HEADER    SIGNALING PROTEIN                       19-JUL-18   6E59              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN NK1 TACHYKININ RECEPTOR                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUBSTANCE-P RECEPTOR, GLGA GLYCOGEN SYNTHASE, SUBSTANCE-P  
COMPND   3 RECEPTOR CHIMERA;                                                    
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: RECEPTOR (UNP RESIDUES 1-227, 238-346) WITH INTERVENING    
COMPND   6 GLYCOGEN SYNTHASE (UNP RESIDUES 218-413);                            
COMPND   7 SYNONYM: SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1,GLYCOGEN      
COMPND   8 SYNTHASE;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 /   
SOURCE   3 ORSAY);                                                              
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   6 STRAIN: GE5 / ORSAY;                                                 
SOURCE   7 GENE: TACR1, NK1R, TAC1R, PAB2292;                                   
SOURCE   8 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 2 RZ-2014;             
SOURCE   9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 1491790                                     
KEYWDS    G PROTEIN-COUPLED RECEPTOR FUSION PROTEIN, SIGNALING PROTEIN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YIN,L.CLARK,K.CHAPMAN,Z.SHAO,D.BOREK,Q.XU,J.WANG,D.M.ROSENBAUM      
REVDAT   4   18-DEC-19 6E59    1       REMARK                                   
REVDAT   3   09-JAN-19 6E59    1       JRNL                                     
REVDAT   2   26-DEC-18 6E59    1       JRNL                                     
REVDAT   1   12-DEC-18 6E59    0                                                
JRNL        AUTH   J.YIN,K.CHAPMAN,L.D.CLARK,Z.SHAO,D.BOREK,Q.XU,J.WANG,        
JRNL        AUTH 2 D.M.ROSENBAUM                                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN NK1TACHYKININ RECEPTOR.       
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115 13264 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30538204                                                     
JRNL        DOI    10.1073/PNAS.1812717115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0232                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11310                          
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) : 0.251                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 586                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 263                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 25.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 15                           
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3844                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.95000                                              
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : -0.54000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.667         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.498         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 67.704        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.846                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.756                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3992 ; 0.011 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  3802 ; 0.007 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5425 ; 1.515 ; 1.645       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8757 ; 1.534 ; 1.577       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   478 ; 5.788 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;32.667 ;21.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   670 ;14.734 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;13.023 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   521 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4342 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   910 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    28        A   227                          
REMARK   3    RESIDUE RANGE :   A  1001        A  1196                          
REMARK   3    RESIDUE RANGE :   A   238        A   320                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.7333  53.0530  24.8756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3470 T22:   0.0939                                     
REMARK   3      T33:   0.0192 T12:   0.0211                                     
REMARK   3      T13:   0.0166 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5641 L22:   1.0467                                     
REMARK   3      L33:   3.4727 L12:  -0.0857                                     
REMARK   3      L13:   1.3482 L23:  -0.5112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0447 S12:   0.1291 S13:   0.0060                       
REMARK   3      S21:   0.5774 S22:   0.0060 S23:   0.0512                       
REMARK   3      S31:  -0.0236 S32:   0.3199 S33:  -0.0507                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6E59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000235680.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11937                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.16800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4ZJ8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE, PH 5.4, 30%       
REMARK 280  PEG300, 200 MM POTASSIUM NITRATE, 2% 2,5-HEXANEDIOL, LIPIDIC        
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       61.89450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.98750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       61.89450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.98750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 24900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     PHE A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     CYS A   322                                                      
REMARK 465     CYS A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     PHE A   325                                                      
REMARK 465     ILE A   326                                                      
REMARK 465     SER A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     TYR A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     GLU A   335                                                      
REMARK 465     MET A   336                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     THR A   339                                                      
REMARK 465     ARG A   340                                                      
REMARK 465     TYR A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     GLN A   343                                                      
REMARK 465     THR A   344                                                      
REMARK 465     GLN A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     HIS A   347                                                      
REMARK 465     HIS A   348                                                      
REMARK 465     HIS A   349                                                      
REMARK 465     HIS A   350                                                      
REMARK 465     HIS A   351                                                      
REMARK 465     HIS A   352                                                      
REMARK 465     HIS A   353                                                      
REMARK 465     HIS A   354                                                      
REMARK 465     HIS A   355                                                      
REMARK 465     HIS A   356                                                      
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    LEU A 102     -130.53     46.52                                   
REMARK 500    TYR A 205      -69.84   -133.05                                   
REMARK 500    GLN A1045      -69.82    -90.20                                   
REMARK 500    PRO A1118       45.05    -87.06                                   
REMARK 500    TYR A 272      -68.11   -139.05                                   
REMARK 500    ILE A 283      -66.76   -127.58                                   
REMARK 500    ALA A 319      -74.69   -118.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue L76 A 2001                
DBREF  6E59 A    1   227  UNP    P25103   NK1R_HUMAN       1    227             
DBREF  6E59 A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  6E59 A  238   346  UNP    P25103   NK1R_HUMAN     238    346             
SEQADV 6E59 HIS A  347  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  348  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  349  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  350  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  351  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  352  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  353  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  354  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  355  UNP  P25103              EXPRESSION TAG                 
SEQADV 6E59 HIS A  356  UNP  P25103              EXPRESSION TAG                 
SEQRES   1 A  542  MET ASP ASN VAL LEU PRO VAL ASP SER ASP LEU SER PRO          
SEQRES   2 A  542  ASN ILE SER THR ASN THR SER GLU PRO ASN GLN PHE VAL          
SEQRES   3 A  542  GLN PRO ALA TRP GLN ILE VAL LEU TRP ALA ALA ALA TYR          
SEQRES   4 A  542  THR VAL ILE VAL VAL THR SER VAL VAL GLY ASN VAL VAL          
SEQRES   5 A  542  VAL MET TRP ILE ILE LEU ALA HIS LYS ARG MET ARG THR          
SEQRES   6 A  542  VAL THR ASN TYR PHE LEU VAL ASN LEU ALA PHE ALA GLU          
SEQRES   7 A  542  ALA SER MET ALA ALA PHE ASN THR VAL VAL ASN PHE THR          
SEQRES   8 A  542  TYR ALA VAL HIS ASN GLU TRP TYR TYR GLY LEU PHE TYR          
SEQRES   9 A  542  CYS LYS PHE HIS ASN PHE PHE PRO ILE ALA ALA VAL PHE          
SEQRES  10 A  542  ALA SER ILE TYR SER MET THR ALA VAL ALA PHE ASP ARG          
SEQRES  11 A  542  TYR MET ALA ILE ILE HIS PRO LEU GLN PRO ARG LEU SER          
SEQRES  12 A  542  ALA THR ALA THR LYS VAL VAL ILE CYS VAL ILE TRP VAL          
SEQRES  13 A  542  LEU ALA LEU LEU LEU ALA PHE PRO GLN GLY TYR TYR SER          
SEQRES  14 A  542  THR THR GLU THR MET PRO SER ARG VAL VAL CYS MET ILE          
SEQRES  15 A  542  GLU TRP PRO GLU HIS PRO ASN LYS ILE TYR GLU LYS VAL          
SEQRES  16 A  542  TYR HIS ILE CYS VAL THR VAL LEU ILE TYR PHE LEU PRO          
SEQRES  17 A  542  LEU LEU VAL ILE GLY TYR ALA TYR THR VAL VAL GLY ILE          
SEQRES  18 A  542  THR LEU TRP ALA SER GLU GLY ILE ASP CYS SER PHE TRP          
SEQRES  19 A  542  ASN GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS          
SEQRES  20 A  542  LYS SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL          
SEQRES  21 A  542  THR PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS          
SEQRES  22 A  542  GLY VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER          
SEQRES  23 A  542  SER LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE          
SEQRES  24 A  542  GLY LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER          
SEQRES  25 A  542  LEU GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU          
SEQRES  26 A  542  MET LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER          
SEQRES  27 A  542  VAL ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE          
SEQRES  28 A  542  GLY LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE          
SEQRES  29 A  542  PRO ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE          
SEQRES  30 A  542  THR ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO          
SEQRES  31 A  542  GLY GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU          
SEQRES  32 A  542  SER ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS          
SEQRES  33 A  542  LYS ARG ALA MET SER PHE SER GLU GLN VAL SER ALA LYS          
SEQRES  34 A  542  ARG LYS VAL VAL LYS MET MET ILE VAL VAL VAL CYS THR          
SEQRES  35 A  542  PHE ALA ILE CYS TRP LEU PRO PHE HIS ILE PHE PHE LEU          
SEQRES  36 A  542  LEU PRO TYR ILE ASN PRO ASP LEU TYR LEU LYS LYS PHE          
SEQRES  37 A  542  ILE GLN GLN VAL TYR LEU ALA ILE MET TRP LEU ALA MET          
SEQRES  38 A  542  SER SER THR MET TYR ASN PRO ILE ILE TYR CYS CYS LEU          
SEQRES  39 A  542  ASN ASP ARG PHE ARG LEU GLY PHE LYS HIS ALA PHE ARG          
SEQRES  40 A  542  CYS CYS PRO PHE ILE SER ALA GLY ASP TYR GLU GLY LEU          
SEQRES  41 A  542  GLU MET LYS SER THR ARG TYR LEU GLN THR GLN GLY HIS          
SEQRES  42 A  542  HIS HIS HIS HIS HIS HIS HIS HIS HIS                          
HET    L76  A2001      40                                                       
HETNAM     L76 1-(4-{[(2R,3S)-2-{(1R)-1-[3,5-BIS(TRIFLUOROMETHYL)               
HETNAM   2 L76  PHENYL]ETHOXY}-3-(4-FLUOROPHENYL)MORPHOLIN-4-                   
HETNAM   3 L76  YL]METHYL}-1H-1,2,3-TRIAZOL-5-YL)-N,N-                          
HETNAM   4 L76  DIMETHYLMETHANAMINE                                             
FORMUL   2  L76    C26 H28 F7 N5 O2                                             
HELIX    1 AA1 VAL A   33  HIS A   60  1                                  28    
HELIX    2 AA2 THR A   65  ALA A   79  1                                  15    
HELIX    3 AA3 MET A   81  VAL A   94  1                                  14    
HELIX    4 AA4 PHE A  103  HIS A  136  1                                  34    
HELIX    5 AA5 SER A  143  TYR A  167  1                                  25    
HELIX    6 AA6 PRO A  188  TYR A  205  1                                  18    
HELIX    7 AA7 TYR A  205  ALA A  225  1                                  21    
HELIX    8 AA8 ASN A 1008  LEU A 1012  5                                   5    
HELIX    9 AA9 SER A 1015  PHE A 1027  1                                  13    
HELIX   10 AB1 GLY A 1047  SER A 1060  1                                  14    
HELIX   11 AB2 LYS A 1061  GLN A 1065  5                                   5    
HELIX   12 AB3 ASP A 1076  HIS A 1090  1                                  15    
HELIX   13 AB4 SER A 1101  GLY A 1110  1                                  10    
HELIX   14 AB5 GLY A 1125  LEU A 1134  1                                  10    
HELIX   15 AB6 GLY A 1144  ILE A 1150  1                                   7    
HELIX   16 AB7 ASP A 1162  SER A 1177  1                                  16    
HELIX   17 AB8 LEU A 1181  TRP A  261  1                                  40    
HELIX   18 AB9 TRP A  261  LEU A  270  1                                  10    
HELIX   19 AC1 ILE A  283  SER A  297  1                                  15    
HELIX   20 AC2 TYR A  300  ASN A  309  1                                  10    
HELIX   21 AC3 ASN A  309  ALA A  319  1                                  11    
SHEET    1 AA1 2 THR A 170  THR A 173  0                                        
SHEET    2 AA1 2 VAL A 178  MET A 181 -1  O  VAL A 179   N  GLU A 172           
SHEET    1 AA2 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA2 6 MET A1067  ILE A1072  1  N  ILE A1071   O  LYS A1094           
SHEET    3 AA2 6 VAL A1033  ILE A1038  1  N  PHE A1035   O  ARG A1068           
SHEET    4 AA2 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5 AA2 6 ILE A1137  SER A1141  1  O  ILE A1139   N  VAL A1115           
SHEET    6 AA2 6 ILE A1156  VAL A1158  1  O  ILE A1156   N  PRO A1138           
SSBOND   1 CYS A  105    CYS A  180                          1555   1555  2.06  
SITE     1 AC1 12 PHE A  90  ASN A 109  PRO A 112  ILE A 113                    
SITE     2 AC1 12 VAL A 116  GLN A 165  HIS A 197  THR A 201                    
SITE     3 AC1 12 ILE A 204  PHE A 264  PHE A 268  TYR A 272                    
CRYST1  123.789   61.975  142.942  90.00 100.18  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008078  0.000000  0.001451        0.00000                         
SCALE2      0.000000  0.016136  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007108        0.00000                         
ATOM      1  N   PRO A  28     -14.430  30.123  65.418  1.00137.62           N  
ANISOU    1  N   PRO A  28    29700  11128  11459   -190  -3966   -152       N  
ATOM      2  CA  PRO A  28     -14.667  29.511  64.075  1.00150.58           C  
ANISOU    2  CA  PRO A  28    31135  12853  13224    -93  -4003   -181       C  
ATOM      3  C   PRO A  28     -13.410  28.999  63.358  1.00160.36           C  
ANISOU    3  C   PRO A  28    32273  14124  14532    225  -4317   -311       C  
ATOM      4  O   PRO A  28     -12.747  29.693  62.596  1.00167.85           O  
ANISOU    4  O   PRO A  28    32846  15297  15630    405  -4295   -384       O  
ATOM      5  CB  PRO A  28     -15.344  30.626  63.254  1.00132.47           C  
ANISOU    5  CB  PRO A  28    28410  10822  11101   -145  -3660   -155       C  
ATOM      6  CG  PRO A  28     -15.941  31.538  64.299  1.00123.31           C  
ANISOU    6  CG  PRO A  28    27338   9660   9853   -344  -3409    -75       C  
ATOM      7  CD  PRO A  28     -14.941  31.501  65.434  1.00122.12           C  
ANISOU    7  CD  PRO A  28    27473   9351   9573   -285  -3631   -114       C  
ATOM      8  N   ALA A  29     -13.057  27.757  63.653  1.00171.70           N  
ANISOU    8  N   ALA A  29    34065  15334  15838    299  -4626   -338       N  
ATOM      9  CA  ALA A  29     -11.824  27.145  63.109  1.00168.11           C  
ANISOU    9  CA  ALA A  29    33572  14895  15406    639  -4958   -470       C  
ATOM     10  C   ALA A  29     -11.995  26.767  61.638  1.00144.13           C  
ANISOU   10  C   ALA A  29    30274  11991  12496    791  -4961   -520       C  
ATOM     11  O   ALA A  29     -11.076  26.994  60.777  1.00120.51           O  
ANISOU   11  O   ALA A  29    26958   9212   9617   1078  -5051   -627       O  
ATOM     12  CB  ALA A  29     -11.445  25.941  63.940  1.00202.12           C  
ANISOU   12  CB  ALA A  29    38385  18895  19515    679  -5294   -485       C  
ATOM     13  N   TRP A  30     -13.144  26.161  61.358  1.00157.59           N  
ANISOU   13  N   TRP A  30    32126  13580  14170    598  -4875   -439       N  
ATOM     14  CA  TRP A  30     -13.512  25.703  60.000  1.00153.26           C  
ANISOU   14  CA  TRP A  30    31395  13113  13721    694  -4876   -468       C  
ATOM     15  C   TRP A  30     -13.510  26.884  59.033  1.00144.46           C  
ANISOU   15  C   TRP A  30    29732  12335  12819    758  -4608   -493       C  
ATOM     16  O   TRP A  30     -13.152  26.707  57.844  1.00110.40           O  
ANISOU   16  O   TRP A  30    25171   8165   8608    984  -4676   -576       O  
ATOM     17  CB  TRP A  30     -14.880  25.002  60.003  1.00147.13           C  
ANISOU   17  CB  TRP A  30    30868  12165  12870    397  -4796   -342       C  
ATOM     18  CG  TRP A  30     -14.885  23.597  60.527  1.00144.90           C  
ANISOU   18  CG  TRP A  30    31121  11546  12385    366  -5123   -327       C  
ATOM     19  CD1 TRP A  30     -14.649  22.457  59.813  1.00125.11           C  
ANISOU   19  CD1 TRP A  30    28803   8898   9832    550  -5420   -394       C  
ATOM     20  CD2 TRP A  30     -15.186  23.170  61.872  1.00153.02           C  
ANISOU   20  CD2 TRP A  30    32597  12324  13217    129  -5195   -233       C  
ATOM     21  NE1 TRP A  30     -14.764  21.357  60.620  1.00132.58           N  
ANISOU   21  NE1 TRP A  30    30294   9511  10568    442  -5686   -349       N  
ATOM     22  CE2 TRP A  30     -15.093  21.761  61.889  1.00140.77           C  
ANISOU   22  CE2 TRP A  30    31494  10480  11510    174  -5552   -246       C  
ATOM     23  CE3 TRP A  30     -15.511  23.836  63.063  1.00136.43           C  
ANISOU   23  CE3 TRP A  30    30579  10214  11042   -107  -5003   -141       C  
ATOM     24  CZ2 TRP A  30     -15.316  21.014  63.047  1.00132.14           C  
ANISOU   24  CZ2 TRP A  30    30917   9091  10197    -31  -5720   -162       C  
ATOM     25  CZ3 TRP A  30     -15.731  23.097  64.206  1.00130.77           C  
ANISOU   25  CZ3 TRP A  30    30357   9222  10108   -301  -5154    -61       C  
ATOM     26  CH2 TRP A  30     -15.635  21.705  64.195  1.00133.75           C  
ANISOU   26  CH2 TRP A  30    31165   9312  10338   -274  -5509    -67       C  
ATOM     27  N   GLN A  31     -13.902  28.058  59.521  1.00170.38           N  
ANISOU   27  N   GLN A  31    32845  15736  16155    570  -4319   -425       N  
ATOM     28  CA  GLN A  31     -14.139  29.201  58.612  1.00147.30           C  
ANISOU   28  CA  GLN A  31    29439  13105  13423    575  -4041   -426       C  
ATOM     29  C   GLN A  31     -12.866  30.002  58.370  1.00139.47           C  
ANISOU   29  C   GLN A  31    28144  12327  12521    807  -4108   -521       C  
ATOM     30  O   GLN A  31     -12.972  31.125  57.814  1.00118.31           O  
ANISOU   30  O   GLN A  31    25089   9880   9983    782  -3881   -512       O  
ATOM     31  CB  GLN A  31     -15.272  30.073  59.164  1.00131.33           C  
ANISOU   31  CB  GLN A  31    27385  11109  11403    274  -3696   -307       C  
ATOM     32  CG  GLN A  31     -16.657  29.474  58.942  1.00122.77           C  
ANISOU   32  CG  GLN A  31    26419   9942  10285     46  -3563   -201       C  
ATOM     33  CD  GLN A  31     -16.905  28.231  59.766  1.00123.20           C  
ANISOU   33  CD  GLN A  31    26963   9704  10141    -75  -3770   -147       C  
ATOM     34  OE1 GLN A  31     -16.696  28.212  60.979  1.00144.98           O  
ANISOU   34  OE1 GLN A  31    30006  12320  12757   -159  -3826   -119       O  
ATOM     35  NE2 GLN A  31     -17.366  27.178  59.110  1.00103.97           N  
ANISOU   35  NE2 GLN A  31    24651   7167   7684    -97  -3896   -128       N  
ATOM     36  N   ILE A  32     -11.705  29.530  58.803  1.00147.51           N  
ANISOU   36  N   ILE A  32    29307  13283  13454   1009  -4404   -599       N  
ATOM     37  CA  ILE A  32     -10.494  30.390  58.788  1.00133.14           C  
ANISOU   37  CA  ILE A  32    27206  11683  11697   1176  -4462   -661       C  
ATOM     38  C   ILE A  32      -9.989  30.570  57.346  1.00112.04           C  
ANISOU   38  C   ILE A  32    24096   9302   9171   1407  -4469   -736       C  
ATOM     39  O   ILE A  32      -9.857  31.725  56.862  1.00 96.09           O  
ANISOU   39  O   ILE A  32    21697   7532   7280   1376  -4285   -722       O  
ATOM     40  CB  ILE A  32      -9.386  29.797  59.697  1.00156.89           C  
ANISOU   40  CB  ILE A  32    30489  14559  14563   1332  -4790   -717       C  
ATOM     41  CG1 ILE A  32      -9.784  29.796  61.177  1.00143.99           C  
ANISOU   41  CG1 ILE A  32    29265  12661  12782   1097  -4773   -640       C  
ATOM     42  CG2 ILE A  32      -8.058  30.515  59.477  1.00185.85           C  
ANISOU   42  CG2 ILE A  32    33823  18497  18294   1534  -4893   -781       C  
ATOM     43  CD1 ILE A  32      -8.754  29.177  62.106  1.00123.02           C  
ANISOU   43  CD1 ILE A  32    26911   9850   9980   1237  -5103   -691       C  
ATOM     44  N   VAL A  33      -9.524  29.455  56.807  1.00118.11           N  
ANISOU   44  N   VAL A  33    24948  10034   9891   1657  -4719   -821       N  
ATOM     45  CA  VAL A  33      -8.864  29.479  55.476  1.00131.00           C  
ANISOU   45  CA  VAL A  33    26191  11955  11627   1935  -4773   -908       C  
ATOM     46  C   VAL A  33      -9.876  29.794  54.394  1.00156.44           C  
ANISOU   46  C   VAL A  33    29175  15278  14985   1825  -4516   -870       C  
ATOM     47  O   VAL A  33      -9.442  30.130  53.325  1.00144.96           O  
ANISOU   47  O   VAL A  33    27348  14094  13633   1993  -4487   -921       O  
ATOM     48  CB  VAL A  33      -8.091  28.177  55.187  1.00138.17           C  
ANISOU   48  CB  VAL A  33    27274  12797  12425   2275  -5121  -1021       C  
ATOM     49  CG1 VAL A  33      -7.418  28.210  53.822  1.00144.94           C  
ANISOU   49  CG1 VAL A  33    27723  13978  13369   2580  -5163  -1113       C  
ATOM     50  CG2 VAL A  33      -7.064  27.881  56.269  1.00135.20           C  
ANISOU   50  CG2 VAL A  33    27126  12329  11914   2397  -5386  -1060       C  
ATOM     51  N   LEU A  34     -11.166  29.726  54.685  1.00164.00           N  
ANISOU   51  N   LEU A  34    30328  16047  15937   1546  -4332   -777       N  
ATOM     52  CA  LEU A  34     -12.235  30.012  53.714  1.00131.46           C  
ANISOU   52  CA  LEU A  34    25995  12012  11939   1419  -4084   -729       C  
ATOM     53  C   LEU A  34     -12.170  31.472  53.262  1.00104.27           C  
ANISOU   53  C   LEU A  34    22112   8855   8650   1359  -3830   -707       C  
ATOM     54  O   LEU A  34     -12.126  31.768  52.022  1.00120.86           O  
ANISOU   54  O   LEU A  34    23862  11181  10876   1467  -3753   -740       O  
ATOM     55  CB  LEU A  34     -13.567  29.713  54.416  1.00128.69           C  
ANISOU   55  CB  LEU A  34    25962  11414  11519   1104  -3945   -615       C  
ATOM     56  CG  LEU A  34     -14.846  29.981  53.626  1.00120.68           C  
ANISOU   56  CG  LEU A  34    24776  10465  10613    921  -3678   -540       C  
ATOM     57  CD1 LEU A  34     -14.998  28.977  52.495  1.00125.98           C  
ANISOU   57  CD1 LEU A  34    25453  11111  11301   1065  -3819   -587       C  
ATOM     58  CD2 LEU A  34     -16.062  29.941  54.542  1.00100.00           C  
ANISOU   58  CD2 LEU A  34    22418   7667   7909    592  -3509   -410       C  
ATOM     59  N   TRP A  35     -12.153  32.363  54.232  1.00 91.15           N  
ANISOU   59  N   TRP A  35    20486   7177   6970   1193  -3717   -651       N  
ATOM     60  CA  TRP A  35     -12.169  33.810  53.929  1.00102.26           C  
ANISOU   60  CA  TRP A  35    21540   8811   8503   1105  -3486   -619       C  
ATOM     61  C   TRP A  35     -10.766  34.331  53.654  1.00103.77           C  
ANISOU   61  C   TRP A  35    21458   9242   8729   1297  -3632   -682       C  
ATOM     62  O   TRP A  35     -10.673  35.502  53.370  1.00134.72           O  
ANISOU   62  O   TRP A  35    25098  13348  12742   1222  -3480   -652       O  
ATOM     63  CB  TRP A  35     -12.896  34.579  55.040  1.00118.46           C  
ANISOU   63  CB  TRP A  35    23767  10735  10507    840  -3287   -529       C  
ATOM     64  CG  TRP A  35     -14.340  34.193  55.168  1.00137.28           C  
ANISOU   64  CG  TRP A  35    26330  12964  12864    641  -3103   -451       C  
ATOM     65  CD1 TRP A  35     -14.880  33.334  56.080  1.00139.72           C  
ANISOU   65  CD1 TRP A  35    27036  13021  13028    520  -3160   -404       C  
ATOM     66  CD2 TRP A  35     -15.432  34.617  54.331  1.00165.30           C  
ANISOU   66  CD2 TRP A  35    29659  16618  16528    531  -2841   -402       C  
ATOM     67  NE1 TRP A  35     -16.229  33.209  55.883  1.00147.29           N  
ANISOU   67  NE1 TRP A  35    28021  13941  13998    330  -2947   -320       N  
ATOM     68  CE2 TRP A  35     -16.598  33.985  54.817  1.00154.66           C  
ANISOU   68  CE2 TRP A  35    28577  15091  15093    341  -2749   -320       C  
ATOM     69  CE3 TRP A  35     -15.546  35.472  53.229  1.00161.31           C  
ANISOU   69  CE3 TRP A  35    28760  16347  16182    566  -2681   -412       C  
ATOM     70  CZ2 TRP A  35     -17.853  34.185  54.241  1.00136.45           C  
ANISOU   70  CZ2 TRP A  35    26137  12849  12859    195  -2503   -249       C  
ATOM     71  CZ3 TRP A  35     -16.787  35.672  52.661  1.00148.27           C  
ANISOU   71  CZ3 TRP A  35    26996  14734  14606    432  -2441   -351       C  
ATOM     72  CH2 TRP A  35     -17.924  35.036  53.162  1.00129.82           C  
ANISOU   72  CH2 TRP A  35    24908  12231  12183    253  -2353   -271       C  
ATOM     73  N   ALA A  36      -9.745  33.497  53.770  1.00 94.26           N  
ANISOU   73  N   ALA A  36    20343   8031   7439   1527  -3921   -758       N  
ATOM     74  CA  ALA A  36      -8.393  33.880  53.300  1.00 84.72           C  
ANISOU   74  CA  ALA A  36    18810   7118   6261   1740  -4067   -816       C  
ATOM     75  C   ALA A  36      -8.342  33.800  51.774  1.00 96.36           C  
ANISOU   75  C   ALA A  36    19922   8845   7843   1908  -4024   -863       C  
ATOM     76  O   ALA A  36      -7.973  34.792  51.093  1.00 95.39           O  
ANISOU   76  O   ALA A  36    19408   9012   7823   1899  -3917   -847       O  
ATOM     77  CB  ALA A  36      -7.347  32.995  53.931  1.00 80.18           C  
ANISOU   77  CB  ALA A  36    18442   6472   5548   1955  -4390   -883       C  
ATOM     78  N   ALA A  37      -8.805  32.673  51.272  1.00104.90           N  
ANISOU   78  N   ALA A  37    21162   9799   8895   2027  -4096   -910       N  
ATOM     79  CA  ALA A  37      -8.959  32.395  49.838  1.00116.04           C  
ANISOU   79  CA  ALA A  37    22315  11386  10389   2185  -4058   -959       C  
ATOM     80  C   ALA A  37      -9.948  33.339  49.188  1.00114.22           C  
ANISOU   80  C   ALA A  37    21847  11243  10306   1962  -3745   -885       C  
ATOM     81  O   ALA A  37      -9.639  33.826  48.091  1.00 95.80           O  
ANISOU   81  O   ALA A  37    19134   9193   8070   2060  -3679   -908       O  
ATOM     82  CB  ALA A  37      -9.357  30.955  49.621  1.00124.51           C  
ANISOU   82  CB  ALA A  37    23705  12229  11374   2321  -4222  -1014       C  
ATOM     83  N   ALA A  38     -11.089  33.581  49.830  1.00113.94           N  
ANISOU   83  N   ALA A  38    22023  10989  10278   1683  -3562   -800       N  
ATOM     84  CA  ALA A  38     -12.065  34.587  49.394  1.00 87.64           C  
ANISOU   84  CA  ALA A  38    18489   7734   7076   1465  -3257   -725       C  
ATOM     85  C   ALA A  38     -11.431  35.931  49.041  1.00 79.17           C  
ANISOU   85  C   ALA A  38    17040   6943   6096   1450  -3161   -712       C  
ATOM     86  O   ALA A  38     -11.760  36.479  47.982  1.00 83.31           O  
ANISOU   86  O   ALA A  38    17264   7648   6740   1436  -3008   -702       O  
ATOM     87  CB  ALA A  38     -13.134  34.724  50.453  1.00 87.19           C  
ANISOU   87  CB  ALA A  38    18730   7427   6969   1196  -3105   -637       C  
ATOM     88  N   TYR A  39     -10.637  36.512  49.918  1.00 79.97           N  
ANISOU   88  N   TYR A  39    17173   7069   6143   1418  -3238   -699       N  
ATOM     89  CA  TYR A  39     -10.072  37.849  49.661  1.00 87.24           C  
ANISOU   89  CA  TYR A  39    17772   8236   7138   1354  -3161   -666       C  
ATOM     90  C   TYR A  39      -8.904  37.769  48.675  1.00 86.86           C  
ANISOU   90  C   TYR A  39    17371   8513   7117   1585  -3312   -723       C  
ATOM     91  O   TYR A  39      -8.687  38.727  47.907  1.00122.22           O  
ANISOU   91  O   TYR A  39    21505  13243  11687   1540  -3212   -694       O  
ATOM     92  CB  TYR A  39      -9.757  38.530  50.999  1.00 88.77           C  
ANISOU   92  CB  TYR A  39    18161   8312   7253   1203  -3188   -618       C  
ATOM     93  CG  TYR A  39     -10.995  38.996  51.733  1.00 91.68           C  
ANISOU   93  CG  TYR A  39    18770   8450   7613    966  -2965   -551       C  
ATOM     94  CD1 TYR A  39     -11.920  38.085  52.225  1.00107.76           C  
ANISOU   94  CD1 TYR A  39    21123  10235   9584    917  -2926   -543       C  
ATOM     95  CD2 TYR A  39     -11.271  40.346  51.916  1.00 80.87           C  
ANISOU   95  CD2 TYR A  39    17315   7124   6287    792  -2795   -491       C  
ATOM     96  CE1 TYR A  39     -13.073  38.496  52.878  1.00 91.72           C  
ANISOU   96  CE1 TYR A  39    19280   8038   7530    710  -2709   -475       C  
ATOM     97  CE2 TYR A  39     -12.419  40.775  52.569  1.00 77.25           C  
ANISOU   97  CE2 TYR A  39    17068   6480   5804    613  -2584   -438       C  
ATOM     98  CZ  TYR A  39     -13.331  39.846  53.045  1.00 81.82           C  
ANISOU   98  CZ  TYR A  39    17924   6846   6317    574  -2530   -428       C  
ATOM     99  OH  TYR A  39     -14.469  40.249  53.684  1.00 71.93           O  
ANISOU   99  OH  TYR A  39    16852   5452   5025    406  -2312   -369       O  
ATOM    100  N   THR A  40      -8.209  36.642  48.724  1.00 80.55           N  
ANISOU  100  N   THR A  40    16673   7704   6226   1826  -3548   -800       N  
ATOM    101  CA  THR A  40      -6.986  36.398  47.926  1.00 91.01           C  
ANISOU  101  CA  THR A  40    17689   9354   7535   2099  -3725   -866       C  
ATOM    102  C   THR A  40      -7.304  36.444  46.448  1.00 80.12           C  
ANISOU  102  C   THR A  40    15999   8185   6258   2185  -3605   -888       C  
ATOM    103  O   THR A  40      -6.615  37.176  45.676  1.00 71.92           O  
ANISOU  103  O   THR A  40    14561   7494   5270   2226  -3583   -875       O  
ATOM    104  CB  THR A  40      -6.366  35.030  48.226  1.00108.15           C  
ANISOU  104  CB  THR A  40    20084  11434   9574   2381  -3999   -959       C  
ATOM    105  OG1 THR A  40      -6.082  34.993  49.622  1.00111.29           O  
ANISOU  105  OG1 THR A  40    20783  11626   9874   2292  -4114   -935       O  
ATOM    106  CG2 THR A  40      -5.109  34.755  47.429  1.00104.69           C  
ANISOU  106  CG2 THR A  40    19321  11358   9098   2700  -4178  -1033       C  
ATOM    107  N   VAL A  41      -8.364  35.762  46.067  1.00 79.23           N  
ANISOU  107  N   VAL A  41    16058   7871   6172   2177  -3520   -907       N  
ATOM    108  CA  VAL A  41      -8.829  35.757  44.654  1.00 87.89           C  
ANISOU  108  CA  VAL A  41    16900   9125   7367   2242  -3398   -926       C  
ATOM    109  C   VAL A  41      -9.185  37.184  44.229  1.00 86.08           C  
ANISOU  109  C   VAL A  41    16376   9061   7268   2013  -3159   -842       C  
ATOM    110  O   VAL A  41      -8.873  37.560  43.100  1.00100.30           O  
ANISOU  110  O   VAL A  41    17826  11148   9134   2095  -3113   -853       O  
ATOM    111  CB  VAL A  41      -9.986  34.774  44.389  1.00 89.39           C  
ANISOU  111  CB  VAL A  41    17360   9043   7558   2235  -3361   -944       C  
ATOM    112  CG1 VAL A  41      -9.512  33.332  44.463  1.00 97.37           C  
ANISOU  112  CG1 VAL A  41    18623   9936   8436   2516  -3633  -1041       C  
ATOM    113  CG2 VAL A  41     -11.177  34.997  45.303  1.00109.56           C  
ANISOU  113  CG2 VAL A  41    20203  11295  10128   1932  -3200   -858       C  
ATOM    114  N   ILE A  42      -9.811  37.920  45.129  1.00 72.50           N  
ANISOU  114  N   ILE A  42    14818   7159   5568   1748  -3022   -765       N  
ATOM    115  CA  ILE A  42     -10.193  39.322  44.835  1.00 63.08           C  
ANISOU  115  CA  ILE A  42    13403   6080   4481   1531  -2809   -687       C  
ATOM    116  C   ILE A  42      -8.957  40.130  44.472  1.00 61.80           C  
ANISOU  116  C   ILE A  42    12902   6254   4324   1572  -2895   -673       C  
ATOM    117  O   ILE A  42      -8.874  40.654  43.436  1.00 72.42           O  
ANISOU  117  O   ILE A  42    13936   7834   5746   1577  -2817   -661       O  
ATOM    118  CB  ILE A  42     -10.957  39.954  46.009  1.00 61.72           C  
ANISOU  118  CB  ILE A  42    13501   5653   4295   1279  -2678   -617       C  
ATOM    119  CG1 ILE A  42     -12.312  39.268  46.220  1.00 71.07           C  
ANISOU  119  CG1 ILE A  42    14957   6565   5481   1202  -2554   -607       C  
ATOM    120  CG2 ILE A  42     -11.082  41.457  45.789  1.00 55.24           C  
ANISOU  120  CG2 ILE A  42    12472   4961   3555   1094  -2517   -548       C  
ATOM    121  CD1 ILE A  42     -13.163  39.877  47.314  1.00 81.80           C  
ANISOU  121  CD1 ILE A  42    16560   7708   6811    973  -2396   -537       C  
ATOM    122  N   VAL A  43      -8.041  40.283  45.391  1.00 68.92           N  
ANISOU  122  N   VAL A  43    13877   7171   5137   1571  -3052   -662       N  
ATOM    123  CA  VAL A  43      -6.832  41.118  45.166  1.00 73.25           C  
ANISOU  123  CA  VAL A  43    14104   8051   5674   1564  -3149   -624       C  
ATOM    124  C   VAL A  43      -6.112  40.703  43.885  1.00 72.62           C  
ANISOU  124  C   VAL A  43    13659   8329   5604   1804  -3224   -675       C  
ATOM    125  O   VAL A  43      -5.757  41.544  43.088  1.00 86.44           O  
ANISOU  125  O   VAL A  43    15067  10368   7407   1739  -3167   -626       O  
ATOM    126  CB  VAL A  43      -5.864  41.110  46.368  1.00 87.93           C  
ANISOU  126  CB  VAL A  43    16111   9878   7418   1562  -3353   -611       C  
ATOM    127  CG1 VAL A  43      -6.509  41.701  47.612  1.00 99.34           C  
ANISOU  127  CG1 VAL A  43    17898  11001   8843   1314  -3272   -554       C  
ATOM    128  CG2 VAL A  43      -5.296  39.729  46.666  1.00 90.81           C  
ANISOU  128  CG2 VAL A  43    16623  10201   7678   1841  -3569   -703       C  
ATOM    129  N   VAL A  44      -5.896  39.409  43.735  1.00 70.26           N  
ANISOU  129  N   VAL A  44    13456   8002   5238   2080  -3360   -771       N  
ATOM    130  CA  VAL A  44      -5.137  38.906  42.561  1.00 77.61           C  
ANISOU  130  CA  VAL A  44    14059   9282   6146   2365  -3451   -835       C  
ATOM    131  C   VAL A  44      -5.861  39.204  41.261  1.00 73.90           C  
ANISOU  131  C   VAL A  44    13370   8919   5787   2334  -3258   -829       C  
ATOM    132  O   VAL A  44      -5.235  39.839  40.425  1.00 68.01           O  
ANISOU  132  O   VAL A  44    12240   8537   5064   2347  -3238   -798       O  
ATOM    133  CB  VAL A  44      -4.710  37.427  42.662  1.00 85.76           C  
ANISOU  133  CB  VAL A  44    15270  10252   7060   2710  -3664   -952       C  
ATOM    134  CG1 VAL A  44      -3.716  37.214  43.794  1.00 84.10           C  
ANISOU  134  CG1 VAL A  44    15184  10038   6731   2780  -3884   -959       C  
ATOM    135  CG2 VAL A  44      -5.882  36.466  42.762  1.00 90.83           C  
ANISOU  135  CG2 VAL A  44    16295  10503   7711   2729  -3622  -1003       C  
ATOM    136  N   THR A  45      -7.136  38.813  41.140  1.00 73.04           N  
ANISOU  136  N   THR A  45    13496   8511   5742   2267  -3124   -845       N  
ATOM    137  CA  THR A  45      -7.905  38.986  39.906  1.00 73.55           C  
ANISOU  137  CA  THR A  45    13383   8648   5912   2247  -2951   -844       C  
ATOM    138  C   THR A  45      -8.120  40.463  39.593  1.00 64.79           C  
ANISOU  138  C   THR A  45    12032   7678   4906   1979  -2770   -743       C  
ATOM    139  O   THR A  45      -8.165  40.872  38.419  1.00 91.70           O  
ANISOU  139  O   THR A  45    15140  11318   8381   1990  -2677   -732       O  
ATOM    140  CB  THR A  45      -9.259  38.268  39.997  1.00 73.74           C  
ANISOU  140  CB  THR A  45    13733   8309   5974   2196  -2859   -863       C  
ATOM    141  OG1 THR A  45      -9.895  38.655  41.216  1.00 85.79           O  
ANISOU  141  OG1 THR A  45    15544   9546   7504   1951  -2783   -800       O  
ATOM    142  CG2 THR A  45      -9.115  36.762  39.938  1.00 75.41           C  
ANISOU  142  CG2 THR A  45    14166   8400   6085   2475  -3047   -966       C  
ATOM    143  N   SER A  46      -8.419  41.228  40.623  1.00 57.58           N  
ANISOU  143  N   SER A  46    11292   6578   4004   1734  -2711   -672       N  
ATOM    144  CA  SER A  46      -8.645  42.684  40.539  1.00 54.69           C  
ANISOU  144  CA  SER A  46    10782   6281   3716   1468  -2565   -576       C  
ATOM    145  C   SER A  46      -7.437  43.405  39.985  1.00 53.73           C  
ANISOU  145  C   SER A  46    10285   6556   3571   1469  -2654   -532       C  
ATOM    146  O   SER A  46      -7.534  44.162  39.016  1.00 65.75           O  
ANISOU  146  O   SER A  46    11538   8278   5165   1383  -2550   -488       O  
ATOM    147  CB  SER A  46      -8.986  43.299  41.867  1.00 64.59           C  
ANISOU  147  CB  SER A  46    12325   7270   4945   1251  -2532   -520       C  
ATOM    148  OG  SER A  46      -9.723  44.503  41.674  1.00 54.38           O  
ANISOU  148  OG  SER A  46    10988   5936   3738   1021  -2346   -448       O  
ATOM    149  N   VAL A  47      -6.317  43.218  40.663  1.00 60.28           N  
ANISOU  149  N   VAL A  47    11108   7498   4297   1543  -2849   -533       N  
ATOM    150  CA  VAL A  47      -5.062  43.934  40.307  1.00 68.18           C  
ANISOU  150  CA  VAL A  47    11747   8904   5252   1512  -2959   -469       C  
ATOM    151  C   VAL A  47      -4.600  43.498  38.927  1.00 67.03           C  
ANISOU  151  C   VAL A  47    11235   9127   5106   1736  -2969   -512       C  
ATOM    152  O   VAL A  47      -4.323  44.383  38.104  1.00 74.24           O  
ANISOU  152  O   VAL A  47    11827  10325   6053   1614  -2910   -439       O  
ATOM    153  CB  VAL A  47      -3.911  43.773  41.321  1.00 72.11           C  
ANISOU  153  CB  VAL A  47    12292   9476   5630   1555  -3183   -457       C  
ATOM    154  CG1 VAL A  47      -4.248  44.397  42.666  1.00 77.73           C  
ANISOU  154  CG1 VAL A  47    13342   9861   6330   1307  -3180   -399       C  
ATOM    155  CG2 VAL A  47      -3.451  42.330  41.485  1.00 69.05           C  
ANISOU  155  CG2 VAL A  47    11994   9090   5152   1897  -3343   -571       C  
ATOM    156  N   VAL A  48      -4.532  42.188  38.681  1.00 68.07           N  
ANISOU  156  N   VAL A  48    11432   9243   5186   2051  -3048   -627       N  
ATOM    157  CA  VAL A  48      -4.058  41.685  37.374  1.00 75.80           C  
ANISOU  157  CA  VAL A  48    12083  10576   6138   2313  -3069   -683       C  
ATOM    158  C   VAL A  48      -4.969  42.242  36.285  1.00 79.33           C  
ANISOU  158  C   VAL A  48    12398  11034   6708   2185  -2858   -654       C  
ATOM    159  O   VAL A  48      -4.456  42.789  35.268  1.00 75.50           O  
ANISOU  159  O   VAL A  48    11530  10929   6225   2182  -2825   -612       O  
ATOM    160  CB  VAL A  48      -3.909  40.154  37.245  1.00 73.02           C  
ANISOU  160  CB  VAL A  48    11874  10170   5700   2699  -3201   -823       C  
