531  -0.917   6.162  1.00124.18           C  
ANISOU 5222  CA  PHE B1006    18023  17213  11947    570   3086   2397       C  
ATOM   5223  C   PHE B1006     -19.682  -0.406   4.989  1.00122.05           C  
ANISOU 5223  C   PHE B1006    17740  16790  11846    730   2683   2165       C  
ATOM   5224  O   PHE B1006     -19.577  -1.099   3.981  1.00120.66           O  
ANISOU 5224  O   PHE B1006    17542  16286  12016    618   2650   2121       O  
ATOM   5225  CB  PHE B1006     -21.735   0.011   6.422  1.00126.40           C  
ANISOU 5225  CB  PHE B1006    18008  17901  12117    543   3206   2085       C  
ATOM   5226  CG  PHE B1006     -22.536   0.399   5.200  1.00125.35           C  
ANISOU 5226  CG  PHE B1006    17524  17781  12322    463   3092   1660       C  
ATOM   5227  CD1 PHE B1006     -23.411  -0.503   4.608  1.00130.12           C  
ANISOU 5227  CD1 PHE B1006    17891  18240  13310    130   3294   1587       C  
ATOM   5228  CD2 PHE B1006     -22.445   1.678   4.669  1.00123.57           C  
ANISOU 5228  CD2 PHE B1006    17219  17718  12015    721   2781   1327       C  
ATOM   5229  CE1 PHE B1006     -24.162  -0.141   3.492  1.00129.87           C  
ANISOU 5229  CE1 PHE B1006    17513  18290  13543     90   3136   1173       C  
ATOM   5230  CE2 PHE B1006     -23.199   2.041   3.554  1.00125.37           C  
ANISOU 5230  CE2 PHE B1006    17153  17984  12497    715   2655    965       C  
ATOM   5231  CZ  PHE B1006     -24.055   1.129   2.976  1.00125.74           C  
ANISOU 5231  CZ  PHE B1006    16930  17954  12890    415   2811    882       C  
ATOM   5232  N   TRP B1007     -19.091   0.803   5.122  1.00115.55           N  
ANISOU 5232  N   TRP B1007    16946  16188  10770    973   2403   2007       N  
ATOM   5233  CA  TRP B1007     -18.255   1.442   4.104  1.00111.31           C  
ANISOU 5233  CA  TRP B1007    16411  15533  10348   1110   2068   1808       C  
ATOM   5234  C   TRP B1007     -16.926   0.699   3.938  1.00113.58           C  
ANISOU 5234  C   TRP B1007    16876  15573  10707   1190   1949   2075       C  
ATOM   5235  O   TRP B1007     -15.899   1.106   4.488  1.00112.27           O  
ANISOU 5235  O   TRP B1007    16816  15533  10311   1358   1763   2178       O  
ATOM   5236  CB  TRP B1007     -18.008   2.932   4.414  1.00108.87           C  
ANISOU 5236  CB  TRP B1007    16120  15485   9761   1293   1856   1578       C  
ATOM   5237  CG  TRP B1007     -19.238   3.746   4.682  1.00111.23           C  
ANISOU 5237  CG  TRP B1007    16272  16043   9949   1313   1969   1315       C  
ATOM   5238  CD1 TRP B1007     -19.659   4.217   5.892  1.00116.72           C  
ANISOU 5238  CD1 TRP B1007    17007  17043  10299   1382   2101   1314       C  
ATOM   5239  CD2 TRP B1007     -20.165   4.249   3.710  1.00110.17           C  
ANISOU 5239  CD2 TRP B1007    15928  15915  10016   1326   1941    996       C  
ATOM   5240  NE1 TRP B1007     -20.811   4.952   5.740  1.00116.99           N  
ANISOU 5240  NE1 TRP B1007    16847  17263  10340   1441   2188   1013       N  
ATOM   5241  CE2 TRP B1007     -21.144   4.990   4.409  1.00116.43           C  
ANISOU 5241  CE2 TRP B1007    16609  17023  10605   1420   2074    821       C  
ATOM   5242  CE3 TRP B1007     -20.275   4.131   2.314  1.00109.35           C  
ANISOU 5242  CE3 TRP B1007    15724  15609  10215   1304   1812    837       C  
ATOM   5243  CZ2 TRP B1007     -22.216   5.616   3.758  1.00115.95           C  
ANISOU 5243  CZ2 TRP B1007    16310  17086  10660   1520   2063    502       C  
ATOM   5244  CZ3 TRP B1007     -21.343   4.743   1.675  1.00111.04           C  
ANISOU 5244  CZ3 TRP B1007    15725  15957  10508   1388   1780    528       C  
ATOM   5245  CH2 TRP B1007     -22.295   5.476   2.392  1.00113.81           C  
ANISOU 5245  CH2 TRP B1007    15937  16626  10678   1507   1896    369       C  
ATOM   5246  N   ASN B1008     -16.962  -0.409   3.186  1.00110.51           N  
ANISOU 5246  N   ASN B1008    16503  14842  10643   1076   2055   2160       N  
ATOM   5247  CA  ASN B1008     -15.798  -1.241   2.897  1.00110.39           C  
ANISOU 5247  CA  ASN B1008    16645  14549  10748   1193   1984   2395       C  
ATOM   5248  C   ASN B1008     -15.988  -1.908   1.545  1.00112.75           C  
ANISOU 5248  C   ASN B1008    16911  14496  11433   1082   2017   2234       C  
ATOM   5249  O   ASN B1008     -17.012  -2.553   1.304  1.00113.62           O  
ANISOU 5249  O   ASN B1008    16971  14455  11744    841   2221   2161       O  
ATOM   5250  CB  ASN B1008     -15.572  -2.283   4.004  1.00116.80           C  
ANISOU 5250  CB  ASN B1008    17676  15274  11430   1231   2176   2839       C  
ATOM   5251  CG  ASN B1008     -14.156  -2.354   4.533  1.00147.76           C  
ANISOU 5251  CG  ASN B1008    21726  19267  15150   1534   1969   3102       C  
ATOM   5252  OD1 ASN B1008     -13.647  -1.423   5.172  1.00144.57           O  
ANISOU 5252  OD1 ASN B1008    21275  19221  14433   1670   1756   3056       O  
ATOM   5253  ND2 ASN B1008     -13.496  -3.481   4.305  1.00141.61           N  
ANISOU 5253  ND2 ASN B1008    21105  18154  14546   1658   2020   3366       N  
ATOM   5254  N   GLU B1009     -15.001  -1.737   0.658  1.00107.67           N  
ANISOU 5254  N   GLU B1009    16281  13745  10886   1241   1823   2151       N  
ATOM   5255  CA  GLU B1009     -14.984  -2.302  -0.698  1.00107.25           C  
ANISOU 5255  CA  GLU B1009    16237  13379  11133   1199   1826   1973       C  
ATOM   5256  C   GLU B1009     -14.990  -3.834  -0.694  1.00112.71           C  
ANISOU 5256  C   GLU B1009    17111  13658  12056   1126   2040   2179       C  
ATOM   5257  O   GLU B1009     -15.312  -4.448  -1.714  1.00112.44           O  
ANISOU 5257  O   GLU B1009    17104  13338  12281   1012   2091   1981       O  
ATOM   5258  CB  GLU B1009     -13.816  -1.738  -1.536  1.00106.59           C  
ANISOU 5258  CB  GLU B1009    16142  13311  11048   1410   1624   1880       C  
ATOM   5259  CG  GLU B1009     -12.588  -1.322  -0.736  1.00120.88           C  
ANISOU 5259  CG  GLU B1009    17947  15320  12662   1613   1494   2103       C  
ATOM   5260  CD  GLU B1009     -11.835  -2.407   0.017  1.00145.62           C  
ANISOU 5260  CD  GLU B1009    21205  18329  15796   1776   1559   2476       C  
ATOM   5261  OE1 GLU B1009     -10.934  -3.036  -0.585  1.00142.99           O  
ANISOU 5261  OE1 GLU B1009    20907  17797  15625   1953   1554   2548       O  
ATOM   5262  OE2 GLU B1009     -12.132  -2.610   1.217  1.00136.22           O  
ANISOU 5262  OE2 GLU B1009    20089  17252  14414   1766   1624   2707       O  
ATOM   5263  N   SER B1010     -14.665  -4.439   0.472  1.00111.20           N  
ANISOU 5263  N   SER B1010    17080  13423  11746   1199   2166   2572       N  
ATOM   5264  CA  SER B1010     -14.661  -5.885   0.717  1.00114.60           C  
ANISOU 5264  CA  SER B1010    17772  13413  12359   1159   2411   2858       C  
ATOM   5265  C   SER B1010     -16.091  -6.422   0.647  1.00119.33           C  
ANISOU 5265  C   SER B1010    18344  13834  13160    740   2677   2730       C  
ATOM   5266  O   SER B1010     -16.301  -7.565   0.242  1.00121.36           O  
ANISOU 5266  O   SER B1010    18782  13618  13710    584   2868   2756       O  
ATOM   5267  CB  SER B1010     -14.064  -6.192   2.089  1.00120.35           C  
ANISOU 5267  CB  SER B1010    18690  14223  12815   1375   2463   3334       C  
ATOM   5268  OG  SER B1010     -12.687  -5.860   2.153  1.00126.57           O  
ANISOU 5268  OG  SER B1010    19455  15178  13457   1756   2203   3445       O  
ATOM   5269  N   TYR B1011     -17.070  -5.578   1.021  1.00114.12           N  
ANISOU 5269  N   TYR B1011    17441  13558  12361    554   2693   2560       N  
ATOM   5270  CA  TYR B1011     -18.486  -5.920   1.004  1.00115.93           C  
ANISOU 5270  CA  TYR B1011    17519  13754  12776    144   2936   2396       C  
ATOM   5271  C   TYR B1011     -19.074  -5.854  -0.401  1.00115.05           C  
ANISOU 5271  C   TYR B1011    17196  13573  12945    -28   2805   1910       C  
ATOM   5272  O   TYR B1011     -20.128  -6.437  -0.639  1.00117.04           O  
ANISOU 5272  O   TYR B1011    17319  13702  13449   -403   2985   1733       O  
ATOM   5273  CB  TYR B1011     -19.279  -5.079   2.023  1.00118.19           C  
ANISOU 5273  CB  TYR B1011    17605  14519  12783     75   3030   2414       C  
ATOM   5274  CG  TYR B1011     -18.759  -5.185   3.444  1.00122.72           C  
ANISOU 5274  CG  TYR B1011    18421  15194  13012    246   3160   2882       C  
ATOM   5275  CD1 TYR B1011     -18.319  -6.402   3.960  1.00129.12           C  
ANISOU 5275  CD1 TYR B1011    19585  15605  13869    254   3384   3317       C  
ATOM   5276  CD2 TYR B1011     -18.731  -4.075   4.281  1.00122.33           C  
ANISOU 5276  CD2 TYR B1011    18283  15631  12565    423   3057   2883       C  
ATOM   5277  CE1 TYR B1011     -17.837  -6.505   5.265  1.00133.70           C  
ANISOU 5277  CE1 TYR B1011    20416  16314  14068    466   3475   3767       C  
ATOM   5278  CE2 TYR B1011     -18.249  -4.165   5.587  1.00126.01           C  
ANISOU 5278  CE2 TYR B1011    18987  16238  12652    600   3141   3282       C  
ATOM   5279  CZ  TYR B1011     -17.806  -5.384   6.078  1.00138.45           C  
ANISOU 5279  CZ  TYR B1011    20903  17459  14243    633   3341   3738       C  
ATOM   5280  OH  TYR B1011     -17.337  -5.493   7.366  1.00141.49           O  
ANISOU 5280  OH  TYR B1011    21550  18013  14198    857   3401   4155       O  
ATOM   5281  N   LEU B1012     -18.376  -5.184  -1.339  1.00106.50           N  
ANISOU 5281  N   LEU B1012    16083  12570  11811    232   2499   1695       N  
ATOM   5282  CA  LEU B1012     -18.782  -5.111  -2.747  1.00104.58           C  
ANISOU 5282  CA  LEU B1012    15708  12274  11752    153   2338   1254       C  
ATOM   5283  C   LEU B1012     -18.301  -6.365  -3.466  1.00111.09           C  
ANISOU 5283  C   LEU B1012    16793  12568  12849    107   2417   1249       C  
ATOM   5284  O   LEU B1012     -17.233  -6.891  -3.135  1.00111.24           O  
ANISOU 5284  O   LEU B1012    17084  12331  12853    327   2479   1569       O  
ATOM   5285  CB  LEU B1012     -18.185  -3.882  -3.462  1.00 99.52           C  
ANISOU 5285  CB  LEU B1012    15003  11904  10907    465   2030   1074       C  
ATOM   5286  CG  LEU B1012     -18.740  -2.489  -3.160  1.00100.67           C  
ANISOU 5286  CG  LEU B1012    14920  12518  10813    546   1895    940       C  
ATOM   5287  CD1 LEU B1012     -17.937  -1.458  -3.889  1.00 97.01           C  
ANISOU 5287  CD1 LEU B1012    14512  12164  10185    836   1649    837       C  
ATOM   5288  CD2 LEU B1012     -20.197  -2.348  -3.580  1.00102.75           C  
ANISOU 5288  CD2 LEU B1012    14884  12975  11180    335   1885    590       C  
ATOM   5289  N   THR B1013     -19.065  -6.822  -4.471  1.00109.75           N  
ANISOU 5289  N   THR B1013    16535  12249  12914   -145   2392    857       N  
ATOM   5290  CA  THR B1013     -18.697  -7.994  -5.268  1.00111.99           C  
ANISOU 5290  CA  THR B1013    17091  12004  13458   -202   2460    754       C  
ATOM   5291  C   THR B1013     -18.520  -7.620  -6.750  1.00112.85           C  
ANISOU 5291  C   THR B1013    17166  12185  13527    -48   2187    327       C  
ATOM   5292  O   THR B1013     -19.168  -6.704  -7.263  1.00110.61           O  
ANISOU 5292  O   THR B1013    16610  12307  13109    -51   1972     29       O  
ATOM   5293  CB  THR B1013     -19.649  -9.184  -5.018  1.00126.54           C  
ANISOU 5293  CB  THR B1013    18974  13467  15637   -694   2741    702       C  
ATOM   5294  OG1 THR B1013     -19.162 -10.342  -5.704  1.00130.63           O  
ANISOU 5294  OG1 THR B1013    19844  13387  16402   -710   2824    622       O  
ATOM   5295  CG2 THR B1013     -21.094  -8.899  -5.405  1.00126.30           C  
ANISOU 5295  CG2 THR B1013    18525  13745  15720  -1090   2674    260       C  
ATOM   5296  N   GLY B1014     -17.609  -8.325  -7.400  1.00109.65           N  
ANISOU 5296  N   GLY B1014    17064  11392  13208    138   2211    325       N  
ATOM   5297  CA  GLY B1014     -17.292  -8.122  -8.803  1.00108.19           C  
ANISOU 5297  CA  GLY B1014    16932  11227  12949    320   2013    -39       C  
ATOM   5298  C   GLY B1014     -16.099  -7.222  -8.992  1.00107.38           C  
ANISOU 5298  C   GLY B1014    16863  11358  12579    761   1902    139       C  
ATOM   5299  O   GLY B1014     -15.485  -6.778  -8.022  1.00104.82           O  
ANISOU 5299  O   GLY B1014    16503  11178  12145    916   1944    516       O  
ATOM   5300  N   SER B1015     -15.765  -6.966 -10.251  1.00103.40           N  
ANISOU 5300  N   SER B1015    16430  10899  11958    946   1767   -146       N  
ATOM   5301  CA  SER B1015     -14.653  -6.110 -10.637  1.00100.29           C  
ANISOU 5301  CA  SER B1015    16062  10716  11328   1314   1702    -24       C  
ATOM   5302  C   SER B1015     -15.160  -4.674 -10.615  1.00102.06           C  
ANISOU 5302  C   SER B1015    16062  11414  11302   1322   1509    -78       C  
ATOM   5303  O   SER B1015     -16.323  -4.451 -10.954  1.00103.07           O  
ANISOU 5303  O   SER B1015    16056  11700  11406   1146   1373   -367       O  
ATOM   5304  CB  SER B1015     -14.173  -6.475 -12.039  1.00105.28           C  
ANISOU 5304  CB  SER B1015    16902  11189  11911   1498   1693   -311       C  
ATOM   5305  OG  SER B1015     -14.318  -7.860 -12.322  1.00118.50           O  
ANISOU 5305  OG  SER B1015    18798  12390  13837   1383   1821   -477       O  
ATOM   5306  N   ARG B1016     -14.302  -3.704 -10.217  1.00 95.10           N  
ANISOU 5306  N   ARG B1016    15132  10753  10248   1528   1493    179       N  
ATOM   5307  CA  ARG B1016     -14.640  -2.271 -10.150  1.00 91.64           C  
ANISOU 5307  CA  ARG B1016    14556  10686   9576   1570   1338    157       C  
ATOM   5308  C   ARG B1016     -14.897  -1.652 -11.540  1.00 95.86           C  
ANISOU 5308  C   ARG B1016    15173  11342   9908   1701   1197   -138       C  
ATOM   5309  O   ARG B1016     -15.764  -0.786 -11.670  1.00 94.88           O  
ANISOU 5309  O   ARG B1016    14952  11465   9633   1699   1036   -277       O  
ATOM   5310  CB  ARG B1016     -13.546  -1.491  -9.407  1.00 86.59           C  
ANISOU 5310  CB  ARG B1016    13882  10181   8837   1709   1372    473       C  
ATOM   5311  CG  ARG B1016     -13.973  -0.092  -9.017  1.00 83.96           C  
ANISOU 5311  CG  ARG B1016    13445  10147   8308   1705   1245    469       C  
ATOM   5312  CD  ARG B1016     -12.788   0.780  -8.701  1.00 79.02           C  
ANISOU 5312  CD  ARG B1016    12823   9625   7577   1818   1258    673       C  
ATOM   5313  NE  ARG B1016     -13.217   2.081  -8.187  1.00 72.72           N  
ANISOU 5313  NE  ARG B1016    11978   9041   6613   1795   1153    658       N  
ATOM   5314  CZ  ARG B1016     -13.478   2.337  -6.907  1.00 78.14           C  
ANISOU 5314  CZ  ARG B1016    12560   9858   7272   1709   1133    769       C  
ATOM   5315  NH1 ARG B1016     -13.352   1.378  -5.988  1.00 57.11           N1+
ANISOU 5315  NH1 ARG B1016     9834   7147   4716   1638   1211    947       N1+
ATOM   5316  NH2 ARG B1016     -13.869   3.547  -6.534  1.00 55.43           N  
ANISOU 5316  NH2 ARG B1016     9681   7144   4237   1721   1048    709       N  
ATOM   5317  N   ASP B1017     -14.115  -2.076 -12.552  1.00 93.97           N  
ANISOU 5317  N   ASP B1017    15127  10943   9634   1862   1268   -214       N  
ATOM   5318  CA  ASP B1017     -14.187  -1.659 -13.961  1.00 94.76           C  
ANISOU 5318  CA  ASP B1017    15386  11131   9488   2030   1176   -465       C  
ATOM   5319  C   ASP B1017     -15.516  -2.114 -14.575  1.00 99.84           C  
ANISOU 5319  C   ASP B1017    16000  11809  10124   1901    986   -863       C  
ATOM   5320  O   ASP B1017     -16.143  -1.366 -15.323  1.00 99.63           O  
ANISOU 5320  O   ASP B1017    15989  12024   9841   2015    789  -1058       O  
ATOM   5321  CB  ASP B1017     -12.998  -2.249 -14.753  1.00 98.68           C  
ANISOU 5321  CB  ASP B1017    16089  11431   9972   2222   1363   -449       C  
ATOM   5322  CG  ASP B1017     -12.705  -3.724 -14.464  1.00119.99           C  
ANISOU 5322  CG  ASP B1017    18845  13778  12969   2161   1511   -456       C  
ATOM   5323  OD1 ASP B1017     -12.310  -4.041 -13.308  1.00121.25           O  
ANISOU 5323  OD1 ASP B1017    18895  13841  13332   2103   1608   -163       O  
ATOM   5324  OD2 ASP B1017     -12.861  -4.559 -15.393  1.00130.23           O1-
ANISOU 5324  OD2 ASP B1017    20331  14879  14272   2193   1527   -755       O1-
ATOM   5325  N   GLU B1018     -15.937  -3.342 -14.225  1.00 98.00           N  
ANISOU 5325  N   GLU B1018    15723  11333  10180   1661   1045   -976       N  
ATOM   5326  CA  GLU B1018     -17.173  -4.011 -14.629  1.00100.76           C  
ANISOU 5326  CA  GLU B1018    15982  11671  10632   1422    895  -1379       C  
ATOM   5327  C   GLU B1018     -18.367  -3.326 -13.924  1.00102.35           C  
ANISOU 5327  C   GLU B1018    15843  12204  10842   1258    745  -1405       C  
ATOM   5328  O   GLU B1018     -19.471  -3.298 -14.479  1.00104.45           O  
ANISOU 5328  O   GLU B1018    15942  12681  11062   1165    521  -1772       O  
ATOM   5329  CB  GLU B1018     -17.063  -5.496 -14.240  1.00105.10           C  
ANISOU 5329  CB  GLU B1018    16624  11766  11542   1178   1093  -1395       C  
ATOM   5330  CG  GLU B1018     -18.129  -6.422 -14.797  1.00122.57           C  
ANISOU 5330  CG  GLU B1018    18802  13848  13921    866    987  -1865       C  
ATOM   5331  CD  GLU B1018     -18.407  -7.651 -13.947  1.00150.01           C  
ANISOU 5331  CD  GLU B1018    22286  16898  17815    492   1209  -1800       C  
ATOM   5332  OE1 GLU B1018     -17.526  -8.052 -13.149  1.00136.21           O1-
ANISOU 5332  OE1 GLU B1018    20696  14855  16202    577   1460  -1394       O1-
ATOM   5333  OE2 GLU B1018     -19.517  -8.215 -14.080  1.00152.39           O  
ANISOU 5333  OE2 GLU B1018    22432  17164  18307    110   1132  -2152       O  
ATOM   5334  N   ARG B1019     -18.124  -2.770 -12.701  1.00 94.27           N  
ANISOU 5334  N   ARG B1019    14701  11255   9861   1248    860  -1036       N  
ATOM   5335  CA  ARG B1019     -19.095  -2.020 -11.890  1.00 92.14           C  
ANISOU 5335  CA  ARG B1019    14131  11304   9572   1158    779  -1012       C  
ATOM   5336  C   ARG B1019     -19.289  -0.617 -12.473  1.00 91.99           C  
ANISOU 5336  C   ARG B1019    14112  11618   9221   1467    562  -1080       C  
ATOM   5337  O   ARG B1019     -20.431  -0.176 -12.591  1.00 93.13           O  
ANISOU 5337  O   ARG B1019    14021  12062   9304   1470    374  -1307       O  
ATOM   5338  CB  ARG B1019     -18.669  -1.931 -10.414  1.00 88.84           C  
ANISOU 5338  CB  ARG B1019    13663  10839   9254   1080    983   -612       C  
ATOM   5339  CG  ARG B1019     -18.833  -3.229  -9.632  1.00102.07           C  
ANISOU 5339  CG  ARG B1019    15317  12226  11238    766   1204   -507       C  
ATOM   5340  CD  ARG B1019     -18.744  -3.043  -8.120  1.00110.79           C  
ANISOU 5340  CD  ARG B1019    16341  13397  12359    697   1372   -142       C  
ATOM   5341  NE  ARG B1019     -17.472  -2.473  -7.660  1.00106.64           N  
ANISOU 5341  NE  ARG B1019    15970  12874  11674    956   1396    185       N  
ATOM   5342  CZ  ARG B1019     -16.556  -3.131  -6.953  1.00110.57           C  
ANISOU 5342  CZ  ARG B1019    16615  13147  12250    988   1556    508       C  
ATOM   5343  NH1 ARG B1019     -16.741  -4.407  -6.637  1.00 99.11           N1+
ANISOU 5343  NH1 ARG B1019    15255  11371  11031    800   1739    590       N1+
ATOM   5344  NH2 ARG B1019     -15.448  -2.518  -6.559  1.00 86.72           N  
ANISOU 5344  NH2 ARG B1019    13651  10218   9079   1212   1528    749       N  
ATOM   5345  N   LYS B1020     -18.180   0.079 -12.835  1.00 84.27           N  
ANISOU 5345  N   LYS B1020    13395  10584   8039   1731    604   -879       N  
ATOM   5346  CA  LYS B1020     -18.215   1.402 -13.464  1.00 82.53           C  
ANISOU 5346  CA  LYS B1020    13289  10575   7495   2031    452   -890       C  
ATOM   5347  C   LYS B1020     -18.860   1.292 -14.850  1.00 92.12           C  
ANISOU 5347  C   LYS B1020    14577  11916   8510   2178    225  -1245       C  
ATOM   5348  O   LYS B1020     -19.625   2.183 -15.221  1.00 94.59           O  
ANISOU 5348  O   LYS B1020    14845  12499   8597   2390      7  -1363       O  
ATOM   5349  CB  LYS B1020     -16.816   2.023 -13.584  1.00 80.81           C  
ANISOU 5349  CB  LYS B1020    13335  10219   7150   2193    610   -599       C  
ATOM   5350  CG  LYS B1020     -16.842   3.479 -14.076  1.00 74.59           C  
ANISOU 5350  CG  LYS B1020    12720   9571   6050   2462    513   -549       C  
ATOM   5351  CD  LYS B1020     -15.470   4.100 -14.164  1.00 74.62           C  
ANISOU 5351  CD  LYS B1020    12950   9428   5974   2531    711   -272       C  
ATOM   5352  CE  LYS B1020     -14.904   4.061 -15.559  1.00 82.56           C  
ANISOU 5352  CE  LYS B1020    14243  10370   6757   2715    771   -318       C  
ATOM   5353  NZ  LYS B1020     -13.443   4.341 -15.565  1.00 88.43           N1+
ANISOU 5353  NZ  LYS B1020    15107  10974   7520   2695   1041    -54       N1+
ATOM   5354  N   LYS B1021     -18.575   0.204 -15.606  1.00 89.76           N  
ANISOU 5354  N   LYS B1021    14404  11431   8271   2100    258  -1432       N  
ATOM   5355  CA  LYS B1021     -19.184   0.005 -16.921  1.00 92.68           C  
ANISOU 5355  CA  LYS B1021    14855  11944   8416   2227     14  -1821       C  
ATOM   5356  C   LYS B1021     -20.701  -0.129 -16.782  1.00 99.02           C  
ANISOU 5356  C   LYS B1021    15275  13039   9310   2075   -254  -2157       C  
ATOM   5357  O   LYS B1021     -21.428   0.652 -17.401  1.00101.57           O  
ANISOU 5357  O   LYS B1021    15546  13700   9346   2335   -537  -2326       O  
ATOM   5358  CB  LYS B1021     -18.577  -1.195 -17.668  1.00 96.81           C  
ANISOU 5358  CB  LYS B1021    15603  12181   8999   2155    122  -1999       C  
ATOM   5359  CG  LYS B1021     -17.669  -0.795 -18.829  1.00108.58           C  
ANISOU 5359  CG  LYS B1021    17486  13656  10114   2498    177  -1958       C  
ATOM   5360  CD  LYS B1021     -16.719  -1.929 -19.259  1.00121.40           C  
ANISOU 5360  CD  LYS B1021    19341  14940  11847   2466    412  -2018       C  
ATOM   5361  CE  LYS B1021     -15.385  -1.916 -18.533  1.00124.65           C  
ANISOU 5361  CE  LYS B1021    19800  15123  12438   2486    758  -1588       C  
ATOM   5362  NZ  LYS B1021     -14.577  -3.127 -18.823  1.00131.17           N1+
ANISOU 5362  NZ  LYS B1021    20797  15616  13426   2487    981  -1662       N1+
ATOM   5363  N   SER B1022     -21.172  -1.037 -15.900  1.00 94.33           N  
ANISOU 5363  N   SER B1022    14399  12332   9110   1673   -146  -2214       N  
ATOM   5364  CA  SER B1022     -22.600  -1.267 -15.682  1.00 96.54           C  
ANISOU 5364  CA  SER B1022    14234  12898   9548   1442   -337  -2539       C  
ATOM   5365  C   SER B1022     -23.365  -0.051 -15.183  1.00 99.15           C  
ANISOU 5365  C   SER B1022    14288  13640   9747   1648   -475  -2465       C  
ATOM   5366  O   SER B1022     -24.525   0.097 -15.552  1.00102.45           O  
ANISOU 5366  O   SER B1022    14370  14438  10119   1676   -755  -2807       O  
ATOM   5367  CB  SER B1022     -22.828  -2.452 -14.759  1.00100.52           C  
ANISOU 5367  CB  SER B1022    14549  13137  10508    940    -95  -2533       C  
ATOM   5368  OG  SER B1022     -24.209  -2.605 -14.472  1.00110.83           O  
ANISOU 5368  OG  SER B1022    15363  14753  11992    670   -224  -2828       O  
ATOM   5369  N   LEU B1023     -22.734   0.800 -14.347  1.00 91.59           N  
ANISOU 5369  N   LEU B1023    13451  12616   8731   1801   -292  -2054       N  
ATOM   5370  CA  LEU B1023     -23.316   2.029 -13.795  1.00 90.21           C  
ANISOU 5370  CA  LEU B1023    13104  12751   8422   2042   -375  -1958       C  
ATOM   5371  C   LEU B1023     -23.629   2.996 -14.937  1.00 95.94           C  
ANISOU 5371  C   LEU B1023    13974  13726   8751   2512   -691  -2104       C  
ATOM   5372  O   LEU B1023     -24.764   3.453 -15.058  1.00 97.78           O  
ANISOU 5372  O   LEU B1023    13896  14350   8908   2683   -939  -2332       O  
ATOM   5373  CB  LEU B1023     -22.335   2.670 -12.784  1.00 85.83           C  
ANISOU 5373  CB  LEU B1023    12761  11988   7863   2089   -113  -1519       C  
ATOM   5374  CG  LEU B1023     -22.684   4.060 -12.233  1.00 89.56           C  
ANISOU 5374  CG  LEU B1023    13197  12671   8160   2379   -163  -1402       C  
ATOM   5375  CD1 LEU B1023     -23.791   3.984 -11.200  1.00 91.61           C  
ANISOU 5375  CD1 LEU B1023    13001  13204   8602   2221   -122  -1501       C  
ATOM   5376  CD2 LEU B1023     -21.469   4.725 -11.607  1.00 87.71           C  
ANISOU 5376  CD2 LEU B1023    13284  12181   7862   2433     41  -1033       C  
ATOM   5377  N   LEU B1024     -22.624   3.261 -15.795  1.00 92.44           N  
ANISOU 5377  N   LEU B1024    13999  13073   8050   2735   -668  -1967       N  
ATOM   5378  CA  LEU B1024     -22.716   4.140 -16.965  1.00 94.51           C  
ANISOU 5378  CA  LEU B1024    14539  13495   7873   3203   -910  -2025       C  
ATOM   5379  C   LEU B1024     -23.755   3.606 -17.959  1.00105.57           C  
ANISOU 5379  C   LEU B1024    15729  15232   9152   3267  -1280  -2495       C  
ATOM   5380  O   LEU B1024     -24.522   4.393 -18.510  1.00108.46           O  
ANISOU 5380  O   LEU B1024    16050  15940   9219   3665  -1589  -2622       O  
ATOM   5381  CB  LEU B1024     -21.325   4.334 -17.625  1.00 92.31           C  
ANISOU 5381  CB  LEU B1024    14797  12895   7381   3331   -710  -1763       C  
ATOM   5382  CG  LEU B1024     -20.252   5.064 -16.776  1.00 91.90           C  
ANISOU 5382  CG  LEU B1024    14947  12568   7405   3299   -395  -1327       C  
ATOM   5383  CD1 LEU B1024     -18.859   4.810 -17.295  1.00 89.47           C  
ANISOU 5383  CD1 LEU B1024    14994  11966   7034   3267   -141  -1131       C  
ATOM   5384  CD2 LEU B1024     -20.523   6.552 -16.666  1.00 94.94           C  
ANISOU 5384  CD2 LEU B1024    15485  13035   7555   3645   -470  -1165       C  
ATOM   5385  N   SER B1025     -23.821   2.261 -18.114  1.00104.27           N  
ANISOU 5385  N   SER B1025    15415  14969   9234   2871  -1259  -2768       N  
ATOM   5386  CA  SER B1025     -24.791   1.530 -18.939  1.00109.07           C  
ANISOU 5386  CA  SER B1025    15764  15864   9814   2782  -1601  -3295       C  
ATOM   5387  C   SER B1025     -26.245   1.751 -18.448  1.00116.20           C  
ANISOU 5387  C   SER B1025    16041  17240  10870   2732  -1845  -3553       C  
ATOM   5388  O   SER B1025     -27.150   1.817 -19.282  1.00120.60           O  
ANISOU 5388  O   SER B1025    16380  18222  11220   2923  -2257  -3946       O  
ATOM   5389  CB  SER B1025     -24.462   0.040 -18.950  1.00113.48           C  
ANISOU 5389  CB  SER B1025    16328  16088  10701   2289  -1434  -3493       C  
ATOM   5390  OG  SER B1025     -25.454  -0.710 -19.634  1.00130.00           O  
ANISOU 5390  OG  SER B1025    18128  18437  12830   2103  -1760  -4058       O  
ATOM   5391  N   LYS B1026     -26.461   1.865 -17.105  1.00110.44           N  
ANISOU 5391  N   LYS B1026    15007  16475  10478   2499  -1592  -3342       N  
ATOM   5392  CA  LYS B1026     -27.777   2.123 -16.490  1.00112.93           C  
ANISOU 5392  CA  LYS B1026    14699  17248  10962   2455  -1727  -3540       C  
ATOM   5393  C   LYS B1026     -28.240   3.538 -16.844  1.00117.22           C  
ANISOU 5393  C   LYS B1026    15262  18164  11113   3110  -2008  -3492       C  
ATOM   5394  O   LYS B1026     -29.445   3.775 -16.980  1.00120.95           O  
ANISOU 5394  O   LYS B1026    15231  19155  11568   3268  -2310  -3807       O  
ATOM   5395  CB  LYS B1026     -27.749   1.945 -14.949  1.00112.74           C  
ANISOU 5395  CB  LYS B1026    14450  17067  11321   2091  -1320  -3270       C  
ATOM   5396  CG  LYS B1026     -27.552   0.506 -14.451  1.00122.52           C  
ANISOU 5396  CG  LYS B1026    15602  17965  12985   1441  -1034  -3311       C  
ATOM   5397  CD  LYS B1026     -28.806  -0.369 -14.519  1.00133.32           C  
ANISOU 5397  CD  LYS B1026    16367  19625  14662   1007  -1157  -3786       C  
ATOM   5398  CE  LYS B1026     -28.499  -1.804 -14.166  1.00136.32           C  
ANISOU 5398  CE  LYS B1026    16810  19538  15446    377   -852  -3804       C  
ATOM   5399  NZ  LYS B1026     -29.733  -2.622 -14.048  1.00146.70           N1+
ANISOU 5399  NZ  LYS B1026    17515  21096  17130   -148   -889  -4235       N1+
ATOM   5400  N   PHE B1027     -27.268   4.467 -17.007  1.00109.89           N  
ANISOU 5400  N   PHE B1027    14915  16958   9880   3493  -1898  -3100       N  
ATOM   5401  CA  PHE B1027     -27.491   5.860 -17.395  1.00110.50           C  
ANISOU 5401  CA  PHE B1027    15203  17226   9558   4145  -2103  -2970       C  
ATOM   5402  C   PHE B1027     -27.461   6.034 -18.933  1.00119.52           C  
ANISOU 5402  C   PHE B1027    16684  18504  10224   4560  -2454  -3121       C  
ATOM   5403  O   PHE B1027     -27.670   7.143 -19.438  1.00120.72           O  
ANISOU 5403  O   PHE B1027    17083  18802   9984   5157  -2654  -3007       O  
ATOM   5404  CB  PHE B1027     -26.469   6.787 -16.703  1.00106.87           C  
ANISOU 5404  CB  PHE B1027    15208  16349   9049   4270  -1762  -2474       C  
ATOM   5405  CG  PHE B1027     -26.470   6.798 -15.187  1.00104.88           C  
ANISOU 5405  CG  PHE B1027    14699  16001   9152   3963  -1448  -2311       C  
ATOM   5406  CD1 PHE B1027     -27.648   6.619 -14.470  1.00110.03           C  
ANISOU 5406  CD1 PHE B1027    14734  17040  10035   3855  -1500  -2542       C  
ATOM   5407  CD2 PHE B1027     -25.303   7.047 -14.478  1.00101.83           C  
ANISOU 5407  CD2 PHE B1027    14675  15181   8835   3808  -1103  -1934       C  
ATOM   5408  CE1 PHE B1027     -27.647   6.640 -13.072  1.00108.42           C  
ANISOU 5408  CE1 PHE B1027    14336  16767  10092   3599  -1182  -2379       C  
ATOM   5409  CE2 PHE B1027     -25.306   7.077 -13.079  1.00102.03           C  
ANISOU 5409  CE2 PHE B1027    14497  15156   9114   3564   -843  -1796       C  
ATOM   5410  CZ  PHE B1027     -26.477   6.877 -12.388  1.00102.45           C  
ANISOU 5410  CZ  PHE B1027    13995  15576   9355   3473   -872  -2007       C  
ATOM   5411  N   GLY B1028     -27.222   4.928 -19.649  1.00118.84           N  
ANISOU 5411  N   GLY B1028    16640  18357  10157   4262  -2517  -3378       N  
ATOM   5412  CA  GLY B1028     -27.152   4.877 -21.108  1.00122.78           C  
ANISOU 5412  CA  GLY B1028    17471  18995  10184   4588  -2829  -3574       C  
ATOM   5413  C   GLY B1028     -25.966   5.620 -21.693  1.00125.37           C  
ANISOU 5413  C   GLY B1028    18558  18968  10111   4938  -2630  -3150       C  
ATOM   5414  O   GLY B1028     -26.014   6.051 -22.850  1.00128.68           O  
ANISOU 5414  O   GLY B1028    19328  19559  10007   5407  -2887  -3194       O  
ATOM   5415  N   MET B1029     -24.892   5.760 -20.893  1.00116.83           N  
ANISOU 5415  N   MET B1029    17720  17410   9261   4701  -2165  -2739       N  
ATOM   5416  CA  MET B1029     -23.666   6.472 -21.236  1.00114.42           C  
ANISOU 5416  CA  MET B1029    18056  16732   8687   4911  -1880  -2306       C  
ATOM   5417  C   MET B1029     -22.534   5.539 -21.609  1.00117.58           C  
ANISOU 5417  C   MET B1029    18719  16806   9150   4601  -1599  -2275       C  
ATOM   5418  O   MET B1029     -22.483   4.396 -21.143  1.00115.35           O  
ANISOU 5418  O   MET B1029    18147  16423   9258   4146  -1501  -2460       O  
ATOM   5419  CB  MET B1029     -23.206   7.339 -20.060  1.00112.66           C  
ANISOU 5419  CB  MET B1029    17883  16237   8686   4857  -1571  -1903       C  
ATOM   5420  CG  MET B1029     -24.087   8.532 -19.786  1.00118.49           C  
ANISOU 5420  CG  MET B1029    18550  17193   9279   5293  -1772  -1850       C  
ATOM   5421  SD  MET B1029     -23.935   9.113 -18.071  1.00118.63           S  
ANISOU 5421  SD  MET B1029    18374  16995   9703   5064  -1464  -1597       S  
ATOM   5422  CE  MET B1029     -22.282   9.741 -18.086  1.00111.72           C  
ANISOU 5422  CE  MET B1029    18144  15561   8743   4990  -1053  -1129       C  
ATOM   5423  N   ASP B1030     -21.604   6.064 -22.435  1.00116.10           N  
ANISOU 5423  N   ASP B1030    19104  16431   8577   4870  -1432  -2013       N  
ATOM   5424  CA  ASP B1030     -20.372   5.409 -22.875  1.00115.25           C  
ANISOU 5424  CA  ASP B1030    19308  16022   8460   4687  -1101  -1917       C  
ATOM   5425  C   ASP B1030     -19.362   5.494 -21.716  1.00113.63           C  
ANISOU 5425  C   ASP B1030    19050  15448   8675   4352   -674  -1553       C  
ATOM   5426  O   ASP B1030     -19.438   6.427 -20.903  1.00110.88           O  
ANISOU 5426  O   ASP B1030    18652  15048   8431   4388   -616  -1304       O  
ATOM   5427  CB  ASP B1030     -19.783   6.131 -24.113  1.00120.23           C  
ANISOU 5427  CB  ASP B1030    20553  16631   8498   5118  -1028  -1717       C  
ATOM   5428  CG  ASP B1030     -20.528   5.987 -25.437  1.00140.89           C  
ANISOU 5428  CG  ASP B1030    23345  19614  10573   5505  -1429  -2053       C  
ATOM   5429  OD1 ASP B1030     -21.498   5.193 -25.497  1.00145.47           O1-
ANISOU 5429  OD1 ASP B1030    23527  20486  11261   5394  -1799  -2525       O1-
ATOM   5430  OD2 ASP B1030     -20.133   6.659 -26.417  1.00147.87           O  
ANISOU 5430  OD2 ASP B1030    24769  20502  10913   5904  -1368  -1848       O  
ATOM   5431  N   GLU B1031     -18.413   4.533 -21.659  1.00108.05           N  
ANISOU 5431  N   GLU B1031    18365  14499   8189   4064   -392  -1542       N  
ATOM   5432  CA  GLU B1031     -17.365   4.465 -20.645  1.00103.15           C  
ANISOU 5432  CA  GLU B1031    17672  13581   7940   3775    -22  -1227       C  
ATOM   5433  C   GLU B1031     -16.414   5.666 -20.714  1.00104.84           C  
ANISOU 5433  C   GLU B1031    18222  13639   7971   3923    245   -814       C  
ATOM   5434  O   GLU B1031     -16.041   6.121 -21.796  1.00107.75           O  
ANISOU 5434  O   GLU B1031    18993  14011   7937   4190    320   -731       O  
ATOM   5435  CB  GLU B1031     -16.590   3.144 -20.734  1.00104.49           C  
ANISOU 5435  CB  GLU B1031    17813  13551   8335   3541    190  -1326       C  
ATOM   5436  CG  GLU B1031     -15.904   2.755 -19.431  1.00114.26           C  
ANISOU 5436  CG  GLU B1031    18805  14566  10040   3223    439  -1099       C  
ATOM   5437  CD  GLU B1031     -14.971   1.558 -19.470  1.00145.97           C  
ANISOU 5437  CD  GLU B1031    22838  18346  14277   3081    687  -1117       C  
ATOM   5438  OE1 GLU B1031     -14.903   0.876 -20.519  1.00154.84           O  
ANISOU 5438  OE1 GLU B1031    24158  19447  15225   3191    679  -1370       O  
ATOM   5439  OE2 GLU B1031     -14.310   1.296 -18.438  1.00138.19           O1-
ANISOU 5439  OE2 GLU B1031    21680  17202  13622   2893    880   -889       O1-
ATOM   5440  N   GLY B1032     -16.067   6.169 -19.540  1.00 96.77           N  
ANISOU 5440  N   GLY B1032    17042  12488   7240   3730    389   -571       N  
ATOM   5441  CA  GLY B1032     -15.175   7.300 -19.340  1.00 94.69           C  
ANISOU 5441  CA  GLY B1032    17022  12039   6918   3747    647   -212       C  
ATOM   5442  C   GLY B1032     -14.965   7.566 -17.864  1.00 93.03           C  
ANISOU 5442  C   GLY B1032    16531  11737   7077   3472    721    -71       C  
ATOM   5443  O   GLY B1032     -15.687   7.016 -17.029  1.00 91.15           O  
ANISOU 5443  O   GLY B1032    15950  11608   7076   3336    561   -225       O  
ATOM   5444  N   VAL B1033     -13.973   8.406 -17.542  1.00 87.83           N  
ANISOU 5444  N   VAL B1033    16024  10889   6459   3370    975    210       N  
ATOM   5445  CA  VAL B1033     -13.574   8.811 -16.189  1.00 85.48           C  
ANISOU 5445  CA  VAL B1033    15521  10506   6451   3111   1053    344       C  
ATOM   5446  C   VAL B1033     -14.753   9.456 -15.435  1.00 90.47           C  
ANISOU 5446  C   VAL B1033    16069  11225   7081   3211    812    249       C  
ATOM   5447  O   VAL B1033     -15.073  10.628 -15.645  1.00 93.03           O  
ANISOU 5447  O   VAL B1033    16679  11463   7205   3418    776    319       O  
ATOM   5448  CB  VAL B1033     -12.321   9.711 -16.246  1.00 89.70           C  
ANISOU 5448  CB  VAL B1033    16272  10831   6980   2982   1354    609       C  
ATOM   5449  CG1 VAL B1033     -11.748   9.951 -14.855  1.00 87.12           C  
ANISOU 5449  CG1 VAL B1033    15687  10458   6957   2674   1409    692       C  
ATOM   5450  CG2 VAL B1033     -11.272   9.102 -17.165  1.00 90.83           C  
ANISOU 5450  CG2 VAL B1033    16484  10949   7078   2955   1617    682       C  
ATOM   5451  N   THR B1034     -15.409   8.661 -14.587  1.00 84.85           N  
ANISOU 5451  N   THR B1034    14982  10672   6585   3084    674     94       N  
ATOM   5452  CA  THR B1034     -16.602   9.042 -13.846  1.00 84.77           C  
ANISOU 5452  CA  THR B1034    14796  10817   6595   3172    476    -37       C  
ATOM   5453  C   THR B1034     -16.289   9.811 -12.557  1.00 86.84           C  
ANISOU 5453  C   THR B1034    15021  10992   6981   3027    564     87       C  
ATOM   5454  O   THR B1034     -15.618   9.298 -11.661  1.00 83.63           O  
ANISOU 5454  O   THR B1034    14422  10565   6787   2746    677    169       O  
ATOM   5455  CB  THR B1034     -17.480   7.803 -13.605  1.00 95.39           C  
ANISOU 5455  CB  THR B1034    15760  12379   8106   3063    337   -265       C  
ATOM   5456  OG1 THR B1034     -17.606   7.070 -14.817  1.00 96.57           O  
ANISOU 5456  OG1 THR B1034    15978  12574   8140   3154    257   -419       O  
ATOM   5457  CG2 THR B1034     -18.854   8.151 -13.117  1.00 97.86           C  
ANISOU 5457  CG2 THR B1034    15843  12933   8406   3198    138   -443       C  
ATOM   5458  N   PHE B1035     -16.818  11.045 -12.482  1.00 85.83           N  
ANISOU 5458  N   PHE B1035    15102  10816   6694   3260    494     85       N  
ATOM   5459  CA  PHE B1035     -16.711  11.972 -11.352  1.00 85.25           C  
ANISOU 5459  CA  PHE B1035    15073  10640   6678   3190    546    131       C  
ATOM   5460  C   PHE B1035     -18.052  12.026 -10.678  1.00 90.82           C  
ANISOU 5460  C   PHE B1035    15532  11593   7383   3362    381    -60       C  
ATOM   5461  O   PHE B1035     -19.080  11.950 -11.364  1.00 91.02           O  
ANISOU 5461  O   PHE B1035    15495  11802   7286   3655    205   -203       O  
ATOM   5462  CB  PHE B1035     -16.335  13.389 -11.829  1.00 88.89           C  
ANISOU 5462  CB  PHE B1035    16025  10790   6961   3357    628    257       C  
ATOM   5463  CG  PHE B1035     -14.962  13.479 -12.448  1.00 90.40           C  
ANISOU 5463  CG  PHE B1035    16445  10740   7165   3141    859    460       C  
ATOM   5464  CD1 PHE B1035     -14.779  13.262 -13.808  1.00 94.04           C  
ANISOU 5464  CD1 PHE B1035    17122  11167   7442   3299    909    538       C  
ATOM   5465  CD2 PHE B1035     -13.844  13.728 -11.665  1.00 91.61           C  
ANISOU 5465  CD2 PHE B1035    16555  10749   7502   2776   1027    553       C  
ATOM   5466  CE1 PHE B1035     -13.499  13.271 -14.365  1.00 95.24           C  
ANISOU 5466  CE1 PHE B1035    17432  11142   7612   3089   1177    723       C  
ATOM   5467  CE2 PHE B1035     -12.568  13.763 -12.234  1.00 94.56           C  
ANISOU 5467  CE2 PHE B1035    17045  10961   7923   2554   1261    722       C  
ATOM   5468  CZ  PHE B1035     -12.404  13.540 -13.579  1.00 93.48           C  
ANISOU 5468  CZ  PHE B1035    17114  10786   7616   2711   1362    817       C  
ATOM   5469  N   MET B1036     -18.056  12.137  -9.333  1.00 88.87           N  
ANISOU 5469  N   MET B1036    15116  11396   7254   3192    436    -79       N  
ATOM   5470  CA  MET B1036     -19.308  12.238  -8.587  1.00 90.36           C  
ANISOU 5470  CA  MET B1036    15052  11845   7436   3351    343   -258       C  
ATOM   5471  C   MET B1036     -19.239  13.292  -7.486  1.00 95.79           C  
ANISOU 5471  C   MET B1036    15887  12431   8077   3379    410   -274       C  
ATOM   5472  O   MET B1036     -18.176  13.524  -6.905  1.00 94.09           O  
ANISOU 5472  O   MET B1036    15811  12030   7911   3116    519   -168       O  
ATOM   5473  CB  MET B1036     -19.816  10.868  -8.075  1.00 92.02           C  
ANISOU 5473  CB  MET B1036    14795  12345   7823   3124    349   -334       C  
ATOM   5474  CG  MET B1036     -19.387  10.504  -6.671  1.00 95.24           C  
ANISOU 5474  CG  MET B1036    15053  12794   8340   2830    491   -251       C  
ATOM   5475  SD  MET B1036     -20.263   9.068  -6.009  1.00100.48           S  
ANISOU 5475  SD  MET B1036    15236  13764   9180   2612    551   -316       S  
ATOM   5476  CE  MET B1036     -21.705   9.842  -5.341  1.00 99.66           C  
ANISOU 5476  CE  MET B1036    14926  13963   8975   2873    529   -527       C  
ATOM   5477  N   PHE B1037     -20.378  13.975  -7.272  1.00 96.29           N  
ANISOU 5477  N   PHE B1037    15924  12626   8035   3730    328   -437       N  
ATOM   5478  CA  PHE B1037     -20.617  14.957  -6.219  1.00 98.22           C  
ANISOU 5478  CA  PHE B1037    16293  12817   8210   3847    383   -531       C  
ATOM   5479  C   PHE B1037     -21.833  14.455  -5.467  1.00105.60           C  
ANISOU 5479  C   PHE B1037    16766  14184   9172   3941    375   -706       C  
ATOM   5480  O   PHE B1037     -22.837  14.095  -6.089  1.00106.50           O  
ANISOU 5480  O   PHE B1037    16606  14564   9293   4165    258   -817       O  
ATOM   5481  CB  PHE B1037     -20.887  16.361  -6.775  1.00103.03           C  
ANISOU 5481  CB  PHE B1037    17357  13138   8651   4278    332   -561       C  
ATOM   5482  CG  PHE B1037     -21.328  17.354  -5.715  1.00107.39           C  
ANISOU 5482  CG  PHE B1037    18041  13635   9127   4474    385   -722       C  
ATOM   5483  CD1 PHE B1037     -20.395  18.007  -4.916  1.00110.41           C  
ANISOU 5483  CD1 PHE B1037    18730  13706   9515   4215    503   -715       C  
ATOM   5484  CD2 PHE B1037     -22.680  17.625  -5.507  1.00112.40           C  
ANISOU 5484  CD2 PHE B1037    18466  14556   9683   4922    316   -915       C  
ATOM   5485  CE1 PHE B1037     -20.806  18.911  -3.930  1.00113.95           C  
ANISOU 5485  CE1 PHE B1037    19336  14091   9868   4402    552   -911       C  
ATOM   5486  CE2 PHE B1037     -23.088  18.528  -4.519  1.00117.54           C  
ANISOU 5486  CE2 PHE B1037    19251  15160  10249   5143    394  -1087       C  
ATOM   5487  CZ  PHE B1037     -22.149  19.163  -3.738  1.00115.56           C  
ANISOU 5487  CZ  PHE B1037    19368  14559   9982   4882    513  -1090       C  
ATOM   5488  N   ILE B1038     -21.748  14.440  -4.138  1.00104.29           N  
ANISOU 5488  N   ILE B1038    16501  14117   9008   3765    503   -742       N  
ATOM   5489  CA  ILE B1038     -22.839  13.975  -3.290  1.00106.94           C  
ANISOU 5489  CA  ILE B1038    16408  14870   9356   3811    577   -882       C  
ATOM   5490  C   ILE B1038     -23.125  14.994  -2.165  1.00116.01           C  
ANISOU 5490  C   ILE B1038    17708  16029  10341   4008    673  -1028       C  
ATOM   5491  O   ILE B1038     -22.204  15.585  -1.592  1.00115.55           O  
ANISOU 5491  O   ILE B1038    17999  15703  10203   3870    713   -995       O  
ATOM   5492  CB  ILE B1038     -22.578  12.513  -2.806  1.00108.35           C  
ANISOU 5492  CB  ILE B1038    16250  15237   9682   3366    686   -753       C  
ATOM   5493  CG1 ILE B1038     -23.802  11.897  -2.095  1.00111.17           C  
ANISOU 5493  CG1 ILE B1038    16130  16028  10081   3358    814   -870       C  
ATOM   5494  CG2 ILE B1038     -21.310  12.376  -1.963  1.00107.12           C  
ANISOU 5494  CG2 ILE B1038    16295  14908   9496   3041    771   -583       C  
ATOM   5495  CD1 ILE B1038     -24.352  10.683  -2.776  1.00119.87           C  
ANISOU 5495  CD1 ILE B1038    16845  17311  11390   3177    789   -879       C  
ATOM   5496  N   GLY B1039     -24.408  15.212  -1.910  1.00116.98           N  
ANISOU 5496  N   GLY B1039    17556  16475  10417   4343    702  -1221       N  
ATOM   5497  CA  GLY B1039     -24.881  16.141  -0.896  1.00120.48           C  
ANISOU 5497  CA  GLY B1039    18106  16979  10691   4616    816  -1408       C  
ATOM   5498  C   GLY B1039     -26.108  16.897  -1.349  1.00130.18           C  
ANISOU 5498  C   GLY B1039    19235  18361  11868   5213    744  -1614       C  
ATOM   5499  O   GLY B1039     -26.891  16.385  -2.159  1.00130.45           O  
ANISOU 5499  O   GLY B1039    18886  18675  12006   5352    629  -1646       O  
ATOM   5500  N   ARG B1040     -26.284  18.124  -0.816  1.00131.09           N  
ANISOU 5500  N   ARG B1040    19692  18299  11816   5588    797  -1778       N  
ATOM   5501  CA  ARG B1040     -27.424  18.983  -1.140  1.00135.81           C  
ANISOU 5501  CA  ARG B1040    20249  19011  12340   6263    737  -1980       C  
ATOM   5502  C   ARG B1040     -27.025  20.197  -2.001  1.00141.57           C  
ANISOU 5502  C   ARG B1040    21637  19165  12989   6644    586  -1937       C  
ATOM   5503  O   ARG B1040     -25.865  20.625  -1.991  1.00139.25           O  
ANISOU 5503  O   ARG B1040    21877  18353  12678   6361    605  -1819       O  
ATOM   5504  CB  ARG B1040     -28.214  19.390   0.128  1.00139.62           C  
ANISOU 5504  CB  ARG B1040    20561  19797  12693   6517    960  -2230       C  
ATOM   5505  CG  ARG B1040     -27.560  20.433   1.037  1.00149.68           C  
ANISOU 5505  CG  ARG B1040    22439  20654  13779   6556   1075  -2344       C  
ATOM   5506  CD  ARG B1040     -28.519  20.939   2.103  1.00159.40           C  
ANISOU 5506  CD  ARG B1040    23519  22203  14842   6961   1289  -2637       C  
ATOM   5507  NE  ARG B1040     -29.430  21.963   1.585  1.00167.75           N  
ANISOU 5507  NE  ARG B1040    24683  23193  15861   7729   1216  -2819       N  
ATOM   5508  CZ  ARG B1040     -30.694  21.744   1.233  1.00180.62           C  
ANISOU 5508  CZ  ARG B1040    25728  25346  17555   8168   1197  -2923       C  
ATOM   5509  NH1 ARG B1040     -31.222  20.531   1.345  1.00163.90           N  
ANISOU 5509  NH1 ARG B1040    22874  23834  15568   7845   1273  -2880       N  
ATOM   5510  NH2 ARG B1040     -31.442  22.737   0.772  1.00170.33           N1+
ANISOU 5510  NH2 ARG B1040    24566  23961  16193   8934   1102  -3076       N1+
ATOM   5511  N   PHE B1041     -28.000  20.727  -2.757  1.00142.04           N  
ANISOU 5511  N   PHE B1041    21639  19331  13001   7286    440  -2025       N  
ATOM   5512  CA  PHE B1041     -27.809  21.862  -3.648  1.00144.23           C  
ANISOU 5512  CA  PHE B1041    22553  19078  13170   7752    307  -1947       C  
ATOM   5513  C   PHE B1041     -27.976  23.197  -2.929  1.00151.59           C  
ANISOU 5513  C   PHE B1041    23980  19646  13971   8191    436  -2129       C  
ATOM   5514  O   PHE B1041     -29.100  23.625  -2.652  1.00155.14           O  
ANISOU 5514  O   PHE B1041    24208  20390  14350   8796    445  -2345       O  
ATOM   5515  CB  PHE B1041     -28.719  21.750  -4.882  1.00148.62           C  
ANISOU 5515  CB  PHE B1041    22850  19925  13693   8274     42  -1925       C  
ATOM   5516  N   ASP B1042     -26.834  23.827  -2.591  1.00147.81           N  
ANISOU 5516  N   ASP B1042    24149  18539  13474   7859    545  -2070       N  
ATOM   5517  CA  ASP B1042     -26.737  25.145  -1.937  1.00152.41           C  
ANISOU 5517  CA  ASP B1042    25355  18606  13948   8153    674  -2259       C  
ATOM   5518  C   ASP B1042     -25.417  25.848  -2.314  1.00155.88           C  
ANISOU 5518  C   ASP B1042    26568  18237  14422   7793    706  -2094       C  
ATOM   5519  O   ASP B1042     -24.464  25.184  -2.743  1.00150.38           O  
ANISOU 5519  O   ASP B1042    25819  17486  13833   7205    675  -1867       O  
ATOM   5520  CB  ASP B1042     -26.994  25.102  -0.396  1.00155.25           C  
ANISOU 5520  CB  ASP B1042    25492  19264  14234   8044    869  -2564       C  
ATOM   5521  CG  ASP B1042     -25.960  24.455   0.531  1.00159.84           C  
ANISOU 5521  CG  ASP B1042    25999  19899  14833   7252    968  -2556       C  
ATOM   5522  OD1 ASP B1042     -24.962  23.903   0.026  1.00156.72           O1-
ANISOU 5522  OD1 ASP B1042    25640  19348  14558   6712    890  -2309       O1-
ATOM   5523  OD2 ASP B1042     -26.162  24.496   1.763  1.00165.89           O  
ANISOU 5523  OD2 ASP B1042    26666  20896  15470   7215   1121  -2797       O  
ATOM   5524  N   ARG B1043     -25.397  27.194  -2.212  1.00158.01           N  
ANISOU 5524  N   ARG B1043    27549  17869  14616   8168    784  -2209       N  
ATOM   5525  CA  ARG B1043     -24.255  28.037  -2.585  1.00158.95           C  
ANISOU 5525  CA  ARG B1043    28460  17145  14790   7857    859  -2078       C  
ATOM   5526  C   ARG B1043     -23.010  27.842  -1.697  1.00159.76           C  
ANISOU 5526  C   ARG B1043    28616  17098  14986   7006    958  -2176       C  
ATOM   5527  O   ARG B1043     -21.920  27.615  -2.225  1.00156.60           O  
ANISOU 5527  O   ARG B1043    28349  16442  14711   6448    964  -1948       O  
ATOM   5528  CB  ARG B1043     -24.669  29.521  -2.645  1.00166.05           C  
ANISOU 5528  CB  ARG B1043    30129  17367  15597   8509    938  -2201       C  
ATOM   5529  N   GLY B1044     -23.194  27.928  -0.377  1.00156.77           N  
ANISOU 5529  N   GLY B1044    28116  16924  14525   6946   1030  -2518       N  
ATOM   5530  CA  GLY B1044     -22.126  27.811   0.613  1.00154.74           C  
ANISOU 5530  CA  GLY B1044    27901  16603  14289   6234   1076  -2679       C  
ATOM   5531  C   GLY B1044     -21.510  26.437   0.792  1.00151.89           C  
ANISOU 5531  C   GLY B1044    26908  16805  13998   5623   1005  -2505       C  
ATOM   5532  O   GLY B1044     -20.969  25.857  -0.155  1.00147.83           O  
ANISOU 5532  O   GLY B1044    26260  16281  13628   5353    945  -2186       O  
ATOM   5533  N   GLN B1045     -21.569  25.941   2.044  1.00146.94           N  
ANISOU 5533  N   GLN B1045    25941  16648  13240   5429   1028  -2716       N  
ATOM   5534  CA  GLN B1045     -21.035  24.684   2.600  1.00141.61           C  
ANISOU 5534  CA  GLN B1045    24720  16520  12564   4903    983  -2605       C  
ATOM   5535  C   GLN B1045     -20.624  23.576   1.591  1.00138.81           C  
ANISOU 5535  C   GLN B1045    23977  16359  12407   4618    901  -2212       C  
ATOM   5536  O   GLN B1045     -19.472  23.149   1.622  1.00136.06           O  
ANISOU 5536  O   GLN B1045    23579  15964  12153   4067    849  -2089       O  
ATOM   5537  CB  GLN B1045     -22.014  24.092   3.632  1.00143.24           C  
ANISOU 5537  CB  GLN B1045    24471  17386  12567   5138   1069  -2759       C  
ATOM   5538  CG  GLN B1045     -22.137  24.902   4.932  1.00163.63           C  
ANISOU 5538  CG  GLN B1045    27367  19915  14889   5258   1160  -3170       C  
ATOM   5539  CD  GLN B1045     -20.983  24.715   5.898  1.00181.23           C  
ANISOU 5539  CD  GLN B1045    29671  22188  17001   4662   1089  -3276       C  
ATOM   5540  OE1 GLN B1045     -20.522  23.596   6.165  1.00174.67           O  
ANISOU 5540  OE1 GLN B1045    28415  21787  16163   4280   1035  -3064       O  
ATOM   5541  NE2 GLN B1045     -20.501  25.812   6.460  1.00174.10           N  
ANISOU 5541  NE2 GLN B1045    29318  20838  15993   4591   1073  -3623       N  
ATOM   5542  N   LYS B1046     -21.550  23.102   0.733  1.00132.89           N  
ANISOU 5542  N   LYS B1046    22930  15853  11708   4996    879  -2050       N  
ATOM   5543  CA  LYS B1046     -21.306  21.997  -0.210  1.00127.89           C  
ANISOU 5543  CA  LYS B1046    21925  15435  11231   4775    803  -1736       C  
ATOM   5544  C   LYS B1046     -20.383  22.358  -1.388  1.00130.24           C  
ANISOU 5544  C   LYS B1046    22605  15221  11660   4597    765  -1514       C  
ATOM   5545  O   LYS B1046     -19.555  21.533  -1.779  1.00126.48           O  
ANISOU 5545  O   LYS B1046    21925  14826  11306   4173    738  -1304       O  
ATOM   5546  CB  LYS B1046     -22.634  21.389  -0.719  1.00129.89           C  
ANISOU 5546  CB  LYS B1046    21719  16148  11485   5212    767  -1704       C  
ATOM   5547  CG  LYS B1046     -23.577  20.878   0.382  1.00133.64           C  
ANISOU 5547  CG  LYS B1046    21722  17194  11860   5329    869  -1884       C  
ATOM   5548  CD  LYS B1046     -23.271  19.463   0.860  1.00129.47           C  
ANISOU 5548  CD  LYS B1046    20702  17097  11395   4840    909  -1736       C  
ATOM   5549  CE  LYS B1046     -24.218  19.035   1.954  1.00128.11           C  
ANISOU 5549  CE  LYS B1046    20124  17452  11099   4948   1074  -1884       C  
ATOM   5550  NZ  LYS B1046     -24.068  17.597   2.299  1.00125.77           N  
ANISOU 5550  NZ  LYS B1046    19374  17538  10876   4517   1143  -1690       N  
ATOM   5551  N   GLY B1047     -20.555  23.560  -1.942  1.00129.38           N  
ANISOU 5551  N   GLY B1047    23053  14591  11515   4947    790  -1547       N  
ATOM   5552  CA  GLY B1047     -19.760  24.065  -3.057  1.00129.08           C  
ANISOU 5552  CA  GLY B1047    23472  14009  11564   4820    819  -1319       C  
ATOM   5553  C   GLY B1047     -20.160  23.570  -4.434  1.00130.39           C  
ANISOU 5553  C   GLY B1047    23522  14298  11723   5096    741  -1051       C  
ATOM   5554  O   GLY B1047     -19.305  23.468  -5.320  1.00129.02           O  
ANISOU 5554  O   GLY B1047    23529  13874  11619   4824    785   -808       O  
ATOM   5555  N   VAL B1048     -21.469  23.291  -4.639  1.00126.16           N  
ANISOU 5555  N   VAL B1048    22678  14168  11087   5648    628  -1114       N  
ATOM   5556  CA  VAL B1048     -22.052  22.841  -5.914  1.00124.53           C  
ANISOU 5556  CA  VAL B1048    22324  14165  10825   5994    490   -935       C  
ATOM   5557  C   VAL B1048     -21.727  23.870  -6.992  1.00128.76           C  
ANISOU 5557  C   VAL B1048    23572  14087  11264   6262    524   -729       C  
ATOM   5558  O   VAL B1048     -21.334  23.496  -8.095  1.00127.36           O  
ANISOU 5558  O   VAL B1048    23463  13871  11056   6189    496   -484       O  
ATOM   5559  CB  VAL B1048     -23.592  22.611  -5.847  1.00130.60           C  
ANISOU 5559  CB  VAL B1048    22646  15470  11507   6587    345  -1113       C  
ATOM   5560  CG1 VAL B1048     -24.039  21.603  -6.901  1.00128.79           C  
ANISOU 5560  CG1 VAL B1048    21990  15673  11273   6670    163  -1000       C  
ATOM   5561  CG2 VAL B1048     -24.053  22.177  -4.456  1.00129.87           C  
ANISOU 5561  CG2 VAL B1048    22074  15810  11462   6447    421  -1366       C  
ATOM   5562  N   ASP B1049     -21.857  25.166  -6.641  1.00127.99           N  
ANISOU 5562  N   ASP B1049    24047  13477  11106   6561    616   -827       N  
ATOM   5563  CA  ASP B1049     -21.604  26.329  -7.495  1.00131.70           C  
ANISOU 5563  CA  ASP B1049    25321  13240  11481   6851    704   -628       C  
ATOM   5564  C   ASP B1049     -20.156  26.403  -8.013  1.00133.12           C  
ANISOU 5564  C   ASP B1049    25861  12950  11770   6206    894   -375       C  
ATOM   5565  O   ASP B1049     -19.918  27.009  -9.061  1.00135.47           O  
ANISOU 5565  O   ASP B1049    26727  12783  11963   6394    982    -99       O  
ATOM   5566  CB  ASP B1049     -22.030  27.641  -6.785  1.00138.51           C  
ANISOU 5566  CB  ASP B1049    26712  13617  12298   7252    792   -844       C  
ATOM   5567  CG  ASP B1049     -21.175  28.086  -5.607  1.00142.88           C  
ANISOU 5567  CG  ASP B1049    27465  13821  13001   6671    964  -1076       C  
ATOM   5568  OD1 ASP B1049     -20.802  27.225  -4.780  1.00138.00           O  
ANISOU 5568  OD1 ASP B1049    26294  13659  12480   6157    940  -1218       O  
ATOM   5569  OD2 ASP B1049     -20.894  29.300  -5.505  1.00152.12           O1-
ANISOU 5569  OD2 ASP B1049    29366  14254  14180   6745   1113  -1124       O1-
ATOM   5570  N   VAL B1050     -19.201  25.785  -7.287  1.00124.87           N  
ANISOU 5570  N   VAL B1050    24474  12053  10919   5473    966   -457       N  
ATOM   5571  CA  VAL B1050     -17.795  25.743  -7.698  1.00123.48           C  
ANISOU 5571  CA  VAL B1050    24480  11551  10884   4824   1149   -254       C  
ATOM   5572  C   VAL B1050     -17.653  24.654  -8.769  1.00124.56           C  
ANISOU 5572  C   VAL B1050    24274  12077  10977   4786   1091      3       C  
ATOM   5573  O   VAL B1050     -16.904  24.849  -9.726  1.00125.48           O  
ANISOU 5573  O   VAL B1050    24730  11866  11079   4615   1255    275       O  
ATOM   5574  CB  VAL B1050     -16.797  25.549  -6.521  1.00125.20           C  
ANISOU 5574  CB  VAL B1050    24450  11809  11312   4108   1211   -459       C  
ATOM   5575  CG1 VAL B1050     -15.356  25.785  -6.972  1.00125.58           C  
ANISOU 5575  CG1 VAL B1050    24736  11449  11529   3477   1425   -278       C  
ATOM   5576  CG2 VAL B1050     -17.136  26.466  -5.346  1.00128.43           C  
ANISOU 5576  CG2 VAL B1050    25120  11971  11708   4206   1213   -803       C  
ATOM   5577  N   LEU B1051     -18.408  23.532  -8.626  1.00117.55           N  
ANISOU 5577  N   LEU B1051    22740  11865  10058   4951    883    -94       N  
ATOM   5578  CA  LEU B1051     -18.397  22.414  -9.574  1.00114.10           C  
ANISOU 5578  CA  LEU B1051    21954  11821   9578   4934    798     71       C  
ATOM   5579  C   LEU B1051     -19.167  22.718 -10.870  1.00120.61           C  
ANISOU 5579  C   LEU B1051    23086  12604  10135   5564    691    233       C  
ATOM   5580  O   LEU B1051     -18.623  22.462 -11.946  1.00120.44           O  
ANISOU 5580  O   LEU B1051    23238  12503  10022   5485    761    471       O  
ATOM   5581  CB  LEU B1051     -18.866  21.095  -8.927  1.00109.85           C  
ANISOU 5581  CB  LEU B1051    20655  11947   9136   4803    641   -103       C  
ATOM   5582  CG  LEU B1051     -18.795  19.824  -9.803  1.00111.33           C  
ANISOU 5582  CG  LEU B1051    20469  12509   9322   4707    560     10       C  
ATOM   5583  CD1 LEU B1051     -17.377  19.528 -10.264  1.00109.92           C  
ANISOU 5583  CD1 LEU B1051    20406  12115   9243   4211    751    218       C  
ATOM   5584  CD2 LEU B1051     -19.332  18.644  -9.073  1.00110.06           C  
ANISOU 5584  CD2 LEU B1051    19643  12895   9280   4574    444   -164       C  
ATOM   5585  N   LEU B1052     -20.402  23.271 -10.780  1.00119.86           N  
ANISOU 5585  N   LEU B1052    23062  12588   9890   6216    522    103       N  
ATOM   5586  CA  LEU B1052     -21.207  23.644 -11.959  1.00123.41           C  
ANISOU 5586  CA  LEU B1052    23808  13040  10043   6916    363    244       C  
ATOM   5587  C   LEU B1052     -20.475  24.665 -12.846  1.00130.35           C  
ANISOU 5587  C   LEU B1052    25544  13212  10770   6985    582    580       C  
ATOM   5588  O   LEU B1052     -20.544  24.567 -14.076  1.00131.05           O  
ANISOU 5588  O   LEU B1052    25867  13327  10600   7277    525    813       O  
ATOM   5589  CB  LEU B1052     -22.600  24.185 -11.569  1.00127.01           C  
ANISOU 5589  CB  LEU B1052    24177  13688  10392   7635    160     30       C  
ATOM   5590  CG  LEU B1052     -23.619  23.207 -10.962  1.00129.20           C  
ANISOU 5590  CG  LEU B1052    23593  14739  10759   7715    -61   -276       C  
ATOM   5591  CD1 LEU B1052     -24.951  23.887 -10.751  1.00133.97           C  
ANISOU 5591  CD1 LEU B1052    24150  15517  11236   8498   -229   -459       C  
ATOM   5592  CD2 LEU B1052     -23.833  21.985 -11.835  1.00128.46           C  
ANISOU 5592  CD2 LEU B1052    23019  15178  10611   7640   -261   -252       C  
ATOM   5593  N   LYS B1053     -19.759  25.626 -12.211  1.00128.56           N  
ANISOU 5593  N   LYS B1053    25794  12357  10695   6683    845    595       N  
ATOM   5594  CA  LYS B1053     -18.952  26.641 -12.891  1.00132.52           C  
ANISOU 5594  CA  LYS B1053    27128  12096  11127   6598   1138    908       C  
ATOM   5595  C   LYS B1053     -17.670  26.016 -13.456  1.00134.35           C  
ANISOU 5595  C   LYS B1053    27281  12315  11451   5924   1362   1123       C  
ATOM   5596  O   LYS B1053     -17.207  26.448 -14.515  1.00137.30           O  
ANISOU 5596  O   LYS B1053    28213  12308  11648   5981   1567   1462       O  
ATOM   5597  CB  LYS B1053     -18.621  27.802 -11.947  1.00137.71           C  
ANISOU 5597  CB  LYS B1053    28259  12098  11968   6413   1340    777       C  
ATOM   5598  N   ALA B1054     -17.103  24.995 -12.755  1.00125.30           N  
ANISOU 5598  N   ALA B1054    25453  11594  10562   5325   1343    942       N  
ATOM   5599  CA  ALA B1054     -15.899  24.270 -13.184  1.00122.30           C  
ANISOU 5599  CA  ALA B1054    24870  11297  10300   4720   1538   1100       C  
ATOM   5600  C   ALA B1054     -16.200  23.401 -14.394  1.00124.61           C  
ANISOU 5600  C   ALA B1054    25016  11990  10339   5016   1425   1260       C  
ATOM   5601  O   ALA B1054     -15.328  23.241 -15.249  1.00125.30           O  
ANISOU 5601  O   ALA B1054    25289  11951  10369   4769   1662   1507       O  
ATOM   5602  CB  ALA B1054     -15.354  23.415 -12.056  1.00118.29           C  
ANISOU 5602  CB  ALA B1054    23684  11159  10100   4143   1494    858       C  
ATOM   5603  N   ILE B1055     -17.437  22.850 -14.472  1.00119.21           N  
ANISOU 5603  N   ILE B1055    23988  11806   9499   5537   1074   1095       N  
ATOM   5604  CA  ILE B1055     -17.916  22.044 -15.604  1.00118.51           C  
ANISOU 5604  CA  ILE B1055    23750  12139   9138   5876    886   1162       C  
ATOM   5605  C   ILE B1055     -17.977  22.942 -16.868  1.00128.10           C  
ANISOU 5605  C   ILE B1055    25746  12967   9959   6358    981   1494       C  
ATOM   5606  O   ILE B1055     -17.627  22.483 -17.953  1.00128.81           O  
ANISOU 5606  O   ILE B1055    25953  13170   9817   6380   1040   1675       O  
ATOM   5607  CB  ILE B1055     -19.270  21.333 -15.271  1.00119.55           C  
ANISOU 5607  CB  ILE B1055    23285  12895   9244   6264    481    853       C  
ATOM   5608  CG1 ILE B1055     -19.051  20.176 -14.276  1.00113.72           C  
ANISOU 5608  CG1 ILE B1055    21810  12553   8844   5726    452    614       C  
ATOM   5609  CG2 ILE B1055     -19.999  20.827 -16.537  1.00121.81           C  
ANISOU 5609  CG2 ILE B1055    23543  13564   9176   6763    216    879       C  
ATOM   5610  CD1 ILE B1055     -20.262  19.823 -13.425  1.00117.10           C  
ANISOU 5610  CD1 ILE B1055    21700  13430   9361   5952    191    304       C  
ATOM   5611  N   GLU B1056     -18.361  24.226 -16.698  1.00128.25           N  
ANISOU 5611  N   GLU B1056    26342  12496   9893   6737   1027   1582       N  
ATOM   5612  CA  GLU B1056     -18.453  25.224 -17.762  1.00134.23           C  
ANISOU 5612  CA  GLU B1056    27946  12783  10273   7244   1142   1939       C  
ATOM   5613  C   GLU B1056     -17.107  25.521 -18.447  1.00140.11           C  
ANISOU 5613  C   GLU B1056    29205  13034  10995   6755   1615   2303       C  
ATOM   5614  O   GLU B1056     -17.102  25.856 -19.638  1.00144.86           O  
ANISOU 5614  O   GLU B1056    30384  13463  11193   7128   1712   2639       O  
ATOM   5615  CB  GLU B1056     -19.088  26.520 -17.241  1.00140.19           C  
ANISOU 5615  CB  GLU B1056    29208  13042  11018   7710   1127   1929       C  
ATOM   5616  CG  GLU B1056     -20.599  26.454 -17.095  1.00150.48           C  
ANISOU 5616  CG  GLU B1056    30199  14822  12154   8501    672   1692       C  
ATOM   5617  CD  GLU B1056     -21.318  27.791 -17.027  1.00174.53           C  
ANISOU 5617  CD  GLU B1056    33826  17396  15092   9168    637   1773       C  
ATOM   5618  OE1 GLU B1056     -20.739  28.818 -17.450  1.00170.40           O1-
ANISOU 5618  OE1 GLU B1056    34056  16142  14546   9110    939   2104       O1-
ATOM   5619  OE2 GLU B1056     -22.479  27.806 -16.561  1.00168.03           O  
ANISOU 5619  OE2 GLU B1056    32717  16928  14197   9785    323   1505       O  
ATOM   5620  N   ILE B1057     -15.979  25.415 -17.704  1.00132.66           N  
ANISOU 5620  N   ILE B1057    28048  11895  10463   5940   1911   2239       N  
ATOM   5621  CA  ILE B1057     -14.625  25.652 -18.240  1.00134.03           C  
ANISOU 5621  CA  ILE B1057    28567  11661  10697   5374   2397   2539       C  
ATOM   5622  C   ILE B1057     -14.185  24.420 -19.053  1.00135.21           C  
ANISOU 5622  C   ILE B1057    28309  12349  10718   5224   2412   2595       C  
ATOM   5623  O   ILE B1057     -13.594  24.547 -20.135  1.00137.87           O  
ANISOU 5623  O   ILE B1057    29075  12510  10800   5208   2720   2927       O  
ATOM   5624  CB  ILE B1057     -13.614  26.038 -17.112  1.00135.84           C  
ANISOU 5624  CB  ILE B1057    28658  11534  11422   4578   2661   2398       C  
ATOM   5625  CG1 ILE B1057     -14.100  27.290 -16.346  1.00140.04           C  
ANISOU 5625  CG1 ILE B1057    29674  11488  12047   4767   2645   2299       C  
ATOM   5626  CG2 ILE B1057     -12.192  26.262 -17.664  1.00138.65           C  
ANISOU 5626  CG2 ILE B1057    29264  11529  11886   3941   3182   2683       C  
ATOM   5627  CD1 ILE B1057     -13.656  27.384 -14.919  1.00146.00           C  
ANISOU 5627  CD1 ILE B1057    30052  12188  13234   4187   2638   1946       C  
ATOM   5628  N   LEU B1058     -14.511  23.230 -18.527  1.00125.92           N  
ANISOU 5628  N   LEU B1058    26337  11808   9699   5138   2097   2267       N  
ATOM   5629  CA  LEU B1058     -14.203  21.944 -19.140  1.00122.13           C  
ANISOU 5629  CA  LEU B1058    25413  11845   9145   5015   2060   2230       C  
ATOM   5630  C   LEU B1058     -15.036  21.698 -20.406  1.00128.58           C  
ANISOU 5630  C   LEU B1058    26489  12932   9434   5691   1837   2325       C  
ATOM   5631  O   LEU B1058     -14.473  21.253 -21.408  1.00128.81           O  
ANISOU 5631  O   LEU B1058    26655  13059   9227   5646   2027   2494       O  
ATOM   5632  CB  LEU B1058     -14.378  20.800 -18.123  1.00115.55           C  
ANISOU 5632  CB  LEU B1058    23728  11524   8653   4738   1795   1859       C  
ATOM   5633  CG  LEU B1058     -13.450  20.822 -16.907  1.00116.57           C  
ANISOU 5633  CG  LEU B1058    23524  11517   9250   4069   1974   1751       C  
ATOM   5634  CD1 LEU B1058     -14.104  20.156 -15.728  1.00112.42           C  
ANISOU 5634  CD1 LEU B1058    22380  11381   8953   4038   1647   1413       C  
ATOM   5635  CD2 LEU B1058     -12.102  20.190 -17.212  1.00116.27           C  
ANISOU 5635  CD2 LEU B1058    23265  11541   9371   3537   2292   1862       C  
ATOM   5636  N   SER B1059     -16.360  22.027 -20.372  1.00127.21           N  
ANISOU 5636  N   SER B1059    26385  12897   9051   6338   1438   2207       N  
ATOM   5637  CA  SER B1059     -17.298  21.873 -21.498  1.00130.97           C  
ANISOU 5637  CA  SER B1059    27067  13695   9002   7056   1125   2246       C  
ATOM   5638  C   SER B1059     -16.828  22.626 -22.748  1.00142.58           C  
ANISOU 5638  C   SER B1059    29402  14768  10003   7320   1429   2701       C  
ATOM   5639  O   SER B1059     -17.161  22.228 -23.867  1.00144.69           O  
ANISOU 5639  O   SER B1059    29829  15356   9791   7742   1270   2766       O  
ATOM   5640  CB  SER B1059     -18.710  22.303 -21.110  1.00135.43           C  
ANISOU 5640  CB  SER B1059    27545  14431   9480   7695    685   2054       C  
ATOM   5641  OG  SER B1059     -18.807  23.704 -20.920  1.00147.63           O  
ANISOU 5641  OG  SER B1059    29758  15365  10970   7984    838   2287       O  
ATOM   5642  N   SER B1060     -16.017  23.690 -22.539  1.00142.74           N  
ANISOU 5642  N   SER B1060    29985  14089  10162   7026   1886   3006       N  
ATOM   5643  CA  SER B1060     -15.396  24.512 -23.575  1.00149.00           C  
ANISOU 5643  CA  SER B1060    31652  14372  10590   7127   2316   3497       C  
ATOM   5644  C   SER B1060     -13.973  23.982 -23.930  1.00151.91           C  
ANISOU 5644  C   SER B1060    31910  14714  11095   6412   2819   3637       C  
ATOM   5645  O   SER B1060     -13.121  24.756 -24.383  1.00156.22           O  
ANISOU 5645  O   SER B1060    33068  14717  11573   6170   3344   4025       O  
ATOM   5646  CB  SER B1060     -15.352  25.974 -23.129  1.00157.16           C  
ANISOU 5646  CB  SER B1060    33365  14610  11740   7173   2557   3727       C  
ATOM   5647  OG  SER B1060     -16.653  26.506 -22.932  1.00167.51           O  
ANISOU 5647  OG  SER B1060    34714  15989  12944   7865   2099   3620       O  
ATOM   5648  N   LYS B1061     -13.735  22.656 -23.733  1.00142.56           N  
ANISOU 5648  N   LYS B1061    29944  14114  10109   6093   2677   3323       N  
ATOM   5649  CA  LYS B1061     -12.471  21.961 -24.033  1.00140.43           C  
ANISOU 5649  CA  LYS B1061    29429  13947   9981   5504   3090   3385       C  
ATOM   5650  C   LYS B1061     -12.700  20.519 -24.534  1.00140.12           C  
ANISOU 5650  C   LYS B1061    28873  14589   9777   5640   2819   3116       C  
ATOM   5651  O   LYS B1061     -13.620  19.840 -24.063  1.00135.73           O  
ANISOU 5651  O   LYS B1061    27815  14445   9311   5846   2319   2756       O  
ATOM   5652  CB  LYS B1061     -11.515  21.977 -22.827  1.00139.00           C  
ANISOU 5652  CB  LYS B1061    28779  13577  10457   4716   3331   3258       C  
ATOM   5653  CG  LYS B1061     -10.056  22.000 -23.256  1.00150.64           C  
ANISOU 5653  CG  LYS B1061    30328  14863  12043   4141   3943   3505       C  
ATOM   5654  CD  LYS B1061      -9.078  21.694 -22.140  1.00152.28           C  
ANISOU 5654  CD  LYS B1061    29882  15100  12878   3389   4091   3305       C  
ATOM   5655  CE  LYS B1061      -7.662  21.791 -22.662  1.00162.09           C  
ANISOU 5655  CE  LYS B1061    31176  16193  14216   2859   4715   3556       C  
ATOM   5656  NZ  LYS B1061      -6.691  21.046 -21.821  1.00164.72           N  
ANISOU 5656  NZ  LYS B1061    30696  16816  15074   2248   4784   3320       N  
ATOM   5657  N   LYS B1062     -11.845  20.053 -25.480  1.00137.78           N  
ANISOU 5657  N   LYS B1062    28703  14393   9253   5499   3184   3280       N  
ATOM   5658  CA  LYS B1062     -11.898  18.717 -26.097  1.00135.16           C  
ANISOU 5658  CA  LYS B1062    28000  14624   8730   5611   3018   3035       C  
ATOM   5659  C   LYS B1062     -11.712  17.544 -25.096  1.00132.18           C  
ANISOU 5659  C   LYS B1062    26735  14578   8911   5179   2832   2630       C  
ATOM   5660  O   LYS B1062     -11.813  16.373 -25.480  1.00130.71           O  
ANISOU 5660  O   LYS B1062    26219  14808   8639   5248   2670   2377       O  
ATOM   5661  CB  LYS B1062     -10.887  18.627 -27.254  1.00141.16           C  
ANISOU 5661  CB  LYS B1062    29148  15346   9141   5530   3556   3326       C  
ATOM   5662  N   GLU B1063     -11.472  17.869 -23.814  1.00124.20           N  
ANISOU 5662  N   GLU B1063    25387  13362   8442   4761   2847   2564       N  
ATOM   5663  CA  GLU B1063     -11.260  16.906 -22.737  1.00117.34           C  
ANISOU 5663  CA  GLU B1063    23748  12747   8089   4362   2696   2249       C  
ATOM   5664  C   GLU B1063     -12.562  16.461 -22.057  1.00115.82           C  
ANISOU 5664  C   GLU B1063    23183  12840   7983   4622   2132   1911       C  
ATOM   5665  O   GLU B1063     -12.616  15.341 -21.553  1.00111.57           O  
ANISOU 5665  O   GLU B1063    22070  12614   7707   4440   1959   1639       O  
ATOM   5666  CB  GLU B1063     -10.238  17.451 -21.727  1.00117.62           C  
ANISOU 5666  CB  GLU B1063    23602  12471   8615   3764   3011   2344       C  
ATOM   5667  CG  GLU B1063      -8.791  17.275 -22.175  1.00130.78           C  
ANISOU 5667  CG  GLU B1063    25225  14085  10382   3348   3543   2531       C  
ATOM   5668  CD  GLU B1063      -8.172  18.302 -23.112  1.00160.49           C  
ANISOU 5668  CD  GLU B1063    29653  17460  13864   3318   4046   2929       C  
ATOM   5669  OE1 GLU B1063      -8.894  18.884 -23.954  1.00166.15           O  
ANISOU 5669  OE1 GLU B1063    31005  18032  14093   3806   3990   3109       O  
ATOM   5670  OE2 GLU B1063      -6.942  18.512 -23.011  1.00154.99           O1-
ANISOU 5670  OE2 GLU B1063    28834  16621  13434   2804   4511   3070       O1-
ATOM   5671  N   PHE B1064     -13.618  17.309 -22.086  1.00113.06           N  
ANISOU 5671  N   PHE B1064    23164  12391   7404   5069   1867   1937       N  
ATOM   5672  CA  PHE B1064     -14.946  17.030 -21.518  1.00110.55           C  
ANISOU 5672  CA  PHE B1064    22497  12374   7135   5369   1358   1628       C  
ATOM   5673  C   PHE B1064     -15.578  15.754 -22.077  1.00111.61           C  
ANISOU 5673  C   PHE B1064    22269  13023   7113   5556   1031   1329       C  
ATOM   5674  O   PHE B1064     -16.351  15.103 -21.373  1.00107.80           O  
ANISOU 5674  O   PHE B1064    21259  12836   6864   5526    708   1017       O  
ATOM   5675  CB  PHE B1064     -15.888  18.226 -21.724  1.00116.78           C  
ANISOU 5675  CB  PHE B1064    23779  12974   7620   5928   1174   1749       C  
ATOM   5676  CG  PHE B1064     -17.165  18.210 -20.912  1.00117.27           C  
ANISOU 5676  CG  PHE B1064    23453  13292   7814   6199    733   1453       C  
ATOM   5677  CD1 PHE B1064     -17.172  18.630 -19.587  1.00118.08           C  
ANISOU 5677  CD1 PHE B1064    23333  13213   8319   5937    768   1369       C  
ATOM   5678  CD2 PHE B1064     -18.372  17.833 -21.488  1.00121.50           C  
ANISOU 5678  CD2 PHE B1064    23848  14272   8044   6731    288   1245       C  
ATOM   5679  CE1 PHE B1064     -18.356  18.630 -18.841  1.00118.43           C  
ANISOU 5679  CE1 PHE B1064    23014  13520   8464   6204    416   1100       C  
ATOM   5680  CE2 PHE B1064     -19.560  17.852 -20.746  1.00123.75           C  
ANISOU 5680  CE2 PHE B1064    23719  14831   8467   6978    -82    969       C  
ATOM   5681  CZ  PHE B1064     -19.542  18.240 -19.425  1.00119.28           C  
ANISOU 5681  CZ  PHE B1064    22935  14080   8304   6716     10    909       C  
ATOM   5682  N   GLN B1065     -15.240  15.408 -23.337  1.00110.61           N  
ANISOU 5682  N   GLN B1065    22447  12993   6588   5726   1141   1414       N  
ATOM   5683  CA  GLN B1065     -15.671  14.214 -24.069  1.00110.66           C  
ANISOU 5683  CA  GLN B1065    22225  13437   6386   5882    881   1116       C  
ATOM   5684  C   GLN B1065     -15.415  12.947 -23.247  1.00110.06           C  
ANISOU 5684  C   GLN B1065    21477  13531   6811   5412    855    825       C  
ATOM   5685  O   GLN B1065     -16.312  12.121 -23.065  1.00108.95           O  
ANISOU 5685  O   GLN B1065    20928  13716   6754   5468    481    474       O  
ATOM   5686  CB  GLN B1065     -14.834  14.080 -25.346  1.00115.70           C  
ANISOU 5686  CB  GLN B1065    23320  14037   6605   5962   1206   1307       C  
ATOM   5687  CG  GLN B1065     -15.207  14.984 -26.495  1.00141.38           C  
ANISOU 5687  CG  GLN B1065    27286  17237   9197   6531   1178   1560       C  
ATOM   5688  CD  GLN B1065     -14.357  14.609 -27.687  1.00170.10           C  
ANISOU 5688  CD  GLN B1065    31291  20913  12428   6557   1526   1694       C  
ATOM   5689  OE1 GLN B1065     -13.217  15.065 -27.838  1.00166.99           O  
ANISOU 5689  OE1 GLN B1065    31184  20196  12069   6288   2082   2038       O  
ATOM   5690  NE2 GLN B1065     -14.882  13.746 -28.550  1.00168.11           N  
ANISOU 5690  NE2 GLN B1065    31011  21076  11788   6858   1221   1395       N  
ATOM   5691  N   GLU B1066     -14.165  12.809 -22.774  1.00104.03           N  
ANISOU 5691  N   GLU B1066    20608  12542   6376   4951   1266    985       N  
ATOM   5692  CA  GLU B1066     -13.634  11.694 -21.999  1.00 99.47           C  
ANISOU 5692  CA  GLU B1066    19485  12051   6260   4523   1332    813       C  
ATOM   5693  C   GLU B1066     -14.289  11.541 -20.624  1.00 98.68           C  
ANISOU 5693  C   GLU B1066    18910  12015   6568   4344   1081    643       C  
ATOM   5694  O   GLU B1066     -14.659  10.428 -20.260  1.00 96.20           O  
ANISOU 5694  O   GLU B1066    18177  11908   6466   4220    903    381       O  
ATOM   5695  CB  GLU B1066     -12.106  11.819 -21.901  1.00100.78           C  
ANISOU 5695  CB  GLU B1066    19686  11987   6617   4159   1831   1069       C  
ATOM   5696  CG  GLU B1066     -11.434  11.792 -23.270  1.00119.18           C  
ANISOU 5696  CG  GLU B1066    22431  14307   8544   4317   2143   1218       C  
ATOM   5697  CD  GLU B1066      -9.932  11.994 -23.311  1.00143.01           C  
ANISOU 5697  CD  GLU B1066    25466  17145  11725   3974   2685   1477       C  
ATOM   5698  OE1 GLU B1066      -9.199  11.134 -22.769  1.00137.90           O  
ANISOU 5698  OE1 GLU B1066    24359  16583  11453   3681   2802   1380       O  
ATOM   5699  OE2 GLU B1066      -9.486  13.001 -23.909  1.00137.16           O1-
ANISOU 5699  OE2 GLU B1066    25196  16184  10735   4010   3005   1784       O1-
ATOM   5700  N   MET B1067     -14.459  12.661 -19.885  1.00 94.61           N  
ANISOU 5700  N   MET B1067    18502  11303   6143   4338   1087    786       N  
ATOM   5701  CA  MET B1067     -15.077  12.760 -18.550  1.00 90.97           C  
ANISOU 5701  CA  MET B1067    17675  10891   6001   4212    895    654       C  
ATOM   5702  C   MET B1067     -16.559  12.431 -18.561  1.00 94.36           C  
ANISOU 5702  C   MET B1067    17878  11641   6333   4523    479    372       C  
ATOM   5703  O   MET B1067     -17.248  12.738 -19.532  1.00 97.48           O  
ANISOU 5703  O   MET B1067    18536  12153   6350   4951    287    336       O  
ATOM   5704  CB  MET B1067     -14.958  14.201 -18.034  1.00 94.25           C  
ANISOU 5704  CB  MET B1067    18407  10981   6421   4236   1010    852       C  
ATOM   5705  CG  MET B1067     -13.656  14.504 -17.360  1.00 96.43           C  
ANISOU 5705  CG  MET B1067    18659  10994   6986   3767   1348   1022       C  
ATOM   5706  SD  MET B1067     -12.884  16.064 -17.843  1.00104.63           S  
ANISOU 5706  SD  MET B1067    20359  11528   7866   3745   1702   1358       S  
ATOM   5707  CE  MET B1067     -14.268  17.137 -17.842  1.00104.12           C  
ANISOU 5707  CE  MET B1067    20668  11347   7546   4283   1424   1330       C  
ATOM   5708  N   ARG B1068     -17.053  11.872 -17.450  1.00 87.34           N  
ANISOU 5708  N   ARG B1068    16500  10914   5773   4316    347    185       N  
ATOM   5709  CA  ARG B1068     -18.468  11.571 -17.199  1.00 87.82           C  
ANISOU 5709  CA  ARG B1068    16220  11307   5841   4514      0    -98       C  
ATOM   5710  C   ARG B1068     -18.811  12.167 -15.812  1.00 90.19           C  
ANISOU 5710  C   ARG B1068    16322  11568   6378   4422     10    -92       C  
ATOM   5711  O   ARG B1068     -17.949  12.151 -14.923  1.00 87.13           O  
ANISOU 5711  O   ARG B1068    15874  10997   6235   4064    233     32       O  
ATOM   5712  CB  ARG B1068     -18.738  10.053 -17.205  1.00 86.57           C  
ANISOU 5712  CB  ARG B1068    15626  11395   5874   4273   -105   -359       C  
ATOM   5713  CG  ARG B1068     -18.154   9.258 -18.376  1.00 95.59           C  
ANISOU 5713  CG  ARG B1068    16941  12526   6851   4263    -46   -399       C  
ATOM   5714  CD  ARG B1068     -18.832   9.508 -19.709  1.00106.08           C  
ANISOU 5714  CD  ARG B1068    18534  14049   7722   4708   -300   -524       C  
ATOM   5715  NE  ARG B1068     -17.979   9.093 -20.822  1.00106.93           N  
ANISOU 5715  NE  ARG B1068    18974  14068   7588   4734   -135   -469       N  
ATOM   5716  CZ  ARG B1068     -18.205   9.398 -22.095  1.00127.00           C  
ANISOU 5716  CZ  ARG B1068    21896  16722   9635   5130   -262   -489       C  
ATOM   5717  NH1 ARG B1068     -19.264  10.126 -22.434  1.00117.95           N  
ANISOU 5717  NH1 ARG B1068    20840  15785   8190   5565   -594   -553       N  
ATOM   5718  NH2 ARG B1068     -17.376   8.979 -23.040  1.00118.66           N1+
ANISOU 5718  NH2 ARG B1068    21139  15595   8351   5136    -57   -442       N1+
ATOM   5719  N   PHE B1069     -20.047  12.696 -15.622  1.00 87.62           N  
ANISOU 5719  N   PHE B1069    15887  11446   5959   4770   -235   -242       N  
ATOM   5720  CA  PHE B1069     -20.429  13.304 -14.336  1.00 85.68           C  
ANISOU 5720  CA  PHE B1069    15484  11180   5890   4742   -205   -266       C  
ATOM   5721  C   PHE B1069     -21.719  12.767 -13.725  1.00 90.64           C  
ANISOU 5721  C   PHE B1069    15555  12232   6653   4796   -411   -552       C  
ATOM   5722  O   PHE B1069     -22.740  12.671 -14.410  1.00 93.43           O  
ANISOU 5722  O   PHE B1069    15752  12896   6850   5132   -683   -743       O  
ATOM   5723  CB  PHE B1069     -20.496  14.837 -14.441  1.00 89.35           C  
ANISOU 5723  CB  PHE B1069    16445  11362   6141   5127   -179   -116       C  
ATOM   5724  CG  PHE B1069     -19.155  15.485 -14.673  1.00 90.02           C  
ANISOU 5724  CG  PHE B1069    17040  10972   6193   4931    117    176       C  
ATOM   5725  CD1 PHE B1069     -18.678  15.692 -15.963  1.00 93.42           C  
ANISOU 5725  CD1 PHE B1069    17907  11241   6349   5093    184    359       C  
ATOM   5726  CD2 PHE B1069     -18.367  15.888 -13.603  1.00 91.23           C  
ANISOU 5726  CD2 PHE B1069    17222  10865   6576   4566    336    254       C  
ATOM   5727  CE1 PHE B1069     -17.434  16.286 -16.178  1.00 96.42           C  
ANISOU 5727  CE1 PHE B1069    18715  11195   6724   4860    512    632       C  
ATOM   5728  CE2 PHE B1069     -17.116  16.475 -13.819  1.00 92.54           C  
ANISOU 5728  CE2 PHE B1069    17787  10623   6753   4320    612    488       C  
ATOM   5729  CZ  PHE B1069     -16.664  16.681 -15.106  1.00 93.28           C  
ANISOU 5729  CZ  PHE B1069    18286  10546   6610   4455    722    685       C  
ATOM   5730  N   ILE B1070     -21.658  12.430 -12.416  1.00 85.79           N  
ANISOU 5730  N   ILE B1070    14627  11654   6314   4458   -273   -580       N  
ATOM   5731  CA  ILE B1070     -22.791  11.954 -11.609  1.00 86.91           C  
ANISOU 5731  CA  ILE B1070    14230  12174   6616   4426   -359   -810       C  
ATOM   5732  C   ILE B1070     -22.980  12.968 -10.471  1.00 92.97           C  
ANISOU 5732  C   ILE B1070    15061  12872   7391   4548   -254   -783       C  
ATOM   5733  O   ILE B1070     -22.505  12.741  -9.362  1.00 90.34           O  
ANISOU 5733  O   ILE B1070    14632  12474   7217   4211    -65   -721       O  
ATOM   5734  CB  ILE B1070     -22.621  10.488 -11.064  1.00 87.60           C  
ANISOU 5734  CB  ILE B1070    13913  12377   6993   3913   -250   -861       C  
ATOM   5735  CG1 ILE B1070     -21.872   9.534 -12.034  1.00 86.51           C  
ANISOU 5735  CG1 ILE B1070    13889  12109   6873   3711   -244   -823       C  
ATOM   5736  CG2 ILE B1070     -23.959   9.889 -10.633  1.00 90.70           C  
ANISOU 5736  CG2 ILE B1070    13739  13196   7528   3882   -348  -1126       C  
ATOM   5737  CD1 ILE B1070     -22.517   9.220 -13.417  1.00 95.54           C  
ANISOU 5737  CD1 ILE B1070    15013  13450   7837   3955   -511  -1034       C  
ATOM   5738  N   ILE B1071     -23.633  14.099 -10.749  1.00 95.49           N  
ANISOU 5738  N   ILE B1071    15582  13190   7509   5062   -379   -831       N  
ATOM   5739  CA  ILE B1071     -23.821  15.117  -9.716  1.00 98.19           C  
ANISOU 5739  CA  ILE B1071    16047  13421   7841   5224   -270   -843       C  
ATOM   5740  C   ILE B1071     -25.147  14.911  -8.968  1.00106.38           C  
ANISOU 5740  C   ILE B1071    16528  14934   8957   5383   -329  -1099       C  
ATOM   5741  O   ILE B1071     -26.200  14.790  -9.598  1.00108.59           O  
ANISOU 5741  O   ILE B1071    16509  15573   9176   5721   -552  -1275       O  
ATOM   5742  CB  ILE B1071     -23.617  16.567 -10.227  1.00104.72           C  
ANISOU 5742  CB  ILE B1071    17505  13850   8435   5671   -287   -720       C  
ATOM   5743  CG1 ILE B1071     -24.475  16.886 -11.466  1.00109.67           C  
ANISOU 5743  CG1 ILE B1071    18211  14641   8816   6260   -561   -766       C  
ATOM   5744  CG2 ILE B1071     -22.136  16.823 -10.508  1.00104.16           C  
ANISOU 5744  CG2 ILE B1071    17935  13277   8363   5339    -96   -459       C  
ATOM   5745  CD1 ILE B1071     -24.797  18.350 -11.615  1.00123.29           C  
ANISOU 5745  CD1 ILE B1071    20440  16078  10325   6855   -592   -703       C  
ATOM   5746  N   ILE B1072     -25.069  14.815  -7.617  1.00103.60           N  
ANISOU 5746  N   ILE B1072    16005  14625   8732   5116   -120  -1125       N  
ATOM   5747  CA  ILE B1072     -26.218  14.589  -6.724  1.00106.53           C  
ANISOU 5747  CA  ILE B1072    15845  15448   9182   5191    -71  -1340       C  
ATOM   5748  C   ILE B1072     -26.422  15.758  -5.729  1.00115.80           C  
ANISOU 5748  C   ILE B1072    17232  16524  10243   5486     58  -1407       C  
ATOM   5749  O   ILE B1072     -25.649  15.913  -4.777  1.00113.98           O  
ANISOU 5749  O   ILE B1072    17218  16073  10017   5198    249  -1325       O  
ATOM   5750  CB  ILE B1072     -26.146  13.205  -6.011  1.00107.21           C  
ANISOU 5750  CB  ILE B1072    15485  15759   9491   4615     94  -1328       C  
ATOM   5751  CG1 ILE B1072     -25.993  12.048  -7.017  1.00105.96           C  
ANISOU 5751  CG1 ILE B1072    15154  15647   9457   4345    -30  -1312       C  
ATOM   5752  CG2 ILE B1072     -27.358  12.982  -5.097  1.00110.74           C  
ANISOU 5752  CG2 ILE B1072    15378  16685  10014   4661    211  -1530       C  
ATOM   5753  CD1 ILE B1072     -24.644  11.426  -7.044  1.00105.29           C  
ANISOU 5753  CD1 ILE B1072    15347  15211   9447   3917     83  -1078       C  
ATOM   5754  N   GLY B1073     -27.476  16.543  -5.969  1.00118.34           N  
ANISOU 5754  N   GLY B1073    17478  17033  10453   6084    -65  -1579       N  
ATOM   5755  CA  GLY B1073     -27.846  17.704  -5.164  1.00121.62           C  
ANISOU 5755  CA  GLY B1073    18104  17359  10748   6491     41  -1694       C  
ATOM   5756  C   GLY B1073     -29.338  17.961  -5.151  1.00131.50           C  
ANISOU 5756  C   GLY B1073    18877  19116  11969   7053    -49  -1949       C  
ATOM   5757  O   GLY B1073     -30.014  17.748  -6.162  1.00133.17           O  
ANISOU 5757  O   GLY B1073    18821  19606  12171   7344   -306  -2015       O  
ATOM   5758  N   LYS B1074     -29.856  18.422  -3.995  1.00131.00           N  
ANISOU 5758  N   LYS B1074    18687  19213  11875   7225    158  -2116       N  
ATOM   5759  CA  LYS B1074     -31.273  18.716  -3.763  1.00136.38           C  
ANISOU 5759  CA  LYS B1074    18854  20423  12540   7774    146  -2385       C  
ATOM   5760  C   LYS B1074     -31.406  19.969  -2.884  1.00143.89           C  
ANISOU 5760  C   LYS B1074    20198  21147  13328   8236    322  -2510       C  
ATOM   5761  O   LYS B1074     -30.607  20.164  -1.970  1.00141.01           O  
ANISOU 5761  O   LYS B1074    20207  20458  12912   7902    540  -2464       O  
ATOM   5762  CB  LYS B1074     -31.941  17.509  -3.077  1.00139.11           C  
ANISOU 5762  CB  LYS B1074    18388  21392  13077   7339    328  -2504       C  
ATOM   5763  CG  LYS B1074     -33.452  17.401  -3.273  1.00159.71           C  
ANISOU 5763  CG  LYS B1074    20225  24697  15761   7765    243  -2782       C  
ATOM   5764  CD  LYS B1074     -34.036  16.265  -2.423  1.00168.09           C  
ANISOU 5764  CD  LYS B1074    20536  26305  17026   7239    532  -2880       C  
ATOM   5765  CE  LYS B1074     -35.225  15.593  -3.069  1.00178.96           C  
ANISOU 5765  CE  LYS B1074    21054  28343  18599   7296    361  -3107       C  
ATOM   5766  NZ  LYS B1074     -35.612  14.348  -2.352  1.00184.60           N1+
ANISOU 5766  NZ  LYS B1074    21121  29461  19558   6617    677  -3145       N1+
ATOM   5767  N   GLY B1075     -32.411  20.798  -3.166  1.00146.86           N  
ANISOU 5767  N   GLY B1075    20486  21703  13611   9022    208  -2690       N  
ATOM   5768  CA  GLY B1075     -32.660  22.018  -2.405  1.00151.10           C  
ANISOU 5768  CA  GLY B1075    21404  22013  13994   9565    372  -2851       C  
ATOM   5769  C   GLY B1075     -33.289  23.146  -3.195  1.00161.76           C  
ANISOU 5769  C   GLY B1075    23047  23207  15209  10496    149  -2908       C  
ATOM   5770  O   GLY B1075     -34.443  23.031  -3.624  1.00165.88           O  
ANISOU 5770  O   GLY B1075    22963  24314  15751  11010    -18  -3062       O  
ATOM   5771  N   ASP B1076     -32.534  24.264  -3.364  1.00159.34           N  
ANISOU 5771  N   ASP B1076    23677  22099  14765  10725    153  -2788       N  
ATOM   5772  CA  ASP B1076     -32.981  25.466  -4.083  1.00164.72           C  
ANISOU 5772  CA  ASP B1076    24851  22447  15288  11639    -20  -2778       C  
ATOM   5773  C   ASP B1076     -32.952  25.279  -5.608  1.00167.28           C  
ANISOU 5773  C   ASP B1076    25256  22749  15552  11833   -378  -2532       C  
ATOM   5774  O   ASP B1076     -31.983  24.714  -6.126  1.00161.38           O  
ANISOU 5774  O   ASP B1076    24720  21748  14848  11201   -417  -2291       O  
ATOM   5775  CB  ASP B1076     -32.222  26.739  -3.635  1.00168.11           C  
ANISOU 5775  CB  ASP B1076    26293  21973  15611  11774    168  -2758       C  
ATOM   5776  CG  ASP B1076     -30.751  26.813  -4.004  1.00170.99           C  
ANISOU 5776  CG  ASP B1076    27373  21596  15998  11116    198  -2470       C  
ATOM   5777  OD1 ASP B1076     -30.443  27.265  -5.129  1.00171.34           O  
ANISOU 5777  OD1 ASP B1076    27938  21201  15963  11362     36  -2211       O  
ATOM   5778  OD2 ASP B1076     -29.906  26.460  -3.150  1.00172.65           O1-
ANISOU 5778  OD2 ASP B1076    27633  21678  16288  10381    395  -2502       O1-
ATOM   5779  N   PRO B1077     -34.003  25.740  -6.337  1.00169.19           N  
ANISOU 5779  N   PRO B1077    25324  23291  15669  12737   -646  -2596       N  
ATOM   5780  CA  PRO B1077     -34.043  25.533  -7.799  1.00169.27           C  
ANISOU 5780  CA  PRO B1077    25396  23368  15551  12974  -1024  -2381       C  
ATOM   5781  C   PRO B1077     -33.057  26.366  -8.635  1.00170.99           C  
ANISOU 5781  C   PRO B1077    26665  22658  15645  12985  -1035  -2000       C  
ATOM   5782  O   PRO B1077     -32.927  26.096  -9.833  1.00169.99           O  
ANISOU 5782  O   PRO B1077    26629  22565  15393  13037  -1299  -1784       O  
ATOM   5783  CB  PRO B1077     -35.505  25.846  -8.168  1.00173.66           C  
ANISOU 5783  CB  PRO B1077    25073  24283  16626  13013  -1147  -2436       C  
ATOM   5784  CG  PRO B1077     -36.249  25.935  -6.861  1.00178.12           C  
ANISOU 5784  CG  PRO B1077    24984  25059  17634  12674   -793  -2694       C  
ATOM   5785  CD  PRO B1077     -35.238  26.397  -5.869  1.00174.30           C  
ANISOU 5785  CD  PRO B1077    25405  24130  16690  12961   -534  -2787       C  
ATOM   5786  N   GLU B1078     -32.368  27.362  -8.017  1.00167.62           N  
ANISOU 5786  N   GLU B1078    27105  21441  15142  13063   -758  -1951       N  
ATOM   5787  CA  GLU B1078     -31.391  28.244  -8.677  1.00167.25           C  
ANISOU 5787  CA  GLU B1078    28127  20441  14979  13059   -686  -1606       C  
ATOM   5788  C   GLU B1078     -30.208  27.461  -9.268  1.00162.79           C  
ANISOU 5788  C   GLU B1078    27709  19698  14447  12212   -664  -1334       C  
ATOM   5789  O   GLU B1078     -29.950  27.544 -10.472  1.00162.89           O  
ANISOU 5789  O   GLU B1078    28103  19514  14272  12393   -823  -1039       O  
ATOM   5790  CB  GLU B1078     -30.907  29.345  -7.715  1.00169.05           C  
ANISOU 5790  CB  GLU B1078    28887  19888  15455  12771   -327  -1673       C  
ATOM   5791  N   LEU B1079     -29.514  26.683  -8.426  1.00152.42           N  
ANISOU 5791  N   LEU B1079    26066  18485  13360  11312   -463  -1430       N  
ATOM   5792  CA  LEU B1079     -28.394  25.855  -8.861  1.00145.78           C  
ANISOU 5792  CA  LEU B1079    25250  17537  12604  10488   -419  -1208       C  
ATOM   5793  C   LEU B1079     -28.925  24.578  -9.524  1.00147.27           C  
ANISOU 5793  C   LEU B1079    24653  18503  12800  10389   -684  -1241       C  
ATOM   5794  O   LEU B1079     -28.319  24.107 -10.486  1.00144.39           O  
ANISOU 5794  O   LEU B1079    24436  18057  12367  10123   -769  -1015       O  
ATOM   5795  CB  LEU B1079     -27.444  25.523  -7.691  1.00140.58           C  
ANISOU 5795  CB  LEU B1079    24546  16703  12166   9633   -134  -1296       C  
ATOM   5796  CG  LEU B1079     -26.773  26.695  -6.946  1.00146.52           C  
ANISOU 5796  CG  LEU B1079    26047  16687  12936   9556    122  -1333       C  
ATOM   5797  CD1 LEU B1079     -26.052  26.204  -5.730  1.00141.83           C  
ANISOU 5797  CD1 LEU B1079    25217  16158  12515   8786    313  -1491       C  
ATOM   5798  CD2 LEU B1079     -25.780  27.436  -7.823  1.00150.07           C  
ANISOU 5798  CD2 LEU B1079    27362  16332  13324   9449    210  -1008       C  
ATOM   5799  N   GLU B1080     -30.073  24.041  -9.024  1.00144.81           N  
ANISOU 5799  N   GLU B1080    23513  18938  12570  10604   -798  -1545       N  
ATOM   5800  CA  GLU B1080     -30.746  22.843  -9.552  1.00143.42           C  
ANISOU 5800  CA  GLU B1080    22514  19535  12444  10501  -1053  -1662       C  
ATOM   5801  C   GLU B1080     -31.138  23.000 -11.031  1.00151.30           C  
ANISOU 5801  C   GLU B1080    23669  20644  13174  11088  -1422  -1534       C  
ATOM   5802  O   GLU B1080     -31.067  22.036 -11.790  1.00148.25           O  
ANISOU 5802  O   GLU B1080    22959  20591  12778  10790  -1612  -1519       O  
ATOM   5803  CB  GLU B1080     -31.993  22.511  -8.728  1.00147.11           C  
ANISOU 5803  CB  GLU B1080    22121  20729  13046  10715  -1064  -2019       C  
ATOM   5804  CG  GLU B1080     -31.736  21.664  -7.500  1.00150.17           C  
ANISOU 5804  CG  GLU B1080    22046  21324  13688   9950   -767  -2145       C  
ATOM   5805  CD  GLU B1080     -33.006  21.306  -6.754  1.00169.87           C  
ANISOU 5805  CD  GLU B1080    23672  24567  16304  10143   -726  -2474       C  
ATOM   5806  OE1 GLU B1080     -33.746  22.234  -6.353  1.00163.14           O1-
ANISOU 5806  OE1 GLU B1080    22847  23780  15361  10830   -691  -2633       O1-
ATOM   5807  OE2 GLU B1080     -33.266  20.094  -6.573  1.00160.87           O  
ANISOU 5807  OE2 GLU B1080    21828  23938  15358   9607   -703  -2573       O  
ATOM   5808  N   GLY B1081     -31.571  24.205 -11.403  1.00154.89           N  
ANISOU 5808  N   GLY B1081    24638  20821  13391  11948  -1524  -1455       N  
ATOM   5809  CA  GLY B1081     -31.944  24.556 -12.768  1.00159.65           C  
ANISOU 5809  CA  GLY B1081    25529  21474  13655  12648  -1876  -1289       C  
ATOM   5810  C   GLY B1081     -30.710  24.650 -13.637  1.00161.39           C  
ANISOU 5810  C   GLY B1081    26552  21057  13713  12305  -1779   -897       C  
ATOM   5811  O   GLY B1081     -30.737  24.234 -14.798  1.00162.08           O  
ANISOU 5811  O   GLY B1081    26653  21369  13561  12439  -2046   -782       O  
ATOM   5812  N   TRP B1082     -29.605  25.172 -13.050  1.00155.10           N  
ANISOU 5812  N   TRP B1082    26393  19494  13043  11825  -1383   -719       N  
ATOM   5813  CA  TRP B1082     -28.287  25.317 -13.677  1.00152.44           C  
ANISOU 5813  CA  TRP B1082    26794  18499  12626  11369  -1178   -354       C  
ATOM   5814  C   TRP B1082     -27.692  23.930 -13.944  1.00148.06           C  
ANISOU 5814  C   TRP B1082    25747  18311  12199  10583  -1190   -371       C  
ATOM   5815  O   TRP B1082     -27.086  23.719 -14.992  1.00147.65           O  
ANISOU 5815  O   TRP B1082    26041  18108  11953  10476  -1214   -123       O  
ATOM   5816  CB  TRP B1082     -27.357  26.178 -12.785  1.00150.63           C  
ANISOU 5816  CB  TRP B1082    27195  17461  12577  10991   -766   -267       C  
ATOM   5817  CG  TRP B1082     -25.975  26.453 -13.323  1.00150.35           C  
ANISOU 5817  CG  TRP B1082    27895  16721  12512  10481   -495     90       C  
ATOM   5818  CD1 TRP B1082     -25.546  26.321 -14.613  1.00154.18           C  
ANISOU 5818  CD1 TRP B1082    28746  17094  12741  10533   -542    409       C  
ATOM   5819  CD2 TRP B1082     -24.867  26.995 -12.588  1.00148.72           C  
ANISOU 5819  CD2 TRP B1082    28158  15827  12524   9873   -119    150       C  
ATOM   5820  NE1 TRP B1082     -24.222  26.674 -14.711  1.00152.40           N  
ANISOU 5820  NE1 TRP B1082    29127  16185  12594   9948   -178    676       N  
ATOM   5821  CE2 TRP B1082     -23.784  27.111 -13.488  1.00152.46           C  
ANISOU 5821  CE2 TRP B1082    29198  15825  12907   9528     68    514       C  
ATOM   5822  CE3 TRP B1082     -24.680  27.387 -11.252  1.00149.27           C  
ANISOU 5822  CE3 TRP B1082    28209  15667  12840   9576     74    -93       C  
ATOM   5823  CZ2 TRP B1082     -22.530  27.598 -13.093  1.00150.91           C  
ANISOU 5823  CZ2 TRP B1082    29481  14951  12908   8861    438    631       C  
ATOM   5824  CZ3 TRP B1082     -23.433  27.851 -10.857  1.00149.80           C  
ANISOU 5824  CZ3 TRP B1082    28773  15070  13076   8922    394      0       C  