ATOM    161  CG1 VAL A  48      -2.848  39.605  38.182  1.00 67.99           C  
ANISOU  161  CG1 VAL A  48    11313   9592   4928   2870  -3432   -857       C  
ATOM    162  CG2 VAL A  48      -5.228  39.410  37.392  1.00 74.72           C  
ANISOU  162  CG2 VAL A  48    12478   9936   5973   2702  -3118   -884       C  
ATOM    163  N   GLY A  49      -6.274  42.108  36.479  1.00 76.88           N  
ANISOU  163  N   GLY A  49    12384  10337   6489   2078  -2720   -670       N  
ATOM    164  CA  GLY A  49      -7.246  42.557  35.474  1.00 74.15           C  
ANISOU  164  CA  GLY A  49    11940   9969   6261   1969  -2522   -648       C  
ATOM    165  C   GLY A  49      -7.087  44.004  35.116  1.00 77.36           C  
ANISOU  165  C   GLY A  49    12095  10574   6725   1704  -2430   -534       C  
ATOM    166  O   GLY A  49      -6.954  44.325  33.931  1.00 90.63           O  
ANISOU  166  O   GLY A  49    13470  12530   8435   1725  -2369   -517       O  
ATOM    167  N   ASN A  50      -7.028  44.873  36.116  1.00 65.49           N  
ANISOU  167  N   ASN A  50    10720   8941   5219   1461  -2437   -454       N  
ATOM    168  CA  ASN A  50      -7.065  46.336  35.896  1.00 68.17           C  
ANISOU  168  CA  ASN A  50    10912   9376   5611   1168  -2355   -339       C  
ATOM    169  C   ASN A  50      -5.759  46.886  35.346  1.00 61.17           C  
ANISOU  169  C   ASN A  50     9638   8948   4654   1143  -2470   -269       C  
ATOM    170  O   ASN A  50      -5.785  47.866  34.552  1.00 53.64           O  
ANISOU  170  O   ASN A  50     8461   8173   3743    965  -2395   -187       O  
ATOM    171  CB  ASN A  50      -7.560  47.096  37.130  1.00 81.79           C  
ANISOU  171  CB  ASN A  50    12952  10775   7348    923  -2323   -283       C  
ATOM    172  CG  ASN A  50      -9.043  46.884  37.352  1.00 89.18           C  
ANISOU  172  CG  ASN A  50    14181  11334   8369    891  -2146   -321       C  
ATOM    173  OD1 ASN A  50      -9.866  47.752  37.073  1.00 78.70           O  
ANISOU  173  OD1 ASN A  50    12871   9908   7122    720  -1996   -275       O  
ATOM    174  ND2 ASN A  50      -9.401  45.701  37.814  1.00130.25           N  
ANISOU  174  ND2 ASN A  50    19607  16335  13547   1060  -2170   -403       N  
ATOM    175  N   VAL A  51      -4.641  46.330  35.773  1.00 76.89           N  
ANISOU  175  N   VAL A  51    11547  11134   6531   1298  -2652   -288       N  
ATOM    176  CA  VAL A  51      -3.304  46.788  35.319  1.00 89.44           C  
ANISOU  176  CA  VAL A  51    12737  13214   8031   1279  -2777   -209       C  
ATOM    177  C   VAL A  51      -3.152  46.420  33.850  1.00 83.32           C  
ANISOU  177  C   VAL A  51    11618  12783   7256   1472  -2717   -247       C  
ATOM    178  O   VAL A  51      -2.475  47.149  33.096  1.00 74.96           O  
ANISOU  178  O   VAL A  51    10197  12121   6164   1362  -2728   -153       O  
ATOM    179  CB  VAL A  51      -2.186  46.154  36.185  1.00 91.84           C  
ANISOU  179  CB  VAL A  51    13045  13642   8206   1439  -2991   -232       C  
ATOM    180  CG1 VAL A  51      -2.025  44.648  35.979  1.00 95.56           C  
ANISOU  180  CG1 VAL A  51    13546  14141   8619   1854  -3058   -380       C  
ATOM    181  CG2 VAL A  51      -0.850  46.851  35.975  1.00 85.13           C  
ANISOU  181  CG2 VAL A  51    11807  13277   7260   1331  -3125   -114       C  
ATOM    182  N   VAL A  52      -3.756  45.293  33.464  1.00 81.10           N  
ANISOU  182  N   VAL A  52    11461  12353   6998   1751  -2667   -377       N  
ATOM    183  CA  VAL A  52      -3.663  44.883  32.052  1.00 80.47           C  
ANISOU  183  CA  VAL A  52    11090  12576   6909   1961  -2612   -425       C  
ATOM    184  C   VAL A  52      -4.599  45.740  31.220  1.00 72.18           C  
ANISOU  184  C   VAL A  52     9986  11455   5983   1735  -2423   -368       C  
ATOM    185  O   VAL A  52      -4.401  45.901  29.995  1.00 68.48           O  
ANISOU  185  O   VAL A  52     9205  11306   5508   1788  -2368   -354       O  
ATOM    186  CB  VAL A  52      -3.845  43.369  31.839  1.00 89.76           C  
ANISOU  186  CB  VAL A  52    12411  13651   8041   2355  -2662   -583       C  
ATOM    187  CG1 VAL A  52      -2.811  42.562  32.608  1.00 91.55           C  
ANISOU  187  CG1 VAL A  52    12672  13985   8128   2600  -2870   -640       C  
ATOM    188  CG2 VAL A  52      -5.239  42.890  32.178  1.00 98.85           C  
ANISOU  188  CG2 VAL A  52    13973  14289   9296   2324  -2560   -645       C  
ATOM    189  N   VAL A  53      -5.730  46.127  31.784  1.00 67.09           N  
ANISOU  189  N   VAL A  53     9657  10383   5448   1535  -2312   -354       N  
ATOM    190  CA  VAL A  53      -6.670  47.057  31.100  1.00 67.89           C  
ANISOU  190  CA  VAL A  53     9731  10393   5668   1306  -2137   -293       C  
ATOM    191  C   VAL A  53      -5.904  48.324  30.730  1.00 75.38           C  
ANISOU  191  C   VAL A  53    10384  11669   6586   1060  -2167   -157       C  
ATOM    192  O   VAL A  53      -5.974  48.790  29.584  1.00 78.72           O  
ANISOU  192  O   VAL A  53    10559  12313   7037   1005  -2088   -117       O  
ATOM    193  CB  VAL A  53      -7.872  47.357  32.012  1.00 62.96           C  
ANISOU  193  CB  VAL A  53     9497   9285   5138   1131  -2035   -290       C  
ATOM    194  CG1 VAL A  53      -8.596  48.616  31.557  1.00 62.72           C  
ANISOU  194  CG1 VAL A  53     9434   9191   5203    859  -1894   -203       C  
ATOM    195  CG2 VAL A  53      -8.826  46.170  32.121  1.00 59.56           C  
ANISOU  195  CG2 VAL A  53     9328   8551   4749   1325  -1978   -402       C  
ATOM    196  N   MET A  54      -5.210  48.893  31.714  1.00 88.32           N  
ANISOU  196  N   MET A  54    12073  13323   8161    892  -2288    -79       N  
ATOM    197  CA  MET A  54      -4.464  50.155  31.502  1.00 93.18           C  
ANISOU  197  CA  MET A  54    12451  14220   8732    605  -2349     71       C  
ATOM    198  C   MET A  54      -3.418  49.919  30.416  1.00104.16           C  
ANISOU  198  C   MET A  54    13383  16161  10029    740  -2406     95       C  
ATOM    199  O   MET A  54      -3.237  50.813  29.550  1.00113.59           O  
ANISOU  199  O   MET A  54    14325  17611  11223    543  -2371    200       O  
ATOM    200  CB  MET A  54      -3.760  50.594  32.787  1.00114.65           C  
ANISOU  200  CB  MET A  54    15304  16882  11374    441  -2508    143       C  
ATOM    201  CG  MET A  54      -4.709  50.777  33.960  1.00119.65           C  
ANISOU  201  CG  MET A  54    16399  16991  12069    335  -2459    115       C  
ATOM    202  SD  MET A  54      -3.894  51.259  35.493  1.00 88.56           S  
ANISOU  202  SD  MET A  54    12655  12961   8031    153  -2656    193       S  
ATOM    203  CE  MET A  54      -3.103  52.786  34.986  1.00135.12           C  
ANISOU  203  CE  MET A  54    18280  19182  13874   -212  -2748    383       C  
ATOM    204  N   TRP A  55      -2.802  48.740  30.431  1.00100.57           N  
ANISOU  204  N   TRP A  55    12836  15882   9493   1077  -2489     -2       N  
ATOM    205  CA  TRP A  55      -1.748  48.391  29.460  1.00111.50           C  
ANISOU  205  CA  TRP A  55    13778  17823  10760   1270  -2547      4       C  
ATOM    206  C   TRP A  55      -2.329  48.268  28.070  1.00138.54           C  
ANISOU  206  C   TRP A  55    17047  21353  14238   1368  -2397    -36       C  
ATOM    207  O   TRP A  55      -1.753  48.834  27.114  1.00135.05           O  
ANISOU  207  O   TRP A  55    16234  21341  13739   1281  -2384     54       O  
ATOM    208  CB  TRP A  55      -1.051  47.088  29.894  1.00100.32           C  
ANISOU  208  CB  TRP A  55    12367  16512   9237   1656  -2679   -113       C  
ATOM    209  CG  TRP A  55      -0.005  46.597  28.933  1.00110.90           C  
ANISOU  209  CG  TRP A  55    13270  18428  10439   1929  -2736   -131       C  
ATOM    210  CD1 TRP A  55      -0.217  46.064  27.694  1.00109.12           C  
ANISOU  210  CD1 TRP A  55    12873  18385  10201   2172  -2643   -209       C  
ATOM    211  CD2 TRP A  55       1.423  46.584  29.128  1.00117.78           C  
ANISOU  211  CD2 TRP A  55    13812  19788  11149   2001  -2899    -68       C  
ATOM    212  NE1 TRP A  55       0.972  45.721  27.108  1.00105.68           N  
ANISOU  212  NE1 TRP A  55    12030  18522   9601   2407  -2728   -205       N  
ATOM    213  CE2 TRP A  55       1.997  46.027  27.963  1.00114.49           C  
ANISOU  213  CE2 TRP A  55    13025  19851  10623   2309  -2884   -116       C  
ATOM    214  CE3 TRP A  55       2.274  46.986  30.166  1.00125.95           C  
ANISOU  214  CE3 TRP A  55    14823  20916  12113   1840  -3060     27       C  
ATOM    215  CZ2 TRP A  55       3.375  45.865  27.813  1.00111.73           C  
ANISOU  215  CZ2 TRP A  55    12267  20090  10095   2468  -3014    -72       C  
ATOM    216  CZ3 TRP A  55       3.635  46.828  30.015  1.00119.04           C  
ANISOU  216  CZ3 TRP A  55    13544  20612  11071   1977  -3198     78       C  
ATOM    217  CH2 TRP A  55       4.176  46.276  28.853  1.00111.14           C  
ANISOU  217  CH2 TRP A  55    12159  20105   9961   2291  -3170     29       C  
ATOM    218  N   ILE A  56      -3.467  47.613  27.940  1.00156.94           N  
ANISOU  218  N   ILE A  56    19652  23307  16670   1511  -2287   -153       N  
ATOM    219  CA  ILE A  56      -4.129  47.452  26.622  1.00149.12           C  
ANISOU  219  CA  ILE A  56    18551  22371  15738   1604  -2146   -198       C  
ATOM    220  C   ILE A  56      -4.457  48.820  26.021  1.00173.56           C  
ANISOU  220  C   ILE A  56    21516  25527  18902   1247  -2047    -63       C  
ATOM    221  O   ILE A  56      -4.171  49.064  24.866  1.00358.24           O  
ANISOU  221  O   ILE A  56    44596  49261  42256   1255  -2004    -25       O  
ATOM    222  CB  ILE A  56      -5.368  46.543  26.725  1.00131.84           C  
ANISOU  222  CB  ILE A  56    16719  19723  13649   1773  -2062   -331       C  
ATOM    223  CG1 ILE A  56      -4.949  45.085  26.941  1.00113.31           C  
ANISOU  223  CG1 ILE A  56    14454  17393  11205   2174  -2178   -470       C  
ATOM    224  CG2 ILE A  56      -6.247  46.696  25.489  1.00135.15           C  
ANISOU  224  CG2 ILE A  56    17071  20120  14159   1757  -1908   -343       C  
ATOM    225  CD1 ILE A  56      -6.085  44.136  27.211  1.00104.58           C  
ANISOU  225  CD1 ILE A  56    13737  15821  10175   2309  -2136   -585       C  
ATOM    226  N   ILE A  57      -5.079  49.688  26.808  1.00138.19           N  
ANISOU  226  N   ILE A  57    17293  20701  14510    948  -2017      4       N  
ATOM    227  CA  ILE A  57      -5.540  51.005  26.318  1.00118.58           C  
ANISOU  227  CA  ILE A  57    14768  18191  12096    612  -1935    121       C  
ATOM    228  C   ILE A  57      -4.348  51.817  25.812  1.00152.70           C  
ANISOU  228  C   ILE A  57    18710  23007  16301    429  -2029    266       C  
ATOM    229  O   ILE A  57      -4.454  52.504  24.775  1.00162.92           O  
ANISOU  229  O   ILE A  57    19807  24487  17608    281  -1964    341       O  
ATOM    230  CB  ILE A  57      -6.359  51.739  27.403  1.00 89.92           C  
ANISOU  230  CB  ILE A  57    11519  14092   8553    368  -1908    155       C  
ATOM    231  CG1 ILE A  57      -7.703  51.031  27.613  1.00 81.19           C  
ANISOU  231  CG1 ILE A  57    10730  12551   7565    519  -1776     33       C  
ATOM    232  CG2 ILE A  57      -6.533  53.218  27.072  1.00 75.89           C  
ANISOU  232  CG2 ILE A  57     9707  12323   6803     11  -1886    293       C  
ATOM    233  CD1 ILE A  57      -8.577  51.621  28.698  1.00 84.51           C  
ANISOU  233  CD1 ILE A  57    11524  12528   8057    333  -1730     50       C  
ATOM    234  N   LEU A  58      -3.234  51.734  26.507  1.00155.14           N  
ANISOU  234  N   LEU A  58    18912  23541  16493    429  -2186    313       N  
ATOM    235  CA  LEU A  58      -2.086  52.614  26.194  1.00138.17           C  
ANISOU  235  CA  LEU A  58    16414  21860  14223    188  -2296    482       C  
ATOM    236  C   LEU A  58      -1.221  51.979  25.113  1.00137.91           C  
ANISOU  236  C   LEU A  58    15936  22390  14072    436  -2302    466       C  
ATOM    237  O   LEU A  58      -0.546  52.749  24.370  1.00 90.70           O  
ANISOU  237  O   LEU A  58     9615  16839   8008    228  -2329    610       O  
ATOM    238  CB  LEU A  58      -1.281  52.871  27.474  1.00140.36           C  
ANISOU  238  CB  LEU A  58    16776  22131  14423     50  -2473    555       C  
ATOM    239  CG  LEU A  58      -2.002  53.639  28.587  1.00130.15           C  
ANISOU  239  CG  LEU A  58    15917  20321  13213   -216  -2486    588       C  
ATOM    240  CD1 LEU A  58      -1.049  53.949  29.733  1.00119.82           C  
ANISOU  240  CD1 LEU A  58    14647  19073  11803   -370  -2684    678       C  
ATOM    241  CD2 LEU A  58      -2.636  54.925  28.074  1.00127.33           C  
ANISOU  241  CD2 LEU A  58    15624  19835  12919   -555  -2420    695       C  
ATOM    242  N   ALA A  59      -1.182  50.640  25.077  1.00177.03           N  
ANISOU  242  N   ALA A  59    20901  27359  19000    860  -2293    304       N  
ATOM    243  CA  ALA A  59      -0.246  49.920  24.180  1.00154.71           C  
ANISOU  243  CA  ALA A  59    17667  25087  16028   1167  -2320    269       C  
ATOM    244  C   ALA A  59      -0.715  49.933  22.724  1.00154.80           C  
ANISOU  244  C   ALA A  59    17501  25254  16062   1235  -2174    247       C  
ATOM    245  O   ALA A  59       0.106  50.200  21.819  1.00181.60           O  
ANISOU  245  O   ALA A  59    20475  29193  19331   1225  -2181    332       O  
ATOM    246  CB  ALA A  59      -0.016  48.505  24.649  1.00151.41           C  
ANISOU  246  CB  ALA A  59    17357  24615  15555   1611  -2387     99       C  
ATOM    247  N   HIS A  60      -1.990  49.581  22.531  1.00143.47           N  
ANISOU  247  N   HIS A  60    16376  23364  14773   1316  -2051    135       N  
ATOM    248  CA  HIS A  60      -2.674  49.679  21.224  1.00139.42           C  
ANISOU  248  CA  HIS A  60    15773  22885  14313   1337  -1906    115       C  
ATOM    249  C   HIS A  60      -2.492  51.098  20.679  1.00151.95           C  
ANISOU  249  C   HIS A  60    17148  24688  15896    923  -1882    303       C  
ATOM    250  O   HIS A  60      -2.398  52.055  21.507  1.00126.11           O  
ANISOU  250  O   HIS A  60    13990  21273  12649    579  -1950    423       O  
ATOM    251  CB  HIS A  60      -4.177  49.315  21.266  1.00166.76           C  
ANISOU  251  CB  HIS A  60    19632  25776  17952   1387  -1788      2       C  
ATOM    252  CG  HIS A  60      -4.538  47.924  20.811  1.00170.36           C  
ANISOU  252  CG  HIS A  60    20178  26152  18398   1811  -1761   -174       C  
ATOM    253  ND1 HIS A  60      -4.624  47.557  19.464  1.00121.80           N  
ANISOU  253  ND1 HIS A  60    13832  20236  12209   2002  -1687   -224       N  
ATOM    254  CD2 HIS A  60      -4.917  46.825  21.510  1.00162.14           C  
ANISOU  254  CD2 HIS A  60    19442  24786  17378   2065  -1804   -311       C  
ATOM    255  CE1 HIS A  60      -4.993  46.292  19.363  1.00 91.94           C  
ANISOU  255  CE1 HIS A  60    10233  16280   8418   2362  -1700   -385       C  
ATOM    256  NE2 HIS A  60      -5.180  45.817  20.605  1.00107.94           N  
ANISOU  256  NE2 HIS A  60    12569  17960  10480   2400  -1775   -438       N  
ATOM    257  N   LYS A  61      -2.427  51.165  19.348  1.00162.20           N  
ANISOU  257  N   LYS A  61    18168  26309  17148    974  -1801    320       N  
ATOM    258  CA  LYS A  61      -1.929  52.307  18.545  1.00139.82           C  
ANISOU  258  CA  LYS A  61    15016  23865  14244    649  -1797    501       C  
ATOM    259  C   LYS A  61      -2.834  53.485  18.898  1.00129.51           C  
ANISOU  259  C   LYS A  61    13999  22122  13084    240  -1766    593       C  
ATOM    260  O   LYS A  61      -2.354  54.435  19.530  1.00132.08           O  
ANISOU  260  O   LYS A  61    14326  22483  13375    -96  -1872    741       O  
ATOM    261  CB  LYS A  61      -1.930  51.957  17.051  1.00134.53           C  
ANISOU  261  CB  LYS A  61    14071  23531  13512    844  -1693    463       C  
ATOM    262  CG  LYS A  61      -1.185  52.929  16.146  1.00130.71           C  
ANISOU  262  CG  LYS A  61    13186  23571  12904    565  -1700    650       C  
ATOM    263  CD  LYS A  61       0.320  52.791  16.219  1.00123.54           C  
ANISOU  263  CD  LYS A  61    11863  23294  11780    629  -1812    736       C  
ATOM    264  CE  LYS A  61       1.034  53.573  15.139  1.00119.46           C  
ANISOU  264  CE  LYS A  61    10910  23360  11117    399  -1800    913       C  
ATOM    265  NZ  LYS A  61       2.493  53.316  15.153  1.00109.55           N  
ANISOU  265  NZ  LYS A  61     9210  22778   9636    508  -1896    990       N  
ATOM    266  N   ARG A  62      -4.125  53.379  18.606  1.00123.19           N  
ANISOU  266  N   ARG A  62    13469  20895  12440    284  -1640    501       N  
ATOM    267  CA  ARG A  62      -5.093  54.360  19.143  1.00113.46           C  
ANISOU  267  CA  ARG A  62    12572  19186  11349    -31  -1613    556       C  
ATOM    268  C   ARG A  62      -6.303  53.647  19.736  1.00 89.67           C  
ANISOU  268  C   ARG A  62     9949  15632   8488    160  -1528    399       C  
ATOM    269  O   ARG A  62      -7.260  53.339  18.983  1.00 51.05           O  
ANISOU  269  O   ARG A  62     5130  10572   3694    274  -1404    321       O  
ATOM    270  CB  ARG A  62      -5.515  55.354  18.058  1.00153.11           C  
ANISOU  270  CB  ARG A  62    17500  24271  16403   -284  -1544    656       C  
ATOM    271  CG  ARG A  62      -6.364  56.503  18.579  1.00149.31           C  
ANISOU  271  CG  ARG A  62    17343  23354  16034   -614  -1542    727       C  
ATOM    272  CD  ARG A  62      -5.621  57.363  19.584  1.00123.48           C  
ANISOU  272  CD  ARG A  62    14129  20101  12685   -914  -1702    863       C  
ATOM    273  NE  ARG A  62      -6.153  58.718  19.605  1.00143.34           N  
ANISOU  273  NE  ARG A  62    16845  22371  15245  -1278  -1727    977       N  
ATOM    274  CZ  ARG A  62      -7.327  59.075  20.123  1.00150.92           C  
ANISOU  274  CZ  ARG A  62    18190  22813  16339  -1317  -1666    920       C  
ATOM    275  NH1 ARG A  62      -8.117  58.179  20.692  1.00144.50           N  
ANISOU  275  NH1 ARG A  62    17597  21675  15631  -1043  -1569    762       N  
ATOM    276  NH2 ARG A  62      -7.706  60.341  20.077  1.00157.98           N  
ANISOU  276  NH2 ARG A  62    19255  23523  17247  -1630  -1709   1026       N  
ATOM    277  N   MET A  63      -6.266  53.437  21.050  1.00 82.36           N  
ANISOU  277  N   MET A  63     9264  14451   7577    169  -1597    369       N  
ATOM    278  CA  MET A  63      -7.459  53.124  21.854  1.00 95.03           C  
ANISOU  278  CA  MET A  63    11279  15508   9321    225  -1527    270       C  
ATOM    279  C   MET A  63      -7.749  54.283  22.789  1.00 81.25           C  
ANISOU  279  C   MET A  63     9778  13476   7616   -102  -1564    367       C  
ATOM    280  O   MET A  63      -8.662  54.162  23.570  1.00 54.05           O  
ANISOU  280  O   MET A  63     6663   9608   4265    -83  -1510    304       O  
ATOM    281  CB  MET A  63      -7.250  51.811  22.620  1.00 87.14           C  
ANISOU  281  CB  MET A  63    10396  14421   8290    540  -1575    142       C  
ATOM    282  CG  MET A  63      -7.185  50.589  21.711  1.00 93.05           C  
ANISOU  282  CG  MET A  63    10996  15356   9003    902  -1541     21       C  
ATOM    283  SD  MET A  63      -7.945  49.087  22.395  1.00 65.10           S  
ANISOU  283  SD  MET A  63     7806  11411   5518   1232  -1531   -158       S  
ATOM    284  CE  MET A  63      -9.673  49.573  22.437  1.00 54.06           C  
ANISOU  284  CE  MET A  63     6724   9504   4313   1044  -1372   -160       C  
ATOM    285  N   ARG A  64      -7.094  55.417  22.575  1.00 89.36           N  
ANISOU  285  N   ARG A  64    10652  14729   8572   -402  -1646    520       N  
ATOM    286  CA  ARG A  64      -6.929  56.465  23.607  1.00 94.66           C  
ANISOU  286  CA  ARG A  64    11532  15212   9220   -707  -1753    626       C  
ATOM    287  C   ARG A  64      -8.163  57.345  23.742  1.00 65.97           C  
ANISOU  287  C   ARG A  64     8219  11143   5702   -879  -1671    634       C  
ATOM    288  O   ARG A  64      -8.071  58.410  24.379  1.00 58.55           O  
ANISOU  288  O   ARG A  64     7459  10056   4731  -1155  -1765    734       O  
ATOM    289  CB  ARG A  64      -5.686  57.287  23.253  1.00119.47           C  
ANISOU  289  CB  ARG A  64    14376  18796  12221   -971  -1898    800       C  
ATOM    290  CG  ARG A  64      -4.420  56.453  23.110  1.00136.47           C  
ANISOU  290  CG  ARG A  64    16173  21437  14242   -786  -1979    799       C  
ATOM    291  CD  ARG A  64      -3.161  57.277  23.308  1.00141.43           C  
ANISOU  291  CD  ARG A  64    16582  22433  14720  -1087  -2159    985       C  
ATOM    292  NE  ARG A  64      -1.923  56.530  23.094  1.00137.60           N  
ANISOU  292  NE  ARG A  64    15707  22479  14095   -903  -2233    996       N  
ATOM    293  CZ  ARG A  64      -1.276  56.410  21.932  1.00127.85           C  
ANISOU  293  CZ  ARG A  64    14049  21766  12760   -852  -2210   1048       C  
ATOM    294  NH1 ARG A  64      -1.745  56.973  20.829  1.00123.43           N  
ANISOU  294  NH1 ARG A  64    13402  21263  12232   -983  -2118   1096       N  
ATOM    295  NH2 ARG A  64      -0.149  55.719  21.879  1.00109.24           N  
ANISOU  295  NH2 ARG A  64    11353  19888  10262   -655  -2283   1050       N  
ATOM    296  N   THR A  65      -9.286  56.904  23.203  1.00 58.67           N  
ANISOU  296  N   THR A  65     7380  10014   4897   -713  -1512    532       N  
ATOM    297  CA  THR A  65     -10.548  57.673  23.334  1.00 64.09           C  
ANISOU  297  CA  THR A  65     8362  10294   5693   -833  -1421    527       C  
ATOM    298  C   THR A  65     -10.864  58.029  24.784  1.00 60.85           C  
ANISOU  298  C   THR A  65     8315   9517   5286   -910  -1462    521       C  
ATOM    299  O   THR A  65     -10.585  57.211  25.658  1.00 70.87           O  
ANISOU  299  O   THR A  65     9662  10733   6530   -760  -1491    457       O  
ATOM    300  CB  THR A  65     -11.738  56.939  22.698  1.00 68.39           C  
ANISOU  300  CB  THR A  65     8949  10669   6367   -610  -1246    409       C  
ATOM    301  OG1 THR A  65     -12.910  57.740  22.850  1.00 73.95           O  
ANISOU  301  OG1 THR A  65     9912  11019   7163   -723  -1164    413       O  
ATOM    302  CG2 THR A  65     -12.017  55.581  23.295  1.00 59.71           C  
ANISOU  302  CG2 THR A  65     7953   9434   5300   -324  -1198    277       C  
ATOM    303  N   VAL A  66     -11.509  59.179  24.978  1.00 59.18           N  
ANISOU  303  N   VAL A  66     8335   9047   5101  -1111  -1459    575       N  
ATOM    304  CA  VAL A  66     -11.716  59.770  26.313  1.00 89.79           C  
ANISOU  304  CA  VAL A  66    12569  12596   8949  -1218  -1520    588       C  
ATOM    305  C   VAL A  66     -12.444  58.775  27.203  1.00 94.32           C  
ANISOU  305  C   VAL A  66    13350  12902   9585   -975  -1412    458       C  
ATOM    306  O   VAL A  66     -12.103  58.685  28.385  1.00106.99           O  
ANISOU  306  O   VAL A  66    15142  14379  11130   -985  -1489    453       O  
ATOM    307  CB  VAL A  66     -12.477  61.107  26.223  1.00106.00           C  
ANISOU  307  CB  VAL A  66    14856  14397  11022  -1414  -1516    644       C  
ATOM    308  CG1 VAL A  66     -11.733  62.117  25.365  1.00117.61           C  
ANISOU  308  CG1 VAL A  66    16149  16121  12415  -1690  -1647    788       C  
ATOM    309  CG2 VAL A  66     -13.899  60.926  25.725  1.00 99.45           C  
ANISOU  309  CG2 VAL A  66    14111  13349  10325  -1256  -1321    552       C  
ATOM    310  N   THR A  67     -13.339  57.985  26.624  1.00 78.61           N  
ANISOU  310  N   THR A  67    11313  10853   7701   -771  -1251    363       N  
ATOM    311  CA  THR A  67     -14.048  56.927  27.376  1.00 80.37           C  
ANISOU  311  CA  THR A  67    11714  10846   7976   -553  -1152    250       C  
ATOM    312  C   THR A  67     -13.048  55.982  28.022  1.00 78.01           C  
ANISOU  312  C   THR A  67    11358  10684   7598   -440  -1258    220       C  
ATOM    313  O   THR A  67     -13.094  55.765  29.233  1.00 81.64           O  
ANISOU  313  O   THR A  67    12058  10937   8024   -416  -1285    193       O  
ATOM    314  CB  THR A  67     -15.014  56.135  26.487  1.00 93.19           C  
ANISOU  314  CB  THR A  67    13249  12447   9712   -371   -995    169       C  
ATOM    315  OG1 THR A  67     -15.800  57.052  25.727  1.00 79.81           O  
ANISOU  315  OG1 THR A  67    11555  10685   8085   -478   -916    206       O  
ATOM    316  CG2 THR A  67     -15.921  55.234  27.298  1.00106.26           C  
ANISOU  316  CG2 THR A  67    15130  13828  11416   -207   -894     78       C  
ATOM    317  N   ASN A  68     -12.123  55.491  27.222  1.00 81.90           N  
ANISOU  317  N   ASN A  68    11535  11535   8047   -372  -1323    231       N  
ATOM    318  CA  ASN A  68     -11.065  54.577  27.683  1.00 94.27           C  
ANISOU  318  CA  ASN A  68    13000  13292   9524   -234  -1438    201       C  
ATOM    319  C   ASN A  68     -10.101  55.232  28.647  1.00 90.95           C  
ANISOU  319  C   ASN A  68    12643  12915   8997   -415  -1601    288       C  
ATOM    320  O   ASN A  68      -9.617  54.508  29.550  1.00 78.57           O  
ANISOU  320  O   ASN A  68    11160  11318   7374   -299  -1679    244       O  
ATOM    321  CB  ASN A  68     -10.308  53.999  26.483  1.00 89.39           C  
ANISOU  321  CB  ASN A  68    12006  13090   8869   -102  -1464    195       C  
ATOM    322  CG  ASN A  68     -11.159  53.076  25.637  1.00 72.97           C  
ANISOU  322  CG  ASN A  68     9892  10956   6876    123  -1331     91       C  
ATOM    323  OD1 ASN A  68     -12.386  53.077  25.743  1.00 71.24           O  
ANISOU  323  OD1 ASN A  68     9885  10420   6760    127  -1208     49       O  
ATOM    324  ND2 ASN A  68     -10.520  52.289  24.787  1.00 66.00           N  
ANISOU  324  ND2 ASN A  68     8742  10393   5942    316  -1360     51       N  
ATOM    325  N   TYR A  69      -9.834  56.536  28.516  1.00 79.86           N  
ANISOU  325  N   TYR A  69    11227  11558   7557   -693  -1669    408       N  
ATOM    326  CA  TYR A  69      -9.035  57.311  29.483  1.00 80.70           C  
ANISOU  326  CA  TYR A  69    11452  11649   7559   -912  -1840    505       C  
ATOM    327  C   TYR A  69      -9.655  57.307  30.877  1.00 82.69           C  
ANISOU  327  C   TYR A  69    12115  11483   7820   -892  -1824    451       C  
ATOM    328  O   TYR A  69      -8.978  56.961  31.919  1.00 95.09           O  
ANISOU  328  O   TYR A  69    13782  13034   9312   -874  -1942    449       O  
ATOM    329  CB  TYR A  69      -8.886  58.769  29.042  1.00 72.06           C  
ANISOU  329  CB  TYR A  69    10346  10603   6429  -1231  -1913    642       C  
ATOM    330  CG  TYR A  69      -7.734  59.053  28.112  1.00 77.86           C  
ANISOU  330  CG  TYR A  69    10690  11814   7078  -1370  -2025    759       C  
ATOM    331  CD1 TYR A  69      -6.554  58.321  28.155  1.00 76.57           C  
ANISOU  331  CD1 TYR A  69    10247  12018   6826  -1277  -2125    773       C  
ATOM    332  CD2 TYR A  69      -7.815  60.096  27.205  1.00103.12           C  
ANISOU  332  CD2 TYR A  69    13801  15109  10272  -1603  -2039    864       C  
ATOM    333  CE1 TYR A  69      -5.497  58.607  27.304  1.00 97.14           C  
ANISOU  333  CE1 TYR A  69    12468  15105   9336  -1407  -2220    892       C  
ATOM    334  CE2 TYR A  69      -6.766  60.397  26.352  1.00131.55           C  
ANISOU  334  CE2 TYR A  69    17036  19168  13779  -1759  -2140    989       C  
ATOM    335  CZ  TYR A  69      -5.603  59.651  26.400  1.00124.08           C  
ANISOU  335  CZ  TYR A  69    15788  18615  12740  -1661  -2225   1005       C  
ATOM    336  OH  TYR A  69      -4.578  59.949  25.546  1.00106.16           O  
ANISOU  336  OH  TYR A  69    13131  16841  10364  -1811  -2313   1136       O  
ATOM    337  N   PHE A  70     -10.981  57.511  30.931  1.00 71.94           N  
ANISOU  337  N   PHE A  70    10988   9795   6550   -854  -1668    394       N  
ATOM    338  CA  PHE A  70     -11.705  57.434  32.204  1.00 71.80           C  
ANISOU  338  CA  PHE A  70    11348   9397   6535   -805  -1619    335       C  
ATOM    339  C   PHE A  70     -11.693  56.003  32.731  1.00 76.23           C  
ANISOU  339  C   PHE A  70    11929   9930   7103   -563  -1587    234       C  
ATOM    340  O   PHE A  70     -11.702  55.781  33.962  1.00 92.90           O  
ANISOU  340  O   PHE A  70    14300  11832   9165   -540  -1624    207       O  
ATOM    341  CB  PHE A  70     -13.139  57.940  32.035  1.00 61.44           C  
ANISOU  341  CB  PHE A  70    10232   7802   5310   -796  -1448    300       C  
ATOM    342  CG  PHE A  70     -13.264  59.413  31.744  1.00 57.49           C  
ANISOU  342  CG  PHE A  70     9816   7240   4785  -1022  -1497    389       C  
ATOM    343  CD1 PHE A  70     -12.612  60.348  32.528  1.00 54.92           C  
ANISOU  343  CD1 PHE A  70     9678   6840   4346  -1226  -1668    472       C  
ATOM    344  CD2 PHE A  70     -14.063  59.865  30.707  1.00 65.08           C  
ANISOU  344  CD2 PHE A  70    10700   8196   5829  -1031  -1386    391       C  
ATOM    345  CE1 PHE A  70     -12.723  61.703  32.260  1.00 64.51           C  
ANISOU  345  CE1 PHE A  70    11012   7974   5524  -1439  -1740    556       C  
ATOM    346  CE2 PHE A  70     -14.183  61.220  30.443  1.00 76.83           C  
ANISOU  346  CE2 PHE A  70    12298   9608   7286  -1233  -1449    470       C  
ATOM    347  CZ  PHE A  70     -13.507  62.136  31.216  1.00 80.21           C  
ANISOU  347  CZ  PHE A  70    12926   9956   7593  -1437  -1631    553       C  
ATOM    348  N   LEU A  71     -11.636  55.047  31.798  1.00 77.27           N  
ANISOU  348  N   LEU A  71    11804  10270   7284   -385  -1534    180       N  
ATOM    349  CA  LEU A  71     -11.602  53.621  32.189  1.00 73.44           C  
ANISOU  349  CA  LEU A  71    11349   9758   6797   -143  -1527     81       C  
ATOM    350  C   LEU A  71     -10.231  53.295  32.771  1.00 63.00           C  
ANISOU  350  C   LEU A  71     9944   8634   5359   -125  -1718    104       C  
ATOM    351  O   LEU A  71     -10.094  52.381  33.586  1.00 48.17           O  
ANISOU  351  O   LEU A  71     8206   6650   3445     19  -1761     39       O  
ATOM    352  CB  LEU A  71     -11.912  52.768  30.956  1.00 83.38           C  
ANISOU  352  CB  LEU A  71    12379  11176   8125     42  -1438     19       C  
ATOM    353  CG  LEU A  71     -13.328  52.205  30.892  1.00 90.19           C  
ANISOU  353  CG  LEU A  71    13414  11763   9087    150  -1267    -55       C  
ATOM    354  CD1 LEU A  71     -14.369  53.315  30.844  1.00 89.09           C  
ANISOU  354  CD1 LEU A  71    13408  11424   9018    -12  -1143    -13       C  
ATOM    355  CD2 LEU A  71     -13.458  51.275  29.698  1.00 83.30           C  
ANISOU  355  CD2 LEU A  71    12327  11060   8263    336  -1222   -115       C  
ATOM    356  N   VAL A  72      -9.224  54.037  32.327  1.00 65.30           N  
ANISOU  356  N   VAL A  72     9999   9225   5588   -281  -1838    204       N  
ATOM    357  CA  VAL A  72      -7.854  53.887  32.876  1.00 75.33           C  
ANISOU  357  CA  VAL A  72    11156  10727   6737   -299  -2034    250       C  
ATOM    358  C   VAL A  72      -7.883  54.359  34.315  1.00 72.38           C  
ANISOU  358  C   VAL A  72    11131  10055   6315   -434  -2110    276       C  
ATOM    359  O   VAL A  72      -7.374  53.647  35.188  1.00 69.60           O  
ANISOU  359  O   VAL A  72    10869   9672   5901   -324  -2205    237       O  
ATOM    360  CB  VAL A  72      -6.787  54.634  32.051  1.00 89.93           C  
ANISOU  360  CB  VAL A  72    12652  12999   8519   -472  -2146    374       C  
ATOM    361  CG1 VAL A  72      -5.462  54.704  32.796  1.00 91.76           C  
ANISOU  361  CG1 VAL A  72    12804  13437   8621   -552  -2357    448       C  
ATOM    362  CG2 VAL A  72      -6.587  54.017  30.673  1.00 91.37           C  
ANISOU  362  CG2 VAL A  72    12468  13528   8720   -297  -2083    341       C  
ATOM    363  N   ASN A  73      -8.460  55.523  34.551  1.00 83.50           N  
ANISOU  363  N   ASN A  73    12744  11243   7739   -652  -2077    336       N  
ATOM    364  CA  ASN A  73      -8.555  56.099  35.902  1.00 90.18           C  
ANISOU  364  CA  ASN A  73    13956  11784   8524   -783  -2148    361       C  
ATOM    365  C   ASN A  73      -9.436  55.204  36.773  1.00 94.18           C  
ANISOU  365  C   ASN A  73    14750  11968   9063   -587  -2032    244       C  
ATOM    366  O   ASN A  73      -9.196  55.081  37.987  1.00167.31           O  
ANISOU  366  O   ASN A  73    24258  21058  18252   -597  -2116    236       O  
ATOM    367  CB  ASN A  73      -9.093  57.533  35.832  1.00 89.68           C  
ANISOU  367  CB  ASN A  73    14065  11545   8463  -1021  -2130    436       C  
ATOM    368  CG  ASN A  73      -9.055  58.269  37.153  1.00104.66           C  
ANISOU  368  CG  ASN A  73    16341  13154  10270  -1168  -2234    473       C  
ATOM    369  OD1 ASN A  73      -8.280  57.925  38.040  1.00126.81           O  
ANISOU  369  OD1 ASN A  73    19213  15975  12993  -1170  -2373    483       O  
ATOM    370  ND2 ASN A  73      -9.886  59.290  37.292  1.00 94.36           N  
ANISOU  370  ND2 ASN A  73    15297  11584   8970  -1280  -2177    490       N  
ATOM    371  N   LEU A  74     -10.457  54.623  36.159  1.00 60.00           N  
ANISOU  371  N   LEU A  74    10397   7562   4837   -432  -1848    165       N  
ATOM    372  CA  LEU A  74     -11.323  53.670  36.866  1.00 50.40           C  
ANISOU  372  CA  LEU A  74     9422   6078   3648   -259  -1736     67       C  
ATOM    373  C   LEU A  74     -10.491  52.483  37.327  1.00 63.28           C  
ANISOU  373  C   LEU A  74    11013   7809   5219    -96  -1859     18       C  
ATOM    374  O   LEU A  74     -10.488  52.165  38.515  1.00 85.79           O  
ANISOU  374  O   LEU A  74    14131  10454   8010    -76  -1905     -5       O  
ATOM    375  CB  LEU A  74     -12.463  53.220  35.958  1.00 44.20           C  
ANISOU  375  CB  LEU A  74     8564   5250   2980   -140  -1542      9       C  
ATOM    376  CG  LEU A  74     -13.259  52.029  36.474  1.00 39.79           C  
ANISOU  376  CG  LEU A  74     8187   4484   2444     34  -1447    -79       C  
ATOM    377  CD1 LEU A  74     -14.008  52.397  37.740  1.00 36.20           C  
ANISOU  377  CD1 LEU A  74     8098   3704   1952    -32  -1380    -79       C  
ATOM    378  CD2 LEU A  74     -14.207  51.527  35.401  1.00 45.22           C  
ANISOU  378  CD2 LEU A  74     8746   5191   3241    137  -1291   -122       C  
ATOM    379  N   ALA A  75      -9.782  51.873  36.390  1.00 67.23           N  
ANISOU  379  N   ALA A  75    11191   8628   5724     25  -1916      4       N  
ATOM    380  CA  ALA A  75      -8.918  50.713  36.673  1.00 79.67           C  
ANISOU  380  CA  ALA A  75    12697  10340   7231    222  -2048    -50       C  
ATOM    381  C   ALA A  75      -7.885  51.077  37.740  1.00111.29           C  
ANISOU  381  C   ALA A  75    16787  14373  11125    115  -2237      7       C  
ATOM    382  O   ALA A  75      -7.565  50.225  38.597  1.00142.76           O  
ANISOU  382  O   ALA A  75    20924  18266  15049    246  -2326    -46       O  
ATOM    383  CB  ALA A  75      -8.262  50.243  35.390  1.00 68.21           C  
ANISOU  383  CB  ALA A  75    10858   9275   5783    365  -2081    -63       C  
ATOM    384  N   PHE A  76      -7.405  52.315  37.685  1.00102.72           N  
ANISOU  384  N   PHE A  76    15624  13395  10007   -128  -2306    117       N  
ATOM    385  CA  PHE A  76      -6.397  52.807  38.636  1.00110.81           C  
ANISOU  385  CA  PHE A  76    16720  14460  10922   -276  -2503    194       C  
ATOM    386  C   PHE A  76      -6.982  52.914  40.033  1.00 98.60           C  
ANISOU  386  C   PHE A  76    15618  12498   9345   -324  -2492    168       C  
ATOM    387  O   PHE A  76      -6.315  52.443  40.913  1.00123.12           O  
ANISOU  387  O   PHE A  76    18820  15588  12371   -276  -2631    158       O  
ATOM    388  CB  PHE A  76      -5.794  54.132  38.159  1.00127.78           C  
ANISOU  388  CB  PHE A  76    18693  16819  13037   -556  -2593    333       C  
ATOM    389  CG  PHE A  76      -4.582  54.606  38.925  1.00104.06           C  
ANISOU  389  CG  PHE A  76    15682  13944   9910   -727  -2828    434       C  
ATOM    390  CD1 PHE A  76      -3.312  54.138  38.621  1.00 89.78           C  
ANISOU  390  CD1 PHE A  76    13528  12553   8029   -661  -2981    471       C  
ATOM    391  CD2 PHE A  76      -4.712  55.537  39.942  1.00 83.44           C  
ANISOU  391  CD2 PHE A  76    13409  11048   7245   -948  -2902    494       C  
ATOM    392  CE1 PHE A  76      -2.200  54.597  39.310  1.00 83.84           C  
ANISOU  392  CE1 PHE A  76    12749  11942   7162   -837  -3205    578       C  
ATOM    393  CE2 PHE A  76      -3.599  56.002  40.625  1.00 79.73           C  
ANISOU  393  CE2 PHE A  76    12941  10692   6659  -1129  -3135    597       C  
ATOM    394  CZ  PHE A  76      -2.347  55.525  40.314  1.00 84.22           C  
ANISOU  394  CZ  PHE A  76    13146  11686   7165  -1082  -3287    644       C  
ATOM    395  N   ALA A  77      -8.034  53.696  40.177  1.00 87.35           N  
ANISOU  395  N   ALA A  77    14422  10800   7965   -441  -2355    177       N  
ATOM    396  CA  ALA A  77      -8.670  53.936  41.486  1.00124.45           C  
ANISOU  396  CA  ALA A  77    19550  15114  12618   -489  -2324    156       C  
ATOM    397  C   ALA A  77      -9.340  52.681  42.035  1.00119.83           C  
ANISOU  397  C   ALA A  77    19144  14334  12052   -274  -2225     49       C  
ATOM    398  O   ALA A  77      -9.155  52.382  43.227  1.00120.92           O  
ANISOU  398  O   ALA A  77    19544  14292  12107   -262  -2303     32       O  
ATOM    399  CB  ALA A  77      -9.618  55.103  41.386  1.00165.20           C  
ANISOU  399  CB  ALA A  77    24882  20075  17811   -635  -2202    188       C  
ATOM    400  N   GLU A  78      -9.998  51.919  41.171  1.00135.26           N  
ANISOU  400  N   GLU A  78    20954  16339  14098   -117  -2083    -14       N  
ATOM    401  CA  GLU A  78     -10.869  50.825  41.644  1.00164.82           C  
ANISOU  401  CA  GLU A  78    24905  19859  17860     42  -1972   -100       C  
ATOM    402  C   GLU A  78     -10.075  49.635  42.178  1.00154.12           C  
ANISOU  402  C   GLU A  78    23578  18546  16434    199  -2127   -150       C  
ATOM    403  O   GLU A  78     -10.416  49.107  43.238  1.00170.27           O  
ANISOU  403  O   GLU A  78    25923  20345  18425    235  -2126   -184       O  
ATOM    404  CB  GLU A  78     -11.800  50.377  40.527  1.00155.22           C  
ANISOU  404  CB  GLU A  78    23536  18681  16757    143  -1798   -143       C  
ATOM    405  CG  GLU A  78     -12.707  49.218  40.874  1.00147.26           C  
ANISOU  405  CG  GLU A  78    22716  17469  15765    281  -1698   -215       C  
ATOM    406  CD  GLU A  78     -13.503  48.761  39.665  1.00122.60           C  
ANISOU  406  CD  GLU A  78    19414  14416  12751    370  -1559   -247       C  
ATOM    407  OE1 GLU A  78     -13.223  49.255  38.556  1.00122.92           O  
ANISOU  407  OE1 GLU A  78    19173  14682  12850    350  -1553   -223       O  
ATOM    408  OE2 GLU A  78     -14.393  47.921  39.827  1.00114.76           O  
ANISOU  408  OE2 GLU A  78    18567  13258  11778    444  -1466   -288       O  
ATOM    409  N   ALA A  79      -9.023  49.228  41.471  1.00119.77           N  
ANISOU  409  N   ALA A  79    18923  14512  12073    298  -2261   -153       N  
ATOM    410  CA  ALA A  79      -8.301  47.984  41.786  1.00123.65           C  
ANISOU  410  CA  ALA A  79    19413  15070  12498    506  -2409   -217       C  
ATOM    411  C   ALA A  79      -6.848  48.268  42.160  1.00160.70           C  
ANISOU  411  C   ALA A  79    23970  19994  17093    469  -2634   -164       C  
ATOM    412  O   ALA A  79      -6.397  47.853  43.251  1.00189.18           O  
ANISOU  412  O   ALA A  79    27786  23479  20613    503  -2767   -180       O  
ATOM    413  CB  ALA A  79      -8.387  47.075  40.594  1.00110.56           C  
ANISOU  413  CB  ALA A  79    17518  13593  10894    717  -2371   -283       C  
ATOM    414  N   SER A  80      -6.132  48.917  41.246  1.00156.48           N  
ANISOU  414  N   SER A  80    23082  19803  16568    400  -2681    -99       N  
ATOM    415  CA  SER A  80      -4.701  49.212  41.450  1.00155.67           C  
ANISOU  415  CA  SER A  80    22780  19997  16370    348  -2898    -29       C  
ATOM    416  C   SER A  80      -4.502  49.819  42.833  1.00128.41           C  
ANISOU  416  C   SER A  80    19637  16310  12843    160  -3003     25       C  
ATOM    417  O   SER A  80      -3.438  49.586  43.376  1.00 91.94           O  
ANISOU  417  O   SER A  80    14968  11834   8131    188  -3200     47       O  
ATOM    418  CB  SER A  80      -4.134  50.100  40.368  1.00138.28           C  
ANISOU  418  CB  SER A  80    20194  18164  14181    210  -2912     66       C  
ATOM    419  OG  SER A  80      -2.891  50.668  40.772  1.00 90.93           O  
ANISOU  419  OG  SER A  80    14060  12404   8083     63  -3119    169       O  
ATOM    420  N   MET A  81      -5.467  50.557  43.353  1.00111.41           N  
ANISOU  420  N   MET A  81    17784  13826  10719     -6  -2881     43       N  
ATOM    421  CA  MET A  81      -5.265  51.242  44.633  1.00 92.39           C  