ATOM   5825  CH2 TRP B1082     -22.377  27.957 -11.772  1.00150.32           C  
ANISOU 5825  CH2 TRP B1082    29336  14684  13094   8557    571    355       C  
ATOM   5826  N   ALA B1083     -27.904  22.981 -13.021  1.00138.53           N  
ANISOU 5826  N   ALA B1083    23757  17584  11296  10078  -1161   -659       N  
ATOM   5827  CA  ALA B1083     -27.438  21.609 -13.170  1.00132.20           C  
ANISOU 5827  CA  ALA B1083    22463  17119  10649   9370  -1168   -704       C  
ATOM   5828  C   ALA B1083     -28.251  20.871 -14.252  1.00136.97           C  
ANISOU 5828  C   ALA B1083    22632  18344  11067   9685  -1564   -820       C  
ATOM   5829  O   ALA B1083     -27.653  20.292 -15.161  1.00134.40           O  
ANISOU 5829  O   ALA B1083    22456  17987  10621   9433  -1610   -685       O  
ATOM   5830  CB  ALA B1083     -27.529  20.880 -11.839  1.00128.93           C  
ANISOU 5830  CB  ALA B1083    21404  17001  10582   8821  -1011   -950       C  
ATOM   5831  N   ARG B1084     -29.604  20.924 -14.172  1.00137.58           N  
ANISOU 5831  N   ARG B1084    22168  18999  11107  10251  -1850  -1093       N  
ATOM   5832  CA  ARG B1084     -30.519  20.277 -15.122  1.00140.89           C  
ANISOU 5832  CA  ARG B1084    22074  20097  11359  10579  -2287  -1288       C  
ATOM   5833  C   ARG B1084     -30.305  20.773 -16.559  1.00148.69           C  
ANISOU 5833  C   ARG B1084    23727  20887  11881  11109  -2513  -1027       C  
ATOM   5834  O   ARG B1084     -30.412  19.978 -17.502  1.00147.83           O  
ANISOU 5834  O   ARG B1084    23405  21155  11608  11044  -2785  -1109       O  
ATOM   5835  CB  ARG B1084     -31.984  20.457 -14.687  1.00146.66           C  
ANISOU 5835  CB  ARG B1084    22109  21469  12147  11147  -2525  -1625       C  
ATOM   5836  CG  ARG B1084     -32.943  19.411 -15.268  1.00161.46           C  
ANISOU 5836  CG  ARG B1084    23117  24196  14036  11149  -2929  -1970       C  
ATOM   5837  CD  ARG B1084     -33.105  18.192 -14.371  1.00168.63           C  
ANISOU 5837  CD  ARG B1084    23204  25481  15387  10336  -2756  -2248       C  
ATOM   5838  NE  ARG B1084     -34.133  18.398 -13.350  1.00179.13           N  
ANISOU 5838  NE  ARG B1084    23883  27246  16934  10550  -2687  -2512       N  
ATOM   5839  CZ  ARG B1084     -35.368  17.909 -13.415  1.00191.68           C  
ANISOU 5839  CZ  ARG B1084    24506  29276  19049  10055  -2783  -2669       C  
ATOM   5840  NH1 ARG B1084     -35.742  17.163 -14.448  1.00181.43           N1+
ANISOU 5840  NH1 ARG B1084    22902  28795  17240  10687  -3357  -3073       N1+
ATOM   5841  NH2 ARG B1084     -36.236  18.151 -12.441  1.00184.31           N  
ANISOU 5841  NH2 ARG B1084    23048  28978  18003  10740  -2771  -3042       N  
ATOM   5842  N   SER B1085     -29.981  22.084 -16.713  1.00149.21           N  
ANISOU 5842  N   SER B1085    24644  20327  11721  11615  -2378   -711       N  
ATOM   5843  CA  SER B1085     -29.685  22.702 -18.010  1.00153.36           C  
ANISOU 5843  CA  SER B1085    25960  20543  11769  12135  -2501   -370       C  
ATOM   5844  C   SER B1085     -28.383  22.124 -18.554  1.00152.85           C  
ANISOU 5844  C   SER B1085    26270  20130  11674  11431  -2255   -134       C  
ATOM   5845  O   SER B1085     -28.312  21.844 -19.744  1.00154.58           O  
ANISOU 5845  O   SER B1085    26701  20507  11524  11632  -2458    -27       O  
ATOM   5846  CB  SER B1085     -29.639  24.229 -17.922  1.00161.43           C  
ANISOU 5846  CB  SER B1085    27830  20891  12613  12781  -2344    -77       C  
ATOM   5847  OG  SER B1085     -28.480  24.734 -17.278  1.00165.69           O  
ANISOU 5847  OG  SER B1085    28960  20624  13372  12219  -1845    149       O  
ATOM   5848  N   LEU B1086     -27.386  21.878 -17.673  1.00143.90           N  
ANISOU 5848  N   LEU B1086    25157  18601  10919  10621  -1837    -87       N  
ATOM   5849  CA  LEU B1086     -26.119  21.242 -18.047  1.00139.45           C  
ANISOU 5849  CA  LEU B1086    24817  17767  10402   9915  -1575     98       C  
ATOM   5850  C   LEU B1086     -26.357  19.761 -18.383  1.00140.16           C  
ANISOU 5850  C   LEU B1086    24191  18499  10566   9551  -1803   -186       C  
ATOM   5851  O   LEU B1086     -25.636  19.210 -19.216  1.00137.92           O  
ANISOU 5851  O   LEU B1086    24119  18156  10128   9287  -1746    -64       O  
ATOM   5852  CB  LEU B1086     -25.052  21.387 -16.941  1.00134.65           C  
ANISOU 5852  CB  LEU B1086    24335  16640  10184   9200  -1123    184       C  
ATOM   5853  CG  LEU B1086     -24.367  22.755 -16.791  1.00141.88           C  
ANISOU 5853  CG  LEU B1086    26112  16751  11047   9308   -801    500       C  
ATOM   5854  CD1 LEU B1086     -23.533  22.797 -15.537  1.00137.41           C  
ANISOU 5854  CD1 LEU B1086    25471  15849  10891   8608   -462    446       C  
ATOM   5855  CD2 LEU B1086     -23.473  23.082 -17.987  1.00147.33           C  
ANISOU 5855  CD2 LEU B1086    27544  17008  11426   9309   -622    899       C  
ATOM   5856  N   GLU B1087     -27.388  19.132 -17.752  1.00136.46           N  
ANISOU 5856  N   GLU B1087    22890  18628  10330   9542  -2039   -576       N  
ATOM   5857  CA  GLU B1087     -27.783  17.740 -18.011  1.00134.56           C  
ANISOU 5857  CA  GLU B1087    21937  18984  10204   9193  -2268   -900       C  
ATOM   5858  C   GLU B1087     -28.487  17.653 -19.373  1.00144.16           C  
ANISOU 5858  C   GLU B1087    23175  20633  10967   9785  -2729   -997       C  
ATOM   5859  O   GLU B1087     -28.290  16.675 -20.099  1.00143.64           O  
ANISOU 5859  O   GLU B1087    22958  20801  10818   9501  -2857  -1127       O  
ATOM   5860  CB  GLU B1087     -28.698  17.195 -16.899  1.00134.76           C  
ANISOU 5860  CB  GLU B1087    21095  19485  10622   8988  -2325  -1263       C  
ATOM   5861  CG  GLU B1087     -28.836  15.677 -16.923  1.00138.34           C  
ANISOU 5861  CG  GLU B1087    20881  20362  11320   8385  -2410  -1557       C  
ATOM   5862  CD  GLU B1087     -29.885  15.029 -16.038  1.00153.80           C  
ANISOU 5862  CD  GLU B1087    21942  22866  13629   8184  -2484  -1927       C  
ATOM   5863  OE1 GLU B1087     -30.563  15.747 -15.268  1.00161.31           O  
ANISOU 5863  OE1 GLU B1087    22700  23936  14653   8522  -2453  -1984       O  
ATOM   5864  OE2 GLU B1087     -30.028  13.788 -16.121  1.00134.94           O1-
ANISOU 5864  OE2 GLU B1087    19055  20771  11447   7678  -2544  -2166       O1-
ATOM   5865  N   GLU B1088     -29.309  18.673 -19.711  1.00145.72           N  
ANISOU 5865  N   GLU B1088    23573  20941  10852  10641  -2992   -949       N  
ATOM   5866  CA  GLU B1088     -30.018  18.762 -20.990  1.00151.63           C  
ANISOU 5866  CA  GLU B1088    24397  22125  11091  11343  -3480  -1013       C  
ATOM   5867  C   GLU B1088     -29.019  19.119 -22.108  1.00156.20           C  
ANISOU 5867  C   GLU B1088    25917  22224  11206  11461  -3342   -598       C  
ATOM   5868  O   GLU B1088     -29.093  18.549 -23.197  1.00157.63           O  
ANISOU 5868  O   GLU B1088    26122  22745  11026  11578  -3624   -689       O  
ATOM   5869  CB  GLU B1088     -31.148  19.800 -20.900  1.00159.39           C  
ANISOU 5869  CB  GLU B1088    25328  23339  11895  12277  -3772  -1048       C  
ATOM   5870  CG  GLU B1088     -32.272  19.588 -21.903  1.00168.85           C  
ANISOU 5870  CG  GLU B1088    25778  25060  13316  11987  -4191  -1112       C  
ATOM   5871  CD  GLU B1088     -32.125  20.265 -23.253  1.00178.06           C  
ANISOU 5871  CD  GLU B1088    27065  25744  14847  11096  -4081   -480       C  
ATOM   5872  OE1 GLU B1088     -31.169  21.055 -23.435  1.00171.74           O  
ANISOU 5872  OE1 GLU B1088    27307  24401  13544  11680  -3862   -157       O  
ATOM   5873  OE2 GLU B1088     -32.980  20.011 -24.133  1.00171.91           O1-
ANISOU 5873  OE2 GLU B1088    26057  25563  13698  11596  -4603   -661       O1-
ATOM   5874  N   LYS B1089     -28.066  20.035 -21.807  1.00151.75           N  
ANISOU 5874  N   LYS B1089    26115  20877  10665  11379  -2881   -166       N  
ATOM   5875  CA  LYS B1089     -27.000  20.508 -22.697  1.00152.79           C  
ANISOU 5875  CA  LYS B1089    27179  20447  10428  11400  -2603    290       C  
ATOM   5876  C   LYS B1089     -26.046  19.371 -23.044  1.00153.50           C  
ANISOU 5876  C   LYS B1089    27160  20557  10606  10649  -2406    246       C  
ATOM   5877  O   LYS B1089     -25.698  19.210 -24.217  1.00155.73           O  
ANISOU 5877  O   LYS B1089    27869  20872  10431  10818  -2454    393       O  
ATOM   5878  CB  LYS B1089     -26.216  21.661 -22.035  1.00154.07           C  
ANISOU 5878  CB  LYS B1089    28016  19766  10757  11298  -2110    675       C  
ATOM   5879  CG  LYS B1089     -25.429  22.528 -23.010  1.00169.50           C  
ANISOU 5879  CG  LYS B1089    30647  21151  12603  11095  -1819   1214       C  
ATOM   5880  CD  LYS B1089     -25.456  23.998 -22.598  1.00177.00           C  
ANISOU 5880  CD  LYS B1089    31348  21558  14348  10441  -1573   1537       C  
ATOM   5881  CE  LYS B1089     -24.907  24.913 -23.669  1.00182.18           C  
ANISOU 5881  CE  LYS B1089    32056  21857  15308   9790  -1388   2054       C  
ATOM   5882  NZ  LYS B1089     -25.176  26.342 -23.362  1.00187.16           N1+
ANISOU 5882  NZ  LYS B1089    32421  22068  16624   9422  -1305   2292       N1+
ATOM   5883  N   HIS B1090     -25.625  18.589 -22.018  1.00144.92           N  
ANISOU 5883  N   HIS B1090    25528  19452  10082   9865  -2177     52       N  
ATOM   5884  CA  HIS B1090     -24.694  17.459 -22.150  1.00140.39           C  
ANISOU 5884  CA  HIS B1090    24794  18864   9684   9140  -1958     -7       C  
ATOM   5885  C   HIS B1090     -25.319  16.135 -21.680  1.00139.54           C  
ANISOU 5885  C   HIS B1090    23776  19316   9925   8743  -2198   -490       C  
ATOM   5886  O   HIS B1090     -25.562  15.960 -20.482  1.00135.86           O  
ANISOU 5886  O   HIS B1090    22820  18885   9917   8419  -2110   -638       O  
ATOM   5887  CB  HIS B1090     -23.366  17.711 -21.375  1.00136.81           C  
ANISOU 5887  CB  HIS B1090    24621  17778   9583   8514  -1395    275       C  
ATOM   5888  CG  HIS B1090     -22.807  19.104 -21.481  1.00143.32           C  
ANISOU 5888  CG  HIS B1090    26258  17969  10228   8767  -1097    709       C  
ATOM   5889  ND1 HIS B1090     -22.029  19.494 -22.561  1.00148.10           N  
ANISOU 5889  ND1 HIS B1090    27585  18249  10436   8883   -874   1070       N  
ATOM   5890  CD2 HIS B1090     -22.908  20.147 -20.621  1.00145.85           C  
ANISOU 5890  CD2 HIS B1090    26784  17904  10729   8882   -958    818       C  
ATOM   5891  CE1 HIS B1090     -21.699  20.756 -22.332  1.00149.90           C  
ANISOU 5891  CE1 HIS B1090    28432  17882  10640   9038   -603   1401       C  
ATOM   5892  NE2 HIS B1090     -22.203  21.193 -21.177  1.00148.92           N  
ANISOU 5892  NE2 HIS B1090    28037  17685  10860   9049   -657   1246       N  
ATOM   5893  N   GLY B1091     -25.505  15.196 -22.614  1.00135.96           N  
ANISOU 5893  N   GLY B1091    23151  19255   9252   8726  -2457   -726       N  
ATOM   5894  CA  GLY B1091     -25.984  13.847 -22.319  1.00133.38           C  
ANISOU 5894  CA  GLY B1091    22050  19373   9255   8269  -2643  -1184       C  
ATOM   5895  C   GLY B1091     -24.876  13.028 -21.673  1.00130.04           C  
ANISOU 5895  C   GLY B1091    21547  18603   9261   7485  -2209  -1120       C  
ATOM   5896  O   GLY B1091     -24.920  11.794 -21.652  1.00127.57           O  
ANISOU 5896  O   GLY B1091    20801  18496   9171   7049  -2264  -1419       O  
ATOM   5897  N   ASN B1092     -23.874  13.752 -21.129  1.00123.06           N  
ANISOU 5897  N   ASN B1092    21091  17172   8494   7319  -1780   -730       N  
ATOM   5898  CA  ASN B1092     -22.651  13.329 -20.456  1.00116.77           C  
ANISOU 5898  CA  ASN B1092    20323  15986   8058   6681  -1338   -565       C  
ATOM   5899  C   ASN B1092     -22.761  13.553 -18.928  1.00117.07           C  
ANISOU 5899  C   ASN B1092    20013  15917   8551   6394  -1188   -569       C  
ATOM   5900  O   ASN B1092     -22.100  12.862 -18.148  1.00113.12           O  
ANISOU 5900  O   ASN B1092    19272  15292   8417   5843   -948   -567       O  
ATOM   5901  CB  ASN B1092     -21.502  14.174 -21.018  1.00114.83           C  
ANISOU 5901  CB  ASN B1092    20823  15251   7556   6756   -996   -136       C  
ATOM   5902  CG  ASN B1092     -20.141  13.789 -20.536  1.00123.76           C  
ANISOU 5902  CG  ASN B1092    21992  16033   9000   6155   -556     37       C  
ATOM   5903  OD1 ASN B1092     -19.894  12.650 -20.137  1.00118.51           O  
ANISOU 5903  OD1 ASN B1092    20895  15493   8642   5722   -515   -147       O  
ATOM   5904  ND2 ASN B1092     -19.221  14.727 -20.575  1.00110.87           N  
ANISOU 5904  ND2 ASN B1092    20876  13951   7300   6120   -216    397       N  
ATOM   5905  N   VAL B1093     -23.572  14.542 -18.518  1.00114.63           N  
ANISOU 5905  N   VAL B1093    19716  15656   8181   6816  -1324   -565       N  
ATOM   5906  CA  VAL B1093     -23.794  14.887 -17.117  1.00111.96           C  
ANISOU 5906  CA  VAL B1093    19102  15251   8188   6650  -1195   -596       C  
ATOM   5907  C   VAL B1093     -25.122  14.258 -16.664  1.00117.55           C  
ANISOU 5907  C   VAL B1093    19073  16527   9065   6705  -1480   -978       C  
ATOM   5908  O   VAL B1093     -26.079  14.274 -17.438  1.00121.94           O  
ANISOU 5908  O   VAL B1093    19477  17474   9380   7156  -1841  -1168       O  
ATOM   5909  CB  VAL B1093     -23.777  16.431 -16.918  1.00118.02           C  
ANISOU 5909  CB  VAL B1093    20406  15643   8792   7082  -1101   -360       C  
ATOM   5910  CG1 VAL B1093     -23.809  16.799 -15.437  1.00115.74           C  
ANISOU 5910  CG1 VAL B1093    19915  15228   8834   6860   -918   -405       C  
ATOM   5911  CG2 VAL B1093     -22.562  17.069 -17.592  1.00117.94           C  
ANISOU 5911  CG2 VAL B1093    21143  15089   8582   7035   -820     14       C  
ATOM   5912  N   LYS B1094     -25.173  13.676 -15.438  1.00110.96           N  
ANISOU 5912  N   LYS B1094    17766  15766   8628   6240  -1317  -1090       N  
ATOM   5913  CA  LYS B1094     -26.396  13.089 -14.875  1.00112.24           C  
ANISOU 5913  CA  LYS B1094    17203  16445   8997   6206  -1491  -1427       C  
ATOM   5914  C   LYS B1094     -26.698  13.680 -13.508  1.00118.43           C  
ANISOU 5914  C   LYS B1094    17819  17204   9973   6204  -1304  -1415       C  
ATOM   5915  O   LYS B1094     -26.032  13.356 -12.518  1.00113.86           O  
ANISOU 5915  O   LYS B1094    17208  16417   9635   5727  -1012  -1313       O  
ATOM   5916  CB  LYS B1094     -26.379  11.545 -14.836  1.00111.15           C  
ANISOU 5916  CB  LYS B1094    16598  16505   9131   5627  -1478  -1627       C  
ATOM   5917  CG  LYS B1094     -27.709  10.907 -14.380  1.00110.52           C  
ANISOU 5917  CG  LYS B1094    15745  16971   9275   5542  -1641  -1991       C  
ATOM   5918  CD  LYS B1094     -28.725  10.711 -15.519  1.00116.16           C  
ANISOU 5918  CD  LYS B1094    16177  18171   9786   5894  -2090  -2317       C  
ATOM   5919  CE  LYS B1094     -30.089  10.241 -15.055  1.00117.57           C  
ANISOU 5919  CE  LYS B1094    15528  18937  10208   5824  -2247  -2697       C  
ATOM   5920  NZ  LYS B1094     -30.947  11.366 -14.594  1.00122.48           N1+
ANISOU 5920  NZ  LYS B1094    15978  19822  10737   6399  -2330  -2720       N1+
ATOM   5921  N   VAL B1095     -27.720  14.555 -13.475  1.00122.04           N  
ANISOU 5921  N   VAL B1095    18178  17901  10291   6791  -1488  -1531       N  
ATOM   5922  CA  VAL B1095     -28.207  15.244 -12.280  1.00123.75           C  
ANISOU 5922  CA  VAL B1095    18242  18154  10625   6942  -1340  -1578       C  
ATOM   5923  C   VAL B1095     -29.260  14.377 -11.593  1.00132.05           C  
ANISOU 5923  C   VAL B1095    18449  19783  11941   6724  -1365  -1890       C  
ATOM   5924  O   VAL B1095     -30.283  14.025 -12.198  1.00135.93           O  
ANISOU 5924  O   VAL B1095    18458  20784  12406   6953  -1664  -2153       O  
ATOM   5925  CB  VAL B1095     -28.731  16.674 -12.585  1.00131.84           C  
ANISOU 5925  CB  VAL B1095    19638  19089  11365   7744  -1484  -1533       C  
ATOM   5926  CG1 VAL B1095     -29.088  17.428 -11.304  1.00132.25           C  
ANISOU 5926  CG1 VAL B1095    19628  19093  11529   7895  -1278  -1591       C  
ATOM   5927  CG2 VAL B1095     -27.718  17.459 -13.398  1.00131.24           C  
ANISOU 5927  CG2 VAL B1095    20423  18419  11024   7915  -1432  -1200       C  
ATOM   5928  N   ILE B1096     -28.977  14.013 -10.333  1.00127.16           N  
ANISOU 5928  N   ILE B1096    17652  19095  11568   6254  -1042  -1858       N  
ATOM   5929  CA  ILE B1096     -29.864  13.219  -9.489  1.00128.97           C  
ANISOU 5929  CA  ILE B1096    17145  19800  12058   5968   -942  -2087       C  
ATOM   5930  C   ILE B1096     -30.299  14.120  -8.340  1.00136.61           C  
ANISOU 5930  C   ILE B1096    18073  20824  13008   6249   -745  -2117       C  
ATOM   5931  O   ILE B1096     -29.458  14.756  -7.700  1.00133.84           O  
ANISOU 5931  O   ILE B1096    18229  20034  12588   6204   -535  -1922       O  
ATOM   5932  CB  ILE B1096     -29.211  11.891  -8.996  1.00128.11           C  
ANISOU 5932  CB  ILE B1096    16881  19580  12214   5190   -706  -2006       C  
ATOM   5933  CG1 ILE B1096     -28.431  11.179 -10.131  1.00126.23           C  
ANISOU 5933  CG1 ILE B1096    16906  19107  11950   4958   -846  -1928       C  
ATOM   5934  CG2 ILE B1096     -30.270  10.964  -8.360  1.00131.54           C  
ANISOU 5934  CG2 ILE B1096    16539  20521  12921   4876   -609  -2248       C  
ATOM   5935  CD1 ILE B1096     -27.585  10.017  -9.717  1.00128.76           C  
ANISOU 5935  CD1 ILE B1096    17231  19193  12498   4303   -610  -1796       C  
ATOM   5936  N   THR B1097     -31.608  14.202  -8.104  1.00139.37           N  
ANISOU 5936  N   THR B1097    17815  21729  13410   6554   -818  -2389       N  
ATOM   5937  CA  THR B1097     -32.160  15.035  -7.034  1.00142.34           C  
ANISOU 5937  CA  THR B1097    18097  22233  13754   6891   -616  -2470       C  
ATOM   5938  C   THR B1097     -32.688  14.187  -5.876  1.00146.93           C  
ANISOU 5938  C   THR B1097    18043  23205  14577   6417   -299  -2590       C  
ATOM   5939  O   THR B1097     -32.419  14.507  -4.715  1.00145.61           O  
ANISOU 5939  O   THR B1097    18040  22904  14382   6324     19  -2515       O  
ATOM   5940  CB  THR B1097     -33.205  16.013  -7.589  1.00160.77           C  
ANISOU 5940  CB  THR B1097    20297  24872  15915   7745   -894  -2659       C  
ATOM   5941  OG1 THR B1097     -34.043  15.331  -8.529  1.00166.48           O  
ANISOU 5941  OG1 THR B1097    20422  26131  16701   7804  -1227  -2882       O  
ATOM   5942  CG2 THR B1097     -32.571  17.225  -8.252  1.00160.04           C  
ANISOU 5942  CG2 THR B1097    21057  24221  15532   8284  -1040  -2452       C  
ATOM   5943  N   GLU B1098     -33.411  13.090  -6.209  1.00145.27           N  
ANISOU 5943  N   GLU B1098    17143  23462  14590   6090   -376  -2777       N  
ATOM   5944  CA  GLU B1098     -34.052  12.129  -5.295  1.00146.58           C  
ANISOU 5944  CA  GLU B1098    16635  24035  15025   5581    -66  -2894       C  
ATOM   5945  C   GLU B1098     -33.107  11.595  -4.214  1.00145.52           C  
ANISOU 5945  C   GLU B1098    16818  23529  14944   4994    335  -2618       C  
ATOM   5946  O   GLU B1098     -31.909  11.449  -4.468  1.00140.44           O  
ANISOU 5946  O   GLU B1098    16754  22365  14241   4767    301  -2372       O  
ATOM   5947  CB  GLU B1098     -34.663  10.948  -6.083  1.00150.22           C  
ANISOU 5947  CB  GLU B1098    16478  24860  15738   5192   -254  -3111       C  
ATOM   5948  CG  GLU B1098     -35.536  11.331  -7.272  1.00164.15           C  
ANISOU 5948  CG  GLU B1098    17904  27045  17420   5739   -735  -3405       C  
ATOM   5949  CD  GLU B1098     -36.885  11.941  -6.943  1.00185.66           C  
ANISOU 5949  CD  GLU B1098    19952  30432  20160   6262   -762  -3697       C  
ATOM   5950  OE1 GLU B1098     -37.807  11.179  -6.577  1.00185.07           O  
ANISOU 5950  OE1 GLU B1098    19049  30900  20370   5901   -622  -3943       O  
ATOM   5951  OE2 GLU B1098     -37.024  13.179  -7.066  1.00175.89           O1-
ANISOU 5951  OE2 GLU B1098    19008  29163  18660   7037   -908  -3682       O1-
ATOM   5952  N   MET B1099     -33.648  11.300  -3.016  1.00143.52           N  
ANISOU 5952  N   MET B1099    16172  23579  14782   4773    719  -2654       N  
ATOM   5953  CA  MET B1099     -32.869  10.772  -1.895  1.00140.02           C  
ANISOU 5953  CA  MET B1099    15999  22868  14336   4269   1099  -2387       C  
ATOM   5954  C   MET B1099     -32.377   9.358  -2.215  1.00140.22           C  
ANISOU 5954  C   MET B1099    15974  22702  14601   3589   1135  -2242       C  
ATOM   5955  O   MET B1099     -33.191   8.455  -2.431  1.00142.73           O  
ANISOU 5955  O   MET B1099    15699  23351  15182   3263   1182  -2403       O  
ATOM   5956  CB  MET B1099     -33.686  10.807  -0.591  1.00146.61           C  
ANISOU 5956  CB  MET B1099    16420  24129  15158   4250   1520  -2464       C  
ATOM   5957  CG  MET B1099     -32.953  11.467   0.562  1.00148.62           C  
ANISOU 5957  CG  MET B1099    17225  24118  15127   4348   1765  -2286       C  
ATOM   5958  SD  MET B1099     -31.670  10.423   1.309  1.00148.57           S  
ANISOU 5958  SD  MET B1099    17643  23696  15112   3650   2002  -1888       S  
ATOM   5959  CE  MET B1099     -32.621   9.601   2.577  1.00150.20           C  
ANISOU 5959  CE  MET B1099    17285  24404  15381   3292   2549  -1874       C  
ATOM   5960  N   LEU B1100     -31.039   9.192  -2.301  1.00131.08           N  
ANISOU 5960  N   LEU B1100    15436  21002  13367   3389   1100  -1961       N  
ATOM   5961  CA  LEU B1100     -30.382   7.925  -2.636  1.00128.03           C  
ANISOU 5961  CA  LEU B1100    15130  20336  13180   2833   1125  -1798       C  
ATOM   5962  C   LEU B1100     -30.018   7.088  -1.420  1.00132.78           C  
ANISOU 5962  C   LEU B1100    15771  20841  13837   2355   1531  -1539       C  
ATOM   5963  O   LEU B1100     -29.432   7.604  -0.463  1.00130.54           O  
ANISOU 5963  O   LEU B1100    15832  20438  13328   2450   1692  -1356       O  
ATOM   5964  CB  LEU B1100     -29.146   8.151  -3.519  1.00122.97           C  
ANISOU 5964  CB  LEU B1100    15083  19205  12435   2924    861  -1645       C  
ATOM   5965  CG  LEU B1100     -29.416   8.591  -4.950  1.00127.65           C  
ANISOU 5965  CG  LEU B1100    15681  19840  12979   3285    464  -1846       C  
ATOM   5966  CD1 LEU B1100     -28.269   9.388  -5.482  1.00123.82           C  
ANISOU 5966  CD1 LEU B1100    15855  18912  12278   3541    307  -1666       C  
ATOM   5967  CD2 LEU B1100     -29.696   7.407  -5.854  1.00131.15           C  
ANISOU 5967  CD2 LEU B1100    15829  20347  13653   2940    330  -1991       C  
ATOM   5968  N   SER B1101     -30.362   5.780  -1.483  1.00132.57           N  
ANISOU 5968  N   SER B1101    15421  20849  14099   1839   1687  -1531       N  
ATOM   5969  CA  SER B1101     -30.133   4.751  -0.458  1.00133.47           C  
ANISOU 5969  CA  SER B1101    15564  20844  14305   1343   2095  -1256       C  
ATOM   5970  C   SER B1101     -28.668   4.665  -0.042  1.00132.68           C  
ANISOU 5970  C   SER B1101    16106  20275  14030   1303   2113   -891       C  
ATOM   5971  O   SER B1101     -27.781   4.835  -0.882  1.00128.86           O  
ANISOU 5971  O   SER B1101    15968  19471  13522   1427   1824   -859       O  
ATOM   5972  CB  SER B1101     -30.599   3.383  -0.960  1.00140.52           C  
ANISOU 5972  CB  SER B1101    16120  21694  15578    807   2176  -1333       C  
ATOM   5973  OG  SER B1101     -32.008   3.306  -1.108  1.00156.87           O  
ANISOU 5973  OG  SER B1101    17488  24268  17846    724   2230  -1669       O  
ATOM   5974  N   ARG B1102     -28.424   4.379   1.253  1.00129.72           N  
ANISOU 5974  N   ARG B1102    15869  19898  13521   1136   2459   -618       N  
ATOM   5975  CA  ARG B1102     -27.093   4.246   1.852  1.00126.28           C  
ANISOU 5975  CA  ARG B1102    15973  19117  12892   1106   2485   -268       C  
ATOM   5976  C   ARG B1102     -26.253   3.187   1.124  1.00128.70           C  
ANISOU 5976  C   ARG B1102    16491  18985  13423    837   2383   -100       C  
ATOM   5977  O   ARG B1102     -25.048   3.373   0.959  1.00125.00           O  
ANISOU 5977  O   ARG B1102    16424  18229  12843    959   2205     59       O  
ATOM   5978  CB  ARG B1102     -27.216   3.926   3.352  1.00128.71           C  
ANISOU 5978  CB  ARG B1102    16321  19579  13005    956   2894    -16       C  
ATOM   5979  CG  ARG B1102     -26.018   4.366   4.184  1.00135.37           C  
ANISOU 5979  CG  ARG B1102    17670  20273  13492   1126   2844    234       C  
ATOM   5980  CD  ARG B1102     -26.357   4.431   5.662  1.00148.11           C  
ANISOU 5980  CD  ARG B1102    19309  22178  14789   1124   3205    381       C  
ATOM   5981  NE  ARG B1102     -25.163   4.498   6.510  1.00155.89           N  
ANISOU 5981  NE  ARG B1102    20768  23025  15438   1200   3155    661       N  
ATOM   5982  CZ  ARG B1102     -24.559   5.624   6.884  1.00168.62           C  
ANISOU 5982  CZ  ARG B1102    22646  24689  16732   1506   2945    547       C  
ATOM   5983  NH1 ARG B1102     -25.020   6.801   6.477  1.00156.70           N  
ANISOU 5983  NH1 ARG B1102    21042  23298  15199   1794   2791    190       N  
ATOM   5984  NH2 ARG B1102     -23.483   5.581   7.660  1.00152.77           N1+
ANISOU 5984  NH2 ARG B1102    21009  22606  14430   1533   2873    779       N1+
ATOM   5985  N   GLU B1103     -26.906   2.115   0.644  1.00128.11           N  
ANISOU 5985  N   GLU B1103    16126  18870  13679    475   2494   -177       N  
ATOM   5986  CA  GLU B1103     -26.285   1.002  -0.081  1.00127.13           C  
ANISOU 5986  CA  GLU B1103    16186  18315  13804    207   2436    -78       C  
ATOM   5987  C   GLU B1103     -25.854   1.379  -1.514  1.00127.57           C  
ANISOU 5987  C   GLU B1103    16341  18226  13902    428   2024   -308       C  
ATOM   5988  O   GLU B1103     -24.798   0.930  -1.969  1.00124.36           O  
ANISOU 5988  O   GLU B1103    16278  17442  13530    416   1928   -157       O  
ATOM   5989  CB  GLU B1103     -27.222  -0.223  -0.090  1.00133.50           C  
ANISOU 5989  CB  GLU B1103    16658  19105  14960   -294   2713   -141       C  
ATOM   5990  CG  GLU B1103     -27.386  -0.907   1.264  1.00148.52           C  
ANISOU 5990  CG  GLU B1103    18611  20987  16832   -584   3193    208       C  
ATOM   5991  CD  GLU B1103     -28.370  -0.313   2.261  1.00173.93           C  
ANISOU 5991  CD  GLU B1103    21490  24712  19885   -547   3474    166       C  
ATOM   5992  OE1 GLU B1103     -28.970   0.748   1.969  1.00167.97           O  
ANISOU 5992  OE1 GLU B1103    20433  24354  19035   -237   3282   -156       O  
ATOM   5993  OE2 GLU B1103     -28.541  -0.917   3.345  1.00171.71           O1-
ANISOU 5993  OE2 GLU B1103    21269  24425  19550   -799   3909    469       O1-
ATOM   5994  N   PHE B1104     -26.674   2.190  -2.219  1.00124.77           N  
ANISOU 5994  N   PHE B1104    15691  18191  13526    662   1796   -659       N  
ATOM   5995  CA  PHE B1104     -26.408   2.642  -3.592  1.00122.33           C  
ANISOU 5995  CA  PHE B1104    15488  17805  13188    921   1414   -873       C  
ATOM   5996  C   PHE B1104     -25.274   3.662  -3.662  1.00119.98           C  
ANISOU 5996  C   PHE B1104    15646  17328  12614   1288   1256   -711       C  
ATOM   5997  O   PHE B1104     -24.609   3.750  -4.694  1.00117.71           O  
ANISOU 5997  O   PHE B1104    15600  16824  12302   1413   1039   -742       O  
ATOM   5998  CB  PHE B1104     -27.683   3.178  -4.261  1.00127.54           C  
ANISOU 5998  CB  PHE B1104    15691  18894  13874   1105   1210  -1272       C  
ATOM   5999  CG  PHE B1104     -28.608   2.102  -4.784  1.00133.83           C  
ANISOU 5999  CG  PHE B1104    16045  19811  14993    712   1219  -1541       C  
ATOM   6000  CD1 PHE B1104     -29.400   1.355  -3.916  1.00141.25           C  
ANISOU 6000  CD1 PHE B1104    16605  20907  16158    289   1569  -1531       C  
ATOM   6001  CD2 PHE B1104     -28.715   1.859  -6.148  1.00136.99           C  
ANISOU 6001  CD2 PHE B1104    16409  20185  15457    748    885  -1827       C  
ATOM   6002  CE1 PHE B1104     -30.261   0.364  -4.402  1.00146.88           C  
ANISOU 6002  CE1 PHE B1104    16887  21708  17211   -151   1590  -1814       C  
ATOM   6003  CE2 PHE B1104     -29.591   0.880  -6.634  1.00144.50           C  
ANISOU 6003  CE2 PHE B1104    16932  21261  16711    347    861  -2144       C  
ATOM   6004  CZ  PHE B1104     -30.353   0.135  -5.758  1.00146.58           C  
ANISOU 6004  CZ  PHE B1104    16800  21643  17251   -127   1214  -2144       C  
ATOM   6005  N   VAL B1105     -25.042   4.414  -2.562  1.00113.67           N  
ANISOU 6005  N   VAL B1105    14969  16618  11602   1434   1383   -553       N  
ATOM   6006  CA  VAL B1105     -23.951   5.396  -2.444  1.00108.82           C  
ANISOU 6006  CA  VAL B1105    14771  15827  10750   1699   1265   -417       C  
ATOM   6007  C   VAL B1105     -22.638   4.617  -2.268  1.00106.99           C  
ANISOU 6007  C   VAL B1105    14833  15253  10563   1494   1328   -119       C  
ATOM   6008  O   VAL B1105     -21.633   4.994  -2.869  1.00103.79           O  
ANISOU 6008  O   VAL B1105    14706  14627  10100   1616   1174    -61       O  
ATOM   6009  CB  VAL B1105     -24.195   6.446  -1.319  1.00113.14           C  
ANISOU 6009  CB  VAL B1105    15350  16588  11051   1909   1362   -421       C  
ATOM   6010  CG1 VAL B1105     -23.042   7.436  -1.215  1.00110.01           C  
ANISOU 6010  CG1 VAL B1105    15384  15968  10446   2103   1233   -325       C  
ATOM   6011  CG2 VAL B1105     -25.505   7.199  -1.542  1.00115.80           C  
ANISOU 6011  CG2 VAL B1105    15373  17268  11356   2188   1305   -724       C  
ATOM   6012  N   ARG B1106     -22.677   3.499  -1.489  1.00102.50           N  
ANISOU 6012  N   ARG B1106    14193  14644  10108   1193   1573     75       N  
ATOM   6013  CA  ARG B1106     -21.557   2.578  -1.257  1.00100.14           C  
ANISOU 6013  CA  ARG B1106    14142  14036   9871   1038   1650    377       C  
ATOM   6014  C   ARG B1106     -21.132   1.950  -2.597  1.00102.33           C  
ANISOU 6014  C   ARG B1106    14495  14030  10356    996   1513    295       C  
ATOM   6015  O   ARG B1106     -19.935   1.771  -2.834  1.00100.00           O  
ANISOU 6015  O   ARG B1106    14450  13497  10050   1059   1455    461       O  
ATOM   6016  CB  ARG B1106     -21.954   1.496  -0.237  1.00101.32           C  
ANISOU 6016  CB  ARG B1106    14213  14184  10100    753   1967    596       C  
ATOM   6017  CG  ARG B1106     -20.854   0.491   0.084  1.00107.82           C  
ANISOU 6017  CG  ARG B1106    15319  14677  10972    662   2054    945       C  
ATOM   6018  CD  ARG B1106     -21.211  -0.448   1.223  1.00118.43           C  
ANISOU 6018  CD  ARG B1106    16681  16000  12318    434   2393   1231       C  
ATOM   6019  NE  ARG B1106     -22.108  -1.538   0.829  1.00125.53           N  
ANISOU 6019  NE  ARG B1106    17412  16734  13550     85   2601   1155       N  
ATOM   6020  CZ  ARG B1106     -22.351  -2.617   1.571  1.00140.01           C  
ANISOU 6020  CZ  ARG B1106    19327  18392  15479   -185   2941   1432       C  
ATOM   6021  NH1 ARG B1106     -21.756  -2.771   2.749  1.00123.05           N1+
ANISOU 6021  NH1 ARG B1106    17442  16241  13069    -86   3093   1832       N1+
ATOM   6022  NH2 ARG B1106     -23.183  -3.554   1.138  1.00130.68           N  
ANISOU 6022  NH2 ARG B1106    17984  17028  14642   -563   3130   1310       N  
ATOM   6023  N   GLU B1107     -22.118   1.661  -3.480  1.00 99.73           N  
ANISOU 6023  N   GLU B1107    13929  13770  10195    909   1449      6       N  
ATOM   6024  CA  GLU B1107     -21.908   1.118  -4.828  1.00 98.90           C  
ANISOU 6024  CA  GLU B1107    13889  13452  10236    886   1298   -159       C  
ATOM   6025  C   GLU B1107     -21.299   2.171  -5.758  1.00 96.61           C  
ANISOU 6025  C   GLU B1107    13797  13159   9750   1225   1049   -244       C  
ATOM   6026  O   GLU B1107     -20.423   1.835  -6.563  1.00 95.23           O  
ANISOU 6026  O   GLU B1107    13845  12737   9600   1267    991   -207       O  
ATOM   6027  CB  GLU B1107     -23.221   0.582  -5.414  1.00104.21           C  
ANISOU 6027  CB  GLU B1107    14212  14276  11108    684   1265   -493       C  
ATOM   6028  CG  GLU B1107     -23.379  -0.923  -5.272  1.00122.87           C  
ANISOU 6028  CG  GLU B1107    16543  16366  13775    267   1482   -450       C  
ATOM   6029  CD  GLU B1107     -24.810  -1.421  -5.161  1.00160.21           C  
ANISOU 6029  CD  GLU B1107    20828  21315  18728    -71   1585   -707       C  
ATOM   6030  OE1 GLU B1107     -25.702  -0.851  -5.832  1.00172.33           O  
ANISOU 6030  OE1 GLU B1107    22041  23201  20236     37   1358  -1063       O  
ATOM   6031  OE2 GLU B1107     -25.040  -2.389  -4.400  1.00153.53           O1-
ANISOU 6031  OE2 GLU B1107    19948  20299  18087   -441   1901   -543       O1-
ATOM   6032  N   LEU B1108     -21.759   3.440  -5.645  1.00 89.26           N  
ANISOU 6032  N   LEU B1108    12811  12483   8622   1476    936   -347       N  
ATOM   6033  CA  LEU B1108     -21.245   4.562  -6.431  1.00 85.06           C  
ANISOU 6033  CA  LEU B1108    12521  11909   7888   1795    745   -388       C  
ATOM   6034  C   LEU B1108     -19.804   4.872  -6.032  1.00 85.28           C  
ANISOU 6034  C   LEU B1108    12854  11714   7836   1810    812   -116       C  
ATOM   6035  O   LEU B1108     -18.966   4.964  -6.923  1.00 83.69           O  
ANISOU 6035  O   LEU B1108    12868  11327   7604   1891    750    -81       O  
ATOM   6036  CB  LEU B1108     -22.122   5.805  -6.284  1.00 85.29           C  
ANISOU 6036  CB  LEU B1108    12455  12206   7744   2078    639   -547       C  
ATOM   6037  CG  LEU B1108     -23.412   5.809  -7.064  1.00 91.70           C  
ANISOU 6037  CG  LEU B1108    12973  13290   8580   2205    468   -858       C  
ATOM   6038  CD1 LEU B1108     -24.490   6.499  -6.278  1.00 94.13           C  
ANISOU 6038  CD1 LEU B1108    12998  13936   8830   2359    501   -980       C  
ATOM   6039  CD2 LEU B1108     -23.238   6.494  -8.402  1.00 92.68           C  
ANISOU 6039  CD2 LEU B1108    13338  13354   8522   2537    222   -958       C  
ATOM   6040  N   TYR B1109     -19.494   4.952  -4.697  1.00 80.36           N  
ANISOU 6040  N   TYR B1109    12225  11136   7171   1718    945     68       N  
ATOM   6041  CA  TYR B1109     -18.132   5.196  -4.187  1.00 77.67           C  
ANISOU 6041  CA  TYR B1109    12097  10656   6759   1707    972    297       C  
ATOM   6042  C   TYR B1109     -17.197   4.089  -4.667  1.00 80.60           C  
ANISOU 6042  C   TYR B1109    12534  10800   7292   1600   1022    447       C  
ATOM   6043  O   TYR B1109     -16.025   4.347  -4.908  1.00 79.69           O  
ANISOU 6043  O   TYR B1109    12563  10566   7149   1650    995    559       O  
ATOM   6044  CB  TYR B1109     -18.079   5.247  -2.646  1.00 79.32           C  
ANISOU 6044  CB  TYR B1109    12267  11010   6863   1629   1079    443       C  
ATOM   6045  CG  TYR B1109     -18.672   6.455  -1.949  1.00 81.98           C  
ANISOU 6045  CG  TYR B1109    12607  11548   6993   1768   1056    311       C  
ATOM   6046  CD1 TYR B1109     -18.609   7.723  -2.523  1.00 83.49           C  
ANISOU 6046  CD1 TYR B1109    12961  11682   7078   1971    923    158       C  
ATOM   6047  CD2 TYR B1109     -19.212   6.347  -0.670  1.00 84.48           C  
ANISOU 6047  CD2 TYR B1109    12819  12082   7196   1714   1194    356       C  
ATOM   6048  CE1 TYR B1109     -19.132   8.841  -1.872  1.00 84.80           C  
ANISOU 6048  CE1 TYR B1109    13183  11975   7063   2134    913     19       C  
ATOM   6049  CE2 TYR B1109     -19.731   7.460  -0.005  1.00 86.58           C  
ANISOU 6049  CE2 TYR B1109    13113  12531   7253   1876   1192    204       C  
ATOM   6050  CZ  TYR B1109     -19.693   8.705  -0.613  1.00 93.69           C  
ANISOU 6050  CZ  TYR B1109    14177  13340   8081   2094   1043     22       C  
ATOM   6051  OH  TYR B1109     -20.204   9.804   0.032  1.00 98.93           O  
ANISOU 6051  OH  TYR B1109    14915  14127   8548   2289   1052   -148       O  
ATOM   6052  N   GLY B1110     -17.736   2.884  -4.830  1.00 77.83           N  
ANISOU 6052  N   GLY B1110    12069  10381   7122   1450   1107    427       N  
ATOM   6053  CA  GLY B1110     -16.991   1.723  -5.294  1.00 77.73           C  
ANISOU 6053  CA  GLY B1110    12148  10105   7283   1378   1177    537       C  
ATOM   6054  C   GLY B1110     -17.170   1.357  -6.756  1.00 81.55           C  
ANISOU 6054  C   GLY B1110    12678  10457   7851   1413   1101    311       C  
ATOM   6055  O   GLY B1110     -17.119   0.175  -7.100  1.00 83.27           O  
ANISOU 6055  O   GLY B1110    12925  10459   8254   1297   1183    297       O  
ATOM   6056  N   SER B1111     -17.364   2.363  -7.627  1.00 75.81           N  
ANISOU 6056  N   SER B1111    12002   9838   6966   1591    948    133       N  
ATOM   6057  CA  SER B1111     -17.483   2.203  -9.083  1.00 75.73           C  
ANISOU 6057  CA  SER B1111    12086   9760   6929   1691    845    -84       C  
ATOM   6058  C   SER B1111     -16.948   3.451  -9.783  1.00 77.17           C  
ANISOU 6058  C   SER B1111    12472   9973   6877   1937    759    -72       C  
ATOM   6059  O   SER B1111     -16.151   3.330 -10.714  1.00 76.72           O  
ANISOU 6059  O   SER B1111    12602   9779   6771   2027    790    -56       O  
ATOM   6060  CB  SER B1111     -18.915   1.880  -9.511  1.00 81.65           C  
ANISOU 6060  CB  SER B1111    12629  10665   7729   1620    726   -395       C  
ATOM   6061  OG  SER B1111     -19.857   2.853  -9.095  1.00 89.85           O  
ANISOU 6061  OG  SER B1111    13497  11992   8650   1721    627   -485       O  
ATOM   6062  N   VAL B1112     -17.314   4.649  -9.278  1.00 72.18           N  
ANISOU 6062  N   VAL B1112    11834   9491   6101   2042    695    -59       N  
ATOM   6063  CA  VAL B1112     -16.825   5.922  -9.802  1.00 71.00           C  
ANISOU 6063  CA  VAL B1112    11932   9300   5745   2246    653    -14       C  
ATOM   6064  C   VAL B1112     -15.312   6.043  -9.582  1.00 75.65           C  
ANISOU 6064  C   VAL B1112    12650   9722   6370   2159    799    219       C  
ATOM   6065  O   VAL B1112     -14.756   5.417  -8.681  1.00 74.33           O  
ANISOU 6065  O   VAL B1112    12353   9542   6346   1998    884    357       O  
ATOM   6066  CB  VAL B1112     -17.613   7.173  -9.317  1.00 74.70           C  
ANISOU 6066  CB  VAL B1112    12411   9906   6067   2406    560    -80       C  
ATOM   6067  CG1 VAL B1112     -19.108   7.036  -9.590  1.00 76.31           C  
ANISOU 6067  CG1 VAL B1112    12399  10347   6247   2530    405   -330       C  
ATOM   6068  CG2 VAL B1112     -17.344   7.500  -7.849  1.00 73.57           C  
ANISOU 6068  CG2 VAL B1112    12189   9798   5965   2272    646     42       C  
ATOM   6069  N   ASP B1113     -14.645   6.816 -10.432  1.00 75.12           N  
ANISOU 6069  N   ASP B1113    12828   9546   6169   2272    834    267       N  
ATOM   6070  CA  ASP B1113     -13.198   6.977 -10.349  1.00 75.06           C  
ANISOU 6070  CA  ASP B1113    12879   9422   6217   2165    988    457       C  
ATOM   6071  C   ASP B1113     -12.771   7.996  -9.319  1.00 78.65           C  
ANISOU 6071  C   ASP B1113    13339   9881   6663   2056    994    544       C  
ATOM   6072  O   ASP B1113     -11.846   7.724  -8.548  1.00 78.62           O  
ANISOU 6072  O   ASP B1113    13186   9908   6779   1895   1049    664       O  
ATOM   6073  CB  ASP B1113     -12.588   7.285 -11.728  1.00 77.74           C  
ANISOU 6073  CB  ASP B1113    13469   9642   6428   2281   1094    483       C  
ATOM   6074  CG  ASP B1113     -12.835   6.203 -12.756  1.00 95.89           C  
ANISOU 6074  CG  ASP B1113    15786  11938   8708   2386   1092    363       C  
ATOM   6075  OD1 ASP B1113     -12.519   5.024 -12.471  1.00 98.12           O  
ANISOU 6075  OD1 ASP B1113    15896  12203   9183   2291   1145    369       O  
ATOM   6076  OD2 ASP B1113     -13.345   6.529 -13.841  1.00106.91           O1-
ANISOU 6076  OD2 ASP B1113    17398  13340   9882   2581   1029    256       O1-
ATOM   6077  N   PHE B1114     -13.440   9.162  -9.311  1.00 74.43           N  
ANISOU 6077  N   PHE B1114    12984   9319   5977   2170    921    465       N  
ATOM   6078  CA  PHE B1114     -13.120  10.278  -8.435  1.00 74.36           C  
ANISOU 6078  CA  PHE B1114    13063   9255   5937   2077    924    485       C  
ATOM   6079  C   PHE B1114     -14.355  10.863  -7.746  1.00 80.00           C  
ANISOU 6079  C   PHE B1114    13788  10060   6549   2221    803    340       C  
ATOM   6080  O   PHE B1114     -15.425  10.921  -8.353  1.00 81.20           O  
ANISOU 6080  O   PHE B1114    13981  10264   6606   2461    718    230       O  
ATOM   6081  CB  PHE B1114     -12.391  11.381  -9.233  1.00 77.32           C  
ANISOU 6081  CB  PHE B1114    13760   9385   6233   2071   1040    556       C  
ATOM   6082  CG  PHE B1114     -11.094  10.987  -9.922  1.00 79.03           C  
ANISOU 6082  CG  PHE B1114    13948   9538   6542   1922   1220    698       C  
ATOM   6083  CD1 PHE B1114     -11.104  10.420 -11.192  1.00 81.20           C  
ANISOU 6083  CD1 PHE B1114    14316   9791   6747   2074   1297    725       C  
ATOM   6084  CD2 PHE B1114      -9.863  11.253  -9.332  1.00 81.98           C  
ANISOU 6084  CD2 PHE B1114    14194   9899   7054   1643   1313    776       C  
ATOM   6085  CE1 PHE B1114      -9.911  10.053 -11.821  1.00 82.75           C  
ANISOU 6085  CE1 PHE B1114    14473   9954   7016   1969   1505    844       C  
ATOM   6086  CE2 PHE B1114      -8.668  10.901  -9.974  1.00 85.02           C  
ANISOU 6086  CE2 PHE B1114    14484  10277   7542   1524   1504    895       C  
ATOM   6087  CZ  PHE B1114      -8.702  10.303 -11.211  1.00 82.68           C  
ANISOU 6087  CZ  PHE B1114    14286   9954   7176   1700   1621    937       C  
ATOM   6088  N   VAL B1115     -14.196  11.311  -6.481  1.00 76.65           N  
ANISOU 6088  N   VAL B1115    13312   9686   6124   2098    789    318       N  
ATOM   6089  CA  VAL B1115     -15.247  11.967  -5.691  1.00 77.57           C  
ANISOU 6089  CA  VAL B1115    13452   9893   6126   2245    719    166       C  
ATOM   6090  C   VAL B1115     -14.860  13.431  -5.482  1.00 83.68           C  
ANISOU 6090  C   VAL B1115    14557  10426   6811   2249    735    110       C  
ATOM   6091  O   VAL B1115     -13.815  13.724  -4.894  1.00 83.29           O  
ANISOU 6091  O   VAL B1115    14532  10306   6810   1989    767    142       O  
ATOM   6092  CB  VAL B1115     -15.609  11.237  -4.368  1.00 80.77           C  
ANISOU 6092  CB  VAL B1115    13570  10570   6548   2141    713    152       C  
ATOM   6093  CG1 VAL B1115     -16.480  12.113  -3.468  1.00 82.13           C  
ANISOU 6093  CG1 VAL B1115    13802  10835   6570   2288    689    -17       C  
ATOM   6094  CG2 VAL B1115     -16.311   9.916  -4.651  1.00 79.77           C  
ANISOU 6094  CG2 VAL B1115    13177  10610   6523   2150    725    174       C  
ATOM   6095  N   ILE B1116     -15.694  14.340  -5.996  1.00 82.17           N  
ANISOU 6095  N   ILE B1116    14624  10099   6498   2549    704     16       N  
ATOM   6096  CA  ILE B1116     -15.468  15.775  -5.903  1.00 84.50           C  
ANISOU 6096  CA  ILE B1116    15324  10067   6713   2598    742    -42       C  
ATOM   6097  C   ILE B1116     -16.124  16.332  -4.654  1.00 90.38           C  
ANISOU 6097  C   ILE B1116    16067  10903   7371   2693    697   -240       C  
ATOM   6098  O   ILE B1116     -17.336  16.174  -4.461  1.00 91.40           O  
ANISOU 6098  O   ILE B1116    16047  11259   7423   2988    641   -350       O  
ATOM   6099  CB  ILE B1116     -15.884  16.522  -7.205  1.00 89.59           C  
ANISOU 6099  CB  ILE B1116    16351  10445   7243   2927    754     11       C  
ATOM   6100  CG1 ILE B1116     -15.156  15.919  -8.443  1.00 89.18           C  
ANISOU 6100  CG1 ILE B1116    16320  10337   7228   2825    832    205       C  
ATOM   6101  CG2 ILE B1116     -15.640  18.053  -7.093  1.00 93.22           C  
ANISOU 6101  CG2 ILE B1116    17320  10460   7638   2975    833    -25       C  
ATOM   6102  CD1 ILE B1116     -15.787  16.224  -9.778  1.00 96.09           C  
ANISOU 6102  CD1 ILE B1116    17478  11114   7918   3216    797    264       C  
ATOM   6103  N   ILE B1117     -15.305  16.949  -3.785  1.00 87.35           N  
ANISOU 6103  N   ILE B1117    15814  10379   6995   2427    724   -311       N  
ATOM   6104  CA  ILE B1117     -15.747  17.597  -2.549  1.00 88.53           C  
ANISOU 6104  CA  ILE B1117    16040  10577   7020   2492    695   -537       C  
ATOM   6105  C   ILE B1117     -15.271  19.069  -2.631  1.00 95.11           C  
ANISOU 6105  C   ILE B1117    17385  10914   7838   2447    745   -649       C  
ATOM   6106  O   ILE B1117     -14.190  19.404  -2.143  1.00 95.22           O  
ANISOU 6106  O   ILE B1117    17468  10794   7916   2059    752   -702       O  
ATOM   6107  CB  ILE B1117     -15.310  16.841  -1.252  1.00 90.43           C  
ANISOU 6107  CB  ILE B1117    15955  11170   7232   2220    651   -565       C  
ATOM   6108  CG1 ILE B1117     -15.610  15.325  -1.336  1.00 87.63           C  
ANISOU 6108  CG1 ILE B1117    15172  11183   6941   2211    651   -389       C  
ATOM   6109  CG2 ILE B1117     -15.994  17.441  -0.024  1.00 93.36           C  
ANISOU 6109  CG2 ILE B1117    16413  11656   7403   2369    641   -815       C  
ATOM   6110  CD1 ILE B1117     -14.452  14.432  -1.016  1.00 89.39           C  
ANISOU 6110  CD1 ILE B1117    15168  11541   7256   1884    625   -227       C  
ATOM   6111  N   PRO B1118     -16.047  19.948  -3.308  1.00 94.21           N  
ANISOU 6111  N   PRO B1118    17639  10506   7652   2840    778   -681       N  
ATOM   6112  CA  PRO B1118     -15.615  21.350  -3.472  1.00 98.52           C  
ANISOU 6112  CA  PRO B1118    18759  10475   8200   2804    866   -755       C  
ATOM   6113  C   PRO B1118     -16.136  22.269  -2.362  1.00107.37           C  
ANISOU 6113  C   PRO B1118    20119  11477   9198   2966    850  -1069       C  
ATOM   6114  O   PRO B1118     -16.591  23.392  -2.622  1.00110.15           O  
ANISOU 6114  O   PRO B1118    20969  11393   9490   3280    908  -1155       O  
ATOM   6115  CB  PRO B1118     -16.180  21.716  -4.848  1.00101.34           C  
ANISOU 6115  CB  PRO B1118    19423  10576   8504   3214    909   -574       C  
ATOM   6116  CG  PRO B1118     -17.378  20.790  -5.027  1.00103.44           C  
ANISOU 6116  CG  PRO B1118    19268  11350   8685   3608    780   -571       C  
ATOM   6117  CD  PRO B1118     -17.345  19.722  -3.970  1.00 95.50           C  
ANISOU 6117  CD  PRO B1118    17721  10839   7726   3347    728   -655       C  
ATOM   6118  N   SER B1119     -16.030  21.785  -1.110  1.00104.64           N  
ANISOU 6118  N   SER B1119    19454  11510   8793   2768    780  -1237       N  
ATOM   6119  CA  SER B1119     -16.528  22.434   0.099  1.00107.77           C  
ANISOU 6119  CA  SER B1119    19999  11930   9018   2913    767  -1566       C  
ATOM   6120  C   SER B1119     -15.726  23.662   0.549  1.00116.84           C  
ANISOU 6120  C   SER B1119    21644  12563  10186   2630    792  -1808       C  
ATOM   6121  O   SER B1119     -14.494  23.637   0.512  1.00116.21           O  
ANISOU 6121  O   SER B1119    21543  12362  10251   2105    774  -1768       O  
ATOM   6122  CB  SER B1119     -16.635  21.409   1.221  1.00109.03           C  
ANISOU 6122  CB  SER B1119    19673  12696   9058   2790    701  -1616       C  
ATOM   6123  OG  SER B1119     -17.416  20.303   0.795  1.00113.52           O  
ANISOU 6123  OG  SER B1119    19815  13672   9647   3003    709  -1413       O  
ATOM   6124  N   TYR B1120     -16.442  24.744   0.952  1.00118.69           N  
ANISOU 6124  N   TYR B1120    22316  12489  10291   2986    842  -2081       N  
ATOM   6125  CA  TYR B1120     -15.859  25.990   1.476  1.00124.41           C  
ANISOU 6125  CA  TYR B1120    23584  12664  11024   2756    876  -2392       C  
ATOM   6126  C   TYR B1120     -15.450  25.792   2.949  1.00130.13           C  
ANISOU 6126  C   TYR B1120    24108  13753  11584   2447    756  -2714       C  
ATOM   6127  O   TYR B1120     -14.411  26.301   3.378  1.00132.52           O  
ANISOU 6127  O   TYR B1120    24590  13810  11952   1944    700  -2920       O  
ATOM   6128  CB  TYR B1120     -16.864  27.153   1.385  1.00130.53           C  
ANISOU 6128  CB  TYR B1120    24924  12973  11699   3342    979  -2576       C  
ATOM   6129  CG  TYR B1120     -17.005  27.771   0.011  1.00134.28           C  
ANISOU 6129  CG  TYR B1120    25840  12878  12303   3600   1092  -2308       C  
ATOM   6130  CD1 TYR B1120     -16.150  28.786  -0.410  1.00140.37           C  
ANISOU 6130  CD1 TYR B1120    27212  12888  13236   3267   1215  -2312       C  
ATOM   6131  CD2 TYR B1120     -18.042  27.397  -0.840  1.00133.44           C  
ANISOU 6131  CD2 TYR B1120    25582  12985  12133   4196   1081  -2066       C  
ATOM   6132  CE1 TYR B1120     -16.297  29.386  -1.661  1.00143.27           C  
ANISOU 6132  CE1 TYR B1120    28064  12701  13671   3540   1354  -2022       C  
ATOM   6133  CE2 TYR B1120     -18.205  27.995  -2.090  1.00136.55           C  
ANISOU 6133  CE2 TYR B1120    26431  12881  12571   4507   1162  -1810       C  
ATOM   6134  CZ  TYR B1120     -17.325  28.986  -2.500  1.00148.70           C  
ANISOU 6134  CZ  TYR B1120    28617  13643  14241   4192   1313  -1762       C  
ATOM   6135  OH  TYR B1120     -17.469  29.574  -3.737  1.00153.55           O  
ANISOU 6135  OH  TYR B1120    29742  13745  14855   4512   1425  -1458       O  
ATOM   6136  N   PHE B1121     -16.300  25.079   3.720  1.00125.40           N  
ANISOU 6136  N   PHE B1121    23145  13748  10752   2754    724  -2765       N  
ATOM   6137  CA  PHE B1121     -16.108  24.753   5.133  1.00126.55           C  
ANISOU 6137  CA  PHE B1121    23095  14344  10643   2580    626  -3017       C  
ATOM   6138  C   PHE B1121     -16.547  23.311   5.357  1.00126.35           C  
ANISOU 6138  C   PHE B1121    22458  15025  10522   2675    614  -2745       C  
ATOM   6139  O   PHE B1121     -17.682  22.950   5.035  1.00124.24           O  
ANISOU 6139  O   PHE B1121    22016  14962  10230   3113    725  -2624       O  
ATOM   6140  CB  PHE B1121     -16.887  25.727   6.042  1.00133.48           C  
ANISOU 6140  CB  PHE B1121    24375  15086  11257   2949    695  -3453       C  
ATOM   6141  CG  PHE B1121     -16.326  27.131   6.088  1.00140.66           C  
ANISOU 6141  CG  PHE B1121    25938  15266  12239   2765    697  -3796       C  
ATOM   6142  CD1 PHE B1121     -16.751  28.099   5.182  1.00146.41           C  
ANISOU 6142  CD1 PHE B1121    27173  15323  13134   3081    838  -3773       C  
ATOM   6143  CD2 PHE B1121     -15.388  27.493   7.050  1.00146.48           C  
ANISOU 6143  CD2 PHE B1121    26809  15978  12870   2282    553  -4155       C  
ATOM   6144  CE1 PHE B1121     -16.230  29.399   5.224  1.00153.28           C  
ANISOU 6144  CE1 PHE B1121    28712  15431  14097   2881    879  -4078       C  
ATOM   6145  CE2 PHE B1121     -14.875  28.796   7.100  1.00155.21           C  
ANISOU 6145  CE2 PHE B1121    28531  16364  14076   2047    565  -4516       C  
ATOM   6146  CZ  PHE B1121     -15.300  29.741   6.187  1.00155.76           C  
ANISOU 6146  CZ  PHE B1121    29139  15698  14344   2334    752  -4466       C  
ATOM   6147  N   GLU B1122     -15.617  22.477   5.848  1.00122.05           N  
ANISOU 6147  N   GLU B1122    21585  14838   9951   2254    479  -2640       N  
ATOM   6148  CA  GLU B1122     -15.821  21.045   6.098  1.00118.52           C  
ANISOU 6148  CA  GLU B1122    20613  14986   9432   2267    474  -2347       C  
ATOM   6149  C   GLU B1122     -15.003  20.641   7.343  1.00122.27           C  
ANISOU 6149  C   GLU B1122    20952  15849   9656   1964    310  -2447       C  
ATOM   6150  O   GLU B1122     -13.789  20.437   7.237  1.00120.78           O  
ANISOU 6150  O   GLU B1122    20648  15646   9596   1562    144  -2377       O  
ATOM   6151  CB  GLU B1122     -15.434  20.216   4.843  1.00115.78           C  
ANISOU 6151  CB  GLU B1122    19989  14594   9409   2131    476  -1946       C  
ATOM   6152  CG  GLU B1122     -15.917  18.772   4.848  1.00126.05           C  
ANISOU 6152  CG  GLU B1122    20819  16376  10699   2221    525  -1641       C  
ATOM   6153  CD  GLU B1122     -17.421  18.567   4.854  1.00151.06           C  
ANISOU 6153  CD  GLU B1122    23871  19747  13779   2652    688  -1647       C  
ATOM   6154  OE1 GLU B1122     -18.035  18.637   3.764  1.00135.85           O1-
ANISOU 6154  OE1 GLU B1122    21931  17650  12035   2876    742  -1557       O1-
ATOM   6155  OE2 GLU B1122     -17.985  18.332   5.949  1.00149.13           O  
ANISOU 6155  OE2 GLU B1122    23529  19868  13266   2770    764  -1747       O  
ATOM   6156  N   PRO B1123     -15.636  20.583   8.543  1.00120.76           N  
ANISOU 6156  N   PRO B1123    20779  16025   9079   2174    353  -2629       N  
ATOM   6157  CA  PRO B1123     -14.866  20.274   9.759  1.00122.38           C  
ANISOU 6157  CA  PRO B1123    20917  16618   8963   1938    168  -2737       C  
ATOM   6158  C   PRO B1123     -14.442  18.820   9.892  1.00122.21           C  
ANISOU 6158  C   PRO B1123    20455  17052   8926   1815    107  -2320       C  
ATOM   6159  O   PRO B1123     -13.342  18.562  10.380  1.00122.62           O  
ANISOU 6159  O   PRO B1123    20405  17299   8888   1532   -133  -2320       O  
ATOM   6160  CB  PRO B1123     -15.793  20.714  10.906  1.00128.00           C  
ANISOU 6160  CB  PRO B1123    21848  17557   9230   2267    290  -3051       C  
ATOM   6161  CG  PRO B1123     -16.999  21.339  10.261  1.00132.52           C  
ANISOU 6161  CG  PRO B1123    22583  17827   9943   2676    534  -3132       C  
ATOM   6162  CD  PRO B1123     -17.058  20.822   8.863  1.00123.59           C  
ANISOU 6162  CD  PRO B1123    21212  16498   9247   2654    577  -2755       C  
ATOM   6163  N   PHE B1124     -15.294  17.879   9.465  1.00115.47           N  
ANISOU 6163  N   PHE B1124    19341  16364   8168   2029    313  -1982       N  
ATOM   6164  CA  PHE B1124     -14.973  16.466   9.592  1.00113.58           C  
ANISOU 6164  CA  PHE B1124    18750  16480   7927   1937    298  -1576       C  
ATOM   6165  C   PHE B1124     -14.465  15.847   8.284  1.00114.07           C  
ANISOU 6165  C   PHE B1124    18585  16316   8439   1782    274  -1267       C  
ATOM   6166  O   PHE B1124     -13.324  15.388   8.248  1.00113.37           O  
ANISOU 6166  O   PHE B1124    18349  16293   8432   1546     91  -1125       O  
ATOM   6167  CB  PHE B1124     -16.146  15.682  10.207  1.00115.96           C  
ANISOU 6167  CB  PHE B1124    18915  17153   7992   2196    560  -1410       C  
ATOM   6168  CG  PHE B1124     -16.293  15.957  11.689  1.00122.44           C  
ANISOU 6168  CG  PHE B1124    19920  18331   8271   2300    566  -1622       C  
ATOM   6169  CD1 PHE B1124     -17.086  17.008  12.145  1.00128.89           C  
ANISOU 6169  CD1 PHE B1124    21002  19103   8869   2538    690  -2016       C  
ATOM   6170  CD2 PHE B1124     -15.599  15.199  12.628  1.00126.28           C  
ANISOU 6170  CD2 PHE B1124    20347  19199   8434   2201    435  -1439       C  
ATOM   6171  CE1 PHE B1124     -17.186  17.290  13.513  1.00134.36           C  
ANISOU 6171  CE1 PHE B1124    21901  20135   9015   2646    701  -2250       C  
ATOM   6172  CE2 PHE B1124     -15.706  15.478  13.996  1.00134.00           C  
ANISOU 6172  CE2 PHE B1124    21537  20537   8841   2318    423  -1645       C  
ATOM   6173  CZ  PHE B1124     -16.498  16.522  14.428  1.00135.04           C  
ANISOU 6173  CZ  PHE B1124    21934  20625   8749   2526    564  -2063       C  
ATOM   6174  N   GLY B1125     -15.280  15.869   7.233  1.00108.48           N  
ANISOU 6174  N   GLY B1125    17847  15374   7996   1941    441  -1193       N  
ATOM   6175  CA  GLY B1125     -14.918  15.295   5.937  1.00104.83           C  
ANISOU 6175  CA  GLY B1125    17212  14707   7913   1838    441   -930       C  
ATOM   6176  C   GLY B1125     -15.198  13.805   5.848  1.00106.13           C  
ANISOU 6176  C   GLY B1125    17054  15126   8145   1856    540   -577       C  
ATOM   6177  O   GLY B1125     -14.355  13.036   5.375  1.00103.75           O  
ANISOU 6177  O   GLY B1125    16590  14800   8029   1694    467   -342       O  
ATOM   6178  N   LEU B1126     -16.396  13.395   6.322  1.00102.55           N  
ANISOU 6178  N   LEU B1126    16509  14907   7549   2050    733   -551       N  
ATOM   6179  CA  LEU B1126     -16.871  12.010   6.343  1.00100.31           C  
ANISOU 6179  CA  LEU B1126    15955  14829   7329   2039    890   -242       C  
ATOM   6180  C   LEU B1126     -17.167  11.481   4.950  1.00 97.57           C  
ANISOU 6180  C   LEU B1126    15444  14269   7360   2029    934   -118       C  
ATOM   6181  O   LEU B1126     -16.921  10.306   4.692  1.00 94.73           O  
ANISOU 6181  O   LEU B1126    14916  13929   7149   1913    973    150       O  
ATOM   6182  CB  LEU B1126     -18.097  11.853   7.262  1.00103.20           C  
ANISOU 6182  CB  LEU B1126    16259  15510   7442   2201   1132   -286       C  
ATOM   6183  CG  LEU B1126     -17.873  12.163   8.745  1.00112.69           C  
ANISOU 6183  CG  LEU B1126    17636  16996   8183   2235   1125   -378       C  
ATOM   6184  CD1 LEU B1126     -19.184  12.230   9.491  1.00116.27           C  
ANISOU 6184  CD1 LEU B1126    18041  17740   8396   2433   1422   -475       C  
ATOM   6185  CD2 LEU B1126     -16.950  11.148   9.389  1.00116.54           C  
ANISOU 6185  CD2 LEU B1126    18091  17660   8528   2084   1042    -59       C  
ATOM   6186  N   VAL B1127     -17.676  12.344   4.048  1.00 92.38           N  
ANISOU 6186  N   VAL B1127    14871  13395   6834   2177    918   -316       N  
ATOM   6187  CA  VAL B1127     -17.963  11.971   2.661  1.00 89.99           C  
ANISOU 6187  CA  VAL B1127    14452  12913   6825   2207    919   -242       C  
ATOM   6188  C   VAL B1127     -16.675  11.402   2.079  1.00 90.98           C  
ANISOU 6188  C   VAL B1127    14577  12868   7124   1988    815    -38       C  
ATOM   6189  O   VAL B1127     -16.692  10.282   1.579  1.00 88.91           O  
ANISOU 6189  O   VAL B1127    14133  12616   7033   1915    865    150       O  
ATOM   6190  CB  VAL B1127     -18.515  13.156   1.822  1.00 94.60           C  
ANISOU 6190  CB  VAL B1127    15217  13278   7449   2455    874   -467       C  
ATOM   6191  CG1 VAL B1127     -18.578  12.807   0.336  1.00 92.46           C  
ANISOU 6191  CG1 VAL B1127    14886  12830   7416   2489    825   -379       C  
ATOM   6192  CG2 VAL B1127     -19.882  13.608   2.333  1.00 97.09           C  
ANISOU 6192  CG2 VAL B1127    15458  13811   7621   2744    989   -671       C  
ATOM   6193  N   ALA B1128     -15.553  12.141   2.248  1.00 87.57           N  
ANISOU 6193  N   ALA B1128    14330  12298   6644   1870    685    -96       N  
ATOM   6194  CA  ALA B1128     -14.203  11.779   1.812  1.00 85.79           C  
ANISOU 6194  CA  ALA B1128    14062  11962   6571   1666    592     59       C  
ATOM   6195  C   ALA B1128     -13.731  10.463   2.411  1.00 87.14           C  
ANISOU 6195  C   ALA B1128    14018  12358   6732   1582    592    314       C  
ATOM   6196  O   ALA B1128     -13.139   9.662   1.689  1.00 84.39           O  
ANISOU 6196  O   ALA B1128    13552  11923   6589   1525    599    497       O  
ATOM   6197  CB  ALA B1128     -13.223  12.887   2.167  1.00 88.49           C  
ANISOU 6197  CB  ALA B1128    14584  12195   6843   1514    464   -109       C  
ATOM   6198  N   LEU B1129     -13.999  10.234   3.721  1.00 85.15           N  
ANISOU 6198  N   LEU B1129    13751  12383   6218   1610    603    336       N  
ATOM   6199  CA  LEU B1129     -13.602   9.006   4.418  1.00 85.27           C  
ANISOU 6199  CA  LEU B1129    13636  12600   6163   1584    615    622       C  
ATOM   6200  C   LEU B1129     -14.390   7.817   3.926  1.00 89.00           C  
ANISOU 6200  C   LEU B1129    13985  13013   6817   1613    812    823       C  
ATOM   6201  O   LEU B1129     -13.800   6.764   3.676  1.00 89.10           O  
ANISOU 6201  O   LEU B1129    13916  12961   6975   1580    820   1069       O  
ATOM   6202  CB  LEU B1129     -13.713   9.147   5.934  1.00 88.12           C  
ANISOU 6202  CB  LEU B1129    14076  13278   6129   1629    591    602       C  
ATOM   6203  CG  LEU B1129     -12.655  10.007   6.592  1.00 94.71           C  
ANISOU 6203  CG  LEU B1129    14996  14226   6763   1553    336    424       C  
ATOM   6204  CD1 LEU B1129     -13.123  10.478   7.934  1.00 98.43           C  
ANISOU 6204  CD1 LEU B1129    15622  14979   6798   1637    335    272       C  
ATOM   6205  CD2 LEU B1129     -11.347   9.261   6.731  1.00 98.15           C  
ANISOU 6205  CD2 LEU B1129    15277  14779   7238   1496    156    651       C  
ATOM   6206  N   GLU B1130     -15.713   8.001   3.737  1.00 85.30           N  
ANISOU 6206  N   GLU B1130    13491  12555   6363   1678    967    690       N  
ATOM   6207  CA  GLU B1130     -16.635   6.993   3.209  1.00 84.45           C  
ANISOU 6207  CA  GLU B1130    13227  12402   6460   1650   1151    791       C  
ATOM   6208  C   GLU B1130     -16.279   6.665   1.762  1.00 84.37           C  
ANISOU 6208  C   GLU B1130    13179  12119   6759   1620   1086    794       C  
ATOM   6209  O   GLU B1130     -16.338   5.503   1.378  1.00 84.27           O  
ANISOU 6209  O   GLU B1130    13082  12005   6934   1542   1177    954       O  
ATOM   6210  CB  GLU B1130     -18.085   7.488   3.283  1.00 87.10           C  
ANISOU 6210  CB  GLU B1130    13472  12879   6743   1742   1286    575       C  
ATOM   6211  CG  GLU B1130     -18.647   7.561   4.692  1.00100.23           C  
ANISOU 6211  CG  GLU B1130    15141  14844   8099   1775   1448    591       C  
ATOM   6212  CD  GLU B1130     -19.854   8.460   4.875  1.00126.24           C  
ANISOU 6212  CD  GLU B1130    18367  18316  11284   1945   1549    305       C  
ATOM   6213  OE1 GLU B1130     -20.132   9.295   3.982  1.00125.78           O  
ANISOU 6213  OE1 GLU B1130    18320  18127  11343   2088   1431     75       O  
ATOM   6214  OE2 GLU B1130     -20.519   8.333   5.929  1.00127.74           O  
ANISOU 6214  OE2 GLU B1130    18504  18784  11248   1968   1763    325       O  
ATOM   6215  N   ALA B1131     -15.896   7.689   0.971  1.00 78.65           N  
ANISOU 6215  N   ALA B1131    12559  11254   6071   1680    950    618       N  
ATOM   6216  CA  ALA B1131     -15.511   7.560  -0.434  1.00 76.01           C  
ANISOU 6216  CA  ALA B1131    12240  10684   5957   1682    902    609       C  
ATOM   6217  C   ALA B1131     -14.176   6.846  -0.556  1.00 79.44           C  
ANISOU 6217  C   ALA B1131    12656  11032   6497   1594    869    819       C  
ATOM   6218  O   ALA B1131     -14.028   5.978  -1.425  1.00 79.03           O  
ANISOU 6218  O   ALA B1131    12557  10834   6637   1585    918    898       O  
ATOM   6219  CB  ALA B1131     -15.421   8.933  -1.085  1.00 76.01           C  
ANISOU 6219  CB  ALA B1131    12419  10550   5911   1777    811    415       C  
ATOM   6220  N   MET B1132     -13.212   7.205   0.323  1.00 75.48           N  
ANISOU 6220  N   MET B1132    12176  10642   5862   1547    775    879       N  
ATOM   6221  CA  MET B1132     -11.875   6.636   0.330  1.00 75.16           C  
ANISOU 6221  CA  MET B1132    12053  10600   5905   1507    712   1061       C  
ATOM   6222  C   MET B1132     -11.862   5.172   0.719  1.00 80.47           C  
ANISOU 6222  C   MET B1132    12649  11296   6631   1552    795   1325       C  
ATOM   6223  O   MET B1132     -11.140   4.388   0.101  1.00 80.19           O  
ANISOU 6223  O   MET B1132    12555  11133   6780   1590    816   1460       O  
ATOM   6224  CB  MET B1132     -10.940   7.455   1.205  1.00 79.03           C  
ANISOU 6224  CB  MET B1132    12538  11262   6226   1438    546   1003       C  
ATOM   6225  CG  MET B1132     -10.259   8.561   0.460  1.00 82.88           C  
ANISOU 6225  CG  MET B1132    13077  11608   6808   1328    491    831       C  
ATOM   6226  SD  MET B1132      -9.766   9.957   1.495  1.00 90.45           S  
ANISOU 6226  SD  MET B1132    14120  12695   7551   1178    315    591       S  
ATOM   6227  CE  MET B1132      -8.559   9.173   2.562  1.00 89.91           C  
ANISOU 6227  CE  MET B1132    13793  12982   7385   1157    127    760       C  
ATOM   6228  N   CYS B1133     -12.694   4.791   1.698  1.00 78.75           N  
ANISOU 6228  N   CYS B1133    12456  11211   6254   1560    879   1403       N  
ATOM   6229  CA  CYS B1133     -12.809   3.409   2.153  1.00 80.62           C  
ANISOU 6229  CA  CYS B1133    12693  11412   6527   1585   1010   1690       C  
ATOM   6230  C   CYS B1133     -13.352   2.474   1.083  1.00 86.27           C  
ANISOU 6230  C   CYS B1133    13394  11842   7543   1538   1163   1699       C  
ATOM   6231  O   CYS B1133     -13.129   1.266   1.170  1.00 87.82           O  
ANISOU 6231  O   CYS B1133    13631  11884   7853   1560   1267   1935       O  
ATOM   6232  CB  CYS B1133     -13.633   3.335   3.428  1.00 83.04           C  
ANISOU 6232  CB  CYS B1133    13055  11929   6567   1573   1120   1771       C  
ATOM   6233  SG  CYS B1133     -12.731   3.852   4.901  1.00 89.51           S  
ANISOU 6233  SG  CYS B1133    13938  13096   6973   1673    924   1860       S  
ATOM   6234  N   LEU B1134     -14.041   3.036   0.064  1.00 82.22           N  
ANISOU 6234  N   LEU B1134    12850  11248   7144   1495   1163   1433       N  
ATOM   6235  CA  LEU B1134     -14.608   2.300  -1.074  1.00 81.72           C  
ANISOU 6235  CA  LEU B1134    12763  10955   7330   1443   1252   1346       C  
ATOM   6236  C   LEU B1134     -13.693   2.266  -2.310  1.00 83.87           C  
ANISOU 6236  C   LEU B1134    13076  11042   7749   1519   1182   1297       C  
ATOM   6237  O   LEU B1134     -13.954   1.509  -3.249  1.00 84.31           O  
ANISOU 6237  O   LEU B1134    13151  10897   7988   1500   1245   1230       O  
ATOM   6238  CB  LEU B1134     -16.007   2.831  -1.439  1.00 81.38           C  
ANISOU 6238  CB  LEU B1134    12634  11003   7284   1394   1274   1080       C  
ATOM   6239  CG  LEU B1134     -17.236   2.158  -0.806  1.00 87.17           C  
ANISOU 6239  CG  LEU B1134    13248  11819   8054   1247   1460   1096       C  
ATOM   6240  CD1 LEU B1134     -17.261   0.659  -1.054  1.00 88.64           C  
ANISOU 6240  CD1 LEU B1134    13455  11739   8483   1098   1613   1240       C  
ATOM   6241  CD2 LEU B1134     -17.381   2.504   0.653  1.00 89.22           C  
ANISOU 6241  CD2 LEU B1134    13518  12321   8059   1256   1539   1229       C  
ATOM   6242  N   GLY B1135     -12.626   3.058  -2.284  1.00 78.37           N  
ANISOU 6242  N   GLY B1135    12388  10423   6968   1585   1069   1314       N  
ATOM   6243  CA  GLY B1135     -11.636   3.068  -3.350  1.00 77.01           C  
ANISOU 6243  CA  GLY B1135    12226  10120   6914   1648   1056   1299       C  
ATOM   6244  C   GLY B1135     -11.590   4.320  -4.186  1.00 79.17           C  
ANISOU 6244  C   GLY B1135    12568  10387   7127   1647   1002   1106       C  
ATOM   6245  O   GLY B1135     -10.626   4.514  -4.926  1.00 78.82           O  
ANISOU 6245  O   GLY B1135    12530  10276   7142   1673   1025   1120       O  
ATOM   6246  N   ALA B1136     -12.625   5.174  -4.086  1.00 75.27           N  
ANISOU 6246  N   ALA B1136    12136   9954   6510   1638    958    940       N  
ATOM   6247  CA  ALA B1136     -12.721   6.415  -4.851  1.00 74.07           C  
ANISOU 6247  CA  ALA B1136    12126   9743   6275   1684    915    782       C  
ATOM   6248  C   ALA B1136     -11.621   7.387  -4.440  1.00 79.84           C  
ANISOU 6248  C   ALA B1136    12893  10494   6949   1600    877    814       C  
ATOM   6249  O   ALA B1136     -11.334   7.532  -3.243  1.00 79.96           O  
ANISOU 6249  O   ALA B1136    12831  10660   6889   1527    812    855       O  
ATOM   6250  CB  ALA B1136     -14.088   7.046  -4.659  1.00 74.49           C  
ANISOU 6250  CB  ALA B1136    12219   9874   6210   1758    868    609       C  
ATOM   6251  N   ILE B1137     -10.962   7.996  -5.441  1.00 77.22           N  
ANISOU 6251  N   ILE B1137    12675  10017   6647   1590    928    794       N  
ATOM   6252  CA  ILE B1137      -9.891   8.977  -5.238  1.00 78.50           C  
ANISOU 6252  CA  ILE B1137    12863  10157   6807   1437    929    797       C  
ATOM   6253  C   ILE B1137     -10.543  10.370  -5.098  1.00 83.80           C  
ANISOU 6253  C   ILE B1137    13789  10715   7336   1440    888    638       C  
ATOM   6254  O   ILE B1137     -11.210  10.796  -6.033  1.00 84.82           O  
ANISOU 6254  O   ILE B1137    14135  10686   7406   1585    930    585       O  
ATOM   6255  CB  ILE B1137      -8.868   8.916  -6.399  1.00 81.98           C  
ANISOU 6255  CB  ILE B1137    13305  10484   7360   1401   1076    874       C  
ATOM   6256  CG1 ILE B1137      -8.247   7.503  -6.524  1.00 82.09           C  
ANISOU 6256  CG1 ILE B1137    13082  10591   7517   1469   1127   1009       C  
ATOM   6257  CG2 ILE B1137      -7.795  10.014  -6.265  1.00 84.42           C  
ANISOU 6257  CG2 ILE B1137    13617  10754   7706   1167   1118    857       C  
ATOM   6258  CD1 ILE B1137      -8.285   6.954  -7.926  1.00 85.69           C  
ANISOU 6258  CD1 ILE B1137    13644  10908   8008   1605   1275   1014       C  
ATOM   6259  N   PRO B1138     -10.401  11.111  -3.981  1.00 80.78           N  
ANISOU 6259  N   PRO B1138    13420  10401   6874   1321    797    547       N  
ATOM   6260  CA  PRO B1138     -11.095  12.395  -3.903  1.00 81.82           C  
ANISOU 6260  CA  PRO B1138    13846  10366   6877   1379    780    378       C  
ATOM   6261  C   PRO B1138     -10.352  13.595  -4.470  1.00 88.53           C  
ANISOU 6261  C   PRO B1138    14948  10923   7767   1222    863    339       C  
ATOM   6262  O   PRO B1138      -9.122  13.704  -4.384  1.00 89.00           O  
ANISOU 6262  O   PRO B1138    14884  10988   7945    950    895    376       O  
ATOM   6263  CB  PRO B1138     -11.366  12.554  -2.405  1.00 84.36           C  
ANISOU 6263  CB  PRO B1138    14097  10890   7066   1341    663    267       C  
ATOM   6264  CG  PRO B1138     -10.233  11.838  -1.745  1.00 89.10           C  
ANISOU 6264  CG  PRO B1138    14418  11710   7727   1156    596    378       C  
ATOM   6265  CD  PRO B1138      -9.688  10.813  -2.720  1.00 83.48           C  
ANISOU 6265  CD  PRO B1138    13539  10982   7198   1178    687    574       C  
ATOM   6266  N   ILE B1139     -11.138  14.511  -5.044  1.00 86.86           N  
ANISOU 6266  N   ILE B1139    15089  10454   7458   1404    905    266       N  
ATOM   6267  CA  ILE B1139     -10.688  15.822  -5.510  1.00 89.38           C  
ANISOU 6267  CA  ILE B1139    15779  10397   7784   1289   1014    233       C  
ATOM   6268  C   ILE B1139     -11.428  16.761  -4.559  1.00 94.72           C  
ANISOU 6268  C   ILE B1139    16675  10984   8332   1384    919     14       C  
ATOM   6269  O   ILE B1139     -12.641  16.947  -4.699  1.00 94.55           O  
ANISOU 6269  O   ILE B1139    16800  10947   8179   1743    880    -45       O  
ATOM   6270  CB  ILE B1139     -10.997  16.133  -6.999  1.00 92.60           C  
ANISOU 6270  CB  ILE B1139    16508  10540   8136   1504   1154    362       C  
ATOM   6271  CG1 ILE B1139     -10.588  14.975  -7.930  1.00 91.41           C  
ANISOU 6271  CG1 ILE B1139    16131  10553   8048   1522   1231    532       C  
ATOM   6272  CG2 ILE B1139     -10.347  17.463  -7.415  1.00 95.72           C  
ANISOU 6272  CG2 ILE B1139    17320  10491   8557   1316   1329    384       C  
ATOM   6273  CD1 ILE B1139     -11.424  14.903  -9.157  1.00 97.38           C  
ANISOU 6273  CD1 ILE B1139    17123  11229   8647   1875   1252    592       C  
ATOM   6274  N   ALA B1140     -10.732  17.251  -3.526  1.00 92.15           N  
ANISOU 6274  N   ALA B1140    16315  10664   8031   1086    861   -135       N  
ATOM   6275  CA  ALA B1140     -11.365  18.097  -2.520  1.00 93.50           C  
ANISOU 6275  CA  ALA B1140    16703  10769   8055   1173    775   -388       C  
ATOM   6276  C   ALA B1140     -10.582  19.350  -2.215  1.00101.07           C  
ANISOU 6276  C   ALA B1140    17962  11368   9071    847    810   -570       C  
ATOM   6277  O   ALA B1140      -9.365  19.374  -2.390  1.00101.66           O  
ANISOU 6277  O   ALA B1140    17906  11403   9318    447    854   -525       O  
ATOM   6278  CB  ALA B1140     -11.606  17.305  -1.241  1.00 92.89           C  
ANISOU 6278  CB  ALA B1140    16287  11148   7859   1188    624   -466       C  
ATOM   6279  N   SER B1141     -11.286  20.392  -1.749  1.00100.34           N  
ANISOU 6279  N   SER B1141    18260  11012   8851   1015    800   -798       N  
ATOM   6280  CA  SER B1141     -10.683  21.660  -1.334  1.00104.59           C  
ANISOU 6280  CA  SER B1141    19162  11140   9439    704    830  -1041       C  
ATOM   6281  C   SER B1141     -10.001  21.470   0.025  1.00105.82           C  
ANISOU 6281  C   SER B1141    19024  11639   9544    370    634  -1285       C  
ATOM   6282  O   SER B1141     -10.548  20.783   0.894  1.00102.56           O  
ANISOU 6282  O   SER B1141    18364  11666   8937    575    496  -1335       O  
ATOM   6283  CB  SER B1141     -11.742  22.756  -1.251  1.00112.69           C  
ANISOU 6283  CB  SER B1141    20727  11767  10323   1079    880  -1220       C  
ATOM   6284  OG  SER B1141     -12.233  23.110  -2.537  1.00125.77           O  
ANISOU 6284  OG  SER B1141    22721  13060  12004   1387   1038   -995       O  
ATOM   6285  N   ALA B1142      -8.803  22.049   0.194  1.00104.40           N  
ANISOU 6285  N   ALA B1142    18856  11285   9527   -151    626  -1428       N  
ATOM   6286  CA  ALA B1142      -8.044  21.930   1.435  1.00106.28           C  
ANISOU 6286  CA  ALA B1142    18800  11881   9702   -485    389  -1691       C  
ATOM   6287  C   ALA B1142      -8.623  22.821   2.559  1.00114.02           C  
ANISOU 6287  C   ALA B1142    20143  12739  10442   -402    277  -2106       C  
ATOM   6288  O   ALA B1142      -8.029  23.838   2.939  1.00118.62           O  
ANISOU 6288  O   ALA B1142    20978  13002  11092   -783    244  -2435       O  
ATOM   6289  CB  ALA B1142      -6.572  22.225   1.184  1.00110.19           C  
ANISOU 6289  CB  ALA B1142    19102  12288  10477  -1090    405  -1738       C  
ATOM   6290  N   VAL B1143      -9.813  22.429   3.071  1.00107.91           N  
ANISOU 6290  N   VAL B1143    19394  12215   9393     93    244  -2106       N  
ATOM   6291  CA  VAL B1143     -10.544  23.127   4.134  1.00110.11           C  
ANISOU 6291  CA  VAL B1143    19991  12457   9387    297    180  -2478       C  
ATOM   6292  C   VAL B1143     -10.835  22.175   5.302  1.00112.60           C  
ANISOU 6292  C   VAL B1143    19948  13453   9383    459     10  -2499       C  
ATOM   6293  O   VAL B1143     -11.280  21.038   5.080  1.00107.61           O  
ANISOU 6293  O   VAL B1143    18978  13186   8724    700     47  -2171       O  
ATOM   6294  CB  VAL B1143     -11.823  23.887   3.647  1.00114.06           C  
ANISOU 6294  CB  VAL B1143    20978  12521   9837    794    375  -2510       C  
ATOM   6295  CG1 VAL B1143     -11.523  24.810   2.465  1.00115.71           C  
ANISOU 6295  CG1 VAL B1143    21617  12027  10321    673    559  -2422       C  
ATOM   6296  CG2 VAL B1143     -12.970  22.933   3.312  1.00109.28           C  
ANISOU 6296  CG2 VAL B1143    20113  12277   9133   1307    442  -2225       C  
ATOM   6297  N   GLY B1144     -10.571  22.662   6.518  1.00113.10           N  
ANISOU 6297  N   GLY B1144    20125  13651   9196    313   -162  -2890       N  
ATOM   6298  CA  GLY B1144     -10.787  21.958   7.780  1.00113.11           C  
ANISOU 6298  CA  GLY B1144    19899  14272   8804    458   -320  -2956       C  
ATOM   6299  C   GLY B1144     -10.288  20.528   7.856  1.00113.68           C  
ANISOU 6299  C   GLY B1144    19428  14898   8868    415   -430  -2579       C  
ATOM   6300  O   GLY B1144      -9.077  20.282   7.879  1.00114.24           O  
ANISOU 6300  O   GLY B1144    19222  15123   9062     48   -621  -2558       O  
ATOM   6301  N   GLY B1145     -11.242  19.600   7.897  1.00107.02           N  
ANISOU 6301  N   GLY B1145    18431  14339   7892    796   -296  -2294       N  
ATOM   6302  CA  GLY B1145     -11.007  18.165   7.998  1.00104.40           C  
ANISOU 6302  CA  GLY B1145    17668  14468   7533    840   -342  -1904       C  
ATOM   6303  C   GLY B1145     -10.458  17.488   6.758  1.00105.96           C  
ANISOU 6303  C   GLY B1145    17594  14535   8131    720   -286  -1551       C  
ATOM   6304  O   GLY B1145      -9.674  16.543   6.885  1.00105.73           O  
ANISOU 6304  O   GLY B1145    17222  14818   8131    619   -410  -1324       O  
ATOM   6305  N   LEU B1146     -10.876  17.942   5.547  1.00100.08           N  
ANISOU 6305  N   LEU B1146    17018  13342   7666    780    -97  -1496       N  
ATOM   6306  CA  LEU B1146     -10.422  17.375   4.269  1.00 96.52           C  
ANISOU 6306  CA  LEU B1146    16370  12745   7557    697     -8  -1187       C  
ATOM   6307  C   LEU B1146      -8.898  17.493   4.145  1.00105.02           C  
ANISOU 6307  C   LEU B1146    17255  13827   8822    276   -145  -1212       C  
ATOM   6308  O   LEU B1146      -8.238  16.502   3.857  1.00103.19           O  
ANISOU 6308  O   LEU B1146    16661  13831   8716    224   -181   -952       O  
ATOM   6309  CB  LEU B1146     -11.136  18.018   3.056  1.00 94.72           C  
ANISOU 6309  CB  LEU B1146    16437  12045   7508    863    195  -1160       C  
ATOM   6310  CG  LEU B1146     -12.676  18.031   3.037  1.00 97.08           C  
ANISOU 6310  CG  LEU B1146    16873  12348   7663   1305    318  -1175       C  
ATOM   6311  CD1 LEU B1146     -13.196  19.005   2.008  1.00 97.40           C  
ANISOU 6311  CD1 LEU B1146    17282  11901   7824   1480    445  -1227       C  
ATOM   6312  CD2 LEU B1146     -13.251  16.655   2.774  1.00 94.84           C  
ANISOU 6312  CD2 LEU B1146    16243  12386   7404   1486    378   -880       C  
ATOM   6313  N   ARG B1147      -8.345  18.682   4.464  1.00108.10           N  
ANISOU 6313  N   ARG B1147    17865  13985   9223    -24   -226  -1555       N  
ATOM   6314  CA  ARG B1147      -6.911  19.022   4.491  1.00112.16           C  
ANISOU 6314  CA  ARG B1147    18178  14517   9922   -505   -365  -1687       C  
ATOM   6315  C   ARG B1147      -6.160  18.167   5.558  1.00119.18           C  
ANISOU 6315  C   ARG B1147    18625  16037  10619   -562   -668  -1682       C  
ATOM   6316  O   ARG B1147      -4.944  17.962   5.443  1.00120.94           O  
ANISOU 6316  O   ARG B1147    18476  16449  11028   -863   -796  -1666       O  
ATOM   6317  CB  ARG B1147      -6.770  20.534   4.785  1.00117.19           C  
ANISOU 6317  CB  ARG B1147    19231  14730  10565   -797   -380  -2126       C  
ATOM   6318  CG  ARG B1147      -5.353  21.097   4.793  1.00129.25           C  
ANISOU 6318  CG  ARG B1147    20574  16205  12328  -1390   -495  -2344       C  
ATOM   6319  CD  ARG B1147      -5.240  22.259   5.763  1.00141.35           C  
ANISOU 6319  CD  ARG B1147    22428  17571  13709  -1658   -660  -2879       C  
ATOM   6320  NE  ARG B1147      -5.585  21.865   7.133  1.00147.51           N  
ANISOU 6320  NE  ARG B1147    23136  18872  14040  -1424   -938  -3061       N  
ATOM   6321  CZ  ARG B1147      -5.621  22.693   8.173  1.00161.29           C  
ANISOU 6321  CZ  ARG B1147    25158  20599  15526  -1551  -1122  -3552       C  
ATOM   6322  NH1 ARG B1147      -5.326  23.979   8.018  1.00151.08           N1+
ANISOU 6322  NH1 ARG B1147    24240  18742  14421  -1940  -1065  -3934       N1+
ATOM   6323  NH2 ARG B1147      -5.949  22.241   9.376  1.00144.07           N  
ANISOU 6323  NH2 ARG B1147    22918  18942  12881  -1292  -1347  -3666       N  
ATOM   6324  N   ASP B1148      -6.903  17.669   6.579  1.00115.61           N  
ANISOU 6324  N   ASP B1148    18215  15928   9784   -243   -765  -1678       N  
ATOM   6325  CA  ASP B1148      -6.414  16.816   7.664  1.00116.74           C  
ANISOU 6325  CA  ASP B1148    18048  16668   9639   -174  -1035  -1615       C  
ATOM   6326  C   ASP B1148      -6.486  15.315   7.286  1.00116.02           C  
ANISOU 6326  C   ASP B1148    17650  16816   9617    100   -952  -1118       C  
ATOM   6327  O   ASP B1148      -5.782  14.507   7.896  1.00117.69           O  
ANISOU 6327  O   ASP B1148    17553  17468   9695    149  -1168   -975       O  
ATOM   6328  CB  ASP B1148      -7.189  17.111   8.961  1.00121.07           C  
ANISOU 6328  CB  ASP B1148    18878  17429   9696     25  -1127  -1856       C  
ATOM   6329  CG  ASP B1148      -6.714  16.354  10.189  1.00139.95           C  
ANISOU 6329  CG  ASP B1148    21044  20445  11686    126  -1420  -1805       C  
ATOM   6330  OD1 ASP B1148      -5.500  16.425  10.505  1.00144.73           O  
ANISOU 6330  OD1 ASP B1148    21368  21314  12308   -134  -1732  -1945       O  
ATOM   6331  OD2 ASP B1148      -7.556  15.700  10.843  1.00147.38           O1-
ANISOU 6331  OD2 ASP B1148    22084  21630  12283    470  -1334  -1621       O1-
ATOM   6332  N   ILE B1149      -7.312  14.948   6.274  1.00106.50           N  
ANISOU 6332  N   ILE B1149    16540  15311   8614    290   -658   -870       N  
ATOM   6333  CA  ILE B1149      -7.440  13.561   5.800  1.00102.16           C  
ANISOU 6333  CA  ILE B1149    15757  14888   8173    514   -549   -446       C  
ATOM   6334  C   ILE B1149      -6.592  13.354   4.535  1.00104.27           C  
ANISOU 6334  C   ILE B1149    15805  14964   8849    360   -463   -297       C  
ATOM   6335  O   ILE B1149      -5.698  12.510   4.523  1.00104.58           O  
ANISOU 6335  O   ILE B1149    15503  15254   8979    366   -561   -103       O  
ATOM   6336  CB  ILE B1149      -8.920  13.139   5.576  1.00101.54           C  
ANISOU 6336  CB  ILE B1149    15870  14684   8028    812   -302   -299       C  
ATOM   6337  CG1 ILE B1149      -9.729  13.202   6.869  1.00103.71           C  
ANISOU 6337  CG1 ILE B1149    16307  15217   7883    981   -328   -406       C  
ATOM   6338  CG2 ILE B1149      -9.017  11.745   4.961  1.00 98.79           C  
ANISOU 6338  CG2 ILE B1149    15311  14373   7852    970   -176     90       C  
ATOM   6339  CD1 ILE B1149     -11.181  13.518   6.638  1.00110.00           C  
ANISOU 6339  CD1 ILE B1149    17326  15828   8642   1183    -86   -473       C  
ATOM   6340  N   ILE B1150      -6.893  14.115   3.476  1.00 98.95           N  
ANISOU 6340  N   ILE B1150    15347  13856   8395    266   -266   -376       N  
ATOM   6341  CA  ILE B1150      -6.229  14.039   2.176  1.00 97.64           C  
ANISOU 6341  CA  ILE B1150    15058  13471   8570    134   -112   -238       C  
ATOM   6342  C   ILE B1150      -4.822  14.629   2.219  1.00107.48           C  
ANISOU 6342  C   ILE B1150    16073  14781   9981   -261   -223   -397       C  
ATOM   6343  O   ILE B1150      -4.633  15.766   2.656  1.00109.82           O  
ANISOU 6343  O   ILE B1150    16542  14947  10237   -533   -304   -711       O  
ATOM   6344  CB  ILE B1150      -7.112  14.663   1.046  1.00 97.95           C  
ANISOU 6344  CB  ILE B1150    15464  13039   8713    220    138   -240       C  
ATOM   6345  CG1 ILE B1150      -8.473  13.954   0.939  1.00 94.39           C  
ANISOU 6345  CG1 ILE B1150    15116  12607   8140    593    226   -100       C  
ATOM   6346  CG2 ILE B1150      -6.403  14.666  -0.316  1.00 97.97           C  
ANISOU 6346  CG2 ILE B1150    15402  12816   9006     84    328    -95       C  
ATOM   6347  CD1 ILE B1150      -9.640  14.895   0.924  1.00 98.53           C  
ANISOU 6347  CD1 ILE B1150    16018  12881   8538    746    297   -284       C  
ATOM   6348  N   THR B1151      -3.845  13.841   1.753  1.00106.75           N  
ANISOU 6348  N   THR B1151    15579  14888  10093   -295   -214   -200       N  
ATOM   6349  CA  THR B1151      -2.446  14.247   1.639  1.00111.92           C  
ANISOU 6349  CA  THR B1151    15885  15672  10968   -672   -279   -321       C  
ATOM   6350  C   THR B1151      -2.029  14.278   0.147  1.00117.66           C  
ANISOU 6350  C   THR B1151    16575  16113  12018   -778     54   -160       C  
ATOM   6351  O   THR B1151      -2.887  14.410  -0.738  1.00114.19           O  
ANISOU 6351  O   THR B1151    16508  15293  11587   -626    297    -51       O  
ATOM   6352  CB  THR B1151      -1.526  13.410   2.560  1.00124.13           C  
ANISOU 6352  CB  THR B1151    16926  17803  12434   -603   -590   -278       C  
ATOM   6353  OG1 THR B1151      -1.697  12.018   2.288  1.00122.80           O  
ANISOU 6353  OG1 THR B1151    16616  17776  12266   -195   -526     82       O  
ATOM   6354  CG2 THR B1151      -1.745  13.707   4.042  1.00125.30           C  
ANISOU 6354  CG2 THR B1151    17152  18238  12218   -594   -927   -509       C  
ATOM   6355  N   ASN B1152      -0.714  14.203  -0.118  1.00119.10           N  
ANISOU 6355  N   ASN B1152    16300  16511  12443  -1033     64   -164       N  
ATOM   6356  CA  ASN B1152      -0.131  14.226  -1.460  1.00119.54           C  
ANISOU 6356  CA  ASN B1152    16259  16375  12785  -1163    410    -18       C  
ATOM   6357  C   ASN B1152      -0.306  12.882  -2.172  1.00120.99           C  
ANISOU 6357  C   ASN B1152    16329  16650  12991   -727    547    305       C  
ATOM   6358  O   ASN B1152      -0.569  12.855  -3.378  1.00118.59           O  
ANISOU 6358  O   ASN B1152    16244  16046  12769   -654    862    448       O  
ATOM   6359  CB  ASN B1152       1.361  14.644  -1.403  1.00125.30           C  
ANISOU 6359  CB  ASN B1152    16465  17362  13780  -1622    391   -172       C  
ATOM   6360  CG  ASN B1152       2.209  13.989  -0.316  1.00144.22           C  
ANISOU 6360  CG  ASN B1152    18264  20394  16138  -1569      2   -249       C  
ATOM   6361  OD1 ASN B1152       1.887  14.018   0.885  1.00134.74           O  
ANISOU 6361  OD1 ASN B1152    17115  19405  14674  -1491   -354   -400       O  
ATOM   6362  ND2 ASN B1152       3.340  13.414  -0.712  1.00136.49           N  
ANISOU 6362  ND2 ASN B1152    16699  19762  15397  -1587     63   -151       N  
ATOM   6363  N   GLU B1153      -0.174  11.774  -1.408  1.00117.85           N  
ANISOU 6363  N   GLU B1153    15634  16648  12494   -423    306    414       N  
ATOM   6364  CA  GLU B1153      -0.248  10.391  -1.892  1.00115.58           C  
ANISOU 6364  CA  GLU B1153    15230  16445  12240     -5    400    697       C  
ATOM   6365  C   GLU B1153      -1.670   9.820  -1.919  1.00114.39           C  
ANISOU 6365  C   GLU B1153    15507  16059  11897    323    431    820       C  
ATOM   6366  O   GLU B1153      -1.925   8.843  -2.635  1.00111.31           O  
ANISOU 6366  O   GLU B1153    15153  15575  11566    600    589   1010       O  
ATOM   6367  CB  GLU B1153       0.662   9.485  -1.041  1.00119.93           C  
ANISOU 6367  CB  GLU B1153    15274  17504  12791    180    136    779       C  
ATOM   6368  CG  GLU B1153       2.153   9.745  -1.201  1.00136.82           C  
ANISOU 6368  CG  GLU B1153    16838  19968  15179    -66    127    685       C  
ATOM   6369  CD  GLU B1153       3.015   9.026  -0.180  1.00165.74           C  
ANISOU 6369  CD  GLU B1153    19985  24199  18788    143   -229    720       C  
ATOM   6370  OE1 GLU B1153       3.101   9.508   0.974  1.00162.25           O1-
ANISOU 6370  OE1 GLU B1153    19473  24019  18155     -1   -581    532       O1-
ATOM   6371  OE2 GLU B1153       3.603   7.978  -0.534  1.00162.31           O  
ANISOU 6371  OE2 GLU B1153    19238  23954  18480    487   -166    929       O  
ATOM   6372  N   THR B1154      -2.588  10.412  -1.137  1.00109.95           N  
ANISOU 6372  N   THR B1154    15247  15415  11112    283    291    685       N  
ATOM   6373  CA  THR B1154      -3.951   9.904  -1.050  1.00106.47           C  
ANISOU 6373  CA  THR B1154    15129  14822  10503    558    322    775       C  
ATOM   6374  C   THR B1154      -4.879  10.497  -2.125  1.00108.59           C  
ANISOU 6374  C   THR B1154    15783  14684  10794    560    546    727       C  
ATOM   6375  O   THR B1154      -5.518   9.729  -2.839  1.00106.84           O  
ANISOU 6375  O   THR B1154    15662  14339  10595    785    674    858       O  
ATOM   6376  CB  THR B1154      -4.504  10.046   0.368  1.00114.70           C  
ANISOU 6376  CB  THR B1154    16257  16058  11265    598     87    685       C  
ATOM   6377  OG1 THR B1154      -3.522   9.591   1.303  1.00116.31           O  
ANISOU 6377  OG1 THR B1154    16112  16672  11409    613   -153    728       O  
ATOM   6378  CG2 THR B1154      -5.761   9.243   0.562  1.00111.65           C  
ANISOU 6378  CG2 THR B1154    16076  15610  10738    877    148    827       C  
ATOM   6379  N   GLY B1155      -4.959  11.822  -2.229  1.00105.16           N  
ANISOU 6379  N   GLY B1155    15578  14038  10342    329    579    536       N  
ATOM   6380  CA  GLY B1155      -5.824  12.462  -3.216  1.00102.74           C  
ANISOU 6380  CA  GLY B1155    15671  13350  10015    395    765    512       C  
ATOM   6381  C   GLY B1155      -5.297  13.750  -3.813  1.00107.21           C  
ANISOU 6381  C   GLY B1155    16438  13620  10676    104    914    410       C  
ATOM   6382  O   GLY B1155      -4.084  14.003  -3.805  1.00109.18           O  
ANISOU 6382  O   GLY B1155    16435  13956  11091   -203    949    383       O  
ATOM   6383  N   ILE B1156      -6.227  14.572  -4.349  1.00101.87           N  
ANISOU 6383  N   ILE B1156    16217  12588   9901    208   1014    361       N  
ATOM   6384  CA  ILE B1156      -5.912  15.860  -4.973  1.00103.73           C  
ANISOU 6384  CA  ILE B1156    16787  12427  10200    -24   1198    304       C  
ATOM   6385  C   ILE B1156      -6.579  17.024  -4.195  1.00106.52           C  
ANISOU 6385  C   ILE B1156    17506  12543  10426    -56   1092     68       C  
ATOM   6386  O   ILE B1156      -7.794  17.235  -4.295  1.00104.47           O  
ANISOU 6386  O   ILE B1156    17555  12140   9998    280   1069     45       O  
ATOM   6387  CB  ILE B1156      -6.209  15.869  -6.518  1.00106.45           C  
ANISOU 6387  CB  ILE B1156    17417  12502  10526    166   1459    501       C  
ATOM   6388  CG1 ILE B1156      -5.333  14.839  -7.281  1.00106.61           C  
ANISOU 6388  CG1 ILE B1156    17091  12738  10680    149   1608    685       C  
ATOM   6389  CG2 ILE B1156      -6.022  17.265  -7.138  1.00110.53           C  
ANISOU 6389  CG2 ILE B1156    18398  12538  11061    -29   1681    493       C  
ATOM   6390  CD1 ILE B1156      -5.962  13.446  -7.504  1.00112.49           C  
ANISOU 6390  CD1 ILE B1156    17671  13717  11354    519   1521    780       C  
ATOM   6391  N   LEU B1157      -5.766  17.757  -3.402  1.00104.79           N  
ANISOU 6391  N   LEU B1157    17220  12307  10289   -454   1016   -140       N  
ATOM   6392  CA  LEU B1157      -6.217  18.920  -2.633  1.00106.53           C  
ANISOU 6392  CA  LEU B1157    17810  12262  10403   -535    929   -420       C  
ATOM   6393  C   LEU B1157      -6.119  20.193  -3.473  1.00114.74           C  
ANISOU 6393  C   LEU B1157    19360  12694  11542   -710   1188   -429       C  
ATOM   6394  O   LEU B1157      -5.158  20.358  -4.230  1.00116.98           O  
ANISOU 6394  O   LEU B1157    19572  12844  12030  -1035   1403   -308       O  
ATOM   6395  CB  LEU B1157      -5.430  19.098  -1.319  1.00108.97           C  
ANISOU 6395  CB  LEU B1157    17839  12847  10719   -886    687   -697       C  
ATOM   6396  CG  LEU B1157      -5.837  18.262  -0.104  1.00110.88           C  
ANISOU 6396  CG  LEU B1157    17811  13588  10730   -656    401   -762       C  
ATOM   6397  CD1 LEU B1157      -5.045  18.674   1.105  1.00115.07           C  
ANISOU 6397  CD1 LEU B1157    18162  14349  11211  -1000    150  -1073       C  
ATOM   6398  CD2 LEU B1157      -7.321  18.389   0.215  1.00110.56           C  
ANISOU 6398  CD2 LEU B1157    18115  13455  10438   -232    389   -813       C  
ATOM   6399  N   VAL B1158      -7.119  21.086  -3.345  1.00112.44           N  
ANISOU 6399  N   VAL B1158    19594  12027  11101   -472   1194   -555       N  
ATOM   6400  CA  VAL B1158      -7.196  22.365  -4.074  1.00115.93           C  
ANISOU 6400  CA  VAL B1158    20649  11803  11595   -545   1439   -544       C  
ATOM   6401  C   VAL B1158      -7.577  23.525  -3.141  1.00122.88           C  
ANISOU 6401  C   VAL B1158    21948  12336  12405   -600   1351   -896       C  
ATOM   6402  O   VAL B1158      -7.491  23.389  -1.918  1.00122.48           O  
ANISOU 6402  O   VAL B1158    21656  12596  12285   -714   1109  -1177       O  
ATOM   6403  CB  VAL B1158      -8.122  22.297  -5.329  1.00118.03           C  
ANISOU 6403  CB  VAL B1158    21266  11853  11727    -37   1599   -252       C  
ATOM   6404  CG1 VAL B1158      -7.491  21.478  -6.448  1.00116.34           C  
ANISOU 6404  CG1 VAL B1158    20794  11811  11600    -97   1775     60       C  
ATOM   6405  CG2 VAL B1158      -9.522  21.782  -4.987  1.00114.23           C  
ANISOU 6405  CG2 VAL B1158    20749  11643  11009    546   1392   -294       C  
ATOM   6406  N   LYS B1159      -7.987  24.664  -3.722  1.00122.86           N  
ANISOU 6406  N   LYS B1159    22610  11675  12396   -491   1554   -878       N  
ATOM   6407  CA  LYS B1159      -8.448  25.821  -2.963  1.00126.61           C  
ANISOU 6407  CA  LYS B1159    23590  11715  12802   -459   1511  -1211       C  
ATOM   6408  C   LYS B1159      -9.917  26.085  -3.267  1.00129.35           C  
ANISOU 6408  C   LYS B1159    24357  11880  12910    277   1513  -1141       C  
ATOM   6409  O   LYS B1159     -10.306  26.147  -4.439  1.00129.16           O  
ANISOU 6409  O   LYS B1159    24605  11623  12848    594   1679   -825       O  
ATOM   6410  CB  LYS B1159      -7.564  27.060  -3.194  1.00135.26           C  
ANISOU 6410  CB  LYS B1159    25140  12119  14134  -1019   1750  -1316       C  
ATOM   6411  CG  LYS B1159      -6.245  27.043  -2.409  1.00146.75           C  
ANISOU 6411  CG  LYS B1159    26152  13795  15810  -1773   1647  -1597       C  
ATOM   6412  CD  LYS B1159      -6.413  27.343  -0.910  1.00152.25           C  
ANISOU 6412  CD  LYS B1159    26818  14655  16376  -1848   1336  -2098       C  
ATOM   6413  CE  LYS B1159      -6.220  26.117  -0.050  1.00147.78           C  
ANISOU 6413  CE  LYS B1159    25513  14961  15676  -1808   1007  -2158       C  
ATOM   6414  NZ  LYS B1159      -6.791  26.309   1.306  1.00153.40           N1+
ANISOU 6414  NZ  LYS B1159    26302  15869  16116  -1633    732  -2562       N1+
ATOM   6415  N   ALA B1160     -10.735  26.169  -2.202  1.00124.70           N  
ANISOU 6415  N   ALA B1160    23769  11477  12134    575   1316  -1438       N  
ATOM   6416  CA  ALA B1160     -12.176  26.380  -2.279  1.00123.81           C  
ANISOU 6416  CA  ALA B1160    23929  11314  11798   1296   1289  -1443       C  
ATOM   6417  C   ALA B1160     -12.537  27.742  -2.856  1.00132.98           C  
ANISOU 6417  C   ALA B1160    25894  11669  12963   1535   1483  -1440       C  
ATOM   6418  O   ALA B1160     -11.968  28.762  -2.451  1.00137.52           O  
ANISOU 6418  O   ALA B1160    26896  11703  13652   1167   1575  -1677       O  
ATOM   6419  CB  ALA B1160     -12.799  26.206  -0.905  1.00124.19           C  
ANISOU 6419  CB  ALA B1160    23772  11758  11656   1476   1091  -1789       C  
ATOM   6420  N   GLY B1161     -13.464  27.733  -3.811  1.00129.05           N  
ANISOU 6420  N   GLY B1161    25604  11092  12336   2147   1533  -1174       N  
ATOM   6421  CA  GLY B1161     -13.964  28.943  -4.453  1.00134.23           C  
ANISOU 6421  CA  GLY B1161    27049  11012  12938   2545   1700  -1097       C  
ATOM   6422  C   GLY B1161     -13.491  29.237  -5.863  1.00139.76           C  
ANISOU 6422  C   GLY B1161    28146  11261  13697   2484   1941   -678       C  
ATOM   6423  O   GLY B1161     -14.047  30.136  -6.501  1.00144.01           O  
ANISOU 6423  O   GLY B1161    29360  11230  14129   2948   2066   -537       O  
ATOM   6424  N   ASP B1162     -12.460  28.521  -6.359  1.00132.98           N  
ANISOU 6424  N   ASP B1162    26910  10635  12983   1951   2028   -467       N  
ATOM   6425  CA  ASP B1162     -11.947  28.747  -7.713  1.00134.79           C  
ANISOU 6425  CA  ASP B1162    27497  10484  13233   1866   2308    -56       C  
ATOM   6426  C   ASP B1162     -12.351  27.616  -8.680  1.00134.20           C  
ANISOU 6426  C   ASP B1162    27036  10971  12983   2243   2221    252       C  
ATOM   6427  O   ASP B1162     -11.839  26.494  -8.552  1.00129.79           O  