ANISOU  421  CA  MET A  81    15684  11196   8224   -188  -2986     98       C  
ATOM    422  C   MET A  81      -6.166  50.657  45.708  1.00 80.75           C  
ANISOU  422  C   MET A  81    14625   9322   6732   -107  -2896     20       C  
ATOM    423  O   MET A  81      -5.707  50.206  46.696  1.00108.27           O  
ANISOU  423  O   MET A  81    18296  12706  10133    -68  -3026      4       O  
ATOM    424  CB  MET A  81      -5.541  52.736  44.466  1.00102.52           C  
ANISOU  424  CB  MET A  81    17009  12424   9517   -460  -2949    195       C  
ATOM    425  CG  MET A  81      -4.416  53.461  43.742  1.00117.24           C  
ANISOU  425  CG  MET A  81    18522  14672  11352   -620  -3105    310       C  
ATOM    426  SD  MET A  81      -2.796  53.262  44.546  1.00120.53           S  
ANISOU  426  SD  MET A  81    18852  15308  11632   -663  -3413    378       S  
ATOM    427  CE  MET A  81      -1.800  54.458  43.655  1.00 94.59           C  
ANISOU  427  CE  MET A  81    15190  12436   8311   -948  -3554    549       C  
ATOM    428  N   ALA A  82      -7.458  50.708  45.488  1.00 73.80           N  
ANISOU  428  N   ALA A  82    13879   8233   5925    -93  -2674    -19       N  
ATOM    429  CA  ALA A  82      -8.459  50.256  46.474  1.00 74.54           C  
ANISOU  429  CA  ALA A  82    14358   7966   5994    -46  -2559    -77       C  
ATOM    430  C   ALA A  82      -8.219  48.814  46.891  1.00 87.82           C  
ANISOU  430  C   ALA A  82    16115   9613   7639    154  -2636   -152       C  
ATOM    431  O   ALA A  82      -8.127  48.572  48.101  1.00179.68           O  
ANISOU  431  O   ALA A  82    28052  21037  19180    142  -2711   -162       O  
ATOM    432  CB  ALA A  82      -9.866  50.468  45.970  1.00 75.51           C  
ANISOU  432  CB  ALA A  82    14531   7951   6208    -47  -2304   -100       C  
ATOM    433  N   ALA A  83      -8.206  47.851  45.970  1.00100.63           N  
ANISOU  433  N   ALA A  83    17515  11397   9320    340  -2617   -210       N  
ATOM    434  CA  ALA A  83      -8.047  46.444  46.385  1.00103.35           C  
ANISOU  434  CA  ALA A  83    17986  11666   9615    542  -2707   -287       C  
ATOM    435  C   ALA A  83      -6.846  46.241  47.304  1.00 87.10           C  
ANISOU  435  C   ALA A  83    16003   9647   7441    567  -2951   -278       C  
ATOM    436  O   ALA A  83      -6.993  45.757  48.490  1.00 95.00           O  
ANISOU  436  O   ALA A  83    17350  10384   8359    576  -3004   -301       O  
ATOM    437  CB  ALA A  83      -7.961  45.532  45.188  1.00126.24           C  
ANISOU  437  CB  ALA A  83    20618  14773  12572    752  -2703   -348       C  
ATOM    438  N   PHE A  84      -5.691  46.673  46.799  1.00 88.11           N  
ANISOU  438  N   PHE A  84    15813  10106   7555    555  -3096   -232       N  
ATOM    439  CA  PHE A  84      -4.378  46.510  47.471  1.00131.43           C  
ANISOU  439  CA  PHE A  84    21273  15727  12935    588  -3351   -211       C  
ATOM    440  C   PHE A  84      -4.385  47.201  48.833  1.00130.54           C  
ANISOU  440  C   PHE A  84    21504  15349  12744    386  -3408   -157       C  
ATOM    441  O   PHE A  84      -3.892  46.585  49.806  1.00109.36           O  
ANISOU  441  O   PHE A  84    19023  12558   9968    459  -3565   -183       O  
ATOM    442  CB  PHE A  84      -3.259  47.072  46.594  1.00144.62           C  
ANISOU  442  CB  PHE A  84    22500  17840  14605    556  -3464   -142       C  
ATOM    443  CG  PHE A  84      -1.884  47.034  47.210  1.00150.43           C  
ANISOU  443  CG  PHE A  84    23153  18772  15231    564  -3726   -100       C  
ATOM    444  CD1 PHE A  84      -1.139  45.864  47.202  1.00168.61           C  
ANISOU  444  CD1 PHE A  84    25356  21235  17473    846  -3878   -173       C  
ATOM    445  CD2 PHE A  84      -1.334  48.167  47.794  1.00102.30           C  
ANISOU  445  CD2 PHE A  84    17086  12698   9082    295  -3835     15       C  
ATOM    446  CE1 PHE A  84       0.126  45.828  47.770  1.00177.68           C  
ANISOU  446  CE1 PHE A  84    26409  22584  18516    864  -4123   -132       C  
ATOM    447  CE2 PHE A  84      -0.068  48.131  48.357  1.00114.80           C  
ANISOU  447  CE2 PHE A  84    18579  14476  10563    288  -4086     65       C  
ATOM    448  CZ  PHE A  84       0.658  46.961  48.346  1.00152.24           C  
ANISOU  448  CZ  PHE A  84    23195  19397  15250    576  -4224     -7       C  
ATOM    449  N   ASN A  85      -4.949  48.414  48.940  1.00109.98           N  
ANISOU  449  N   ASN A  85    18998  12623  10165    155  -3294    -90       N  
ATOM    450  CA  ASN A  85      -4.941  49.015  50.310  1.00100.44           C  
ANISOU  450  CA  ASN A  85    18162  11141   8859     -9  -3364    -49       C  
ATOM    451  C   ASN A  85      -5.991  48.393  51.251  1.00 93.56           C  
ANISOU  451  C   ASN A  85    17704   9889   7954     50  -3239   -116       C  
ATOM    452  O   ASN A  85      -5.694  48.159  52.473  1.00120.37           O  
ANISOU  452  O   ASN A  85    21398  13094  11240     35  -3361   -120       O  
ATOM    453  CB  ASN A  85      -5.177  50.521  50.196  1.00107.08           C  
ANISOU  453  CB  ASN A  85    19023  11950   9710   -259  -3309     38       C  
ATOM    454  CG  ASN A  85      -5.403  51.203  51.526  1.00148.94           C  
ANISOU  454  CG  ASN A  85    24752  16930  14908   -412  -3345     68       C  
ATOM    455  OD1 ASN A  85      -6.248  52.089  51.637  1.00173.09           O  
ANISOU  455  OD1 ASN A  85    27995  19800  17971   -528  -3205     86       O  
ATOM    456  ND2 ASN A  85      -4.645  50.810  52.536  1.00266.73           N  
ANISOU  456  ND2 ASN A  85    39835  31786  29723   -400  -3539     71       N  
ATOM    457  N   THR A  86      -7.210  48.210  50.770  1.00103.65           N  
ANISOU  457  N   THR A  86    19015  11054   9310     91  -3003   -156       N  
ATOM    458  CA  THR A  86      -8.372  47.893  51.628  1.00121.73           C  
ANISOU  458  CA  THR A  86    21682  13006  11561     90  -2845   -191       C  
ATOM    459  C   THR A  86      -8.357  46.471  52.245  1.00100.71           C  
ANISOU  459  C   THR A  86    19210  10214   8838    246  -2919   -256       C  
ATOM    460  O   THR A  86      -8.679  46.290  53.446  1.00135.76           O  
ANISOU  460  O   THR A  86    24014  14391  13176    205  -2921   -260       O  
ATOM    461  CB  THR A  86      -9.656  48.181  50.840  1.00195.92           C  
ANISOU  461  CB  THR A  86    31009  22370  21060     76  -2576   -200       C  
ATOM    462  OG1 THR A  86      -9.502  49.424  50.151  1.00245.91           O  
ANISOU  462  OG1 THR A  86    37142  28846  27444    -49  -2550   -143       O  
ATOM    463  CG2 THR A  86     -10.895  48.235  51.706  1.00216.07           C  
ANISOU  463  CG2 THR A  86    33914  24622  23560     30  -2389   -209       C  
ATOM    464  N   VAL A  87      -8.176  45.483  51.374  1.00 88.33           N  
ANISOU  464  N   VAL A  87    17422   8807   7329    423  -2951   -307       N  
ATOM    465  CA  VAL A  87      -8.452  44.057  51.694  1.00 99.89           C  
ANISOU  465  CA  VAL A  87    19075  10126   8752    580  -2990   -374       C  
ATOM    466  C   VAL A  87      -7.619  43.670  52.921  1.00103.65           C  
ANISOU  466  C   VAL A  87    19800  10485   9094    602  -3213   -380       C  
ATOM    467  O   VAL A  87      -8.183  43.088  53.905  1.00 95.06           O  
ANISOU  467  O   VAL A  87    19078   9117   7923    587  -3193   -396       O  
ATOM    468  CB  VAL A  87      -8.083  43.151  50.498  1.00107.49           C  
ANISOU  468  CB  VAL A  87    19744  11317   9779    791  -3054   -432       C  
ATOM    469  CG1 VAL A  87      -7.856  41.705  50.921  1.00100.22           C  
ANISOU  469  CG1 VAL A  87    19023  10277   8776    979  -3212   -502       C  
ATOM    470  CG2 VAL A  87      -9.110  43.229  49.382  1.00117.12           C  
ANISOU  470  CG2 VAL A  87    20796  12583  11119    786  -2831   -437       C  
ATOM    471  N   VAL A  88      -6.321  43.910  52.763  1.00104.25           N  
ANISOU  471  N   VAL A  88    19658  10800   9152    643  -3419   -365       N  
ATOM    472  CA  VAL A  88      -5.315  43.481  53.772  1.00 99.87           C  
ANISOU  472  CA  VAL A  88    19268  10200   8476    696  -3673   -373       C  
ATOM    473  C   VAL A  88      -5.714  44.135  55.077  1.00 89.21           C  
ANISOU  473  C   VAL A  88    18296   8558   7040    501  -3636   -328       C  
ATOM    474  O   VAL A  88      -5.588  43.461  56.104  1.00 82.30           O  
ANISOU  474  O   VAL A  88    17730   7479   6059    541  -3749   -352       O  
ATOM    475  CB  VAL A  88      -3.857  43.791  53.369  1.00110.45           C  
ANISOU  475  CB  VAL A  88    20267  11893   9806    746  -3893   -344       C  
ATOM    476  CG1 VAL A  88      -3.664  45.215  52.863  1.00115.48           C  
ANISOU  476  CG1 VAL A  88    20659  12717  10499    539  -3833   -253       C  
ATOM    477  CG2 VAL A  88      -2.880  43.493  54.503  1.00124.57           C  
ANISOU  477  CG2 VAL A  88    22240  13622  11466    772  -4151   -339       C  
ATOM    478  N   ASN A  89      -6.010  45.423  55.043  1.00 95.74           N  
ANISOU  478  N   ASN A  89    19096   9383   7895    309  -3520   -264       N  
ATOM    479  CA  ASN A  89      -6.344  46.174  56.272  1.00 87.11           C  
ANISOU  479  CA  ASN A  89    18372   8021   6703    136  -3493   -223       C  
ATOM    480  C   ASN A  89      -7.640  45.713  56.933  1.00 87.33           C  
ANISOU  480  C   ASN A  89    18748   7745   6685    132  -3295   -253       C  
ATOM    481  O   ASN A  89      -7.672  45.613  58.162  1.00197.90           O  
ANISOU  481  O   ASN A  89    33109  21519  20565     84  -3350   -249       O  
ATOM    482  CB  ASN A  89      -6.343  47.673  56.004  1.00 94.22           C  
ANISOU  482  CB  ASN A  89    19176   8990   7632    -50  -3436   -151       C  
ATOM    483  CG  ASN A  89      -4.979  48.172  55.573  1.00109.01           C  
ANISOU  483  CG  ASN A  89    20747  11157   9513    -99  -3664    -94       C  
ATOM    484  OD1 ASN A  89      -4.863  49.269  55.030  1.00175.86           O  
ANISOU  484  OD1 ASN A  89    29048  19749  18020   -243  -3643    -30       O  
ATOM    485  ND2 ASN A  89      -3.945  47.372  55.793  1.00101.23           N  
ANISOU  485  ND2 ASN A  89    19682  10297   8482     17  -3889   -112       N  
ATOM    486  N   PHE A  90      -8.694  45.477  56.173  1.00 79.19           N  
ANISOU  486  N   PHE A  90    17622   6721   5744    169  -3070   -275       N  
ATOM    487  CA  PHE A  90      -9.924  44.946  56.782  1.00 81.76           C  
ANISOU  487  CA  PHE A  90    18250   6798   6017    156  -2888   -290       C  
ATOM    488  C   PHE A  90      -9.669  43.537  57.322  1.00 88.52           C  
ANISOU  488  C   PHE A  90    19296   7541   6796    268  -3036   -332       C  
ATOM    489  O   PHE A  90     -10.250  43.148  58.414  1.00112.84           O  
ANISOU  489  O   PHE A  90    22747  10370   9757    216  -2992   -326       O  
ATOM    490  CB  PHE A  90     -11.119  45.004  55.841  1.00101.44           C  
ANISOU  490  CB  PHE A  90    20583   9339   8618    157  -2624   -292       C  
ATOM    491  CG  PHE A  90     -11.814  46.338  55.873  1.00130.62           C  
ANISOU  491  CG  PHE A  90    24302  13002  12324     31  -2432   -251       C  
ATOM    492  CD1 PHE A  90     -12.710  46.650  56.885  1.00142.91           C  
ANISOU  492  CD1 PHE A  90    26188  14340  13772    -42  -2281   -235       C  
ATOM    493  CD2 PHE A  90     -11.539  47.296  54.913  1.00143.51           C  
ANISOU  493  CD2 PHE A  90    25640  14826  14059     -3  -2414   -230       C  
ATOM    494  CE1 PHE A  90     -13.349  47.880  56.911  1.00151.59           C  
ANISOU  494  CE1 PHE A  90    27324  15407  14863   -120  -2113   -209       C  
ATOM    495  CE2 PHE A  90     -12.176  48.529  54.943  1.00146.24           C  
ANISOU  495  CE2 PHE A  90    26040  15120  14402   -104  -2259   -199       C  
ATOM    496  CZ  PHE A  90     -13.075  48.821  55.945  1.00145.73           C  
ANISOU  496  CZ  PHE A  90    26311  14833  14227   -148  -2112   -193       C  
ATOM    497  N   THR A  91      -8.762  42.810  56.670  1.00 88.68           N  
ANISOU  497  N   THR A  91    19095   7737   6859    422  -3226   -372       N  
ATOM    498  CA  THR A  91      -8.365  41.486  57.200  1.00104.91           C  
ANISOU  498  CA  THR A  91    21354   9680   8827    554  -3417   -419       C  
ATOM    499  C   THR A  91      -7.684  41.641  58.556  1.00123.64           C  
ANISOU  499  C   THR A  91    24019  11898  11059    495  -3594   -401       C  
ATOM    500  O   THR A  91      -7.878  40.804  59.466  1.00109.69           O  
ANISOU  500  O   THR A  91    22594   9902   9179    511  -3662   -417       O  
ATOM    501  CB  THR A  91      -7.517  40.690  56.198  1.00 99.23           C  
ANISOU  501  CB  THR A  91    20341   9194   8166    773  -3590   -476       C  
ATOM    502  OG1 THR A  91      -8.241  40.536  54.976  1.00113.66           O  
ANISOU  502  OG1 THR A  91    21935  11135  10113    819  -3419   -492       O  
ATOM    503  CG2 THR A  91      -7.154  39.316  56.718  1.00 93.77           C  
ANISOU  503  CG2 THR A  91    19890   8364   7373    932  -3800   -533       C  
ATOM    504  N   TYR A  92      -6.900  42.698  58.684  1.00136.70           N  
ANISOU  504  N   TYR A  92    25553  13672  12714    415  -3677   -361       N  
ATOM    505  CA  TYR A  92      -6.271  43.028  59.984  1.00114.73           C  
ANISOU  505  CA  TYR A  92    23055  10738   9797    329  -3844   -333       C  
ATOM    506  C   TYR A  92      -7.387  43.295  60.984  1.00118.43           C  
ANISOU  506  C   TYR A  92    23919  10906  10173    191  -3655   -311       C  
ATOM    507  O   TYR A  92      -7.324  42.897  62.141  1.00206.34           O  
ANISOU  507  O   TYR A  92    35406  21821  21171    167  -3746   -312       O  
ATOM    508  CB  TYR A  92      -5.342  44.242  59.851  1.00113.83           C  
ANISOU  508  CB  TYR A  92    22735  10811   9703    226  -3955   -277       C  
ATOM    509  CG  TYR A  92      -3.983  43.977  59.248  1.00129.89           C  
ANISOU  509  CG  TYR A  92    24427  13152  11770    346  -4203   -282       C  
ATOM    510  CD1 TYR A  92      -3.709  42.812  58.546  1.00147.27           C  
ANISOU  510  CD1 TYR A  92    26447  15495  14011    575  -4277   -349       C  
ATOM    511  CD2 TYR A  92      -2.968  44.918  59.357  1.00113.16           C  
ANISOU  511  CD2 TYR A  92    22163  11200   9632    233  -4368   -214       C  
ATOM    512  CE1 TYR A  92      -2.461  42.577  57.993  1.00137.37           C  
ANISOU  512  CE1 TYR A  92    24864  14558  12771    716  -4495   -357       C  
ATOM    513  CE2 TYR A  92      -1.725  44.710  58.780  1.00121.17           C  
ANISOU  513  CE2 TYR A  92    22822  12548  10667    338  -4584   -205       C  
ATOM    514  CZ  TYR A  92      -1.465  43.529  58.105  1.00135.88           C  
ANISOU  514  CZ  TYR A  92    24495  14568  12564    595  -4642   -281       C  
ATOM    515  OH  TYR A  92      -0.246  43.296  57.537  1.00127.72           O  
ANISOU  515  OH  TYR A  92    23100  13893  11534    733  -4847   -278       O  
ATOM    516  N   ALA A  93      -8.439  43.933  60.508  1.00118.92           N  
ANISOU  516  N   ALA A  93    23913  10970  10300    113  -3386   -291       N  
ATOM    517  CA  ALA A  93      -9.441  44.568  61.387  1.00116.88           C  
ANISOU  517  CA  ALA A  93    23971  10491   9947    -17  -3187   -261       C  
ATOM    518  C   ALA A  93     -10.499  43.584  61.843  1.00106.55           C  
ANISOU  518  C   ALA A  93    22909   9004   8570     -4  -3044   -272       C  
ATOM    519  O   ALA A  93     -11.335  44.015  62.669  1.00120.55           O  
ANISOU  519  O   ALA A  93    24955  10611  10238   -100  -2876   -245       O  
ATOM    520  CB  ALA A  93     -10.031  45.784  60.711  1.00149.10           C  
ANISOU  520  CB  ALA A  93    27871  14667  14110    -93  -2982   -234       C  
ATOM    521  N   VAL A  94     -10.440  42.336  61.394  1.00 90.84           N  
ANISOU  521  N   VAL A  94    20853   7044   6618    104  -3122   -306       N  
ATOM    522  CA  VAL A  94     -11.447  41.316  61.773  1.00 98.72           C  
ANISOU  522  CA  VAL A  94    22090   7873   7544     87  -3011   -302       C  
ATOM    523  C   VAL A  94     -11.412  41.057  63.280  1.00133.88           C  
ANISOU  523  C   VAL A  94    26983  12077  11805     15  -3090   -283       C  
ATOM    524  O   VAL A  94     -12.447  41.169  63.970  1.00231.51           O  
ANISOU  524  O   VAL A  94    39587  24305  24070    -92  -2890   -244       O  
ATOM    525  CB  VAL A  94     -11.263  40.015  60.959  1.00101.58           C  
ANISOU  525  CB  VAL A  94    22324   8298   7973    225  -3133   -344       C  
ATOM    526  CG1 VAL A  94     -11.521  40.248  59.475  1.00116.55           C  
ANISOU  526  CG1 VAL A  94    23812  10426  10046    285  -3012   -358       C  
ATOM    527  CG2 VAL A  94      -9.907  39.347  61.166  1.00 90.55           C  
ANISOU  527  CG2 VAL A  94    20955   6914   6536    366  -3467   -392       C  
ATOM    528  N   HIS A  95     -10.283  40.623  63.792  1.00148.12           N  
ANISOU  528  N   HIS A  95    28898  13831  13548     82  -3376   -309       N  
ATOM    529  CA  HIS A  95     -10.196  40.270  65.231  1.00116.10           C  
ANISOU  529  CA  HIS A  95    25281   9526   9303     18  -3478   -294       C  
ATOM    530  C   HIS A  95      -9.490  41.357  66.027  1.00104.91           C  
ANISOU  530  C   HIS A  95    23975   8070   7816    -47  -3569   -277       C  
ATOM    531  O   HIS A  95      -9.248  41.129  67.214  1.00113.02           O  
ANISOU  531  O   HIS A  95    25356   8899   8686    -90  -3687   -268       O  
ATOM    532  CB  HIS A  95      -9.577  38.879  65.448  1.00108.92           C  
ANISOU  532  CB  HIS A  95    24519   8527   8338    131  -3743   -332       C  
ATOM    533  CG  HIS A  95     -10.597  37.792  65.432  1.00113.14           C  
ANISOU  533  CG  HIS A  95    25224   8936   8826    101  -3643   -318       C  
ATOM    534  ND1 HIS A  95     -11.098  37.277  64.253  1.00124.91           N  
ANISOU  534  ND1 HIS A  95    26470  10549  10441    163  -3557   -332       N  
ATOM    535  CD2 HIS A  95     -11.257  37.170  66.431  1.00111.64           C  
ANISOU  535  CD2 HIS A  95    25425   8518   8474     -7  -3609   -278       C  
ATOM    536  CE1 HIS A  95     -11.998  36.355  64.527  1.00121.69           C  
ANISOU  536  CE1 HIS A  95    26300   9987   9950     88  -3493   -299       C  
ATOM    537  NE2 HIS A  95     -12.118  36.274  65.857  1.00125.30           N  
ANISOU  537  NE2 HIS A  95    27142  10237  10230    -23  -3519   -262       N  
ATOM    538  N   ASN A  96      -9.324  42.540  65.429  1.00115.99           N  
ANISOU  538  N   ASN A  96    25112   9639   9320    -71  -3501   -266       N  
ATOM    539  CA  ASN A  96      -8.499  43.624  65.976  1.00126.50           C  
ANISOU  539  CA  ASN A  96    26498  10964  10601   -141  -3639   -244       C  
ATOM    540  C   ASN A  96      -7.053  43.190  66.204  1.00145.66           C  
ANISOU  540  C   ASN A  96    28879  13449  13014    -71  -3986   -258       C  
ATOM    541  O   ASN A  96      -6.462  43.485  67.243  1.00164.32           O  
ANISOU  541  O   ASN A  96    31524  15662  15246   -138  -4136   -239       O  
ATOM    542  CB  ASN A  96      -9.076  44.169  67.291  1.00107.43           C  
ANISOU  542  CB  ASN A  96    24520   8295   8000   -255  -3558   -216       C  
ATOM    543  CG  ASN A  96     -10.542  44.542  67.184  1.00101.65           C  
ANISOU  543  CG  ASN A  96    23868   7511   7241   -309  -3213   -200       C  
ATOM    544  OD1 ASN A  96     -11.325  43.861  66.522  1.00101.44           O  
ANISOU  544  OD1 ASN A  96    23729   7538   7276   -276  -3041   -204       O  
ATOM    545  ND2 ASN A  96     -10.921  45.632  67.844  1.00 85.48           N  
ANISOU  545  ND2 ASN A  96    22031   5359   5088   -385  -3118   -180       N  
ATOM    546  N   GLU A  97      -6.491  42.489  65.223  1.00160.95           N  
ANISOU  546  N   GLU A  97    30496  15591  15064     67  -4109   -292       N  
ATOM    547  CA  GLU A  97      -5.104  42.041  65.287  1.00133.14           C  
ANISOU  547  CA  GLU A  97    26880  12179  11529    175  -4439   -310       C  
ATOM    548  C   GLU A  97      -4.139  43.206  65.071  1.00119.19           C  
ANISOU  548  C   GLU A  97    24862  10616   9807     99  -4557   -263       C  
ATOM    549  O   GLU A  97      -3.147  43.340  65.789  1.00111.53           O  
ANISOU  549  O   GLU A  97    24012   9615   8748     65  -4794   -240       O  
ATOM    550  CB  GLU A  97      -4.851  40.945  64.250  1.00122.05           C  
ANISOU  550  CB  GLU A  97    25213  10943  10215    382  -4511   -369       C  
ATOM    551  CG  GLU A  97      -5.864  39.813  64.294  1.00106.32           C  
ANISOU  551  CG  GLU A  97    23452   8756   8186    433  -4399   -403       C  
ATOM    552  CD  GLU A  97      -5.648  38.796  63.193  1.00 99.40           C  
ANISOU  552  CD  GLU A  97    22351   8019   7394    636  -4460   -464       C  
ATOM    553  OE1 GLU A  97      -6.627  38.462  62.493  1.00 91.06           O  
ANISOU  553  OE1 GLU A  97    21242   6951   6404    626  -4251   -469       O  
ATOM    554  OE2 GLU A  97      -4.502  38.327  63.032  1.00 99.22           O  
ANISOU  554  OE2 GLU A  97    22218   8118   7362    815  -4724   -508       O  
ATOM    555  N   TRP A  98      -4.450  44.039  64.080  1.00122.69           N  
ANISOU  555  N   TRP A  98    25004  11241  10371     46  -4392   -240       N  
ATOM    556  CA  TRP A  98      -3.658  45.219  63.723  1.00124.47           C  
ANISOU  556  CA  TRP A  98    25020  11643  10628    -77  -4485   -176       C  
ATOM    557  C   TRP A  98      -2.157  44.931  63.658  1.00125.74           C  
ANISOU  557  C   TRP A  98    24987  12013  10773    -13  -4813   -161       C  
ATOM    558  O   TRP A  98      -1.384  45.421  64.484  1.00102.52           O  
ANISOU  558  O   TRP A  98    22167   9036   7748   -139  -4994   -105       O  
ATOM    559  CB  TRP A  98      -3.932  46.361  64.706  1.00117.38           C  
ANISOU  559  CB  TRP A  98    24477  10505   9617   -271  -4434   -128       C  
ATOM    560  CG  TRP A  98      -5.382  46.762  64.775  1.00129.49           C  
ANISOU  560  CG  TRP A  98    26190  11863  11145   -316  -4110   -140       C  
ATOM    561  CD1 TRP A  98      -6.263  46.479  65.778  1.00133.46           C  
ANISOU  561  CD1 TRP A  98    27088  12090  11527   -323  -3974   -161       C  
ATOM    562  CD2 TRP A  98      -6.117  47.508  63.795  1.00171.69           C  
ANISOU  562  CD2 TRP A  98    31309  17322  16602   -352  -3881   -130       C  
ATOM    563  NE1 TRP A  98      -7.498  47.007  65.488  1.00161.00           N  
ANISOU  563  NE1 TRP A  98    30596  15534  15043   -354  -3671   -163       N  
ATOM    564  CE2 TRP A  98      -7.436  47.642  64.276  1.00177.61           C  
ANISOU  564  CE2 TRP A  98    32330  17861  17290   -367  -3612   -147       C  
ATOM    565  CE3 TRP A  98      -5.789  48.076  62.559  1.00169.20           C  
ANISOU  565  CE3 TRP A  98    30590  17274  16422   -375  -3879   -103       C  
ATOM    566  CZ2 TRP A  98      -8.425  48.321  63.566  1.00157.23           C  
ANISOU  566  CZ2 TRP A  98    29623  15328  14787   -387  -3349   -145       C  
ATOM    567  CZ3 TRP A  98      -6.774  48.750  61.855  1.00142.56           C  
ANISOU  567  CZ3 TRP A  98    27117  13923  13126   -408  -3624   -100       C  
ATOM    568  CH2 TRP A  98      -8.075  48.866  62.361  1.00143.88           C  
ANISOU  568  CH2 TRP A  98    27553  13877  13236   -405  -3365   -124       C  
ATOM    569  N   TYR A  99      -1.764  44.132  62.668  1.00166.36           N  
ANISOU  569  N   TYR A  99    29810  17398  15999    178  -4879   -205       N  
ATOM    570  CA  TYR A  99      -0.368  43.769  62.438  1.00177.40           C  
ANISOU  570  CA  TYR A  99    30938  19074  17389    298  -5172   -201       C  
ATOM    571  C   TYR A  99       0.484  45.027  62.273  1.00185.48           C  
ANISOU  571  C   TYR A  99    31721  20325  18428    110  -5276   -100       C  
ATOM    572  O   TYR A  99       1.434  45.244  63.030  1.00132.11           O  
ANISOU  572  O   TYR A  99    24950  13653  11593     47  -5534    -44       O  
ATOM    573  CB  TYR A  99      -0.276  42.860  61.205  1.00205.00           C  
ANISOU  573  CB  TYR A  99    34094  22809  20984    542  -5133   -271       C  
ATOM    574  CG  TYR A  99       1.113  42.450  60.760  1.00204.05           C  
ANISOU  574  CG  TYR A  99    33605  23055  20867    725  -5386   -279       C  
ATOM    575  CD1 TYR A  99       1.820  43.211  59.837  1.00221.90           C  
ANISOU  575  CD1 TYR A  99    35407  25705  23200    674  -5414   -216       C  
ATOM    576  CD2 TYR A  99       1.697  41.280  61.227  1.00173.42           C  
ANISOU  576  CD2 TYR A  99    29825  19152  16912    966  -5591   -352       C  
ATOM    577  CE1 TYR A  99       3.083  42.833  59.413  1.00180.94           C  
ANISOU  577  CE1 TYR A  99    29846  20902  18001    856  -5631   -219       C  
ATOM    578  CE2 TYR A  99       2.959  40.893  60.808  1.00162.87           C  
ANISOU  578  CE2 TYR A  99    28136  18181  15566   1175  -5818   -368       C  
ATOM    579  CZ  TYR A  99       3.646  41.674  59.901  1.00152.24           C  
ANISOU  579  CZ  TYR A  99    26306  17251  14286   1123  -5830   -300       C  
ATOM    580  OH  TYR A  99       4.900  41.294  59.482  1.00132.86           O  
ANISOU  580  OH  TYR A  99    23471  15201  11806   1336  -6042   -308       O  
ATOM    581  N   TYR A 100       0.145  45.851  61.284  1.00222.13           N  
ANISOU  581  N   TYR A 100    36149  25079  23170      8  -5080    -67       N  
ATOM    582  CA  TYR A 100       0.670  47.211  61.220  1.00218.12           C  
ANISOU  582  CA  TYR A 100    35428  24768  22679   -209  -5151     40       C  
ATOM    583  C   TYR A 100      -0.458  48.225  61.370  1.00185.75           C  
ANISOU  583  C   TYR A 100    31564  20425  18585   -397  -4924     66       C  
ATOM    584  O   TYR A 100      -1.215  48.459  60.426  1.00152.00           O  
ANISOU  584  O   TYR A 100    27145  16192  14414   -391  -4683     48       O  
ATOM    585  CB  TYR A 100       1.401  47.444  59.894  1.00245.01           C  
ANISOU  585  CB  TYR A 100    38272  28631  26187   -152  -5189     71       C  
ATOM    586  CG  TYR A 100       2.897  47.226  59.946  1.00261.38           C  
ANISOU  586  CG  TYR A 100    40073  31031  28208   -122  -5500    127       C  
ATOM    587  CD1 TYR A 100       3.442  46.173  60.668  1.00228.31           C  
ANISOU  587  CD1 TYR A 100    35991  26813  23942     74  -5690     69       C  
ATOM    588  CD2 TYR A 100       3.765  48.068  59.258  1.00262.89           C  
ANISOU  588  CD2 TYR A 100    39897  31570  28415   -291  -5614    243       C  
ATOM    589  CE1 TYR A 100       4.805  45.972  60.715  1.00178.05           C  
ANISOU  589  CE1 TYR A 100    29361  20768  17520    126  -5977    117       C  
ATOM    590  CE2 TYR A 100       5.129  47.874  59.300  1.00232.22           C  
ANISOU  590  CE2 TYR A 100    35734  28026  24472   -266  -5898    305       C  
ATOM    591  CZ  TYR A 100       5.644  46.824  60.029  1.00189.62           C  
ANISOU  591  CZ  TYR A 100    30435  22609  19003    -46  -6077    239       C  
ATOM    592  OH  TYR A 100       7.005  46.627  60.071  1.00154.97           O  
ANISOU  592  OH  TYR A 100    25758  18574  14549      0  -6358    299       O  
ATOM    593  N   GLY A 101      -0.487  48.912  62.515  1.00148.60           N  
ANISOU  593  N   GLY A 101    27255  15448  13757   -538  -5006     98       N  
ATOM    594  CA  GLY A 101      -1.450  50.019  62.651  1.00146.47           C  
ANISOU  594  CA  GLY A 101    27200  14985  13466   -725  -4850    137       C  
ATOM    595  C   GLY A 101      -0.802  51.281  62.101  1.00146.92           C  
ANISOU  595  C   GLY A 101    26996  15269  13557   -921  -4956    241       C  
ATOM    596  O   GLY A 101      -1.304  51.796  61.085  1.00205.97           O  
ANISOU  596  O   GLY A 101    34228  22886  21143   -946  -4785    251       O  
ATOM    597  N   LEU A 102       0.275  51.749  62.749  1.00153.81           N  
ANISOU  597  N   LEU A 102    27962  16148  14328  -1085  -5232    326       N  
ATOM    598  CA  LEU A 102       1.096  52.906  62.286  1.00144.75           C  
ANISOU  598  CA  LEU A 102    26618  15202  13178  -1326  -5399    452       C  
ATOM    599  C   LEU A 102       0.186  54.068  61.879  1.00132.22           C  
ANISOU  599  C   LEU A 102    25135  13480  11621  -1450  -5194    468       C  
ATOM    600  O   LEU A 102      -0.701  54.446  62.668  1.00116.34           O  
ANISOU  600  O   LEU A 102    23548  11112   9542  -1450  -5040    420       O  
ATOM    601  CB  LEU A 102       1.980  52.465  61.115  1.00142.97           C  
ANISOU  601  CB  LEU A 102    25806  15460  13053  -1258  -5496    489       C  
ATOM    602  CG  LEU A 102       3.069  51.451  61.461  1.00150.86           C  
ANISOU  602  CG  LEU A 102    26654  16651  14011  -1119  -5734    481       C  
ATOM    603  CD1 LEU A 102       2.458  50.119  61.858  1.00163.44           C  
ANISOU  603  CD1 LEU A 102    28489  18015  15593   -855  -5634    345       C  
ATOM    604  CD2 LEU A 102       4.029  51.268  60.297  1.00143.12           C  
ANISOU  604  CD2 LEU A 102    25074  16188  13114  -1038  -5812    519       C  
ATOM    605  N   PHE A 103       0.442  54.614  60.686  1.00146.67           N  
ANISOU  605  N   PHE A 103    26588  15601  13538  -1553  -5202    539       N  
ATOM    606  CA  PHE A 103      -0.430  55.647  60.078  1.00159.21           C  
ANISOU  606  CA  PHE A 103    28226  17098  15166  -1659  -5020    555       C  
ATOM    607  C   PHE A 103      -1.431  54.985  59.142  1.00154.66           C  
ANISOU  607  C   PHE A 103    27438  16591  14733  -1444  -4705    455       C  
ATOM    608  O   PHE A 103      -2.254  55.683  58.560  1.00130.76           O  
ANISOU  608  O   PHE A 103    24422  13503  11755  -1485  -4524    451       O  
ATOM    609  CB  PHE A 103       0.409  56.718  59.372  1.00172.68           C  
ANISOU  609  CB  PHE A 103    29672  19061  16874  -1922  -5211    699       C  
ATOM    610  CG  PHE A 103       1.059  56.280  58.085  1.00160.85           C  
ANISOU  610  CG  PHE A 103    27575  18041  15498  -1876  -5225    736       C  
ATOM    611  CD1 PHE A 103       2.283  55.631  58.096  1.00152.76           C  
ANISOU  611  CD1 PHE A 103    26250  17335  14457  -1846  -5447    781       C  
ATOM    612  CD2 PHE A 103       0.454  56.529  56.863  1.00141.56           C  
ANISOU  612  CD2 PHE A 103    24870  15743  13174  -1851  -5020    724       C  
ATOM    613  CE1 PHE A 103       2.888  55.238  56.912  1.00136.92           C  
ANISOU  613  CE1 PHE A 103    23689  15793  12542  -1779  -5454    812       C  
ATOM    614  CE2 PHE A 103       1.060  56.136  55.680  1.00136.28           C  
ANISOU  614  CE2 PHE A 103    23658  15521  12601  -1801  -5031    757       C  
ATOM    615  CZ  PHE A 103       2.274  55.490  55.707  1.00133.08           C  
ANISOU  615  CZ  PHE A 103    22954  15440  12167  -1759  -5243    799       C  
ATOM    616  N   TYR A 104      -1.282  53.696  58.950  1.00178.83           N  
ANISOU  616  N   TYR A 104    30299  19793  17854  -1226  -4671    384       N  
ATOM    617  CA  TYR A 104      -2.156  52.959  57.999  1.00191.02           C  
ANISOU  617  CA  TYR A 104    31624  21421  19533  -1024  -4401    294       C  
ATOM    618  C   TYR A 104      -3.613  53.045  58.462  1.00186.89           C  
ANISOU  618  C   TYR A 104    31471  20545  18994   -968  -4131    220       C  
ATOM    619  O   TYR A 104      -4.450  52.706  57.681  1.00240.97           O  
ANISOU  619  O   TYR A 104    38171  27439  25947   -854  -3903    166       O  
ATOM    620  CB  TYR A 104      -1.659  51.512  57.845  1.00209.52           C  
ANISOU  620  CB  TYR A 104    33754  23942  21912   -793  -4460    229       C  
ATOM    621  CG  TYR A 104      -0.304  51.402  57.195  1.00198.89           C  
ANISOU  621  CG  TYR A 104    31969  23014  20585   -802  -4687    295       C  
ATOM    622  CD1 TYR A 104      -0.168  51.398  55.813  1.00179.49           C  
ANISOU  622  CD1 TYR A 104    29054  20904  18240   -755  -4615    309       C  
ATOM    623  CD2 TYR A 104       0.851  51.311  57.957  1.00212.04           C  
ANISOU  623  CD2 TYR A 104    33665  24751  22149   -855  -4975    349       C  
ATOM    624  CE1 TYR A 104       1.075  51.304  55.208  1.00176.67           C  
ANISOU  624  CE1 TYR A 104    28270  20972  17883   -755  -4812    375       C  
ATOM    625  CE2 TYR A 104       2.101  51.219  57.366  1.00194.32           C  
ANISOU  625  CE2 TYR A 104    30988  22934  19910   -858  -5181    419       C  
ATOM    626  CZ  TYR A 104       2.214  51.210  55.989  1.00180.07           C  
ANISOU  626  CZ  TYR A 104    28718  21491  18207   -803  -5094    432       C  
ATOM    627  OH  TYR A 104       3.450  51.116  55.423  1.00192.48           O  
ANISOU  627  OH  TYR A 104    29847  23519  19766   -797  -5288    505       O  
ATOM    628  N   CYS A 105      -3.973  53.409  59.731  1.00127.39           N  
ANISOU  628  N   CYS A 105    24413  12668  11321  -1029  -4143    212       N  
ATOM    629  CA  CYS A 105      -5.358  53.513  60.198  1.00129.49           C  
ANISOU  629  CA  CYS A 105    25013  12637  11548   -965  -3878    147       C  
ATOM    630  C   CYS A 105      -6.059  54.661  59.479  1.00115.59           C  
ANISOU  630  C   CYS A 105    23210  10872   9834  -1047  -3725    171       C  
ATOM    631  O   CYS A 105      -7.123  54.479  58.855  1.00105.72           O  
ANISOU  631  O   CYS A 105    21869   9626   8670   -940  -3460    119       O  
ATOM    632  CB  CYS A 105      -5.429  53.733  61.710  1.00136.51           C  
ANISOU  632  CB  CYS A 105    26410  13199  12256  -1013  -3954    143       C  
ATOM    633  SG  CYS A 105      -5.777  52.225  62.637  1.00163.80           S  
ANISOU  633  SG  CYS A 105    30274  16334  15628   -955  -3637     83       S  
ATOM    634  N   LYS A 106      -5.389  55.785  59.563  1.00111.92           N  
ANISOU  634  N   LYS A 106    22806  10410   9308  -1243  -3920    256       N  
ATOM    635  CA  LYS A 106      -5.966  56.972  58.934  1.00140.15           C  
ANISOU  635  CA  LYS A 106    26389  13955  12906  -1336  -3821    285       C  
ATOM    636  C   LYS A 106      -5.852  56.884  57.424  1.00182.33           C  
ANISOU  636  C   LYS A 106    31231  19628  18419  -1329  -3757    307       C  
ATOM    637  O   LYS A 106      -6.797  57.379  56.737  1.00217.96           O  
ANISOU  637  O   LYS A 106    35704  24114  22995  -1299  -3549    283       O  
ATOM    638  CB  LYS A 106      -5.283  58.235  59.452  1.00156.88           C  
ANISOU  638  CB  LYS A 106    28756  15957  14894  -1570  -4076    378       C  
ATOM    639  CG  LYS A 106      -3.828  58.395  59.038  1.00181.91           C  
ANISOU  639  CG  LYS A 106    31621  19412  18083  -1757  -4380    493       C  
ATOM    640  CD  LYS A 106      -3.011  59.229  60.005  1.00188.74           C  
ANISOU  640  CD  LYS A 106    32812  20117  18782  -1979  -4683    583       C  
ATOM    641  CE  LYS A 106      -2.771  58.528  61.325  1.00173.25           C  
ANISOU  641  CE  LYS A 106    31152  17964  16708  -1902  -4770    540       C  
ATOM    642  NZ  LYS A 106      -1.650  59.138  62.074  1.00185.27           N  
ANISOU  642  NZ  LYS A 106    32858  19440  18096  -2134  -5123    648       N  
ATOM    643  N   PHE A 107      -4.874  56.149  56.912  1.00192.11           N  
ANISOU  643  N   PHE A 107    32098  21166  19727  -1313  -3894    334       N  
ATOM    644  CA  PHE A 107      -4.753  56.053  55.435  1.00149.90           C  
ANISOU  644  CA  PHE A 107    26266  16155  14530  -1293  -3828    353       C  
ATOM    645  C   PHE A 107      -5.861  55.167  54.876  1.00106.16           C  
ANISOU  645  C   PHE A 107    20622  10608   9105  -1069  -3534    249       C  
ATOM    646  O   PHE A 107      -6.469  55.483  53.883  1.00 78.13           O  
ANISOU  646  O   PHE A 107    16883   7148   5654  -1056  -3372    243       O  
ATOM    647  CB  PHE A 107      -3.365  55.528  55.089  1.00145.05           C  
ANISOU  647  CB  PHE A 107    25289  15888  13934  -1316  -4062    411       C  
ATOM    648  CG  PHE A 107      -3.229  55.045  53.674  1.00135.74           C  
ANISOU  648  CG  PHE A 107    23610  15069  12894  -1219  -3978    403       C  
ATOM    649  CD1 PHE A 107      -3.395  55.909  52.605  1.00129.77           C  
ANISOU  649  CD1 PHE A 107    22635  14465  12206  -1341  -3918    462       C  
ATOM    650  CD2 PHE A 107      -2.922  53.723  53.417  1.00134.25           C  
ANISOU  650  CD2 PHE A 107    23191  15059  12756   -997  -3973    336       C  
ATOM    651  CE1 PHE A 107      -3.239  55.458  51.305  1.00119.86           C  
ANISOU  651  CE1 PHE A 107    20922  13550  11067  -1249  -3844    456       C  
ATOM    652  CE2 PHE A 107      -2.769  53.271  52.116  1.00145.88           C  
ANISOU  652  CE2 PHE A 107    24220  16866  14341   -889  -3905    324       C  
ATOM    653  CZ  PHE A 107      -2.934  54.138  51.061  1.00124.69           C  
ANISOU  653  CZ  PHE A 107    21308  14343  11724  -1016  -3833    384       C  
ATOM    654  N   HIS A 108      -5.993  54.031  55.560  1.00100.92           N  
ANISOU  654  N   HIS A 108    20085   9844   8414   -911  -3505    177       N  
ATOM    655  CA  HIS A 108      -6.957  52.941  55.294  1.00116.69           C  
ANISOU  655  CA  HIS A 108    22046  11801  10487   -705  -3273     83       C  
ATOM    656  C   HIS A 108      -8.395  53.440  55.452  1.00101.18           C  
ANISOU  656  C   HIS A 108    20326   9601   8517   -692  -3006     48       C  
ATOM    657  O   HIS A 108      -9.343  52.906  54.809  1.00115.30           O  
ANISOU  657  O   HIS A 108    21990  11418  10400   -573  -2780     -2       O  
ATOM    658  CB  HIS A 108      -6.702  51.789  56.275  1.00155.42           C  
ANISOU  658  CB  HIS A 108    27146  16589  15317   -591  -3356     34       C  
ATOM    659  CG  HIS A 108      -7.920  51.014  56.649  1.00194.32           C  
ANISOU  659  CG  HIS A 108    32286  21308  20238   -463  -3127    -40       C  
ATOM    660  ND1 HIS A 108      -8.669  51.304  57.777  1.00228.79           N  
ANISOU  660  ND1 HIS A 108    37072  25372  24483   -496  -3029    -52       N  
ATOM    661  CD2 HIS A 108      -8.529  49.975  56.049  1.00186.43           C  
ANISOU  661  CD2 HIS A 108    31142  20367  19326   -314  -2981    -97       C  
ATOM    662  CE1 HIS A 108      -9.681  50.467  57.857  1.00186.16           C  
ANISOU  662  CE1 HIS A 108    31755  19878  19098   -385  -2828   -105       C  
ATOM    663  NE2 HIS A 108      -9.612  49.641  56.812  1.00171.54           N  
ANISOU  663  NE2 HIS A 108    29571  18231  17374   -282  -2805   -131       N  
ATOM    664  N   ASN A 109      -8.564  54.382  56.361  1.00102.15           N  
ANISOU  664  N   ASN A 109    20807   9491   8514   -799  -3038     73       N  
ATOM    665  CA  ASN A 109      -9.868  55.021  56.610  1.00116.59           C  
ANISOU  665  CA  ASN A 109    22893  11103  10303   -773  -2802     42       C  
ATOM    666  C   ASN A 109     -10.146  56.076  55.567  1.00112.34           C  
ANISOU  666  C   ASN A 109    22176  10663   9842   -846  -2740     76       C  
ATOM    667  O   ASN A 109     -11.343  56.242  55.148  1.00133.96           O  
ANISOU  667  O   ASN A 109    24913  13355  12629   -759  -2487     35       O  
ATOM    668  CB  ASN A 109      -9.989  55.626  58.008  1.00152.77           C  
ANISOU  668  CB  ASN A 109    27962  15386  14697   -826  -2857     43       C  
ATOM    669  CG  ASN A 109     -11.338  56.283  58.208  1.00180.11           C  
ANISOU  669  CG  ASN A 109    31662  18665  18105   -761  -2606      5       C  
ATOM    670  OD1 ASN A 109     -11.443  57.506  58.268  1.00218.62           O  
ANISOU  670  OD1 ASN A 109    36568  23503  22995   -628  -2368    -47       O  
ATOM    671  ND2 ASN A 109     -12.376  55.480  58.336  1.00198.82           N  
ANISOU  671  ND2 ASN A 109    34202  20932  20405   -852  -2664     36       N  
ATOM    672  N   PHE A 110      -9.097  56.758  55.111  1.00128.75           N  
ANISOU  672  N   PHE A 110    24094  12893  11932  -1005  -2963    154       N  
ATOM    673  CA  PHE A 110      -9.203  57.902  54.198  1.00130.78           C  
ANISOU  673  CA  PHE A 110    24228  13226  12236  -1120  -2960    205       C  
ATOM    674  C   PHE A 110      -9.426  57.471  52.753  1.00106.71           C  
ANISOU  674  C   PHE A 110    20727  10453   9363  -1052  -2828    195       C  
ATOM    675  O   PHE A 110     -10.266  58.036  52.043  1.00 84.69           O  
ANISOU  675  O   PHE A 110    17887   7653   6635  -1035  -2664    184       O  
ATOM    676  CB  PHE A 110      -7.959  58.786  54.324  1.00126.67           C  
ANISOU  676  CB  PHE A 110    23725  12765  11638  -1355  -3273    312       C  
ATOM    677  CG  PHE A 110      -7.797  59.844  53.265  1.00113.65           C  
ANISOU  677  CG  PHE A 110    21889  11252  10038  -1513  -3327    389       C  
ATOM    678  CD1 PHE A 110      -8.326  61.117  53.436  1.00103.13           C  
ANISOU  678  CD1 PHE A 110    20870   9692   8622  -1604  -3329    409       C  
ATOM    679  CD2 PHE A 110      -7.093  59.567  52.103  1.00104.45           C  
ANISOU  679  CD2 PHE A 110    20249  10448   8990  -1566  -3388    443       C  
ATOM    680  CE1 PHE A 110      -8.155  62.090  52.464  1.00105.88           C  
ANISOU  680  CE1 PHE A 110    21071  10151   9005  -1765  -3402    486       C  
ATOM    681  CE2 PHE A 110      -6.923  60.543  51.133  1.00123.70           C  