ANISOU 6427  O   ASP B1162    25809  10993  12512   1935   2135    254       O  
ATOM   6428  CB  ASP B1162     -10.428  29.017  -7.720  1.00139.34           C  
ANISOU 6428  CB  ASP B1162    28056  10776  14110    981   2565    -44       C  
ATOM   6429  CG  ASP B1162     -10.024  30.249  -8.520  1.00159.17           C  
ANISOU 6429  CG  ASP B1162    31406  12379  16690    821   2956    179       C  
ATOM   6430  OD1 ASP B1162      -9.932  30.147  -9.769  1.00161.01           O  
ANISOU 6430  OD1 ASP B1162    31869  12496  16812    981   3179    606       O  
ATOM   6431  OD2 ASP B1162      -9.794  31.313  -7.900  1.00168.97           O1-
ANISOU 6431  OD2 ASP B1162    33110  13008  18084    528   3054    -74       O1-
ATOM   6432  N   PRO B1163     -13.288  27.882  -9.635  1.00131.72           N  
ANISOU 6432  N   PRO B1163    27141  10501  12406   2938   2219    492       N  
ATOM   6433  CA  PRO B1163     -13.702  26.828 -10.585  1.00127.46           C  
ANISOU 6433  CA  PRO B1163    26257  10500  11674   3290   2104    728       C  
ATOM   6434  C   PRO B1163     -12.593  26.428 -11.558  1.00130.36           C  
ANISOU 6434  C   PRO B1163    26592  10844  12094   2855   2369   1036       C  
ATOM   6435  O   PRO B1163     -12.585  25.296 -12.030  1.00125.49           O  
ANISOU 6435  O   PRO B1163    25495  10774  11410   2904   2272   1123       O  
ATOM   6436  CB  PRO B1163     -14.900  27.452 -11.320  1.00132.55           C  
ANISOU 6436  CB  PRO B1163    27441  10916  12006   4134   2025    875       C  
ATOM   6437  CG  PRO B1163     -15.275  28.665 -10.538  1.00141.61           C  
ANISOU 6437  CG  PRO B1163    29097  11508  13200   4300   2055    666       C  
ATOM   6438  CD  PRO B1163     -14.005  29.140  -9.913  1.00139.02           C  
ANISOU 6438  CD  PRO B1163    28883  10758  13180   3466   2300    550       C  
ATOM   6439  N   GLY B1164     -11.675  27.358 -11.833  1.00131.63           N  
ANISOU 6439  N   GLY B1164    27265  10362  12386   2423   2725   1181       N  
ATOM   6440  CA  GLY B1164     -10.526  27.158 -12.711  1.00132.45           C  
ANISOU 6440  CA  GLY B1164    27376  10383  12565   1950   3070   1472       C  
ATOM   6441  C   GLY B1164      -9.484  26.232 -12.122  1.00131.90           C  
ANISOU 6441  C   GLY B1164    26519  10809  12788   1295   3057   1310       C  
ATOM   6442  O   GLY B1164      -8.804  25.522 -12.865  1.00129.72           O  
ANISOU 6442  O   GLY B1164    25970  10800  12516   1104   3224   1514       O  
ATOM   6443  N   GLU B1165      -9.357  26.243 -10.779  1.00127.52           N  
ANISOU 6443  N   GLU B1165    25612  10391  12449    992   2854    938       N  
ATOM   6444  CA  GLU B1165      -8.447  25.397 -10.004  1.00124.64           C  
ANISOU 6444  CA  GLU B1165    24489  10534  12335    446   2758    746       C  
ATOM   6445  C   GLU B1165      -9.036  23.978  -9.869  1.00123.15           C  
ANISOU 6445  C   GLU B1165    23680  11088  12024    807   2450    715       C  
ATOM   6446  O   GLU B1165      -8.280  23.000  -9.822  1.00119.91           O  
ANISOU 6446  O   GLU B1165    22693  11122  11745    517   2443    735       O  
ATOM   6447  CB  GLU B1165      -8.208  26.011  -8.620  1.00127.96           C  
ANISOU 6447  CB  GLU B1165    24859  10816  12945     69   2622    353       C  
ATOM   6448  CG  GLU B1165      -6.836  25.706  -8.040  1.00140.49           C  
ANISOU 6448  CG  GLU B1165    25893  12651  14838   -682   2659    202       C  
ATOM   6449  CD  GLU B1165      -6.394  26.547  -6.853  1.00166.58           C  
ANISOU 6449  CD  GLU B1165    29260  15707  18326  -1166   2574   -197       C  
ATOM   6450  OE1 GLU B1165      -7.066  27.556  -6.537  1.00163.49           O  
ANISOU 6450  OE1 GLU B1165    29471  14793  17854   -972   2567   -352       O  
ATOM   6451  OE2 GLU B1165      -5.357  26.199  -6.244  1.00161.07           O1-
ANISOU 6451  OE2 GLU B1165    28007  15347  17846  -1724   2503   -374       O1-
ATOM   6452  N   LEU B1166     -10.388  23.877  -9.803  1.00118.15           N  
ANISOU 6452  N   LEU B1166    23163  10573  11155   1439   2209    659       N  
ATOM   6453  CA  LEU B1166     -11.124  22.612  -9.718  1.00112.54           C  
ANISOU 6453  CA  LEU B1166    21932  10494  10333   1785   1939    619       C  
ATOM   6454  C   LEU B1166     -11.190  21.950 -11.102  1.00114.65           C  
ANISOU 6454  C   LEU B1166    22213  10908  10441   2036   2028    902       C  
ATOM   6455  O   LEU B1166     -11.027  20.732 -11.198  1.00110.15           O  
ANISOU 6455  O   LEU B1166    21133  10813   9907   1990   1941    909       O  
ATOM   6456  CB  LEU B1166     -12.537  22.826  -9.132  1.00112.13           C  
ANISOU 6456  CB  LEU B1166    21957  10531  10115   2322   1682    425       C  
ATOM   6457  CG  LEU B1166     -13.437  21.583  -8.986  1.00112.73           C  
ANISOU 6457  CG  LEU B1166    21496  11235  10100   2648   1424    356       C  
ATOM   6458  CD1 LEU B1166     -12.886  20.591  -7.952  1.00109.72           C  
ANISOU 6458  CD1 LEU B1166    20497  11297   9893   2248   1327    220       C  
ATOM   6459  CD2 LEU B1166     -14.846  21.974  -8.619  1.00116.10           C  
ANISOU 6459  CD2 LEU B1166    22035  11715  10361   3203   1240    191       C  
ATOM   6460  N   ALA B1167     -11.412  22.757 -12.170  1.00114.51           N  
ANISOU 6460  N   ALA B1167    22823  10461  10224   2315   2207   1133       N  
ATOM   6461  CA  ALA B1167     -11.443  22.289 -13.560  1.00114.19           C  
ANISOU 6461  CA  ALA B1167    22913  10521   9953   2576   2311   1404       C  
ATOM   6462  C   ALA B1167     -10.051  21.780 -13.951  1.00117.48           C  
ANISOU 6462  C   ALA B1167    23077  11017  10543   2036   2607   1543       C  
ATOM   6463  O   ALA B1167      -9.949  20.793 -14.683  1.00114.78           O  
ANISOU 6463  O   ALA B1167    22486  11029  10096   2147   2611   1633       O  
ATOM   6464  CB  ALA B1167     -11.872  23.413 -14.492  1.00120.07           C  
ANISOU 6464  CB  ALA B1167    24461  10739  10420   2975   2464   1648       C  
ATOM   6465  N   ASN B1168      -8.985  22.435 -13.425  1.00116.16           N  
ANISOU 6465  N   ASN B1168    22937  10546  10654   1447   2846   1521       N  
ATOM   6466  CA  ASN B1168      -7.585  22.063 -13.639  1.00116.36           C  
ANISOU 6466  CA  ASN B1168    22633  10674  10905    883   3139   1613       C  
ATOM   6467  C   ASN B1168      -7.281  20.754 -12.916  1.00114.47           C  
ANISOU 6467  C   ASN B1168    21597  11055  10843    743   2905   1423       C  
ATOM   6468  O   ASN B1168      -6.519  19.934 -13.432  1.00113.62           O  
ANISOU 6468  O   ASN B1168    21146  11229  10797    600   3058   1527       O  
ATOM   6469  CB  ASN B1168      -6.651  23.164 -13.146  1.00121.40           C  
ANISOU 6469  CB  ASN B1168    23459  10848  11819    275   3398   1570       C  
ATOM   6470  CG  ASN B1168      -5.283  23.112 -13.764  1.00143.21           C  
ANISOU 6470  CG  ASN B1168    26061  13590  14761   -253   3825   1751       C  
ATOM   6471  OD1 ASN B1168      -4.986  23.829 -14.728  1.00136.85           O  
ANISOU 6471  OD1 ASN B1168    25792  12347  13858   -323   4229   2034       O  
ATOM   6472  ND2 ASN B1168      -4.416  22.262 -13.222  1.00133.24           N  
ANISOU 6472  ND2 ASN B1168    24056  12813  13757   -615   3764   1607       N  
ATOM   6473  N   ALA B1169      -7.883  20.559 -11.722  1.00107.12           N  
ANISOU 6473  N   ALA B1169    20403  10323   9975    818   2556   1158       N  
ATOM   6474  CA  ALA B1169      -7.728  19.345 -10.921  1.00102.04           C  
ANISOU 6474  CA  ALA B1169    19083  10226   9461    742   2317   1005       C  
ATOM   6475  C   ALA B1169      -8.459  18.196 -11.597  1.00101.23           C  
ANISOU 6475  C   ALA B1169    18826  10460   9179   1184   2193   1077       C  
ATOM   6476  O   ALA B1169      -7.916  17.097 -11.643  1.00 98.50           O  
ANISOU 6476  O   ALA B1169    18032  10458   8936   1090   2194   1097       O  
ATOM   6477  CB  ALA B1169      -8.265  19.566  -9.523  1.00101.70           C  
ANISOU 6477  CB  ALA B1169    18919  10262   9461    736   2028    734       C  
ATOM   6478  N   ILE B1170      -9.669  18.460 -12.159  1.00 97.37           N  
ANISOU 6478  N   ILE B1170    18710   9864   8424   1675   2083   1103       N  
ATOM   6479  CA  ILE B1170     -10.465  17.488 -12.924  1.00 94.51           C  
ANISOU 6479  CA  ILE B1170    18248   9796   7865   2091   1943   1127       C  
ATOM   6480  C   ILE B1170      -9.663  17.126 -14.192  1.00100.41           C  
ANISOU 6480  C   ILE B1170    19090  10531   8530   2041   2223   1339       C  
ATOM   6481  O   ILE B1170      -9.602  15.948 -14.558  1.00 98.13           O  
ANISOU 6481  O   ILE B1170    18487  10564   8235   2115   2177   1316       O  
ATOM   6482  CB  ILE B1170     -11.908  18.005 -13.233  1.00 97.88           C  
ANISOU 6482  CB  ILE B1170    19027  10145   8020   2632   1738   1080       C  
ATOM   6483  CG1 ILE B1170     -12.765  18.059 -11.957  1.00 95.76           C  
ANISOU 6483  CG1 ILE B1170    18529  10024   7833   2718   1475    837       C  
ATOM   6484  CG2 ILE B1170     -12.608  17.143 -14.292  1.00 97.99           C  
ANISOU 6484  CG2 ILE B1170    18997  10437   7798   3025   1611   1100       C  
ATOM   6485  CD1 ILE B1170     -13.976  18.992 -12.019  1.00100.12           C  
ANISOU 6485  CD1 ILE B1170    19461  10403   8179   3203   1337    776       C  
ATOM   6486  N   LEU B1171      -8.992  18.129 -14.810  1.00101.47           N  
ANISOU 6486  N   LEU B1171    19664  10275   8617   1882   2549   1540       N  
ATOM   6487  CA  LEU B1171      -8.138  17.916 -15.990  1.00104.14           C  
ANISOU 6487  CA  LEU B1171    20121  10590   8859   1800   2901   1764       C  
ATOM   6488  C   LEU B1171      -6.818  17.216 -15.612  1.00107.96           C  
ANISOU 6488  C   LEU B1171    20043  11311   9666   1330   3079   1739       C  
ATOM   6489  O   LEU B1171      -6.145  16.692 -16.504  1.00109.89           O  
ANISOU 6489  O   LEU B1171    20226  11676   9852   1311   3343   1870       O  
ATOM   6490  CB  LEU B1171      -7.886  19.212 -16.790  1.00109.51           C  
ANISOU 6490  CB  LEU B1171    21484  10759   9364   1779   3246   2027       C  
ATOM   6491  N   LYS B1172      -6.455  17.204 -14.299  1.00101.87           N  
ANISOU 6491  N   LYS B1172    18862  10637   9206    996   2926   1563       N  
ATOM   6492  CA  LYS B1172      -5.272  16.495 -13.787  1.00100.97           C  
ANISOU 6492  CA  LYS B1172    18145  10823   9395    623   3002   1514       C  
ATOM   6493  C   LYS B1172      -5.682  15.043 -13.434  1.00 99.82           C  
ANISOU 6493  C   LYS B1172    17561  11101   9265    880   2718   1397       C  
ATOM   6494  O   LYS B1172      -4.856  14.125 -13.521  1.00 99.24           O  
ANISOU 6494  O   LYS B1172    17074  11297   9336    795   2813   1419       O  
ATOM   6495  CB  LYS B1172      -4.641  17.214 -12.571  1.00104.63           C  
ANISOU 6495  CB  LYS B1172    18405  11210  10141    150   2949   1372       C  
ATOM   6496  CG  LYS B1172      -3.306  16.593 -12.124  1.00111.73           C  
ANISOU 6496  CG  LYS B1172    18657  12456  11340   -225   3026   1332       C  
ATOM   6497  CD  LYS B1172      -2.654  17.307 -10.953  1.00118.35           C  
ANISOU 6497  CD  LYS B1172    19266  13274  12429   -706   2928   1147       C  
ATOM   6498  CE  LYS B1172      -1.480  16.512 -10.430  1.00122.14           C  
ANISOU 6498  CE  LYS B1172    19021  14220  13166   -952   2891   1086       C  
ATOM   6499  NZ  LYS B1172      -0.778  17.216  -9.326  1.00131.89           N1+
ANISOU 6499  NZ  LYS B1172    19993  15495  14624  -1445   2761    867       N1+
ATOM   6500  N   ALA B1173      -6.966  14.858 -13.045  1.00 91.84           N  
ANISOU 6500  N   ALA B1173    16650  10130   8117   1198   2396   1277       N  
ATOM   6501  CA  ALA B1173      -7.579  13.578 -12.711  1.00 87.35           C  
ANISOU 6501  CA  ALA B1173    15755   9878   7554   1423   2143   1167       C  
ATOM   6502  C   ALA B1173      -7.665  12.712 -13.985  1.00 91.41           C  
ANISOU 6502  C   ALA B1173    16338  10483   7911   1686   2251   1230       C  
ATOM   6503  O   ALA B1173      -7.297  11.528 -13.961  1.00 88.82           O  
ANISOU 6503  O   ALA B1173    15670  10378   7699   1700   2245   1200       O  
ATOM   6504  CB  ALA B1173      -8.959  13.813 -12.126  1.00 86.13           C  
ANISOU 6504  CB  ALA B1173    15727   9717   7282   1663   1848   1027       C  
ATOM   6505  N   LEU B1174      -8.086  13.332 -15.109  1.00 91.16           N  
ANISOU 6505  N   LEU B1174    16783  10259   7594   1908   2363   1320       N  
ATOM   6506  CA  LEU B1174      -8.165  12.692 -16.426  1.00 92.54           C  
ANISOU 6506  CA  LEU B1174    17120  10510   7529   2175   2473   1362       C  
ATOM   6507  C   LEU B1174      -6.755  12.259 -16.911  1.00 97.54           C  
ANISOU 6507  C   LEU B1174    17566  11212   8282   1964   2841   1481       C  
ATOM   6508  O   LEU B1174      -6.597  11.144 -17.411  1.00 96.25           O  
ANISOU 6508  O   LEU B1174    17239  11238   8095   2109   2870   1419       O  
ATOM   6509  CB  LEU B1174      -8.831  13.647 -17.424  1.00 95.77           C  
ANISOU 6509  CB  LEU B1174    18127  10701   7560   2468   2513   1470       C  
ATOM   6510  CG  LEU B1174      -9.327  13.050 -18.736  1.00102.62           C  
ANISOU 6510  CG  LEU B1174    19228  11699   8065   2854   2487   1449       C  
ATOM   6511  CD1 LEU B1174     -10.534  12.182 -18.513  1.00100.90           C  
ANISOU 6511  CD1 LEU B1174    18794  11728   7817   3103   2072   1184       C  
ATOM   6512  CD2 LEU B1174      -9.699  14.149 -19.715  1.00108.96           C  
ANISOU 6512  CD2 LEU B1174    20670  12268   8462   3132   2589   1638       C  
ATOM   6513  N   GLU B1175      -5.730  13.123 -16.703  1.00 95.83           N  
ANISOU 6513  N   GLU B1175    17341  10848   8224   1606   3124   1621       N  
ATOM   6514  CA  GLU B1175      -4.325  12.859 -17.041  1.00 97.43           C  
ANISOU 6514  CA  GLU B1175    17271  11156   8591   1355   3502   1726       C  
ATOM   6515  C   GLU B1175      -3.835  11.620 -16.273  1.00 97.03           C  
ANISOU 6515  C   GLU B1175    16606  11431   8829   1315   3358   1598       C  
ATOM   6516  O   GLU B1175      -3.169  10.763 -16.860  1.00 96.23           O  
ANISOU 6516  O   GLU B1175    16306  11505   8751   1409   3561   1617       O  
ATOM   6517  CB  GLU B1175      -3.456  14.089 -16.695  1.00102.27           C  
ANISOU 6517  CB  GLU B1175    17912  11556   9390    892   3762   1841       C  
ATOM   6518  CG  GLU B1175      -2.004  14.027 -17.164  1.00118.71           C  
ANISOU 6518  CG  GLU B1175    19710  13753  11642    590   4220   1962       C  
ATOM   6519  CD  GLU B1175      -1.689  14.586 -18.545  1.00147.64           C  
ANISOU 6519  CD  GLU B1175    23843  17221  15035    615   4706   2198       C  
ATOM   6520  OE1 GLU B1175      -2.615  15.094 -19.218  1.00152.93           O1-
ANISOU 6520  OE1 GLU B1175    25135  17634  15336    907   4670   2294       O1-
ATOM   6521  OE2 GLU B1175      -0.506  14.517 -18.953  1.00136.40           O  
ANISOU 6521  OE2 GLU B1175    22152  15925  13749    362   5133   2297       O  
ATOM   6522  N   LEU B1176      -4.200  11.524 -14.966  1.00 90.67           N  
ANISOU 6522  N   LEU B1176    15544  10696   8211   1223   3016   1476       N  
ATOM   6523  CA  LEU B1176      -3.821  10.427 -14.076  1.00 88.33           C  
ANISOU 6523  CA  LEU B1176    14729  10675   8156   1216   2843   1395       C  
ATOM   6524  C   LEU B1176      -4.505   9.121 -14.411  1.00 89.17           C  
ANISOU 6524  C   LEU B1176    14830  10872   8177   1567   2704   1314       C  
ATOM   6525  O   LEU B1176      -3.872   8.068 -14.327  1.00 87.91           O  
ANISOU 6525  O   LEU B1176    14348  10881   8173   1640   2753   1311       O  
ATOM   6526  CB  LEU B1176      -4.091  10.783 -12.612  1.00 86.92           C  
ANISOU 6526  CB  LEU B1176    14370  10538   8118   1036   2536   1306       C  
ATOM   6527  CG  LEU B1176      -2.982  11.508 -11.852  1.00 94.52           C  
ANISOU 6527  CG  LEU B1176    15038  11570   9306    627   2599   1308       C  
ATOM   6528  CD1 LEU B1176      -3.497  12.014 -10.506  1.00 93.27           C  
ANISOU 6528  CD1 LEU B1176    14857  11409   9171    500   2276   1179       C  
ATOM   6529  CD2 LEU B1176      -1.762  10.607 -11.642  1.00 99.15           C  
ANISOU 6529  CD2 LEU B1176    15063  12486  10124    579   2677   1340       C  
ATOM   6530  N   SER B1177      -5.791   9.187 -14.790  1.00 85.54           N  
ANISOU 6530  N   SER B1177    14721  10297   7483   1789   2527   1233       N  
ATOM   6531  CA  SER B1177      -6.601   8.013 -15.121  1.00 84.96           C  
ANISOU 6531  CA  SER B1177    14662  10284   7334   2063   2367   1100       C  
ATOM   6532  C   SER B1177      -6.112   7.206 -16.341  1.00 93.44           C  
ANISOU 6532  C   SER B1177    15811  11389   8305   2252   2602   1086       C  
ATOM   6533  O   SER B1177      -6.371   6.003 -16.415  1.00 93.43           O  
ANISOU 6533  O   SER B1177    15709  11431   8358   2406   2515    961       O  
ATOM   6534  CB  SER B1177      -8.058   8.409 -15.294  1.00 87.82           C  
ANISOU 6534  CB  SER B1177    15323  10573   7471   2233   2119    987       C  
ATOM   6535  OG  SER B1177      -8.164   9.313 -16.377  1.00101.02           O  
ANISOU 6535  OG  SER B1177    17414  12119   8851   2353   2259   1060       O  
ATOM   6536  N   ARG B1178      -5.396   7.861 -17.276  1.00 92.88           N  
ANISOU 6536  N   ARG B1178    15935  11273   8081   2231   2929   1210       N  
ATOM   6537  CA  ARG B1178      -4.828   7.261 -18.488  1.00 95.02           C  
ANISOU 6537  CA  ARG B1178    16313  11595   8197   2417   3225   1207       C  
ATOM   6538  C   ARG B1178      -3.846   6.125 -18.196  1.00100.29           C  
ANISOU 6538  C   ARG B1178    16551  12407   9147   2434   3355   1182       C  
ATOM   6539  O   ARG B1178      -3.611   5.291 -19.070  1.00101.50           O  
ANISOU 6539  O   ARG B1178    16781  12595   9190   2667   3525   1097       O  
ATOM   6540  CB  ARG B1178      -4.166   8.338 -19.348  1.00 97.33           C  
ANISOU 6540  CB  ARG B1178    16876  11815   8291   2326   3609   1401       C  
ATOM   6541  CG  ARG B1178      -5.161   9.349 -19.872  1.00100.61           C  
ANISOU 6541  CG  ARG B1178    17824  12050   8351   2440   3501   1449       C  
ATOM   6542  CD  ARG B1178      -4.484  10.510 -20.544  1.00107.97           C  
ANISOU 6542  CD  ARG B1178    19067  12833   9123   2298   3909   1700       C  
ATOM   6543  NE  ARG B1178      -5.379  11.661 -20.623  1.00116.05           N  
ANISOU 6543  NE  ARG B1178    20565  13618   9911   2367   3764   1787       N  
ATOM   6544  CZ  ARG B1178      -6.269  11.859 -21.590  1.00130.80           C  
ANISOU 6544  CZ  ARG B1178    22936  15436  11325   2741   3669   1794       C  
ATOM   6545  NH1 ARG B1178      -6.392  10.982 -22.579  1.00117.87           N1+
ANISOU 6545  NH1 ARG B1178    21405  13977   9402   3039   3698   1688       N1+
ATOM   6546  NH2 ARG B1178      -7.042  12.937 -21.577  1.00119.03           N  
ANISOU 6546  NH2 ARG B1178    21856  13725   9645   2850   3529   1890       N  
ATOM   6547  N   SER B1179      -3.284   6.097 -16.971  1.00 96.70           N  
ANISOU 6547  N   SER B1179    15668  12045   9030   2228   3264   1244       N  
ATOM   6548  CA  SER B1179      -2.372   5.065 -16.474  1.00 97.55           C  
ANISOU 6548  CA  SER B1179    15333  12310   9423   2291   3320   1249       C  
ATOM   6549  C   SER B1179      -3.070   4.320 -15.331  1.00 99.13           C  
ANISOU 6549  C   SER B1179    15397  12486   9782   2332   2947   1185       C  
ATOM   6550  O   SER B1179      -4.194   4.672 -14.978  1.00 96.05           O  
ANISOU 6550  O   SER B1179    15211  11994   9290   2275   2691   1124       O  
ATOM   6551  CB  SER B1179      -1.070   5.695 -15.989  1.00103.55           C  
ANISOU 6551  CB  SER B1179    15679  13256  10408   2028   3511   1388       C  
ATOM   6552  OG  SER B1179      -0.111   4.704 -15.662  1.00113.48           O  
ANISOU 6552  OG  SER B1179    16488  14717  11911   2175   3582   1400       O  
ATOM   6553  N   ASP B1180      -2.428   3.288 -14.767  1.00 97.78           N  
ANISOU 6553  N   ASP B1180    14895  12409   9846   2456   2936   1212       N  
ATOM   6554  CA  ASP B1180      -3.013   2.513 -13.678  1.00 96.40           C  
ANISOU 6554  CA  ASP B1180    14632  12187   9807   2504   2640   1205       C  
ATOM   6555  C   ASP B1180      -3.216   3.359 -12.423  1.00 98.69           C  
ANISOU 6555  C   ASP B1180    14775  12579  10143   2245   2400   1281       C  
ATOM   6556  O   ASP B1180      -2.250   3.899 -11.876  1.00 99.50           O  
ANISOU 6556  O   ASP B1180    14561  12882  10363   2094   2427   1372       O  
ATOM   6557  CB  ASP B1180      -2.180   1.250 -13.382  1.00100.92           C  
ANISOU 6557  CB  ASP B1180    14936  12810  10599   2755   2707   1263       C  
ATOM   6558  CG  ASP B1180      -2.692   0.414 -12.222  1.00112.90           C  
ANISOU 6558  CG  ASP B1180    16408  14247  12243   2817   2448   1321       C  
ATOM   6559  OD1 ASP B1180      -3.791  -0.179 -12.354  1.00111.24           O  
ANISOU 6559  OD1 ASP B1180    16488  13797  11981   2849   2352   1212       O  
ATOM   6560  OD2 ASP B1180      -1.993   0.349 -11.182  1.00122.84           O1-
ANISOU 6560  OD2 ASP B1180    17335  15697  13640   2824   2344   1474       O1-
ATOM   6561  N   LEU B1181      -4.488   3.480 -11.991  1.00 93.34           N  
ANISOU 6561  N   LEU B1181    14313  11785   9368   2190   2168   1211       N  
ATOM   6562  CA  LEU B1181      -4.883   4.222 -10.787  1.00 91.92           C  
ANISOU 6562  CA  LEU B1181    14058  11684   9183   1988   1942   1243       C  
ATOM   6563  C   LEU B1181      -5.027   3.332  -9.546  1.00 96.93           C  
ANISOU 6563  C   LEU B1181    14515  12384   9931   2046   1757   1322       C  
ATOM   6564  O   LEU B1181      -5.322   3.862  -8.478  1.00 95.46           O  
ANISOU 6564  O   LEU B1181    14269  12298   9706   1907   1577   1345       O  
ATOM   6565  CB  LEU B1181      -6.220   4.950 -11.009  1.00 89.75           C  
ANISOU 6565  CB  LEU B1181    14106  11281   8714   1935   1825   1124       C  
ATOM   6566  CG  LEU B1181      -6.241   6.234 -11.813  1.00 94.56           C  
ANISOU 6566  CG  LEU B1181    14957  11814   9157   1852   1934   1099       C  
ATOM   6567  CD1 LEU B1181      -7.627   6.853 -11.761  1.00 92.72           C  
ANISOU 6567  CD1 LEU B1181    14990  11492   8748   1883   1753    991       C  
ATOM   6568  CD2 LEU B1181      -5.204   7.230 -11.310  1.00 99.09           C  
ANISOU 6568  CD2 LEU B1181    15363  12468   9818   1600   2011   1185       C  
ATOM   6569  N   SER B1182      -4.849   1.994  -9.682  1.00 96.11           N  
ANISOU 6569  N   SER B1182    14376  12196   9943   2267   1817   1366       N  
ATOM   6570  CA  SER B1182      -5.014   1.000  -8.604  1.00 96.54           C  
ANISOU 6570  CA  SER B1182    14352  12236  10092   2366   1691   1491       C  
ATOM   6571  C   SER B1182      -4.220   1.278  -7.325  1.00100.48           C  
ANISOU 6571  C   SER B1182    14550  13011  10615   2333   1541   1653       C  
ATOM   6572  O   SER B1182      -4.714   0.963  -6.244  1.00100.01           O  
ANISOU 6572  O   SER B1182    14513  12977  10511   2330   1390   1750       O  
ATOM   6573  CB  SER B1182      -4.710  -0.408  -9.103  1.00102.78           C  
ANISOU 6573  CB  SER B1182    15195  12832  11025   2637   1831   1520       C  
ATOM   6574  OG  SER B1182      -5.065  -1.369  -8.122  1.00115.69           O  
ANISOU 6574  OG  SER B1182    16865  14358  12734   2720   1739   1663       O  
ATOM   6575  N   LYS B1183      -3.001   1.843  -7.448  1.00 97.66           N  
ANISOU 6575  N   LYS B1183    13905  12885  10317   2301   1589   1673       N  
ATOM   6576  CA  LYS B1183      -2.126   2.190  -6.321  1.00 98.31           C  
ANISOU 6576  CA  LYS B1183    13636  13300  10416   2250   1408   1768       C  
ATOM   6577  C   LYS B1183      -2.719   3.359  -5.531  1.00 98.23           C  
ANISOU 6577  C   LYS B1183    13705  13372  10246   1950   1222   1678       C  
ATOM   6578  O   LYS B1183      -2.655   3.356  -4.309  1.00 98.78           O  
ANISOU 6578  O   LYS B1183    13660  13641  10232   1946   1001   1744       O  
ATOM   6579  CB  LYS B1183      -0.699   2.521  -6.807  1.00103.79           C  
ANISOU 6579  CB  LYS B1183    13945  14236  11252   2239   1536   1757       C  
ATOM   6580  CG  LYS B1183       0.082   1.319  -7.358  1.00115.81           C  
ANISOU 6580  CG  LYS B1183    15308  15760  12935   2617   1706   1852       C  
ATOM   6581  CD  LYS B1183       1.423   1.737  -7.974  1.00122.44           C  
ANISOU 6581  CD  LYS B1183    15729  16873  13919   2583   1899   1815       C  
ATOM   6582  CE  LYS B1183       2.201   0.566  -8.526  1.00124.36           C  
ANISOU 6582  CE  LYS B1183    15799  17137  14313   3016   2091   1887       C  
ATOM   6583  NZ  LYS B1183       3.580   0.954  -8.931  1.00130.66           N1+
ANISOU 6583  NZ  LYS B1183    16070  18306  15270   2992   2275   1858       N1+
ATOM   6584  N   PHE B1184      -3.323   4.328  -6.227  1.00 92.13           N  
ANISOU 6584  N   PHE B1184    13167  12436   9400   1746   1312   1528       N  
ATOM   6585  CA  PHE B1184      -3.963   5.496  -5.624  1.00 90.95           C  
ANISOU 6585  CA  PHE B1184    13161  12292   9104   1505   1174   1413       C  
ATOM   6586  C   PHE B1184      -5.143   5.083  -4.724  1.00 91.89           C  
ANISOU 6586  C   PHE B1184    13450  12378   9086   1581   1022   1434       C  
ATOM   6587  O   PHE B1184      -5.297   5.625  -3.628  1.00 92.32           O  
ANISOU 6587  O   PHE B1184    13479  12587   9013   1475    848   1401       O  
ATOM   6588  CB  PHE B1184      -4.444   6.462  -6.724  1.00 92.22           C  
ANISOU 6588  CB  PHE B1184    13610  12221   9210   1379   1334   1289       C  
ATOM   6589  CG  PHE B1184      -3.898   7.867  -6.648  1.00 96.09           C  
ANISOU 6589  CG  PHE B1184    14085  12729   9696   1080   1351   1198       C  
ATOM   6590  CD1 PHE B1184      -4.384   8.772  -5.710  1.00 99.41           C  
ANISOU 6590  CD1 PHE B1184    14615  13155  10001    917   1171   1084       C  
ATOM   6591  CD2 PHE B1184      -2.937   8.305  -7.551  1.00101.22           C  
ANISOU 6591  CD2 PHE B1184    14646  13355  10456    947   1584   1211       C  
ATOM   6592  CE1 PHE B1184      -3.893  10.081  -5.652  1.00102.61           C  
ANISOU 6592  CE1 PHE B1184    15063  13499  10426    610   1199    969       C  
ATOM   6593  CE2 PHE B1184      -2.447   9.615  -7.495  1.00106.59           C  
ANISOU 6593  CE2 PHE B1184    15345  13988  11166    605   1639   1127       C  
ATOM   6594  CZ  PHE B1184      -2.929  10.494  -6.546  1.00104.59           C  
ANISOU 6594  CZ  PHE B1184    15228  13693  10820    432   1436    997       C  
ATOM   6595  N   ARG B1185      -5.953   4.115  -5.192  1.00 85.73           N  
ANISOU 6595  N   ARG B1185    12837  11406   8332   1746   1108   1472       N  
ATOM   6596  CA  ARG B1185      -7.137   3.570  -4.512  1.00 84.00           C  
ANISOU 6596  CA  ARG B1185    12759  11129   8030   1785   1044   1498       C  
ATOM   6597  C   ARG B1185      -6.747   2.764  -3.264  1.00 91.24           C  
ANISOU 6597  C   ARG B1185    13543  12202   8922   1890    944   1707       C  
ATOM   6598  O   ARG B1185      -7.426   2.854  -2.232  1.00 91.35           O  
ANISOU 6598  O   ARG B1185    13621  12309   8780   1845    856   1740       O  
ATOM   6599  CB  ARG B1185      -7.945   2.686  -5.472  1.00 80.99           C  
ANISOU 6599  CB  ARG B1185    12549  10490   7734   1879   1176   1450       C  
ATOM   6600  CG  ARG B1185      -8.219   3.323  -6.829  1.00 84.04           C  
ANISOU 6600  CG  ARG B1185    13084  10751   8094   1857   1260   1269       C  
ATOM   6601  CD  ARG B1185      -9.420   2.697  -7.485  1.00 85.05           C  
ANISOU 6601  CD  ARG B1185    13380  10708   8229   1900   1288   1140       C  
ATOM   6602  NE  ARG B1185      -9.706   3.288  -8.783  1.00 89.15           N  
ANISOU 6602  NE  ARG B1185    14065  11151   8656   1937   1328    974       N  
ATOM   6603  CZ  ARG B1185     -10.515   4.320  -8.982  1.00106.06           C  
ANISOU 6603  CZ  ARG B1185    16329  13325  10643   1910   1247    850       C  
ATOM   6604  NH1 ARG B1185     -11.115   4.913  -7.955  1.00 90.93           N1+
ANISOU 6604  NH1 ARG B1185    14368  11516   8666   1831   1137    843       N1+
ATOM   6605  NH2 ARG B1185     -10.717   4.783 -10.207  1.00100.77           N  
ANISOU 6605  NH2 ARG B1185    15851  12584   9851   2002   1280    739       N  
ATOM   6606  N   GLU B1186      -5.648   1.971  -3.372  1.00 89.65           N  
ANISOU 6606  N   GLU B1186    13168  12043   8851   2072    970   1859       N  
ATOM   6607  CA  GLU B1186      -5.072   1.160  -2.299  1.00 91.26           C  
ANISOU 6607  CA  GLU B1186    13249  12405   9020   2267    860   2098       C  
ATOM   6608  C   GLU B1186      -4.468   2.085  -1.236  1.00 95.31           C  
ANISOU 6608  C   GLU B1186    13556  13300   9357   2165    622   2073       C  
ATOM   6609  O   GLU B1186      -4.438   1.706  -0.066  1.00 97.79           O  
ANISOU 6609  O   GLU B1186    13861  13793   9501   2281    475   2238       O  
ATOM   6610  CB  GLU B1186      -4.029   0.171  -2.846  1.00 94.89           C  
ANISOU 6610  CB  GLU B1186    13564  12814   9678   2551    951   2231       C  
ATOM   6611  CG  GLU B1186      -4.622  -0.967  -3.674  1.00107.73           C  
ANISOU 6611  CG  GLU B1186    15447  14030  11456   2684   1165   2254       C  
ATOM   6612  CD  GLU B1186      -5.019  -2.252  -2.961  1.00140.38           C  
ANISOU 6612  CD  GLU B1186    19778  17955  15605   2872   1197   2499       C  
ATOM   6613  OE1 GLU B1186      -5.667  -2.175  -1.889  1.00134.04           O  
ANISOU 6613  OE1 GLU B1186    19071  17229  14630   2780   1110   2612       O  
ATOM   6614  OE2 GLU B1186      -4.705  -3.341  -3.497  1.00137.62           O1-
ANISOU 6614  OE2 GLU B1186    19523  17333  15431   3113   1341   2577       O1-
ATOM   6615  N   ASN B1187      -4.030   3.306  -1.643  1.00 89.39           N  
ANISOU 6615  N   ASN B1187    12680  12655   8629   1933    592   1860       N  
ATOM   6616  CA  ASN B1187      -3.510   4.364  -0.770  1.00 90.22           C  
ANISOU 6616  CA  ASN B1187    12615  13072   8594   1742    370   1737       C  
ATOM   6617  C   ASN B1187      -4.688   5.083  -0.110  1.00 91.54           C  
ANISOU 6617  C   ASN B1187    13061  13188   8530   1593    311   1611       C  
ATOM   6618  O   ASN B1187      -4.535   5.635   0.980  1.00 92.88           O  
ANISOU 6618  O   ASN B1187    13183  13614   8494   1513    103   1540       O  
ATOM   6619  CB  ASN B1187      -2.730   5.407  -1.580  1.00 91.35           C  
ANISOU 6619  CB  ASN B1187    12590  13229   8889   1490    437   1545       C  
ATOM   6620  CG  ASN B1187      -1.327   5.056  -1.994  1.00117.00           C  
ANISOU 6620  CG  ASN B1187    15430  16682  12345   1565    469   1605       C  
ATOM   6621  OD1 ASN B1187      -0.705   4.092  -1.522  1.00111.76           O  
ANISOU 6621  OD1 ASN B1187    14536  16227  11702   1851    365   1782       O  
ATOM   6622  ND2 ASN B1187      -0.796   5.863  -2.901  1.00111.14           N  
ANISOU 6622  ND2 ASN B1187    14591  15883  11755   1325    636   1468       N  
ATOM   6623  N   CYS B1188      -5.842   5.132  -0.813  1.00 84.28           N  
ANISOU 6623  N   CYS B1188    12414  11969   7639   1566    487   1548       N  
ATOM   6624  CA  CYS B1188      -7.074   5.770  -0.365  1.00 82.09           C  
ANISOU 6624  CA  CYS B1188    12374  11639   7179   1479    479   1416       C  
ATOM   6625  C   CYS B1188      -7.731   4.980   0.754  1.00 88.09           C  
ANISOU 6625  C   CYS B1188    13200  12513   7756   1604    448   1579       C  
ATOM   6626  O   CYS B1188      -8.068   5.565   1.788  1.00 89.55           O  
ANISOU 6626  O   CYS B1188    13447  12884   7693   1554    340   1502       O  
ATOM   6627  CB  CYS B1188      -8.024   5.998  -1.534  1.00 79.34           C  
ANISOU 6627  CB  CYS B1188    12224  10998   6925   1462    649   1301       C  
ATOM   6628  SG  CYS B1188      -7.868   7.632  -2.290  1.00 82.60           S  
ANISOU 6628  SG  CYS B1188    12763  11276   7344   1277    668   1060       S  
ATOM   6629  N   LYS B1189      -7.902   3.654   0.553  1.00 84.34           N  
ANISOU 6629  N   LYS B1189    12745  11908   7394   1763    568   1802       N  
ATOM   6630  CA  LYS B1189      -8.468   2.734   1.541  1.00 85.67           C  
ANISOU 6630  CA  LYS B1189    13015  12118   7418   1871    608   2027       C  
ATOM   6631  C   LYS B1189      -7.574   2.731   2.800  1.00 95.08           C  
ANISOU 6631  C   LYS B1189    14106  13655   8366   1986    392   2175       C  
ATOM   6632  O   LYS B1189      -8.086   2.933   3.904  1.00 97.09           O  
ANISOU 6632  O   LYS B1189    14469  14098   8322   1981    345   2204       O  
ATOM   6633  CB  LYS B1189      -8.576   1.304   0.966  1.00 87.64           C  
ANISOU 6633  CB  LYS B1189    13330  12078   7891   2003    788   2235       C  
ATOM   6634  CG  LYS B1189      -9.527   1.143  -0.210  1.00 89.07           C  
ANISOU 6634  CG  LYS B1189    13609  11956   8278   1893    966   2067       C  
ATOM   6635  CD  LYS B1189      -9.209  -0.130  -0.985  1.00 93.93           C  
ANISOU 6635  CD  LYS B1189    14273  12272   9144   2021   1101   2191       C  
ATOM   6636  CE  LYS B1189      -9.485   0.032  -2.462  1.00 94.00           C  
ANISOU 6636  CE  LYS B1189    14308  12076   9332   1957   1181   1944       C  
ATOM   6637  NZ  LYS B1189     -10.222  -1.124  -3.033  1.00 94.90           N1+
ANISOU 6637  NZ  LYS B1189    14569  11859   9630   1937   1346   1934       N1+
ATOM   6638  N   LYS B1190      -6.234   2.551   2.615  1.00 93.38           N  
ANISOU 6638  N   LYS B1190    13660  13566   8255   2102    254   2241       N  
ATOM   6639  CA  LYS B1190      -5.196   2.506   3.663  1.00 96.55           C  
ANISOU 6639  CA  LYS B1190    13878  14358   8448   2254    -16   2357       C  
ATOM   6640  C   LYS B1190      -5.201   3.744   4.584  1.00100.85           C  
ANISOU 6640  C   LYS B1190    14403  15223   8691   2068   -241   2113       C  
ATOM   6641  O   LYS B1190      -5.189   3.589   5.805  1.00103.35           O  
ANISOU 6641  O   LYS B1190    14781  15825   8664   2194   -401   2226       O  
ATOM   6642  CB  LYS B1190      -3.803   2.301   3.033  1.00 99.91           C  
ANISOU 6642  CB  LYS B1190    13963  14883   9113   2368   -104   2375       C  
ATOM   6643  CG  LYS B1190      -2.820   1.538   3.910  1.00115.18           C  
ANISOU 6643  CG  LYS B1190    15711  17143  10908   2710   -329   2635       C  
ATOM   6644  CD  LYS B1190      -1.454   1.334   3.230  1.00124.65           C  
ANISOU 6644  CD  LYS B1190    16497  18486  12381   2853   -392   2629       C  
ATOM   6645  CE  LYS B1190      -1.226  -0.084   2.746  1.00130.43           C  
ANISOU 6645  CE  LYS B1190    17288  18964  13305   3248   -219   2930       C  
ATOM   6646  NZ  LYS B1190       0.106  -0.253   2.103  1.00135.16           N1+
ANISOU 6646  NZ  LYS B1190    17446  19751  14158   3430   -255   2904       N1+
ATOM   6647  N   ARG B1191      -5.230   4.956   3.996  1.00 95.19           N  
ANISOU 6647  N   ARG B1191    13650  14434   8083   1785   -239   1782       N  
ATOM   6648  CA  ARG B1191      -5.234   6.229   4.723  1.00 96.29           C  
ANISOU 6648  CA  ARG B1191    13819  14779   7990   1574   -426   1483       C  
ATOM   6649  C   ARG B1191      -6.551   6.475   5.461  1.00100.15           C  
ANISOU 6649  C   ARG B1191    14626  15241   8185   1581   -339   1433       C  
ATOM   6650  O   ARG B1191      -6.530   7.029   6.559  1.00102.84           O  
ANISOU 6650  O   ARG B1191    15027  15862   8187   1557   -523   1300       O  
ATOM   6651  CB  ARG B1191      -4.882   7.397   3.771  1.00 94.57           C  
ANISOU 6651  CB  ARG B1191    13533  14382   8015   1274   -388   1181       C  
ATOM   6652  CG  ARG B1191      -5.132   8.816   4.303  1.00 99.08           C  
ANISOU 6652  CG  ARG B1191    14256  14982   8408   1022   -501    827       C  
ATOM   6653  CD  ARG B1191      -3.985   9.381   5.114  1.00103.39           C  
ANISOU 6653  CD  ARG B1191    14555  15894   8836    861   -823    635       C  
ATOM   6654  NE  ARG B1191      -4.458  10.460   5.978  1.00107.21           N  
ANISOU 6654  NE  ARG B1191    15278  16425   9032    707   -946    314       N  
ATOM   6655  CZ  ARG B1191      -3.675  11.324   6.615  1.00116.66           C  
ANISOU 6655  CZ  ARG B1191    16355  17845  10125    460  -1218      0       C  
ATOM   6656  NH1 ARG B1191      -2.355  11.255   6.488  1.00 97.85           N  
ANISOU 6656  NH1 ARG B1191    13548  15710   7923    316  -1404    -31       N  
ATOM   6657  NH2 ARG B1191      -4.205  12.269   7.377  1.00105.88           N1+
ANISOU 6657  NH2 ARG B1191    15278  16470   8484    351  -1302   -316       N1+
ATOM   6658  N   ALA B1192      -7.683   6.073   4.870  1.00 94.00           N  
ANISOU 6658  N   ALA B1192    14025  14164   7525   1614    -63   1511       N  
ATOM   6659  CA  ALA B1192      -8.995   6.266   5.480  1.00 93.94           C  
ANISOU 6659  CA  ALA B1192    14248  14158   7286   1623     70   1460       C  
ATOM   6660  C   ALA B1192      -9.294   5.281   6.627  1.00101.94           C  
ANISOU 6660  C   ALA B1192    15353  15375   8004   1805    110   1763       C  
ATOM   6661  O   ALA B1192      -9.892   5.682   7.624  1.00102.11           O  
ANISOU 6661  O   ALA B1192    15520  15600   7676   1819    116   1689       O  
ATOM   6662  CB  ALA B1192     -10.072   6.190   4.421  1.00 91.41           C  
ANISOU 6662  CB  ALA B1192    14010  13509   7213   1583    324   1408       C  
ATOM   6663  N   MET B1193      -8.896   3.998   6.480  1.00101.58           N  
ANISOU 6663  N   MET B1193    15261  15250   8084   1962    167   2111       N  
ATOM   6664  CA  MET B1193      -9.119   2.960   7.499  1.00105.51           C  
ANISOU 6664  CA  MET B1193    15909  15864   8316   2155    244   2476       C  
ATOM   6665  C   MET B1193      -8.270   3.194   8.752  1.00112.26           C  
ANISOU 6665  C   MET B1193    16749  17167   8737   2310    -65   2527       C  
ATOM   6666  O   MET B1193      -8.676   2.798   9.848  1.00115.14           O  
ANISOU 6666  O   MET B1193    17317  17719   8711   2445    -10   2741       O  
ATOM   6667  CB  MET B1193      -8.910   1.547   6.926  1.00108.82           C  
ANISOU 6667  CB  MET B1193    16344  15985   9017   2299    402   2824       C  
ATOM   6668  CG  MET B1193     -10.042   1.101   6.018  1.00110.97           C  
ANISOU 6668  CG  MET B1193    16701  15861   9604   2141    730   2795       C  
ATOM   6669  SD  MET B1193      -9.550  -0.175   4.826  1.00115.80           S  
ANISOU 6669  SD  MET B1193    17290  16042  10666   2244    851   2984       S  
ATOM   6670  CE  MET B1193     -10.919  -0.053   3.653  1.00108.91           C  
ANISOU 6670  CE  MET B1193    16438  14844  10101   1963   1105   2708       C  
ATOM   6671  N   SER B1194      -7.108   3.862   8.590  1.00107.85           N  
ANISOU 6671  N   SER B1194    15944  16803   8232   2273   -384   2317       N  
ATOM   6672  CA  SER B1194      -6.219   4.216   9.698  1.00111.02           C  
ANISOU 6672  CA  SER B1194    16257  17686   8238   2381   -757   2265       C  
ATOM   6673  C   SER B1194      -6.830   5.364  10.528  1.00112.63           C  
ANISOU 6673  C   SER B1194    16636  18095   8063   2224   -821   1924       C  
ATOM   6674  O   SER B1194      -6.520   5.499  11.715  1.00116.75           O  
ANISOU 6674  O   SER B1194    17224  19028   8106   2350  -1062   1916       O  
ATOM   6675  CB  SER B1194      -4.815   4.554   9.195  1.00115.21           C  
ANISOU 6675  CB  SER B1194    16398  18369   9008   2332  -1053   2107       C  
ATOM   6676  OG  SER B1194      -4.797   5.609   8.247  1.00119.57           O  
ANISOU 6676  OG  SER B1194    16839  18709   9882   1994  -1001   1734       O  
ATOM   6677  N   PHE B1195      -7.729   6.155   9.907  1.00102.67           N  
ANISOU 6677  N   PHE B1195    15474  16548   6987   1995   -606   1647       N  
ATOM   6678  CA  PHE B1195      -8.450   7.253  10.549  1.00102.05           C  
ANISOU 6678  CA  PHE B1195    15596  16573   6606   1885   -599   1302       C  
ATOM   6679  C   PHE B1195      -9.623   6.689  11.355  1.00103.34           C  
ANISOU 6679  C   PHE B1195    16016  16815   6434   2043   -320   1522       C  
ATOM   6680  O   PHE B1195      -9.877   7.164  12.453  1.00105.41           O  
ANISOU 6680  O   PHE B1195    16453  17380   6218   2103   -385   1386       O  
ATOM   6681  CB  PHE B1195      -8.959   8.249   9.493  1.00100.44           C  
ANISOU 6681  CB  PHE B1195    15407  16004   6751   1658   -460    969       C  
ATOM   6682  CG  PHE B1195      -8.701   9.706   9.792  1.00104.25           C  
ANISOU 6682  CG  PHE B1195    15963  16542   7104   1472   -657    496       C  
ATOM   6683  CD1 PHE B1195      -7.512  10.314   9.399  1.00109.05           C  
ANISOU 6683  CD1 PHE B1195    16375  17144   7915   1257   -910    288       C  
ATOM   6684  CD2 PHE B1195      -9.664  10.484  10.425  1.00107.60           C  
ANISOU 6684  CD2 PHE B1195    16655  16994   7235   1496   -557    238       C  
ATOM   6685  CE1 PHE B1195      -7.276  11.668   9.669  1.00112.20           C  
ANISOU 6685  CE1 PHE B1195    16880  17522   8229   1026  -1071   -171       C  
ATOM   6686  CE2 PHE B1195      -9.431  11.839  10.688  1.00112.54           C  
ANISOU 6686  CE2 PHE B1195    17411  17593   7757   1328   -725   -228       C  
ATOM   6687  CZ  PHE B1195      -8.237  12.420  10.314  1.00111.93           C  
ANISOU 6687  CZ  PHE B1195    17171  17464   7892   1072   -985   -431       C  
ATOM   6688  N   SER B1196     -10.331   5.676  10.804  1.00 95.99           N  
ANISOU 6688  N   SER B1196    15107  15613   5752   2088      9   1842       N  
ATOM   6689  CA  SER B1196     -11.477   4.993  11.415  1.00 96.04           C  
ANISOU 6689  CA  SER B1196    15308  15638   5544   2168    358   2094       C  
ATOM   6690  C   SER B1196     -11.063   4.217  12.658  1.00102.96           C  
ANISOU 6690  C   SER B1196    16350  16832   5939   2402    290   2460       C  
ATOM   6691  O   SER B1196     -11.830   4.182  13.621  1.00106.09           O  
ANISOU 6691  O   SER B1196    16961  17433   5917   2468    490   2541       O  
ATOM   6692  CB  SER B1196     -12.130   4.038  10.420  1.00 96.77           C  
ANISOU 6692  CB  SER B1196    15344  15332   6092   2097    678   2319       C  
ATOM   6693  OG  SER B1196     -12.692   4.716   9.309  1.00100.93           O  
ANISOU 6693  OG  SER B1196    15752  15609   6989   1928    755   2000       O  
ATOM   6694  N   VAL B 372      -9.862   3.588  12.635  1.00 95.79           N  
ANISOU 6694  N   VAL B 372    15410  14433   6553  -2719   1336    492       N  
ATOM   6695  CA  VAL B 372      -9.318   2.830  13.768  1.00 92.12           C  
ANISOU 6695  CA  VAL B 372    14630  13978   6393  -2702   1397    319       C  
ATOM   6696  C   VAL B 372      -8.827   3.759  14.864  1.00 92.38           C  
ANISOU 6696  C   VAL B 372    14628  13854   6617  -2820   1458    427       C  
ATOM   6697  O   VAL B 372      -8.927   3.405  16.038  1.00 89.97           O  
ANISOU 6697  O   VAL B 372    14123  13468   6596  -2741   1398    346       O  
ATOM   6698  CB  VAL B 372      -8.263   1.752  13.408  1.00 97.03           C  
ANISOU 6698  CB  VAL B 372    15051  14842   6975  -2744   1594    109       C  
ATOM   6699  CG1 VAL B 372      -8.864   0.662  12.533  1.00 97.66           C  
ANISOU 6699  CG1 VAL B 372    15144  15042   6918  -2602   1508    -43       C  
ATOM   6700  CG2 VAL B 372      -7.011   2.347  12.766  1.00 99.58           C  
ANISOU 6700  CG2 VAL B 372    15431  15311   7093  -2974   1855    175       C  
ATOM   6701  N   ALA B 373      -8.304   4.940  14.487  1.00 89.09           N  
ANISOU 6701  N   ALA B 373    14419  13392   6041  -3016   1581    609       N  
ATOM   6702  CA  ALA B 373      -7.830   5.956  15.423  1.00 88.43           C  
ANISOU 6702  CA  ALA B 373    14352  13145   6104  -3167   1648    718       C  
ATOM   6703  C   ALA B 373      -9.003   6.526  16.225  1.00 91.91           C  
ANISOU 6703  C   ALA B 373    14898  13314   6707  -3012   1419    826       C  
ATOM   6704  O   ALA B 373      -8.861   6.770  17.428  1.00 91.47           O  
ANISOU 6704  O   ALA B 373    14722  13137   6897  -3029   1406    809       O  
ATOM   6705  CB  ALA B 373      -7.115   7.068  14.673  1.00 92.27           C  
ANISOU 6705  CB  ALA B 373    15085  13626   6345  -3422   1831    891       C  
ATOM   6706  N   GLN B 374     -10.168   6.706  15.563  1.00 88.59           N  
ANISOU 6706  N   GLN B 374    14693  12823   6146  -2850   1236    927       N  
ATOM   6707  CA  GLN B 374     -11.395   7.213  16.180  1.00 86.90           C  
ANISOU 6707  CA  GLN B 374    14578  12384   6055  -2665   1009   1029       C  
ATOM   6708  C   GLN B 374     -12.051   6.148  17.043  1.00 87.48           C  
ANISOU 6708  C   GLN B 374    14371  12477   6391  -2472    861    851       C  
ATOM   6709  O   GLN B 374     -12.530   6.477  18.126  1.00 84.74           O  
ANISOU 6709  O   GLN B 374    13977  11958   6264  -2391    763    878       O  
ATOM   6710  CB  GLN B 374     -12.390   7.779  15.140  1.00 90.19           C  
ANISOU 6710  CB  GLN B 374    15304  12753   6212  -2544    862   1199       C  
ATOM   6711  CG  GLN B 374     -11.871   8.925  14.232  1.00118.04           C  
ANISOU 6711  CG  GLN B 374    19178  16223   9450  -2718   1001   1413       C  
ATOM   6712  CD  GLN B 374     -10.942   9.969  14.854  1.00149.38           C  
ANISOU 6712  CD  GLN B 374    23244  20022  13492  -2959   1184   1518       C  
ATOM   6713  OE1 GLN B 374     -11.092  10.400  16.014  1.00142.66           O  
ANISOU 6713  OE1 GLN B 374    22344  18979  12883  -2941   1136   1530       O  
ATOM   6714  NE2 GLN B 374      -9.963  10.420  14.068  1.00146.43           N  
ANISOU 6714  NE2 GLN B 374    23022  19719  12895  -3206   1406   1596       N  
ATOM   6715  N   ALA B 375     -12.064   4.876  16.570  1.00 84.33           N  
ANISOU 6715  N   ALA B 375    13800  12278   5962  -2404    855    668       N  
ATOM   6716  CA  ALA B 375     -12.632   3.729  17.286  1.00 82.08           C  
ANISOU 6716  CA  ALA B 375    13263  12017   5907  -2243    739    487       C  
ATOM   6717  C   ALA B 375     -11.828   3.409  18.553  1.00 86.92           C  
ANISOU 6717  C   ALA B 375    13634  12600   6792  -2296    847    386       C  
ATOM   6718  O   ALA B 375     -12.428   3.054  19.576  1.00 84.73           O  
ANISOU 6718  O   ALA B 375    13218  12224   6751  -2170    732    330       O  
ATOM   6719  CB  ALA B 375     -12.696   2.516  16.380  1.00 83.09           C  
ANISOU 6719  CB  ALA B 375    13314  12348   5908  -2193    739    318       C  
ATOM   6720  N   ARG B 376     -10.474   3.568  18.491  1.00 85.43           N  
ANISOU 6720  N   ARG B 376    13391  12509   6557  -2483   1067    366       N  
ATOM   6721  CA  ARG B 376      -9.548   3.375  19.619  1.00 83.66           C  
ANISOU 6721  CA  ARG B 376    12935  12297   6553  -2551   1181    278       C  
ATOM   6722  C   ARG B 376      -9.771   4.457  20.669  1.00 87.96           C  
ANISOU 6722  C   ARG B 376    13549  12624   7250  -2587   1123    407       C  
ATOM   6723  O   ARG B 376      -9.563   4.210  21.851  1.00 86.67           O  
ANISOU 6723  O   ARG B 376    13195  12418   7316  -2554   1116    333       O  
ATOM   6724  CB  ARG B 376      -8.080   3.390  19.153  1.00 83.46           C  
ANISOU 6724  CB  ARG B 376    12838  12468   6405  -2753   1428    234       C  
ATOM   6725  CG  ARG B 376      -7.481   2.000  19.038  1.00 90.18           C  
ANISOU 6725  CG  ARG B 376    13443  13531   7291  -2677   1518     18       C  
ATOM   6726  CD  ARG B 376      -6.147   1.991  18.327  1.00100.58           C  
ANISOU 6726  CD  ARG B 376    14700  15080   8437  -2852   1759    -26       C  
ATOM   6727  NE  ARG B 376      -5.779   0.642  17.892  1.00109.57           N  
ANISOU 6727  NE  ARG B 376    15672  16414   9546  -2736   1831   -226       N  
ATOM   6728  CZ  ARG B 376      -4.663   0.339  17.234  1.00122.19           C  
ANISOU 6728  CZ  ARG B 376    17176  18252  10997  -2830   2042   -310       C  
ATOM   6729  NH1 ARG B 376      -3.784   1.287  16.930  1.00104.90           N  
ANISOU 6729  NH1 ARG B 376    15028  16152   8679  -3068   2210   -210       N  
ATOM   6730  NH2 ARG B 376      -4.415  -0.916  16.879  1.00108.70           N1+
ANISOU 6730  NH2 ARG B 376    15336  16695   9270  -2690   2097   -498       N1+
ATOM   6731  N   GLU B 377     -10.176   5.656  20.231  1.00 86.89           N  
ANISOU 6731  N   GLU B 377    13698  12344   6974  -2647   1085    599       N  
ATOM   6732  CA  GLU B 377     -10.463   6.793  21.096  1.00 87.12           C  
ANISOU 6732  CA  GLU B 377    13855  12134   7114  -2674   1030    733       C  
ATOM   6733  C   GLU B 377     -11.858   6.628  21.716  1.00 87.76           C  
ANISOU 6733  C   GLU B 377    13928  12071   7347  -2422    800    741       C  
ATOM   6734  O   GLU B 377     -12.041   6.921  22.901  1.00 86.67           O  
ANISOU 6734  O   GLU B 377    13724  11792   7415  -2382    751    740       O  
ATOM   6735  CB  GLU B 377     -10.331   8.117  20.297  1.00 91.99           C  
ANISOU 6735  CB  GLU B 377    14815  12636   7499  -2827   1094    941       C  
ATOM   6736  CG  GLU B 377     -10.510   9.401  21.108  1.00111.01           C  
ANISOU 6736  CG  GLU B 377    17409  14770   9998  -2881   1068   1082       C  
ATOM   6737  CD  GLU B 377      -9.616   9.581  22.325  1.00148.06           C  
ANISOU 6737  CD  GLU B 377    21924  19435  14896  -3036   1171   1000       C  
ATOM   6738  OE1 GLU B 377      -8.389   9.757  22.141  1.00154.73           O1-
ANISOU 6738  OE1 GLU B 377    22717  20398  15675  -3291   1369    971       O1-
ATOM   6739  OE2 GLU B 377     -10.144   9.557  23.461  1.00144.62           O  
ANISOU 6739  OE2 GLU B 377    21395  18875  14679  -2905   1055    962       O  
ATOM   6740  N   LYS B 378     -12.822   6.144  20.911  1.00 82.77           N  
ANISOU 6740  N   LYS B 378    13351  11495   6603  -2262    664    739       N  
ATOM   6741  CA  LYS B 378     -14.214   5.894  21.276  1.00 80.69           C  
ANISOU 6741  CA  LYS B 378    13061  11152   6447  -2028    444    736       C  
ATOM   6742  C   LYS B 378     -14.317   4.832  22.374  1.00 81.08           C  
ANISOU 6742  C   LYS B 378    12813  11230   6764  -1940    415    562       C  
ATOM   6743  O   LYS B 378     -15.085   5.015  23.320  1.00 78.74           O  
ANISOU 6743  O   LYS B 378    12472  10800   6643  -1816    298    580       O  
ATOM   6744  CB  LYS B 378     -14.994   5.442  20.035  1.00 84.34           C  
ANISOU 6744  CB  LYS B 378    13604  11739   6700  -1923    332    734       C  
ATOM   6745  CG  LYS B 378     -16.313   6.172  19.809  1.00100.84           C  
ANISOU 6745  CG  LYS B 378    15877  13718   8718  -1746    127    880       C  
ATOM   6746  CD  LYS B 378     -17.228   5.406  18.827  1.00111.04           C  
ANISOU 6746  CD  LYS B 378    17147  15179   9862  -1615    -24    815       C  
ATOM   6747  CE  LYS B 378     -18.290   4.544  19.494  1.00112.92           C  
ANISOU 6747  CE  LYS B 378    17158  15443  10303  -1449   -189    683       C  
ATOM   6748  NZ  LYS B 378     -17.718   3.393  20.251  1.00114.78           N1+
ANISOU 6748  NZ  LYS B 378    17129  15727  10754  -1509    -89    485       N1+
ATOM   6749  N   ARG B 379     -13.541   3.725  22.239  1.00 77.24           N  
ANISOU 6749  N   ARG B 379    12134  10915   6298  -1993    527    396       N  
ATOM   6750  CA  ARG B 379     -13.484   2.607  23.190  1.00 74.87           C  
ANISOU 6750  CA  ARG B 379    11572  10647   6227  -1913    526    229       C  
ATOM   6751  C   ARG B 379     -12.857   3.058  24.482  1.00 76.39           C  
ANISOU 6751  C   ARG B 379    11671  10745   6607  -1969    593    242       C  
ATOM   6752  O   ARG B 379     -13.397   2.782  25.550  1.00 73.22           O  
ANISOU 6752  O   ARG B 379    11158  10254   6409  -1855    509    205       O  
ATOM   6753  CB  ARG B 379     -12.648   1.445  22.640  1.00 77.07           C  
ANISOU 6753  CB  ARG B 379    11712  11121   6449  -1953    655     65       C  
ATOM   6754  CG  ARG B 379     -13.404   0.483  21.739  1.00 93.57           C  
ANISOU 6754  CG  ARG B 379    13810  13302   8440  -1855    567    -33       C  
ATOM   6755  CD  ARG B 379     -12.665  -0.842  21.574  1.00104.49           C  
ANISOU 6755  CD  ARG B 379    15031  14829   9844  -1849    688   -228       C  
ATOM   6756  NE  ARG B 379     -11.289  -0.681  21.089  1.00109.79           N  
ANISOU 6756  NE  ARG B 379    15689  15639  10385  -1986    890   -240       N  
ATOM   6757  CZ  ARG B 379     -10.940  -0.629  19.806  1.00126.86           C  
ANISOU 6757  CZ  ARG B 379    17969  17939  12295  -2065    968   -238       C  
ATOM   6758  NH1 ARG B 379     -11.864  -0.716  18.853  1.00114.09           N  
ANISOU 6758  NH1 ARG B 379    16499  16336  10513  -2016    847   -223       N  
ATOM   6759  NH2 ARG B 379      -9.667  -0.491  19.465  1.00114.88           N1+
ANISOU 6759  NH2 ARG B 379    16412  16562  10676  -2196   1167   -255       N1+
ATOM   6760  N   PHE B 380     -11.706   3.748  24.382  1.00 74.37           N  
ANISOU 6760  N   PHE B 380    11459  10523   6275  -2157    748    289       N  
ATOM   6761  CA  PHE B 380     -10.950   4.262  25.527  1.00 73.88           C  
ANISOU 6761  CA  PHE B 380    11310  10401   6360  -2253    823    292       C  
ATOM   6762  C   PHE B 380     -11.790   5.177  26.445  1.00 74.95           C  
ANISOU 6762  C   PHE B 380    11557  10303   6617  -2184    698    399       C  
ATOM   6763  O   PHE B 380     -11.697   5.065  27.663  1.00 72.62           O  
ANISOU 6763  O   PHE B 380    11124   9955   6512  -2146    684    346       O  
ATOM   6764  CB  PHE B 380      -9.662   4.952  25.055  1.00 77.90           C  
ANISOU 6764  CB  PHE B 380    11871  10998   6727  -2502   1009    332       C  
ATOM   6765  N   THR B 381     -12.641   6.026  25.854  1.00 70.97           N  
ANISOU 6765  N   THR B 381    11303   9668   5995  -2144    604    545       N  
ATOM   6766  CA  THR B 381     -13.536   6.915  26.579  1.00 69.57           C  
ANISOU 6766  CA  THR B 381    11258   9268   5907  -2044    483    651       C  
ATOM   6767  C   THR B 381     -14.600   6.075  27.299  1.00 70.54           C  
ANISOU 6767  C   THR B 381    11212   9383   6210  -1819    337    568       C  
ATOM   6768  O   THR B 381     -14.966   6.399  28.426  1.00 67.97           O  
ANISOU 6768  O   THR B 381    10852   8927   6047  -1747    284    576       O  
ATOM   6769  CB  THR B 381     -14.131   7.954  25.611  1.00 82.05           C  
ANISOU 6769  CB  THR B 381    13155  10733   7285  -2031    425    831       C  
ATOM   6770  OG1 THR B 381     -13.086   8.561  24.832  1.00 86.11           O  
ANISOU 6770  OG1 THR B 381    13822  11280   7617  -2263    586    899       O  
ATOM   6771  CG2 THR B 381     -14.933   9.027  26.326  1.00 79.31           C  
ANISOU 6771  CG2 THR B 381    12980  10139   7013  -1925    322    951       C  
ATOM   6772  N   PHE B 382     -15.074   4.981  26.658  1.00 68.37           N  
ANISOU 6772  N   PHE B 382    10831   9247   5899  -1723    281    481       N  
ATOM   6773  CA  PHE B 382     -16.084   4.068  27.228  1.00 66.87           C  
ANISOU 6773  CA  PHE B 382    10476   9064   5866  -1543    158    390       C  
ATOM   6774  C   PHE B 382     -15.524   3.226  28.380  1.00 70.29           C  
ANISOU 6774  C   PHE B 382    10678   9526   6504  -1542    228    259       C  
ATOM   6775  O   PHE B 382     -16.107   3.242  29.461  1.00 69.46           O  
ANISOU 6775  O   PHE B 382    10503   9322   6567  -1440    161    254       O  
ATOM   6776  CB  PHE B 382     -16.737   3.165  26.150  1.00 68.50           C  
ANISOU 6776  CB  PHE B 382    10658   9408   5960  -1473     82    324       C  
ATOM   6777  CG  PHE B 382     -17.508   1.985  26.706  1.00 67.59           C  
ANISOU 6777  CG  PHE B 382    10344   9326   6010  -1350      2    192       C  
ATOM   6778  CD1 PHE B 382     -18.781   2.150  27.235  1.00 69.48           C  
ANISOU 6778  CD1 PHE B 382    10560   9488   6350  -1206   -147    225       C  
ATOM   6779  CD2 PHE B 382     -16.952   0.711  26.715  1.00 68.31           C  
ANISOU 6779  CD2 PHE B 382    10278   9521   6154  -1378     88     33       C  
ATOM   6780  CE1 PHE B 382     -19.480   1.062  27.767  1.00 69.04           C  
ANISOU 6780  CE1 PHE B 382    10323   9463   6446  -1123   -202    104       C  
ATOM   6781  CE2 PHE B 382     -17.657  -0.376  27.241  1.00 69.37           C  
ANISOU 6781  CE2 PHE B 382    10261   9658   6440  -1283     29    -83       C  
ATOM   6782  CZ  PHE B 382     -18.913  -0.193  27.766  1.00 66.88           C  
ANISOU 6782  CZ  PHE B 382     9920   9268   6223  -1171   -112    -46       C  
ATOM   6783  N   VAL B 383     -14.417   2.478  28.137  1.00 66.88           N  
ANISOU 6783  N   VAL B 383    10130   9236   6046  -1637    363    154       N  
ATOM   6784  CA  VAL B 383     -13.753   1.613  29.121  1.00 65.60           C  
ANISOU 6784  CA  VAL B 383     9754   9123   6047  -1618    437     32       C  
ATOM   6785  C   VAL B 383     -13.453   2.406  30.370  1.00 69.02           C  
ANISOU 6785  C   VAL B 383    10170   9448   6606  -1647    448     81       C  
ATOM   6786  O   VAL B 383     -13.597   1.883  31.472  1.00 67.19           O  
ANISOU 6786  O   VAL B 383     9801   9186   6544  -1554    426     20       O  
ATOM   6787  CB  VAL B 383     -12.489   0.912  28.555  1.00 71.22           C  
ANISOU 6787  CB  VAL B 383    10366  10018   6677  -1709    591    -70       C  
ATOM   6788  CG1 VAL B 383     -11.826   0.006  29.594  1.00 69.95           C  
ANISOU 6788  CG1 VAL B 383     9988   9911   6679  -1649    655   -188       C  
ATOM   6789  CG2 VAL B 383     -12.816   0.114  27.296  1.00 72.13           C  
ANISOU 6789  CG2 VAL B 383    10518  10234   6654  -1678    581   -132       C  
ATOM   6790  N   LEU B 384     -13.135   3.694  30.203  1.00 68.16           N  
ANISOU 6790  N   LEU B 384    10226   9263   6409  -1773    476    194       N  
ATOM   6791  CA  LEU B 384     -12.850   4.564  31.333  1.00 67.92           C  
ANISOU 6791  CA  LEU B 384    10213   9115   6479  -1824    487    234       C  
ATOM   6792  C   LEU B 384     -14.102   5.145  32.018  1.00 70.31           C  
ANISOU 6792  C   LEU B 384    10614   9225   6875  -1679    349    310       C  
ATOM   6793  O   LEU B 384     -13.971   5.551  33.166  1.00 71.52           O  
ANISOU 6793  O   LEU B 384    10737   9292   7146  -1678    349    304       O  
ATOM   6794  CB  LEU B 384     -11.828   5.639  30.994  1.00 69.59           C  
ANISOU 6794  CB  LEU B 384    10549   9322   6571  -2052    600    299       C  
ATOM   6795  CG  LEU B 384     -10.443   5.116  31.339  1.00 74.75           C  
ANISOU 6795  CG  LEU B 384    10988  10162   7252  -2173    736    184       C  
ATOM   6796  CD1 LEU B 384      -9.508   5.134  30.174  1.00 76.26           C  
ANISOU 6796  CD1 LEU B 384    11197  10512   7265  -2344    869    180       C  
ATOM   6797  CD2 LEU B 384      -9.904   5.722  32.626  1.00 78.58           C  
ANISOU 6797  CD2 LEU B 384    11414  10591   7851  -2252    756    165       C  
ATOM   6798  N   ALA B 385     -15.307   5.087  31.410  1.00 63.79           N  
ANISOU 6798  N   ALA B 385     9874   8356   6005  -1543    231    363       N  
ATOM   6799  CA  ALA B 385     -16.535   5.502  32.106  1.00 62.14           C  
ANISOU 6799  CA  ALA B 385     9711   8003   5896  -1376    103    417       C  
ATOM   6800  C   ALA B 385     -16.857   4.382  33.118  1.00 64.65           C  
ANISOU 6800  C   ALA B 385     9797   8369   6400  -1264     81    300       C  
ATOM   6801  O   ALA B 385     -17.322   4.644  34.235  1.00 62.52           O  
ANISOU 6801  O   ALA B 385     9496   7997   6260  -1177     40    306       O  
ATOM   6802  CB  ALA B 385     -17.683   5.651  31.117  1.00 63.73           C  
ANISOU 6802  CB  ALA B 385    10028   8198   5987  -1259    -20    491       C  
ATOM   6803  N   VAL B 386     -16.550   3.123  32.707  1.00 60.86           N  
ANISOU 6803  N   VAL B 386     9169   8036   5920  -1272    122    192       N  
ATOM   6804  CA  VAL B 386     -16.713   1.865  33.444  1.00 57.79           C  
ANISOU 6804  CA  VAL B 386     8583   7696   5679  -1184    127     78       C  
ATOM   6805  C   VAL B 386     -15.751   1.850  34.645  1.00 61.88           C  
ANISOU 6805  C   VAL B 386     9000   8209   6303  -1221    212     37       C  
ATOM   6806  O   VAL B 386     -16.211   1.605  35.745  1.00 62.62           O  
ANISOU 6806  O   VAL B 386     9015   8242   6534  -1122    180     17       O  
ATOM   6807  CB  VAL B 386     -16.555   0.637  32.491  1.00 59.89           C  
ANISOU 6807  CB  VAL B 386     8776   8098   5882  -1194    159    -22       C  
ATOM   6808  CG1 VAL B 386     -16.551  -0.690  33.247  1.00 57.61           C  
ANISOU 6808  CG1 VAL B 386     8317   7834   5738  -1116    190   -139       C  
ATOM   6809  CG2 VAL B 386     -17.635   0.640  31.412  1.00 60.31           C  
ANISOU 6809  CG2 VAL B 386     8916   8170   5831  -1151     49      7       C  
ATOM   6810  N   VAL B 387     -14.448   2.148  34.452  1.00 58.29           N  
ANISOU 6810  N   VAL B 387     8542   7831   5776  -1363    319     24       N  
ATOM   6811  CA  VAL B 387     -13.426   2.207  35.515  1.00 57.60           C  
ANISOU 6811  CA  VAL B 387     8344   7779   5763  -1413    393    -21       C  
ATOM   6812  C   VAL B 387     -13.887   3.201  36.632  1.00 64.07           C  
ANISOU 6812  C   VAL B 387     9237   8442   6666  -1388    334     40       C  
ATOM   6813  O   VAL B 387     -13.831   2.877  37.828  1.00 62.86           O  
ANISOU 6813  O   VAL B 387     8973   8279   6631  -1315    329     -5       O  
ATOM   6814  CB  VAL B 387     -12.047   2.640  34.921  1.00 62.15           C  
ANISOU 6814  CB  VAL B 387     8921   8478   6218  -1606    511    -31       C  
ATOM   6815  CG1 VAL B 387     -11.024   2.925  36.020  1.00 61.23           C  
ANISOU 6815  CG1 VAL B 387     8690   8413   6163  -1680    569    -75       C  
ATOM   6816  CG2 VAL B 387     -11.502   1.616  33.925  1.00 62.39           C  
ANISOU 6816  CG2 VAL B 387     8863   8678   6166  -1613    586   -109       C  
ATOM   6817  N   MET B 388     -14.328   4.412  36.211  1.00 61.75           N  
ANISOU 6817  N   MET B 388     9145   8020   6296  -1439    293    145       N  
ATOM   6818  CA  MET B 388     -14.803   5.494  37.064  1.00 60.62           C  
ANISOU 6818  CA  MET B 388     9123   7704   6204  -1413    242    208       C  
ATOM   6819  C   MET B 388     -16.070   5.082  37.797  1.00 62.05           C  
ANISOU 6819  C   MET B 388     9251   7816   6509  -1206    146    204       C  
ATOM   6820  O   MET B 388     -16.170   5.298  39.001  1.00 61.73           O  
ANISOU 6820  O   MET B 388     9177   7709   6566  -1154    136    186       O  
ATOM   6821  CB  MET B 388     -15.046   6.743  36.217  1.00 64.77           C  
ANISOU 6821  CB  MET B 388     9906   8103   6601  -1487    224    328       C  
ATOM   6822  CG  MET B 388     -13.761   7.418  35.775  1.00 70.59           C  
ANISOU 6822  CG  MET B 388    10722   8871   7227  -1731    338    341       C  
ATOM   6823  SD  MET B 388     -14.022   8.836  34.672  1.00 77.47           S  
ANISOU 6823  SD  MET B 388    11940   9571   7923  -1825    336    501       S  
ATOM   6824  CE  MET B 388     -12.401   8.943  33.914  1.00 75.73           C  
ANISOU 6824  CE  MET B 388    11703   9503   7570  -2128    503    474       C  
ATOM   6825  N   GLY B 389     -17.009   4.475  37.065  1.00 56.83           N  
ANISOU 6825  N   GLY B 389     8573   7186   5833  -1101     81    214       N  
ATOM   6826  CA  GLY B 389     -18.282   3.980  37.586  1.00 54.19           C  
ANISOU 6826  CA  GLY B 389     8164   6820   5607   -924     -4    203       C  
ATOM   6827  C   GLY B 389     -18.074   2.921  38.643  1.00 53.77           C  
ANISOU 6827  C   GLY B 389     7925   6821   5686   -875     38    110       C  
ATOM   6828  O   GLY B 389     -18.703   2.978  39.700  1.00 52.96           O  
ANISOU 6828  O   GLY B 389     7785   6651   5686   -772      8    111       O  
ATOM   6829  N   VAL B 390     -17.145   1.980  38.380  1.00 48.89           N  
ANISOU 6829  N   VAL B 390     7201   6322   5054   -941    115     34       N  
ATOM   6830  CA  VAL B 390     -16.750   0.902  39.289  1.00 48.16           C  
ANISOU 6830  CA  VAL B 390     6950   6284   5064   -888    167    -48       C  
ATOM   6831  C   VAL B 390     -16.040   1.467  40.537  1.00 53.43           C  
ANISOU 6831  C   VAL B 390     7596   6927   5777   -907    200    -50       C  
ATOM   6832  O   VAL B 390     -16.318   0.992  41.620  1.00 53.94           O  
ANISOU 6832  O   VAL B 390     7583   6970   5940   -807    198    -75       O  
ATOM   6833  CB  VAL B 390     -15.925  -0.205  38.571  1.00 52.80           C  
ANISOU 6833  CB  VAL B 390     7451   7002   5607   -927    242   -129       C  
ATOM   6834  CG1 VAL B 390     -15.293  -1.173  39.564  1.00 52.05           C  
ANISOU 6834  CG1 VAL B 390     7220   6956   5600   -859    304   -199       C  
ATOM   6835  CG2 VAL B 390     -16.772  -0.967  37.544  1.00 52.67           C  
ANISOU 6835  CG2 VAL B 390     7447   7004   5563   -895    203   -154       C  
ATOM   6836  N   TRP B 391     -15.179   2.500  40.398  1.00 51.72           N  
ANISOU 6836  N   TRP B 391     7458   6712   5483  -1042    231    -25       N  
ATOM   6837  CA  TRP B 391     -14.453   3.143  41.506  1.00 51.46           C  
ANISOU 6837  CA  TRP B 391     7412   6667   5475  -1096    255    -41       C  
ATOM   6838  C   TRP B 391     -15.406   3.799  42.481  1.00 55.25           C  
ANISOU 6838  C   TRP B 391     7970   6997   6025   -998    192     -2       C  
ATOM   6839  O   TRP B 391     -15.210   3.683  43.696  1.00 54.68           O  
ANISOU 6839  O   TRP B 391     7828   6930   6016   -949    198    -40       O  
ATOM   6840  CB  TRP B 391     -13.411   4.161  40.981  1.00 51.96           C  
ANISOU 6840  CB  TRP B 391     7559   6754   5428  -1302    307    -26       C  
ATOM   6841  CG  TRP B 391     -12.547   4.792  42.041  1.00 53.43           C  
ANISOU 6841  CG  TRP B 391     7717   6957   5627  -1396    334    -67       C  
ATOM   6842  CD1 TRP B 391     -11.373   4.305  42.542  1.00 56.84           C  
ANISOU 6842  CD1 TRP B 391     7973   7566   6059  -1449    388   -151       C  
ATOM   6843  CD2 TRP B 391     -12.821   6.008  42.767  1.00 53.40           C  
ANISOU 6843  CD2 TRP B 391     7862   6795   5632  -1437    300    -35       C  
ATOM   6844  NE1 TRP B 391     -10.916   5.121  43.563  1.00 56.96           N  
ANISOU 6844  NE1 TRP B 391     8004   7557   6081  -1531    381   -179       N  
ATOM   6845  CE2 TRP B 391     -11.780   6.179  43.711  1.00 57.36           C  
ANISOU 6845  CE2 TRP B 391     8265   7391   6138  -1534    333   -113       C  
ATOM   6846  CE3 TRP B 391     -13.869   6.943  42.741  1.00 54.46           C  
ANISOU 6846  CE3 TRP B 391     8202   6720   5769  -1383    243     45       C  
ATOM   6847  CZ2 TRP B 391     -11.738   7.262  44.586  1.00 56.14           C  
ANISOU 6847  CZ2 TRP B 391     8226   7119   5987  -1605    314   -121       C  
ATOM   6848  CZ3 TRP B 391     -13.834   8.007  43.628  1.00 56.10           C  
ANISOU 6848  CZ3 TRP B 391     8533   6796   5986  -1430    232     42       C  
ATOM   6849  CH2 TRP B 391     -12.789   8.146  44.549  1.00 56.68           C  
ANISOU 6849  CH2 TRP B 391     8517   6957   6063  -1548    268    -45       C  
ATOM   6850  N   VAL B 392     -16.432   4.488  41.959  1.00 53.01           N  
ANISOU 6850  N   VAL B 392     7831   6589   5720   -955    130     74       N  
ATOM   6851  CA  VAL B 392     -17.443   5.157  42.786  1.00 53.75           C  
ANISOU 6851  CA  VAL B 392     8005   6543   5874   -835     72    112       C  
ATOM   6852  C   VAL B 392     -18.221   4.127  43.615  1.00 58.73           C  
ANISOU 6852  C   VAL B 392     8488   7207   6618   -676     56     75       C  
ATOM   6853  O   VAL B 392     -18.315   4.305  44.815  1.00 58.73           O  
ANISOU 6853  O   VAL B 392     8472   7167   6677   -617     61     57       O  
ATOM   6854  CB  VAL B 392     -18.386   6.090  41.977  1.00 59.03           C  
ANISOU 6854  CB  VAL B 392     8854   7089   6485   -789      5    206       C  
ATOM   6855  CG1 VAL B 392     -19.476   6.683  42.862  1.00 58.89           C  
ANISOU 6855  CG1 VAL B 392     8895   6946   6534   -628    -50    235       C  
ATOM   6856  CG2 VAL B 392     -17.612   7.199  41.267  1.00 60.29           C  
ANISOU 6856  CG2 VAL B 392     9202   7179   6525   -955     35    257       C  
ATOM   6857  N   LEU B 393     -18.730   3.040  42.994  1.00 56.55           N  
ANISOU 6857  N   LEU B 393     8116   7006   6366   -624     47     59       N  
ATOM   6858  CA  LEU B 393     -19.476   1.979  43.687  1.00 56.31           C  
ANISOU 6858  CA  LEU B 393     7957   6998   6439   -505     49     25       C  
ATOM   6859  C   LEU B 393     -18.672   1.297  44.769  1.00 56.63           C  
ANISOU 6859  C   LEU B 393     7901   7089   6529   -494    114    -29       C  
ATOM   6860  O   LEU B 393     -19.231   0.865  45.773  1.00 55.62           O  
ANISOU 6860  O   LEU B 393     7716   6937   6479   -394    123    -37       O  
ATOM   6861  CB  LEU B 393     -20.015   0.932  42.699  1.00 57.91           C  
ANISOU 6861  CB  LEU B 393     8093   7266   6643   -496     35      1       C  
ATOM   6862  CG  LEU B 393     -21.097   1.419  41.718  1.00 66.54           C  
ANISOU 6862  CG  LEU B 393     9250   8341   7692   -466    -52     50       C  
ATOM   6863  CD1 LEU B 393     -21.292   0.420  40.588  1.00 69.05           C  
ANISOU 6863  CD1 LEU B 393     9513   8748   7977   -505    -61      6       C  
ATOM   6864  CD2 LEU B 393     -22.437   1.686  42.417  1.00 70.14           C  
ANISOU 6864  CD2 LEU B 393     9678   8748   8226   -332   -105     77       C  
ATOM   6865  N   CYS B 394     -17.368   1.200  44.570  1.00 53.31           N  
ANISOU 6865  N   CYS B 394     7454   6748   6053   -591    162    -64       N  
ATOM   6866  CA  CYS B 394     -16.459   0.592  45.529  1.00 53.72           C  
ANISOU 6866  CA  CYS B 394     7405   6877   6128   -568    214   -115       C  
ATOM   6867  C   CYS B 394     -16.213   1.461  46.756  1.00 55.86           C  
ANISOU 6867  C   CYS B 394     7707   7112   6404   -565    202   -114       C  
ATOM   6868  O   CYS B 394     -16.138   0.928  47.877  1.00 55.72           O  
ANISOU 6868  O   CYS B 394     7621   7120   6430   -473    219   -136       O  
ATOM   6869  CB  CYS B 394     -15.151   0.200  44.851  1.00 55.39           C  
ANISOU 6869  CB  CYS B 394     7552   7221   6272   -660    266   -161       C  
ATOM   6870  SG  CYS B 394     -15.305  -1.206  43.722  1.00 59.85           S  
ANISOU 6870  SG  CYS B 394     8063   7841   6838   -625    301   -196       S  
ATOM   6871  N   TRP B 395     -16.069   2.792  46.548  1.00 50.13           N  
ANISOU 6871  N   TRP B 395     7104   6320   5624   -666    177    -89       N  
ATOM   6872  CA  TRP B 395     -15.791   3.714  47.642  1.00 49.59           C  
ANISOU 6872  CA  TRP B 395     7091   6203   5547   -688    166   -105       C  
ATOM   6873  C   TRP B 395     -17.008   4.395  48.226  1.00 53.45           C  
ANISOU 6873  C   TRP B 395     7689   6542   6079   -581    125    -65       C  
ATOM   6874  O   TRP B 395     -16.887   4.963  49.312  1.00 54.95           O  
ANISOU 6874  O   TRP B 395     7917   6694   6269   -566    122    -91       O  
ATOM   6875  CB  TRP B 395     -14.741   4.748  47.246  1.00 49.37           C  
ANISOU 6875  CB  TRP B 395     7140   6187   5432   -884    181   -121       C  
ATOM   6876  CG  TRP B 395     -13.368   4.169  47.170  1.00 50.26           C  
ANISOU 6876  CG  TRP B 395     7103   6491   5504   -978    229   -186       C  
ATOM   6877  CD1 TRP B 395     -12.677   3.829  46.040  1.00 53.33           C  
ANISOU 6877  CD1 TRP B 395     7439   6984   5838  -1077    271   -193       C  
ATOM   6878  CD2 TRP B 395     -12.537   3.801  48.281  1.00 49.81           C  
ANISOU 6878  CD2 TRP B 395     6914   6564   5448   -957    238   -254       C  
ATOM   6879  NE1 TRP B 395     -11.455   3.296  46.376  1.00 53.31           N  
ANISOU 6879  NE1 TRP B 395     7270   7175   5810  -1115    310   -266       N  
ATOM   6880  CE2 TRP B 395     -11.348   3.253  47.750  1.00 54.33           C  
ANISOU 6880  CE2 TRP B 395     7345   7328   5971  -1036    284   -302       C  
ATOM   6881  CE3 TRP B 395     -12.692   3.860  49.680  1.00 50.21           C  
ANISOU 6881  CE3 TRP B 395     6949   6603   5525   -864    212   -281       C  
ATOM   6882  CZ2 TRP B 395     -10.297   2.804  48.575  1.00 53.25           C  
ANISOU 6882  CZ2 TRP B 395     7041   7378   5812  -1019    293   -374       C  
ATOM   6883  CZ3 TRP B 395     -11.674   3.365  50.488  1.00 51.31           C  
ANISOU 6883  CZ3 TRP B 395     6938   6923   5637   -850    219   -348       C  
ATOM   6884  CH2 TRP B 395     -10.496   2.842  49.936  1.00 52.27           C  
ANISOU 6884  CH2 TRP B 395     6909   7239   5711   -919    254   -392       C  
ATOM   6885  N   PHE B 396     -18.166   4.348  47.557  1.00 49.63           N  
ANISOU 6885  N   PHE B 396     7245   5989   5623   -500     92    -11       N  
ATOM   6886  CA  PHE B 396     -19.366   4.992  48.081  1.00 50.86           C  
ANISOU 6886  CA  PHE B 396     7481   6025   5817   -373     54     24       C  
ATOM   6887  C   PHE B 396     -19.755   4.447  49.470  1.00 54.38           C  
ANISOU 6887  C   PHE B 396     7839   6493   6331   -251     79     -7       C  
ATOM   6888  O   PHE B 396     -19.951   5.289  50.366  1.00 55.23           O  
ANISOU 6888  O   PHE B 396     8032   6520   6433   -207     73    -16       O  
ATOM   6889  CB  PHE B 396     -20.568   4.984  47.096  1.00 53.67           C  
ANISOU 6889  CB  PHE B 396     7861   6346   6185   -292      4     82       C  
ATOM   6890  CG  PHE B 396     -21.775   5.747  47.620  1.00 56.61           C  
ANISOU 6890  CG  PHE B 396     8306   6614   6589   -141    -34    116       C  
ATOM   6891  CD1 PHE B 396     -21.912   7.114  47.387  1.00 61.66           C  
ANISOU 6891  CD1 PHE B 396     9140   7115   7172   -134    -69    159       C  
ATOM   6892  CD2 PHE B 396     -22.760   5.102  48.369  1.00 58.24           C  
ANISOU 6892  CD2 PHE B 396     8393   6857   6878     -4    -26    104       C  
ATOM   6893  CE1 PHE B 396     -23.009   7.823  47.904  1.00 63.65           C  
ANISOU 6893  CE1 PHE B 396     9462   7272   7451     37   -100    184       C  
ATOM   6894  CE2 PHE B 396     -23.839   5.813  48.900  1.00 62.54           C  
ANISOU 6894  CE2 PHE B 396     8985   7329   7447    147    -50    126       C  
ATOM   6895  CZ  PHE B 396     -23.958   7.169  48.663  1.00 62.56           C  
ANISOU 6895  CZ  PHE B 396     9177   7199   7394    180    -90    164       C  
ATOM   6896  N   PRO B 397     -19.857   3.099  49.703  1.00 46.42           N  
ANISOU 6896  N   PRO B 397     6684   5577   5375   -197    113    -24       N  
ATOM   6897  CA  PRO B 397     -20.253   2.624  51.038  1.00 44.89           C  
ANISOU 6897  CA  PRO B 397     6432   5394   5230    -84    147    -38       C  
ATOM   6898  C   PRO B 397     -19.439   3.224  52.181  1.00 49.64           C  
ANISOU 6898  C   PRO B 397     7076   5999   5784   -101    156    -77       C  
ATOM   6899  O   PRO B 397     -20.050   3.802  53.068  1.00 50.89           O  
ANISOU 6899  O   PRO B 397     7291   6093   5950    -19    155    -78       O  
ATOM   6900  CB  PRO B 397     -20.128   1.111  50.928  1.00 45.83           C  
ANISOU 6900  CB  PRO B 397     6427   5597   5389    -65    192    -47       C  
ATOM   6901  CG  PRO B 397     -20.365   0.842  49.493  1.00 50.99           C  
ANISOU 6901  CG  PRO B 397     7072   6259   6043   -126    169    -35       C  
ATOM   6902  CD  PRO B 397     -19.681   1.961  48.782  1.00 47.00           C  
ANISOU 6902  CD  PRO B 397     6664   5732   5460   -232    131    -29       C  
ATOM   6903  N   PHE B 398     -18.090   3.182  52.119  1.00 45.20           N  
ANISOU 6903  N   PHE B 398     6487   5521   5165   -211    162   -117       N  
ATOM   6904  CA  PHE B 398     -17.203   3.760  53.135  1.00 44.63           C  
ANISOU 6904  CA  PHE B 398     6437   5486   5035   -255    157   -172       C  
ATOM   6905  C   PHE B 398     -17.318   5.262  53.237  1.00 49.81           C  
ANISOU 6905  C   PHE B 398     7257   6017   5652   -323    127   -185       C  
ATOM   6906  O   PHE B 398     -17.474   5.772  54.337  1.00 49.95           O  
ANISOU 6906  O   PHE B 398     7331   5995   5652   -274    124   -218       O  
ATOM   6907  CB  PHE B 398     -15.729   3.382  52.897  1.00 46.60           C  
ANISOU 6907  CB  PHE B 398     6589   5888   5228   -366    166   -219       C  
ATOM   6908  CG  PHE B 398     -14.740   4.182  53.721  1.00 49.15           C  
ANISOU 6908  CG  PHE B 398     6929   6269   5476   -462    146   -290       C  
ATOM   6909  CD1 PHE B 398     -14.433   3.809  55.029  1.00 53.20           C  
ANISOU 6909  CD1 PHE B 398     7379   6873   5962   -373    142   -328       C  
ATOM   6910  CD2 PHE B 398     -14.092   5.289  53.180  1.00 51.61           C  
ANISOU 6910  CD2 PHE B 398     7324   6551   5733   -654    133   -321       C  
ATOM   6911  CE1 PHE B 398     -13.514   4.541  55.788  1.00 55.28           C  
ANISOU 6911  CE1 PHE B 398     7646   7213   6144   -472    112   -408       C  
ATOM   6912  CE2 PHE B 398     -13.177   6.023  53.939  1.00 56.65           C  
ANISOU 6912  CE2 PHE B 398     7974   7251   6301   -773    115   -403       C  
ATOM   6913  CZ  PHE B 398     -12.897   5.648  55.243  1.00 55.42           C  
ANISOU 6913  CZ  PHE B 398     7738   7201   6117   -681     98   -453       C  
ATOM   6914  N   PHE B 399     -17.181   5.981  52.114  1.00 47.90           N  
ANISOU 6914  N   PHE B 399     7109   5706   5385   -441    111   -162       N  
ATOM   6915  CA  PHE B 399     -17.196   7.446  52.132  1.00 48.79           C  
ANISOU 6915  CA  PHE B 399     7418   5668   5453   -520     91   -169       C  
ATOM   6916  C   PHE B 399     -18.525   8.060  52.602  1.00 54.99           C  
ANISOU 6916  C   PHE B 399     8323   6298   6273   -355     75   -138       C  
ATOM   6917  O   PHE B 399     -18.500   9.130  53.193  1.00 55.56           O  
ANISOU 6917  O   PHE B 399     8550   6251   6310   -375     69   -172       O  
ATOM   6918  CB  PHE B 399     -16.745   8.024  50.791  1.00 50.01           C  
ANISOU 6918  CB  PHE B 399     7665   5776   5560   -681     89   -135       C  
ATOM   6919  CG  PHE B 399     -15.239   8.120  50.748  1.00 50.84           C  
ANISOU 6919  CG  PHE B 399     7716   6000   5600   -891    114   -200       C  
ATOM   6920  CD1 PHE B 399     -14.562   9.065  51.513  1.00 53.11           C  
ANISOU 6920  CD1 PHE B 399     8092   6251   5836  -1020    115   -271       C  
ATOM   6921  CD2 PHE B 399     -14.492   7.252  49.964  1.00 52.21           C  
ANISOU 6921  CD2 PHE B 399     7739   6339   5761   -962    140   -203       C  
ATOM   6922  CE1 PHE B 399     -13.171   9.141  51.485  1.00 53.89           C  
ANISOU 6922  CE1 PHE B 399     8108   6496   5873  -1229    136   -343       C  
ATOM   6923  CE2 PHE B 399     -13.094   7.348  49.924  1.00 54.96           C  
ANISOU 6923  CE2 PHE B 399     8006   6830   6046  -1151    168   -270       C  
ATOM   6924  CZ  PHE B 399     -12.445   8.285  50.690  1.00 52.61           C  
ANISOU 6924  CZ  PHE B 399     7775   6515   5700  -1288    163   -340       C  
ATOM   6925  N   PHE B 400     -19.657   7.371  52.376  1.00 51.61           N  
ANISOU 6925  N   PHE B 400     7816   5880   5912   -197     72    -85       N  
ATOM   6926  CA  PHE B 400     -20.975   7.783  52.832  1.00 51.44           C  
ANISOU 6926  CA  PHE B 400     7854   5762   5930    -18     63    -59       C  
ATOM   6927  C   PHE B 400     -21.026   7.482  54.337  1.00 54.56           C  
ANISOU 6927  C   PHE B 400     8193   6204   6334     67     99   -113       C  
ATOM   6928  O   PHE B 400     -21.474   8.336  55.104  1.00 55.77           O  
ANISOU 6928  O   PHE B 400     8463   6258   6470    148    102   -138       O  
ATOM   6929  CB  PHE B 400     -22.076   7.041  52.031  1.00 53.27           C  
ANISOU 6929  CB  PHE B 400     7979   6037   6224     90     48      2       C  
ATOM   6930  CG  PHE B 400     -23.494   7.281  52.489  1.00 56.18           C  
ANISOU 6930  CG  PHE B 400     8345   6362   6639    285     44     24       C  
ATOM   6931  CD1 PHE B 400     -24.218   8.369  52.020  1.00 61.37           C  
ANISOU 6931  CD1 PHE B 400     9144   6896   7277    375      0     63       C  
ATOM   6932  CD2 PHE B 400     -24.104   6.423  53.397  1.00 58.39           C  
ANISOU 6932  CD2 PHE B 400     8483   6727   6975    386     91      8       C  
ATOM   6933  CE1 PHE B 400     -25.523   8.608  52.466  1.00 63.05           C  
ANISOU 6933  CE1 PHE B 400     9333   7093   7529    578     -1     75       C  
ATOM   6934  CE2 PHE B 400     -25.413   6.655  53.837  1.00 61.88           C  
ANISOU 6934  CE2 PHE B 400     8901   7155   7457    560    100     20       C  
ATOM   6935  CZ  PHE B 400     -26.115   7.746  53.367  1.00 61.38           C  
ANISOU 6935  CZ  PHE B 400     8954   6990   7377    662     52     49       C  
ATOM   6936  N   SER B 401     -20.498   6.297  54.761  1.00 49.55           N  
ANISOU 6936  N   SER B 401     7399   5716   5712     53    129   -131       N  
ATOM   6937  CA  SER B 401     -20.444   5.838  56.163  1.00 48.31           C  
ANISOU 6937  CA  SER B 401     7186   5627   5544    134    165   -168       C  
ATOM   6938  C   SER B 401     -19.600   6.738  57.029  1.00 51.94           C  
ANISOU 6938  C   SER B 401     7748   6068   5921     63    150   -244       C  
ATOM   6939  O   SER B 401     -20.037   7.096  58.114  1.00 52.13           O  
ANISOU 6939  O   SER B 401     7827   6058   5922    159    167   -276       O  
ATOM   6940  CB  SER B 401     -19.913   4.415  56.264  1.00 50.39           C  
ANISOU 6940  CB  SER B 401     7288   6034   5822    132    195   -159       C  
ATOM   6941  OG  SER B 401     -20.958   3.484  56.077  1.00 59.51           O  
ANISOU 6941  OG  SER B 401     8358   7199   7054    232    232   -106       O  
ATOM   6942  N   TYR B 402     -18.399   7.086  56.556  1.00 49.32           N  
ANISOU 6942  N   TYR B 402     7434   5768   5537   -115    123   -282       N  
ATOM   6943  CA  TYR B 402     -17.444   7.976  57.207  1.00 51.84           C  
ANISOU 6943  CA  TYR B 402     7841   6085   5771   -242    103   -371       C  
ATOM   6944  C   TYR B 402     -18.071   9.380  57.398  1.00 58.30           C  
ANISOU 6944  C   TYR B 402     8885   6693   6572   -230     96   -392       C  
ATOM   6945  O   TYR B 402     -17.994   9.924  58.510  1.00 59.05           O  
ANISOU 6945  O   TYR B 402     9061   6762   6614   -210     96   -468       O  
ATOM   6946  CB  TYR B 402     -16.158   8.046  56.358  1.00 54.40           C  
ANISOU 6946  CB  TYR B 402     8121   6491   6056   -457     87   -396       C  
ATOM   6947  CG  TYR B 402     -14.947   8.691  57.001  1.00 58.08           C  
ANISOU 6947  CG  TYR B 402     8607   7030   6432   -628     66   -504       C  
ATOM   6948  CD1 TYR B 402     -14.641   8.466  58.341  1.00 59.97           C  
ANISOU 6948  CD1 TYR B 402     8788   7379   6618   -566     51   -573       C  
ATOM   6949  CD2 TYR B 402     -14.029   9.408  56.236  1.00 59.83           C  
ANISOU 6949  CD2 TYR B 402     8880   7241   6611   -864     62   -538       C  
ATOM   6950  CE1 TYR B 402     -13.497   9.005  58.923  1.00 61.96           C  
ANISOU 6950  CE1 TYR B 402     9032   7733   6777   -733     19   -686       C  
ATOM   6951  CE2 TYR B 402     -12.893   9.973  56.812  1.00 62.55           C  
ANISOU 6951  CE2 TYR B 402     9218   7677   6871  -1051     43   -650       C  
ATOM   6952  CZ  TYR B 402     -12.618   9.751  58.154  1.00 71.97           C  
ANISOU 6952  CZ  TYR B 402    10340   8992   8013   -984     14   -730       C  
ATOM   6953  OH  TYR B 402     -11.487  10.275  58.742  1.00 77.20           O  
ANISOU 6953  OH  TYR B 402    10973   9777   8583  -1174    -18   -854       O  
ATOM   6954  N   SER B 403     -18.758   9.914  56.335  1.00 53.79           N  
ANISOU 6954  N   SER B 403     8423   5975   6039   -214     89   -324       N  
ATOM   6955  CA  SER B 403     -19.451  11.213  56.314  1.00 54.18           C  
ANISOU 6955  CA  SER B 403     8707   5802   6076   -163     84   -322       C  
ATOM   6956  C   SER B 403     -20.567  11.249  57.315  1.00 57.25           C  
ANISOU 6956  C   SER B 403     9110   6154   6489     63    105   -332       C  
ATOM   6957  O   SER B 403     -20.626  12.183  58.123  1.00 58.76           O  
ANISOU 6957  O   SER B 403     9467   6228   6632     85    113   -401       O  
ATOM   6958  CB  SER B 403     -20.022  11.516  54.935  1.00 56.70           C  
ANISOU 6958  CB  SER B 403     9104   6015   6426   -145     65   -226       C  
ATOM   6959  OG  SER B 403     -18.958  11.646  54.013  1.00 68.70           O  
ANISOU 6959  OG  SER B 403    10644   7554   7904   -370     59   -220       O  
ATOM   6960  N   LEU B 404     -21.454  10.238  57.271  1.00 50.51           N  
ANISOU 6960  N   LEU B 404     8086   5400   5705    220    123   -271       N  
ATOM   6961  CA  LEU B 404     -22.552  10.134  58.217  1.00 50.44           C  
ANISOU 6961  CA  LEU B 404     8052   5393   5720    429    161   -276       C  
ATOM   6962  C   LEU B 404     -22.003  10.258  59.660  1.00 54.13           C  
ANISOU 6962  C   LEU B 404     8551   5902   6114    418    185   -371       C  
ATOM   6963  O   LEU B 404     -22.506  11.065  60.415  1.00 54.04           O  
ANISOU 6963  O   LEU B 404     8674   5790   6070    520    205   -420       O  
ATOM   6964  CB  LEU B 404     -23.242   8.767  58.054  1.00 48.97           C  
ANISOU 6964  CB  LEU B 404     7642   5354   5610    521    189   -212       C  
ATOM   6965  CG  LEU B 404     -24.439   8.621  57.135  1.00 52.03           C  
ANISOU 6965  CG  LEU B 404     7972   5727   6072    634    178   -138       C  
ATOM   6966  CD1 LEU B 404     -25.199   7.359  57.502  1.00 50.97           C  
ANISOU 6966  CD1 LEU B 404     7633   5734   6001    723    231   -109       C  
ATOM   6967  CD2 LEU B 404     -25.377   9.816  57.218  1.00 53.71           C  
ANISOU 6967  CD2 LEU B 404     8334   5798   6277    790    169   -138       C  
ATOM   6968  N   TYR B 405     -20.939   9.488  59.998  1.00 50.74           N  
ANISOU 6968  N   TYR B 405     8004   5626   5649    302    179   -399       N  
ATOM   6969  CA  TYR B 405     -20.270   9.454  61.293  1.00 51.88           C  
ANISOU 6969  CA  TYR B 405     8149   5858   5706    283    185   -485       C  
ATOM   6970  C   TYR B 405     -19.834  10.846  61.729  1.00 57.84           C  
ANISOU 6970  C   TYR B 405     9118   6479   6380    191    161   -589       C  
ATOM   6971  O   TYR B 405     -20.139  11.258  62.846  1.00 58.40           O  
ANISOU 6971  O   TYR B 405     9274   6524   6393    281    182   -657       O  
ATOM   6972  CB  TYR B 405     -19.089   8.441  61.295  1.00 53.45           C  
ANISOU 6972  CB  TYR B 405     8181   6253   5877    173    164   -489       C  
ATOM   6973  CG  TYR B 405     -18.231   8.492  62.546  1.00 58.38           C  
ANISOU 6973  CG  TYR B 405     8802   6992   6387    140    145   -583       C  
ATOM   6974  CD1 TYR B 405     -18.727   8.060  63.775  1.00 61.83           C  
ANISOU 6974  CD1 TYR B 405     9219   7493   6781    300    183   -589       C  
ATOM   6975  CD2 TYR B 405     -16.940   9.021  62.511  1.00 60.28           C  
ANISOU 6975  CD2 TYR B 405     9061   7290   6553    -60     90   -672       C  
ATOM   6976  CE1 TYR B 405     -17.963   8.163  64.943  1.00 64.49           C  
ANISOU 6976  CE1 TYR B 405     9566   7945   6991    280    155   -678       C  
ATOM   6977  CE2 TYR B 405     -16.166   9.120  63.669  1.00 62.20           C  
ANISOU 6977  CE2 TYR B 405     9292   7662   6679    -93     57   -772       C  
ATOM   6978  CZ  TYR B 405     -16.685   8.694  64.883  1.00 70.90           C  
ANISOU 6978  CZ  TYR B 405    10385   8823   7729     85     84   -774       C  
ATOM   6979  OH  TYR B 405     -15.928   8.766  66.023  1.00 73.93           O  
ANISOU 6979  OH  TYR B 405    10759   9352   7979     63     43   -871       O  
ATOM   6980  N   GLY B 406     -19.159  11.571  60.837  1.00 54.66           N  
ANISOU 6980  N   GLY B 406     8815   5982   5969      6    125   -603       N  
ATOM   6981  CA  GLY B 406     -18.718  12.935  61.098  1.00 55.61           C  
ANISOU 6981  CA  GLY B 406     9170   5941   6019   -121    110   -701       C  
ATOM   6982  C   GLY B 406     -19.860  13.866  61.462  1.00 59.70           C  
ANISOU 6982  C   GLY B 406     9895   6245   6542     56    140   -712       C  
ATOM   6983  O   GLY B 406     -19.660  14.797  62.237  1.00 61.91           O  
ANISOU 6983  O   GLY B 406    10362   6415   6747     18    143   -820       O  
ATOM   6984  N   ILE B 407     -21.074  13.602  60.939  1.00 54.16           N  
ANISOU 6984  N   ILE B 407     9156   5498   5924    259    162   -608       N  
ATOM   6985  CA  ILE B 407     -22.273  14.412  61.186  1.00 54.15           C  
ANISOU 6985  CA  ILE B 407     9318   5321   5934    475    192   -606       C  
ATOM   6986  C   ILE B 407     -23.032  13.999  62.467  1.00 59.68           C  
ANISOU 6986  C   ILE B 407     9937   6119   6620    679    245   -644       C  
ATOM   6987  O   ILE B 407     -23.342  14.875  63.279  1.00 61.61           O  
ANISOU 6987  O   ILE B 407    10361   6240   6806    768    273   -729       O  
ATOM   6988  CB  ILE B 407     -23.212  14.448  59.944  1.00 55.71           C  
ANISOU 6988  CB  ILE B 407     9511   5442   6215    597    180   -483       C  
ATOM   6989  CG1 ILE B 407     -22.490  14.962  58.702  1.00 56.37           C  
ANISOU 6989  CG1 ILE B 407     9715   5412   6290    401    138   -441       C  
ATOM   6990  CG2 ILE B 407     -24.432  15.291  60.203  1.00 57.00           C  
ANISOU 6990  CG2 ILE B 407     9827   5446   6385    848    206   -482       C  
ATOM   6991  CD1 ILE B 407     -23.021  14.392  57.404  1.00 56.80           C  
ANISOU 6991  CD1 ILE B 407     9649   5519   6414    455    110   -314       C  
ATOM   6992  N   CYS B 408     -23.370  12.705  62.633  1.00 55.46           N  
ANISOU 6992  N   CYS B 408     9153   5788   6132    754    271   -581       N  
ATOM   6993  CA  CYS B 408     -24.174  12.295  63.785  1.00 56.96           C  
ANISOU 6993  CA  CYS B 408     9270   6069   6304    944    339   -600       C  
ATOM   6994  C   CYS B 408     -23.494  11.303  64.732  1.00 58.88           C  
ANISOU 6994  C   CYS B 408     9375   6509   6487    888    356   -625       C  
ATOM   6995  O   CYS B 408     -24.118  10.911  65.711  1.00 59.62           O  
ANISOU 6995  O   CYS B 408     9417   6685   6553   1033    422   -632       O  
ATOM   6996  CB  CYS B 408     -25.558  11.799  63.368  1.00 58.05           C  
ANISOU 6996  CB  CYS B 408     9271   6246   6538   1139    383   -506       C  
ATOM   6997  SG  CYS B 408     -25.687  11.247  61.648  1.00 61.39           S  
ANISOU 6997  SG  CYS B 408     9567   6687   7071   1068    328   -387       S  
ATOM   6998  N   ARG B 409     -22.228  10.948  64.494  1.00 53.27           N  
ANISOU 6998  N   ARG B 409     8614   5881   5745    692    300   -641       N  
ATOM   6999  CA  ARG B 409     -21.403  10.078  65.348  1.00 51.98           C  
ANISOU 6999  CA  ARG B 409     8333   5911   5506    646    295   -666       C  
ATOM   7000  C   ARG B 409     -22.102   8.762  65.718  1.00 55.77           C  
ANISOU 7000  C   ARG B 409     8638   6526   6024    792    364   -574       C  
ATOM   7001  O   ARG B 409     -22.522   8.056  64.809  1.00 53.45           O  
ANISOU 7001  O   ARG B 409     8227   6247   5835    802    377   -479       O  
ATOM   7002  CB  ARG B 409     -20.890  10.838  66.590  1.00 52.43           C  
ANISOU 7002  CB  ARG B 409     8530   5967   5422    621    282   -801       C  
ATOM   7003  CG  ARG B 409     -20.108  12.109  66.278  1.00 58.25           C  
ANISOU 7003  CG  ARG B 409     9453   6564   6116    434    221   -907       C  
ATOM   7004  CD  ARG B 409     -18.628  11.844  66.229  1.00 69.42           C  
ANISOU 7004  CD  ARG B 409    10780   8129   7467    215    149   -960       C  
ATOM   7005  NE  ARG B 409     -17.897  12.933  65.585  1.00 75.39           N  
ANISOU 7005  NE  ARG B 409    11684   8751   8211    -10    104  -1034       N  
ATOM   7006  CZ  ARG B 409     -16.597  12.895  65.306  1.00 84.89           C  
ANISOU 7006  CZ  ARG B 409    12811  10072   9370   -240     46  -1087       C  
ATOM   7007  NH1 ARG B 409     -15.872  11.826  65.616  1.00 73.85           N1+
ANISOU 7007  NH1 ARG B 409    11191   8934   7936   -246     15  -1074       N1+
ATOM   7008  NH2 ARG B 409     -16.011  13.925  64.715  1.00 60.06           N  
ANISOU 7008  NH2 ARG B 409     9815   6789   6215   -463     24  -1151       N  
ATOM   7009  N   GLU B 410     -22.268   8.440  67.027  1.00 55.09           N  
ANISOU 7009  N   GLU B 410     8549   6534   5849    898    414   -601       N  
ATOM   7010  CA  GLU B 410     -22.884   7.162  67.445  1.00 54.66           C  
ANISOU 7010  CA  GLU B 410     8352   6599   5818   1016    496   -506       C  
ATOM   7011  C   GLU B 410     -24.392   7.082  67.175  1.00 56.35           C  
ANISOU 7011  C   GLU B 410     8523   6755   6133   1154    582   -443       C  
ATOM   7012  O   GLU B 410     -24.949   5.999  67.317  1.00 55.43           O  
ANISOU 7012  O   GLU B 410     8280   6723   6057   1213    657   -360       O  
ATOM   7013  CB  GLU B 410     -22.552   6.781  68.905  1.00 57.04           C  
ANISOU 7013  CB  GLU B 410     8670   7027   5974   1084    528   -538       C  
ATOM   7014  CG  GLU B 410     -23.101   7.734  69.955  1.00 71.79           C  
ANISOU 7014  CG  GLU B 410    10684   8846   7747   1188    570   -631       C  
ATOM   7015  CD  GLU B 410     -22.321   9.003  70.244  1.00 86.49           C  
ANISOU 7015  CD  GLU B 410    12714  10635   9511   1090    488   -777       C  
ATOM   7016  OE1 GLU B 410     -21.322   9.275  69.536  1.00 79.07           O  
ANISOU 7016  OE1 GLU B 410    11777   9679   8586    917    394   -810       O  
ATOM   7017  OE2 GLU B 410     -22.717   9.730  71.186  1.00 76.37           O  
ANISOU 7017  OE2 GLU B 410    11568   9315   8136   1179    526   -866       O  
ATOM   7018  N   ALA B 411     -25.027   8.193  66.746  1.00 52.28           N  
ANISOU 7018  N   ALA B 411     8108   6100   5657   1200    571   -481       N  
ATOM   7019  CA  ALA B 411     -26.443   8.229  66.371  1.00 52.08           C  
ANISOU 7019  CA  ALA B 411     8020   6042   5726   1342    634   -431       C  
ATOM   7020  C   ALA B 411     -26.657   7.720  64.929  1.00 57.26           C  
ANISOU 7020  C   ALA B 411     8554   6692   6510   1275    593   -345       C  
ATOM   7021  O   ALA B 411     -27.779   7.388  64.558  1.00 58.51           O  
ANISOU 7021  O   ALA B 411     8598   6882   6752   1367    640   -291       O  
ATOM   7022  CB  ALA B 411     -27.006   9.630  66.533  1.00 53.70           C  
ANISOU 7022  CB  ALA B 411     8394   6104   5906   1455    633   -506       C  
ATOM   7023  N   CYS B 412     -25.589   7.636  64.128  1.00 52.93           N  
ANISOU 7023  N   CYS B 412     8018   6123   5968   1111    509   -338       N  
ATOM   7024  CA  CYS B 412     -25.665   7.119  62.768  1.00 52.32           C  
ANISOU 7024  CA  CYS B 412     7840   6050   5992   1037    470   -266       C  
ATOM   7025  C   CYS B 412     -24.345   6.419  62.403  1.00 54.52           C  
ANISOU 7025  C   CYS B 412     8073   6393   6251    870    424   -257       C  
ATOM   7026  O   CYS B 412     -23.839   6.537  61.286  1.00 54.68           O  
ANISOU 7026  O   CYS B 412     8096   6378   6303    757    362   -242       O  
ATOM   7027  CB  CYS B 412     -26.015   8.234  61.789  1.00 54.32           C  
ANISOU 7027  CB  CYS B 412     8199   6162   6277   1050    409   -269       C  
ATOM   7028  SG  CYS B 412     -24.706   9.465  61.578  1.00 59.51           S  
ANISOU 7028  SG  CYS B 412     9080   6680   6853    895    329   -343       S  
ATOM   7029  N   GLN B 413     -23.784   5.694  63.365  1.00 49.94           N  
ANISOU 7029  N   GLN B 413     7452   5916   5606    870    457   -266       N  
ATOM   7030  CA  GLN B 413     -22.530   4.989  63.186  1.00 48.92           C  