ANISOU  681  CE2 PHE A 110    22519  13019  11461  -1734  -3446    524       C  
ATOM    682  CZ  PHE A 110      -7.456  61.801  51.315  1.00120.55           C  
ANISOU  682  CZ  PHE A 110    22447  12372  10982  -1843  -3458    548       C  
ATOM    683  N   PHE A 111      -8.671  56.459  52.348  1.00105.90           N  
ANISOU  683  N   PHE A 111    20314  10592   9332   -998  -2908    194       N  
ATOM    684  CA  PHE A 111      -8.399  56.129  50.931  1.00117.58           C  
ANISOU  684  CA  PHE A 111    21322  12398  10953   -969  -2879    208       C  
ATOM    685  C   PHE A 111      -9.579  55.522  50.187  1.00 96.97           C  
ANISOU  685  C   PHE A 111    18584   9797   8463   -799  -2601    132       C  
ATOM    686  O   PHE A 111      -9.746  55.803  49.008  1.00 79.00           O  
ANISOU  686  O   PHE A 111    16026   7700   6290   -813  -2530    149       O  
ATOM    687  CB  PHE A 111      -7.186  55.200  50.815  1.00136.74           C  
ANISOU  687  CB  PHE A 111    23481  15083  13389   -926  -3064    222       C  
ATOM    688  CG  PHE A 111      -6.516  55.198  49.463  1.00123.53           C  
ANISOU  688  CG  PHE A 111    21333  13791  11810   -951  -3118    269       C  
ATOM    689  CD1 PHE A 111      -6.251  56.387  48.797  1.00126.70           C  
ANISOU  689  CD1 PHE A 111    21612  14311  12218  -1153  -3181    363       C  
ATOM    690  CD2 PHE A 111      -6.120  54.010  48.870  1.00108.43           C  
ANISOU  690  CD2 PHE A 111    19111  12122   9962   -772  -3119    222       C  
ATOM    691  CE1 PHE A 111      -5.623  56.385  47.563  1.00113.02           C  
ANISOU  691  CE1 PHE A 111    19436  12950  10556  -1186  -3226    415       C  
ATOM    692  CE2 PHE A 111      -5.477  54.014  47.644  1.00116.15           C  
ANISOU  692  CE2 PHE A 111    19651  13473  11007   -779  -3166    265       C  
ATOM    693  CZ  PHE A 111      -5.238  55.198  46.987  1.00119.09           C  
ANISOU  693  CZ  PHE A 111    19883  13978  11385   -991  -3210    363       C  
ATOM    694  N   PRO A 112     -10.367  54.596  50.770  1.00 96.27           N  
ANISOU  694  N   PRO A 112    18665   9546   8366   -645  -2451     54       N  
ATOM    695  CA  PRO A 112     -11.448  53.972  50.022  1.00 92.53           C  
ANISOU  695  CA  PRO A 112    18049   9103   8005   -507  -2208     -2       C  
ATOM    696  C   PRO A 112     -12.507  54.943  49.511  1.00 92.54           C  
ANISOU  696  C   PRO A 112    18078   9033   8047   -537  -2019      2       C  
ATOM    697  O   PRO A 112     -13.047  54.837  48.382  1.00155.15           O  
ANISOU  697  O   PRO A 112    25748  17100  16100   -487  -1882     -9       O  
ATOM    698  CB  PRO A 112     -12.114  53.054  51.057  1.00 87.09           C  
ANISOU  698  CB  PRO A 112    17640   8199   7248   -398  -2109    -59       C  
ATOM    699  CG  PRO A 112     -11.032  52.789  52.069  1.00106.02           C  
ANISOU  699  CG  PRO A 112    20201  10546   9533   -436  -2343    -44       C  
ATOM    700  CD  PRO A 112     -10.276  54.100  52.153  1.00133.53           C  
ANISOU  700  CD  PRO A 112    23721  14051  12963   -612  -2512     28       C  
ATOM    701  N   ILE A 113     -12.669  56.010  50.290  1.00103.77           N  
ANISOU  701  N   ILE A 113    19815  10255   9358   -628  -2048     26       N  
ATOM    702  CA  ILE A 113     -13.570  57.144  49.971  1.00129.00           C  
ANISOU  702  CA  ILE A 113    23109  13350  12553   -653  -1913     30       C  
ATOM    703  C   ILE A 113     -13.087  57.895  48.748  1.00115.98           C  
ANISOU  703  C   ILE A 113    21177  11899  10990   -767  -1998     88       C  
ATOM    704  O   ILE A 113     -13.890  58.101  47.822  1.00120.92           O  
ANISOU  704  O   ILE A 113    21645  12584  11714   -717  -1832     73       O  
ATOM    705  CB  ILE A 113     -13.781  58.093  51.173  1.00156.25           C  
ANISOU  705  CB  ILE A 113    27012  16521  15834   -699  -1954     34       C  
ATOM    706  CG1 ILE A 113     -14.464  57.380  52.346  1.00131.84           C  
ANISOU  706  CG1 ILE A 113    24201  13242  12647   -575  -1823    -23       C  
ATOM    707  CG2 ILE A 113     -14.560  59.328  50.735  1.00192.95           C  
ANISOU  707  CG2 ILE A 113    31752  21083  20473   -711  -1858     38       C  
ATOM    708  CD1 ILE A 113     -14.994  58.308  53.419  1.00134.28           C  
ANISOU  708  CD1 ILE A 113    24951  13283  12785   -565  -1791    -37       C  
ATOM    709  N   ALA A 114     -11.799  58.224  48.695  1.00105.48           N  
ANISOU  709  N   ALA A 114    19757  10693   9625   -921  -2251    160       N  
ATOM    710  CA  ALA A 114     -11.176  58.883  47.538  1.00123.83           C  
ANISOU  710  CA  ALA A 114    21785  13250  12014  -1062  -2359    235       C  
ATOM    711  C   ALA A 114     -11.201  57.983  46.304  1.00126.47           C  
ANISOU  711  C   ALA A 114    21684  13867  12500   -958  -2256    211       C  
ATOM    712  O   ALA A 114     -11.567  58.425  45.207  1.00114.23           O  
ANISOU  712  O   ALA A 114    19933  12431  11038   -981  -2174    228       O  
ATOM    713  CB  ALA A 114      -9.758  59.277  47.890  1.00122.79           C  
ANISOU  713  CB  ALA A 114    21644  13216  11792  -1255  -2658    328       C  
ATOM    714  N   ALA A 115     -10.775  56.740  46.481  1.00126.66           N  
ANISOU  714  N   ALA A 115    21581  13997  12545   -840  -2279    172       N  
ATOM    715  CA  ALA A 115     -10.616  55.790  45.365  1.00 96.19           C  
ANISOU  715  CA  ALA A 115    17328  10413   8805   -722  -2226    145       C  
ATOM    716  C   ALA A 115     -11.953  55.498  44.698  1.00 79.55           C  
ANISOU  716  C   ALA A 115    15172   8246   6805   -596  -1965     84       C  
ATOM    717  O   ALA A 115     -12.029  55.483  43.465  1.00143.48           O  
ANISOU  717  O   ALA A 115    22966  16545  15004   -580  -1908     91       O  
ATOM    718  CB  ALA A 115      -9.952  54.523  45.844  1.00103.38           C  
ANISOU  718  CB  ALA A 115    18195  11395   9690   -597  -2320    105       C  
ATOM    719  N   VAL A 116     -12.984  55.278  45.499  1.00 59.91           N  
ANISOU  719  N   VAL A 116    12973   5501   4287   -515  -1812     31       N  
ATOM    720  CA  VAL A 116     -14.319  54.932  44.961  1.00 59.60           C  
ANISOU  720  CA  VAL A 116    12890   5413   4341   -400  -1562    -18       C  
ATOM    721  C   VAL A 116     -14.941  56.181  44.352  1.00 67.77           C  
ANISOU  721  C   VAL A 116    13919   6420   5408   -475  -1474     10       C  
ATOM    722  O   VAL A 116     -15.632  56.069  43.323  1.00 94.31           O  
ANISOU  722  O   VAL A 116    17074   9877   8882   -418  -1330     -4       O  
ATOM    723  CB  VAL A 116     -15.226  54.292  46.028  1.00 51.37           C  
ANISOU  723  CB  VAL A 116    12137   4140   3238   -303  -1425    -69       C  
ATOM    724  CG1 VAL A 116     -16.690  54.234  45.602  1.00 46.42           C  
ANISOU  724  CG1 VAL A 116    11496   3458   2681   -224  -1166    -97       C  
ATOM    725  CG2 VAL A 116     -14.719  52.906  46.386  1.00 55.47           C  
ANISOU  725  CG2 VAL A 116    12633   4696   3745   -215  -1506   -102       C  
ATOM    726  N   PHE A 117     -14.714  57.330  44.977  1.00 66.67           N  
ANISOU  726  N   PHE A 117    14023   6141   5165   -594  -1570     50       N  
ATOM    727  CA  PHE A 117     -15.198  58.608  44.430  1.00 70.46           C  
ANISOU  727  CA  PHE A 117    14541   6575   5654   -668  -1531     79       C  
ATOM    728  C   PHE A 117     -14.627  58.775  43.035  1.00 83.20           C  
ANISOU  728  C   PHE A 117    15781   8459   7371   -750  -1599    128       C  
ATOM    729  O   PHE A 117     -15.379  59.013  42.080  1.00117.98           O  
ANISOU  729  O   PHE A 117    20040  12915  11870   -712  -1461    118       O  
ATOM    730  CB  PHE A 117     -14.804  59.784  45.325  1.00 72.03           C  
ANISOU  730  CB  PHE A 117    15083   6580   5703   -799  -1689    122       C  
ATOM    731  CG  PHE A 117     -15.455  61.089  44.945  1.00 71.16           C  
ANISOU  731  CG  PHE A 117    15107   6355   5573   -843  -1650    137       C  
ATOM    732  CD1 PHE A 117     -14.864  61.942  44.026  1.00 68.68           C  
ANISOU  732  CD1 PHE A 117    14643   6166   5285  -1011  -1793    213       C  
ATOM    733  CD2 PHE A 117     -16.674  61.458  45.495  1.00 69.37           C  
ANISOU  733  CD2 PHE A 117    15158   5907   5292   -708  -1472     78       C  
ATOM    734  CE1 PHE A 117     -15.467  63.144  43.683  1.00 75.45           C  
ANISOU  734  CE1 PHE A 117    15659   6894   6114  -1046  -1777    225       C  
ATOM    735  CE2 PHE A 117     -17.275  62.659  45.147  1.00 73.62           C  
ANISOU  735  CE2 PHE A 117    15836   6334   5799   -716  -1448     83       C  
ATOM    736  CZ  PHE A 117     -16.671  63.503  44.244  1.00 75.07           C  
ANISOU  736  CZ  PHE A 117    15901   6610   6011   -886  -1608    155       C  
ATOM    737  N   ALA A 118     -13.312  58.609  42.924  1.00 86.11           N  
ANISOU  737  N   ALA A 118    15983   9016   7716   -854  -1807    182       N  
ATOM    738  CA  ALA A 118     -12.589  58.790  41.655  1.00 97.36           C  
ANISOU  738  CA  ALA A 118    17037  10743   9209   -949  -1894    244       C  
ATOM    739  C   ALA A 118     -13.058  57.785  40.622  1.00 94.52           C  
ANISOU  739  C   ALA A 118    16368  10558   8984   -786  -1733    187       C  
ATOM    740  O   ALA A 118     -13.181  58.171  39.404  1.00 70.20           O  
ANISOU  740  O   ALA A 118    13046   7643   5984   -827  -1692    216       O  
ATOM    741  CB  ALA A 118     -11.106  58.661  41.903  1.00108.45           C  
ANISOU  741  CB  ALA A 118    18323  12342  10542  -1065  -2138    311       C  
ATOM    742  N   SER A 119     -13.411  56.595  41.086  1.00 95.64           N  
ANISOU  742  N   SER A 119    16553  10640   9146   -615  -1643    112       N  
ATOM    743  CA  SER A 119     -13.838  55.488  40.199  1.00 87.72           C  
ANISOU  743  CA  SER A 119    15300   9775   8255   -453  -1515     55       C  
ATOM    744  C   SER A 119     -15.197  55.778  39.591  1.00 73.12           C  
ANISOU  744  C   SER A 119    13455   7830   6495   -408  -1298     29       C  
ATOM    745  O   SER A 119     -15.336  55.719  38.353  1.00 77.20           O  
ANISOU  745  O   SER A 119    13699   8523   7109   -388  -1245     33       O  
ATOM    746  CB  SER A 119     -13.869  54.166  40.928  1.00 91.22           C  
ANISOU  746  CB  SER A 119    15839  10143   8675   -304  -1505     -9       C  
ATOM    747  OG  SER A 119     -12.582  53.813  41.409  1.00 80.10           O  
ANISOU  747  OG  SER A 119    14397   8848   7188   -318  -1713      8       O  
ATOM    748  N   ILE A 120     -16.186  56.038  40.440  1.00 61.85           N  
ANISOU  748  N   ILE A 120    12323   6145   5029   -379  -1174      3       N  
ATOM    749  CA  ILE A 120     -17.588  56.208  39.986  1.00 58.17           C  
ANISOU  749  CA  ILE A 120    11866   5595   4639   -309   -952    -23       C  
ATOM    750  C   ILE A 120     -17.734  57.475  39.148  1.00 68.67           C  
ANISOU  750  C   ILE A 120    13123   6966   6002   -405   -954     18       C  
ATOM    751  O   ILE A 120     -18.585  57.514  38.249  1.00137.14           O  
ANISOU  751  O   ILE A 120    21653  15682  14772   -352   -812      5       O  
ATOM    752  CB  ILE A 120     -18.552  56.219  41.186  1.00 75.45           C  
ANISOU  752  CB  ILE A 120    14383   7532   6749   -247   -822    -55       C  
ATOM    753  CG1 ILE A 120     -20.014  56.194  40.734  1.00 66.48           C  
ANISOU  753  CG1 ILE A 120    13214   6358   5688   -156   -587    -80       C  
ATOM    754  CG2 ILE A 120     -18.258  57.393  42.117  1.00106.25           C  
ANISOU  754  CG2 ILE A 120    18584  11265  10519   -337   -919    -29       C  
ATOM    755  CD1 ILE A 120     -20.994  56.144  41.875  1.00104.17           C  
ANISOU  755  CD1 ILE A 120    18270  10937  10372    -85   -440   -104       C  
ATOM    756  N   TYR A 121     -16.950  58.498  39.450  1.00 74.71           N  
ANISOU  756  N   TYR A 121    14001   7704   6679   -551  -1123     73       N  
ATOM    757  CA  TYR A 121     -17.048  59.779  38.738  1.00 84.20           C  
ANISOU  757  CA  TYR A 121    15189   8912   7888   -666  -1158    123       C  
ATOM    758  C   TYR A 121     -16.278  59.721  37.444  1.00 82.88           C  
ANISOU  758  C   TYR A 121    14657   9035   7796   -751  -1244    173       C  
ATOM    759  O   TYR A 121     -16.546  60.567  36.539  1.00101.15           O  
ANISOU  759  O   TYR A 121    16890  11390  10149   -827  -1234    209       O  
ATOM    760  CB  TYR A 121     -16.570  60.931  39.636  1.00 76.73           C  
ANISOU  760  CB  TYR A 121    14564   7790   6798   -806  -1323    170       C  
ATOM    761  CG  TYR A 121     -17.671  61.463  40.514  1.00 75.62           C  
ANISOU  761  CG  TYR A 121    14783   7362   6585   -707  -1199    120       C  
ATOM    762  CD1 TYR A 121     -17.941  60.898  41.749  1.00 82.72           C  
ANISOU  762  CD1 TYR A 121    15913   8108   7408   -606  -1139     72       C  
ATOM    763  CD2 TYR A 121     -18.502  62.479  40.073  1.00 80.97           C  
ANISOU  763  CD2 TYR A 121    15561   7937   7265   -691  -1128    118       C  
ATOM    764  CE1 TYR A 121     -18.975  61.361  42.547  1.00 80.49           C  
ANISOU  764  CE1 TYR A 121    15943   7596   7042   -495  -1008     26       C  
ATOM    765  CE2 TYR A 121     -19.546  62.948  40.852  1.00 76.81           C  
ANISOU  765  CE2 TYR A 121    15348   7176   6659   -560  -1003     65       C  
ATOM    766  CZ  TYR A 121     -19.779  62.392  42.095  1.00 72.08           C  
ANISOU  766  CZ  TYR A 121    14963   6447   5974   -461   -938     20       C  
ATOM    767  OH  TYR A 121     -20.815  62.858  42.850  1.00 79.51           O  
ANISOU  767  OH  TYR A 121    16198   7192   6821   -318   -803    -30       O  
ATOM    768  N   SER A 122     -15.394  58.744  37.307  1.00 69.00           N  
ANISOU  768  N   SER A 122    12683   7480   6052   -725  -1322    172       N  
ATOM    769  CA  SER A 122     -14.761  58.408  36.019  1.00 55.39           C  
ANISOU  769  CA  SER A 122    10572   6073   4399   -742  -1365    201       C  
ATOM    770  C   SER A 122     -15.803  57.722  35.158  1.00 48.75           C  
ANISOU  770  C   SER A 122     9581   5255   3684   -584  -1164    137       C  
ATOM    771  O   SER A 122     -15.903  58.075  33.922  1.00 64.09           O  
ANISOU  771  O   SER A 122    11296   7355   5697   -623  -1135    165       O  
ATOM    772  CB  SER A 122     -13.573  57.485  36.213  1.00 52.40           C  
ANISOU  772  CB  SER A 122    10027   5901   3979   -708  -1501    203       C  
ATOM    773  OG  SER A 122     -12.628  58.029  37.118  1.00 52.37           O  
ANISOU  773  OG  SER A 122    10170   5871   3856   -854  -1693    265       O  
ATOM    774  N   MET A 123     -16.604  56.867  35.793  1.00 42.68           N  
ANISOU  774  N   MET A 123     8955   4325   2936   -434  -1035     66       N  
ATOM    775  CA  MET A 123     -17.681  56.128  35.110  1.00 44.71           C  
ANISOU  775  CA  MET A 123     9103   4580   3304   -296   -851     12       C  
ATOM    776  C   MET A 123     -18.827  57.066  34.754  1.00 44.63           C  
ANISOU  776  C   MET A 123     9168   4447   3341   -319   -711     20       C  
ATOM    777  O   MET A 123     -19.524  56.819  33.740  1.00 73.29           O  
ANISOU  777  O   MET A 123    12618   8151   7075   -260   -596      5       O  
ATOM    778  CB  MET A 123     -18.247  54.971  35.944  1.00 51.57           C  
ANISOU  778  CB  MET A 123    10120   5308   4163   -163   -764    -47       C  
ATOM    779  CG  MET A 123     -17.202  53.968  36.399  1.00 66.40           C  
ANISOU  779  CG  MET A 123    11972   7271   5987   -110   -907    -67       C  
ATOM    780  SD  MET A 123     -17.893  52.406  37.038  1.00 81.06           S  
ANISOU  780  SD  MET A 123    13966   8987   7844     44   -821   -134       S  
ATOM    781  CE  MET A 123     -19.299  53.008  37.972  1.00 85.99           C  
ANISOU  781  CE  MET A 123    14887   9341   8442     12   -634   -129       C  
ATOM    782  N   THR A 124     -19.052  58.086  35.576  1.00 38.19           N  
ANISOU  782  N   THR A 124     8624   3441   2443   -385   -726     39       N  
ATOM    783  CA  THR A 124     -20.054  59.122  35.302  1.00 42.48           C  
ANISOU  783  CA  THR A 124     9272   3863   3005   -390   -622     43       C  
ATOM    784  C   THR A 124     -19.649  59.912  34.076  1.00 36.47           C  
ANISOU  784  C   THR A 124     8315   3252   2289   -506   -703     97       C  
ATOM    785  O   THR A 124     -20.500  60.247  33.229  1.00 36.87           O  
ANISOU  785  O   THR A 124     8280   3308   2420   -470   -593     90       O  
ATOM    786  CB  THR A 124     -20.273  60.073  36.489  1.00 58.57           C  
ANISOU  786  CB  THR A 124    11680   5659   4916   -416   -649     45       C  
ATOM    787  OG1 THR A 124     -20.434  59.310  37.686  1.00 60.51           O  
ANISOU  787  OG1 THR A 124    12104   5789   5098   -331   -599      6       O  
ATOM    788  CG2 THR A 124     -21.497  60.951  36.317  1.00 58.25           C  
ANISOU  788  CG2 THR A 124    11767   5482   4883   -348   -513     28       C  
ATOM    789  N   ALA A 125     -18.366  60.230  34.017  1.00 34.12           N  
ANISOU  789  N   ALA A 125     7952   3080   1930   -654   -900    157       N  
ATOM    790  CA  ALA A 125     -17.712  60.997  32.951  1.00 32.23           C  
ANISOU  790  CA  ALA A 125     7525   3019   1700   -814  -1019    232       C  
ATOM    791  C   ALA A 125     -17.981  60.287  31.632  1.00 33.11           C  
ANISOU  791  C   ALA A 125     7300   3342   1937   -732   -916    212       C  
ATOM    792  O   ALA A 125     -18.288  60.954  30.604  1.00 34.40           O  
ANISOU  792  O   ALA A 125     7355   3565   2150   -793   -897    244       O  
ATOM    793  CB  ALA A 125     -16.224  61.130  33.188  1.00 31.63           C  
ANISOU  793  CB  ALA A 125     7382   3104   1531   -977  -1240    306       C  
ATOM    794  N   VAL A 126     -17.853  58.964  31.664  1.00 33.47           N  
ANISOU  794  N   VAL A 126     7205   3487   2023   -596   -866    159       N  
ATOM    795  CA  VAL A 126     -18.065  58.200  30.413  1.00 40.64           C  
ANISOU  795  CA  VAL A 126     7813   4590   3038   -503   -784    134       C  
ATOM    796  C   VAL A 126     -19.527  58.260  30.051  1.00 36.74           C  
ANISOU  796  C   VAL A 126     7371   3949   2638   -414   -597     95       C  
ATOM    797  O   VAL A 126     -19.808  58.440  28.847  1.00 39.07           O  
ANISOU  797  O   VAL A 126     7473   4361   3010   -423   -555    108       O  
ATOM    798  CB  VAL A 126     -17.511  56.760  30.398  1.00 43.48           C  
ANISOU  798  CB  VAL A 126     8015   5099   3404   -368   -805     86       C  
ATOM    799  CG1 VAL A 126     -16.016  56.709  30.685  1.00 44.46           C  
ANISOU  799  CG1 VAL A 126     8046   5416   3429   -440   -996    128       C  
ATOM    800  CG2 VAL A 126     -18.277  55.839  31.322  1.00 45.28           C  
ANISOU  800  CG2 VAL A 126     8439   5123   3643   -228   -703     17       C  
ATOM    801  N   ALA A 127     -20.412  58.166  31.033  1.00 33.07           N  
ANISOU  801  N   ALA A 127     7150   3254   2159   -337   -492     55       N  
ATOM    802  CA  ALA A 127     -21.864  58.133  30.768  1.00 39.11           C  
ANISOU  802  CA  ALA A 127     7946   3907   3006   -239   -303     23       C  
ATOM    803  C   ALA A 127     -22.308  59.399  30.030  1.00 46.08           C  
ANISOU  803  C   ALA A 127     8826   4767   3915   -308   -291     57       C  
ATOM    804  O   ALA A 127     -23.214  59.355  29.149  1.00 88.67           O  
ANISOU  804  O   ALA A 127    14094  10188   9406   -249   -173     45       O  
ATOM    805  CB  ALA A 127     -22.563  57.947  32.090  1.00 39.82           C  
ANISOU  805  CB  ALA A 127     8304   3787   3038   -165   -212     -9       C  
ATOM    806  N   PHE A 128     -21.599  60.491  30.331  1.00 44.16           N  
ANISOU  806  N   PHE A 128     8716   4482   3579   -444   -435    104       N  
ATOM    807  CA  PHE A 128     -21.974  61.798  29.730  1.00 67.02           C  
ANISOU  807  CA  PHE A 128    11673   7317   6473   -521   -458    140       C  
ATOM    808  C   PHE A 128     -21.194  62.078  28.459  1.00 81.84           C  
ANISOU  808  C   PHE A 128    13294   9416   8382   -658   -567    201       C  
ATOM    809  O   PHE A 128     -21.757  62.827  27.621  1.00 92.10           O  
ANISOU  809  O   PHE A 128    14570  10698   9725   -685   -541    220       O  
ATOM    810  CB  PHE A 128     -21.802  62.917  30.768  1.00 65.39           C  
ANISOU  810  CB  PHE A 128    11812   6898   6132   -594   -562    161       C  
ATOM    811  CG  PHE A 128     -23.062  63.240  31.536  1.00 82.32           C  
ANISOU  811  CG  PHE A 128    14216   8812   8250   -439   -416    104       C  
ATOM    812  CD1 PHE A 128     -24.243  63.539  30.870  1.00 76.53           C  
ANISOU  812  CD1 PHE A 128    13438   8047   7592   -332   -276     79       C  
ATOM    813  CD2 PHE A 128     -23.073  63.243  32.922  1.00 79.15           C  
ANISOU  813  CD2 PHE A 128    14092   8241   7738   -389   -418     77       C  
ATOM    814  CE1 PHE A 128     -25.411  63.820  31.564  1.00 62.50           C  
ANISOU  814  CE1 PHE A 128    11867   6101   5778   -169   -134     29       C  
ATOM    815  CE2 PHE A 128     -24.236  63.535  33.618  1.00 80.84           C  
ANISOU  815  CE2 PHE A 128    14527   8278   7909   -229   -273     25       C  
ATOM    816  CZ  PHE A 128     -25.404  63.817  32.940  1.00 88.58           C  
ANISOU  816  CZ  PHE A 128    15438   9255   8961   -114   -128      2       C  
ATOM    817  N   ASP A 129     -20.082  61.370  28.283  1.00 72.87           N  
ANISOU  817  N   ASP A 129    11960   8495   7232   -707   -660    223       N  
ATOM    818  CA  ASP A 129     -19.351  61.439  27.009  1.00 54.98           C  
ANISOU  818  CA  ASP A 129     9398   6498   4990   -810   -738    279       C  
ATOM    819  C   ASP A 129     -20.202  60.776  25.945  1.00 50.83           C  
ANISOU  819  C   ASP A 129     8671   6048   4594   -677   -585    232       C  
ATOM    820  O   ASP A 129     -20.285  61.255  24.828  1.00 85.93           O  
ANISOU  820  O   ASP A 129    12970  10599   9078   -743   -591    268       O  
ATOM    821  CB  ASP A 129     -17.967  60.804  27.142  1.00 62.43           C  
ANISOU  821  CB  ASP A 129    10170   7680   5870   -859   -868    308       C  
ATOM    822  CG  ASP A 129     -17.318  60.609  25.787  1.00 62.65           C  
ANISOU  822  CG  ASP A 129     9850   8033   5921   -907   -907    350       C  
ATOM    823  OD1 ASP A 129     -17.345  61.565  24.994  1.00 59.39           O  
ANISOU  823  OD1 ASP A 129     9392   7666   5506  -1052   -948    416       O  
ATOM    824  OD2 ASP A 129     -16.824  59.497  25.526  1.00 76.73           O  
ANISOU  824  OD2 ASP A 129    11423  10014   7717   -788   -898    313       O  
ATOM    825  N   ARG A 130     -20.842  59.695  26.330  1.00 45.13           N  
ANISOU  825  N   ARG A 130     7961   5258   3927   -504   -460    158       N  
ATOM    826  CA  ARG A 130     -21.743  58.952  25.422  1.00 46.82           C  
ANISOU  826  CA  ARG A 130     8012   5516   4260   -377   -320    114       C  
ATOM    827  C   ARG A 130     -23.055  59.712  25.278  1.00 47.34           C  
ANISOU  827  C   ARG A 130     8199   5403   4382   -353   -203    109       C  
ATOM    828  O   ARG A 130     -23.628  59.694  24.184  1.00 72.16           O  
ANISOU  828  O   ARG A 130    11187   8614   7614   -328   -138    108       O  
ATOM    829  CB  ARG A 130     -21.953  57.527  25.943  1.00 51.07           C  
ANISOU  829  CB  ARG A 130     8550   6031   4821   -226   -253     51       C  
ATOM    830  CG  ARG A 130     -20.713  56.642  25.855  1.00 55.13           C  
ANISOU  830  CG  ARG A 130     8911   6748   5286   -200   -368     42       C  
ATOM    831  CD  ARG A 130     -20.215  56.431  24.434  1.00 60.51           C  
ANISOU  831  CD  ARG A 130     9298   7691   6000   -196   -405     55       C  
ATOM    832  NE  ARG A 130     -19.281  57.455  23.968  1.00 60.80           N  
ANISOU  832  NE  ARG A 130     9226   7898   5974   -362   -523    132       N  
ATOM    833  CZ  ARG A 130     -19.042  57.760  22.688  1.00 88.41           C  
ANISOU  833  CZ  ARG A 130    12498  11601   9493   -415   -540    169       C  
ATOM    834  NH1 ARG A 130     -19.666  57.124  21.707  1.00 88.07           N  
ANISOU  834  NH1 ARG A 130    12316  11609   9536   -301   -447    127       N  
ATOM    835  NH2 ARG A 130     -18.163  58.702  22.386  1.00102.23           N  
ANISOU  835  NH2 ARG A 130    14166  13507  11167   -597   -658    255       N  
ATOM    836  N   TYR A 131     -23.520  60.355  26.329  1.00 51.43           N  
ANISOU  836  N   TYR A 131     8987   5710   4844   -347   -179    102       N  
ATOM    837  CA  TYR A 131     -24.721  61.191  26.234  1.00 58.84           C  
ANISOU  837  CA  TYR A 131    10051   6493   5812   -300    -80     94       C  
ATOM    838  C   TYR A 131     -24.526  62.236  25.140  1.00 63.90           C  
ANISOU  838  C   TYR A 131    10618   7195   6465   -416   -165    144       C  
ATOM    839  O   TYR A 131     -25.349  62.353  24.219  1.00 37.75           O  
ANISOU  839  O   TYR A 131     7197   3903   3242   -367    -81    138       O  
ATOM    840  CB  TYR A 131     -25.064  61.824  27.574  1.00 52.54           C  
ANISOU  840  CB  TYR A 131     9574   5473   4913   -265    -68     78       C  
ATOM    841  CG  TYR A 131     -26.252  62.736  27.478  1.00 53.29           C  
ANISOU  841  CG  TYR A 131     9802   5426   5017   -184     23     64       C  
ATOM    842  CD1 TYR A 131     -27.545  62.243  27.511  1.00 40.78           C  
ANISOU  842  CD1 TYR A 131     8178   3814   3501    -27    213     25       C  
ATOM    843  CD2 TYR A 131     -26.071  64.095  27.293  1.00 70.57           C  
ANISOU  843  CD2 TYR A 131    12150   7521   7140   -268    -93     95       C  
ATOM    844  CE1 TYR A 131     -28.633  63.091  27.411  1.00 42.53           C  
ANISOU  844  CE1 TYR A 131     8501   3934   3722     70    296     10       C  
ATOM    845  CE2 TYR A 131     -27.147  64.954  27.192  1.00 67.24           C  
ANISOU  845  CE2 TYR A 131    11867   6965   6714   -165    -24     73       C  
ATOM    846  CZ  TYR A 131     -28.432  64.451  27.250  1.00 53.35           C  
ANISOU  846  CZ  TYR A 131    10047   5198   5023     17    176     27       C  
ATOM    847  OH  TYR A 131     -29.477  65.320  27.133  1.00 50.18           O  
ANISOU  847  OH  TYR A 131     9765   4691   4609    140    240      5       O  
ATOM    848  N   MET A 132     -23.457  63.007  25.254  1.00 64.22           N  
ANISOU  848  N   MET A 132    10726   7263   6409   -582   -340    202       N  
ATOM    849  CA  MET A 132     -23.154  64.042  24.234  1.00 64.13           C  
ANISOU  849  CA  MET A 132    10662   7315   6387   -734   -449    268       C  
ATOM    850  C   MET A 132     -22.922  63.450  22.858  1.00 43.19           C  
ANISOU  850  C   MET A 132     7672   4914   3822   -752   -427    285       C  
ATOM    851  O   MET A 132     -23.481  63.939  21.914  1.00 23.47           O  
ANISOU  851  O   MET A 132     5116   2420   1379   -765   -401    298       O  
ATOM    852  CB  MET A 132     -21.908  64.828  24.642  1.00 68.53           C  
ANISOU  852  CB  MET A 132    11332   7894   6811   -947   -661    347       C  
ATOM    853  CG  MET A 132     -22.235  65.968  25.573  1.00 64.54           C  
ANISOU  853  CG  MET A 132    11209   7107   6204   -973   -730    350       C  
ATOM    854  SD  MET A 132     -20.796  67.007  25.848  1.00110.83           S  
ANISOU  854  SD  MET A 132    17210  12991  11906  -1275  -1016    467       S  
ATOM    855  CE  MET A 132     -19.504  65.773  26.009  1.00101.19           C  
ANISOU  855  CE  MET A 132    15695  12070  10682  -1322  -1053    489       C  
ATOM    856  N   ALA A 133     -22.147  62.395  22.739  1.00 37.43           N  
ANISOU  856  N   ALA A 133     6735   4386   3099   -734   -439    277       N  
ATOM    857  CA  ALA A 133     -21.776  61.787  21.456  1.00 37.79           C  
ANISOU  857  CA  ALA A 133     6464   4693   3199   -733   -433    289       C  
ATOM    858  C   ALA A 133     -23.029  61.326  20.695  1.00 27.37           C  
ANISOU  858  C   ALA A 133     5063   3325   2009   -590   -276    236       C  
ATOM    859  O   ALA A 133     -23.160  61.418  19.437  1.00 19.03           O  
ANISOU  859  O   ALA A 133     3825   2397   1006   -614   -266    255       O  
ATOM    860  CB  ALA A 133     -20.844  60.620  21.716  1.00 35.72           C  
ANISOU  860  CB  ALA A 133     6049   4616   2905   -673   -466    266       C  
ATOM    861  N   ILE A 134     -24.020  60.894  21.441  1.00 20.21           N  
ANISOU  861  N   ILE A 134     4295   2234   1149   -451   -154    177       N  
ATOM    862  CA  ILE A 134     -25.234  60.265  20.844  1.00 24.44           C  
ANISOU  862  CA  ILE A 134     4742   2738   1804   -316     -5    134       C  
ATOM    863  C   ILE A 134     -26.341  61.301  20.666  1.00 34.61           C  
ANISOU  863  C   ILE A 134     6151   3869   3130   -307     56    141       C  
ATOM    864  O   ILE A 134     -26.944  61.426  19.537  1.00 96.39           O  
ANISOU  864  O   ILE A 134    13843  11743  11038   -294     98    148       O  
ATOM    865  CB  ILE A 134     -25.748  59.088  21.714  1.00 24.23           C  
ANISOU  865  CB  ILE A 134     4773   2630   1801   -179     95     78       C  
ATOM    866  CG1 ILE A 134     -24.780  57.901  21.741  1.00 30.99           C  
ANISOU  866  CG1 ILE A 134     5508   3636   2629   -146     32     57       C  
ATOM    867  CG2 ILE A 134     -27.142  58.633  21.295  1.00 21.78           C  
ANISOU  867  CG2 ILE A 134     4416   2259   1598    -73    242     53       C  
ATOM    868  CD1 ILE A 134     -24.427  57.364  20.375  1.00 43.21           C  
ANISOU  868  CD1 ILE A 134     6802   5393   4222   -129      4     56       C  
ATOM    869  N   ILE A 135     -26.563  62.106  21.714  1.00 31.38           N  
ANISOU  869  N   ILE A 135     5999   3275   2648   -309     46    140       N  
ATOM    870  CA  ILE A 135     -27.708  63.046  21.774  1.00 35.17           C  
ANISOU  870  CA  ILE A 135     6636   3585   3141   -243    112    131       C  
ATOM    871  C   ILE A 135     -27.331  64.370  21.121  1.00 34.27           C  
ANISOU  871  C   ILE A 135     6590   3449   2980   -377    -23    182       C  
ATOM    872  O   ILE A 135     -28.194  64.946  20.348  1.00 27.09           O  
ANISOU  872  O   ILE A 135     5668   2496   2128   -335     14    182       O  
ATOM    873  CB  ILE A 135     -28.187  63.291  23.218  1.00 45.72           C  
ANISOU  873  CB  ILE A 135     8240   4731   4399   -148    169     97       C  
ATOM    874  CG1 ILE A 135     -28.587  61.992  23.922  1.00 44.08           C  
ANISOU  874  CG1 ILE A 135     7983   4540   4222    -39    299     59       C  
ATOM    875  CG2 ILE A 135     -29.311  64.322  23.217  1.00 59.26           C  
ANISOU  875  CG2 ILE A 135    10111   6295   6107    -50    226     82       C  
ATOM    876  CD1 ILE A 135     -29.655  61.212  23.189  1.00 37.63           C  
ANISOU  876  CD1 ILE A 135     6971   3795   3530     55    441     45       C  
ATOM    877  N   HIS A 136     -26.114  64.870  21.422  1.00 29.41           N  
ANISOU  877  N   HIS A 136     6055   2859   2257   -542   -189    231       N  
ATOM    878  CA  HIS A 136     -25.611  66.113  20.819  1.00 35.87           C  
ANISOU  878  CA  HIS A 136     6950   3667   3010   -720   -352    301       C  
ATOM    879  C   HIS A 136     -24.297  65.917  20.072  1.00 39.10           C  
ANISOU  879  C   HIS A 136     7135   4330   3389   -913   -477    374       C  
ATOM    880  O   HIS A 136     -23.274  66.490  20.465  1.00 47.23           O  
ANISOU  880  O   HIS A 136     8260   5380   4304  -1090   -640    439       O  
ATOM    881  CB  HIS A 136     -25.485  67.213  21.894  1.00 41.69           C  
ANISOU  881  CB  HIS A 136     8053   4173   3614   -767   -465    313       C  
ATOM    882  CG  HIS A 136     -26.773  67.540  22.573  1.00 42.22           C  
ANISOU  882  CG  HIS A 136     8344   4014   3683   -557   -345    242       C  
ATOM    883  ND1 HIS A 136     -27.011  67.234  23.899  1.00 42.71           N  
ANISOU  883  ND1 HIS A 136     8582   3954   3691   -435   -275    191       N  
ATOM    884  CD2 HIS A 136     -27.903  68.117  22.111  1.00 53.01           C  
ANISOU  884  CD2 HIS A 136     9772   5276   5091   -435   -278    213       C  
ATOM    885  CE1 HIS A 136     -28.225  67.624  24.228  1.00 43.86           C  
ANISOU  885  CE1 HIS A 136     8880   3947   3836   -244   -164    136       C  
ATOM    886  NE2 HIS A 136     -28.794  68.166  23.149  1.00 52.99           N  
ANISOU  886  NE2 HIS A 136     9967   5112   5053   -233   -165    147       N  
ATOM    887  N   PRO A 137     -24.282  65.102  18.999  1.00 31.03           N  
ANISOU  887  N   PRO A 137     5811   3519   2458   -881   -409    369       N  
ATOM    888  CA  PRO A 137     -23.043  64.695  18.343  1.00 33.09           C  
ANISOU  888  CA  PRO A 137     5822   4069   2681  -1010   -498    424       C  
ATOM    889  C   PRO A 137     -22.242  65.815  17.698  1.00 33.21           C  
ANISOU  889  C   PRO A 137     5835   4181   2603  -1262   -671    533       C  
ATOM    890  O   PRO A 137     -21.075  65.606  17.388  1.00 28.90           O  
ANISOU  890  O   PRO A 137     5099   3892   1988  -1394   -763    595       O  
ATOM    891  CB  PRO A 137     -23.522  63.739  17.245  1.00 26.37           C  
ANISOU  891  CB  PRO A 137     4706   3367   1945   -886   -377    382       C  
ATOM    892  CG  PRO A 137     -24.918  64.222  16.950  1.00 27.72           C  
ANISOU  892  CG  PRO A 137     4990   3337   2203   -795   -283    350       C  
ATOM    893  CD  PRO A 137     -25.473  64.619  18.299  1.00 25.18           C  
ANISOU  893  CD  PRO A 137     4959   2758   1847   -721   -255    315       C  
ATOM    894  N   LEU A 138     -22.864  66.982  17.556  1.00 41.50           N  
ANISOU  894  N   LEU A 138     7101   5028   3637  -1323   -721    557       N  
ATOM    895  CA  LEU A 138     -22.251  68.147  16.875  1.00 83.35           C  
ANISOU  895  CA  LEU A 138    12444  10380   8843  -1583   -902    670       C  
ATOM    896  C   LEU A 138     -21.190  68.849  17.724  1.00116.80           C  
ANISOU  896  C   LEU A 138    16859  14592  12926  -1800  -1095    754       C  
ATOM    897  O   LEU A 138     -20.241  69.425  17.136  1.00129.99           O  
ANISOU  897  O   LEU A 138    18446  16442  14501  -2063  -1256    874       O  
ATOM    898  CB  LEU A 138     -23.372  69.114  16.492  1.00110.09           C  
ANISOU  898  CB  LEU A 138    16043  13521  12262  -1543   -899    655       C  
ATOM    899  CG  LEU A 138     -24.177  68.681  15.270  1.00135.09           C  
ANISOU  899  CG  LEU A 138    18994  16774  15558  -1429   -770    619       C  
ATOM    900  CD1 LEU A 138     -25.652  69.008  15.440  1.00150.56           C  
ANISOU  900  CD1 LEU A 138    21142  18468  17597  -1223   -666    539       C  
ATOM    901  CD2 LEU A 138     -23.616  69.308  13.999  1.00118.22           C  
ANISOU  901  CD2 LEU A 138    16734  14806  13375  -1655   -892    721       C  
ATOM    902  N   GLN A 139     -21.287  68.765  19.054  1.00105.13           N  
ANISOU  902  N   GLN A 139    15605  12923  11414  -1710  -1088    704       N  
ATOM    903  CA  GLN A 139     -20.248  69.340  19.922  1.00105.55           C  
ANISOU  903  CA  GLN A 139    15832  12952  11320  -1915  -1280    784       C  
ATOM    904  C   GLN A 139     -19.393  68.246  20.552  1.00137.79           C  
ANISOU  904  C   GLN A 139    19727  17232  15393  -1875  -1251    769       C  
ATOM    905  O   GLN A 139     -19.809  67.556  21.478  1.00254.73           O  
ANISOU  905  O   GLN A 139    34621  31919  30243  -1677  -1140    675       O  
ATOM    906  CB  GLN A 139     -20.809  70.330  20.944  1.00 99.80           C  
ANISOU  906  CB  GLN A 139    15555  11848  10515  -1892  -1356    760       C  
ATOM    907  CG  GLN A 139     -22.022  69.839  21.714  1.00105.71           C  
ANISOU  907  CG  GLN A 139    16441  12379  11345  -1576  -1159    623       C  
ATOM    908  CD  GLN A 139     -22.506  70.873  22.703  1.00100.31           C  
ANISOU  908  CD  GLN A 139    16207  11349  10556  -1537  -1242    599       C  
ATOM    909  OE1 GLN A 139     -21.725  71.640  23.271  1.00 72.71           O  
ANISOU  909  OE1 GLN A 139    12945   7762   6919  -1732  -1449    671       O  
ATOM    910  NE2 GLN A 139     -23.811  70.889  22.925  1.00 82.12           N  
ANISOU  910  NE2 GLN A 139    14031   8857   8310  -1278  -1086    499       N  
ATOM    911  N   PRO A 140     -18.152  68.055  20.056  1.00130.36           N  
ANISOU  911  N   PRO A 140    18522  16621  14388  -2062  -1357    865       N  
ATOM    912  CA  PRO A 140     -17.208  67.138  20.691  1.00159.90           C  
ANISOU  912  CA  PRO A 140    22100  20559  18092  -2034  -1368    861       C  
ATOM    913  C   PRO A 140     -16.494  67.815  21.860  1.00117.93           C  
ANISOU  913  C   PRO A 140    17045  15121  12642  -2210  -1552    927       C  
ATOM    914  O   PRO A 140     -15.322  68.189  21.733  1.00140.58           O  
ANISOU  914  O   PRO A 140    19804  18212  15396  -2464  -1728   1054       O  
ATOM    915  CB  PRO A 140     -16.258  66.784  19.532  1.00153.37           C  
ANISOU  915  CB  PRO A 140    20872  20162  17239  -2149  -1404    941       C  
ATOM    916  CG  PRO A 140     -16.232  68.033  18.677  1.00107.17           C  
ANISOU  916  CG  PRO A 140    15078  14311  11328  -2407  -1528   1056       C  
ATOM    917  CD  PRO A 140     -17.602  68.665  18.835  1.00121.15           C  
ANISOU  917  CD  PRO A 140    17178  15681  13171  -2297  -1464    983       C  
ATOM    918  N   ARG A 141     -17.209  67.963  22.970  1.00 97.41           N  
ANISOU  918  N   ARG A 141    14780  12182  10048  -2078  -1513    848       N  
ATOM    919  CA  ARG A 141     -16.806  68.904  24.052  1.00147.39           C  
ANISOU  919  CA  ARG A 141    21468  18292  16240  -2244  -1702    906       C  
ATOM    920  C   ARG A 141     -15.432  68.591  24.627  1.00146.55           C  
ANISOU  920  C   ARG A 141    21246  18402  16034  -2402  -1846    985       C  
ATOM    921  O   ARG A 141     -14.699  69.561  24.930  1.00198.17           O  
ANISOU  921  O   ARG A 141    27955  24905  22433  -2680  -2075   1105       O  
ATOM    922  CB  ARG A 141     -17.858  68.897  25.161  1.00179.79           C  
ANISOU  922  CB  ARG A 141    25915  22031  20366  -2012  -1594    786       C  
ATOM    923  CG  ARG A 141     -17.662  69.941  26.250  1.00189.41           C  
ANISOU  923  CG  ARG A 141    27565  22964  21436  -2137  -1778    824       C  
ATOM    924  CD  ARG A 141     -18.811  69.889  27.239  1.00169.10           C  
ANISOU  924  CD  ARG A 141    25302  20065  18882  -1867  -1638    695       C  
ATOM    925  NE  ARG A 141     -20.035  70.434  26.658  1.00153.77           N  
ANISOU  925  NE  ARG A 141    23471  17957  16997  -1730  -1538    641       N  
ATOM    926  CZ  ARG A 141     -20.546  71.637  26.921  1.00139.34           C  
ANISOU  926  CZ  ARG A 141    22028  15839  15075  -1741  -1641    641       C  
ATOM    927  NH1 ARG A 141     -19.959  72.454  27.782  1.00113.24           N  
ANISOU  927  NH1 ARG A 141    19066  12349  11608  -1893  -1855    694       N  
ATOM    928  NH2 ARG A 141     -21.661  72.019  26.321  1.00141.53           N  
ANISOU  928  NH2 ARG A 141    22357  16002  15413  -1587  -1539    586       N  
ATOM    929  N   LEU A 142     -15.103  67.305  24.774  1.00107.96           N  
ANISOU  929  N   LEU A 142    16095  13720  11205  -2234  -1734    923       N  
ATOM    930  CA  LEU A 142     -13.924  66.871  25.537  1.00 96.86           C  
ANISOU  930  CA  LEU A 142    14608  12482   9710  -2314  -1853    970       C  
ATOM    931  C   LEU A 142     -12.731  66.605  24.626  1.00 77.94           C  
ANISOU  931  C   LEU A 142    11795  10549   7266  -2470  -1938   1077       C  
ATOM    932  O   LEU A 142     -12.683  65.579  23.954  1.00 74.52           O  
ANISOU  932  O   LEU A 142    11039  10366   6909  -2293  -1806   1020       O  
ATOM    933  CB  LEU A 142     -14.300  65.621  26.339  1.00123.65           C  
ANISOU  933  CB  LEU A 142    18003  15799  13177  -2017  -1694    833       C  
ATOM    934  CG  LEU A 142     -15.540  65.767  27.221  1.00125.28           C  
ANISOU  934  CG  LEU A 142    18579  15596  13425  -1841  -1578    726       C  
ATOM    935  CD1 LEU A 142     -15.795  64.499  28.021  1.00133.81           C  
ANISOU  935  CD1 LEU A 142    19649  16634  14559  -1591  -1440    613       C  
ATOM    936  CD2 LEU A 142     -15.416  66.970  28.145  1.00103.18           C  
ANISOU  936  CD2 LEU A 142    16181  12525  10497  -2012  -1751    783       C  
ATOM    937  N   SER A 143     -11.722  67.456  24.759  1.00 86.53           N  
ANISOU  937  N   SER A 143    12908  11754   8214  -2789  -2167   1230       N  
ATOM    938  CA  SER A 143     -10.402  67.259  24.132  1.00 95.39           C  
ANISOU  938  CA  SER A 143    13633  13359   9251  -2969  -2277   1357       C  
ATOM    939  C   SER A 143      -9.535  66.388  25.028  1.00113.03           C  
ANISOU  939  C   SER A 143    15753  15752  11441  -2881  -2317   1338       C  
ATOM    940  O   SER A 143      -9.959  66.032  26.139  1.00160.61           O  
ANISOU  940  O   SER A 143    22040  21485  17497  -2716  -2274   1236       O  
ATOM    941  CB  SER A 143      -9.736  68.588  23.823  1.00 83.65           C  
ANISOU  941  CB  SER A 143    12214  11944   7622  -3384  -2516   1551       C  