ANISOU 7030  CA  GLN B 413     7268   5875   5446    755    417   -262       C  
ATOM   7031  C   GLN B 413     -22.825   3.612  62.611  1.00 53.93           C  
ANISOU 7031  C   GLN B 413     7760   6568   6163    759    459   -175       C  
ATOM   7032  O   GLN B 413     -23.461   2.796  63.287  1.00 54.94           O  
ANISOU 7032  O   GLN B 413     7834   6741   6298    850    542   -130       O  
ATOM   7033  CB  GLN B 413     -21.856   4.856  64.544  1.00 50.39           C  
ANISOU 7033  CB  GLN B 413     7484   6154   5508    787    426   -308       C  
ATOM   7034  CG  GLN B 413     -20.365   4.626  64.521  1.00 46.42           C  
ANISOU 7034  CG  GLN B 413     6950   5751   4935    674    356   -345       C  
ATOM   7035  CD  GLN B 413     -19.853   4.412  65.916  1.00 59.04           C  
ANISOU 7035  CD  GLN B 413     8565   7467   6400    738    360   -382       C  
ATOM   7036  OE1 GLN B 413     -18.793   3.838  66.119  1.00 60.19           O  
ANISOU 7036  OE1 GLN B 413     8645   7745   6481    708    318   -388       O  
ATOM   7037  NE2 GLN B 413     -20.586   4.855  66.922  1.00 52.97           N  
ANISOU 7037  NE2 GLN B 413     7882   6668   5576    843    409   -410       N  
ATOM   7038  N   VAL B 414     -22.387   3.343  61.368  1.00 49.47           N  
ANISOU 7038  N   VAL B 414     7146   5996   5654    655    413   -154       N  
ATOM   7039  CA  VAL B 414     -22.623   2.015  60.801  1.00 48.22           C  
ANISOU 7039  CA  VAL B 414     6873   5881   5569    650    454    -87       C  
ATOM   7040  C   VAL B 414     -21.789   1.013  61.620  1.00 51.40           C  
ANISOU 7040  C   VAL B 414     7245   6378   5908    677    485    -73       C  
ATOM   7041  O   VAL B 414     -20.739   1.404  62.149  1.00 50.73           O  
ANISOU 7041  O   VAL B 414     7196   6351   5729    655    436   -122       O  
ATOM   7042  CB  VAL B 414     -22.500   1.862  59.250  1.00 50.91           C  
ANISOU 7042  CB  VAL B 414     7170   6195   5979    549    407    -70       C  
ATOM   7043  CG1 VAL B 414     -23.020   3.090  58.523  1.00 50.59           C  
ANISOU 7043  CG1 VAL B 414     7201   6064   5959    531    353    -85       C  
ATOM   7044  CG2 VAL B 414     -21.082   1.512  58.807  1.00 50.50           C  
ANISOU 7044  CG2 VAL B 414     7096   6206   5885    450    366    -89       C  
ATOM   7045  N   PRO B 415     -22.277  -0.227  61.844  1.00 46.65           N  
ANISOU 7045  N   PRO B 415     6587   5794   5345    733    567     -8       N  
ATOM   7046  CA  PRO B 415     -21.550  -1.124  62.733  1.00 46.22           C  
ANISOU 7046  CA  PRO B 415     6537   5813   5213    794    601     20       C  
ATOM   7047  C   PRO B 415     -20.102  -1.376  62.345  1.00 52.60           C  
ANISOU 7047  C   PRO B 415     7317   6696   5972    748    530     -5       C  
ATOM   7048  O   PRO B 415     -19.779  -1.483  61.157  1.00 51.79           O  
ANISOU 7048  O   PRO B 415     7170   6580   5928    661    495    -14       O  
ATOM   7049  CB  PRO B 415     -22.394  -2.381  62.720  1.00 47.70           C  
ANISOU 7049  CB  PRO B 415     6690   5964   5470    829    708     99       C  
ATOM   7050  CG  PRO B 415     -23.727  -1.938  62.358  1.00 52.42           C  
ANISOU 7050  CG  PRO B 415     7258   6507   6154    811    740     98       C  
ATOM   7051  CD  PRO B 415     -23.531  -0.849  61.377  1.00 47.53           C  
ANISOU 7051  CD  PRO B 415     6639   5861   5561    740    638     42       C  
ATOM   7052  N   GLY B 416     -19.252  -1.410  63.379  1.00 50.71           N  
ANISOU 7052  N   GLY B 416     7099   6556   5614    813    507    -22       N  
ATOM   7053  CA  GLY B 416     -17.820  -1.657  63.300  1.00 50.23           C  
ANISOU 7053  CA  GLY B 416     6988   6618   5480    801    439    -52       C  
ATOM   7054  C   GLY B 416     -17.461  -2.614  62.192  1.00 54.36           C  
ANISOU 7054  C   GLY B 416     7445   7133   6075    776    452    -19       C  
ATOM   7055  O   GLY B 416     -16.797  -2.183  61.257  1.00 53.86           O  
ANISOU 7055  O   GLY B 416     7332   7103   6029    668    393    -70       O  
ATOM   7056  N   PRO B 417     -17.955  -3.891  62.203  1.00 52.28           N  
ANISOU 7056  N   PRO B 417     7194   6811   5859    858    540     63       N  
ATOM   7057  CA  PRO B 417     -17.600  -4.836  61.125  1.00 51.84           C  
ANISOU 7057  CA  PRO B 417     7096   6733   5868    837    558     81       C  
ATOM   7058  C   PRO B 417     -17.950  -4.375  59.713  1.00 56.79           C  
ANISOU 7058  C   PRO B 417     7687   7298   6591    693    532     43       C  
ATOM   7059  O   PRO B 417     -17.171  -4.594  58.779  1.00 57.91           O  
ANISOU 7059  O   PRO B 417     7778   7484   6741    644    501     14       O  
ATOM   7060  CB  PRO B 417     -18.404  -6.085  61.485  1.00 53.23           C  
ANISOU 7060  CB  PRO B 417     7333   6806   6085    922    672    169       C  
ATOM   7061  CG  PRO B 417     -18.579  -6.003  62.916  1.00 57.83           C  
ANISOU 7061  CG  PRO B 417     7975   7422   6575   1028    701    206       C  
ATOM   7062  CD  PRO B 417     -18.770  -4.570  63.232  1.00 53.70           C  
ANISOU 7062  CD  PRO B 417     7442   6940   6022    969    637    139       C  
ATOM   7063  N   LEU B 418     -19.123  -3.758  59.550  1.00 51.34           N  
ANISOU 7063  N   LEU B 418     7021   6521   5966    638    546     46       N  
ATOM   7064  CA  LEU B 418     -19.576  -3.319  58.244  1.00 49.51           C  
ANISOU 7064  CA  LEU B 418     6766   6234   5812    523    515     22       C  
ATOM   7065  C   LEU B 418     -18.771  -2.135  57.730  1.00 55.07           C  
ANISOU 7065  C   LEU B 418     7467   6986   6470    429    425    -39       C  
ATOM   7066  O   LEU B 418     -18.436  -2.110  56.558  1.00 57.48           O  
ANISOU 7066  O   LEU B 418     7745   7295   6800    340    398    -57       O  
ATOM   7067  CB  LEU B 418     -21.079  -3.060  58.264  1.00 48.73           C  
ANISOU 7067  CB  LEU B 418     6679   6051   5786    521    553     46       C  
ATOM   7068  CG  LEU B 418     -21.731  -2.866  56.939  1.00 51.35           C  
ANISOU 7068  CG  LEU B 418     6978   6337   6194    432    524     35       C  
ATOM   7069  CD1 LEU B 418     -21.473  -4.047  56.030  1.00 51.47           C  
ANISOU 7069  CD1 LEU B 418     6961   6344   6250    388    551     40       C  
ATOM   7070  CD2 LEU B 418     -23.186  -2.532  57.101  1.00 50.84           C  
ANISOU 7070  CD2 LEU B 418     6899   6230   6189    455    552     52       C  
ATOM   7071  N   PHE B 419     -18.401  -1.204  58.598  1.00 51.22           N  
ANISOU 7071  N   PHE B 419     7016   6538   5909    437    387    -74       N  
ATOM   7072  CA  PHE B 419     -17.554  -0.079  58.237  1.00 51.12           C  
ANISOU 7072  CA  PHE B 419     7016   6563   5844    322    313   -138       C  
ATOM   7073  C   PHE B 419     -16.168  -0.593  57.738  1.00 55.68           C  
ANISOU 7073  C   PHE B 419     7506   7272   6379    274    290   -167       C  
ATOM   7074  O   PHE B 419     -15.692  -0.131  56.704  1.00 55.53           O  
ANISOU 7074  O   PHE B 419     7471   7264   6363    149    260   -196       O  
ATOM   7075  CB  PHE B 419     -17.407   0.840  59.446  1.00 53.66           C  
ANISOU 7075  CB  PHE B 419     7400   6904   6085    343    285   -183       C  
ATOM   7076  CG  PHE B 419     -16.678   2.125  59.162  1.00 57.10           C  
ANISOU 7076  CG  PHE B 419     7880   7347   6469    198    219   -257       C  
ATOM   7077  CD1 PHE B 419     -17.336   3.205  58.584  1.00 61.41           C  
ANISOU 7077  CD1 PHE B 419     8528   7754   7050    129    203   -263       C  
ATOM   7078  CD2 PHE B 419     -15.341   2.277  59.511  1.00 60.94           C  
ANISOU 7078  CD2 PHE B 419     8312   7979   6864    131    173   -323       C  
ATOM   7079  CE1 PHE B 419     -16.669   4.411  58.360  1.00 63.35           C  
ANISOU 7079  CE1 PHE B 419     8852   7975   7244    -19    156   -328       C  
ATOM   7080  CE2 PHE B 419     -14.665   3.476  59.252  1.00 64.70           C  
ANISOU 7080  CE2 PHE B 419     8834   8457   7293    -40    123   -400       C  
ATOM   7081  CZ  PHE B 419     -15.340   4.541  58.705  1.00 62.66           C  
ANISOU 7081  CZ  PHE B 419     8709   8027   7072   -119    121   -400       C  
ATOM   7082  N   LYS B 420     -15.559  -1.575  58.449  1.00 52.56           N  
ANISOU 7082  N   LYS B 420     7056   6977   5938    388    310   -153       N  
ATOM   7083  CA  LYS B 420     -14.279  -2.229  58.109  1.00 52.41           C  
ANISOU 7083  CA  LYS B 420     6936   7104   5873    399    296   -178       C  
ATOM   7084  C   LYS B 420     -14.343  -2.954  56.745  1.00 53.75           C  
ANISOU 7084  C   LYS B 420     7075   7230   6115    364    332   -161       C  
ATOM   7085  O   LYS B 420     -13.360  -2.936  56.017  1.00 54.96           O  
ANISOU 7085  O   LYS B 420     7153   7491   6240    298    313   -204       O  
ATOM   7086  CB  LYS B 420     -13.872  -3.248  59.194  1.00 55.26           C  
ANISOU 7086  CB  LYS B 420     7274   7551   6172    583    316   -144       C  
ATOM   7087  CG  LYS B 420     -13.512  -2.646  60.547  1.00 67.95           C  
ANISOU 7087  CG  LYS B 420     8891   9257   7671    628    267   -175       C  
ATOM   7088  CD  LYS B 420     -13.610  -3.721  61.613  1.00 83.49           C  
ANISOU 7088  CD  LYS B 420    10889  11246   9587    832    309   -103       C  
ATOM   7089  CE  LYS B 420     -13.148  -3.275  62.981  1.00 98.28           C  
ANISOU 7089  CE  LYS B 420    12766  13251  11324    902    253   -133       C  
ATOM   7090  NZ  LYS B 420     -13.192  -4.396  63.963  1.00107.44           N1+
ANISOU 7090  NZ  LYS B 420    13971  14434  12418   1116    297    -46       N1+
ATOM   7091  N   PHE B 421     -15.477  -3.619  56.418  1.00 46.52           N  
ANISOU 7091  N   PHE B 421     6214   6174   5287    401    390   -106       N  
ATOM   7092  CA  PHE B 421     -15.678  -4.324  55.149  1.00 44.13           C  
ANISOU 7092  CA  PHE B 421     5899   5820   5049    361    423   -100       C  
ATOM   7093  C   PHE B 421     -15.726  -3.296  54.047  1.00 50.34           C  
ANISOU 7093  C   PHE B 421     6689   6595   5844    202    377   -134       C  
ATOM   7094  O   PHE B 421     -15.071  -3.484  53.021  1.00 53.36           O  
ANISOU 7094  O   PHE B 421     7028   7032   6213    138    376   -164       O  
ATOM   7095  CB  PHE B 421     -16.983  -5.148  55.169  1.00 44.74           C  
ANISOU 7095  CB  PHE B 421     6032   5755   5211    408    489    -47       C  
ATOM   7096  CG  PHE B 421     -17.362  -5.840  53.874  1.00 45.51           C  
ANISOU 7096  CG  PHE B 421     6129   5790   5374    347    518    -56       C  
ATOM   7097  CD1 PHE B 421     -16.658  -6.952  53.426  1.00 48.12           C  
ANISOU 7097  CD1 PHE B 421     6447   6140   5696    398    560    -70       C  
ATOM   7098  CD2 PHE B 421     -18.432  -5.386  53.110  1.00 47.69           C  
ANISOU 7098  CD2 PHE B 421     6419   5993   5708    251    499    -57       C  
ATOM   7099  CE1 PHE B 421     -17.018  -7.598  52.240  1.00 48.94           C  
ANISOU 7099  CE1 PHE B 421     6565   6182   5850    336    588    -94       C  
ATOM   7100  CE2 PHE B 421     -18.796  -6.034  51.927  1.00 49.81           C  
ANISOU 7100  CE2 PHE B 421     6685   6220   6021    189    516    -76       C  
ATOM   7101  CZ  PHE B 421     -18.082  -7.134  51.497  1.00 48.21           C  
ANISOU 7101  CZ  PHE B 421     6482   6028   5809    223    563    -99       C  
ATOM   7102  N   PHE B 422     -16.473  -2.189  54.264  1.00 44.51           N  
ANISOU 7102  N   PHE B 422     6012   5784   5117    149    343   -127       N  
ATOM   7103  CA  PHE B 422     -16.615  -1.086  53.319  1.00 43.71           C  
ANISOU 7103  CA  PHE B 422     5953   5642   5013     16    298   -142       C  
ATOM   7104  C   PHE B 422     -15.292  -0.545  52.777  1.00 50.27           C  
ANISOU 7104  C   PHE B 422     6749   6581   5772   -105    271   -192       C  
ATOM   7105  O   PHE B 422     -15.222  -0.255  51.585  1.00 51.51           O  
ANISOU 7105  O   PHE B 422     6921   6724   5925   -210    263   -193       O  
ATOM   7106  CB  PHE B 422     -17.458   0.038  53.920  1.00 45.26           C  
ANISOU 7106  CB  PHE B 422     6236   5744   5215     21    269   -130       C  
ATOM   7107  CG  PHE B 422     -18.925  -0.302  53.984  1.00 46.46           C  
ANISOU 7107  CG  PHE B 422     6405   5802   5445    102    295    -84       C  
ATOM   7108  CD1 PHE B 422     -19.428  -1.439  53.335  1.00 48.64           C  
ANISOU 7108  CD1 PHE B 422     6632   6068   5782    120    333    -63       C  
ATOM   7109  CD2 PHE B 422     -19.814   0.520  54.669  1.00 48.30           C  
ANISOU 7109  CD2 PHE B 422     6700   5964   5689    155    286    -73       C  
ATOM   7110  CE1 PHE B 422     -20.793  -1.745  53.375  1.00 49.44           C  
ANISOU 7110  CE1 PHE B 422     6726   6106   5955    167    357    -32       C  
ATOM   7111  CE2 PHE B 422     -21.179   0.213  54.711  1.00 51.63           C  
ANISOU 7111  CE2 PHE B 422     7105   6332   6181    228    314    -38       C  
ATOM   7112  CZ  PHE B 422     -21.664  -0.910  54.051  1.00 49.56           C  
ANISOU 7112  CZ  PHE B 422     6774   6076   5980    222    348    -18       C  
ATOM   7113  N   PHE B 423     -14.245  -0.414  53.614  1.00 48.00           N  
ANISOU 7113  N   PHE B 423     6406   6416   5418   -100    257   -234       N  
ATOM   7114  CA  PHE B 423     -12.996   0.070  53.040  1.00 48.79           C  
ANISOU 7114  CA  PHE B 423     6445   6642   5450   -239    241   -290       C  
ATOM   7115  C   PHE B 423     -12.223  -1.050  52.382  1.00 55.88           C  
ANISOU 7115  C   PHE B 423     7227   7663   6340   -197    279   -304       C  
ATOM   7116  O   PHE B 423     -11.423  -0.763  51.492  1.00 57.71           O  
ANISOU 7116  O   PHE B 423     7410   7986   6532   -323    286   -340       O  
ATOM   7117  CB  PHE B 423     -12.131   0.927  53.973  1.00 50.88           C  
ANISOU 7117  CB  PHE B 423     6686   7009   5636   -308    200   -352       C  
ATOM   7118  CG  PHE B 423     -11.731   0.434  55.330  1.00 51.81           C  
ANISOU 7118  CG  PHE B 423     6736   7238   5710   -173    184   -371       C  
ATOM   7119  CD1 PHE B 423     -10.690  -0.478  55.477  1.00 54.10           C  
ANISOU 7119  CD1 PHE B 423     6881   7721   5955    -90    189   -396       C  
ATOM   7120  CD2 PHE B 423     -12.301   0.980  56.478  1.00 54.65           C  
ANISOU 7120  CD2 PHE B 423     7181   7528   6054   -125    159   -372       C  
ATOM   7121  CE1 PHE B 423     -10.288  -0.905  56.747  1.00 55.30           C  
ANISOU 7121  CE1 PHE B 423     6977   7989   6045     53    163   -407       C  
ATOM   7122  CE2 PHE B 423     -11.896   0.558  57.752  1.00 57.46           C  
ANISOU 7122  CE2 PHE B 423     7485   8002   6346      1    140   -389       C  
ATOM   7123  CZ  PHE B 423     -10.894  -0.384  57.875  1.00 55.43           C  
ANISOU 7123  CZ  PHE B 423     7087   7934   6041     91    137   -401       C  
ATOM   7124  N   TRP B 424     -12.531  -2.325  52.721  1.00 51.91           N  
ANISOU 7124  N   TRP B 424     6702   7146   5876    -26    316   -273       N  
ATOM   7125  CA  TRP B 424     -11.939  -3.482  52.043  1.00 51.05           C  
ANISOU 7125  CA  TRP B 424     6518   7114   5766     42    362   -286       C  
ATOM   7126  C   TRP B 424     -12.563  -3.655  50.685  1.00 53.94           C  
ANISOU 7126  C   TRP B 424     6936   7381   6178    -35    388   -275       C  
ATOM   7127  O   TRP B 424     -11.844  -4.043  49.775  1.00 55.80           O  
ANISOU 7127  O   TRP B 424     7113   7705   6384    -66    418   -312       O  
ATOM   7128  CB  TRP B 424     -12.001  -4.746  52.880  1.00 50.16           C  
ANISOU 7128  CB  TRP B 424     6397   6993   5668    248    398   -254       C  
ATOM   7129  CG  TRP B 424     -10.866  -4.815  53.855  1.00 52.31           C  
ANISOU 7129  CG  TRP B 424     6571   7450   5856    342    370   -282       C  
ATOM   7130  CD1 TRP B 424     -10.893  -4.476  55.177  1.00 55.37           C  
ANISOU 7130  CD1 TRP B 424     6969   7867   6201    406    332   -270       C  
ATOM   7131  CD2 TRP B 424      -9.503  -5.178  53.562  1.00 53.19           C  
ANISOU 7131  CD2 TRP B 424     6539   7770   5900    381    372   -338       C  
ATOM   7132  NE1 TRP B 424      -9.641  -4.635  55.734  1.00 55.86           N  
ANISOU 7132  NE1 TRP B 424     6904   8149   6171    484    298   -312       N  
ATOM   7133  CE2 TRP B 424      -8.768  -5.060  54.762  1.00 57.35           C  
ANISOU 7133  CE2 TRP B 424     6986   8457   6346    473    322   -355       C  
ATOM   7134  CE3 TRP B 424      -8.832  -5.585  52.391  1.00 54.44           C  
ANISOU 7134  CE3 TRP B 424     6623   8014   6050    351    411   -380       C  
ATOM   7135  CZ2 TRP B 424      -7.403  -5.363  54.839  1.00 57.60           C  
ANISOU 7135  CZ2 TRP B 424     6848   8743   6294    547    304   -411       C  
ATOM   7136  CZ3 TRP B 424      -7.486  -5.909  52.475  1.00 57.11           C  
ANISOU 7136  CZ3 TRP B 424     6797   8592   6310    430    408   -435       C  
ATOM   7137  CH2 TRP B 424      -6.786  -5.800  53.688  1.00 58.50           C  
ANISOU 7137  CH2 TRP B 424     6879   8938   6412    530    351   -449       C  
ATOM   7138  N   ILE B 425     -13.848  -3.239  50.493  1.00 48.78           N  
ANISOU 7138  N   ILE B 425     6383   6568   5582    -76    372   -233       N  
ATOM   7139  CA  ILE B 425     -14.473  -3.184  49.156  1.00 48.37           C  
ANISOU 7139  CA  ILE B 425     6380   6446   5554   -164    373   -227       C  
ATOM   7140  C   ILE B 425     -13.664  -2.143  48.371  1.00 55.89           C  
ANISOU 7140  C   ILE B 425     7327   7476   6431   -323    351   -252       C  
ATOM   7141  O   ILE B 425     -13.428  -2.313  47.169  1.00 57.04           O  
ANISOU 7141  O   ILE B 425     7470   7654   6547   -394    371   -269       O  
ATOM   7142  CB  ILE B 425     -15.953  -2.724  49.160  1.00 50.81           C  
ANISOU 7142  CB  ILE B 425     6775   6608   5922   -171    342   -180       C  
ATOM   7143  CG1 ILE B 425     -16.886  -3.649  49.930  1.00 50.71           C  
ANISOU 7143  CG1 ILE B 425     6767   6516   5984    -50    375   -152       C  
ATOM   7144  CG2 ILE B 425     -16.467  -2.511  47.739  1.00 52.20           C  
ANISOU 7144  CG2 ILE B 425     6993   6747   6093   -264    321   -175       C  
ATOM   7145  CD1 ILE B 425     -18.308  -2.926  50.179  1.00 55.32           C  
ANISOU 7145  CD1 ILE B 425     7405   6997   6619    -51    341   -112       C  
ATOM   7146  N   GLY B 426     -13.270  -1.064  49.071  1.00 53.71           N  
ANISOU 7146  N   GLY B 426     7065   7225   6119   -387    317   -259       N  
ATOM   7147  CA  GLY B 426     -12.465   0.025  48.529  1.00 54.03           C  
ANISOU 7147  CA  GLY B 426     7117   7326   6086   -565    307   -284       C  
ATOM   7148  C   GLY B 426     -11.115  -0.445  48.022  1.00 58.08           C  
ANISOU 7148  C   GLY B 426     7498   8034   6538   -613    351   -341       C  
ATOM   7149  O   GLY B 426     -10.713  -0.085  46.908  1.00 58.15           O  
ANISOU 7149  O   GLY B 426     7516   8082   6496   -750    376   -350       O  
ATOM   7150  N   TYR B 427     -10.415  -1.264  48.845  1.00 54.68           N  
ANISOU 7150  N   TYR B 427     6941   7733   6101   -488    364   -377       N  
ATOM   7151  CA  TYR B 427      -9.119  -1.882  48.532  1.00 55.93           C  
ANISOU 7151  CA  TYR B 427     6942   8105   6203   -473    405   -438       C  
ATOM   7152  C   TYR B 427      -9.240  -2.913  47.403  1.00 62.11           C  
ANISOU 7152  C   TYR B 427     7723   8877   7001   -412    463   -439       C  
ATOM   7153  O   TYR B 427      -8.258  -3.124  46.691  1.00 62.36           O  
ANISOU 7153  O   TYR B 427     7651   9069   6972   -454    510   -490       O  
ATOM   7154  CB  TYR B 427      -8.495  -2.568  49.766  1.00 56.65           C  
ANISOU 7154  CB  TYR B 427     6917   8326   6282   -300    392   -463       C  
ATOM   7155  CG  TYR B 427      -7.963  -1.667  50.864  1.00 57.23           C  
ANISOU 7155  CG  TYR B 427     6942   8498   6306   -364    335   -496       C  
ATOM   7156  CD1 TYR B 427      -7.507  -0.380  50.581  1.00 59.99           C  
ANISOU 7156  CD1 TYR B 427     7297   8891   6607   -602    319   -535       C  
ATOM   7157  CD2 TYR B 427      -7.835  -2.130  52.171  1.00 56.99           C  
ANISOU 7157  CD2 TYR B 427     6866   8526   6263   -194    301   -495       C  
ATOM   7158  CE1 TYR B 427      -6.991   0.440  51.588  1.00 62.36           C  
ANISOU 7158  CE1 TYR B 427     7558   9279   6856   -683    267   -585       C  
ATOM   7159  CE2 TYR B 427      -7.315  -1.322  53.183  1.00 57.39           C  
ANISOU 7159  CE2 TYR B 427     6868   8685   6251   -257    241   -541       C  
ATOM   7160  CZ  TYR B 427      -6.892  -0.039  52.887  1.00 60.94           C  
ANISOU 7160  CZ  TYR B 427     7321   9173   6662   -508    223   -595       C  
ATOM   7161  OH  TYR B 427      -6.349   0.740  53.871  1.00 55.88           O  
ANISOU 7161  OH  TYR B 427     6637   8641   5955   -590    164   -659       O  
ATOM   7162  N   CYS B 428     -10.427  -3.563  47.254  1.00 60.14           N  
ANISOU 7162  N   CYS B 428     7579   8449   6825   -319    465   -394       N  
ATOM   7163  CA  CYS B 428     -10.697  -4.549  46.195  1.00 61.55           C  
ANISOU 7163  CA  CYS B 428     7781   8587   7017   -275    515   -408       C  
ATOM   7164  C   CYS B 428     -10.712  -3.915  44.849  1.00 66.94           C  
ANISOU 7164  C   CYS B 428     8508   9279   7648   -443    522   -414       C  
ATOM   7165  O   CYS B 428     -10.388  -4.594  43.883  1.00 67.59           O  
ANISOU 7165  O   CYS B 428     8570   9415   7697   -435    574   -454       O  
ATOM   7166  CB  CYS B 428     -11.981  -5.329  46.442  1.00 61.52           C  
ANISOU 7166  CB  CYS B 428     7874   8400   7102   -170    513   -369       C  
ATOM   7167  SG  CYS B 428     -11.835  -6.595  47.723  1.00 66.04           S  
ANISOU 7167  SG  CYS B 428     8418   8956   7716     59    548   -360       S  
ATOM   7168  N   ASN B 429     -11.074  -2.612  44.772  1.00 64.28           N  
ANISOU 7168  N   ASN B 429     8248   8882   7293   -588    474   -373       N  
ATOM   7169  CA  ASN B 429     -11.110  -1.842  43.519  1.00 64.73           C  
ANISOU 7169  CA  ASN B 429     8380   8931   7282   -754    477   -358       C  
ATOM   7170  C   ASN B 429      -9.754  -1.796  42.851  1.00 69.82           C  
ANISOU 7170  C   ASN B 429     8924   9771   7834   -854    545   -413       C  
ATOM   7171  O   ASN B 429      -9.686  -1.617  41.634  1.00 73.09           O  
ANISOU 7171  O   ASN B 429     9387  10206   8179   -958    576   -411       O  
ATOM   7172  CB  ASN B 429     -11.628  -0.416  43.733  1.00 63.76           C  
ANISOU 7172  CB  ASN B 429     8379   8697   7153   -869    420   -299       C  
ATOM   7173  CG  ASN B 429     -11.802   0.341  42.445  1.00 80.97           C  
ANISOU 7173  CG  ASN B 429    10673  10838   9255  -1013    421   -261       C  
ATOM   7174  OD1 ASN B 429     -10.966   1.153  42.075  1.00 76.05           O  
ANISOU 7174  OD1 ASN B 429    10061  10282   8551  -1176    454   -265       O  
ATOM   7175  ND2 ASN B 429     -12.861   0.057  41.705  1.00 77.04           N  
ANISOU 7175  ND2 ASN B 429    10259  10244   8769   -965    388   -226       N  
ATOM   7176  N   SER B 430      -8.678  -1.991  43.628  1.00 63.85           N  
ANISOU 7176  N   SER B 430     8018   9176   7065   -818    568   -465       N  
ATOM   7177  CA  SER B 430      -7.324  -1.977  43.103  1.00 64.47           C  
ANISOU 7177  CA  SER B 430     7956   9482   7056   -905    637   -529       C  
ATOM   7178  C   SER B 430      -7.010  -3.162  42.197  1.00 67.59           C  
ANISOU 7178  C   SER B 430     8294   9961   7425   -800    710   -578       C  
ATOM   7179  O   SER B 430      -6.114  -3.053  41.371  1.00 68.28           O  
ANISOU 7179  O   SER B 430     8302  10216   7426   -899    780   -623       O  
ATOM   7180  CB  SER B 430      -6.306  -1.845  44.226  1.00 68.86           C  
ANISOU 7180  CB  SER B 430     8347  10216   7601   -883    627   -579       C  
ATOM   7181  OG  SER B 430      -6.244  -0.505  44.684  1.00 78.21           O  
ANISOU 7181  OG  SER B 430     9581  11371   8766  -1071    587   -563       O  
ATOM   7182  N   SER B 431      -7.763  -4.261  42.303  1.00 63.17           N  
ANISOU 7182  N   SER B 431     7789   9279   6935   -617    703   -573       N  
ATOM   7183  CA  SER B 431      -7.538  -5.447  41.469  1.00 64.08           C  
ANISOU 7183  CA  SER B 431     7883   9437   7028   -508    774   -630       C  
ATOM   7184  C   SER B 431      -8.445  -5.508  40.248  1.00 67.29           C  
ANISOU 7184  C   SER B 431     8436   9716   7414   -584    775   -617       C  
ATOM   7185  O   SER B 431      -8.162  -6.281  39.317  1.00 68.34           O  
ANISOU 7185  O   SER B 431     8565   9904   7498   -545    842   -678       O  
ATOM   7186  CB  SER B 431      -7.719  -6.720  42.295  1.00 68.52           C  
ANISOU 7186  CB  SER B 431     8433   9935   7666   -265    779   -644       C  
ATOM   7187  OG  SER B 431      -9.006  -6.806  42.884  1.00 77.35           O  
ANISOU 7187  OG  SER B 431     9678  10834   8877   -228    719   -582       O  
ATOM   7188  N   LEU B 432      -9.542  -4.705  40.269  1.00 61.04           N  
ANISOU 7188  N   LEU B 432     7774   8765   6655   -677    697   -542       N  
ATOM   7189  CA  LEU B 432     -10.620  -4.676  39.271  1.00 59.49           C  
ANISOU 7189  CA  LEU B 432     7716   8445   6444   -733    665   -517       C  
ATOM   7190  C   LEU B 432     -10.264  -4.072  37.924  1.00 63.99           C  
ANISOU 7190  C   LEU B 432     8331   9098   6883   -890    697   -518       C  
ATOM   7191  O   LEU B 432     -10.771  -4.565  36.914  1.00 63.13           O  
ANISOU 7191  O   LEU B 432     8296   8960   6732   -890    701   -542       O  
ATOM   7192  CB  LEU B 432     -11.874  -3.981  39.828  1.00 57.73           C  
ANISOU 7192  CB  LEU B 432     7592   8051   6291   -748    568   -436       C  
ATOM   7193  CG  LEU B 432     -12.444  -4.567  41.120  1.00 60.86           C  
ANISOU 7193  CG  LEU B 432     7966   8349   6808   -603    541   -425       C  
ATOM   7194  CD1 LEU B 432     -13.696  -3.864  41.526  1.00 59.89           C  
ANISOU 7194  CD1 LEU B 432     7929   8084   6743   -618    458   -354       C  
ATOM   7195  CD2 LEU B 432     -12.698  -6.062  41.005  1.00 62.55           C  
ANISOU 7195  CD2 LEU B 432     8174   8522   7069   -476    584   -482       C  
ATOM   7196  N   ASN B 433      -9.454  -2.981  37.907  1.00 60.45           N  
ANISOU 7196  N   ASN B 433     7855   8747   6366  -1037    720   -491       N  
ATOM   7197  CA  ASN B 433      -9.069  -2.250  36.689  1.00 60.49           C  
ANISOU 7197  CA  ASN B 433     7923   8825   6236  -1213    764   -472       C  
ATOM   7198  C   ASN B 433      -8.467  -3.140  35.602  1.00 64.24           C  
ANISOU 7198  C   ASN B 433     8347   9440   6619  -1192    858   -554       C  
ATOM   7199  O   ASN B 433      -8.984  -3.097  34.479  1.00 62.43           O  
ANISOU 7199  O   ASN B 433     8238   9178   6306  -1247    852   -539       O  
ATOM   7200  CB  ASN B 433      -8.159  -1.075  37.009  1.00 60.90           C  
ANISOU 7200  CB  ASN B 433     7937   8963   6238  -1386    796   -446       C  
ATOM   7201  CG  ASN B 433      -8.880   0.116  37.559  1.00 72.64           C  
ANISOU 7201  CG  ASN B 433     9562  10276   7761  -1462    712   -354       C  
ATOM   7202  OD1 ASN B 433      -9.882   0.006  38.291  1.00 72.04           O  
ANISOU 7202  OD1 ASN B 433     9537  10048   7786  -1341    626   -322       O  
ATOM   7203  ND2 ASN B 433      -8.362   1.283  37.218  1.00 55.48           N  
ANISOU 7203  ND2 ASN B 433     7458   8121   5500  -1667    746   -312       N  
ATOM   7204  N   PRO B 434      -7.460  -4.016  35.903  1.00 61.98           N  
ANISOU 7204  N   PRO B 434     7894   9310   6343  -1088    938   -645       N  
ATOM   7205  CA  PRO B 434      -6.946  -4.916  34.854  1.00 62.68           C  
ANISOU 7205  CA  PRO B 434     7949   9521   6344  -1041   1034   -734       C  
ATOM   7206  C   PRO B 434      -8.013  -5.896  34.342  1.00 66.31           C  
ANISOU 7206  C   PRO B 434     8534   9830   6833   -930    998   -764       C  
ATOM   7207  O   PRO B 434      -7.936  -6.303  33.188  1.00 67.82           O  
ANISOU 7207  O   PRO B 434     8774  10075   6920   -952   1052   -819       O  
ATOM   7208  CB  PRO B 434      -5.758  -5.606  35.534  1.00 64.72           C  
ANISOU 7208  CB  PRO B 434     8003   9958   6629   -908   1108   -815       C  
ATOM   7209  CG  PRO B 434      -5.383  -4.668  36.654  1.00 69.12           C  
ANISOU 7209  CG  PRO B 434     8474  10553   7235   -984   1063   -765       C  
ATOM   7210  CD  PRO B 434      -6.706  -4.215  37.157  1.00 63.05           C  
ANISOU 7210  CD  PRO B 434     7867   9537   6554   -995    946   -675       C  
ATOM   7211  N   VAL B 435      -9.042  -6.207  35.165  1.00 60.65           N  
ANISOU 7211  N   VAL B 435     7872   8928   6245   -834    908   -732       N  
ATOM   7212  CA  VAL B 435     -10.178  -7.058  34.777  1.00 59.43           C  
ANISOU 7212  CA  VAL B 435     7829   8622   6128   -766    864   -761       C  
ATOM   7213  C   VAL B 435     -11.113  -6.246  33.842  1.00 62.09           C  
ANISOU 7213  C   VAL B 435     8301   8902   6388   -907    786   -700       C  
ATOM   7214  O   VAL B 435     -11.583  -6.785  32.849  1.00 62.65           O  
ANISOU 7214  O   VAL B 435     8450   8961   6393   -916    783   -753       O  
ATOM   7215  CB  VAL B 435     -10.950  -7.645  35.989  1.00 61.96           C  
ANISOU 7215  CB  VAL B 435     8153   8781   6607   -637    809   -744       C  
ATOM   7216  CG1 VAL B 435     -11.905  -8.743  35.549  1.00 61.70           C  
ANISOU 7216  CG1 VAL B 435     8215   8618   6610   -581    797   -806       C  
ATOM   7217  CG2 VAL B 435      -9.999  -8.167  37.063  1.00 62.06           C  
ANISOU 7217  CG2 VAL B 435     8043   8857   6680   -493    866   -769       C  
ATOM   7218  N   ILE B 436     -11.360  -4.959  34.152  1.00 57.42           N  
ANISOU 7218  N   ILE B 436     7746   8277   5795  -1006    722   -593       N  
ATOM   7219  CA  ILE B 436     -12.184  -4.043  33.350  1.00 57.14           C  
ANISOU 7219  CA  ILE B 436     7847   8187   5675  -1113    643   -514       C  
ATOM   7220  C   ILE B 436     -11.594  -3.847  31.941  1.00 64.42           C  
ANISOU 7220  C   ILE B 436     8825   9238   6413  -1224    710   -532       C  
ATOM   7221  O   ILE B 436     -12.347  -3.816  30.958  1.00 64.78           O  
ANISOU 7221  O   ILE B 436     8984   9262   6368  -1253    655   -520       O  
ATOM   7222  CB  ILE B 436     -12.374  -2.692  34.083  1.00 59.43           C  
ANISOU 7222  CB  ILE B 436     8178   8402   6000  -1178    583   -399       C  
ATOM   7223  CG1 ILE B 436     -13.242  -2.859  35.361  1.00 57.04           C  
ANISOU 7223  CG1 ILE B 436     7847   7963   5862  -1063    506   -377       C  
ATOM   7224  CG2 ILE B 436     -12.915  -1.595  33.125  1.00 61.60           C  
ANISOU 7224  CG2 ILE B 436     8616   8638   6150  -1287    526   -303       C  
ATOM   7225  CD1 ILE B 436     -13.216  -1.672  36.346  1.00 55.14           C  
ANISOU 7225  CD1 ILE B 436     7627   7655   5670  -1100    468   -293       C  
ATOM   7226  N   TYR B 437     -10.255  -3.702  31.844  1.00 63.04           N  
ANISOU 7226  N   TYR B 437     8562   9216   6174  -1286    828   -562       N  
ATOM   7227  CA  TYR B 437      -9.585  -3.528  30.551  1.00 64.42           C  
ANISOU 7227  CA  TYR B 437     8776   9536   6166  -1398    918   -582       C  
ATOM   7228  C   TYR B 437      -9.674  -4.802  29.726  1.00 69.91           C  
ANISOU 7228  C   TYR B 437     9473  10280   6809  -1306    959   -702       C  
ATOM   7229  O   TYR B 437     -10.015  -4.725  28.544  1.00 72.08           O  
ANISOU 7229  O   TYR B 437     9865  10583   6940  -1369    952   -703       O  
ATOM   7230  CB  TYR B 437      -8.113  -3.115  30.705  1.00 65.99           C  
ANISOU 7230  CB  TYR B 437     8845   9912   6314  -1494   1046   -598       C  
ATOM   7231  CG  TYR B 437      -7.854  -1.880  31.536  1.00 66.03           C  
ANISOU 7231  CG  TYR B 437     8845   9881   6364  -1614   1023   -504       C  
ATOM   7232  CD1 TYR B 437      -8.553  -0.701  31.302  1.00 67.91           C  
ANISOU 7232  CD1 TYR B 437     9265   9982   6557  -1729    950   -380       C  
ATOM   7233  CD2 TYR B 437      -6.835  -1.856  32.479  1.00 66.52           C  
ANISOU 7233  CD2 TYR B 437     8726  10057   6491  -1618   1080   -546       C  
ATOM   7234  CE1 TYR B 437      -8.308   0.445  32.056  1.00 69.22           C  
ANISOU 7234  CE1 TYR B 437     9454  10088   6759  -1845    937   -305       C  
ATOM   7235  CE2 TYR B 437      -6.569  -0.713  33.230  1.00 67.28           C  
ANISOU 7235  CE2 TYR B 437     8824  10121   6618  -1751   1060   -479       C  
ATOM   7236  CZ  TYR B 437      -7.313   0.436  33.019  1.00 75.34           C  
ANISOU 7236  CZ  TYR B 437    10049  10972   7604  -1870    993   -361       C  
ATOM   7237  OH  TYR B 437      -7.054   1.571  33.752  1.00 77.29           O  
ANISOU 7237  OH  TYR B 437    10326  11161   7878  -2006    980   -304       O  
ATOM   7238  N   THR B 438      -9.386  -5.971  30.339  1.00 64.99           N  
ANISOU 7238  N   THR B 438     8742   9658   6292  -1153   1001   -805       N  
ATOM   7239  CA  THR B 438      -9.439  -7.258  29.641  1.00 65.81           C  
ANISOU 7239  CA  THR B 438     8869   9779   6358  -1055   1051   -935       C  
ATOM   7240  C   THR B 438     -10.805  -7.438  28.997  1.00 69.43           C  
ANISOU 7240  C   THR B 438     9476  10112   6791  -1078    939   -934       C  
ATOM   7241  O   THR B 438     -10.886  -7.677  27.790  1.00 71.42           O  
ANISOU 7241  O   THR B 438     9812  10430   6895  -1124    960   -991       O  
ATOM   7242  CB  THR B 438      -9.111  -8.427  30.585  1.00 77.76           C  
ANISOU 7242  CB  THR B 438    10283  11250   8011   -868   1095  -1020       C  
ATOM   7243  OG1 THR B 438      -7.938  -8.129  31.334  1.00 80.80           O  
ANISOU 7243  OG1 THR B 438    10508  11768   8424   -839   1166  -1006       O  
ATOM   7244  CG2 THR B 438      -8.911  -9.740  29.841  1.00 77.98           C  
ANISOU 7244  CG2 THR B 438    10346  11297   7985   -763   1179  -1166       C  
ATOM   7245  N   VAL B 439     -11.868  -7.259  29.796  1.00 62.72           N  
ANISOU 7245  N   VAL B 439     8650   9106   6075  -1051    818   -870       N  
ATOM   7246  CA  VAL B 439     -13.260  -7.421  29.377  1.00 61.67           C  
ANISOU 7246  CA  VAL B 439     8618   8871   5944  -1066    696   -871       C  
ATOM   7247  C   VAL B 439     -13.680  -6.405  28.297  1.00 65.95           C  
ANISOU 7247  C   VAL B 439     9272   9471   6317  -1184    626   -791       C  
ATOM   7248  O   VAL B 439     -14.110  -6.831  27.231  1.00 66.83           O  
ANISOU 7248  O   VAL B 439     9461   9622   6308  -1209    600   -858       O  
ATOM   7249  CB  VAL B 439     -14.240  -7.424  30.596  1.00 63.11           C  
ANISOU 7249  CB  VAL B 439     8769   8897   6313  -1004    599   -818       C  
ATOM   7250  CG1 VAL B 439     -15.697  -7.475  30.150  1.00 62.83           C  
ANISOU 7250  CG1 VAL B 439     8805   8796   6274  -1032    468   -818       C  
ATOM   7251  CG2 VAL B 439     -13.939  -8.571  31.551  1.00 61.99           C  
ANISOU 7251  CG2 VAL B 439     8554   8683   6315   -881    669   -896       C  
ATOM   7252  N   PHE B 440     -13.524  -5.089  28.549  1.00 61.87           N  
ANISOU 7252  N   PHE B 440     8778   8953   5776  -1253    599   -653       N  
ATOM   7253  CA  PHE B 440     -14.050  -4.031  27.673  1.00 62.35           C  
ANISOU 7253  CA  PHE B 440     8976   9028   5687  -1340    519   -546       C  
ATOM   7254  C   PHE B 440     -13.114  -3.443  26.588  1.00 69.67           C  
ANISOU 7254  C   PHE B 440     9980  10089   6402  -1460    617   -515       C  
ATOM   7255  O   PHE B 440     -13.620  -2.851  25.626  1.00 69.73           O  
ANISOU 7255  O   PHE B 440    10129  10116   6250  -1513    554   -446       O  
ATOM   7256  CB  PHE B 440     -14.619  -2.904  28.532  1.00 62.29           C  
ANISOU 7256  CB  PHE B 440     8997   8900   5769  -1336    426   -406       C  
ATOM   7257  CG  PHE B 440     -15.785  -3.397  29.353  1.00 61.74           C  
ANISOU 7257  CG  PHE B 440     8873   8718   5867  -1228    318   -427       C  
ATOM   7258  CD1 PHE B 440     -17.040  -3.552  28.783  1.00 64.59           C  
ANISOU 7258  CD1 PHE B 440     9285   9066   6192  -1198    190   -433       C  
ATOM   7259  CD2 PHE B 440     -15.620  -3.744  30.685  1.00 62.01           C  
ANISOU 7259  CD2 PHE B 440     8796   8679   6085  -1160    347   -447       C  
ATOM   7260  CE1 PHE B 440     -18.116  -4.019  29.540  1.00 64.44           C  
ANISOU 7260  CE1 PHE B 440     9194   8964   6327  -1119    104   -459       C  
ATOM   7261  CE2 PHE B 440     -16.696  -4.198  31.441  1.00 63.44           C  
ANISOU 7261  CE2 PHE B 440     8930   8762   6412  -1074    265   -462       C  
ATOM   7262  CZ  PHE B 440     -17.938  -4.332  30.863  1.00 61.67           C  
ANISOU 7262  CZ  PHE B 440     8745   8528   6159  -1062    149   -470       C  
ATOM   7263  N   ASN B 441     -11.797  -3.614  26.705  1.00 68.91           N  
ANISOU 7263  N   ASN B 441     9791  10099   6291  -1498    770   -563       N  
ATOM   7264  CA  ASN B 441     -10.893  -3.096  25.678  1.00 71.58           C  
ANISOU 7264  CA  ASN B 441    10187  10583   6425  -1628    883   -540       C  
ATOM   7265  C   ASN B 441     -10.152  -4.235  24.975  1.00 77.98           C  
ANISOU 7265  C   ASN B 441    10930  11546   7153  -1592   1009   -697       C  
ATOM   7266  O   ASN B 441      -9.361  -4.948  25.607  1.00 79.00           O  
ANISOU 7266  O   ASN B 441    10904  11728   7384  -1518   1102   -790       O  
ATOM   7267  CB  ASN B 441      -9.934  -2.037  26.251  1.00 73.48           C  
ANISOU 7267  CB  ASN B 441    10386  10853   6681  -1749    966   -449       C  
ATOM   7268  CG  ASN B 441      -9.188  -1.259  25.194  1.00 97.13           C  
ANISOU 7268  CG  ASN B 441    13477  13970   9458  -1923   1076   -389       C  
ATOM   7269  OD1 ASN B 441      -7.978  -1.404  25.039  1.00 95.05           O  
ANISOU 7269  OD1 ASN B 441    13100  13874   9140  -1996   1232   -449       O  
ATOM   7270  ND2 ASN B 441      -9.889  -0.426  24.434  1.00 88.96           N  
ANISOU 7270  ND2 ASN B 441    12651  12865   8284  -1986   1001   -267       N  
ATOM   7271  N   GLN B 442     -10.437  -4.421  23.676  1.00 74.26           N  
ANISOU 7271  N   GLN B 442    10582  11145   6489  -1626   1007   -728       N  
ATOM   7272  CA  GLN B 442      -9.818  -5.459  22.843  1.00 74.68           C  
ANISOU 7272  CA  GLN B 442    10608  11339   6430  -1592   1127   -885       C  
ATOM   7273  C   GLN B 442      -8.286  -5.360  22.745  1.00 77.57           C  
ANISOU 7273  C   GLN B 442    10856  11889   6729  -1649   1326   -917       C  
ATOM   7274  O   GLN B 442      -7.627  -6.391  22.672  1.00 76.48           O  
ANISOU 7274  O   GLN B 442    10616  11842   6599  -1551   1435  -1064       O  
ATOM   7275  CB  GLN B 442     -10.450  -5.508  21.438  1.00 77.62           C  
ANISOU 7275  CB  GLN B 442    11152  11761   6578  -1636   1076   -902       C  
ATOM   7276  CG  GLN B 442     -10.440  -4.193  20.657  1.00 93.38           C  
ANISOU 7276  CG  GLN B 442    13298  13809   8373  -1780   1068   -739       C  
ATOM   7277  CD  GLN B 442     -10.552  -4.423  19.170  1.00116.12           C  
ANISOU 7277  CD  GLN B 442    16319  16816  10986  -1819   1088   -788       C  
ATOM   7278  OE1 GLN B 442      -9.608  -4.887  18.511  1.00112.95           O  
ANISOU 7278  OE1 GLN B 442    15887  16573  10454  -1846   1252   -887       O  
ATOM   7279  NE2 GLN B 442     -11.708  -4.095  18.606  1.00109.24           N  
ANISOU 7279  NE2 GLN B 442    15598  15892  10015  -1814    920   -723       N  
ATOM   7280  N   ASP B 443      -7.733  -4.127  22.757  1.00 74.76           N  
ANISOU 7280  N   ASP B 443    10514  11586   6307  -1805   1376   -784       N  
ATOM   7281  CA  ASP B 443      -6.290  -3.846  22.662  1.00 75.58           C  
ANISOU 7281  CA  ASP B 443    10491  11890   6338  -1906   1566   -802       C  
ATOM   7282  C   ASP B 443      -5.513  -4.332  23.890  1.00 77.31           C  
ANISOU 7282  C   ASP B 443    10471  12151   6752  -1808   1619   -877       C  
ATOM   7283  O   ASP B 443      -4.443  -4.909  23.722  1.00 79.02           O  
ANISOU 7283  O   ASP B 443    10535  12562   6927  -1770   1770   -988       O  
ATOM   7284  CB  ASP B 443      -6.025  -2.353  22.374  1.00 78.29           C  
ANISOU 7284  CB  ASP B 443    10940  12244   6561  -2130   1599   -635       C  
ATOM   7285  CG  ASP B 443      -6.727  -1.802  21.137  1.00 88.52           C  
ANISOU 7285  CG  ASP B 443    12489  13507   7637  -2213   1549   -539       C  
ATOM   7286  OD1 ASP B 443      -6.406  -2.260  20.008  1.00 90.34           O1-
ANISOU 7286  OD1 ASP B 443    12762  13889   7672  -2228   1645   -611       O1-
ATOM   7287  OD2 ASP B 443      -7.587  -0.911  21.294  1.00 94.26           O  
ANISOU 7287  OD2 ASP B 443    13376  14064   8376  -2249   1416   -392       O  
ATOM   7288  N   PHE B 444      -6.058  -4.125  25.112  1.00 69.65           N  
ANISOU 7288  N   PHE B 444     9468  11013   5982  -1751   1496   -820       N  
ATOM   7289  CA  PHE B 444      -5.455  -4.608  26.362  1.00 67.62           C  
ANISOU 7289  CA  PHE B 444     9004  10783   5907  -1635   1519   -881       C  
ATOM   7290  C   PHE B 444      -5.593  -6.120  26.428  1.00 73.82           C  
ANISOU 7290  C   PHE B 444     9739  11549   6761  -1410   1528  -1027       C  
ATOM   7291  O   PHE B 444      -4.636  -6.788  26.804  1.00 75.35           O  
ANISOU 7291  O   PHE B 444     9760  11877   6993  -1299   1630  -1123       O  
ATOM   7292  CB  PHE B 444      -6.134  -4.002  27.600  1.00 66.20           C  
ANISOU 7292  CB  PHE B 444     8836  10414   5902  -1628   1381   -780       C  
ATOM   7293  CG  PHE B 444      -5.538  -2.717  28.122  1.00 66.24           C  
ANISOU 7293  CG  PHE B 444     8803  10456   5909  -1808   1405   -681       C  
ATOM   7294  CD1 PHE B 444      -4.294  -2.708  28.736  1.00 68.66           C  
ANISOU 7294  CD1 PHE B 444     8892  10946   6249  -1835   1508   -736       C  
ATOM   7295  CD2 PHE B 444      -6.247  -1.524  28.051  1.00 66.97           C  
ANISOU 7295  CD2 PHE B 444     9078  10395   5974  -1942   1319   -539       C  
ATOM   7296  CE1 PHE B 444      -3.750  -1.522  29.222  1.00 69.81           C  
ANISOU 7296  CE1 PHE B 444     9004  11126   6394  -2030   1530   -661       C  
ATOM   7297  CE2 PHE B 444      -5.707  -0.344  28.554  1.00 69.80           C  
ANISOU 7297  CE2 PHE B 444     9429  10757   6336  -2120   1348   -457       C  
ATOM   7298  CZ  PHE B 444      -4.461  -0.352  29.128  1.00 68.63           C  
ANISOU 7298  CZ  PHE B 444     9065  10795   6218  -2179   1454   -524       C  
ATOM   7299  N   ARG B 445      -6.784  -6.660  26.072  1.00 69.66           N  
ANISOU 7299  N   ARG B 445     9365  10856   6247  -1343   1421  -1047       N  
ATOM   7300  CA  ARG B 445      -7.065  -8.099  26.031  1.00 69.49           C  
ANISOU 7300  CA  ARG B 445     9350  10773   6281  -1160   1428  -1189       C  
ATOM   7301  C   ARG B 445      -6.021  -8.799  25.148  1.00 76.54           C  
ANISOU 7301  C   ARG B 445    10189  11864   7031  -1111   1598  -1324       C  
ATOM   7302  O   ARG B 445      -5.438  -9.789  25.571  1.00 76.40           O  
ANISOU 7302  O   ARG B 445    10068  11876   7086   -936   1675  -1434       O  
ATOM   7303  CB  ARG B 445      -8.477  -8.349  25.478  1.00 68.28           C  
ANISOU 7303  CB  ARG B 445     9378  10458   6107  -1173   1295  -1192       C  
ATOM   7304  CG  ARG B 445      -9.085  -9.694  25.876  1.00 74.71           C  
ANISOU 7304  CG  ARG B 445    10214  11123   7051  -1014   1261  -1310       C  
ATOM   7305  CD  ARG B 445     -10.173 -10.172  24.917  1.00 86.56           C  
ANISOU 7305  CD  ARG B 445    11876  12547   8465  -1049   1179  -1378       C  
ATOM   7306  NE  ARG B 445     -11.019  -9.086  24.408  1.00103.87           N  
ANISOU 7306  NE  ARG B 445    14165  14736  10567  -1189   1052  -1255       N  
ATOM   7307  CZ  ARG B 445     -12.119  -8.633  25.005  1.00125.54           C  
ANISOU 7307  CZ  ARG B 445    16933  17345  13422  -1206    900  -1162       C  
ATOM   7308  NH1 ARG B 445     -12.535  -9.169  26.147  1.00115.26           N  
ANISOU 7308  NH1 ARG B 445    15567  15899  12326  -1114    862  -1175       N  
ATOM   7309  NH2 ARG B 445     -12.812  -7.640  24.463  1.00114.36           N1+
ANISOU 7309  NH2 ARG B 445    15609  15940  11901  -1303    790  -1051       N1+
ATOM   7310  N   ARG B 446      -5.757  -8.236  23.951  1.00 76.36           N  
ANISOU 7310  N   ARG B 446    10238  11979   6796  -1258   1663  -1308       N  
ATOM   7311  CA  ARG B 446      -4.783  -8.709  22.965  1.00 79.21           C  
ANISOU 7311  CA  ARG B 446    10558  12555   6983  -1242   1837  -1425       C  
ATOM   7312  C   ARG B 446      -3.360  -8.515  23.512  1.00 83.95           C  
ANISOU 7312  C   ARG B 446    10918  13369   7609  -1228   1980  -1439       C  
ATOM   7313  O   ARG B 446      -2.467  -9.299  23.190  1.00 84.71           O  
ANISOU 7313  O   ARG B 446    10906  13632   7647  -1107   2125  -1572       O  
ATOM   7314  CB  ARG B 446      -4.989  -7.934  21.639  1.00 83.89           C  
ANISOU 7314  CB  ARG B 446    11308  13229   7336  -1432   1852  -1364       C  
ATOM   7315  CG  ARG B 446      -4.219  -8.409  20.392  1.00104.18           C  
ANISOU 7315  CG  ARG B 446    13889  16013   9682  -1434   2024  -1486       C  
ATOM   7316  CD  ARG B 446      -2.805  -7.831  20.261  1.00124.88           C  
ANISOU 7316  CD  ARG B 446    16339  18902  12209  -1534   2214  -1469       C  
ATOM   7317  NE  ARG B 446      -2.747  -6.379  20.462  1.00138.21           N  
ANISOU 7317  NE  ARG B 446    18044  20595  13875  -1762   2187  -1285       N  
ATOM   7318  CZ  ARG B 446      -1.646  -5.700  20.778  1.00153.81           C  
ANISOU 7318  CZ  ARG B 446    19846  22752  15841  -1887   2313  -1244       C  
ATOM   7319  NH1 ARG B 446      -0.488  -6.333  20.938  1.00140.23           N1+
ANISOU 7319  NH1 ARG B 446    17892  21258  14131  -1788   2469  -1373       N1+
ATOM   7320  NH2 ARG B 446      -1.694  -4.385  20.937  1.00141.66           N  
ANISOU 7320  NH2 ARG B 446    18369  21174  14282  -2109   2285  -1080       N  
ATOM   7321  N   SER B 447      -3.146  -7.473  24.325  1.00 80.75           N  
ANISOU 7321  N   SER B 447    10427  12970   7285  -1349   1940  -1312       N  
ATOM   7322  CA  SER B 447      -1.828  -7.218  24.894  1.00 82.61           C  
ANISOU 7322  CA  SER B 447    10414  13429   7544  -1363   2059  -1330       C  
ATOM   7323  C   SER B 447      -1.489  -8.227  25.988  1.00 86.86           C  
ANISOU 7323  C   SER B 447    10789  13957   8256  -1106   2050  -1419       C  
ATOM   7324  O   SER B 447      -0.388  -8.777  25.978  1.00 88.27           O  
ANISOU 7324  O   SER B 447    10777  14358   8403   -989   2184  -1524       O  
ATOM   7325  CB  SER B 447      -1.726  -5.795  25.429  1.00 86.98           C  
ANISOU 7325  CB  SER B 447    10945  13979   8123  -1590   2016  -1180       C  
ATOM   7326  OG  SER B 447      -0.376  -5.528  25.770  1.00 99.70           O  
ANISOU 7326  OG  SER B 447    12307  15856   9720  -1648   2147  -1218       O  
ATOM   7327  N   PHE B 448      -2.446  -8.485  26.907  1.00 81.41           N  
ANISOU 7327  N   PHE B 448    10178  13016   7740  -1006   1898  -1375       N  
ATOM   7328  CA  PHE B 448      -2.320  -9.428  28.020  1.00 80.55           C  
ANISOU 7328  CA  PHE B 448     9966  12843   7798   -759   1871  -1432       C  
ATOM   7329  C   PHE B 448      -2.148 -10.863  27.526  1.00 86.10           C  
ANISOU 7329  C   PHE B 448    10700  13542   8471   -529   1957  -1586       C  
ATOM   7330  O   PHE B 448      -1.492 -11.661  28.188  1.00 86.24           O  
ANISOU 7330  O   PHE B 448    10587  13618   8563   -304   2007  -1657       O  
ATOM   7331  CB  PHE B 448      -3.522  -9.323  28.980  1.00 79.67           C  