ATOM    942  OG  SER A 143      -9.391  69.292  25.010  1.00 70.34           O  
ANISOU  942  OG  SER A 143    10878  10017   5829  -3565  -2713   1612       O  
ATOM    943  N   ALA A 144      -8.329  66.104  24.571  1.00 99.25           N  
ANISOU  943  N   ALA A 144    13629  14469   9610  -2998  -2408   1441       N  
ATOM    944  CA  ALA A 144      -7.399  65.176  25.246  1.00111.73           C  
ANISOU  944  CA  ALA A 144    15026  16283  11143  -2887  -2448   1424       C  
ATOM    945  C   ALA A 144      -6.872  65.778  26.546  1.00131.12           C  
ANISOU  945  C   ALA A 144    17773  18553  13493  -3088  -2652   1500       C  
ATOM    946  O   ALA A 144      -6.936  65.133  27.644  1.00117.95           O  
ANISOU  946  O   ALA A 144    16266  16705  11845  -2903  -2629   1401       O  
ATOM    947  CB  ALA A 144      -6.268  64.834  24.306  1.00 97.42           C  
ANISOU  947  CB  ALA A 144    12714  15052   9249  -2959  -2494   1526       C  
ATOM    948  N   THR A 145      -6.465  67.039  26.424  1.00133.37           N  
ANISOU  948  N   THR A 145    18170  18837  13666  -3467  -2852   1669       N  
ATOM    949  CA  THR A 145      -6.078  67.925  27.541  1.00135.05           C  
ANISOU  949  CA  THR A 145    18740  18808  13762  -3727  -3084   1765       C  
ATOM    950  C   THR A 145      -7.210  68.027  28.543  1.00119.50           C  
ANISOU  950  C   THR A 145    17262  16281  11860  -3537  -3002   1618       C  
ATOM    951  O   THR A 145      -6.961  67.774  29.751  1.00111.26           O  
ANISOU  951  O   THR A 145    16414  15082  10776  -3486  -3067   1584       O  
ATOM    952  CB  THR A 145      -5.706  69.331  27.046  1.00134.07           C  
ANISOU  952  CB  THR A 145    18711  18714  13515  -4165  -3305   1964       C  
ATOM    953  OG1 THR A 145      -4.512  69.220  26.272  1.00188.36           O  
ANISOU  953  OG1 THR A 145    25113  26157  20298  -4370  -3398   2123       O  
ATOM    954  CG2 THR A 145      -5.487  70.332  28.162  1.00103.19           C  
ANISOU  954  CG2 THR A 145    15255  14471   9480  -4427  -3554   2052       C  
ATOM    955  N   ALA A 146      -8.405  68.411  28.070  1.00117.67           N  
ANISOU  955  N   ALA A 146    17221  15770  11717  -3436  -2868   1539       N  
ATOM    956  CA  ALA A 146      -9.551  68.594  28.976  1.00121.81           C  
ANISOU  956  CA  ALA A 146    18204  15788  12289  -3248  -2780   1406       C  
ATOM    957  C   ALA A 146      -9.793  67.306  29.758  1.00117.75           C  
ANISOU  957  C   ALA A 146    17653  15229  11855  -2916  -2613   1254       C  
ATOM    958  O   ALA A 146     -10.127  67.363  30.939  1.00120.62           O  
ANISOU  958  O   ALA A 146    18365  15273  12190  -2837  -2627   1191       O  
ATOM    959  CB  ALA A 146     -10.764  69.010  28.175  1.00145.74           C  
ANISOU  959  CB  ALA A 146    21337  18624  15413  -3148  -2636   1341       C  
ATOM    960  N   THR A 147      -9.632  66.162  29.095  1.00117.89           N  
ANISOU  960  N   THR A 147    17271  15559  11961  -2722  -2465   1196       N  
ATOM    961  CA  THR A 147      -9.861  64.857  29.725  1.00123.42           C  
ANISOU  961  CA  THR A 147    17932  16227  12734  -2406  -2317   1053       C  
ATOM    962  C   THR A 147      -8.885  64.662  30.878  1.00137.44           C  
ANISOU  962  C   THR A 147    19782  18034  14404  -2478  -2483   1094       C  
ATOM    963  O   THR A 147      -9.333  64.250  31.995  1.00135.94           O  
ANISOU  963  O   THR A 147    19867  17557  14225  -2313  -2430    994       O  
ATOM    964  CB  THR A 147      -9.791  63.709  28.718  1.00103.31           C  
ANISOU  964  CB  THR A 147    14962  14012  10278  -2196  -2165    992       C  
ATOM    965  OG1 THR A 147     -10.621  64.055  27.608  1.00 95.60           O  
ANISOU  965  OG1 THR A 147    13926  13010   9385  -2181  -2044    978       O  
ATOM    966  CG2 THR A 147     -10.266  62.414  29.344  1.00 86.90           C  
ANISOU  966  CG2 THR A 147    12922  11817   8278  -1867  -2013    837       C  
ATOM    967  N   LYS A 148      -7.632  65.013  30.652  1.00122.00           N  
ANISOU  967  N   LYS A 148    17608  16406  12338  -2731  -2683   1244       N  
ATOM    968  CA  LYS A 148      -6.612  64.899  31.714  1.00132.20           C  
ANISOU  968  CA  LYS A 148    18949  17759  13519  -2830  -2869   1303       C  
ATOM    969  C   LYS A 148      -6.974  65.806  32.868  1.00144.08           C  
ANISOU  969  C   LYS A 148    20971  18819  14954  -2961  -2985   1316       C  
ATOM    970  O   LYS A 148      -6.886  65.369  34.022  1.00133.74           O  
ANISOU  970  O   LYS A 148    19858  17339  13617  -2855  -3009   1256       O  
ATOM    971  CB  LYS A 148      -5.191  65.146  31.194  1.00118.72           C  
ANISOU  971  CB  LYS A 148    16875  16536  11697  -3097  -3067   1481       C  
ATOM    972  CG  LYS A 148      -4.109  64.849  32.231  1.00142.45           C  
ANISOU  972  CG  LYS A 148    19867  19659  14597  -3162  -3249   1536       C  
ATOM    973  CD  LYS A 148      -4.238  63.472  32.890  1.00134.15           C  
ANISOU  973  CD  LYS A 148    18790  18568  13612  -2791  -3120   1371       C  
ATOM    974  CE  LYS A 148      -3.581  63.356  34.251  1.00 99.61           C  
ANISOU  974  CE  LYS A 148    14610  14089   9146  -2837  -3289   1391       C  
ATOM    975  NZ  LYS A 148      -2.109  63.249  34.149  1.00 91.97           N  
ANISOU  975  NZ  LYS A 148    13279  13600   8063  -2996  -3487   1531       N  
ATOM    976  N   VAL A 149      -7.416  67.012  32.560  1.00137.06           N  
ANISOU  976  N   VAL A 149    20314  17730  14029  -3164  -3053   1383       N  
ATOM    977  CA  VAL A 149      -7.825  67.983  33.606  1.00109.91           C  
ANISOU  977  CA  VAL A 149    17415  13841  10504  -3272  -3176   1389       C  
ATOM    978  C   VAL A 149      -8.933  67.381  34.468  1.00101.59           C  
ANISOU  978  C   VAL A 149    16640  12430   9527  -2932  -2970   1203       C  
ATOM    979  O   VAL A 149      -8.859  67.414  35.678  1.00116.15           O  
ANISOU  979  O   VAL A 149    18791  14041  11298  -2913  -3044   1176       O  
ATOM    980  CB  VAL A 149      -8.293  69.292  32.946  1.00 99.90           C  
ANISOU  980  CB  VAL A 149    16348  12410   9198  -3482  -3255   1466       C  
ATOM    981  CG1 VAL A 149      -8.914  70.240  33.959  1.00 92.77           C  
ANISOU  981  CG1 VAL A 149    16034  11006   8207  -3512  -3352   1437       C  
ATOM    982  CG2 VAL A 149      -7.165  69.979  32.187  1.00110.67           C  
ANISOU  982  CG2 VAL A 149    17476  14114  10459  -3873  -3488   1676       C  
ATOM    983  N   VAL A 150      -9.969  66.868  33.832  1.00 87.56           N  
ANISOU  983  N   VAL A 150    14763  10617   7887  -2680  -2717   1084       N  
ATOM    984  CA  VAL A 150     -11.086  66.174  34.508  1.00 85.71           C  
ANISOU  984  CA  VAL A 150    14724  10106   7733  -2356  -2494    916       C  
ATOM    985  C   VAL A 150     -10.587  65.132  35.500  1.00 96.35           C  
ANISOU  985  C   VAL A 150    16053  11490   9064  -2227  -2494    863       C  
ATOM    986  O   VAL A 150     -11.021  65.139  36.656  1.00104.27           O  
ANISOU  986  O   VAL A 150    17407  12188  10021  -2134  -2476    798       O  
ATOM    987  CB  VAL A 150     -12.087  65.570  33.503  1.00 70.75           C  
ANISOU  987  CB  VAL A 150    12611   8274   5995  -2129  -2236    819       C  
ATOM    988  CG1 VAL A 150     -13.128  64.699  34.196  1.00 58.32           C  
ANISOU  988  CG1 VAL A 150    11181   6480   4495  -1821  -2015    667       C  
ATOM    989  CG2 VAL A 150     -12.789  66.664  32.708  1.00 67.77           C  
ANISOU  989  CG2 VAL A 150    12345   7774   5631  -2223  -2228    852       C  
ATOM    990  N   ILE A 151      -9.706  64.246  35.047  1.00103.84           N  
ANISOU  990  N   ILE A 151    16604  12809  10039  -2205  -2515    888       N  
ATOM    991  CA  ILE A 151      -9.184  63.141  35.898  1.00122.60           C  
ANISOU  991  CA  ILE A 151    18932  15246  12401  -2056  -2523    832       C  
ATOM    992  C   ILE A 151      -8.474  63.753  37.105  1.00118.40           C  
ANISOU  992  C   ILE A 151    18694  14566  11725  -2246  -2750    906       C  
ATOM    993  O   ILE A 151      -8.651  63.243  38.229  1.00 98.78           O  
ANISOU  993  O   ILE A 151    16443  11872   9216  -2109  -2726    829       O  
ATOM    994  CB  ILE A 151      -8.246  62.211  35.094  1.00120.47           C  
ANISOU  994  CB  ILE A 151    18175  15438  12161  -2002  -2540    855       C  
ATOM    995  CG1 ILE A 151      -8.936  61.656  33.845  1.00138.45           C  
ANISOU  995  CG1 ILE A 151    20184  17852  14568  -1824  -2332    785       C  
ATOM    996  CG2 ILE A 151      -7.700  61.095  35.974  1.00114.54           C  
ANISOU  996  CG2 ILE A 151    17400  14734  11383  -1834  -2571    794       C  
ATOM    997  CD1 ILE A 151     -10.154  60.819  34.132  1.00165.44           C  
ANISOU  997  CD1 ILE A 151    23754  21012  18090  -1536  -2106    631       C  
ATOM    998  N   CYS A 152      -7.709  64.823  36.872  1.00106.33           N  
ANISOU  998  N   CYS A 152    17165  13136  10096  -2565  -2972   1059       N  
ATOM    999  CA  CYS A 152      -6.971  65.500  37.956  1.00 87.10           C  
ANISOU  999  CA  CYS A 152    15018  10565   7511  -2789  -3225   1151       C  
ATOM   1000  C   CYS A 152      -7.932  66.152  38.947  1.00 80.51           C  
ANISOU 1000  C   CYS A 152    14733   9228   6628  -2737  -3198   1080       C  
ATOM   1001  O   CYS A 152      -7.770  65.990  40.157  1.00134.68           O  
ANISOU 1001  O   CYS A 152    21863  15893  13413  -2701  -3268   1050       O  
ATOM   1002  CB  CYS A 152      -5.952  66.509  37.446  1.00 85.11           C  
ANISOU 1002  CB  CYS A 152    14647  10537   7151  -3174  -3486   1348       C  
ATOM   1003  SG  CYS A 152      -4.436  65.704  36.870  1.00100.42           S  
ANISOU 1003  SG  CYS A 152    15987  13096   9071  -3251  -3593   1454       S  
ATOM   1004  N   VAL A 153      -8.930  66.848  38.433  1.00 69.73           N  
ANISOU 1004  N   VAL A 153    13528   7667   5300  -2711  -3094   1047       N  
ATOM   1005  CA  VAL A 153      -9.942  67.549  39.259  1.00 73.10           C  
ANISOU 1005  CA  VAL A 153    14472   7634   5668  -2625  -3053    972       C  
ATOM   1006  C   VAL A 153     -10.670  66.544  40.138  1.00 83.64           C  
ANISOU 1006  C   VAL A 153    15924   8804   7051  -2309  -2841    819       C  
ATOM   1007  O   VAL A 153     -10.903  66.823  41.333  1.00120.43           O  
ANISOU 1007  O   VAL A 153    20992  13158  11607  -2269  -2886    781       O  
ATOM   1008  CB  VAL A 153     -10.933  68.298  38.343  1.00 64.60           C  
ANISOU 1008  CB  VAL A 153    13454   6445   4643  -2599  -2946    952       C  
ATOM   1009  CG1 VAL A 153     -12.200  68.712  39.073  1.00 61.99           C  
ANISOU 1009  CG1 VAL A 153    13572   5699   4282  -2390  -2817    834       C  
ATOM   1010  CG2 VAL A 153     -10.286  69.496  37.662  1.00 66.66           C  
ANISOU 1010  CG2 VAL A 153    13727   6780   4818  -2945  -3193   1112       C  
ATOM   1011  N   ILE A 154     -11.072  65.432  39.547  1.00 85.31           N  
ANISOU 1011  N   ILE A 154    15808   9199   7406  -2092  -2619    737       N  
ATOM   1012  CA  ILE A 154     -11.863  64.395  40.254  1.00104.98           C  
ANISOU 1012  CA  ILE A 154    18386  11550   9950  -1801  -2404    599       C  
ATOM   1013  C   ILE A 154     -11.076  63.901  41.456  1.00101.20           C  
ANISOU 1013  C   ILE A 154    18038  11033   9379  -1817  -2534    603       C  
ATOM   1014  O   ILE A 154     -11.659  63.730  42.549  1.00 87.63           O  
ANISOU 1014  O   ILE A 154    16646   9041   7606  -1683  -2460    525       O  
ATOM   1015  CB  ILE A 154     -12.223  63.250  39.278  1.00119.81           C  
ANISOU 1015  CB  ILE A 154    19859  13672  11989  -1614  -2197    534       C  
ATOM   1016  CG1 ILE A 154     -13.306  63.694  38.291  1.00 90.85           C  
ANISOU 1016  CG1 ILE A 154    16143   9962   8414  -1550  -2028    504       C  
ATOM   1017  CG2 ILE A 154     -12.631  61.974  40.019  1.00159.45           C  
ANISOU 1017  CG2 ILE A 154    24912  18624  17045  -1374  -2047    425       C  
ATOM   1018  CD1 ILE A 154     -13.665  62.651  37.264  1.00 85.94           C  
ANISOU 1018  CD1 ILE A 154    15142   9568   7942  -1388  -1845    449       C  
ATOM   1019  N   TRP A 155      -9.782  63.665  41.249  1.00 88.97           N  
ANISOU 1019  N   TRP A 155    16226   9772   7804  -1971  -2722    695       N  
ATOM   1020  CA  TRP A 155      -8.894  63.096  42.286  1.00 91.36           C  
ANISOU 1020  CA  TRP A 155    16588  10096   8026  -1985  -2865    707       C  
ATOM   1021  C   TRP A 155      -8.822  64.090  43.450  1.00109.50           C  
ANISOU 1021  C   TRP A 155    19369  12067  10169  -2132  -3034    746       C  
ATOM   1022  O   TRP A 155      -8.844  63.694  44.639  1.00113.14           O  
ANISOU 1022  O   TRP A 155    20090  12334  10562  -2041  -3046    692       O  
ATOM   1023  CB  TRP A 155      -7.499  62.804  41.706  1.00 83.18           C  
ANISOU 1023  CB  TRP A 155    15141   9480   6982  -2133  -3047    814       C  
ATOM   1024  CG  TRP A 155      -7.298  61.375  41.307  1.00 83.48           C  
ANISOU 1024  CG  TRP A 155    14821   9781   7115  -1903  -2931    739       C  
ATOM   1025  CD1 TRP A 155      -7.028  60.898  40.057  1.00 79.20           C  
ANISOU 1025  CD1 TRP A 155    13836   9595   6658  -1852  -2870    751       C  
ATOM   1026  CD2 TRP A 155      -7.370  60.223  42.169  1.00 77.23           C  
ANISOU 1026  CD2 TRP A 155    14114   8900   6328  -1682  -2871    638       C  
ATOM   1027  NE1 TRP A 155      -6.925  59.533  40.082  1.00 77.58           N  
ANISOU 1027  NE1 TRP A 155    13449   9518   6507  -1600  -2785    658       N  
ATOM   1028  CE2 TRP A 155      -7.133  59.090  41.362  1.00 78.05           C  
ANISOU 1028  CE2 TRP A 155    13828   9306   6521  -1500  -2788    590       C  
ATOM   1029  CE3 TRP A 155      -7.621  60.035  43.535  1.00 65.56           C  
ANISOU 1029  CE3 TRP A 155    13018   7113   4778  -1617  -2884    583       C  
ATOM   1030  CZ2 TRP A 155      -7.138  57.796  41.881  1.00 71.42           C  
ANISOU 1030  CZ2 TRP A 155    12988   8448   5698  -1264  -2736    491       C  
ATOM   1031  CZ3 TRP A 155      -7.622  58.755  44.045  1.00 62.82           C  
ANISOU 1031  CZ3 TRP A 155    12652   6764   4452  -1400  -2822    492       C  
ATOM   1032  CH2 TRP A 155      -7.383  57.652  43.227  1.00 63.72           C  
ANISOU 1032  CH2 TRP A 155    12393   7163   4654  -1228  -2756    447       C  
ATOM   1033  N   VAL A 156      -8.654  65.370  43.118  1.00 97.71           N  
ANISOU 1033  N   VAL A 156    18004  10514   8604  -2371  -3189    846       N  
ATOM   1034  CA  VAL A 156      -8.489  66.372  44.189  1.00 82.57           C  
ANISOU 1034  CA  VAL A 156    16573   8280   6519  -2528  -3392    893       C  
ATOM   1035  C   VAL A 156      -9.786  66.467  44.982  1.00 83.40           C  
ANISOU 1035  C   VAL A 156    17094   7995   6596  -2289  -3202    757       C  
ATOM   1036  O   VAL A 156      -9.707  66.442  46.204  1.00120.99           O  
ANISOU 1036  O   VAL A 156    22189  12533  11247  -2257  -3270    728       O  
ATOM   1037  CB  VAL A 156      -7.931  67.715  43.691  1.00 76.89           C  
ANISOU 1037  CB  VAL A 156    15931   7576   5707  -2865  -3645   1045       C  
ATOM   1038  CG1 VAL A 156      -6.582  67.532  43.013  1.00 74.30           C  
ANISOU 1038  CG1 VAL A 156    15160   7684   5386  -3109  -3829   1192       C  
ATOM   1039  CG2 VAL A 156      -8.888  68.433  42.772  1.00 77.37           C  
ANISOU 1039  CG2 VAL A 156    16035   7541   5821  -2834  -3523   1022       C  
ATOM   1040  N   LEU A 157     -10.927  66.505  44.320  1.00 81.26           N  
ANISOU 1040  N   LEU A 157    16783   7670   6419  -2115  -2967    677       N  
ATOM   1041  CA  LEU A 157     -12.222  66.561  45.015  1.00 82.09           C  
ANISOU 1041  CA  LEU A 157    17235   7458   6494  -1866  -2762    551       C  
ATOM   1042  C   LEU A 157     -12.440  65.313  45.838  1.00100.67           C  
ANISOU 1042  C   LEU A 157    19573   9801   8873  -1657  -2608    459       C  
ATOM   1043  O   LEU A 157     -13.009  65.449  46.956  1.00145.25           O  
ANISOU 1043  O   LEU A 157    25612  15166  14411  -1537  -2556    393       O  
ATOM   1044  CB  LEU A 157     -13.336  66.787  43.987  1.00 69.69           C  
ANISOU 1044  CB  LEU A 157    15542   5900   5033  -1733  -2547    499       C  
ATOM   1045  CG  LEU A 157     -13.841  68.226  43.930  1.00 77.59           C  
ANISOU 1045  CG  LEU A 157    16905   6644   5929  -1793  -2633    516       C  
ATOM   1046  CD1 LEU A 157     -12.783  69.169  43.380  1.00 84.75           C  
ANISOU 1046  CD1 LEU A 157    17789   7635   6774  -2134  -2938    665       C  
ATOM   1047  CD2 LEU A 157     -15.118  68.332  43.119  1.00 78.81           C  
ANISOU 1047  CD2 LEU A 157    16977   6782   6185  -1595  -2387    438       C  
ATOM   1048  N   ALA A 158     -11.961  64.165  45.350  1.00127.08           N  
ANISOU 1048  N   ALA A 158    22509  13436  12337  -1619  -2557    458       N  
ATOM   1049  CA  ALA A 158     -12.090  62.876  46.059  1.00132.12           C  
ANISOU 1049  CA  ALA A 158    23122  14077  13001  -1433  -2436    378       C  
ATOM   1050  C   ALA A 158     -11.327  62.885  47.391  1.00103.85           C  
ANISOU 1050  C   ALA A 158    19833  10352   9274  -1511  -2630    402       C  
ATOM   1051  O   ALA A 158     -11.894  62.420  48.392  1.00 92.28           O  
ANISOU 1051  O   ALA A 158    18622   8686   7752  -1357  -2519    323       O  
ATOM   1052  CB  ALA A 158     -11.625  61.752  45.163  1.00164.30           C  
ANISOU 1052  CB  ALA A 158    26720  18490  17215  -1381  -2390    377       C  
ATOM   1053  N   LEU A 159     -10.097  63.413  47.402  1.00 99.89           N  
ANISOU 1053  N   LEU A 159    19294   9955   8702  -1755  -2912    514       N  
ATOM   1054  CA  LEU A 159      -9.270  63.440  48.615  1.00105.24           C  
ANISOU 1054  CA  LEU A 159    20228  10516   9241  -1855  -3127    551       C  
ATOM   1055  C   LEU A 159      -9.747  64.543  49.558  1.00 92.30           C  
ANISOU 1055  C   LEU A 159    19134   8494   7441  -1897  -3193    543       C  
ATOM   1056  O   LEU A 159      -9.671  64.360  50.809  1.00 87.48           O  
ANISOU 1056  O   LEU A 159    18848   7676   6714  -1852  -3245    510       O  
ATOM   1057  CB  LEU A 159      -7.762  63.535  48.302  1.00110.69           C  
ANISOU 1057  CB  LEU A 159    20654  11492   9910  -2103  -3412    685       C  
ATOM   1058  CG  LEU A 159      -7.220  64.843  47.708  1.00132.20           C  
ANISOU 1058  CG  LEU A 159    23383  14271  12575  -2403  -3627    822       C  
ATOM   1059  CD1 LEU A 159      -6.849  65.868  48.779  1.00116.58           C  
ANISOU 1059  CD1 LEU A 159    21887  11999  10409  -2599  -3880    888       C  
ATOM   1060  CD2 LEU A 159      -6.005  64.565  46.834  1.00134.27           C  
ANISOU 1060  CD2 LEU A 159    23152  14976  12887  -2574  -3779    939       C  
ATOM   1061  N   LEU A 160     -10.272  65.614  48.992  1.00 95.57           N  
ANISOU 1061  N   LEU A 160    19664   8808   7840  -1956  -3185    563       N  
ATOM   1062  CA  LEU A 160     -10.836  66.738  49.760  1.00 82.87           C  
ANISOU 1062  CA  LEU A 160    18592   6826   6068  -1956  -3242    542       C  
ATOM   1063  C   LEU A 160     -12.146  66.365  50.425  1.00 81.41           C  
ANISOU 1063  C   LEU A 160    18642   6426   5863  -1648  -2958    400       C  
ATOM   1064  O   LEU A 160     -12.433  66.894  51.502  1.00 85.98           O  
ANISOU 1064  O   LEU A 160    19686   6707   6275  -1597  -3004    364       O  
ATOM   1065  CB  LEU A 160     -11.025  67.952  48.842  1.00 83.22           C  
ANISOU 1065  CB  LEU A 160    18673   6841   6105  -2094  -3323    603       C  
ATOM   1066  CG  LEU A 160      -9.758  68.722  48.476  1.00 82.97           C  
ANISOU 1066  CG  LEU A 160    18586   6925   6011  -2460  -3668    768       C  
ATOM   1067  CD1 LEU A 160     -10.099  69.891  47.566  1.00 91.81           C  
ANISOU 1067  CD1 LEU A 160    19779   7986   7119  -2580  -3731    820       C  
ATOM   1068  CD2 LEU A 160      -9.028  69.214  49.710  1.00 82.55           C  
ANISOU 1068  CD2 LEU A 160    18947   6649   5767  -2621  -3946    824       C  
ATOM   1069  N   LEU A 161     -12.933  65.479  49.835  1.00 89.77           N  
ANISOU 1069  N   LEU A 161    19399   7635   7072  -1448  -2675    325       N  
ATOM   1070  CA  LEU A 161     -14.132  64.951  50.490  1.00101.77           C  
ANISOU 1070  CA  LEU A 161    21086   9008   8572  -1174  -2399    208       C  
ATOM   1071  C   LEU A 161     -13.751  64.017  51.624  1.00135.85           C  
ANISOU 1071  C   LEU A 161    25509  13280  12826  -1129  -2416    182       C  
ATOM   1072  O   LEU A 161     -14.491  63.933  52.635  1.00178.96           O  
ANISOU 1072  O   LEU A 161    31292  18529  18172   -969  -2288    110       O  
ATOM   1073  CB  LEU A 161     -14.994  64.214  49.460  1.00102.52           C  
ANISOU 1073  CB  LEU A 161    20798   9303   8850  -1017  -2122    157       C  
ATOM   1074  CG  LEU A 161     -16.212  63.484  50.028  1.00 92.32           C  
ANISOU 1074  CG  LEU A 161    19593   7931   7554   -761  -1828     56       C  
ATOM   1075  CD1 LEU A 161     -17.248  64.469  50.548  1.00 83.81           C  
ANISOU 1075  CD1 LEU A 161    18900   6604   6338   -623  -1726      2       C  
ATOM   1076  CD2 LEU A 161     -16.826  62.564  48.987  1.00 90.60           C  
ANISOU 1076  CD2 LEU A 161    18953   7942   7526   -656  -1605     28       C  
ATOM   1077  N   ALA A 162     -12.624  63.337  51.477  1.00158.07           N  
ANISOU 1077  N   ALA A 162    28064  16295  15701  -1258  -2573    241       N  
ATOM   1078  CA  ALA A 162     -12.252  62.244  52.392  1.00147.41           C  
ANISOU 1078  CA  ALA A 162    26746  14941  14320  -1196  -2582    212       C  
ATOM   1079  C   ALA A 162     -11.551  62.727  53.646  1.00140.45           C  
ANISOU 1079  C   ALA A 162    26265  13846  13254  -1309  -2816    246       C  
ATOM   1080  O   ALA A 162     -11.767  62.119  54.717  1.00130.11           O  
ANISOU 1080  O   ALA A 162    25180  12395  11861  -1199  -2758    191       O  
ATOM   1081  CB  ALA A 162     -11.439  61.201  51.663  1.00140.78           C  
ANISOU 1081  CB  ALA A 162    25447  14419  13621  -1228  -2631    242       C  
ATOM   1082  N   PHE A 163     -10.748  63.784  53.544  1.00174.62           N  
ANISOU 1082  N   PHE A 163    30696  18143  17508  -1536  -3082    339       N  
ATOM   1083  CA  PHE A 163      -9.790  64.237  54.575  1.00146.07           C  
ANISOU 1083  CA  PHE A 163    27396  14375  13728  -1709  -3376    403       C  
ATOM   1084  C   PHE A 163     -10.453  64.564  55.910  1.00133.09           C  
ANISOU 1084  C   PHE A 163    26296  12369  11900  -1585  -3328    330       C  
ATOM   1085  O   PHE A 163      -9.861  64.390  57.005  1.00101.93           O  
ANISOU 1085  O   PHE A 163    22604   8294   7831  -1637  -3486    343       O  
ATOM   1086  CB  PHE A 163      -8.911  65.397  54.078  1.00156.84           C  
ANISOU 1086  CB  PHE A 163    28765  15781  15045  -2003  -3672    533       C  
ATOM   1087  CG  PHE A 163      -9.404  66.791  54.384  1.00146.26           C  
ANISOU 1087  CG  PHE A 163    27896  14123  13552  -2054  -3753    537       C  
ATOM   1088  CD1 PHE A 163      -9.112  67.407  55.591  1.00143.14           C  
ANISOU 1088  CD1 PHE A 163    28006  13428  12951  -2128  -3955    552       C  
ATOM   1089  CD2 PHE A 163     -10.151  67.497  53.455  1.00152.86           C  
ANISOU 1089  CD2 PHE A 163    28689  14950  14438  -2019  -3643    524       C  
ATOM   1090  CE1 PHE A 163      -9.573  68.687  55.865  1.00140.29           C  
ANISOU 1090  CE1 PHE A 163    28112  12758  12432  -2150  -4045    547       C  
ATOM   1091  CE2 PHE A 163     -10.611  68.777  53.728  1.00129.24           C  
ANISOU 1091  CE2 PHE A 163    26158  11654  11294  -2038  -3733    520       C  
ATOM   1092  CZ  PHE A 163     -10.318  69.372  54.932  1.00128.50           C  
ANISOU 1092  CZ  PHE A 163    26577  11257  10988  -2099  -3937    529       C  
ATOM   1093  N   PRO A 164     -11.668  65.150  55.937  1.00142.48           N  
ANISOU 1093  N   PRO A 164    27724  13373  13038  -1417  -3129    254       N  
ATOM   1094  CA  PRO A 164     -12.193  65.561  57.236  1.00145.45           C  
ANISOU 1094  CA  PRO A 164    28636  13420  13206  -1300  -3109    191       C  
ATOM   1095  C   PRO A 164     -12.330  64.364  58.189  1.00125.83           C  
ANISOU 1095  C   PRO A 164    26190  10922  10696  -1163  -2982    132       C  
ATOM   1096  O   PRO A 164     -12.241  64.455  59.441  1.00238.78           O  
ANISOU 1096  O   PRO A 164    40904  24998  24821  -1138  -3058    110       O  
ATOM   1097  CB  PRO A 164     -13.574  66.162  56.940  1.00135.95           C  
ANISOU 1097  CB  PRO A 164    27570  12105  11977  -1086  -2861    108       C  
ATOM   1098  CG  PRO A 164     -13.510  66.554  55.486  1.00140.90           C  
ANISOU 1098  CG  PRO A 164    27841  12930  12765  -1187  -2873    160       C  
ATOM   1099  CD  PRO A 164     -12.544  65.579  54.835  1.00139.10           C  
ANISOU 1099  CD  PRO A 164    27120  13018  12713  -1333  -2946    228       C  
ATOM   1100  N   GLN A 165     -12.491  63.184  57.602  1.00104.03           N  
ANISOU 1100  N   GLN A 165    23009   8406   8109  -1083  -2806    110       N  
ATOM   1101  CA  GLN A 165     -12.708  61.958  58.389  1.00 94.45           C  
ANISOU 1101  CA  GLN A 165    21814   7189   6883   -954  -2674     57       C  
ATOM   1102  C   GLN A 165     -11.371  61.255  58.458  1.00102.32           C  
ANISOU 1102  C   GLN A 165    22613   8331   7930  -1105  -2914    120       C  
ATOM   1103  O   GLN A 165     -11.018  60.663  59.451  1.00121.99           O  
ANISOU 1103  O   GLN A 165    25285  10731  10334  -1092  -2984    108       O  
ATOM   1104  CB  GLN A 165     -13.767  61.061  57.725  1.00 98.48           C  
ANISOU 1104  CB  GLN A 165    22020   7861   7537   -771  -2347     -3       C  
ATOM   1105  CG  GLN A 165     -14.017  59.743  58.449  1.00100.44           C  
ANISOU 1105  CG  GLN A 165    22278   8113   7772   -663  -2221    -46       C  
ATOM   1106  CD  GLN A 165     -14.919  58.823  57.663  1.00 92.32           C  
ANISOU 1106  CD  GLN A 165    20917   7264   6897   -532  -1948    -83       C  
ATOM   1107  OE1 GLN A 165     -14.529  57.722  57.272  1.00 80.79           O  
ANISOU 1107  OE1 GLN A 165    19465   5790   5438   -410  -1711   -121       O  
ATOM   1108  NE2 GLN A 165     -16.127  59.291  57.391  1.00 74.50           N  
ANISOU 1108  NE2 GLN A 165    18379   5172   4755   -548  -1988    -74       N  
ATOM   1109  N   GLY A 166     -10.684  61.228  57.335  1.00126.46           N  
ANISOU 1109  N   GLY A 166    25266  11645  11136  -1224  -3017    182       N  
ATOM   1110  CA  GLY A 166      -9.415  60.492  57.200  1.00124.99           C  
ANISOU 1110  CA  GLY A 166    24801  11675  11014  -1335  -3226    241       C  
ATOM   1111  C   GLY A 166      -8.306  61.016  58.076  1.00137.55           C  
ANISOU 1111  C   GLY A 166    26647  13155  12459  -1525  -3551    316       C  
ATOM   1112  O   GLY A 166      -7.607  60.192  58.758  1.00110.56           O  
ANISOU 1112  O   GLY A 166    23233   9763   9009  -1523  -3671    319       O  
ATOM   1113  N   TYR A 167      -8.109  62.327  58.000  1.00173.86           N  
ANISOU 1113  N   TYR A 167    31440  17643  16973  -1693  -3709    381       N  
ATOM   1114  CA  TYR A 167      -6.985  63.035  58.668  1.00193.38           C  
ANISOU 1114  CA  TYR A 167    34145  20024  19305  -1935  -4063    481       C  
ATOM   1115  C   TYR A 167      -7.080  62.904  60.184  1.00182.71           C  
ANISOU 1115  C   TYR A 167    33276  18368  17775  -1870  -4109    434       C  
ATOM   1116  O   TYR A 167      -6.023  62.947  60.899  1.00141.30           O  
ANISOU 1116  O   TYR A 167    28160  13090  12435  -2032  -4396    505       O  
ATOM   1117  CB  TYR A 167      -6.962  64.504  58.232  1.00177.46           C  
ANISOU 1117  CB  TYR A 167    32292  17910  17223  -2121  -4206    555       C  
ATOM   1118  CG  TYR A 167      -5.956  65.385  58.928  1.00159.45           C  
ANISOU 1118  CG  TYR A 167    30322  15486  14774  -2391  -4578    666       C  
ATOM   1119  CD1 TYR A 167      -4.593  65.192  58.764  1.00148.11           C  
ANISOU 1119  CD1 TYR A 167    28612  14300  13363  -2624  -4855    791       C  
ATOM   1120  CD2 TYR A 167      -6.368  66.442  59.724  1.00138.63           C  
ANISOU 1120  CD2 TYR A 167    28255  12472  11943  -2412  -4664    651       C  
ATOM   1121  CE1 TYR A 167      -3.667  66.011  59.389  1.00144.53           C  
ANISOU 1121  CE1 TYR A 167    28435  13726  12751  -2900  -5213    909       C  
ATOM   1122  CE2 TYR A 167      -5.456  67.268  60.359  1.00135.76           C  
ANISOU 1122  CE2 TYR A 167    28209  11956  11416  -2676  -5028    758       C  
ATOM   1123  CZ  TYR A 167      -4.099  67.054  60.189  1.00149.01           C  
ANISOU 1123  CZ  TYR A 167    29598  13888  13128  -2936  -5307    895       C  
ATOM   1124  OH  TYR A 167      -3.197  67.869  60.812  1.00180.63           O  
ANISOU 1124  OH  TYR A 167    33908  17752  16968  -3222  -5679   1015       O  
ATOM   1125  N   TYR A 168      -8.308  62.688  60.673  1.00154.19           N  
ANISOU 1125  N   TYR A 168    29905  14562  14116  -1637  -3831    320       N  
ATOM   1126  CA  TYR A 168      -8.613  62.832  62.119  1.00120.50           C  
ANISOU 1126  CA  TYR A 168    26173   9968   9641  -1563  -3845    270       C  
ATOM   1127  C   TYR A 168      -8.826  61.496  62.803  1.00110.40           C  
ANISOU 1127  C   TYR A 168    24875   8701   8370  -1404  -3701    203       C  
ATOM   1128  O   TYR A 168      -9.181  61.499  63.983  1.00112.89           O  
ANISOU 1128  O   TYR A 168    25611   8765   8514  -1324  -3672    156       O  
ATOM   1129  CB  TYR A 168      -9.825  63.747  62.335  1.00118.54           C  
ANISOU 1129  CB  TYR A 168    26291   9474   9275  -1421  -3663    199       C  
ATOM   1130  CG  TYR A 168      -9.522  65.222  62.241  1.00129.92           C  
ANISOU 1130  CG  TYR A 168    28013  10748  10602  -1586  -3896    261       C  
ATOM   1131  CD1 TYR A 168      -8.365  65.759  62.784  1.00136.09           C  
ANISOU 1131  CD1 TYR A 168    29009  11428  11268  -1833  -4265    358       C  
ATOM   1132  CD2 TYR A 168     -10.403  66.093  61.624  1.00128.11           C  
ANISOU 1132  CD2 TYR A 168    27857  10450  10368  -1500  -3764    226       C  
ATOM   1133  CE1 TYR A 168      -8.088  67.115  62.704  1.00145.72           C  
ANISOU 1133  CE1 TYR A 168    30521  12476  12369  -2009  -4505    425       C  
ATOM   1134  CE2 TYR A 168     -10.142  67.452  61.534  1.00128.83           C  
ANISOU 1134  CE2 TYR A 168    28246  10362  10340  -1651  -3998    282       C  
ATOM   1135  CZ  TYR A 168      -8.980  67.966  62.078  1.00145.27           C  
ANISOU 1135  CZ  TYR A 168    30556  12334  12304  -1916  -4376    385       C  
ATOM   1136  OH  TYR A 168      -8.709  69.302  61.999  1.00172.17           O  
ANISOU 1136  OH  TYR A 168    34287  15546  15580  -2091  -4634    451       O  
ATOM   1137  N   SER A 169      -8.500  60.409  62.113  1.00122.01           N  
ANISOU 1137  N   SER A 169    25892  10449  10016  -1376  -3652    207       N  
ATOM   1138  CA  SER A 169      -8.500  59.045  62.675  1.00144.35           C  
ANISOU 1138  CA  SER A 169    28678  13307  12859  -1254  -3577    158       C  
ATOM   1139  C   SER A 169      -7.446  58.941  63.769  1.00162.22           C  
ANISOU 1139  C   SER A 169    31191  15454  14991  -1367  -3868    201       C  
ATOM   1140  O   SER A 169      -6.264  59.203  63.496  1.00178.10           O  
ANISOU 1140  O   SER A 169    33035  17605  17029  -1546  -4149    289       O  
ATOM   1141  CB  SER A 169      -8.261  57.983  61.618  1.00147.46           C  
ANISOU 1141  CB  SER A 169    28550  14020  13459  -1199  -3512    156       C  
ATOM   1142  OG  SER A 169      -8.155  56.692  62.205  1.00135.78           O  
ANISOU 1142  OG  SER A 169    27076  12540  11974  -1094  -3492    114       O  
ATOM   1143  N   THR A 170      -7.873  58.523  64.950  1.00195.35           N  
ANISOU 1143  N   THR A 170    35753  19425  19046  -1267  -3798    145       N  
ATOM   1144  CA  THR A 170      -6.991  58.494  66.133  1.00196.18           C  
ANISOU 1144  CA  THR A 170    36173  19367  18997  -1365  -4067    178       C  
ATOM   1145  C   THR A 170      -6.998  57.106  66.739  1.00192.80           C  
ANISOU 1145  C   THR A 170    35744  18941  18567  -1246  -4011    130       C  
ATOM   1146  O   THR A 170      -8.069  56.560  67.027  1.00248.07           O  
ANISOU 1146  O   THR A 170    42857  25858  25540  -1086  -3738     58       O  
ATOM   1147  CB  THR A 170      -7.386  59.567  67.153  1.00198.22           C  
ANISOU 1147  CB  THR A 170    36994  19289  19031  -1389  -4101    166       C  
ATOM   1148  OG1 THR A 170      -8.737  59.333  67.547  1.00239.49           O  
ANISOU 1148  OG1 THR A 170    42421  24384  24188  -1181  -3771     73       O  
ATOM   1149  CG2 THR A 170      -7.245  60.975  66.621  1.00209.78           C  
ANISOU 1149  CG2 THR A 170    38518  20714  20473  -1528  -4225    222       C  
ATOM   1150  N   THR A 171      -5.827  56.519  66.928  1.00183.89           N  
ANISOU 1150  N   THR A 171    34489  17918  17460  -1322  -4270    175       N  
ATOM   1151  CA  THR A 171      -5.725  55.218  67.617  1.00211.35           C  
ANISOU 1151  CA  THR A 171    38029  21362  20911  -1214  -4269    131       C  
ATOM   1152  C   THR A 171      -5.762  55.434  69.121  1.00247.46           C  
ANISOU 1152  C   THR A 171    43149  25614  25259  -1239  -4353    121       C  
ATOM   1153  O   THR A 171      -4.938  56.199  69.612  1.00274.86           O  
ANISOU 1153  O   THR A 171    46810  28992  28631  -1393  -4623    182       O  
ATOM   1154  CB  THR A 171      -4.463  54.477  67.170  1.00205.77           C  
ANISOU 1154  CB  THR A 171    36954  20915  20313  -1249  -4515    174       C  
ATOM   1155  OG1 THR A 171      -4.384  54.513  65.744  1.00233.39           O  
ANISOU 1155  OG1 THR A 171    39961  24716  23997  -1242  -4450    193       O  
ATOM   1156  CG2 THR A 171      -4.453  53.049  67.654  1.00206.90           C  
ANISOU 1156  CG2 THR A 171    37120  21040  20450  -1105  -4498    118       C  
ATOM   1157  N   GLU A 172      -6.654  54.732  69.806  1.00228.41           N  
ANISOU 1157  N   GLU A 172    40967  23051  22764  -1102  -4141     53       N  
ATOM   1158  CA  GLU A 172      -6.830  54.854  71.258  1.00161.73           C  
ANISOU 1158  CA  GLU A 172    33054  14303  14089  -1102  -4178     35       C  
ATOM   1159  C   GLU A 172      -6.521  53.508  71.897  1.00159.81           C  
ANISOU 1159  C   GLU A 172    32858  14039  13821  -1046  -4242     15       C  
ATOM   1160  O   GLU A 172      -7.294  52.539  71.743  1.00198.41           O  
ANISOU 1160  O   GLU A 172    37657  18974  18756   -924  -4017    -30       O  
ATOM   1161  CB  GLU A 172      -8.213  55.421  71.583  1.00145.73           C  
ANISOU 1161  CB  GLU A 172    31312  12115  11944   -999  -3868    -17       C  
ATOM   1162  CG  GLU A 172      -8.334  56.875  71.157  1.00137.95           C  
ANISOU 1162  CG  GLU A 172    30387  11089  10938  -1059  -3887      2       C  
ATOM   1163  CD  GLU A 172      -9.695  57.522  71.287  1.00129.88           C  
ANISOU 1163  CD  GLU A 172    29588   9950   9810   -922  -3582    -55       C  
ATOM   1164  OE1 GLU A 172     -10.652  56.819  71.660  1.00159.15           O  
ANISOU 1164  OE1 GLU A 172    33362  13642  13465   -782  -3315   -106       O  
ATOM   1165  OE2 GLU A 172      -9.784  58.733  71.019  1.00117.88           O  
ANISOU 1165  OE2 GLU A 172    28178   8361   8249   -956  -3622    -45       O  
ATOM   1166  N   THR A 173      -5.461  53.519  72.710  1.00166.71           N  
ANISOU 1166  N   THR A 173    33931  14812  14597  -1143  -4555     53       N  
ATOM   1167  CA  THR A 173      -4.776  52.327  73.234  1.00187.18           C  
ANISOU 1167  CA  THR A 173    36531  17409  17178  -1113  -4726     49       C  
ATOM   1168  C   THR A 173      -5.526  51.797  74.455  1.00177.55           C  
ANISOU 1168  C   THR A 173    35762  15927  15771  -1043  -4593      3       C  
ATOM   1169  O   THR A 173      -5.812  52.523  75.434  1.00164.41           O  
ANISOU 1169  O   THR A 173    34539  14018  13910  -1083  -4587      2       O  
ATOM   1170  CB  THR A 173      -3.309  52.570  73.607  1.00177.06           C  
ANISOU 1170  CB  THR A 173    35263  16147  15864  -1248  -5128    116       C  
ATOM   1171  OG1 THR A 173      -2.709  53.371  72.588  1.00165.66           O  
ANISOU 1171  OG1 THR A 173    33466  14928  14547  -1356  -5241    178       O  
ATOM   1172  CG2 THR A 173      -2.550  51.270  73.792  1.00170.42           C  
ANISOU 1172  CG2 THR A 173    34293  15395  15060  -1178  -5304    106       C  
ATOM   1173  N   MET A 174      -5.752  50.497  74.428  1.00172.83           N  
ANISOU 1173  N   MET A 174    35069  15378  15218   -944  -4518    -29       N  
ATOM   1174  CA  MET A 174      -6.413  49.766  75.531  1.00167.54           C  
ANISOU 1174  CA  MET A 174    34788  14492  14375   -894  -4405    -60       C  
ATOM   1175  C   MET A 174      -5.507  48.603  75.902  1.00163.69           C  
ANISOU 1175  C   MET A 174    34300  14002  13892   -877  -4663    -58       C  
ATOM   1176  O   MET A 174      -4.463  48.363  75.290  1.00185.36           O  
ANISOU 1176  O   MET A 174    36731  16927  16770   -878  -4897    -41       O  
ATOM   1177  CB  MET A 174      -7.803  49.281  75.108  1.00180.04           C  
ANISOU 1177  CB  MET A 174    36282  16131  15993   -798  -4030    -95       C  
ATOM   1178  CG  MET A 174      -8.642  50.357  74.445  1.00170.19           C  
ANISOU 1178  CG  MET A 174    34920  14955  14788   -783  -3782   -100       C  
ATOM   1179  SD  MET A 174     -10.337  50.432  75.080  1.00156.56           S  
ANISOU 1179  SD  MET A 174    33490  13110  12883   -705  -3376   -129       S  
ATOM   1180  CE  MET A 174     -10.069  51.291  76.628  1.00136.97           C  
ANISOU 1180  CE  MET A 174    31604  10326  10112   -751  -3510   -128       C  
ATOM   1181  N   PRO A 175      -5.800  47.876  77.000  1.00147.79           N  
ANISOU 1181  N   PRO A 175    32663  11780  11710   -860  -4655    -74       N  
ATOM   1182  CA  PRO A 175      -4.878  46.851  77.520  1.00153.21           C  
ANISOU 1182  CA  PRO A 175    33429  12415  12366   -843  -4940    -74       C  
ATOM   1183  C   PRO A 175      -4.526  45.677  76.600  1.00144.65           C  
ANISOU 1183  C   PRO A 175    31965  11535  11458   -736  -5009    -96       C  
ATOM   1184  O   PRO A 175      -3.366  45.282  76.541  1.00137.27           O  
ANISOU 1184  O   PRO A 175    30903  10682  10570   -709  -5312    -90       O  
ATOM   1185  CB  PRO A 175      -5.611  46.300  78.755  1.00155.91           C  
ANISOU 1185  CB  PRO A 175    34251  12498  12490   -846  -4830    -86       C  
ATOM   1186  CG  PRO A 175      -6.577  47.403  79.144  1.00147.35           C  
ANISOU 1186  CG  PRO A 175    33402  11306  11276   -884  -4570    -84       C  
ATOM   1187  CD  PRO A 175      -7.005  48.012  77.827  1.00138.66           C  
ANISOU 1187  CD  PRO A 175    31883  10433  10366   -852  -4381    -89       C  
ATOM   1188  N   SER A 176      -5.536  45.154  75.914  1.00140.61           N  
ANISOU 1188  N   SER A 176    31289  11107  11027   -669  -4734   -120       N  
ATOM   1189  CA  SER A 176      -5.419  44.023  74.981  1.00168.62           C  
ANISOU 1189  CA  SER A 176    34510  14828  14729   -554  -4760   -149       C  
ATOM   1190  C   SER A 176      -5.074  44.517  73.576  1.00206.78           C  
ANISOU 1190  C   SER A 176    38831  19956  19777   -516  -4746   -148       C  
ATOM   1191  O   SER A 176      -4.233  43.904  72.893  1.00234.30           O  
ANISOU 1191  O   SER A 176    42017  23625  23380   -420  -4938   -165       O  
ATOM   1192  CB  SER A 176      -6.693  43.222  74.958  1.00181.35           C  
ANISOU 1192  CB  SER A 176    36221  16374  16309   -529  -4486   -162       C  
ATOM   1193  OG  SER A 176      -7.776  43.980  74.434  1.00230.34           O  
ANISOU 1193  OG  SER A 176    42305  22654  22558   -559  -4156   -154       O  
ATOM   1194  N   ARG A 177      -5.710  45.600  73.152  1.00227.64           N  
ANISOU 1194  N   ARG A 177    41381  22651  22460   -577  -4528   -132       N  
ATOM   1195  CA  ARG A 177      -5.682  45.999  71.739  1.00198.76           C  
ANISOU 1195  CA  ARG A 177    37247  19267  19004   -546  -4447   -131       C  
ATOM   1196  C   ARG A 177      -5.377  47.483  71.582  1.00209.06           C  
ANISOU 1196  C   ARG A 177    38497  20617  20319   -658  -4475    -90       C  
ATOM   1197  O   ARG A 177      -5.449  48.279  72.534  1.00159.44           O  
ANISOU 1197  O   ARG A 177    32568  14131  13879   -751  -4497    -69       O  
ATOM   1198  CB  ARG A 177      -7.034  45.704  71.095  1.00180.89           C  
ANISOU 1198  CB  ARG A 177    34876  17043  16807   -497  -4102   -154       C  
ATOM   1199  CG  ARG A 177      -7.429  44.238  71.124  1.00188.84           C  
ANISOU 1199  CG  ARG A 177    35933  18009  17807   -412  -4072   -182       C  
ATOM   1200  CD  ARG A 177      -8.896  44.106  70.773  1.00195.19           C  
ANISOU 1200  CD  ARG A 177    36721  18813  18626   -415  -3720   -182       C  
ATOM   1201  NE  ARG A 177      -9.259  42.723  70.511  1.00200.53           N  
ANISOU 1201  NE  ARG A 177    37375  19489  19329   -351  -3705   -199       N  
ATOM   1202  CZ  ARG A 177      -9.667  41.854  71.432  1.00161.06           C  
ANISOU 1202  CZ  ARG A 177    32723  14296  14176   -381  -3707   -189       C  
ATOM   1203  NH1 ARG A 177      -9.972  40.619  71.068  1.00167.83           N  
ANISOU 1203  NH1 ARG A 177    33549  15154  15062   -334  -3717   -199       N  
ATOM   1204  NH2 ARG A 177      -9.777  42.211  72.701  1.00124.93           N  
ANISOU 1204  NH2 ARG A 177    28539   9521   9407   -463  -3706   -167       N  
ATOM   1205  N   VAL A 178      -5.054  47.832  70.358  1.00241.69           N  
ANISOU 1205  N   VAL A 178    42195  25010  24623   -648  -4479    -78       N  
ATOM   1206  CA  VAL A 178      -4.894  49.246  69.933  1.00240.94           C  
ANISOU 1206  CA  VAL A 178    41994  24989  24563   -764  -4479    -32       C  
ATOM   1207  C   VAL A 178      -5.763  49.450  68.709  1.00227.20           C  
ANISOU 1207  C   VAL A 178    39935  23414  22974   -715  -4205    -49       C  
ATOM   1208  O   VAL A 178      -5.475  48.889  67.652  1.00288.06           O  
ANISOU 1208  O   VAL A 178    47243  31365  30840   -640  -4218    -59       O  
ATOM   1209  CB  VAL A 178      -3.427  49.585  69.642  1.00257.24           C  
ANISOU 1209  CB  VAL A 178    43819  27241  26676   -841  -4811     24       C  
ATOM   1210  CG1 VAL A 178      -3.252  51.071  69.487  1.00258.79           C  
ANISOU 1210  CG1 VAL A 178    44030  27442  26855  -1006  -4855     87       C  
ATOM   1211  CG2 VAL A 178      -2.510  49.037  70.722  1.00213.23           C  
ANISOU 1211  CG2 VAL A 178    38486  21550  20979   -849  -5099     33       C  
ATOM   1212  N   VAL A 179      -6.808  50.239  68.843  1.00194.59           N  
ANISOU 1212  N   VAL A 179    35983  19161  18790   -743  -3965    -55       N  
ATOM   1213  CA  VAL A 179      -7.813  50.380  67.759  1.00224.43           C  
ANISOU 1213  CA  VAL A 179    39495  23076  22700   -684  -3676    -76       C  
ATOM   1214  C   VAL A 179      -8.085  51.851  67.469  1.00238.88           C  
ANISOU 1214  C   VAL A 179    41347  24892  24522   -765  -3608    -49       C  
ATOM   1215  O   VAL A 179      -7.946  52.724  68.359  1.00305.28           O  
ANISOU 1215  O   VAL A 179    50112  33105  32776   -845  -3697    -30       O  
ATOM   1216  CB  VAL A 179      -9.104  49.632  68.128  1.00204.73           C  
ANISOU 1216  CB  VAL A 179    37174  20466  20147   -596  -3394   -116       C  
ATOM   1217  CG1 VAL A 179      -9.850  50.310  69.269  1.00193.68           C  
ANISOU 1217  CG1 VAL A 179    36223  18821  18543   -624  -3263   -119       C  
ATOM   1218  CG2 VAL A 179     -10.001  49.464  66.913  1.00193.46           C  
ANISOU 1218  CG2 VAL A 179    35406  19218  18879   -528  -3137   -133       C  
ATOM   1219  N   CYS A 180      -8.427  52.178  66.236  1.00179.85           N  
ANISOU 1219  N   CYS A 180    33521  17609  17202   -747  -3475    -48       N  
ATOM   1220  CA  CYS A 180      -8.579  53.575  65.798  1.00173.75           C  
ANISOU 1220  CA  CYS A 180    32737  16842  16437   -828  -3447    -19       C  
ATOM   1221  C   CYS A 180      -9.997  53.885  65.321  1.00164.00           C  
ANISOU 1221  C   CYS A 180    31479  15600  15234   -738  -3105    -57       C  
ATOM   1222  O   CYS A 180     -10.647  53.059  64.698  1.00127.62           O  
ANISOU 1222  O   CYS A 180    26639  11114  10735   -642  -2914    -86       O  
ATOM   1223  CB  CYS A 180      -7.585  53.887  64.694  1.00172.48           C  
ANISOU 1223  CB  CYS A 180    32165  16942  16427   -915  -3632     33       C  
ATOM   1224  SG  CYS A 180      -7.656  52.747  63.298  1.00136.33           S  
ANISOU 1224  SG  CYS A 180    27060  12678  12062   -793  -3566      7       S  
ATOM   1225  N   MET A 181     -10.454  55.083  65.538  1.00174.66           N  
ANISOU 1225  N   MET A 181    33053  16820  16490   -765  -3044    -54       N  
ATOM   1226  CA  MET A 181     -11.769  55.570  65.037  1.00150.33           C  
ANISOU 1226  CA  MET A 181    29940  13748  13430   -667  -2735    -88       C  
ATOM   1227  C   MET A 181     -11.730  57.082  64.848  1.00129.42           C  
ANISOU 1227  C   MET A 181    27422  11020  10729   -732  -2802    -68       C  
ATOM   1228  O   MET A 181     -10.721  57.732  65.215  1.00119.11           O  
ANISOU 1228  O   MET A 181    26273   9630   9353   -871  -3087    -21       O  
ATOM   1229  CB  MET A 181     -12.896  55.200  66.009  1.00152.97           C  
ANISOU 1229  CB  MET A 181    30588  13925  13608   -549  -2492   -134       C  
ATOM   1230  CG  MET A 181     -13.423  53.782  65.844  1.00151.09           C  
ANISOU 1230  CG  MET A 181    30165  13795  13445   -477  -2328   -151       C  
ATOM   1231  SD  MET A 181     -14.695  53.419  67.068  1.00187.17           S  
ANISOU 1231  SD  MET A 181    35112  18204  17797   -380  -2059   -180       S  
ATOM   1232  CE  MET A 181     -13.675  53.092  68.506  1.00170.67           C  
ANISOU 1232  CE  MET A 181    33425  15894  15528   -456  -2337   -169       C  
ATOM   1233  N   ILE A 182     -12.818  57.615  64.298  1.00135.16           N  
ANISOU 1233  N   ILE A 182    28101  11771  11483   -635  -2554    -99       N  
ATOM   1234  CA  ILE A 182     -12.944  59.048  63.924  1.00161.98           C  
ANISOU 1234  CA  ILE A 182    31603  15099  14843   -670  -2594    -88       C  
ATOM   1235  C   ILE A 182     -14.252  59.593  64.458  1.00158.97           C  
ANISOU 1235  C   ILE A 182    31528  14564  14307   -499  -2337   -150       C  
ATOM   1236  O   ILE A 182     -15.318  59.248  63.892  1.00215.08           O  
ANISOU 1236  O   ILE A 182    38426  21799  21495   -367  -2048   -185       O  
ATOM   1237  CB  ILE A 182     -12.907  59.225  62.393  1.00195.79           C  
ANISOU 1237  CB  ILE A 182    35428  19621  19341   -708  -2563    -62       C  
ATOM   1238  CG1 ILE A 182     -11.879  58.311  61.722  1.00195.32           C  
ANISOU 1238  CG1 ILE A 182    34963  19795  19452   -804  -2718    -18       C  
ATOM   1239  CG2 ILE A 182     -12.718  60.692  62.052  1.00197.33           C  
ANISOU 1239  CG2 ILE A 182    35754  19730  19489   -798  -2697    -31       C  
ATOM   1240  CD1 ILE A 182     -12.423  56.962  61.314  1.00157.86           C  
ANISOU 1240  CD1 ILE A 182    29937  15208  14833   -682  -2511    -56       C  
ATOM   1241  N   GLU A 183     -14.192  60.531  65.420  1.00123.96           N  
ANISOU 1241  N   GLU A 183    27566   9877   9654   -495  -2445   -162       N  
ATOM   1242  CA  GLU A 183     -15.398  61.113  66.037  1.00115.13           C  
ANISOU 1242  CA  GLU A 183    26782   8613   8348   -299  -2213   -229       C  
ATOM   1243  C   GLU A 183     -15.092  62.500  66.600  1.00114.45           C  
ANISOU 1243  C   GLU A 183    27155   8266   8065   -324  -2418   -233       C  
ATOM   1244  O   GLU A 183     -13.924  62.833  66.816  1.00105.00           O  
ANISOU 1244  O   GLU A 183    26075   6972   6846   -517  -2745   -176       O  
ATOM   1245  CB  GLU A 183     -15.934  60.196  67.146  1.00114.49           C  
ANISOU 1245  CB  GLU A 183    26891   8479   8129   -193  -2043   -263       C  
ATOM   1246  CG  GLU A 183     -16.810  59.048  66.658  1.00121.55           C  
ANISOU 1246  CG  GLU A 183    27431   9597   9153   -105  -1745   -274       C  
ATOM   1247  CD  GLU A 183     -16.088  57.774  66.229  1.00117.39           C  
ANISOU 1247  CD  GLU A 183    26565   9224   8814   -226  -1843   -233       C  
ATOM   1248  OE1 GLU A 183     -14.914  57.616  66.610  1.00141.15           O  
ANISOU 1248  OE1 GLU A 183    29656  12160  11814   -359  -2127   -201       O  
ATOM   1249  OE2 GLU A 183     -16.693  56.936  65.510  1.00 87.63           O  
ANISOU 1249  OE2 GLU A 183    22453   5649   5191   -182  -1646   -233       O  
ATOM   1250  N   TRP A 184     -16.147  63.273  66.824  1.00133.08           N  
ANISOU 1250  N   TRP A 184    29767  10520  10274   -125  -2230   -298       N  
ATOM   1251  CA  TRP A 184     -16.094  64.551  67.576  1.00157.98           C  
ANISOU 1251  CA  TRP A 184    33466  13380  13179    -80  -2388   -325       C  
ATOM   1252  C   TRP A 184     -17.397  64.722  68.349  1.00165.81           C  
ANISOU 1252  C   TRP A 184    34752  14295  13952    214  -2090   -417       C  
ATOM   1253  O   TRP A 184     -18.459  64.809  67.754  1.00164.16           O  
ANISOU 1253  O   TRP A 184    34355  14229  13790    394  -1814   -459       O  
ATOM   1254  CB  TRP A 184     -15.802  65.737  66.645  1.00199.81           C  
ANISOU 1254  CB  TRP A 184    38744  18637  18535   -168  -2568   -297       C  
ATOM   1255  CG  TRP A 184     -14.924  66.767  67.286  1.00221.44           C  
ANISOU 1255  CG  TRP A 184    41957  21087  21092   -310  -2932   -264       C  
ATOM   1256  CD1 TRP A 184     -15.332  67.898  67.927  1.00224.39           C  
ANISOU 1256  CD1 TRP A 184    42868  21180  21210   -174  -2990   -319       C  
ATOM   1257  CD2 TRP A 184     -13.490  66.732  67.404  1.00211.62           C  
ANISOU 1257  CD2 TRP A 184    40711  19806  19888   -612  -3301   -165       C  
ATOM   1258  NE1 TRP A 184     -14.253  68.590  68.406  1.00227.59           N  
ANISOU 1258  NE1 TRP A 184    43622  21354  21497   -391  -3382   -257       N  
ATOM   1259  CE2 TRP A 184     -13.108  67.898  68.104  1.00215.85           C  
ANISOU 1259  CE2 TRP A 184    41799  20022  20189   -671  -3577   -156       C  
ATOM   1260  CE3 TRP A 184     -12.493  65.845  66.977  1.00176.82           C  
ANISOU 1260  CE3 TRP A 184    35889  15611  15680   -828  -3432    -82       C  
ATOM   1261  CZ2 TRP A 184     -11.773  68.192  68.383  1.00188.04           C  
ANISOU 1261  CZ2 TRP A 184    38410  16399  16636   -968  -3978    -54       C  
ATOM   1262  CZ3 TRP A 184     -11.175  66.138  67.252  1.00159.97           C  
ANISOU 1262  CZ3 TRP A 184    33866  13400  13513  -1096  -3816     11       C  
ATOM   1263  CH2 TRP A 184     -10.822  67.297  67.946  1.00173.02           C  
ANISOU 1263  CH2 TRP A 184    36055  14744  14940  -1180  -4086     31       C  
ATOM   1264  N   PRO A 185     -17.395  64.666  69.697  1.00180.94           N  
ANISOU 1264  N   PRO A 185    37104  16020  15623    280  -2112   -447       N  
ATOM   1265  CA  PRO A 185     -18.635  64.646  70.489  1.00175.58           C  
ANISOU 1265  CA  PRO A 185    36661  15325  14724    565  -1799   -526       C  
ATOM   1266  C   PRO A 185     -19.280  65.937  71.012  1.00169.42           C  
ANISOU 1266  C   PRO A 185    36370  14334  13667    806  -1773   -608       C  
ATOM   1267  O   PRO A 185     -20.215  65.843  71.789  1.00206.67           O  
ANISOU 1267  O   PRO A 185    41287  19060  18177   1045  -1521   -670       O  
ATOM   1268  CB  PRO A 185     -18.170  63.819  71.700  1.00174.19           C  
ANISOU 1268  CB  PRO A 185    36703  15058  14424    491  -1862   -509       C  
ATOM   1269  CG  PRO A 185     -16.703  64.172  71.837  1.00185.12           C  
ANISOU 1269  CG  PRO A 185    38246  16255  15834    232  -2291   -449       C  
ATOM   1270  CD  PRO A 185     -16.189  64.295  70.422  1.00191.57           C  
ANISOU 1270  CD  PRO A 185    38615  17237  16936     67  -2407   -392       C  
ATOM   1271  N   GLU A 186     -18.776  67.092  70.583  1.00160.92           N  
ANISOU 1271  N   GLU A 186    35479  13083  12578    741  -2035   -602       N  
ATOM   1272  CA  GLU A 186     -19.236  68.413  71.076  1.00186.52           C  
ANISOU 1272  CA  GLU A 186    39257  16070  15539    962  -2087   -682       C  
ATOM   1273  C   GLU A 186     -20.758  68.408  71.293  1.00194.61           C  
ANISOU 1273  C   GLU A 186    40294  17229  16418   1340  -1674   -777       C  
ATOM   1274  O   GLU A 186     -21.210  68.877  72.365  1.00164.17           O  
ANISOU 1274  O   GLU A 186    36923  13203  12249   1570  -1623   -852       O  
ATOM   1275  CB  GLU A 186     -18.876  69.525  70.085  1.00207.42           C  
ANISOU 1275  CB  GLU A 186    41915  18622  18271    871  -2319   -660       C  
ATOM   1276  CG  GLU A 186     -17.427  69.966  70.149  1.00208.23           C  
ANISOU 1276  CG  GLU A 186    42207  18517  18392    533  -2777   -571       C  
ATOM   1277  CD  GLU A 186     -17.072  71.078  69.174  1.00204.22           C  
ANISOU 1277  CD  GLU A 186    41722  17919  17950    411  -3020   -533       C  
ATOM   1278  OE1 GLU A 186     -17.991  71.600  68.511  1.00185.35           O  
ANISOU 1278  OE1 GLU A 186    39266  15587  15569    623  -2840   -593       O  
ATOM   1279  OE2 GLU A 186     -15.879  71.420  69.078  1.00218.86           O  
ANISOU 1279  OE2 GLU A 186    43658  19656  19840     96  -3394   -437       O  
ATOM   1280  N   HIS A 187     -21.502  67.946  70.281  1.00210.93           N  
ANISOU 1280  N   HIS A 187    41848  19598  18697   1404  -1404   -772       N  
ATOM   1281  CA  HIS A 187     -22.976  67.726  70.283  1.00211.47           C  
ANISOU 1281  CA  HIS A 187    41767  19894  18687   1724   -982   -837       C  
ATOM   1282  C   HIS A 187     -23.228  66.224  70.149  1.00182.47           C  
ANISOU 1282  C   HIS A 187    37615  16520  15195   1617   -743   -777       C  
ATOM   1283  O   HIS A 187     -22.319  65.483  69.785  1.00173.44           O  
ANISOU 1283  O   HIS A 187    36214  15414  14270   1330   -905   -700       O  
ATOM   1284  CB  HIS A 187     -23.633  68.555  69.164  1.00206.69           C  
ANISOU 1284  CB  HIS A 187    40995  19368  18168   1879   -905   -874       C  
ATOM   1285  CG  HIS A 187     -23.370  70.023  69.265  1.00226.64           C  
ANISOU 1285  CG  HIS A 187    44023  21578  20512   1973  -1169   -929       C  
ATOM   1286  ND1 HIS A 187     -23.930  70.810  70.255  1.00234.76           N  
ANISOU 1286  ND1 HIS A 187    45593  22417  21187   2285  -1130  -1028       N  
ATOM   1287  CD2 HIS A 187     -22.610  70.850  68.514  1.00216.35           C  
ANISOU 1287  CD2 HIS A 187    42784  20109  19310   1795  -1487   -895       C  
ATOM   1288  CE1 HIS A 187     -23.530  72.058  70.107  1.00197.03           C  
ANISOU 1288  CE1 HIS A 187    41214  17346  16302   2300  -1426  -1057       C  
ATOM   1289  NE2 HIS A 187     -22.718  72.109  69.045  1.00212.90           N  
ANISOU 1289  NE2 HIS A 187    42938  19365  18587   1986  -1651   -970       N  
ATOM   1290  N   PRO A 188     -24.445  65.699  70.429  1.00166.28           N  
ANISOU 1290  N   PRO A 188    35425  14699  13052   1835   -365   -804       N  
ATOM   1291  CA  PRO A 188     -24.665  64.244  70.333  1.00171.38           C  
ANISOU 1291  CA  PRO A 188    35654  15607  13855   1700   -169   -735       C  
ATOM   1292  C   PRO A 188     -24.137  63.576  69.059  1.00219.28           C  
ANISOU 1292  C   PRO A 188    41201  21825  20290   1449   -252   -662       C  
ATOM   1293  O   PRO A 188     -24.284  64.153  67.981  1.00285.99           O  
ANISOU 1293  O   PRO A 188    49440  30333  28889   1476   -265   -671       O  
ATOM   1294  CB  PRO A 188     -26.199  64.138  70.390  1.00149.58           C  
ANISOU 1294  CB  PRO A 188    32749  13111  10972   1986    243   -768       C  
ATOM   1295  CG  PRO A 188     -26.629  65.339  71.206  1.00147.39           C  
ANISOU 1295  CG  PRO A 188    32988  12655  10356   2294    255   -867       C  
ATOM   1296  CD  PRO A 188     -25.653  66.436  70.834  1.00152.74           C  
ANISOU 1296  CD  PRO A 188    33935  13024  11075   2212   -118   -894       C  
ATOM   1297  N   ASN A 189     -23.569  62.373  69.208  1.00252.21           N  
ANISOU 1297  N   ASN A 189    45188  26056  24582   1228   -302   -596       N  
ATOM   1298  CA  ASN A 189     -22.879  61.675  68.106  1.00233.12           C  
ANISOU 1298  CA  ASN A 189    42324  23758  22490    991   -426   -531       C  
ATOM   1299  C   ASN A 189     -23.810  61.536  66.910  1.00242.62           C  
ANISOU 1299  C   ASN A 189    43076  25229  23878   1072   -183   -526       C  
ATOM   1300  O   ASN A 189     -23.355  61.657  65.764  1.00259.97           O  
ANISOU 1300  O   ASN A 189    44979  27485  26312    957   -302   -502       O  
ATOM   1301  CB  ASN A 189     -22.335  60.307  68.537  1.00196.30           C  
ANISOU 1301  CB  ASN A 189    37556  19136  17893    803   -475   -473       C  
ATOM   1302  CG  ASN A 189     -21.041  60.422  69.316  1.00174.55           C  
ANISOU 1302  CG  ASN A 189    35133  16129  15060    649   -814   -461       C  
ATOM   1303  OD1 ASN A 189     -20.857  61.373  70.075  1.00178.64           O  
ANISOU 1303  OD1 ASN A 189    36089  16422  15362    725   -931   -501       O  
ATOM   1304  ND2 ASN A 189     -20.136  59.475  69.122  1.00137.28           N  
ANISOU 1304  ND2 ASN A 189    30213  11442  10505    442   -984   -406       N  
ATOM   1305  N   LYS A 190     -25.077  61.251  67.162  1.00233.55           N  
ANISOU 1305  N   LYS A 190    41856  24260  22621   1254    150   -539       N  
ATOM   1306  CA  LYS A 190     -26.049  61.138  66.051  1.00213.44           C  
ANISOU 1306  CA  LYS A 190    38879  21980  20237   1339    390   -530       C  
ATOM   1307  C   LYS A 190     -25.976  62.369  65.148  1.00218.15           C  
ANISOU 1307  C   LYS A 190    39466  22510  20909   1422    285   -574       C  
ATOM   1308  O   LYS A 190     -25.806  62.223  63.908  1.00259.42           O  
ANISOU 1308  O   LYS A 190    44315  27854  26398   1314    246   -543       O  
ATOM   1309  CB  LYS A 190     -27.450  60.896  66.626  1.00206.74           C  
ANISOU 1309  CB  LYS A 190    38026  21330  19196   1551    753   -538       C  
ATOM   1310  CG  LYS A 190     -27.601  59.638  67.475  1.00196.11           C  
ANISOU 1310  CG  LYS A 190    36676  20068  17767   1442    865   -477       C  
ATOM   1311  CD  LYS A 190     -27.215  58.351  66.766  1.00181.13           C  
ANISOU 1311  CD  LYS A 190    34394  18289  16136   1187    814   -397       C  
ATOM   1312  CE  LYS A 190     -26.647  57.300  67.697  1.00170.37           C  
ANISOU 1312  CE  LYS A 190    33190  16840  14701   1015    720   -350       C  
ATOM   1313  NZ  LYS A 190     -25.290  57.666  68.171  1.00188.67           N  
ANISOU 1313  NZ  LYS A 190    35821  18867  16997    916    380   -378       N  
ATOM   1314  N   ILE A 191     -26.187  63.531  65.754  1.00224.47           N  
ANISOU 1314  N   ILE A 191    40681  23135  21472   1625    255   -646       N  
ATOM   1315  CA  ILE A 191     -26.349  64.806  65.027  1.00208.70           C  
ANISOU 1315  CA  ILE A 191    38751  21059  19484   1759    181   -698       C  
ATOM   1316  C   ILE A 191     -25.207  64.985  64.050  1.00213.32           C  
ANISOU 1316  C   ILE A 191    39176  21561  20315   1499   -120   -653       C  
ATOM   1317  O   ILE A 191     -25.502  65.498  62.948  1.00184.48           O  
ANISOU 1317  O   ILE A 191    35301  17988  16802   1537   -102   -659       O  
ATOM   1318  CB  ILE A 191     -26.503  66.009  65.987  1.00205.66           C  
ANISOU 1318  CB  ILE A 191    38941  20426  18773   1996    114   -783       C  
ATOM   1319  CG1 ILE A 191     -27.663  65.827  66.974  1.00196.23           C  
ANISOU 1319  CG1 ILE A 191    37890  19356  17311   2279    436   -828       C  
ATOM   1320  CG2 ILE A 191     -26.649  67.310  65.208  1.00191.13           C  
ANISOU 1320  CG2 ILE A 191    37198  18482  16939   2127      9   -836       C  
ATOM   1321  CD1 ILE A 191     -29.000  65.543  66.326  1.00172.63           C  
ANISOU 1321  CD1 ILE A 191    34495  16711  14385   2463    792   -828       C  
ATOM   1322  N   TYR A 192     -23.981  64.682  64.444  1.00229.71           N  
ANISOU 1322  N   TYR A 192    41376  23485  22418   1261   -391   -610       N  
ATOM   1323  CA  TYR A 192     -22.790  64.958  63.600  1.00194.17           C  
ANISOU 1323  CA  TYR A 192    36748  18914  18113   1008   -706   -559       C  
ATOM   1324  C   TYR A 192     -22.530  63.791  62.650  1.00168.24           C  
ANISOU 1324  C   TYR A 192    32921  15878  15123    828   -659   -494       C  
ATOM   1325  O   TYR A 192     -22.498  63.965  61.385  1.00109.15           O  
ANISOU 1325  O   TYR A 192    25103   8521   7849    767   -676   -471       O  
ATOM   1326  CB  TYR A 192     -21.566  65.201  64.497  1.00205.73           C  
ANISOU 1326  CB  TYR A 192    38595  20118  19453    841  -1034   -537       C  
ATOM   1327  CG  TYR A 192     -20.218  64.814  63.929  1.00208.57           C  
ANISOU 1327  CG  TYR A 192    38726  20500  20019    530  -1320   -455       C  
ATOM   1328  CD1 TYR A 192     -19.552  65.618  63.012  1.00182.36           C  
ANISOU 1328  CD1 TYR A 192    35328  17147  16811    384  -1553   -417       C  
ATOM   1329  CD2 TYR A 192     -19.587  63.644  64.332  1.00232.04           C  
ANISOU 1329  CD2 TYR A 192    41567  23537  23058    383  -1368   -412       C  
ATOM   1330  CE1 TYR A 192     -18.319  65.257  62.491  1.00173.82           C  
ANISOU 1330  CE1 TYR A 192    34006  16133  15902    107  -1803   -335       C  
ATOM   1331  CE2 TYR A 192     -18.347  63.279  63.833  1.00212.21           C  
ANISOU 1331  CE2 TYR A 192    38835  21074  20719    130  -1628   -341       C  
ATOM   1332  CZ  TYR A 192     -17.711  64.085  62.907  1.00180.96           C  
ANISOU 1332  CZ  TYR A 192    34768  17118  16869     -6  -1838   -300       C  
ATOM   1333  OH  TYR A 192     -16.494  63.708  62.419  1.00147.35           O  
ANISOU 1333  OH  TYR A 192    30264  12954  12767   -246  -2082   -224       O  
ATOM   1334  N   GLU A 193     -22.351  62.614  63.248  1.00205.86           N  
ANISOU 1334  N   GLU A 193    37618  20705  19894    750   -608   -465       N  
ATOM   1335  CA  GLU A 193     -22.103  61.355  62.514  1.00181.93           C  
ANISOU 1335  CA  GLU A 193    34130  17886  17108    599   -572   -409       C  
ATOM   1336  C   GLU A 193     -23.076  61.154  61.364  1.00179.88           C  
ANISOU 1336  C   GLU A 193    33461  17868  17018    683   -330   -409       C  
ATOM   1337  O   GLU A 193     -22.629  60.896  60.219  1.00182.35           O  
ANISOU 1337  O   GLU A 193    33417  18303  17565    557   -413   -374       O  
ATOM   1338  CB  GLU A 193     -22.162  60.140  63.443  1.00149.35           C  
ANISOU 1338  CB  GLU A 193    30051  13784  12908    568   -487   -391       C  
ATOM   1339  CG  GLU A 193     -21.130  60.159  64.562  1.00128.24           C  
ANISOU 1339  CG  GLU A 193    27751  10885  10087    465   -739   -385       C  
ATOM   1340  CD  GLU A 193     -19.756  59.630  64.199  1.00127.57           C  
ANISOU 1340  CD  GLU A 193    27502  10799  10168    236  -1031   -334       C  
ATOM   1341  OE1 GLU A 193     -19.102  60.217  63.322  1.00133.90           O  
ANISOU 1341  OE1 GLU A 193    28152  11620  11104    140  -1209   -314       O  
ATOM   1342  OE2 GLU A 193     -19.340  58.617  64.797  1.00125.94           O  
ANISOU 1342  OE2 GLU A 193    27318  10585   9948    158  -1083   -311       O  
ATOM   1343  N   LYS A 194     -24.369  61.232  61.671  1.00178.34           N  
ANISOU 1343  N   LYS A 194    33303  17756  16700    892    -37   -442       N  
ATOM   1344  CA  LYS A 194     -25.446  61.015  60.679  1.00158.73           C  
ANISOU 1344  CA  LYS A 194    30437  15517  14354    988    218   -437       C  
ATOM   1345  C   LYS A 194     -25.231  61.897  59.470  1.00139.55           C  
ANISOU 1345  C   LYS A 194    27850  13092  12079    975    108   -446       C  
ATOM   1346  O   LYS A 194     -25.394  61.414  58.321  1.00135.69           O  
ANISOU 1346  O   LYS A 194    26947  12791  11816    909    169   -415       O  
ATOM   1347  CB  LYS A 194     -26.822  61.340  61.275  1.00172.85           C  
ANISOU 1347  CB  LYS A 194    32354  17382  15936   1248    518   -477       C  
ATOM   1348  CG  LYS A 194     -27.391  60.289  62.217  1.00175.21           C  
ANISOU 1348  CG  LYS A 194    32677  17785  16110   1258    717   -446       C  
ATOM   1349  CD  LYS A 194     -28.823  60.537  62.668  1.00185.44           C  
ANISOU 1349  CD  LYS A 194    34008  19238  17210   1510   1043   -469       C  
ATOM   1350  CE  LYS A 194     -29.012  61.826  63.443  1.00171.04           C  
ANISOU 1350  CE  LYS A 194    32624  17242  15119   1752   1030   -553       C  
ATOM   1351  NZ  LYS A 194     -30.333  61.880  64.115  1.00143.39           N  
ANISOU 1351  NZ  LYS A 194    29175  13921  11385   2006   1355   -572       N  
ATOM   1352  N   VAL A 195     -24.854  63.145  59.722  1.00120.42           N  
ANISOU 1352  N   VAL A 195    25768  10457   9527   1027    -64   -485       N  
ATOM   1353  CA  VAL A 195     -24.668  64.149  58.655  1.00115.75           C  
ANISOU 1353  CA  VAL A 195    25101   9837   9042   1014   -191   -492       C  
ATOM   1354  C   VAL A 195     -23.517  63.737  57.745  1.00121.22           C  
ANISOU 1354  C   VAL A 195    25499  10586   9970    743   -415   -426       C  
ATOM   1355  O   VAL A 195     -23.710  63.586  56.513  1.00220.78           O  
ANISOU 1355  O   VAL A 195    37728  23369  22786    705   -359   -404       O  
ATOM   1356  CB  VAL A 195     -24.414  65.559  59.219  1.00108.76           C  
ANISOU 1356  CB  VAL A 195    24709   8674   7940   1101   -376   -539       C  
ATOM   1357  CG1 VAL A 195     -23.849  66.483  58.148  1.00 89.81           C  
ANISOU 1357  CG1 VAL A 195    22252   6212   5658    987   -599   -518       C  
ATOM   1358  CG2 VAL A 195     -25.667  66.153  59.846  1.00117.94           C  
ANISOU 1358  CG2 VAL A 195    26126   9812   8873   1430   -143   -619       C  
ATOM   1359  N   TYR A 196     -22.356  63.501  58.324  1.00107.42           N  
ANISOU 1359  N   TYR A 196    23903   8719   8191    565   -656   -393       N  
ATOM   1360  CA  TYR A 196     -21.145  63.273  57.507  1.00 92.21           C  
ANISOU 1360  CA  TYR A 196    21723   6857   6456    319   -900   -329       C  
ATOM   1361  C   TYR A 196     -21.319  61.994  56.696  1.00 89.49           C  
ANISOU 1361  C   TYR A 196    20897   6771   6333    274   -757   -302       C  
ATOM   1362  O   TYR A 196     -21.011  61.911  55.501  1.00 89.60           O  
ANISOU 1362  O   TYR A 196    20567   6933   6541    180   -807   -269       O  
ATOM   1363  CB  TYR A 196     -19.853  63.267  58.323  1.00 91.67           C  
ANISOU 1363  CB  TYR A 196    21899   6630   6299    143  -1196   -294       C  
ATOM   1364  CG  TYR A 196     -18.630  63.107  57.457  1.00 80.30           C  
ANISOU 1364  CG  TYR A 196    20173   5300   5038    -93  -1441   -222       C  
ATOM   1365  CD1 TYR A 196     -18.196  61.844  57.079  1.00 79.80           C  
ANISOU 1365  CD1 TYR A 196    19751   5431   5137   -174  -1427   -192       C  
ATOM   1366  CD2 TYR A 196     -17.939  64.207  56.974  1.00 69.14           C  
ANISOU 1366  CD2 TYR A 196    18838   3812   3620   -231  -1684   -181       C  
ATOM   1367  CE1 TYR A 196     -17.090  61.672  56.268  1.00 73.84           C  
ANISOU 1367  CE1 TYR A 196    18709   4815   4531   -360  -1637   -131       C  
ATOM   1368  CE2 TYR A 196     -16.829  64.051  56.161  1.00 66.73           C  
ANISOU 1368  CE2 TYR A 196    18234   3653   3465   -452  -1895   -104       C  
ATOM   1369  CZ  TYR A 196     -16.408  62.780  55.808  1.00 71.24           C  
ANISOU 1369  CZ  TYR A 196    18432   4441   4193   -503  -1863    -83       C  
ATOM   1370  OH  TYR A 196     -15.318  62.560  55.024  1.00 70.00           O  
ANISOU 1370  OH  TYR A 196    17961   4464   4169   -688  -2057    -12       O  
ATOM   1371  N   HIS A 197     -21.813  60.991  57.396  1.00104.71           N  
ANISOU 1371  N   HIS A 197    22831   8743   8211    340   -587   -312       N  
ATOM   1372  CA  HIS A 197     -22.045  59.613  56.906  1.00125.23           C  
ANISOU 1372  CA  HIS A 197    25062  11546  10972    303   -456   -286       C  
ATOM   1373  C   HIS A 197     -22.946  59.641  55.673  1.00129.82           C  
ANISOU 1373  C   HIS A 197    25293  12317  11713    376   -263   -288       C  
ATOM   1374  O   HIS A 197     -22.663  59.001  54.642  1.00203.68           O  
ANISOU 1374  O   HIS A 197    34288  21832  21270    287   -289   -259       O  
ATOM   1375  CB  HIS A 197     -22.614  58.794  58.080  1.00180.76           C  
ANISOU 1375  CB  HIS A 197    32276  18547  17855    372   -299   -295       C  
ATOM   1376  CG  HIS A 197     -23.352  57.558  57.700  1.00192.16           C  
ANISOU 1376  CG  HIS A 197    33421  20183  19405    380    -93   -271       C  
ATOM   1377  ND1 HIS A 197     -24.561  57.604  57.040  1.00181.03           N  
ANISOU 1377  ND1 HIS A 197    31793  18933  18054    490    159   -273       N  
ATOM   1378  CD2 HIS A 197     -23.095  56.254  57.940  1.00171.59           C  
ANISOU 1378  CD2 HIS A 197    30729  17624  16841    292   -112   -241       C  
ATOM   1379  CE1 HIS A 197     -24.994  56.382  56.853  1.00149.09           C  
ANISOU 1379  CE1 HIS A 197    27530  15029  14087    447    280   -237       C  
ATOM   1380  NE2 HIS A 197     -24.116  55.531  57.396  1.00137.96           N  
ANISOU 1380  NE2 HIS A 197    26209  13544  12666    328    114   -219       N  
ATOM   1381  N   ILE A 198     -24.069  60.322  55.826  1.00125.39           N  
ANISOU 1381  N   ILE A 198    24846  11747  11048    554    -62   -324       N  
ATOM   1382  CA  ILE A 198     -25.115  60.368  54.773  1.00117.30           C  
ANISOU 1382  CA  ILE A 198    23511  10907  10150    652    149   -327       C  
ATOM   1383  C   ILE A 198     -24.591  61.208  53.622  1.00126.03           C  
ANISOU 1383  C   ILE A 198    24478  12014  11391    585    -10   -322       C  
ATOM   1384  O   ILE A 198     -24.958  60.955  52.465  1.00172.66           O  
ANISOU 1384  O   ILE A 198    30033  18092  17479    575     74   -305       O  
ATOM   1385  CB  ILE A 198     -26.466  60.893  55.314  1.00107.18           C  
ANISOU 1385  CB  ILE A 198    22387   9637   8697    887    407   -368       C  
ATOM   1386  CG1 ILE A 198     -27.157  59.865  56.218  1.00110.32           C  
ANISOU 1386  CG1 ILE A 198    22807  10120   8989    929    614   -350       C  
ATOM   1387  CG2 ILE A 198     -27.384  61.347  54.184  1.00 89.39           C  
ANISOU 1387  CG2 ILE A 198    19868   7536   6558    999    561   -377       C  
ATOM   1388  CD1 ILE A 198     -27.481  58.548  55.551  1.00 97.94           C  
ANISOU 1388  CD1 ILE A 198    20851   8760   7600    826    725   -294       C  
ATOM   1389  N   CYS A 199     -23.770  62.205  53.932  1.00134.65           N  
ANISOU 1389  N   CYS A 199    25853  12917  12387    528   -243   -329       N  
ATOM   1390  CA  CYS A 199     -23.205  63.087  52.885  1.00141.43           C  
ANISOU 1390  CA  CYS A 199    26616  13770  13351    431   -423   -308       C  
ATOM   1391  C   CYS A 199     -22.311  62.302  51.939  1.00142.31           C  
ANISOU 1391  C   CYS A 199    26344  14048  13676    237   -544   -253       C  
ATOM   1392  O   CYS A 199     -22.498  62.386  50.718  1.00141.68           O  
ANISOU 1392  O   CYS A 199    25962  14112  13758    216   -508   -238       O  
ATOM   1393  CB  CYS A 199     -22.442  64.254  53.504  1.00140.78           C  
ANISOU 1393  CB  CYS A 199    26947  13441  13102    372   -680   -310       C  
ATOM   1394  SG  CYS A 199     -23.513  65.634  53.985  1.00170.72           S  
ANISOU 1394  SG  CYS A 199    31148  17044  16672    631   -583   -386       S  
ATOM   1395  N   VAL A 200     -21.370  61.557  52.494  1.00134.34           N  
ANISOU 1395  N   VAL A 200    25357  13026  12659    114   -685   -226       N  
ATOM   1396  CA  VAL A 200     -20.403  60.785  51.677  1.00123.18           C  
ANISOU 1396  CA  VAL A 200    23597  11782  11422    -43   -822   -179       C  
ATOM   1397  C   VAL A 200     -21.117  59.621  51.009  1.00114.57           C  
ANISOU 1397  C   VAL A 200    22160  10886  10482     22   -610   -187       C  
ATOM   1398  O   VAL A 200     -20.741  59.237  49.886  1.00114.68           O  
ANISOU 1398  O   VAL A 200    21832  11073  10667    -46   -654   -162       O  
ATOM   1399  CB  VAL A 200     -19.194  60.305  52.511  1.00157.39           C  
ANISOU 1399  CB  VAL A 200    28060  16050  15688   -168  -1043   -153       C  
ATOM   1400  CG1 VAL A 200     -19.588  59.367  53.644  1.00202.48           C  
ANISOU 1400  CG1 VAL A 200    33941  21693  21300    -85   -926   -182       C  
ATOM   1401  CG2 VAL A 200     -18.126  59.651  51.646  1.00143.53           C  
ANISOU 1401  CG2 VAL A 200    25952  14490  14093   -305  -1203   -108       C  
ATOM   1402  N   THR A 201     -22.118  59.070  51.687  1.00113.43           N  
ANISOU 1402  N   THR A 201    22110  10722  10266    147   -392   -214       N  
ATOM   1403  CA  THR A 201     -22.877  57.927  51.129  1.00 96.56           C  
ANISOU 1403  CA  THR A 201    19676   8758   8254    190   -197   -208       C  
ATOM   1404  C   THR A 201     -23.662  58.371  49.915  1.00 85.00           C  
ANISOU 1404  C   THR A 201    17956   7422   6918    249    -63   -210       C  
ATOM   1405  O   THR A 201     -23.588  57.715  48.886  1.00 78.71           O  
ANISOU 1405  O   THR A 201    16833   6782   6290    203    -56   -192       O  
ATOM   1406  CB  THR A 201     -23.860  57.369  52.167  1.00106.08           C  
ANISOU 1406  CB  THR A 201    21054   9925   9325    290     10   -220       C  
ATOM   1407  OG1 THR A 201     -23.128  56.757  53.230  1.00165.89           O  
ANISOU 1407  OG1 THR A 201    28842  17391  16796    225   -115   -214       O  
ATOM   1408  CG2 THR A 201     -24.830  56.368  51.585  1.00101.24           C  
ANISOU 1408  CG2 THR A 201    20160   9486   8820    322    218   -200       C  
ATOM   1409  N   VAL A 202     -24.366  59.491  50.039  1.00 92.43           N  
ANISOU 1409  N   VAL A 202    19061   8288   7768    359     24   -236       N  
ATOM   1410  CA  VAL A 202     -25.213  59.995  48.938  1.00113.65           C  
ANISOU 1410  CA  VAL A 202    21532  11087  10563    437    156   -242       C  
ATOM   1411  C   VAL A 202     -24.341  60.499  47.799  1.00119.85           C  
ANISOU 1411  C   VAL A 202    22137  11916  11483    313    -35   -219       C  
ATOM   1412  O   VAL A 202     -24.682  60.372  46.641  1.00108.51           O  
ANISOU 1412  O   VAL A 202    20402  10625  10200    311     29   -208       O  
ATOM   1413  CB  VAL A 202     -26.244  61.054  49.378  1.00110.15           C  
ANISOU 1413  CB  VAL A 202    21320  10560   9971    625    301   -283       C  
ATOM   1414  CG1 VAL A 202     -25.615  62.407  49.666  1.00120.28           C  
ANISOU 1414  CG1 VAL A 202    22925  11642  11135    616    100   -304       C  
ATOM   1415  CG2 VAL A 202     -27.350  61.206  48.343  1.00 92.00           C  
ANISOU 1415  CG2 VAL A 202    18752   8418   7785    731    492   -287       C  
ATOM   1416  N   LEU A 203     -23.239  61.133  48.137  1.00119.41           N  
ANISOU 1416  N   LEU A 203    22274  11737  11356    201   -276   -205       N  
ATOM   1417  CA  LEU A 203     -22.336  61.699  47.105  1.00125.95           C  
ANISOU 1417  CA  LEU A 203    22943  12624  12287     53   -477   -166       C  
ATOM   1418  C   LEU A 203     -21.555  60.623  46.359  1.00112.28           C  
ANISOU 1418  C   LEU A 203    20857  11089  10715    -60   -550   -132       C  
ATOM   1419  O   LEU A 203     -21.364  60.851  45.122  1.00123.63           O  
ANISOU 1419  O   LEU A 203    22025  12663  12282   -122   -589   -106       O  
ATOM   1420  CB  LEU A 203     -21.388  62.674  47.809  1.00144.10           C  
ANISOU 1420  CB  LEU A 203    25575  14737  14437    -53   -727   -147       C  
ATOM   1421  CG  LEU A 203     -20.543  63.551  46.889  1.00152.21           C  
ANISOU 1421  CG  LEU A 203    26516  15798  15517   -224   -947    -92       C  
ATOM   1422  CD1 LEU A 203     -21.416  64.353  45.937  1.00156.47           C  
ANISOU 1422  CD1 LEU A 203    26983  16354  16112   -144   -845   -106       C  
ATOM   1423  CD2 LEU A 203     -19.657  64.479  47.705  1.00169.11           C  
ANISOU 1423  CD2 LEU A 203    29023  17739  17489   -349  -1206    -61       C  
ATOM   1424  N   ILE A 204     -21.159  59.554  47.039  1.00110.40           N  
ANISOU 1424  N   ILE A 204    20629  10861  10456    -73   -569   -134       N  
ATOM   1425  CA  ILE A 204     -20.288  58.533  46.424  1.00106.75           C  
ANISOU 1425  CA  ILE A 204    19872  10572  10116   -155   -673   -111       C  
ATOM   1426  C   ILE A 204     -21.115  57.396  45.858  1.00107.40           C  
ANISOU 1426  C   ILE A 204    19708  10782  10316    -66   -481   -129       C  
ATOM   1427  O   ILE A 204     -20.533  56.664  45.115  1.00 84.48           O  
ANISOU 1427  O   ILE A 204    16547   8030   7522   -104   -554   -118       O  
ATOM   1428  CB  ILE A 204     -19.230  58.006  47.405  1.00127.85           C  
ANISOU 1428  CB  ILE A 204    22694  13184  12697   -222   -852   -101       C  
ATOM   1429  CG1 ILE A 204     -17.940  57.662  46.661  1.00107.76           C  
ANISOU 1429  CG1 ILE A 204    19879  10822  10242   -333  -1058    -64       C  
ATOM   1430  CG2 ILE A 204     -19.765  56.824  48.200  1.00161.88           C  
ANISOU 1430  CG2 ILE A 204    27087  17450  16970   -133   -724   -131       C  
ATOM   1431  CD1 ILE A 204     -16.804  57.275  47.571  1.00117.71           C  
ANISOU 1431  CD1 ILE A 204    21271  12041  11409   -401  -1263    -48       C  
ATOM   1432  N   TYR A 205     -22.406  57.335  46.148  1.00 90.51           N  
ANISOU 1432  N   TYR A 205    17644   8596   8147     45   -254   -151       N  
ATOM   1433  CA  TYR A 205     -23.211  56.197  45.659  1.00 61.23           C  
ANISOU 1433  CA  TYR A 205    13715   5008   4540    100    -87   -152       C  
ATOM   1434  C   TYR A 205     -24.514  56.668  45.038  1.00 66.55           C  
ANISOU 1434  C   TYR A 205    14282   5737   5265    188    125   -156       C  
ATOM   1435  O   TYR A 205     -24.707  56.525  43.836  1.00111.43           O  
ANISOU 1435  O   TYR A 205    19686  11556  11095    180    155   -147       O  
ATOM   1436  CB  TYR A 205     -23.478  55.195  46.780  1.00 55.36           C  
ANISOU 1436  CB  TYR A 205    13142   4192   3698    123    -26   -156       C  
ATOM   1437  CG  TYR A 205     -24.251  53.979  46.346  1.00 51.18           C  
ANISOU 1437  CG  TYR A 205    12422   3768   3254    145    111   -143       C  
ATOM   1438  CD1 TYR A 205     -23.597  52.881  45.807  1.00 55.70           C  
ANISOU 1438  CD1 TYR A 205    12823   4419   3919    104     -6   -140       C  
ATOM   1439  CD2 TYR A 205     -25.629  53.919  46.485  1.00 49.71           C  
ANISOU 1439  CD2 TYR A 205    12236   3610   3042    210    347   -129       C  
ATOM   1440  CE1 TYR A 205     -24.290  51.745  45.419  1.00 59.72           C  
ANISOU 1440  CE1 TYR A 205    13199   4999   4492    112     90   -124       C  
ATOM   1441  CE2 TYR A 205     -26.338  52.791  46.104  1.00 54.69           C  
ANISOU 1441  CE2 TYR A 205    12703   4335   3740    197    454   -101       C  
ATOM   1442  CZ  TYR A 205     -25.666  51.702  45.570  1.00 61.29           C  
ANISOU 1442  CZ  TYR A 205    13403   5215   4667    141    317    -98       C  
ATOM   1443  OH  TYR A 205     -26.346  50.583  45.185  1.00 57.32           O  
ANISOU 1443  OH  TYR A 205    12776   4781   4221    119    393    -68       O  
ATOM   1444  N   PHE A 206     -25.424  57.166  45.853  1.00 73.53           N  
ANISOU 1444  N   PHE A 206    15382   6532   6025    283    276   -170       N  
ATOM   1445  CA  PHE A 206     -26.845  57.356  45.465  1.00 79.58           C  
ANISOU 1445  CA  PHE A 206    16040   7379   6816    396    514   -171       C  
ATOM   1446  C   PHE A 206     -27.005  58.377  44.340  1.00 73.73           C  
ANISOU 1446  C   PHE A 206    15160   6684   6169    421    502   -178       C  
ATOM   1447  O   PHE A 206     -27.675  58.052  43.311  1.00 87.24           O  
ANISOU 1447  O   PHE A 206    16590   8538   8016    440    612   -163       O  
ATOM   1448  CB  PHE A 206     -27.693  57.751  46.677  1.00 89.03           C  
ANISOU 1448  CB  PHE A 206    17513   8489   7825    517    669   -187       C  
ATOM   1449  CG  PHE A 206     -27.969  56.600  47.608  1.00 96.39           C  
ANISOU 1449  CG  PHE A 206    18517   9428   8678    497    755   -165       C  
ATOM   1450  CD1 PHE A 206     -28.967  55.678  47.322  1.00 95.30           C  
ANISOU 1450  CD1 PHE A 206    18176   9437   8594    502    937   -126       C  
ATOM   1451  CD2 PHE A 206     -27.203  56.417  48.747  1.00102.44           C  
ANISOU 1451  CD2 PHE A 206    19557  10052   9311    453    635   -173       C  
ATOM   1452  CE1 PHE A 206     -29.206  54.609  48.170  1.00 97.76           C  
ANISOU 1452  CE1 PHE A 206    18570   9750   8822    454    996    -93       C  
ATOM   1453  CE2 PHE A 206     -27.446  55.347  49.595  1.00112.71           C  
ANISOU 1453  CE2 PHE A 206    20939  11351  10533    422    702   -148       C  
ATOM   1454  CZ  PHE A 206     -28.445  54.447  49.306  1.00110.69           C  
ANISOU 1454  CZ  PHE A 206    20491  11239  10325    417    881   -106       C  
ATOM   1455  N   LEU A 207     -26.364  59.528  44.468  1.00 68.56           N  
ANISOU 1455  N   LEU A 207    14692   5909   5446    403    352   -192       N  
ATOM   1456  CA  LEU A 207     -26.583  60.634  43.502  1.00 69.43           C  
ANISOU 1456  CA  LEU A 207    14733   6032   5614    428    331   -197       C  
ATOM   1457  C   LEU A 207     -25.961  60.330  42.147  1.00 83.16           C  
ANISOU 1457  C   LEU A 207    16146   7914   7535    306    229   -166       C  
ATOM   1458  O   LEU A 207     -26.646  60.417  41.135  1.00 65.80           O  
ANISOU 1458  O   LEU A 207    13730   5822   5449    348    329   -163       O  
ATOM   1459  CB  LEU A 207     -26.056  61.969  44.035  1.00 63.56           C  
ANISOU 1459  CB  LEU A 207    14323   5097   4727    422    171   -212       C  
ATOM   1460  CG  LEU A 207     -26.314  63.157  43.103  1.00 50.82           C  
ANISOU 1460  CG  LEU A 207    12692   3467   3150    447    131   -216       C  
ATOM   1461  CD1 LEU A 207     -27.738  63.673  43.259  1.00 50.03           C  
ANISOU 1461  CD1 LEU A 207    12677   3349   2982    674    345   -260       C  
ATOM   1462  CD2 LEU A 207     -25.304  64.266  43.343  1.00 49.10           C  
ANISOU 1462  CD2 LEU A 207    12748   3079   2829    334   -128   -202       C  