ANISOU 7331  CB  PHE B 448     9967  12448   7854   -739   1699  -1341       C  
ATOM   7332  CG  PHE B 448      -3.743  -8.000  29.686  1.00 79.71           C  
ANISOU 7332  CG  PHE B 448     9953  12418   7915   -917   1607  -1199       C  
ATOM   7333  CD1 PHE B 448      -2.674  -7.164  29.991  1.00 83.56           C  
ANISOU 7333  CD1 PHE B 448    10264  13118   8366  -1035   1671  -1171       C  
ATOM   7334  CD2 PHE B 448      -5.011  -7.625  30.111  1.00 79.98           C  
ANISOU 7334  CD2 PHE B 448    10138  12209   8043   -959   1459  -1104       C  
ATOM   7335  CE1 PHE B 448      -2.882  -5.955  30.661  1.00 83.64           C  
ANISOU 7335  CE1 PHE B 448    10283  13070   8426  -1206   1590  -1053       C  
ATOM   7336  CE2 PHE B 448      -5.213  -6.424  30.799  1.00 81.62           C  
ANISOU 7336  CE2 PHE B 448    10344  12368   8301  -1100   1380   -983       C  
ATOM   7337  CZ  PHE B 448      -4.149  -5.598  31.069  1.00 80.59           C  
ANISOU 7337  CZ  PHE B 448    10068  12423   8130  -1224   1446   -960       C  
ATOM   7338  N   LYS B 449      -2.711 -11.180  26.356  1.00 83.88           N  
ANISOU 7338  N   LYS B 449    10601  13198   8072   -577   1974  -1641       N  
ATOM   7339  CA  LYS B 449      -2.561 -12.492  25.746  1.00 85.78           C  
ANISOU 7339  CA  LYS B 449    10906  13425   8260   -384   2066  -1803       C  
ATOM   7340  C   LYS B 449      -1.157 -12.615  25.151  1.00 93.89           C  
ANISOU 7340  C   LYS B 449    11760  14768   9146   -330   2254  -1898       C  
ATOM   7341  O   LYS B 449      -0.578 -13.694  25.170  1.00 94.26           O  
ANISOU 7341  O   LYS B 449    11757  14860   9199    -87   2352  -2028       O  
ATOM   7342  CB  LYS B 449      -3.671 -12.748  24.713  1.00 88.47           C  
ANISOU 7342  CB  LYS B 449    11497  13606   8512   -473   2007  -1841       C  
ATOM   7343  CG  LYS B 449      -5.025 -13.081  25.366  1.00101.40           C  
ANISOU 7343  CG  LYS B 449    13280  14936  10310   -453   1843  -1801       C  
ATOM   7344  CD  LYS B 449      -6.213 -12.917  24.407  1.00108.03           C  
ANISOU 7344  CD  LYS B 449    14326  15665  11054   -608   1745  -1801       C  
ATOM   7345  CE  LYS B 449      -7.550 -13.211  25.055  1.00103.97           C  
ANISOU 7345  CE  LYS B 449    13920  14884  10698   -606   1588  -1767       C  
ATOM   7346  NZ  LYS B 449      -8.656 -13.174  24.059  1.00104.20           N1+
ANISOU 7346  NZ  LYS B 449    14124  14847  10621   -738   1492  -1795       N1+
ATOM   7347  N   HIS B 450      -0.582 -11.496  24.698  1.00 94.43           N  
ANISOU 7347  N   HIS B 450    11731  15056   9093   -550   2312  -1829       N  
ATOM   7348  CA  HIS B 450       0.765 -11.444  24.127  1.00 98.56           C  
ANISOU 7348  CA  HIS B 450    12059  15918   9472   -548   2502  -1908       C  
ATOM   7349  C   HIS B 450       1.870 -11.596  25.205  1.00103.70           C  
ANISOU 7349  C   HIS B 450    12412  16762  10228   -390   2552  -1932       C  
ATOM   7350  O   HIS B 450       2.936 -12.134  24.904  1.00105.97           O  
ANISOU 7350  O   HIS B 450    12526  17302  10437   -243   2706  -2050       O  
ATOM   7351  CB  HIS B 450       0.934 -10.156  23.301  1.00101.02           C  
ANISOU 7351  CB  HIS B 450    12390  16379   9616   -870   2550  -1813       C  
ATOM   7352  CG  HIS B 450       2.236 -10.052  22.570  1.00108.16           C  
ANISOU 7352  CG  HIS B 450    13108  17641  10348   -913   2762  -1892       C  
ATOM   7353  ND1 HIS B 450       3.329  -9.405  23.129  1.00111.28           N  
ANISOU 7353  ND1 HIS B 450    13223  18298  10760  -1000   2840  -1864       N  
ATOM   7354  CD2 HIS B 450       2.575 -10.501  21.338  1.00112.85           C  
ANISOU 7354  CD2 HIS B 450    13755  18377  10745   -892   2910  -2001       C  
ATOM   7355  CE1 HIS B 450       4.294  -9.486  22.226  1.00113.81           C  
ANISOU 7355  CE1 HIS B 450    13422  18920  10901  -1030   3038  -1954       C  
ATOM   7356  NE2 HIS B 450       3.886 -10.132  21.128  1.00115.03           N  
ANISOU 7356  NE2 HIS B 450    13775  19011  10918   -961   3091  -2036       N  
ATOM   7357  N   ILE B 451       1.607 -11.147  26.454  1.00 98.41           N  
ANISOU 7357  N   ILE B 451    11681  15986   9725   -406   2419  -1827       N  
ATOM   7358  CA  ILE B 451       2.548 -11.217  27.591  1.00 97.95           C  
ANISOU 7358  CA  ILE B 451    11345  16105   9765   -264   2429  -1837       C  
ATOM   7359  C   ILE B 451       2.496 -12.597  28.279  1.00101.81           C  
ANISOU 7359  C   ILE B 451    11847  16466  10371    109   2408  -1919       C  
ATOM   7360  O   ILE B 451       3.536 -13.217  28.506  1.00103.01           O  
ANISOU 7360  O   ILE B 451    11793  16839  10508    339   2505  -2012       O  
ATOM   7361  CB  ILE B 451       2.316 -10.060  28.632  1.00 98.34           C  
ANISOU 7361  CB  ILE B 451    11337  16107   9922   -460   2298  -1693       C  
ATOM   7362  CG1 ILE B 451       2.207  -8.669  27.970  1.00 98.02           C  
ANISOU 7362  CG1 ILE B 451    11355  16114   9772   -833   2311  -1595       C  
ATOM   7363  CG2 ILE B 451       3.411 -10.052  29.698  1.00 99.33           C  
ANISOU 7363  CG2 ILE B 451    11150  16479  10111   -343   2314  -1720       C  
ATOM   7364  CD1 ILE B 451       1.279  -7.697  28.682  1.00 97.90           C  
ANISOU 7364  CD1 ILE B 451    11474  15862   9862  -1008   2147  -1446       C  
ATOM   7365  N   LEU B 452       1.280 -13.048  28.618  1.00 97.02           N  
ANISOU 7365  N   LEU B 452    11483  15506   9877    165   2284  -1878       N  
ATOM   7366  CA  LEU B 452       0.992 -14.276  29.364  1.00 96.88           C  
ANISOU 7366  CA  LEU B 452    11543  15284   9985    475   2248  -1923       C  
ATOM   7367  C   LEU B 452       0.857 -15.573  28.550  1.00103.34           C  
ANISOU 7367  C   LEU B 452    12533  15986  10747    678   2342  -2067       C  
ATOM   7368  O   LEU B 452       1.140 -16.651  29.090  1.00104.43           O  
ANISOU 7368  O   LEU B 452    12676  16052  10951    985   2375  -2131       O  
ATOM   7369  CB  LEU B 452      -0.295 -14.087  30.199  1.00 93.88           C  
ANISOU 7369  CB  LEU B 452    11337  14576   9757    406   2076  -1806       C  
ATOM   7370  CG  LEU B 452      -0.348 -12.914  31.161  1.00 96.17           C  
ANISOU 7370  CG  LEU B 452    11508  14907  10123    239   1967  -1668       C  
ATOM   7371  CD1 LEU B 452      -1.771 -12.455  31.359  1.00 93.55           C  
ANISOU 7371  CD1 LEU B 452    11388  14281   9874     74   1824  -1564       C  
ATOM   7372  CD2 LEU B 452       0.300 -13.259  32.481  1.00 98.95           C  
ANISOU 7372  CD2 LEU B 452    11685  15336  10575    464   1942  -1656       C  
ATOM   7373  N   PHE B 453       0.360 -15.481  27.295  1.00100.07           N  
ANISOU 7373  N   PHE B 453    12287  15527  10209    511   2377  -2114       N  
ATOM   7374  CA  PHE B 453       0.061 -16.619  26.407  1.00117.98           C  
ANISOU 7374  CA  PHE B 453    14762  17659  12408    645   2453  -2261       C  
ATOM   7375  C   PHE B 453      -1.091 -17.478  26.973  1.00148.84           C  
ANISOU 7375  C   PHE B 453    18911  21178  16465    743   2348  -2260       C  
ATOM   7376  O   PHE B 453      -1.920 -17.000  27.762  1.00103.05           O  
ANISOU 7376  O   PHE B 453    13152  15210  10793    629   2204  -2133       O  
ATOM   7377  CB  PHE B 453       1.307 -17.472  26.090  1.00122.41           C  
ANISOU 7377  CB  PHE B 453    15192  18435  12883    926   2633  -2411       C  
ATOM   7378  CG  PHE B 453       2.358 -16.787  25.250  1.00125.77           C  
ANISOU 7378  CG  PHE B 453    15408  19247  13130    811   2770  -2447       C  
ATOM   7379  CD1 PHE B 453       3.322 -15.973  25.836  1.00129.12           C  
ANISOU 7379  CD1 PHE B 453    15523  19974  13563    762   2792  -2379       C  
ATOM   7380  CD2 PHE B 453       2.417 -16.995  23.876  1.00129.50           C  
ANISOU 7380  CD2 PHE B 453    15991  19795  13418    750   2887  -2561       C  
ATOM   7381  CE1 PHE B 453       4.310 -15.355  25.058  1.00131.93           C  
ANISOU 7381  CE1 PHE B 453    15677  20698  13752    632   2936  -2417       C  
ATOM   7382  CE2 PHE B 453       3.407 -16.380  23.099  1.00134.03           C  
ANISOU 7382  CE2 PHE B 453    16373  20737  13817    638   3033  -2592       C  
ATOM   7383  CZ  PHE B 453       4.347 -15.565  23.695  1.00132.39           C  
ANISOU 7383  CZ  PHE B 453    15852  20823  13627    573   3062  -2518       C  
TER    7384      PHE B 453                                                      
HETATM 7385  C1  E33 A1201     -30.895 -12.938  60.350  1.00 77.92           C  
HETATM 7386  C2  E33 A1201     -31.600 -14.271  60.491  1.00 80.44           C  
HETATM 7387  C3  E33 A1201     -33.812 -15.108  58.080  1.00 67.63           C  
HETATM 7388  C4  E33 A1201     -34.168 -13.789  57.402  1.00 66.53           C  
HETATM 7389  C5  E33 A1201     -33.621 -13.663  55.990  1.00 66.55           C  
HETATM 7390  C6  E33 A1201     -32.147 -14.041  55.800  1.00 66.74           C  
HETATM 7391  C12 E33 A1201     -32.365 -16.798  51.478  1.00 61.72           C  
HETATM 7392  C13 E33 A1201     -32.106 -15.409  52.059  1.00 62.47           C  
HETATM 7393  C14 E33 A1201     -31.799 -14.189  54.318  1.00 64.81           C  
HETATM 7394  C15 E33 A1201     -31.642 -18.989  51.542  1.00 52.27           C  
HETATM 7395  C16 E33 A1201     -31.198 -20.089  52.274  1.00 50.25           C  
HETATM 7396  C17 E33 A1201     -31.063 -20.000  53.678  1.00 50.55           C  
HETATM 7397  S1  E33 A1201     -31.206 -15.428  59.137  1.00 81.90           S  
HETATM 7398  O1  E33 A1201     -29.779 -15.230  58.623  1.00 81.76           O  
HETATM 7399  O2  E33 A1201     -31.215 -16.860  59.632  1.00 81.47           O  
HETATM 7400  N1  E33 A1201     -32.347 -15.328  57.865  1.00 72.86           N  
HETATM 7401  C7  E33 A1201     -31.867 -15.397  56.459  1.00 68.72           C  
HETATM 7402  C8  E33 A1201     -32.486 -16.489  55.628  1.00 68.01           C  
HETATM 7403  C9  E33 A1201     -32.388 -16.630  54.094  1.00 64.96           C  
HETATM 7404  C10 E33 A1201     -31.625 -17.683  53.644  1.00 58.94           C  
HETATM 7405  C11 E33 A1201     -31.907 -17.832  52.274  1.00 57.33           C  
HETATM 7406  N2  E33 A1201     -32.403 -15.247  53.495  1.00 63.60           N1+
HETATM 7407  C18 E33 A1201     -31.375 -18.840  54.389  1.00 52.06           C  
HETATM 7408  O3  E33 A1201     -30.874 -21.248  51.622  1.00 47.26           O  
HETATM 7409  C19 E33 A1201     -31.874 -22.243  51.767  1.00 45.03           C  
HETATM 7410  C1  CLR A1202     -26.940  -1.340  57.323  1.00 66.80           C  
HETATM 7411  C2  CLR A1202     -26.499  -1.885  58.688  1.00 67.99           C  
HETATM 7412  C3  CLR A1202     -27.667  -2.443  59.480  1.00 66.80           C  
HETATM 7413  C4  CLR A1202     -28.414  -3.493  58.665  1.00 66.55           C  
HETATM 7414  C5  CLR A1202     -28.786  -3.012  57.275  1.00 66.40           C  
HETATM 7415  C6  CLR A1202     -30.028  -3.168  56.811  1.00 66.19           C  
HETATM 7416  C7  CLR A1202     -30.497  -2.745  55.448  1.00 68.06           C  
HETATM 7417  C8  CLR A1202     -29.344  -2.486  54.474  1.00 66.02           C  
HETATM 7418  C9  CLR A1202     -28.237  -1.674  55.184  1.00 67.29           C  
HETATM 7419  C10 CLR A1202     -27.660  -2.391  56.447  1.00 67.46           C  
HETATM 7420  C11 CLR A1202     -27.134  -1.208  54.210  1.00 67.69           C  
HETATM 7421  C12 CLR A1202     -27.638  -0.602  52.894  1.00 69.04           C  
HETATM 7422  C13 CLR A1202     -28.693  -1.472  52.171  1.00 69.19           C  
HETATM 7423  C14 CLR A1202     -29.812  -1.716  53.219  1.00 66.59           C  
HETATM 7424  C15 CLR A1202     -30.993  -2.239  52.379  1.00 68.60           C  
HETATM 7425  C16 CLR A1202     -30.830  -1.576  50.991  1.00 69.22           C  
HETATM 7426  C17 CLR A1202     -29.516  -0.765  51.054  1.00 69.46           C  
HETATM 7427  C18 CLR A1202     -28.048  -2.785  51.652  1.00 69.11           C  
HETATM 7428  C19 CLR A1202     -26.679  -3.519  56.059  1.00 68.76           C  
HETATM 7429  C20 CLR A1202     -28.884  -0.529  49.658  1.00 69.01           C  
HETATM 7430  C21 CLR A1202     -27.733   0.479  49.683  1.00 67.54           C  
HETATM 7431  C22 CLR A1202     -29.926  -0.117  48.594  1.00 69.46           C  
HETATM 7432  C23 CLR A1202     -29.444  -0.269  47.150  1.00 69.86           C  
HETATM 7433  C24 CLR A1202     -30.470   0.007  46.042  1.00 70.85           C  
HETATM 7434  C25 CLR A1202     -30.429  -0.927  44.778  1.00 70.25           C  
HETATM 7435  C26 CLR A1202     -31.547  -0.651  43.801  1.00 69.30           C  
HETATM 7436  C27 CLR A1202     -29.096  -0.972  44.037  1.00 69.42           C  
HETATM 7437  O1  CLR A1202     -27.141  -3.040  60.673  1.00 65.43           O  
HETATM 7438  C18 OLC A1203     -21.006  -2.871  32.646  1.00 71.79           C  
HETATM 7439  C10 OLC A1203     -22.387  -3.577  25.805  1.00 82.15           C  
HETATM 7440  C9  OLC A1203     -22.006  -4.841  25.536  1.00 82.83           C  
HETATM 7441  C17 OLC A1203     -21.546  -1.665  31.913  1.00 73.42           C  
HETATM 7442  C11 OLC A1203     -23.826  -3.089  25.881  1.00 81.77           C  
HETATM 7443  C8  OLC A1203     -22.930  -6.022  25.270  1.00 82.27           C  
HETATM 7444  C16 OLC A1203     -21.496  -1.861  30.397  1.00 75.22           C  
HETATM 7445  C12 OLC A1203     -23.879  -1.584  26.142  1.00 81.14           C  
HETATM 7446  C15 OLC A1203     -22.879  -1.639  29.790  1.00 77.35           C  
HETATM 7447  C13 OLC A1203     -24.113  -1.238  27.612  1.00 81.79           C  
HETATM 7448  C14 OLC A1203     -22.807  -1.034  28.391  1.00 80.21           C  
HETATM 7449  C10 OLC A1204     -33.234 -32.852  36.410  1.00 71.74           C  
HETATM 7450  C9  OLC A1204     -33.416 -32.916  35.080  1.00 71.26           C  
HETATM 7451  C11 OLC A1204     -34.252 -33.266  37.459  1.00 71.38           C  
HETATM 7452  C8  OLC A1204     -34.661 -33.424  34.375  1.00 71.02           C  
HETATM 7453  C24 OLC A1204     -33.784 -33.278  21.744  1.00 99.08           C  
HETATM 7454  C12 OLC A1204     -34.186 -32.331  38.663  1.00 70.82           C  
HETATM 7455  C7  OLC A1204     -35.202 -32.396  33.378  1.00 72.34           C  
HETATM 7456  C15 OLC A1204     -33.930 -32.847  42.504  1.00 70.96           C  
HETATM 7457  C13 OLC A1204     -33.868 -33.063  39.968  1.00 70.49           C  
HETATM 7458  C6  OLC A1204     -34.561 -32.500  31.996  1.00 73.60           C  
HETATM 7459  C14 OLC A1204     -34.079 -32.131  41.160  1.00 70.66           C  
HETATM 7460  C5  OLC A1204     -35.565 -32.852  30.904  1.00 75.76           C  
HETATM 7461  C4  OLC A1204     -34.968 -33.866  29.921  1.00 79.05           C  
HETATM 7462  C3  OLC A1204     -35.495 -33.701  28.495  1.00 82.97           C  
HETATM 7463  C2  OLC A1204     -34.432 -33.082  27.580  1.00 86.94           C  
HETATM 7464  C21 OLC A1204     -33.888 -32.979  24.261  1.00 97.19           C  
HETATM 7465  C1  OLC A1204     -34.974 -32.340  26.361  1.00 90.59           C  
HETATM 7466  C22 OLC A1204     -33.812 -32.276  22.902  1.00 98.31           C  
HETATM 7467  O19 OLC A1204     -36.144 -31.981  26.264  1.00 89.45           O  
HETATM 7468  O25 OLC A1204     -35.065 -33.872  21.491  1.00 98.93           O  
HETATM 7469  O23 OLC A1204     -34.877 -31.334  22.734  1.00 97.75           O  
HETATM 7470  O20 OLC A1204     -34.119 -32.041  25.322  1.00 94.54           O  
HETATM 7471  C18 OLC A1205     -30.587 -30.895  45.736  1.00 63.53           C  
HETATM 7472  C10 OLC A1205     -32.683 -27.917  37.029  1.00 62.57           C  
HETATM 7473  C9  OLC A1205     -33.618 -28.106  36.079  1.00 64.17           C  
HETATM 7474  C17 OLC A1205     -30.054 -31.004  44.319  1.00 63.71           C  
HETATM 7475  C11 OLC A1205     -32.909 -27.873  38.523  1.00 59.58           C  
HETATM 7476  C8  OLC A1205     -35.113 -28.322  36.274  1.00 63.11           C  
HETATM 7477  C16 OLC A1205     -29.929 -29.645  43.636  1.00 64.50           C  
HETATM 7478  C12 OLC A1205     -31.576 -27.930  39.259  1.00 58.41           C  
HETATM 7479  C7  OLC A1205     -35.915 -27.708  35.121  1.00 62.42           C  
HETATM 7480  C15 OLC A1205     -30.888 -29.514  42.451  1.00 65.00           C  
HETATM 7481  C13 OLC A1205     -31.823 -27.873  40.766  1.00 61.26           C  
HETATM 7482  C6  OLC A1205     -35.833 -28.483  33.801  1.00 60.24           C  
HETATM 7483  C14 OLC A1205     -30.607 -28.275  41.603  1.00 63.22           C  
HETATM 7484  C24 OLC A1206     -46.774 -18.125  33.198  1.00 76.90           C  
HETATM 7485  C6  OLC A1206     -54.896 -18.607  31.568  1.00 87.67           C  
HETATM 7486  C5  OLC A1206     -53.389 -18.763  31.433  1.00 88.25           C  
HETATM 7487  C4  OLC A1206     -52.976 -18.601  29.972  1.00 89.53           C  
HETATM 7488  C3  OLC A1206     -52.227 -17.294  29.727  1.00 90.57           C  
HETATM 7489  C2  OLC A1206     -50.855 -17.575  29.124  1.00 91.90           C  
HETATM 7490  C21 OLC A1206     -48.557 -17.574  31.525  1.00 86.45           C  
HETATM 7491  C1  OLC A1206     -49.792 -16.606  29.620  1.00 92.54           C  
HETATM 7492  C22 OLC A1206     -47.960 -17.206  32.883  1.00 81.35           C  
HETATM 7493  O19 OLC A1206     -49.269 -15.864  28.799  1.00 92.69           O  
HETATM 7494  O25 OLC A1206     -46.328 -17.934  34.549  1.00 73.34           O  
HETATM 7495  O23 OLC A1206     -47.544 -15.837  32.889  1.00 80.56           O  
HETATM 7496  O20 OLC A1206     -49.382 -16.543  30.951  1.00 90.45           O  
HETATM 7497  C10 OLC A1207     -23.688   2.262  52.656  1.00 72.91           C  
HETATM 7498  C9  OLC A1207     -24.005   2.728  53.879  1.00 74.71           C  
HETATM 7499  C11 OLC A1207     -24.649   1.877  51.546  1.00 69.99           C  
HETATM 7500  C8  OLC A1207     -25.408   2.986  54.399  1.00 76.61           C  
HETATM 7501  C24 OLC A1207     -26.617  -1.843  65.718  1.00 99.56           C  
HETATM 7502  C7  OLC A1207     -25.654   2.405  55.791  1.00 78.84           C  
HETATM 7503  C6  OLC A1207     -26.006   3.478  56.830  1.00 80.91           C  
HETATM 7504  C5  OLC A1207     -26.786   2.936  58.037  1.00 82.35           C  
HETATM 7505  C4  OLC A1207     -26.679   3.841  59.273  1.00 83.70           C  
HETATM 7506  C3  OLC A1207     -27.305   3.211  60.527  1.00 84.31           C  
HETATM 7507  C2  OLC A1207     -26.303   2.474  61.417  1.00 84.97           C  
HETATM 7508  C21 OLC A1207     -27.030   0.373  64.480  1.00 95.17           C  
HETATM 7509  C1  OLC A1207     -26.856   2.220  62.804  1.00 88.76           C  
HETATM 7510  C22 OLC A1207     -26.540  -1.078  64.398  1.00 99.41           C  
HETATM 7511  O19 OLC A1207     -27.005   3.143  63.606  1.00 90.85           O  
HETATM 7512  O25 OLC A1207     -26.380  -3.250  65.502  1.00 98.36           O  
HETATM 7513  O23 OLC A1207     -27.232  -1.822  63.385  1.00102.50           O  
HETATM 7514  O20 OLC A1207     -27.195   0.932  63.161  1.00 91.37           O  
HETATM 7515  C1  OLA A1208     -29.515   8.395  58.898  1.00 61.10           C  
HETATM 7516  O1  OLA A1208     -28.300   8.580  58.682  1.00 65.37           O  
HETATM 7517  O2  OLA A1208     -30.003   8.846  59.959  1.00 61.16           O  
HETATM 7518  C2  OLA A1208     -30.361   7.649  57.897  1.00 56.73           C  
HETATM 7519  C3  OLA A1208     -29.711   6.328  57.517  1.00 57.81           C  
HETATM 7520  C4  OLA A1208     -29.010   6.500  56.177  1.00 61.61           C  
HETATM 7521  C5  OLA A1208     -28.432   5.217  55.605  1.00 64.43           C  
HETATM 7522  C6  OLA A1208     -29.366   4.579  54.586  1.00 68.02           C  
HETATM 7523  C7  OLA A1208     -28.596   3.881  53.465  1.00 70.47           C  
HETATM 7524  C8  OLA A1208     -28.283   4.854  52.327  1.00 70.62           C  
HETATM 7525  C9  OLA A1208     -27.445   4.206  51.246  1.00 70.49           C  
HETATM 7526  C10 OLA A1208     -27.437   4.617  49.968  1.00 72.71           C  
HETATM 7527  C11 OLA A1208     -28.277   5.749  49.401  1.00 76.09           C  
HETATM 7528  C12 OLA A1208     -27.607   7.114  49.582  1.00 78.72           C  
HETATM 7529  C13 OLA A1208     -27.739   8.019  48.351  1.00 80.96           C  
HETATM 7530  C14 OLA A1208     -28.099   9.478  48.677  1.00 82.69           C  
HETATM 7531  C15 OLA A1208     -27.017  10.227  49.462  1.00 84.42           C  
HETATM 7532  C16 OLA A1208     -25.946  10.891  48.596  1.00 85.73           C  
HETATM 7533  C17 OLA A1208     -24.626  11.008  49.363  1.00 85.91           C  
HETATM 7534  C18 OLA A1208     -24.166  12.459  49.520  1.00 85.39           C  
HETATM 7535  C1  OLA A1209     -14.525 -14.181  62.163  1.00 84.07           C  
HETATM 7536  O1  OLA A1209     -14.776 -12.950  62.139  1.00 85.02           O  
HETATM 7537  O2  OLA A1209     -14.125 -14.696  63.238  1.00 86.67           O  
HETATM 7538  C2  OLA A1209     -14.721 -15.058  60.947  1.00 80.65           C  
HETATM 7539  C3  OLA A1209     -14.343 -14.361  59.644  1.00 81.73           C  
HETATM 7540  C4  OLA A1209     -13.885 -15.356  58.573  1.00 84.09           C  
HETATM 7541  C5  OLA A1209     -14.936 -15.584  57.490  1.00 87.65           C  
HETATM 7542  C6  OLA A1209     -14.804 -14.590  56.329  1.00 92.56           C  
HETATM 7543  C7  OLA A1209     -15.703 -14.936  55.136  1.00 94.07           C  
HETATM 7544  C8  OLA A1209     -16.078 -13.695  54.318  1.00 93.31           C  
HETATM 7545  C9  OLA A1209     -17.283 -14.010  53.445  1.00 90.63           C  
HETATM 7546  C10 OLA A1209     -17.529 -13.491  52.234  1.00 86.81           C  
HETATM 7547  C11 OLA A1209     -16.629 -12.495  51.543  1.00 83.39           C  
HETATM 7548  C12 OLA A1209     -17.110 -12.332  50.113  1.00 82.08           C  
HETATM 7549  C13 OLA A1209     -17.500 -10.880  49.858  1.00 83.64           C  
HETATM 7550  C14 OLA A1209     -17.210 -10.427  48.427  1.00 83.79           C  
HETATM 7551  C15 OLA A1209     -16.967  -8.918  48.336  1.00 81.54           C  
HETATM 7552  C16 OLA A1209     -15.689  -8.622  47.560  1.00 79.23           C  
HETATM 7553  C17 OLA A1209     -15.507  -7.126  47.369  1.00 78.98           C  
HETATM 7554  C18 OLA A1209     -15.498  -6.763  45.886  1.00 79.27           C  
HETATM 7555  C1  E33 B1201     -11.285   2.126  61.110  1.00 74.94           C  
HETATM 7556  C2  E33 B1201      -9.984   2.896  61.021  1.00 74.95           C  
HETATM 7557  C3  E33 B1201      -7.580   3.814  58.837  1.00 64.51           C  
HETATM 7558  C4  E33 B1201      -7.259   2.550  58.037  1.00 64.50           C  
HETATM 7559  C5  E33 B1201      -7.733   2.607  56.593  1.00 62.64           C  
HETATM 7560  C6  E33 B1201      -9.197   3.017  56.421  1.00 63.44           C  
HETATM 7561  C12 E33 B1201      -8.892   5.928  52.229  1.00 64.62           C  
HETATM 7562  C13 E33 B1201      -9.192   4.520  52.725  1.00 63.00           C  
HETATM 7563  C14 E33 B1201      -9.538   3.215  54.943  1.00 62.94           C  
HETATM 7564  C15 E33 B1201      -9.608   8.123  52.401  1.00 64.54           C  
HETATM 7565  C16 E33 B1201     -10.070   9.204  53.170  1.00 62.81           C  
HETATM 7566  C17 E33 B1201     -10.249   9.051  54.571  1.00 63.57           C  
HETATM 7567  S1  E33 B1201     -10.097   4.347  59.929  1.00 75.28           S  
HETATM 7568  O1  E33 B1201     -11.526   4.635  59.501  1.00 74.60           O  
HETATM 7569  O2  E33 B1201      -9.789   5.640  60.662  1.00 74.96           O  
HETATM 7570  N1  E33 B1201      -9.008   4.192  58.603  1.00 68.57           N  
HETATM 7571  C7  E33 B1201      -9.473   4.333  57.177  1.00 65.50           C  
HETATM 7572  C8  E33 B1201      -8.843   5.439  56.377  1.00 67.14           C  
HETATM 7573  C9  E33 B1201      -8.925   5.643  54.836  1.00 68.08           C  
HETATM 7574  C10 E33 B1201      -9.683   6.717  54.426  1.00 66.46           C  
HETATM 7575  C11 E33 B1201      -9.373   6.918  53.068  1.00 65.02           C  
HETATM 7576  N2  E33 B1201      -8.921   4.292  54.158  1.00 64.42           N1+
HETATM 7577  C18 E33 B1201      -9.955   7.845  55.223  1.00 64.03           C  
HETATM 7578  O3  E33 B1201     -10.386  10.387  52.539  1.00 58.50           O  
HETATM 7579  C19 E33 B1201      -9.389  11.395  52.658  1.00 56.67           C  
HETATM 7580  C1  CLR B1202     -14.467 -10.033  57.434  1.00 95.58           C  
HETATM 7581  C2  CLR B1202     -15.014  -9.543  58.783  1.00 96.82           C  
HETATM 7582  C3  CLR B1202     -13.971  -8.778  59.584  1.00 97.32           C  
HETATM 7583  C4  CLR B1202     -13.373  -7.645  58.753  1.00 96.45           C  
HETATM 7584  C5  CLR B1202     -12.901  -8.104  57.386  1.00 95.90           C  
HETATM 7585  C6  CLR B1202     -11.671  -7.808  56.954  1.00 94.17           C  
HETATM 7586  C7  CLR B1202     -11.115  -8.210  55.619  1.00 92.90           C  
HETATM 7587  C8  CLR B1202     -12.224  -8.547  54.624  1.00 92.25           C  
HETATM 7588  C9  CLR B1202     -13.242  -9.508  55.283  1.00 94.22           C  
HETATM 7589  C10 CLR B1202     -13.914  -8.891  56.553  1.00 96.10           C  
HETATM 7590  C11 CLR B1202     -14.279 -10.056  54.270  1.00 92.89           C  
HETATM 7591  C12 CLR B1202     -13.740 -10.450  52.885  1.00 90.56           C  
HETATM 7592  C13 CLR B1202     -12.798  -9.399  52.254  1.00 87.99           C  
HETATM 7593  C14 CLR B1202     -11.692  -9.174  53.318  1.00 88.67           C  
HETATM 7594  C15 CLR B1202     -10.551  -8.492  52.539  1.00 86.59           C  
HETATM 7595  C16 CLR B1202     -10.738  -8.886  51.065  1.00 85.16           C  
HETATM 7596  C17 CLR B1202     -11.932  -9.861  51.052  1.00 86.40           C  
HETATM 7597  C18 CLR B1202     -13.584  -8.110  51.915  1.00 86.97           C  
HETATM 7598  C19 CLR B1202     -15.053  -7.925  56.172  1.00 98.05           C  
HETATM 7599  C20 CLR B1202     -12.564 -10.009  49.645  1.00 86.76           C  
HETATM 7600  C21 CLR B1202     -13.662 -11.071  49.582  1.00 85.96           C  
HETATM 7601  C22 CLR B1202     -11.502 -10.289  48.561  1.00 87.87           C  
HETATM 7602  C23 CLR B1202     -12.004 -10.209  47.124  1.00 90.02           C  
HETATM 7603  C24 CLR B1202     -11.328 -11.178  46.156  1.00 92.24           C  
HETATM 7604  C25 CLR B1202     -10.595 -10.568  44.946  1.00 94.72           C  
HETATM 7605  C26 CLR B1202      -9.845 -11.624  44.145  1.00 96.60           C  
HETATM 7606  C27 CLR B1202     -11.486  -9.731  44.026  1.00 93.66           C  
HETATM 7607  O1  CLR B1202     -14.613  -8.234  60.746  1.00 96.99           O  
HETATM 7608  C18 OLC B1203     -21.043  -0.342  36.661  1.00 65.15           C  
HETATM 7609  C10 OLC B1203     -21.820   3.582  28.479  1.00 87.32           C  
HETATM 7610  C9  OLC B1203     -22.952   3.900  27.827  1.00 90.63           C  
HETATM 7611  C17 OLC B1203     -21.125   1.147  36.395  1.00 63.98           C  
HETATM 7612  C11 OLC B1203     -21.316   4.210  29.764  1.00 83.17           C  
HETATM 7613  C8  OLC B1203     -23.960   4.958  28.247  1.00 92.17           C  
HETATM 7614  C16 OLC B1203     -20.373   1.521  35.120  1.00 63.75           C  
HETATM 7615  C12 OLC B1203     -20.622   3.175  30.649  1.00 78.25           C  
HETATM 7616  C7  OLC B1203     -24.896   5.291  27.084  1.00 92.88           C  
HETATM 7617  C15 OLC B1203     -20.913   2.805  34.505  1.00 65.46           C  
HETATM 7618  C13 OLC B1203     -21.274   3.153  32.031  1.00 74.48           C  
HETATM 7619  C14 OLC B1203     -20.249   3.072  33.160  1.00 70.42           C  
HETATM 7620  C18 OLC B1204     -21.200   9.985  39.902  1.00 79.54           C  
HETATM 7621  C17 OLC B1204     -19.939   9.911  39.068  1.00 80.42           C  
HETATM 7622  C11 OLC B1204     -20.268   7.685  33.062  1.00 83.45           C  
HETATM 7623  C16 OLC B1204     -20.105   8.897  37.943  1.00 81.35           C  
HETATM 7624  C12 OLC B1204     -19.891   7.244  34.479  1.00 83.27           C  
HETATM 7625  C15 OLC B1204     -18.760   8.447  37.377  1.00 82.34           C  
HETATM 7626  C13 OLC B1204     -18.514   7.739  34.936  1.00 82.13           C  
HETATM 7627  C14 OLC B1204     -18.603   8.900  35.926  1.00 82.00           C  
HETATM 7628  O   HOH A1301     -35.412 -12.078  60.078  1.00 52.14           O  
HETATM 7629  O   HOH B1301      -5.786   3.024  50.455  1.00 65.71           O  
CONECT  625 1185                                                                
CONECT 1185  625                                                                
CONECT 3303 3330                                                                
CONECT 3330 3303                                                                
CONECT 4326 4887                                                                
CONECT 4887 4326                                                                
CONECT 6997 7028                                                                
CONECT 7028 6997                                                                
CONECT 7385 7386                                                                
CONECT 7386 7385 7397                                                           
CONECT 7387 7388 7400                                                           
CONECT 7388 7387 7389                                                           
CONECT 7389 7388 7390                                                           
CONECT 7390 7389 7393 7401                                                      
CONECT 7391 7392 7405                                                           
CONECT 7392 7391 7406                                                           
CONECT 7393 7390 7406                                                           
CONECT 7394 7395 7405                                                           
CONECT 7395 7394 7396 7408                                                      
CONECT 7396 7395 7407                                                           
CONECT 7397 7386 7398 7399 7400                                                 
CONECT 7398 7397                                                                
CONECT 7399 7397                                                                
CONECT 7400 7387 7397 7401                                                      
CONECT 7401 7390 7400 7402                                                      
CONECT 7402 7401 7403                                                           
CONECT 7403 7402 7404 7406                                                      
CONECT 7404 7403 7405 7407                                                      
CONECT 7405 7391 7394 7404                                                      
CONECT 7406 7392 7393 7403                                                      
CONECT 7407 7396 7404                                                           
CONECT 7408 7395 7409                                                           
CONECT 7409 7408                                                                
CONECT 7410 7411 7419                                                           
CONECT 7411 7410 7412                                                           
CONECT 7412 7411 7413 7437                                                      
CONECT 7413 7412 7414                                                           
CONECT 7414 7413 7415 7419                                                      
CONECT 7415 7414 7416                                                           
CONECT 7416 7415 7417                                                           
CONECT 7417 7416 7418 7423                                                      
CONECT 7418 7417 7419 7420                                                      
CONECT 7419 7410 7414 7418 7428                                                 
CONECT 7420 7418 7421                                                           
CONECT 7421 7420 7422                                                           
CONECT 7422 7421 7423 7426 7427                                                 
CONECT 7423 7417 7422 7424                                                      
CONECT 7424 7423 7425                                                           
CONECT 7425 7424 7426                                                           
CONECT 7426 7422 7425 7429                                                      
CONECT 7427 7422                                                                
CONECT 7428 7419                                                                
CONECT 7429 7426 7430 7431                                                      
CONECT 7430 7429                                                                
CONECT 7431 7429 7432                                                           
CONECT 7432 7431 7433                                                           
CONECT 7433 7432 7434                                                           
CONECT 7434 7433 7435 7436                                                      
CONECT 7435 7434                                                                
CONECT 7436 7434                                                                
CONECT 7437 7412                                                                
CONECT 7438 7441                                                                
CONECT 7439 7440 7442                                                           
CONECT 7440 7439 7443                                                           
CONECT 7441 7438 7444                                                           
CONECT 7442 7439 7445                                                           
CONECT 7443 7440                                                                
CONECT 7444 7441 7446                                                           
CONECT 7445 7442 7447                                                           
CONECT 7446 7444 7448                                                           
CONECT 7447 7445 7448                                                           
CONECT 7448 7446 7447                                                           
CONECT 7449 7450 7451                                                           
CONECT 7450 7449 7452                                                           
CONECT 7451 7449 7454                                                           
CONECT 7452 7450 7455                                                           
CONECT 7453 7466 7468                                                           
CONECT 7454 7451 7457                                                           
CONECT 7455 7452 7458                                                           
CONECT 7456 7459                                                                
CONECT 7457 7454 7459                                                           
CONECT 7458 7455 7460                                                           
CONECT 7459 7456 7457                                                           
CONECT 7460 7458 7461                                                           
CONECT 7461 7460 7462                                                           
CONECT 7462 7461 7463                                                           
CONECT 7463 7462 7465                                                           
CONECT 7464 7466 7470                                                           
CONECT 7465 7463 7467 7470                                                      
CONECT 7466 7453 7464 7469                                                      
CONECT 7467 7465                                                                
CONECT 7468 7453                                                                
CONECT 7469 7466                                                                
CONECT 7470 7464 7465                                                           
CONECT 7471 7474                                                                
CONECT 7472 7473 7475                                                           
CONECT 7473 7472 7476                                                           
CONECT 7474 7471 7477                                                           
CONECT 7475 7472 7478                                                           
CONECT 7476 7473 7479                                                           
CONECT 7477 7474 7480                                                           
CONECT 7478 7475 7481                                                           
CONECT 7479 7476 7482                                                           
CONECT 7480 7477 7483                                                           
CONECT 7481 7478 7483                                                           
CONECT 7482 7479                                                                
CONECT 7483 7480 7481                                                           
CONECT 7484 7492 7494                                                           
CONECT 7485 7486                                                                
CONECT 7486 7485 7487                                                           
CONECT 7487 7486 7488                                                           
CONECT 7488 7487 7489                                                           
CONECT 7489 7488 7491                                                           
CONECT 7490 7492 7496                                                           
CONECT 7491 7489 7493 7496                                                      
CONECT 7492 7484 7490 7495                                                      
CONECT 7493 7491                                                                
CONECT 7494 7484                                                                
CONECT 7495 7492                                                                
CONECT 7496 7490 7491                                                           
CONECT 7497 7498 7499                                                           
CONECT 7498 7497 7500                                                           
CONECT 7499 7497                                                                
CONECT 7500 7498 7502                                                           
CONECT 7501 7510 7512                                                           
CONECT 7502 7500 7503                                                           
CONECT 7503 7502 7504                                                           
CONECT 7504 7503 7505                                                           
CONECT 7505 7504 7506                                                           
CONECT 7506 7505 7507                                                           
CONECT 7507 7506 7509                                                           
CONECT 7508 7510 7514                                                           
CONECT 7509 7507 7511 7514                                                      
CONECT 7510 7501 7508 7513                                                      
CONECT 7511 7509                                                                
CONECT 7512 7501                                                                
CONECT 7513 7510                                                                
CONECT 7514 7508 7509                                                           
CONECT 7515 7516 7517 7518                                                      
CONECT 7516 7515                                                                
CONECT 7517 7515                                                                
CONECT 7518 7515 7519                                                           
CONECT 7519 7518 7520                                                           
CONECT 7520 7519 7521                                                           
CONECT 7521 7520 7522                                                           
CONECT 7522 7521 7523                                                           
CONECT 7523 7522 7524                                                           
CONECT 7524 7523 7525                                                           
CONECT 7525 7524 7526                                                           
CONECT 7526 7525 7527                                                           
CONECT 7527 7526 7528                                                           
CONECT 7528 7527 7529                                                           
CONECT 7529 7528 7530                                                           
CONECT 7530 7529 7531                                                           
CONECT 7531 7530 7532                                                           
CONECT 7532 7531 7533                                                           
CONECT 7533 7532 7534                                                           
CONECT 7534 7533                                                                
CONECT 7535 7536 7537 7538                                                      
CONECT 7536 7535                                                                
CONECT 7537 7535                                                                
CONECT 7538 7535 7539                                                           
CONECT 7539 7538 7540                                                           
CONECT 7540 7539 7541                                                           
CONECT 7541 7540 7542                                                           
CONECT 7542 7541 7543                                                           
CONECT 7543 7542 7544                                                           
CONECT 7544 7543 7545                                                           
CONECT 7545 7544 7546                                                           
CONECT 7546 7545 7547                                                           
CONECT 7547 7546 7548                                                           
CONECT 7548 7547 7549                                                           
CONECT 7549 7548 7550                                                           
CONECT 7550 7549 7551                                                           
CONECT 7551 7550 7552                                                           
CONECT 7552 7551 7553                                                           
CONECT 7553 7552 7554                                                           
CONECT 7554 7553                                                                
CONECT 7555 7556                                                                
CONECT 7556 7555 7567                                                           
CONECT 7557 7558 7570                                                           
CONECT 7558 7557 7559                                                           
CONECT 7559 7558 7560                                                           
CONECT 7560 7559 7563 7571                                                      
CONECT 7561 7562 7575                                                           
CONECT 7562 7561 7576                                                           
CONECT 7563 7560 7576                                                           
CONECT 7564 7565 7575                                                           
CONECT 7565 7564 7566 7578                                                      
CONECT 7566 7565 7577                                                           
CONECT 7567 7556 7568 7569 7570                                                 
CONECT 7568 7567                                                                
CONECT 7569 7567                                                                
CONECT 7570 7557 7567 7571                                                      
CONECT 7571 7560 7570 7572                                                      
CONECT 7572 7571 7573                                                           
CONECT 7573 7572 7574 7576                                                      
CONECT 7574 7573 7575 7577                                                      
CONECT 7575 7561 7564 7574                                                      
CONECT 7576 7562 7563 7573                                                      
CONECT 7577 7566 7574                                                           
CONECT 7578 7565 7579                                                           
CONECT 7579 7578                                                                
CONECT 7580 7581 7589                                                           
CONECT 7581 7580 7582                                                           
CONECT 7582 7581 7583 7607                                                      
CONECT 7583 7582 7584                                                           
CONECT 7584 7583 7585 7589                                                      
CONECT 7585 7584 7586                                                           
CONECT 7586 7585 7587                                                           
CONECT 7587 7586 7588 7593                                                      
CONECT 7588 7587 7589 7590                                                      
CONECT 7589 7580 7584 7588 7598                                                 
CONECT 7590 7588 7591                                                           
CONECT 7591 7590 7592                                                           
CONECT 7592 7591 7593 7596 7597                                                 
CONECT 7593 7587 7592 7594                                                      
CONECT 7594 7593 7595                                                           
CONECT 7595 7594 7596                                                           
CONECT 7596 7592 7595 7599                                                      
CONECT 7597 7592                                                                
CONECT 7598 7589                                                                
CONECT 7599 7596 7600 7601                                                      
CONECT 7600 7599                                                                
CONECT 7601 7599 7602                                                           
CONECT 7602 7601 7603                                                           
CONECT 7603 7602 7604                                                           
CONECT 7604 7603 7605 7606                                                      
CONECT 7605 7604                                                                
CONECT 7606 7604                                                                
CONECT 7607 7582                                                                
CONECT 7608 7611                                                                
CONECT 7609 7610 7612                                                           
CONECT 7610 7609 7613                                                           
CONECT 7611 7608 7614                                                           
CONECT 7612 7609 7615                                                           
CONECT 7613 7610 7616                                                           
CONECT 7614 7611 7617                                                           
CONECT 7615 7612 7618                                                           
CONECT 7616 7613                                                                
CONECT 7617 7614 7619                                                           
CONECT 7618 7615 7619                                                           
CONECT 7619 7617 7618                                                           
CONECT 7620 7621                                                                
CONECT 7621 7620 7623                                                           
CONECT 7622 7624                                                                
CONECT 7623 7621 7625                                                           
CONECT 7624 7622 7626                                                           
CONECT 7625 7623 7627                                                           
CONECT 7626 7624 7627                                                           
CONECT 7627 7625 7626                                                           
MASTER      475    0   13   44   12    0   24    6 7615    2  251   78          
END