ATOM   1463  N   PRO A 208     -24.658  59.991  42.079  1.00 83.99           N  
ANISOU 1463  N   PRO A 208    16206   8040   7665    162     27   -143       N  
ATOM   1464  CA  PRO A 208     -24.059  59.678  40.788  1.00 74.66           C  
ANISOU 1464  CA  PRO A 208    14702   7026   6638     66    -60   -115       C  
ATOM   1465  C   PRO A 208     -24.696  58.515  40.025  1.00 58.38           C  
ANISOU 1465  C   PRO A 208    12345   5121   4715    114     84   -117       C  
ATOM   1466  O   PRO A 208     -24.650  58.494  38.808  1.00 49.12           O  
ANISOU 1466  O   PRO A 208    10916   4080   3667     84     73   -104       O  
ATOM   1467  CB  PRO A 208     -22.604  59.311  41.126  1.00 72.88           C  
ANISOU 1467  CB  PRO A 208    14491   6818   6380    -60   -279    -92       C  
ATOM   1468  CG  PRO A 208     -22.391  59.799  42.543  1.00 67.24           C  
ANISOU 1468  CG  PRO A 208    14152   5904   5490    -58   -341   -103       C  
ATOM   1469  CD  PRO A 208     -23.749  59.720  43.203  1.00 65.88           C  
ANISOU 1469  CD  PRO A 208    14129   5644   5256     99   -110   -140       C  
ATOM   1470  N   LEU A 209     -25.282  57.578  40.756  1.00 58.31           N  
ANISOU 1470  N   LEU A 209    12393   5091   4671    177    208   -129       N  
ATOM   1471  CA  LEU A 209     -26.005  56.426  40.185  1.00 49.28           C  
ANISOU 1471  CA  LEU A 209    11022   4067   3634    209    340   -122       C  
ATOM   1472  C   LEU A 209     -27.343  56.876  39.612  1.00 53.92           C  
ANISOU 1472  C   LEU A 209    11508   4705   4274    294    533   -118       C  
ATOM   1473  O   LEU A 209     -27.834  56.294  38.641  1.00 65.11           O  
ANISOU 1473  O   LEU A 209    12676   6245   5816    295    602   -104       O  
ATOM   1474  CB  LEU A 209     -26.213  55.334  41.244  1.00 44.86           C  
ANISOU 1474  CB  LEU A 209    10593   3455   2994    222    394   -120       C  
ATOM   1475  CG  LEU A 209     -25.341  54.081  41.079  1.00 55.23           C  
ANISOU 1475  CG  LEU A 209    11810   4819   4356    165    258   -119       C  
ATOM   1476  CD1 LEU A 209     -23.863  54.424  40.934  1.00 47.42           C  
ANISOU 1476  CD1 LEU A 209    10812   3842   3361    102     30   -127       C  
ATOM   1477  CD2 LEU A 209     -25.531  53.106  42.236  1.00 77.24           C  
ANISOU 1477  CD2 LEU A 209    14784   7520   7040    166    290   -114       C  
ATOM   1478  N   LEU A 210     -27.930  57.886  40.223  1.00 63.72           N  
ANISOU 1478  N   LEU A 210    12949   5852   5409    377    613   -133       N  
ATOM   1479  CA  LEU A 210     -29.160  58.505  39.702  1.00 69.14           C  
ANISOU 1479  CA  LEU A 210    13552   6590   6126    486    782   -136       C  
ATOM   1480  C   LEU A 210     -28.847  59.175  38.375  1.00 73.45           C  
ANISOU 1480  C   LEU A 210    13922   7191   6793    444    690   -132       C  
ATOM   1481  O   LEU A 210     -29.588  59.009  37.400  1.00 60.40           O  
ANISOU 1481  O   LEU A 210    12037   5654   5256    474    790   -120       O  
ATOM   1482  CB  LEU A 210     -29.693  59.504  40.737  1.00 71.96           C  
ANISOU 1482  CB  LEU A 210    14207   6822   6311    613    856   -165       C  
ATOM   1483  CG  LEU A 210     -31.154  59.919  40.571  1.00 76.23           C  
ANISOU 1483  CG  LEU A 210    14687   7438   6837    776   1074   -171       C  
ATOM   1484  CD1 LEU A 210     -31.742  60.355  41.905  1.00 81.40           C  
ANISOU 1484  CD1 LEU A 210    15628   8011   7288    922   1188   -198       C  
ATOM   1485  CD2 LEU A 210     -31.301  61.025  39.531  1.00 71.20           C  
ANISOU 1485  CD2 LEU A 210    13985   6799   6268    822   1028   -187       C  
ATOM   1486  N   VAL A 211     -27.743  59.904  38.361  1.00 75.86           N  
ANISOU 1486  N   VAL A 211    14341   7418   7062    360    494   -135       N  
ATOM   1487  CA  VAL A 211     -27.327  60.710  37.193  1.00 72.74           C  
ANISOU 1487  CA  VAL A 211    13822   7064   6748    293    380   -121       C  
ATOM   1488  C   VAL A 211     -26.989  59.802  36.006  1.00 61.71           C  
ANISOU 1488  C   VAL A 211    12086   5848   5514    216    355    -98       C  
ATOM   1489  O   VAL A 211     -27.446  60.060  34.892  1.00 51.32           O  
ANISOU 1489  O   VAL A 211    10580   4617   4301    227    398    -89       O  
ATOM   1490  CB  VAL A 211     -26.153  61.628  37.584  1.00 57.00           C  
ANISOU 1490  CB  VAL A 211    12046   4955   4655    184    156   -109       C  
ATOM   1491  CG1 VAL A 211     -25.527  62.304  36.373  1.00 45.97           C  
ANISOU 1491  CG1 VAL A 211    10500   3631   3335     63     12    -74       C  
ATOM   1492  CG2 VAL A 211     -26.583  62.663  38.619  1.00 54.40           C  
ANISOU 1492  CG2 VAL A 211    12083   4426   4158    281    170   -139       C  
ATOM   1493  N   ILE A 212     -26.192  58.776  36.242  1.00 45.15           N  
ANISOU 1493  N   ILE A 212     9926   3800   3425    153    278    -92       N  
ATOM   1494  CA  ILE A 212     -25.846  57.814  35.176  1.00 42.73           C  
ANISOU 1494  CA  ILE A 212     9322   3661   3249    112    247    -81       C  
ATOM   1495  C   ILE A 212     -27.120  57.095  34.745  1.00 44.71           C  
ANISOU 1495  C   ILE A 212     9430   3970   3587    194    436    -83       C  
ATOM   1496  O   ILE A 212     -27.336  56.895  33.542  1.00 38.50           O  
ANISOU 1496  O   ILE A 212     8408   3300   2920    187    453    -74       O  
ATOM   1497  CB  ILE A 212     -24.743  56.850  35.653  1.00 42.33           C  
ANISOU 1497  CB  ILE A 212     9277   3640   3166     64    115    -85       C  
ATOM   1498  CG1 ILE A 212     -23.421  57.573  35.930  1.00 34.15           C  
ANISOU 1498  CG1 ILE A 212     8331   2591   2053    -38    -87    -67       C  
ATOM   1499  CG2 ILE A 212     -24.570  55.722  34.648  1.00 45.88           C  
ANISOU 1499  CG2 ILE A 212     9455   4247   3728     72    103    -87       C  
ATOM   1500  CD1 ILE A 212     -22.310  56.643  36.361  1.00 31.80           C  
ANISOU 1500  CD1 ILE A 212     8014   2346   1719    -68   -224    -70       C  
ATOM   1501  N   GLY A 213     -27.933  56.714  35.723  1.00 43.95           N  
ANISOU 1501  N   GLY A 213     9474   3802   3421    258    568    -88       N  
ATOM   1502  CA  GLY A 213     -29.198  56.030  35.454  1.00 42.15           C  
ANISOU 1502  CA  GLY A 213     9119   3641   3253    312    747    -71       C  
ATOM   1503  C   GLY A 213     -30.005  56.786  34.435  1.00 43.49           C  
ANISOU 1503  C   GLY A 213     9136   3876   3510    358    832    -64       C  
ATOM   1504  O   GLY A 213     -30.497  56.194  33.466  1.00 31.06           O  
ANISOU 1504  O   GLY A 213     7338   2411   2053    349    881    -46       O  
ATOM   1505  N   TYR A 214     -30.123  58.085  34.640  1.00 46.88           N  
ANISOU 1505  N   TYR A 214     9705   4230   3876    409    833    -80       N  
ATOM   1506  CA  TYR A 214     -30.795  58.986  33.677  1.00 47.14           C  
ANISOU 1506  CA  TYR A 214     9629   4303   3977    462    884    -80       C  
ATOM   1507  C   TYR A 214     -30.110  58.937  32.323  1.00 36.82           C  
ANISOU 1507  C   TYR A 214     8105   3087   2797    367    762    -68       C  
ATOM   1508  O   TYR A 214     -30.734  58.648  31.323  1.00 30.29           O  
ANISOU 1508  O   TYR A 214     7062   2362   2083    380    829    -54       O  
ATOM   1509  CB  TYR A 214     -30.750  60.422  34.216  1.00 57.07           C  
ANISOU 1509  CB  TYR A 214    11143   5423   5115    526    843   -106       C  
ATOM   1510  CG  TYR A 214     -30.962  61.475  33.160  1.00 62.68           C  
ANISOU 1510  CG  TYR A 214    11790   6140   5885    544    804   -107       C  
ATOM   1511  CD1 TYR A 214     -32.212  61.656  32.590  1.00 55.42           C  
ANISOU 1511  CD1 TYR A 214    10741   5291   5024    660    956   -108       C  
ATOM   1512  CD2 TYR A 214     -29.906  62.244  32.690  1.00 65.96           C  
ANISOU 1512  CD2 TYR A 214    12260   6506   6295    429    607    -98       C  
ATOM   1513  CE1 TYR A 214     -32.414  62.593  31.592  1.00 73.47           C  
ANISOU 1513  CE1 TYR A 214    12975   7576   7364    679    909   -109       C  
ATOM   1514  CE2 TYR A 214     -30.090  63.185  31.692  1.00 75.82           C  
ANISOU 1514  CE2 TYR A 214    13461   7755   7590    426    558    -91       C  
ATOM   1515  CZ  TYR A 214     -31.350  63.355  31.141  1.00 91.03           C  
ANISOU 1515  CZ  TYR A 214    15277   9731   9578    558    709   -102       C  
ATOM   1516  OH  TYR A 214     -31.557  64.288  30.169  1.00140.78           O  
ANISOU 1516  OH  TYR A 214    21548  16020  15920    563    653    -98       O  
ATOM   1517  N   ALA A 215     -28.820  59.232  32.326  1.00 29.28           N  
ANISOU 1517  N   ALA A 215     7209   2106   1809    269    580    -67       N  
ATOM   1518  CA  ALA A 215     -28.018  59.381  31.095  1.00 26.34           C  
ANISOU 1518  CA  ALA A 215     6643   1841   1523    171    450    -49       C  
ATOM   1519  C   ALA A 215     -28.143  58.142  30.199  1.00 24.99           C  
ANISOU 1519  C   ALA A 215     6203   1816   1473    169    487    -44       C  
ATOM   1520  O   ALA A 215     -28.372  58.285  28.988  1.00 23.76           O  
ANISOU 1520  O   ALA A 215     5856   1755   1416    157    493    -33       O  
ATOM   1521  CB  ALA A 215     -26.579  59.653  31.458  1.00 24.45           C  
ANISOU 1521  CB  ALA A 215     6496   1587   1206     58    256    -38       C  
ATOM   1522  N   TYR A 216     -28.009  56.958  30.789  1.00 24.05           N  
ANISOU 1522  N   TYR A 216     6097   1703   1338    181    501    -53       N  
ATOM   1523  CA  TYR A 216     -28.058  55.715  30.008  1.00 21.27           C  
ANISOU 1523  CA  TYR A 216     5540   1461   1078    184    505    -53       C  
ATOM   1524  C   TYR A 216     -29.492  55.296  29.723  1.00 21.72           C  
ANISOU 1524  C   TYR A 216     5517   1530   1203    236    673    -37       C  
ATOM   1525  O   TYR A 216     -29.738  54.499  28.805  1.00 25.26           O  
ANISOU 1525  O   TYR A 216     5788   2066   1744    233    677    -29       O  
ATOM   1526  CB  TYR A 216     -27.296  54.588  30.702  1.00 20.19           C  
ANISOU 1526  CB  TYR A 216     5469   1313    886    177    421    -68       C  
ATOM   1527  CG  TYR A 216     -25.803  54.670  30.554  1.00 18.66           C  
ANISOU 1527  CG  TYR A 216     5242   1190    657    130    239    -78       C  
ATOM   1528  CD1 TYR A 216     -25.210  55.247  29.448  1.00 17.67           C  
ANISOU 1528  CD1 TYR A 216     4940   1193    579     86    158    -66       C  
ATOM   1529  CD2 TYR A 216     -24.979  54.134  31.522  1.00 22.79           C  
ANISOU 1529  CD2 TYR A 216     5898   1670   1090    127    143    -92       C  
ATOM   1530  CE1 TYR A 216     -23.832  55.296  29.315  1.00 19.96           C  
ANISOU 1530  CE1 TYR A 216     5167   1592    823     35     -5    -62       C  
ATOM   1531  CE2 TYR A 216     -23.601  54.183  31.412  1.00 24.70           C  
ANISOU 1531  CE2 TYR A 216     6086   2007   1292     89    -26    -95       C  
ATOM   1532  CZ  TYR A 216     -23.022  54.765  30.302  1.00 22.40           C  
ANISOU 1532  CZ  TYR A 216     5596   1870   1043     41    -98    -76       C  
ATOM   1533  OH  TYR A 216     -21.663  54.824  30.218  1.00 22.17           O  
ANISOU 1533  OH  TYR A 216     5489   1974    960     -4   -262    -65       O  
ATOM   1534  N   THR A 217     -30.437  55.795  30.509  1.00 21.02           N  
ANISOU 1534  N   THR A 217     5558   1368   1060    288    805    -29       N  
ATOM   1535  CA  THR A 217     -31.854  55.528  30.211  1.00 25.31           C  
ANISOU 1535  CA  THR A 217     5994   1961   1661    334    970      0       C  
ATOM   1536  C   THR A 217     -32.213  56.180  28.895  1.00 31.35           C  
ANISOU 1536  C   THR A 217     6578   2799   2533    346    978      4       C  
ATOM   1537  O   THR A 217     -32.809  55.525  28.060  1.00 34.03           O  
ANISOU 1537  O   THR A 217     6737   3222   2969    335   1020     27       O  
ATOM   1538  CB  THR A 217     -32.873  55.892  31.291  1.00 28.02           C  
ANISOU 1538  CB  THR A 217     6478   2257   1910    409   1129     11       C  
ATOM   1539  OG1 THR A 217     -32.480  57.143  31.845  1.00 39.44           O  
ANISOU 1539  OG1 THR A 217     8113   3607   3265    458   1093    -20       O  
ATOM   1540  CG2 THR A 217     -33.004  54.812  32.342  1.00 33.19           C  
ANISOU 1540  CG2 THR A 217     7235   2887   2488    380   1171     31       C  
ATOM   1541  N   VAL A 218     -31.792  57.423  28.705  1.00 31.60           N  
ANISOU 1541  N   VAL A 218     6674   2790   2542    354    916    -13       N  
ATOM   1542  CA  VAL A 218     -32.149  58.218  27.514  1.00 34.30           C  
ANISOU 1542  CA  VAL A 218     6882   3181   2968    365    914     -7       C  
ATOM   1543  C   VAL A 218     -31.286  57.825  26.324  1.00 38.13           C  
ANISOU 1543  C   VAL A 218     7184   3764   3539    279    789     -3       C  
ATOM   1544  O   VAL A 218     -31.826  57.839  25.152  1.00 40.76           O  
ANISOU 1544  O   VAL A 218     7334   4176   3977    283    818     10       O  
ATOM   1545  CB  VAL A 218     -32.015  59.736  27.781  1.00 37.20           C  
ANISOU 1545  CB  VAL A 218     7429   3447   3257    398    871    -23       C  
ATOM   1546  CG1 VAL A 218     -32.952  60.214  28.883  1.00 51.56           C  
ANISOU 1546  CG1 VAL A 218     9432   5181   4976    527   1003    -37       C  
ATOM   1547  CG2 VAL A 218     -30.585  60.173  28.084  1.00 35.69           C  
ANISOU 1547  CG2 VAL A 218     7368   3200   2991    297    691    -28       C  
ATOM   1548  N   VAL A 219     -30.032  57.469  26.576  1.00 33.97           N  
ANISOU 1548  N   VAL A 219     6692   3248   2965    214    658    -13       N  
ATOM   1549  CA  VAL A 219     -29.146  56.976  25.496  1.00 34.33           C  
ANISOU 1549  CA  VAL A 219     6550   3423   3069    156    544    -12       C  
ATOM   1550  C   VAL A 219     -29.639  55.601  25.059  1.00 45.74           C  
ANISOU 1550  C   VAL A 219     7863   4927   4587    192    594    -15       C  
ATOM   1551  O   VAL A 219     -29.658  55.312  23.845  1.00 47.46           O  
ANISOU 1551  O   VAL A 219     7898   5246   4888    186    570    -12       O  
ATOM   1552  CB  VAL A 219     -27.667  56.965  25.930  1.00 23.74           C  
ANISOU 1552  CB  VAL A 219     5267   2109   1644     93    389    -18       C  
ATOM   1553  CG1 VAL A 219     -26.809  56.194  24.942  1.00 23.12           C  
ANISOU 1553  CG1 VAL A 219     4981   2197   1604     76    292    -24       C  
ATOM   1554  CG2 VAL A 219     -27.117  58.375  26.125  1.00 18.37           C  
ANISOU 1554  CG2 VAL A 219     4705   1380    893     19    304      0       C  
ATOM   1555  N   GLY A 220     -30.097  54.805  26.028  1.00 37.39           N  
ANISOU 1555  N   GLY A 220     6914   3799   3490    220    660    -15       N  
ATOM   1556  CA  GLY A 220     -30.681  53.494  25.735  1.00 38.97           C  
ANISOU 1556  CA  GLY A 220     7036   4027   3742    232    695     -5       C  
ATOM   1557  C   GLY A 220     -31.938  53.598  24.890  1.00 39.26           C  
ANISOU 1557  C   GLY A 220     6932   4106   3878    242    804     26       C  
ATOM   1558  O   GLY A 220     -32.132  52.833  23.952  1.00 34.88           O  
ANISOU 1558  O   GLY A 220     6244   3611   3396    232    777     33       O  
ATOM   1559  N   ILE A 221     -32.778  54.553  25.230  1.00 28.16           N  
ANISOU 1559  N   ILE A 221     5566   2669   2464    271    919     43       N  
ATOM   1560  CA  ILE A 221     -34.029  54.888  24.509  1.00 31.88           C  
ANISOU 1560  CA  ILE A 221     5903   3191   3019    298   1029     75       C  
ATOM   1561  C   ILE A 221     -33.707  55.241  23.071  1.00 31.99           C  
ANISOU 1561  C   ILE A 221     5756   3274   3124    280    952     67       C  
ATOM   1562  O   ILE A 221     -34.455  54.816  22.151  1.00 20.06           O  
ANISOU 1562  O   ILE A 221     4091   1825   1706    274    986     92       O  
ATOM   1563  CB  ILE A 221     -34.731  56.060  25.238  1.00 38.54           C  
ANISOU 1563  CB  ILE A 221     6852   3987   3804    373   1141     76       C  
ATOM   1564  CG1 ILE A 221     -35.484  55.579  26.483  1.00 41.40           C  
ANISOU 1564  CG1 ILE A 221     7315   4329   4085    401   1266    102       C  
ATOM   1565  CG2 ILE A 221     -35.639  56.843  24.288  1.00 44.93           C  
ANISOU 1565  CG2 ILE A 221     7527   4849   4694    423   1203     91       C  
ATOM   1566  CD1 ILE A 221     -36.055  56.695  27.342  1.00 43.99           C  
ANISOU 1566  CD1 ILE A 221     7778   4616   4320    509   1371     90       C  
ATOM   1567  N   THR A 222     -32.614  55.962  22.878  1.00 27.52           N  
ANISOU 1567  N   THR A 222     5225   2705   2526    258    844     40       N  
ATOM   1568  CA  THR A 222     -32.211  56.469  21.550  1.00 26.72           C  
ANISOU 1568  CA  THR A 222     4982   2683   2488    226    766     39       C  
ATOM   1569  C   THR A 222     -31.783  55.313  20.662  1.00 27.00           C  
ANISOU 1569  C   THR A 222     4870   2812   2573    208    697     32       C  
ATOM   1570  O   THR A 222     -32.227  55.231  19.486  1.00 25.16           O  
ANISOU 1570  O   THR A 222     4486   2645   2427    207    702     44       O  
ATOM   1571  CB  THR A 222     -31.041  57.462  21.644  1.00 24.21           C  
ANISOU 1571  CB  THR A 222     4740   2359   2098    173    651     29       C  
ATOM   1572  OG1 THR A 222     -31.489  58.595  22.388  1.00 17.34           O  
ANISOU 1572  OG1 THR A 222     4039   1376   1172    202    697     31       O  
ATOM   1573  CG2 THR A 222     -30.514  57.905  20.291  1.00 19.23           C  
ANISOU 1573  CG2 THR A 222     3956   1834   1513    116    563     40       C  
ATOM   1574  N   LEU A 223     -30.923  54.449  21.191  1.00 25.82           N  
ANISOU 1574  N   LEU A 223     4777   2668   2364    208    623      9       N  
ATOM   1575  CA  LEU A 223     -30.345  53.338  20.406  1.00 33.85           C  
ANISOU 1575  CA  LEU A 223     5688   3772   3399    226    531    -12       C  
ATOM   1576  C   LEU A 223     -31.324  52.175  20.274  1.00 38.90           C  
ANISOU 1576  C   LEU A 223     6318   4373   4088    244    579      2       C  
ATOM   1577  O   LEU A 223     -31.532  51.696  19.155  1.00 31.01           O  
ANISOU 1577  O   LEU A 223     5196   3432   3150    255    549      2       O  
ATOM   1578  CB  LEU A 223     -29.012  52.923  21.032  1.00 33.90           C  
ANISOU 1578  CB  LEU A 223     5766   3805   3308    239    418    -45       C  
ATOM   1579  CG  LEU A 223     -27.885  53.916  20.752  1.00 37.56           C  
ANISOU 1579  CG  LEU A 223     6176   4369   3726    195    332    -44       C  
ATOM   1580  CD1 LEU A 223     -26.695  53.672  21.655  1.00 37.33           C  
ANISOU 1580  CD1 LEU A 223     6234   4357   3592    198    234    -64       C  
ATOM   1581  CD2 LEU A 223     -27.468  53.857  19.290  1.00 40.93           C  
ANISOU 1581  CD2 LEU A 223     6399   4960   4191    200    274    -48       C  
ATOM   1582  N   TRP A 224     -31.937  51.770  21.380  1.00 38.34           N  
ANISOU 1582  N   TRP A 224     6376   4206   3982    235    649     21       N  
ATOM   1583  CA  TRP A 224     -32.832  50.603  21.406  1.00 39.90           C  
ANISOU 1583  CA  TRP A 224     6589   4365   4205    216    677     54       C  
ATOM   1584  C   TRP A 224     -34.293  50.877  21.068  1.00 39.08           C  
ANISOU 1584  C   TRP A 224     6394   4275   4179    183    803    114       C  
ATOM   1585  O   TRP A 224     -35.069  49.906  21.161  1.00 49.83           O  
ANISOU 1585  O   TRP A 224     7768   5613   5550    137    821    159       O  
ATOM   1586  CB  TRP A 224     -32.721  49.857  22.740  1.00 40.51           C  
ANISOU 1586  CB  TRP A 224     6850   4351   4189    202    671     58       C  
ATOM   1587  CG  TRP A 224     -31.590  48.882  22.738  1.00 41.38           C  
ANISOU 1587  CG  TRP A 224     7031   4450   4240    242    515      7       C  
ATOM   1588  CD1 TRP A 224     -31.600  47.593  22.291  1.00 55.96           C  
ANISOU 1588  CD1 TRP A 224     8905   6273   6084    254    418      1       C  
ATOM   1589  CD2 TRP A 224     -30.248  49.152  23.162  1.00 41.39           C  
ANISOU 1589  CD2 TRP A 224     7085   4472   4167    289    424    -44       C  
ATOM   1590  NE1 TRP A 224     -30.357  47.034  22.429  1.00 64.92           N  
ANISOU 1590  NE1 TRP A 224    10111   7413   7143    332    277    -61       N  
ATOM   1591  CE2 TRP A 224     -29.505  47.969  22.958  1.00 46.87           C  
ANISOU 1591  CE2 TRP A 224     7823   5168   4815    350    282    -86       C  
ATOM   1592  CE3 TRP A 224     -29.614  50.280  23.692  1.00 41.58           C  
ANISOU 1592  CE3 TRP A 224     7134   4513   4152    282    436    -55       C  
ATOM   1593  CZ2 TRP A 224     -28.153  47.881  23.283  1.00 40.64           C  
ANISOU 1593  CZ2 TRP A 224     7072   4425   3945    416    165   -138       C  
ATOM   1594  CZ3 TRP A 224     -28.278  50.193  24.006  1.00 45.13           C  
ANISOU 1594  CZ3 TRP A 224     7621   5000   4524    317    314    -96       C  
ATOM   1595  CH2 TRP A 224     -27.562  49.008  23.810  1.00 38.29           C  
ANISOU 1595  CH2 TRP A 224     6768   4161   3616    388    187   -137       C  
ATOM   1596  N   ALA A 225     -34.674  52.088  20.698  1.00 43.82           N  
ANISOU 1596  N   ALA A 225     6911   4912   4824    201    876    120       N  
ATOM   1597  CA  ALA A 225     -36.086  52.361  20.375  1.00 75.04           C  
ANISOU 1597  CA  ALA A 225    10762   8898   8848    192    995    176       C  
ATOM   1598  C   ALA A 225     -36.486  51.589  19.124  1.00 80.57           C  
ANISOU 1598  C   ALA A 225    11328   9645   9637    156    941    200       C  
ATOM   1599  O   ALA A 225     -37.662  51.192  18.987  1.00 54.34           O  
ANISOU 1599  O   ALA A 225     7937   6349   6361    113   1008    264       O  
ATOM   1600  CB  ALA A 225     -36.327  53.840  20.185  1.00 99.67           C  
ANISOU 1600  CB  ALA A 225    13847  12035  11988    243   1057    167       C  
ATOM   1601  N   SER A 226     -35.512  51.400  18.245  1.00 63.78           N  
ANISOU 1601  N   SER A 226     9165   7543   7523    173    818    152       N  
ATOM   1602  CA  SER A 226     -35.693  50.750  16.942  1.00 53.24           C  
ANISOU 1602  CA  SER A 226     7720   6248   6257    160    746    158       C  
ATOM   1603  C   SER A 226     -35.167  49.334  17.010  1.00 31.19           C  
ANISOU 1603  C   SER A 226     5022   3413   3413    160    628    137       C  
ATOM   1604  O   SER A 226     -33.955  49.121  17.222  1.00 15.92           O  
ANISOU 1604  O   SER A 226     3156   1483   1407    215    538     77       O  
ATOM   1605  CB  SER A 226     -35.016  51.511  15.825  1.00 94.95           C  
ANISOU 1605  CB  SER A 226    12896  11606  11574    193    691    120       C  
ATOM   1606  OG  SER A 226     -33.654  51.790  16.125  1.00 82.01           O  
ANISOU 1606  OG  SER A 226    11309   9994   9857    225    619     67       O  
ATOM   1607  N   GLU A 227     -36.023  48.394  16.661  1.00 36.17           N  
ANISOU 1607  N   GLU A 227     5650   4013   4077    105    608    185       N  
ATOM   1608  CA  GLU A 227     -35.657  46.957  16.605  1.00 61.64           C  
ANISOU 1608  CA  GLU A 227     9002   7171   7247    105    469    169       C  
ATOM   1609  C   GLU A 227     -34.565  46.710  15.562  1.00 48.75           C  
ANISOU 1609  C   GLU A 227     7340   5585   5597    209    337     89       C  
ATOM   1610  O   GLU A 227     -33.674  45.839  15.791  1.00 55.30           O  
ANISOU 1610  O   GLU A 227     8295   6377   6338    280    214     34       O  
ATOM   1611  CB  GLU A 227     -36.893  46.097  16.323  1.00 74.84           C  
ANISOU 1611  CB  GLU A 227    10679   8797   8957     -2    458    254       C  
ATOM   1612  CG  GLU A 227     -37.873  46.032  17.488  1.00 90.25           C  
ANISOU 1612  CG  GLU A 227    12674  10727  10888   -110    571    343       C  
ATOM   1613  CD  GLU A 227     -38.662  47.301  17.787  1.00 85.49           C  
ANISOU 1613  CD  GLU A 227    11928  10215  10337   -115    755    383       C  
ATOM   1614  OE1 GLU A 227     -38.536  48.284  17.027  1.00 42.84           O  
ANISOU 1614  OE1 GLU A 227     6399   4875   5001    -49    788    349       O  
ATOM   1615  OE2 GLU A 227     -39.405  47.304  18.786  1.00127.76           O  
ANISOU 1615  OE2 GLU A 227    17307  15580  15654   -177    861    450       O  
ATOM   1616  N   GLY A1001     -34.627  47.462  14.468  1.00 36.89           N  
ANISOU 1616  N   GLY A1001     5677   4172   4165    227    360     82       N  
ATOM   1617  CA  GLY A1001     -33.664  47.333  13.377  1.00 37.18           C  
ANISOU 1617  CA  GLY A1001     5654   4292   4179    323    254     15       C  
ATOM   1618  C   GLY A1001     -34.247  46.473  12.285  1.00 22.76           C  
ANISOU 1618  C   GLY A1001     3822   2438   2388    320    173     28       C  
ATOM   1619  O   GLY A1001     -35.437  46.079  12.399  1.00 13.20           O  
ANISOU 1619  O   GLY A1001     2639   1147   1230    218    202    101       O  
ATOM   1620  N   ILE A1002     -33.459  46.195  11.255  1.00 14.74           N  
ANISOU 1620  N   ILE A1002     2767   1496   1334    425     73    -34       N  
ATOM   1621  CA  ILE A1002     -33.967  45.415  10.091  1.00 18.56           C  
ANISOU 1621  CA  ILE A1002     3261   1948   1841    437    -18    -30       C  
ATOM   1622  C   ILE A1002     -33.133  44.163   9.857  1.00 14.77           C  
ANISOU 1622  C   ILE A1002     2932   1436   1242    577   -186   -107       C  
ATOM   1623  O   ILE A1002     -31.917  44.175  10.179  1.00 36.87           O  
ANISOU 1623  O   ILE A1002     5741   4319   3948    701   -222   -179       O  
ATOM   1624  CB  ILE A1002     -34.002  46.241   8.791  1.00 17.94           C  
ANISOU 1624  CB  ILE A1002     3001   1989   1825    448     11    -33       C  
ATOM   1625  CG1 ILE A1002     -32.602  46.744   8.404  1.00  9.80           C  
ANISOU 1625  CG1 ILE A1002     1881   1124    716    566    -12   -107       C  
ATOM   1626  CG2 ILE A1002     -35.042  47.361   8.889  1.00 12.06           C  
ANISOU 1626  CG2 ILE A1002     2134   1247   1199    323    152     44       C  
ATOM   1627  CD1 ILE A1002     -32.459  47.018   6.926  1.00  9.46           C  
ANISOU 1627  CD1 ILE A1002     1710   1196    685    608    -42   -124       C  
ATOM   1628  N   ASP A1003     -33.812  43.158   9.314  1.00 11.25           N  
ANISOU 1628  N   ASP A1003     2602    876    797    556   -291    -87       N  
ATOM   1629  CA  ASP A1003     -33.206  41.871   8.948  1.00 14.16           C  
ANISOU 1629  CA  ASP A1003     3158   1177   1044    702   -478   -161       C  
ATOM   1630  C   ASP A1003     -32.419  42.099   7.667  1.00 12.69           C  
ANISOU 1630  C   ASP A1003     2853   1147    818    864   -519   -239       C  
ATOM   1631  O   ASP A1003     -33.011  42.355   6.613  1.00 14.76           O  
ANISOU 1631  O   ASP A1003     3026   1434   1148    820   -507   -211       O  
ATOM   1632  CB  ASP A1003     -34.250  40.761   8.832  1.00 19.76           C  
ANISOU 1632  CB  ASP A1003     4060   1691   1756    597   -594   -101       C  
ATOM   1633  CG  ASP A1003     -33.602  39.392   8.694  1.00 35.94           C  
ANISOU 1633  CG  ASP A1003     6371   3627   3656    756   -810   -181       C  
ATOM   1634  OD1 ASP A1003     -32.375  39.283   8.960  1.00 33.32           O  
ANISOU 1634  OD1 ASP A1003     6067   3372   3219    949   -851   -281       O  
ATOM   1635  OD2 ASP A1003     -34.317  38.445   8.310  1.00 37.85           O  
ANISOU 1635  OD2 ASP A1003     6793   3708   3879    691   -948   -143       O  
ATOM   1636  N   CYS A1004     -31.112  42.169   7.834  1.00 12.62           N  
ANISOU 1636  N   CYS A1004     2815   1273    705   1031   -543   -324       N  
ATOM   1637  CA  CYS A1004     -30.169  42.389   6.712  1.00 19.47           C  
ANISOU 1637  CA  CYS A1004     3549   2346   1502   1203   -574   -399       C  
ATOM   1638  C   CYS A1004     -29.976  41.126   5.882  1.00 20.50           C  
ANISOU 1638  C   CYS A1004     3851   2418   1519   1386   -753   -474       C  
ATOM   1639  O   CYS A1004     -29.455  41.233   4.754  1.00 16.32           O  
ANISOU 1639  O   CYS A1004     3217   2049    932   1523   -778   -527       O  
ATOM   1640  CB  CYS A1004     -28.850  42.949   7.222  1.00 30.08           C  
ANISOU 1640  CB  CYS A1004     4773   3889   2765   1302   -536   -448       C  
ATOM   1641  SG  CYS A1004     -29.048  44.644   7.823  1.00 53.64           S  
ANISOU 1641  SG  CYS A1004     7551   6956   5871   1091   -343   -361       S  
ATOM   1642  N   SER A1005     -30.472  39.997   6.381  1.00 21.93           N  
ANISOU 1642  N   SER A1005     4299   2368   1665   1374   -877   -470       N  
ATOM   1643  CA  SER A1005     -30.467  38.748   5.603  1.00 23.09           C  
ANISOU 1643  CA  SER A1005     4671   2402   1701   1530  -1075   -533       C  
ATOM   1644  C   SER A1005     -31.676  38.755   4.684  1.00 20.40           C  
ANISOU 1644  C   SER A1005     4329   1959   1461   1376  -1083   -459       C  
ATOM   1645  O   SER A1005     -31.521  38.432   3.483  1.00 21.01           O  
ANISOU 1645  O   SER A1005     4427   2076   1478   1512  -1171   -513       O  
ATOM   1646  CB  SER A1005     -30.475  37.516   6.474  1.00 30.04           C  
ANISOU 1646  CB  SER A1005     5871   3058   2484   1570  -1238   -553       C  
ATOM   1647  OG  SER A1005     -31.732  37.355   7.119  1.00 28.14           O  
ANISOU 1647  OG  SER A1005     5734   2610   2346   1297  -1220   -433       O  
ATOM   1648  N   PHE A1006     -32.834  39.078   5.264  1.00 14.89           N  
ANISOU 1648  N   PHE A1006     3610   1144    901   1112   -998   -338       N  
ATOM   1649  CA  PHE A1006     -34.103  39.069   4.517  1.00 14.81           C  
ANISOU 1649  CA  PHE A1006     3591   1039    996    938  -1008   -248       C  
ATOM   1650  C   PHE A1006     -34.071  40.107   3.396  1.00 13.81           C  
ANISOU 1650  C   PHE A1006     3206   1097    943    955   -901   -253       C  
ATOM   1651  O   PHE A1006     -34.244  39.676   2.253  1.00 14.33           O  
ANISOU 1651  O   PHE A1006     3330   1136    977   1018  -1006   -276       O  
ATOM   1652  CB  PHE A1006     -35.325  39.331   5.384  1.00 14.51           C  
ANISOU 1652  CB  PHE A1006     3527    900   1083    662   -914   -111       C  
ATOM   1653  CG  PHE A1006     -36.597  39.287   4.576  1.00 14.65           C  
ANISOU 1653  CG  PHE A1006     3516    849   1200    491   -936    -14       C  
ATOM   1654  CD1 PHE A1006     -37.197  38.087   4.240  1.00 16.04           C  
ANISOU 1654  CD1 PHE A1006     3939    831   1322    429  -1133     21       C  
ATOM   1655  CD2 PHE A1006     -37.173  40.454   4.120  1.00 13.55           C  
ANISOU 1655  CD2 PHE A1006     3112    835   1198    394   -777     41       C  
ATOM   1656  CE1 PHE A1006     -38.375  38.066   3.509  1.00 16.28           C  
ANISOU 1656  CE1 PHE A1006     3931    810   1444    254  -1162    122       C  
ATOM   1657  CE2 PHE A1006     -38.346  40.431   3.385  1.00 13.77           C  
ANISOU 1657  CE2 PHE A1006     3100    813   1318    241   -802    134       C  
ATOM   1658  CZ  PHE A1006     -38.953  39.237   3.091  1.00 15.13           C  
ANISOU 1658  CZ  PHE A1006     3498    807   1443    163   -991    178       C  
ATOM   1659  N   TRP A1007     -33.844  41.386   3.719  1.00 12.59           N  
ANISOU 1659  N   TRP A1007     2808   1106    868    901   -717   -231       N  
ATOM   1660  CA  TRP A1007     -33.793  42.475   2.714  1.00 11.70           C  
ANISOU 1660  CA  TRP A1007     2458   1165    821    895   -618   -226       C  
ATOM   1661  C   TRP A1007     -32.413  42.462   2.078  1.00 12.03           C  
ANISOU 1661  C   TRP A1007     2446   1398    724   1125   -660   -336       C  
ATOM   1662  O   TRP A1007     -31.490  43.005   2.673  1.00 11.75           O  
ANISOU 1662  O   TRP A1007     2309   1508    646   1180   -589   -367       O  
ATOM   1663  CB  TRP A1007     -34.140  43.823   3.332  1.00 10.54           C  
ANISOU 1663  CB  TRP A1007     2115   1092    798    741   -432   -155       C  
ATOM   1664  CG  TRP A1007     -35.372  43.782   4.177  1.00 10.52           C  
ANISOU 1664  CG  TRP A1007     2157    939    898    552   -380    -55       C  
ATOM   1665  CD1 TRP A1007     -35.392  43.668   5.527  1.00 10.64           C  
ANISOU 1665  CD1 TRP A1007     2246    891    904    499   -335    -32       C  
ATOM   1666  CD2 TRP A1007     -36.750  43.866   3.769  1.00 10.53           C  
ANISOU 1666  CD2 TRP A1007     2120    863   1017    392   -361     41       C  
ATOM   1667  NE1 TRP A1007     -36.675  43.672   5.986  1.00 10.79           N  
ANISOU 1667  NE1 TRP A1007     2268    814   1017    321   -282     72       N  
ATOM   1668  CE2 TRP A1007     -37.528  43.791   4.932  1.00 10.77           C  
ANISOU 1668  CE2 TRP A1007     2187    807   1094    252   -298    121       C  
ATOM   1669  CE3 TRP A1007     -37.412  43.985   2.549  1.00 10.49           C  
ANISOU 1669  CE3 TRP A1007     2048    862   1076    351   -394     72       C  
ATOM   1670  CZ2 TRP A1007     -38.913  43.850   4.921  1.00 11.05           C  
ANISOU 1670  CZ2 TRP A1007     2172    792   1234     79   -260    234       C  
ATOM   1671  CZ3 TRP A1007     -38.788  44.033   2.531  1.00 10.70           C  
ANISOU 1671  CZ3 TRP A1007     2035    817   1214    177   -368    182       C  
ATOM   1672  CH2 TRP A1007     -39.526  43.966   3.704  1.00 11.03           C  
ANISOU 1672  CH2 TRP A1007     2092    801   1296     45   -299    264       C  
ATOM   1673  N   ASN A1008     -32.309  41.780   0.950  1.00 12.81           N  
ANISOU 1673  N   ASN A1008     2627   1495    744   1257   -781   -390       N  
ATOM   1674  CA  ASN A1008     -31.082  41.659   0.134  1.00 13.47           C  
ANISOU 1674  CA  ASN A1008     2655   1788    673   1503   -829   -495       C  
ATOM   1675  C   ASN A1008     -31.518  41.363  -1.290  1.00 13.89           C  
ANISOU 1675  C   ASN A1008     2744   1823    711   1548   -908   -507       C  
ATOM   1676  O   ASN A1008     -32.517  40.641  -1.500  1.00 14.30           O  
ANISOU 1676  O   ASN A1008     2982   1646    805   1467  -1012   -470       O  
ATOM   1677  CB  ASN A1008     -30.121  40.624   0.721  1.00 14.72           C  
ANISOU 1677  CB  ASN A1008     2991   1937    663   1729   -950   -594       C  
ATOM   1678  CG  ASN A1008     -28.780  40.550   0.010  1.00 15.62           C  
ANISOU 1678  CG  ASN A1008     3011   2321    601   2007   -981   -702       C  
ATOM   1679  OD1 ASN A1008     -28.487  39.545  -0.637  1.00 17.00           O  
ANISOU 1679  OD1 ASN A1008     3358   2466    633   2231  -1130   -789       O  
ATOM   1680  ND2 ASN A1008     -27.957  41.587   0.117  1.00 15.07           N  
ANISOU 1680  ND2 ASN A1008     2677   2524    526   1998   -851   -693       N  
ATOM   1681  N   GLU A1009     -30.830  41.961  -2.245  1.00 13.86           N  
ANISOU 1681  N   GLU A1009     2559   2059    646   1649   -859   -544       N  
ATOM   1682  CA  GLU A1009     -31.264  41.841  -3.660  1.00 14.18           C  
ANISOU 1682  CA  GLU A1009     2611   2097    676   1677   -917   -550       C  
ATOM   1683  C   GLU A1009     -31.081  40.408  -4.138  1.00 15.83           C  
ANISOU 1683  C   GLU A1009     3099   2188    725   1904  -1117   -643       C  
ATOM   1684  O   GLU A1009     -31.623  40.077  -5.191  1.00 16.28           O  
ANISOU 1684  O   GLU A1009     3244   2166    773   1917  -1201   -644       O  
ATOM   1685  CB  GLU A1009     -30.539  42.850  -4.547  1.00 16.67           C  
ANISOU 1685  CB  GLU A1009     2667   2715    950   1719   -815   -560       C  
ATOM   1686  CG  GLU A1009     -31.298  43.207  -5.815  1.00 23.21           C  
ANISOU 1686  CG  GLU A1009     3451   3523   1843   1632   -818   -518       C  
ATOM   1687  CD  GLU A1009     -30.607  44.240  -6.703  1.00 38.10           C  
ANISOU 1687  CD  GLU A1009     5087   5707   3680   1646   -720   -515       C  
ATOM   1688  OE1 GLU A1009     -29.360  44.329  -6.661  1.00 71.10           O  
ANISOU 1688  OE1 GLU A1009     9157  10147   7710   1803   -693   -573       O  
ATOM   1689  OE2 GLU A1009     -31.310  44.964  -7.439  1.00 47.04           O  
ANISOU 1689  OE2 GLU A1009     6132   6823   4917   1492   -676   -449       O  
ATOM   1690  N   SER A1010     -30.422  39.577  -3.339  1.00 16.76           N  
ANISOU 1690  N   SER A1010     3378   2264    726   2068  -1202   -715       N  
ATOM   1691  CA  SER A1010     -30.000  38.235  -3.753  1.00 18.64           C  
ANISOU 1691  CA  SER A1010     3897   2414    768   2346  -1406   -827       C  
ATOM   1692  C   SER A1010     -31.181  37.308  -4.002  1.00 19.26           C  
ANISOU 1692  C   SER A1010     4280   2150    885   2240  -1576   -787       C  
ATOM   1693  O   SER A1010     -31.022  36.354  -4.823  1.00 23.42           O  
ANISOU 1693  O   SER A1010     5042   2599   1256   2454  -1757   -873       O  
ATOM   1694  CB  SER A1010     -29.078  37.644  -2.742  1.00 21.29           C  
ANISOU 1694  CB  SER A1010     4335   2771    980   2529  -1461   -904       C  
ATOM   1695  OG  SER A1010     -27.915  38.437  -2.645  1.00 25.57           O  
ANISOU 1695  OG  SER A1010     4593   3658   1463   2641  -1326   -940       O  
ATOM   1696  N   TYR A1011     -32.281  37.558  -3.300  1.00 18.27           N  
ANISOU 1696  N   TYR A1011     4157   1844    942   1933  -1529   -663       N  
ATOM   1697  CA  TYR A1011     -33.450  36.661  -3.288  1.00 19.02           C  
ANISOU 1697  CA  TYR A1011     4530   1618   1076   1775  -1694   -594       C  
ATOM   1698  C   TYR A1011     -34.371  36.920  -4.470  1.00 18.79           C  
ANISOU 1698  C   TYR A1011     4459   1548   1133   1646  -1711   -532       C  
ATOM   1699  O   TYR A1011     -35.354  36.191  -4.645  1.00 21.10           O  
ANISOU 1699  O   TYR A1011     4971   1593   1450   1505  -1864   -466       O  
ATOM   1700  CB  TYR A1011     -34.210  36.779  -1.966  1.00 18.35           C  
ANISOU 1700  CB  TYR A1011     4448   1395   1128   1504  -1632   -479       C  
ATOM   1701  CG  TYR A1011     -33.410  36.370  -0.758  1.00 18.76           C  
ANISOU 1701  CG  TYR A1011     4599   1437   1090   1614  -1648   -535       C  
ATOM   1702  CD1 TYR A1011     -32.519  37.248  -0.194  1.00 17.77           C  
ANISOU 1702  CD1 TYR A1011     4230   1544    975   1683  -1475   -569       C  
ATOM   1703  CD2 TYR A1011     -33.515  35.109  -0.202  1.00 20.27           C  
ANISOU 1703  CD2 TYR A1011     5143   1382   1176   1646  -1851   -551       C  
ATOM   1704  CE1 TYR A1011     -31.756  36.896   0.897  1.00 18.18           C  
ANISOU 1704  CE1 TYR A1011     4368   1596    944   1787  -1495   -620       C  
ATOM   1705  CE2 TYR A1011     -32.768  34.741   0.898  1.00 20.70           C  
ANISOU 1705  CE2 TYR A1011     5296   1424   1143   1752  -1874   -603       C  
ATOM   1706  CZ  TYR A1011     -31.890  35.648   1.458  1.00 19.60           C  
ANISOU 1706  CZ  TYR A1011     4891   1530   1026   1825  -1689   -639       C  
ATOM   1707  OH  TYR A1011     -31.122  35.378   2.557  1.00 19.97           O  
ANISOU 1707  OH  TYR A1011     5010   1582    993   1926  -1702   -687       O  
ATOM   1708  N   LEU A1012     -33.978  37.862  -5.321  1.00 17.98           N  
ANISOU 1708  N   LEU A1012     4098   1684   1049   1706  -1581   -555       N  
ATOM   1709  CA  LEU A1012     -34.770  38.225  -6.515  1.00 18.95           C  
ANISOU 1709  CA  LEU A1012     4156   1791   1249   1598  -1588   -501       C  
ATOM   1710  C   LEU A1012     -34.053  37.709  -7.754  1.00 19.90           C  
ANISOU 1710  C   LEU A1012     4389   1991   1178   1883  -1704   -621       C  
ATOM   1711  O   LEU A1012     -32.808  37.594  -7.736  1.00 21.10           O  
ANISOU 1711  O   LEU A1012     4513   2336   1168   2155  -1688   -737       O  
ATOM   1712  CB  LEU A1012     -34.952  39.751  -6.562  1.00 17.02           C  
ANISOU 1712  CB  LEU A1012     3550   1745   1169   1431  -1358   -427       C  
ATOM   1713  CG  LEU A1012     -35.446  40.418  -5.274  1.00 14.74           C  
ANISOU 1713  CG  LEU A1012     3125   1431   1041   1208  -1214   -330       C  
ATOM   1714  CD1 LEU A1012     -35.729  41.894  -5.511  1.00 13.27           C  
ANISOU 1714  CD1 LEU A1012     2634   1405   1001   1061  -1025   -262       C  
ATOM   1715  CD2 LEU A1012     -36.677  39.709  -4.710  1.00 15.35           C  
ANISOU 1715  CD2 LEU A1012     3382   1243   1204   1002  -1311   -231       C  
ATOM   1716  N   THR A1013     -34.811  37.439  -8.807  1.00 19.85           N  
ANISOU 1716  N   THR A1013     4494   1861   1184   1828  -1814   -593       N  
ATOM   1717  CA  THR A1013     -34.254  36.860 -10.057  1.00 23.27           C  
ANISOU 1717  CA  THR A1013     5079   2340   1422   2105  -1945   -707       C  
ATOM   1718  C   THR A1013     -34.337  37.825 -11.236  1.00 21.08           C  
ANISOU 1718  C   THR A1013     4564   2253   1192   2070  -1833   -686       C  
ATOM   1719  O   THR A1013     -35.202  38.703 -11.241  1.00 18.81           O  
ANISOU 1719  O   THR A1013     4086   1954   1105   1794  -1724   -567       O  
ATOM   1720  CB  THR A1013     -34.953  35.551 -10.458  1.00 28.16           C  
ANISOU 1720  CB  THR A1013     6109   2630   1960   2116  -2221   -712       C  
ATOM   1721  OG1 THR A1013     -36.368  35.733 -10.413  1.00 31.54           O  
ANISOU 1721  OG1 THR A1013     6531   2865   2587   1762  -2240   -557       O  
ATOM   1722  CG2 THR A1013     -34.576  34.381  -9.580  1.00 31.66           C  
ANISOU 1722  CG2 THR A1013     6869   2891   2267   2254  -2389   -775       C  
ATOM   1723  N   GLY A1014     -33.428  37.650 -12.188  1.00 23.10           N  
ANISOU 1723  N   GLY A1014     4834   2690   1250   2358  -1863   -802       N  
ATOM   1724  CA  GLY A1014     -33.353  38.523 -13.362  1.00 24.88           C  
ANISOU 1724  CA  GLY A1014     4847   3124   1481   2350  -1762   -790       C  
ATOM   1725  C   GLY A1014     -32.719  39.854 -13.054  1.00 23.76           C  
ANISOU 1725  C   GLY A1014     4322   3297   1409   2276  -1523   -756       C  
ATOM   1726  O   GLY A1014     -32.297  40.087 -11.907  1.00 26.89           O  
ANISOU 1726  O   GLY A1014     4617   3753   1844   2246  -1434   -748       O  
ATOM   1727  N   SER A1015     -32.591  40.673 -14.095  1.00 23.66           N  
ANISOU 1727  N   SER A1015     4119   3482   1386   2257  -1436   -740       N  
ATOM   1728  CA  SER A1015     -32.111  42.065 -13.988  1.00 21.92           C  
ANISOU 1728  CA  SER A1015     3546   3546   1234   2134  -1227   -684       C  
ATOM   1729  C   SER A1015     -33.179  42.912 -13.303  1.00 18.41           C  
ANISOU 1729  C   SER A1015     2991   2944   1056   1795  -1140   -551       C  
ATOM   1730  O   SER A1015     -34.375  42.560 -13.303  1.00 17.33           O  
ANISOU 1730  O   SER A1015     2999   2532   1050   1643  -1228   -490       O  
ATOM   1731  CB  SER A1015     -31.754  42.646 -15.336  1.00 25.30           C  
ANISOU 1731  CB  SER A1015     3838   4208   1567   2189  -1183   -694       C  
ATOM   1732  OG  SER A1015     -32.901  43.208 -15.977  1.00 21.31           O  
ANISOU 1732  OG  SER A1015     3316   3549   1229   1951  -1186   -599       O  
ATOM   1733  N   ARG A1016     -32.742  44.027 -12.738  1.00 15.01           N  
ANISOU 1733  N   ARG A1016     2308   2702    692   1682   -976   -503       N  
ATOM   1734  CA  ARG A1016     -33.685  44.978 -12.104  1.00 13.44           C  
ANISOU 1734  CA  ARG A1016     1993   2385    727   1391   -880   -385       C  
ATOM   1735  C   ARG A1016     -34.582  45.561 -13.180  1.00 13.05           C  
ANISOU 1735  C   ARG A1016     1900   2281    778   1246   -888   -318       C  
ATOM   1736  O   ARG A1016     -35.768  45.792 -12.900  1.00 12.32           O  
ANISOU 1736  O   ARG A1016     1821   1988    869   1051   -891   -232       O  
ATOM   1737  CB  ARG A1016     -32.959  46.081 -11.323  1.00 12.60           C  
ANISOU 1737  CB  ARG A1016     1657   2483    646   1313   -723   -354       C  
ATOM   1738  CG  ARG A1016     -33.859  46.880 -10.388  1.00 11.26           C  
ANISOU 1738  CG  ARG A1016     1420   2166    689   1069   -637   -255       C  
ATOM   1739  CD  ARG A1016     -33.257  48.215 -10.009  1.00 10.54           C  
ANISOU 1739  CD  ARG A1016     1115   2269    619    965   -501   -212       C  
ATOM   1740  NE  ARG A1016     -33.978  48.808  -8.903  1.00  9.53           N  
ANISOU 1740  NE  ARG A1016      964   1997    659    793   -429   -141       N  
ATOM   1741  CZ  ARG A1016     -33.843  48.456  -7.626  1.00  9.39           C  
ANISOU 1741  CZ  ARG A1016     1001   1908    656    805   -407   -152       C  
ATOM   1742  NH1 ARG A1016     -33.003  47.505  -7.269  1.00 10.15           N  
ANISOU 1742  NH1 ARG A1016     1184   2055    616    979   -461   -232       N  
ATOM   1743  NH2 ARG A1016     -34.547  49.071  -6.698  1.00  8.59           N  
ANISOU 1743  NH2 ARG A1016      874   1690    697    655   -333    -86       N  
ATOM   1744  N   ASP A1017     -34.030  45.792 -14.364  1.00 14.03           N  
ANISOU 1744  N   ASP A1017     1964   2590    775   1343   -891   -353       N  
ATOM   1745  CA  ASP A1017     -34.776  46.406 -15.474  1.00 19.33           C  
ANISOU 1745  CA  ASP A1017     2592   3230   1523   1214   -902   -293       C  
ATOM   1746  C   ASP A1017     -35.896  45.479 -15.935  1.00 19.46           C  
ANISOU 1746  C   ASP A1017     2833   2963   1597   1195  -1058   -283       C  
ATOM   1747  O   ASP A1017     -37.005  45.947 -16.259  1.00 19.03           O  
ANISOU 1747  O   ASP A1017     2752   2771   1705   1005  -1070   -195       O  
ATOM   1748  CB  ASP A1017     -33.862  46.720 -16.661  1.00 38.51           C  
ANISOU 1748  CB  ASP A1017     4928   5933   3769   1339   -881   -337       C  
ATOM   1749  CG  ASP A1017     -32.493  47.272 -16.287  1.00 66.34           C  
ANISOU 1749  CG  ASP A1017     8259   9786   7160   1413   -763   -363       C  
ATOM   1750  OD1 ASP A1017     -32.385  47.923 -15.228  1.00 85.35           O  
ANISOU 1750  OD1 ASP A1017    10554  12208   9667   1284   -672   -315       O  
ATOM   1751  OD2 ASP A1017     -31.536  47.025 -17.054  1.00 94.25           O  
ANISOU 1751  OD2 ASP A1017    11756  13570  10481   1603   -769   -429       O  
ATOM   1752  N   GLU A1018     -35.595  44.184 -15.983  1.00 19.27           N  
ANISOU 1752  N   GLU A1018     3033   2856   1429   1394  -1191   -370       N  
ATOM   1753  CA  GLU A1018     -36.602  43.166 -16.347  1.00 19.90           C  
ANISOU 1753  CA  GLU A1018     3374   2646   1539   1369  -1375   -357       C  
ATOM   1754  C   GLU A1018     -37.683  43.105 -15.268  1.00 15.89           C  
ANISOU 1754  C   GLU A1018     2887   1916   1234   1143  -1379   -258       C  
ATOM   1755  O   GLU A1018     -38.871  43.009 -15.589  1.00 17.30           O  
ANISOU 1755  O   GLU A1018     3125   1910   1539    972  -1459   -173       O  
ATOM   1756  CB  GLU A1018     -35.925  41.813 -16.543  1.00 24.75           C  
ANISOU 1756  CB  GLU A1018     4255   3218   1928   1651  -1528   -480       C  
ATOM   1757  CG  GLU A1018     -35.016  41.779 -17.758  1.00 37.34           C  
ANISOU 1757  CG  GLU A1018     5846   5034   3307   1892  -1539   -576       C  
ATOM   1758  CD  GLU A1018     -33.787  40.881 -17.655  1.00 53.37           C  
ANISOU 1758  CD  GLU A1018     8001   7195   5080   2239  -1593   -718       C  
ATOM   1759  OE1 GLU A1018     -33.809  39.893 -16.883  1.00 40.52           O  
ANISOU 1759  OE1 GLU A1018     6595   5383   3417   2324  -1707   -760       O  
ATOM   1760  OE2 GLU A1018     -32.799  41.168 -18.362  1.00 87.50           O  
ANISOU 1760  OE2 GLU A1018    12200  11818   9226   2430  -1524   -786       O  
ATOM   1761  N   ARG A1019     -37.266  43.154 -14.013  1.00 14.62           N  
ANISOU 1761  N   ARG A1019     2670   1790   1092   1144  -1294   -264       N  
ATOM   1762  CA  ARG A1019     -38.207  43.090 -12.886  1.00 14.05           C  
ANISOU 1762  CA  ARG A1019     2608   1539   1188    943  -1281   -171       C  
ATOM   1763  C   ARG A1019     -39.150  44.282 -12.929  1.00 12.87           C  
ANISOU 1763  C   ARG A1019     2244   1402   1244    711  -1168    -57       C  
ATOM   1764  O   ARG A1019     -40.332  44.138 -12.618  1.00 12.86           O  
ANISOU 1764  O   ARG A1019     2266   1236   1381    533  -1207     38       O  
ATOM   1765  CB  ARG A1019     -37.443  43.030 -11.564  1.00 13.74           C  
ANISOU 1765  CB  ARG A1019     2539   1565   1114   1005  -1197   -208       C  
ATOM   1766  CG  ARG A1019     -36.830  41.676 -11.254  1.00 15.07           C  
ANISOU 1766  CG  ARG A1019     2968   1644   1110   1205  -1341   -302       C  
ATOM   1767  CD  ARG A1019     -36.495  41.598  -9.776  1.00 14.68           C  
ANISOU 1767  CD  ARG A1019     2907   1588   1082   1188  -1272   -301       C  
ATOM   1768  NE  ARG A1019     -35.494  42.570  -9.376  1.00 13.83           N  
ANISOU 1768  NE  ARG A1019     2564   1734    953   1246  -1101   -332       N  
ATOM   1769  CZ  ARG A1019     -34.189  42.367  -9.456  1.00 14.46           C  
ANISOU 1769  CZ  ARG A1019     2633   2003    855   1481  -1097   -438       C  
ATOM   1770  NH1 ARG A1019     -33.715  41.222  -9.916  1.00 15.96           N  
ANISOU 1770  NH1 ARG A1019     3045   2152    866   1714  -1251   -537       N  
ATOM   1771  NH2 ARG A1019     -33.353  43.306  -9.063  1.00 13.76           N  
ANISOU 1771  NH2 ARG A1019     2319   2151    758   1487   -948   -442       N  
ATOM   1772  N   LYS A1020     -38.640  45.441 -13.315  1.00 12.10           N  
ANISOU 1772  N   LYS A1020     1941   1502   1152    715  -1039    -62       N  
ATOM   1773  CA  LYS A1020     -39.480  46.649 -13.403  1.00 11.13           C  
ANISOU 1773  CA  LYS A1020     1634   1387   1206    522   -944     35       C  
ATOM   1774  C   LYS A1020     -40.437  46.518 -14.569  1.00 11.57           C  
ANISOU 1774  C   LYS A1020     1744   1335   1317    448  -1054     83       C  
ATOM   1775  O   LYS A1020     -41.612  46.873 -14.434  1.00 11.29           O  
ANISOU 1775  O   LYS A1020     1646   1197   1446    278  -1050    180       O  
ATOM   1776  CB  LYS A1020     -38.628  47.913 -13.563  1.00 10.41           C  
ANISOU 1776  CB  LYS A1020     1349   1522   1085    535   -806     20       C  
ATOM   1777  CG  LYS A1020     -39.389  49.241 -13.559  1.00  9.54           C  
ANISOU 1777  CG  LYS A1020     1075   1410   1138    359   -716    111       C  
ATOM   1778  CD  LYS A1020     -38.483  50.471 -13.569  1.00  9.02           C  
ANISOU 1778  CD  LYS A1020      855   1545   1024    349   -602    104       C  
ATOM   1779  CE  LYS A1020     -37.715  50.623 -14.868  1.00  9.55           C  
ANISOU 1779  CE  LYS A1020      902   1778    947    424   -634     64       C  
ATOM   1780  NZ  LYS A1020     -36.900  51.864 -14.900  1.00  9.24           N  
ANISOU 1780  NZ  LYS A1020      713   1938    859    367   -538     83       N  
ATOM   1781  N   LYS A1021     -39.938  46.023 -15.697  1.00 12.39           N  
ANISOU 1781  N   LYS A1021     1957   1474   1274    583  -1152     15       N  
ATOM   1782  CA  LYS A1021     -40.779  45.772 -16.887  1.00 13.00           C  
ANISOU 1782  CA  LYS A1021     2124   1435   1378    528  -1282     51       C  
ATOM   1783  C   LYS A1021     -41.918  44.834 -16.504  1.00 13.63           C  
ANISOU 1783  C   LYS A1021     2358   1273   1547    410  -1417    119       C  
ATOM   1784  O   LYS A1021     -43.064  45.042 -16.906  1.00 13.69           O  
ANISOU 1784  O   LYS A1021     2333   1180   1688    246  -1469    215       O  
ATOM   1785  CB  LYS A1021     -39.889  45.173 -17.978  1.00 14.54           C  
ANISOU 1785  CB  LYS A1021     2457   1709   1358    740  -1372    -54       C  
ATOM   1786  CG  LYS A1021     -40.581  44.785 -19.281  1.00 18.77           C  
ANISOU 1786  CG  LYS A1021     3132   2122   1877    721  -1527    -37       C  
ATOM   1787  CD  LYS A1021     -39.660  43.950 -20.177  1.00 25.18           C  
ANISOU 1787  CD  LYS A1021     4132   2993   2441    977  -1629   -159       C  
ATOM   1788  CE  LYS A1021     -40.196  43.716 -21.568  1.00 26.68           C  
ANISOU 1788  CE  LYS A1021     4454   3092   2590    975  -1769   -152       C  
ATOM   1789  NZ  LYS A1021     -40.204  44.976 -22.347  1.00 33.75           N  
ANISOU 1789  NZ  LYS A1021     5136   4150   3537    889  -1660   -110       N  
ATOM   1790  N   SER A1022     -41.583  43.820 -15.729  1.00 14.24           N  
ANISOU 1790  N   SER A1022     2599   1267   1543    486  -1480     77       N  
ATOM   1791  CA  SER A1022     -42.551  42.805 -15.288  1.00 15.13           C  
ANISOU 1791  CA  SER A1022     2889   1151   1706    360  -1629    148       C  
ATOM   1792  C   SER A1022     -43.568  43.416 -14.332  1.00 14.40           C  
ANISOU 1792  C   SER A1022     2611   1041   1817    133  -1524    276       C  
ATOM   1793  O   SER A1022     -44.776  43.231 -14.508  1.00 15.60           O  
ANISOU 1793  O   SER A1022     2769   1077   2079    -48  -1609    387       O  
ATOM   1794  CB  SER A1022     -41.844  41.643 -14.634  1.00 16.02           C  
ANISOU 1794  CB  SER A1022     3234   1184   1666    504  -1721     68       C  
ATOM   1795  OG  SER A1022     -42.760  40.648 -14.213  1.00 17.06           O  
ANISOU 1795  OG  SER A1022     3562   1089   1832    357  -1883    148       O  
ATOM   1796  N   LEU A1023     -43.078  44.139 -13.338  1.00 13.35           N  
ANISOU 1796  N   LEU A1023     2314   1036   1722    151  -1344    262       N  
ATOM   1797  CA  LEU A1023     -43.937  44.728 -12.289  1.00 12.79           C  
ANISOU 1797  CA  LEU A1023     2074    967   1817    -23  -1228    368       C  
ATOM   1798  C   LEU A1023     -44.943  45.707 -12.888  1.00 12.43           C  
ANISOU 1798  C   LEU A1023     1842    955   1926   -154  -1184    458       C  
ATOM   1799  O   LEU A1023     -46.125  45.673 -12.535  1.00 12.85           O  
ANISOU 1799  O   LEU A1023     1830    949   2102   -320  -1198    573       O  
ATOM   1800  CB  LEU A1023     -43.051  45.425 -11.252  1.00 11.77           C  
ANISOU 1800  CB  LEU A1023     1823    973   1673     53  -1049    316       C  
ATOM   1801  CG  LEU A1023     -43.719  46.504 -10.391  1.00 10.98           C  
ANISOU 1801  CG  LEU A1023     1509    933   1729    -71   -887    398       C  
ATOM   1802  CD1 LEU A1023     -44.761  45.898  -9.452  1.00 11.65           C  
ANISOU 1802  CD1 LEU A1023     1618    915   1893   -219   -910    499       C  
ATOM   1803  CD2 LEU A1023     -42.660  47.287  -9.604  1.00 10.03           C  
ANISOU 1803  CD2 LEU A1023     1297    946   1567     21   -733    333       C  
ATOM   1804  N   LEU A1024     -44.473  46.568 -13.771  1.00 11.83           N  
ANISOU 1804  N   LEU A1024     1677    985   1831    -82  -1135    412       N  
ATOM   1805  CA  LEU A1024     -45.335  47.588 -14.383  1.00 11.52           C  
ANISOU 1805  CA  LEU A1024     1473    975   1926   -185  -1099    487       C  
ATOM   1806  C   LEU A1024     -46.346  46.922 -15.297  1.00 16.21           C  
ANISOU 1806  C   LEU A1024     2159   1441   2559   -283  -1273    555       C  
ATOM   1807  O   LEU A1024     -47.496  47.373 -15.373  1.00 18.48           O  
ANISOU 1807  O   LEU A1024     2319   1712   2988   -419  -1272    659       O  
ATOM   1808  CB  LEU A1024     -44.457  48.579 -15.154  1.00 10.80           C  
ANISOU 1808  CB  LEU A1024     1306   1022   1776    -90  -1028    419       C  
ATOM   1809  CG  LEU A1024     -43.684  49.563 -14.279  1.00  9.84           C  
ANISOU 1809  CG  LEU A1024     1055   1033   1649    -51   -856    387       C  
ATOM   1810  CD1 LEU A1024     -42.681  50.363 -15.095  1.00  9.47           C  
ANISOU 1810  CD1 LEU A1024      960   1131   1504     22   -816    328       C  
ATOM   1811  CD2 LEU A1024     -44.637  50.499 -13.562  1.00  9.45           C  
ANISOU 1811  CD2 LEU A1024      850    975   1763   -161   -758    472       C  
ATOM   1812  N   SER A1025     -45.922  45.863 -15.974  1.00 18.64           N  
ANISOU 1812  N   SER A1025     2688   1661   2731   -205  -1428    498       N  
ATOM   1813  CA  SER A1025     -46.808  45.094 -16.871  1.00 22.12           C  
ANISOU 1813  CA  SER A1025     3269   1952   3182   -300  -1628    559       C  
ATOM   1814  C   SER A1025     -47.963  44.512 -16.078  1.00 19.90           C  
ANISOU 1814  C   SER A1025     2987   1568   3004   -495  -1690    687       C  
ATOM   1815  O   SER A1025     -49.107  44.497 -16.560  1.00 22.13           O  
ANISOU 1815  O   SER A1025     3224   1796   3388   -654  -1783    798       O  
ATOM   1816  CB  SER A1025     -46.037  43.998 -17.554  1.00 28.70           C  
ANISOU 1816  CB  SER A1025     4382   2698   3822   -151  -1787    459       C  
ATOM   1817  OG  SER A1025     -44.961  44.538 -18.305  1.00 68.62           O  
ANISOU 1817  OG  SER A1025     9412   7893   8765     29  -1719    349       O  
ATOM   1818  N   LYS A1026     -47.653  44.007 -14.891  1.00 19.42           N  
ANISOU 1818  N   LYS A1026     2977   1493   2909   -489  -1648    678       N  
ATOM   1819  CA  LYS A1026     -48.670  43.384 -14.020  1.00 21.12           C  
ANISOU 1819  CA  LYS A1026     3196   1630   3197   -687  -1702    807       C  
ATOM   1820  C   LYS A1026     -49.717  44.410 -13.596  1.00 19.44           C  
ANISOU 1820  C   LYS A1026     2681   1537   3165   -825  -1562    924       C  
ATOM   1821  O   LYS A1026     -50.875  44.027 -13.347  1.00 19.52           O  
ANISOU 1821  O   LYS A1026     2644   1517   3255  -1021  -1633   1064       O  
ATOM   1822  CB  LYS A1026     -48.018  42.630 -12.855  1.00 19.89           C  
ANISOU 1822  CB  LYS A1026     3179   1431   2946   -639  -1690    763       C  
ATOM   1823  CG  LYS A1026     -47.231  41.410 -13.335  1.00 22.99           C  
ANISOU 1823  CG  LYS A1026     3909   1673   3150   -510  -1884    665       C  
ATOM   1824  CD  LYS A1026     -47.079  40.271 -12.353  1.00 28.01           C  
ANISOU 1824  CD  LYS A1026     4763   2181   3695   -543  -1981    673       C  
ATOM   1825  CE  LYS A1026     -45.925  39.340 -12.687  1.00 29.07           C  
ANISOU 1825  CE  LYS A1026     5208   2215   3621   -312  -2118    525       C  
ATOM   1826  NZ  LYS A1026     -44.599  39.956 -12.402  1.00 25.81           N  
ANISOU 1826  NZ  LYS A1026     4694   1970   3140    -68  -1942    383       N  
ATOM   1827  N   PHE A1027     -49.324  45.669 -13.539  1.00 16.78           N  
ANISOU 1827  N   PHE A1027     2154   1339   2880   -723  -1381    871       N  
ATOM   1828  CA  PHE A1027     -50.234  46.776 -13.192  1.00 14.74           C  
ANISOU 1828  CA  PHE A1027     1625   1197   2776   -799  -1246    959       C  
ATOM   1829  C   PHE A1027     -50.828  47.377 -14.454  1.00 14.59           C  
ANISOU 1829  C   PHE A1027     1527   1186   2829   -825  -1309    992       C  
ATOM   1830  O   PHE A1027     -51.532  48.411 -14.338  1.00 14.42           O  
ANISOU 1830  O   PHE A1027     1288   1263   2928   -851  -1209   1049       O  
ATOM   1831  CB  PHE A1027     -49.445  47.832 -12.413  1.00 13.12           C  
ANISOU 1831  CB  PHE A1027     1302   1110   2572   -671  -1038    881       C  
ATOM   1832  CG  PHE A1027     -48.999  47.398 -11.036  1.00 13.01           C  
ANISOU 1832  CG  PHE A1027     1331   1103   2508   -656   -957    863       C  
ATOM   1833  CD1 PHE A1027     -49.375  46.170 -10.507  1.00 14.10           C  
ANISOU 1833  CD1 PHE A1027     1596   1150   2611   -764  -1060    924       C  
ATOM   1834  CD2 PHE A1027     -48.251  48.256 -10.247  1.00 11.94           C  
ANISOU 1834  CD2 PHE A1027     1115   1058   2360   -550   -786    795       C  
ATOM   1835  CE1 PHE A1027     -48.979  45.799  -9.237  1.00 14.05           C  
ANISOU 1835  CE1 PHE A1027     1635   1147   2556   -755   -988    910       C  
ATOM   1836  CE2 PHE A1027     -47.857  47.880  -8.976  1.00 11.87           C  
ANISOU 1836  CE2 PHE A1027     1149   1053   2306   -538   -714    780       C  
ATOM   1837  CZ  PHE A1027     -48.224  46.655  -8.475  1.00 12.90           C  
ANISOU 1837  CZ  PHE A1027     1402   1095   2402   -637   -811    836       C  
ATOM   1838  N   GLY A1028     -50.472  46.823 -15.612  1.00 14.89           N  
ANISOU 1838  N   GLY A1028     1744   1129   2782   -791  -1464    944       N  
ATOM   1839  CA  GLY A1028     -51.002  47.274 -16.901  1.00 15.12           C  
ANISOU 1839  CA  GLY A1028     1735   1147   2864   -821  -1550    973       C  
ATOM   1840  C   GLY A1028     -50.332  48.542 -17.383  1.00 14.00           C  
ANISOU 1840  C   GLY A1028     1493   1104   2719   -693  -1428    891       C  
ATOM   1841  O   GLY A1028     -50.952  49.349 -18.108  1.00 16.76           O  
ANISOU 1841  O   GLY A1028     1729   1481   3156   -727  -1437    935       O  
ATOM   1842  N   MET A1029     -49.078  48.715 -17.011  1.00 12.98           N  
ANISOU 1842  N   MET A1029     1413   1032   2486   -556  -1327    780       N  
ATOM   1843  CA  MET A1029     -48.341  49.954 -17.356  1.00 12.12           C  
ANISOU 1843  CA  MET A1029     1213   1033   2357   -461  -1211    714       C  
ATOM   1844  C   MET A1029     -47.193  49.686 -18.324  1.00 13.18           C  
ANISOU 1844  C   MET A1029     1492   1188   2327   -343  -1265    610       C  
ATOM   1845  O   MET A1029     -46.566  48.647 -18.294  1.00 12.23           O  
ANISOU 1845  O   MET A1029     1535   1028   2083   -268  -1333    549       O  
ATOM   1846  CB  MET A1029     -47.823  50.660 -16.102  1.00 11.07           C  
ANISOU 1846  CB  MET A1029      973    995   2238   -414  -1031    686       C  
ATOM   1847  CG  MET A1029     -48.930  51.199 -15.224  1.00 11.83           C  
ANISOU 1847  CG  MET A1029      903   1107   2482   -496   -951    780       C  
ATOM   1848  SD  MET A1029     -48.275  52.116 -13.801  1.00 12.34           S  
ANISOU 1848  SD  MET A1029      877   1269   2544   -423   -748    737       S  
ATOM   1849  CE  MET A1029     -49.757  52.323 -12.816  1.00 14.49           C  
ANISOU 1849  CE  MET A1029      982   1559   2964   -505   -685    854       C  
ATOM   1850  N   ASP A1030     -46.897  50.671 -19.156  1.00 16.32           N  
ANISOU 1850  N   ASP A1030     1827   1660   2713   -318  -1234    589       N  
ATOM   1851  CA  ASP A1030     -45.666  50.644 -19.974  1.00 19.08           C  
ANISOU 1851  CA  ASP A1030     2265   2095   2888   -200  -1243    493       C  
ATOM   1852  C   ASP A1030     -44.500  51.022 -19.078  1.00 11.16           C  
ANISOU 1852  C   ASP A1030     1207   1227   1804   -117  -1098    428       C  
ATOM   1853  O   ASP A1030     -44.734  51.519 -17.977  1.00 10.08           O  
ANISOU 1853  O   ASP A1030      967   1099   1761   -162   -995    461       O  
ATOM   1854  CB  ASP A1030     -45.807  51.560 -21.191  1.00 42.40           C  
ANISOU 1854  CB  ASP A1030     5174   5086   5850   -231  -1269    510       C  
ATOM   1855  CG  ASP A1030     -44.888  51.183 -22.338  1.00 71.35           C  
ANISOU 1855  CG  ASP A1030     8962   8817   9330   -129  -1332    434       C  
ATOM   1856  OD1 ASP A1030     -43.679  50.998 -22.082  1.00 94.57           O  
ANISOU 1856  OD1 ASP A1030    11923  11885  12121    -13  -1265    354       O  
ATOM   1857  OD2 ASP A1030     -45.394  51.059 -23.474  1.00 70.95           O  
ANISOU 1857  OD2 ASP A1030     8982   8699   9276   -158  -1451    456       O  
ATOM   1858  N   GLU A1031     -43.286  50.786 -19.537  1.00 10.75           N  
ANISOU 1858  N   GLU A1031     1219   1290   1576      3  -1094    342       N  
ATOM   1859  CA  GLU A1031     -42.095  51.081 -18.721  1.00 10.26           C  
ANISOU 1859  CA  GLU A1031     1098   1379   1420     80   -970    285       C  
ATOM   1860  C   GLU A1031     -41.908  52.590 -18.563  1.00  9.56           C  
ANISOU 1860  C   GLU A1031      855   1393   1381      0   -857    321       C  
ATOM   1861  O   GLU A1031     -42.226  53.362 -19.486  1.00  9.61           O  
ANISOU 1861  O   GLU A1031      827   1410   1415    -66   -884    358       O  
ATOM   1862  CB  GLU A1031     -40.833  50.469 -19.336  1.00 13.22           C  
ANISOU 1862  CB  GLU A1031     1554   1892   1573    243   -996    188       C  
ATOM   1863  CG  GLU A1031     -40.830  48.951 -19.393  1.00 23.85           C  
ANISOU 1863  CG  GLU A1031     3097   3130   2833    363  -1119    132       C  
ATOM   1864  CD  GLU A1031     -39.541  48.358 -19.954  1.00 37.92           C  
ANISOU 1864  CD  GLU A1031     4959   5071   4375    572  -1140     24       C  
ATOM   1865  OE1 GLU A1031     -39.623  47.443 -20.819  1.00 41.03           O  
ANISOU 1865  OE1 GLU A1031     5531   5392   4667    675  -1276    -20       O  
ATOM   1866  OE2 GLU A1031     -38.450  48.804 -19.518  1.00 45.79           O  
ANISOU 1866  OE2 GLU A1031     5843   6274   5279    639  -1027    -14       O  
ATOM   1867  N   GLY A1032     -41.368  52.980 -17.429  1.00  9.02           N  
ANISOU 1867  N   GLY A1032      721   1392   1314      3   -748    311       N  
ATOM   1868  CA  GLY A1032     -40.951  54.361 -17.185  1.00  8.54           C  
ANISOU 1868  CA  GLY A1032      553   1431   1260    -65   -656    337       C  
ATOM   1869  C   GLY A1032     -40.314  54.447 -15.823  1.00  8.12           C  
ANISOU 1869  C   GLY A1032      466   1430   1189    -41   -558    315       C  
ATOM   1870  O   GLY A1032     -40.136  53.395 -15.157  1.00  8.21           O  
ANISOU 1870  O   GLY A1032      535   1411   1172     38   -561    274       O  
ATOM   1871  N   VAL A1033     -40.006  55.653 -15.390  1.00  7.78           N  
ANISOU 1871  N   VAL A1033      353   1444   1157   -112   -486    343       N  
ATOM   1872  CA  VAL A1033     -39.391  55.836 -14.056  1.00  7.43           C  
ANISOU 1872  CA  VAL A1033      286   1443   1093    -99   -398    327       C  
ATOM   1873  C   VAL A1033     -40.432  55.530 -12.994  1.00  7.15           C  
ANISOU 1873  C   VAL A1033      266   1246   1203   -103   -368    350       C  
ATOM   1874  O   VAL A1033     -41.503  56.141 -12.964  1.00  7.10           O  
ANISOU 1874  O   VAL A1033      234   1137   1327   -160   -366    404       O  
ATOM   1875  CB  VAL A1033     -38.778  57.223 -13.870  1.00  7.34           C  
ANISOU 1875  CB  VAL A1033      225   1520   1041   -189   -351    357       C  
ATOM   1876  CG1 VAL A1033     -38.108  57.337 -12.517  1.00  7.08           C  
ANISOU 1876  CG1 VAL A1033      185   1528    977   -176   -275    340       C  
ATOM   1877  CG2 VAL A1033     -37.793  57.515 -14.986  1.00  7.85           C  
ANISOU 1877  CG2 VAL A1033      258   1773    950   -213   -384    353       C  
ATOM   1878  N   THR A1034     -40.122  54.585 -12.132  1.00  7.12           N  
ANISOU 1878  N   THR A1034      301   1234   1168    -36   -347    312       N  
ATOM   1879  CA  THR A1034     -41.107  54.110 -11.149  1.00  7.06           C  
ANISOU 1879  CA  THR A1034      311   1091   1279    -49   -323    342       C  
ATOM   1880  C   THR A1034     -40.775  54.642  -9.764  1.00  6.70           C  
ANISOU 1880  C   THR A1034      245   1060   1240    -52   -221    340       C  
ATOM   1881  O   THR A1034     -39.648  54.528  -9.276  1.00  6.58           O  
ANISOU 1881  O   THR A1034      246   1137   1117     -8   -191    293       O  
ATOM   1882  CB  THR A1034     -41.201  52.590 -11.218  1.00  7.49           C  
ANISOU 1882  CB  THR A1034      462   1086   1297      8   -401    314       C  
ATOM   1883  OG1 THR A1034     -41.262  52.212 -12.595  1.00  7.91           O  
ANISOU 1883  OG1 THR A1034      556   1142   1307     27   -504    303       O  
ATOM   1884  CG2 THR A1034     -42.413  52.074 -10.480  1.00  7.72           C  
ANISOU 1884  CG2 THR A1034      502    981   1448    -48   -403    373       C  
ATOM   1885  N   PHE A1035     -41.788  55.217  -9.137  1.00  6.67           N  
ANISOU 1885  N   PHE A1035      204    972   1358    -96   -170    392       N  
ATOM   1886  CA  PHE A1035     -41.706  55.749  -7.762  1.00  6.48           C  
ANISOU 1886  CA  PHE A1035      176    937   1349    -92    -72    395       C  
ATOM   1887  C   PHE A1035     -42.678  54.974  -6.879  1.00  6.77           C  
ANISOU 1887  C   PHE A1035      212    892   1466    -92    -42    428       C  
ATOM   1888  O   PHE A1035     -43.782  54.624  -7.323  1.00  7.19           O  
ANISOU 1888  O   PHE A1035      230    892   1609   -126    -82    480       O  
ATOM   1889  CB  PHE A1035     -42.042  57.241  -7.749  1.00  6.50           C  
ANISOU 1889  CB  PHE A1035      145    924   1398   -124    -38    426       C  
ATOM   1890  CG  PHE A1035     -41.171  58.083  -8.644  1.00  6.42           C  
ANISOU 1890  CG  PHE A1035      143    991   1304   -162    -82    414       C  
ATOM   1891  CD1 PHE A1035     -39.996  58.638  -8.172  1.00  6.30           C  
ANISOU 1891  CD1 PHE A1035      155   1056   1182   -182    -57    392       C  
ATOM   1892  CD2 PHE A1035     -41.511  58.293  -9.966  1.00  6.60           C  
ANISOU 1892  CD2 PHE A1035      146   1015   1346   -195   -156    435       C  
ATOM   1893  CE1 PHE A1035     -39.184  59.392  -8.997  1.00  6.46           C  
ANISOU 1893  CE1 PHE A1035      172   1170   1110   -248   -104    399       C  
ATOM   1894  CE2 PHE A1035     -40.704  59.066 -10.785  1.00  6.68           C  
ANISOU 1894  CE2 PHE A1035      164   1109   1265   -249   -198    436       C  
ATOM   1895  CZ  PHE A1035     -39.540  59.609 -10.301  1.00  6.66           C  
ANISOU 1895  CZ  PHE A1035      178   1200   1150   -283   -171    422       C  
ATOM   1896  N   MET A1036     -42.271  54.723  -5.651  1.00  6.67           N  
ANISOU 1896  N   MET A1036      236    879   1416    -67     23    408       N  
ATOM   1897  CA  MET A1036     -43.113  53.949  -4.715  1.00  7.08           C  
ANISOU 1897  CA  MET A1036      294    871   1524    -83     56    447       C  
ATOM   1898  C   MET A1036     -43.212  54.609  -3.342  1.00  7.09           C  
ANISOU 1898  C   MET A1036      286    871   1534    -65    172    454       C  
ATOM   1899  O   MET A1036     -42.222  55.179  -2.846  1.00  6.69           O  
ANISOU 1899  O   MET A1036      277    853   1410    -34    209    408       O  
ATOM   1900  CB  MET A1036     -42.524  52.546  -4.618  1.00  7.19           C  
ANISOU 1900  CB  MET A1036      407    866   1458    -64    -10    411       C  
ATOM   1901  CG  MET A1036     -43.202  51.671  -3.622  1.00  7.72           C  
ANISOU 1901  CG  MET A1036      510    871   1553   -103      6    454       C  
ATOM   1902  SD  MET A1036     -42.115  50.316  -3.219  1.00  7.82           S  
ANISOU 1902  SD  MET A1036      683    854   1434    -47    -67    386       S  
ATOM   1903  CE  MET A1036     -42.882  49.719  -1.714  1.00  8.43           C  
ANISOU 1903  CE  MET A1036      794    866   1541   -118    -10    450       C  
ATOM   1904  N   PHE A1037     -44.395  54.482  -2.745  1.00  7.70           N  
ANISOU 1904  N   PHE A1037      308    925   1691    -88    223    518       N  
ATOM   1905  CA  PHE A1037     -44.686  54.954  -1.381  1.00  7.99           C  
ANISOU 1905  CA  PHE A1037      337    966   1730    -58    340    531       C  
ATOM   1906  C   PHE A1037     -45.269  53.805  -0.556  1.00  8.62           C  
ANISOU 1906  C   PHE A1037      422   1035   1816   -106    361    580       C  
ATOM   1907  O   PHE A1037     -46.214  53.107  -0.976  1.00  9.28           O  
ANISOU 1907  O   PHE A1037      449   1117   1958   -176    313    650       O  
ATOM   1908  CB  PHE A1037     -45.653  56.135  -1.383  1.00  8.50           C  
ANISOU 1908  CB  PHE A1037      312   1048   1867    -18    400    569       C  
ATOM   1909  CG  PHE A1037     -46.081  56.566  -0.004  1.00  9.07           C  
ANISOU 1909  CG  PHE A1037      379   1137   1930     37    522    582       C  
ATOM   1910  CD1 PHE A1037     -45.347  57.479   0.717  1.00  8.81           C  
ANISOU 1910  CD1 PHE A1037      435   1081   1829    101    572    528       C  
ATOM   1911  CD2 PHE A1037     -47.199  56.025   0.593  1.00 10.04           C  
ANISOU 1911  CD2 PHE A1037      412   1306   2096     18    581    654       C  
ATOM   1912  CE1 PHE A1037     -45.736  57.861   1.989  1.00  9.46           C  
ANISOU 1912  CE1 PHE A1037      531   1173   1887    169    681    534       C  
ATOM   1913  CE2 PHE A1037     -47.592  56.413   1.859  1.00 10.73           C  
ANISOU 1913  CE2 PHE A1037      489   1431   2157     83    703    666       C  
ATOM   1914  CZ  PHE A1037     -46.852  57.317   2.562  1.00 10.41           C  
ANISOU 1914  CZ  PHE A1037      554   1353   2047    169    753    600       C  
ATOM   1915  N   ILE A1038     -44.697  53.584   0.608  1.00  8.52           N  
ANISOU 1915  N   ILE A1038      486   1015   1737    -85    419    552       N  
ATOM   1916  CA  ILE A1038     -45.243  52.566   1.539  1.00  9.27           C  
ANISOU 1916  CA  ILE A1038      599   1098   1821   -144    445    606       C  
ATOM   1917  C   ILE A1038     -45.343  53.165   2.939  1.00  9.56           C  
ANISOU 1917  C   ILE A1038      639   1163   1830    -97    580    607       C  
ATOM   1918  O   ILE A1038     -44.336  53.684   3.470  1.00  8.95           O  
ANISOU 1918  O   ILE A1038      646   1067   1686    -34    610    537       O  
ATOM   1919  CB  ILE A1038     -44.455  51.258   1.411  1.00  9.08           C  
ANISOU 1919  CB  ILE A1038      709   1015   1726   -175    336    572       C  
ATOM   1920  CG1 ILE A1038     -45.000  50.198   2.355  1.00  9.99           C  
ANISOU 1920  CG1 ILE A1038      874   1100   1819   -258    339    636       C  
ATOM   1921  CG2 ILE A1038     -42.967  51.475   1.598  1.00  8.23           C  
ANISOU 1921  CG2 ILE A1038      696    905   1525    -92    327    472       C  
ATOM   1922  CD1 ILE A1038     -44.619  48.818   1.928  1.00 10.22           C  
ANISOU 1922  CD1 ILE A1038     1044   1046   1793   -303    188    625       C  
ATOM   1923  N   GLY A1039     -46.538  53.101   3.515  1.00 10.64           N  
ANISOU 1923  N   GLY A1039      679   1354   2006   -127    657    691       N  
ATOM   1924  CA  GLY A1039     -46.792  53.681   4.839  1.00 11.20           C  
ANISOU 1924  CA  GLY A1039      744   1469   2040    -65    796    697       C  
ATOM   1925  C   GLY A1039     -48.248  53.938   5.112  1.00 12.58           C  
ANISOU 1925  C   GLY A1039      756   1758   2266    -63    886    791       C  
ATOM   1926  O   GLY A1039     -49.061  53.952   4.192  1.00 13.01           O  
ANISOU 1926  O   GLY A1039      686   1858   2399    -97    842    846       O  
ATOM   1927  N   ARG A1040     -48.562  54.146   6.385  1.00 13.44           N  
ANISOU 1927  N   ARG A1040      860   1925   2321    -17   1013    810       N  
ATOM   1928  CA  ARG A1040     -49.946  54.438   6.826  1.00 18.04           C  
ANISOU 1928  CA  ARG A1040     1267   2663   2925     12   1125    900       C  
ATOM   1929  C   ARG A1040     -50.376  55.731   6.160  1.00 15.18           C  
ANISOU 1929  C   ARG A1040      819   2332   2615    155   1142    870       C  
ATOM   1930  O   ARG A1040     -49.584  56.686   6.079  1.00 14.31           O  
ANISOU 1930  O   ARG A1040      827   2129   2480    264   1131    774       O  
ATOM   1931  CB  ARG A1040     -50.031  54.518   8.358  1.00 21.91           C  
ANISOU 1931  CB  ARG A1040     1792   3211   3319     64   1264    907       C  
ATOM   1932  CG  ARG A1040     -51.306  55.136   8.911  1.00 29.51           C  
ANISOU 1932  CG  ARG A1040     2578   4360   4272    165   1407    973       C  
ATOM   1933  CD  ARG A1040     -51.323  55.026  10.426  1.00 45.98           C  
ANISOU 1933  CD  ARG A1040     4716   6506   6246    199   1539    984       C  
ATOM   1934  NE  ARG A1040     -52.120  56.065  11.075  1.00 71.85           N  
ANISOU 1934  NE  ARG A1040     7897   9926   9474    397   1688    984       N  
ATOM   1935  CZ  ARG A1040     -53.434  56.010  11.307  1.00 92.26           C  
ANISOU 1935  CZ  ARG A1040    10255  12745  12053    416   1789   1090       C  
ATOM   1936  NH1 ARG A1040     -54.149  54.951  10.951  1.00 91.29           N  
ANISOU 1936  NH1 ARG A1040     9971  12737  11975    213   1751   1223       N  
ATOM   1937  NH2 ARG A1040     -54.032  57.028  11.901  1.00 88.93           N  
ANISOU 1937  NH2 ARG A1040     9771  12449  11568    644   1921   1067       N  
ATOM   1938  N   PHE A1041     -51.620  55.779   5.722  1.00 16.42           N  
ANISOU 1938  N   PHE A1041      780   2621   2835    150   1161    958       N  
ATOM   1939  CA  PHE A1041     -52.192  57.039   5.217  1.00 18.22           C  
ANISOU 1939  CA  PHE A1041      923   2894   3103    315   1184    934       C  
ATOM   1940  C   PHE A1041     -52.595  57.864   6.425  1.00 19.78           C  
ANISOU 1940  C   PHE A1041     1110   3184   3220    497   1337    916       C  
ATOM   1941  O   PHE A1041     -53.560  57.533   7.119  1.00 19.82           O  
ANISOU 1941  O   PHE A1041      960   3369   3200    500   1443   1003       O  
ATOM   1942  CB  PHE A1041     -53.319  56.736   4.229  1.00 18.45           C  
ANISOU 1942  CB  PHE A1041      744   3034   3229    245   1129   1033       C  
ATOM   1943  CG  PHE A1041     -52.855  56.120   2.926  1.00 16.60           C  
ANISOU 1943  CG  PHE A1041      560   2683   3064    102    964   1031       C  
ATOM   1944  CD1 PHE A1041     -51.518  56.071   2.566  1.00 14.86           C  
ANISOU 1944  CD1 PHE A1041      534   2292   2817     80    882    934       C  
ATOM   1945  CD2 PHE A1041     -53.770  55.597   2.039  1.00 17.36           C  
ANISOU 1945  CD2 PHE A1041      501   2853   3241     -5    888   1129       C  
ATOM   1946  CE1 PHE A1041     -51.116  55.499   1.369  1.00 13.95           C  
ANISOU 1946  CE1 PHE A1041      461   2091   2745    -26    739    928       C  
ATOM   1947  CE2 PHE A1041     -53.371  55.023   0.843  1.00 16.38           C  
ANISOU 1947  CE2 PHE A1041      440   2616   3166   -124    732   1123       C  
ATOM   1948  CZ  PHE A1041     -52.043  54.969   0.514  1.00 14.69           C  
ANISOU 1948  CZ  PHE A1041      424   2240   2916   -124    663   1019       C  
ATOM   1949  N   ASP A1042     -51.883  58.954   6.673  1.00 23.02           N  
ANISOU 1949  N   ASP A1042     1688   3481   3579    649   1344    808       N  
ATOM   1950  CA  ASP A1042     -52.292  59.864   7.763  1.00 27.11           C  
ANISOU 1950  CA  ASP A1042     2228   4066   4005    859   1475    777       C  
ATOM   1951  C   ASP A1042     -51.881  61.287   7.427  1.00 25.56           C  
ANISOU 1951  C   ASP A1042     2186   3739   3786   1033   1422    677       C  
ATOM   1952  O   ASP A1042     -50.942  61.493   6.615  1.00 19.98           O  
ANISOU 1952  O   ASP A1042     1607   2873   3109    955   1295    625       O  
ATOM   1953  CB  ASP A1042     -51.711  59.430   9.110  1.00 32.49           C  
ANISOU 1953  CB  ASP A1042     3032   4729   4583    835   1560    760       C  
ATOM   1954  CG  ASP A1042     -50.215  59.172   9.076  1.00 32.06           C  
ANISOU 1954  CG  ASP A1042     3194   4477   4507    727   1465    686       C  
ATOM   1955  OD1 ASP A1042     -49.568  59.611   8.106  1.00 39.70           O  
ANISOU 1955  OD1 ASP A1042     4237   5327   5519    709   1348    635       O  
ATOM   1956  OD2 ASP A1042     -49.710  58.538  10.024  1.00 34.62           O  
ANISOU 1956  OD2 ASP A1042     3606   4784   4765    663   1508    685       O  
ATOM   1957  N   ARG A1043     -52.552  62.223   8.079  1.00 31.06           N  
ANISOU 1957  N   ARG A1043     2881   4506   4411   1264   1513    653       N  
ATOM   1958  CA  ARG A1043     -52.230  63.668   7.930  1.00 43.45           C  
ANISOU 1958  CA  ARG A1043     4646   5933   5930   1454   1452    555       C  
ATOM   1959  C   ARG A1043     -50.938  64.013   8.690  1.00 42.37           C  
ANISOU 1959  C   ARG A1043     4792   5614   5693   1439   1426    473       C  
ATOM   1960  O   ARG A1043     -50.066  64.761   8.114  1.00 32.30           O  
ANISOU 1960  O   ARG A1043     3706   4157   4409   1417   1295    411       O  
ATOM   1961  CB  ARG A1043     -53.403  64.524   8.422  1.00 59.81           C  
ANISOU 1961  CB  ARG A1043     6643   8143   7939   1740   1550    550       C  
ATOM   1962  CG  ARG A1043     -54.716  64.277   7.693  1.00 64.54           C  
ANISOU 1962  CG  ARG A1043     6943   8951   8629   1770   1572    637       C  
ATOM   1963  CD  ARG A1043     -54.714  64.731   6.241  1.00 70.52           C  
ANISOU 1963  CD  ARG A1043     7700   9606   9487   1740   1416    627       C  
ATOM   1964  NE  ARG A1043     -55.020  66.146   6.078  1.00 68.50           N  
ANISOU 1964  NE  ARG A1043     7568   9280   9177   2008   1369    551       N  
ATOM   1965  CZ  ARG A1043     -55.331  66.730   4.920  1.00 90.96           C  
ANISOU 1965  CZ  ARG A1043    10397  12072  12091   2049   1248    545       C  
ATOM   1966  NH1 ARG A1043     -55.377  66.022   3.802  1.00 84.74           N  
ANISOU 1966  NH1 ARG A1043     9465  11299  11431   1839   1168    610       N  
ATOM   1967  NH2 ARG A1043     -55.598  68.026   4.880  1.00109.23           N  
ANISOU 1967  NH2 ARG A1043    12860  14306  14336   2308   1196    471       N  
ATOM   1968  N   GLY A1044     -50.876  63.520   9.929  1.00 32.69           N  
ANISOU 1968  N   GLY A1044     3585   4447   4387   1446   1543    481       N  
ATOM   1969  CA  GLY A1044     -49.953  63.979  10.958  1.00 33.58           C  
ANISOU 1969  CA  GLY A1044     3954   4424   4378   1495   1551    407       C  
ATOM   1970  C   GLY A1044     -48.572  63.436  10.716  1.00 26.13           C  
ANISOU 1970  C   GLY A1044     3131   3341   3454   1274   1447    388       C  
ATOM   1971  O   GLY A1044     -47.650  64.223  10.590  1.00 20.16           O  
ANISOU 1971  O   GLY A1044     2583   2423   2652   1274   1345    325       O  
ATOM   1972  N   GLN A1045     -48.427  62.120  10.678  1.00 26.14           N  
ANISOU 1972  N   GLN A1045     3011   3410   3509   1093   1466    444       N  
ATOM   1973  CA  GLN A1045     -47.064  61.513  10.813  1.00 27.77           C  
ANISOU 1973  CA  GLN A1045     3348   3506   3696    926   1392    416       C  
ATOM   1974  C   GLN A1045     -46.363  61.328   9.460  1.00 18.12           C  
ANISOU 1974  C   GLN A1045     2108   2221   2556    787   1249    411       C  
ATOM   1975  O   GLN A1045     -45.368  61.995   9.173  1.00 18.82           O  
ANISOU 1975  O   GLN A1045     2345   2196   2608    763   1152    358       O  
ATOM   1976  CB  GLN A1045     -47.145  60.191  11.591  1.00 38.57           C  
ANISOU 1976  CB  GLN A1045     4649   4955   5051    821   1470    468       C  
ATOM   1977  CG  GLN A1045     -47.964  60.271  12.876  1.00 46.42           C  
ANISOU 1977  CG  GLN A1045     5623   6054   5958    944   1627    491       C  
ATOM   1978  CD  GLN A1045     -47.448  61.308  13.846  1.00 59.27           C  
ANISOU 1978  CD  GLN A1045     7477   7579   7462   1095   1652    411       C  
ATOM   1979  OE1 GLN A1045     -46.250  61.590  13.907  1.00 58.73           O  
ANISOU 1979  OE1 GLN A1045     7597   7359   7357   1042   1558    351       O  
ATOM   1980  NE2 GLN A1045     -48.359  61.885  14.618  1.00 65.85           N  
ANISOU 1980  NE2 GLN A1045     8294   8506   8218   1288   1776    411       N  
ATOM   1981  N   LYS A1046     -46.886  60.391   8.680  1.00 13.67           N  
ANISOU 1981  N   LYS A1046     1365   1740   2086    687   1234    472       N  
ATOM   1982  CA  LYS A1046     -46.358  60.082   7.342  1.00 13.34           C  
ANISOU 1982  CA  LYS A1046     1289   1661   2118    566   1107    471       C  
ATOM   1983  C   LYS A1046     -46.944  61.076   6.340  1.00 16.02           C  
ANISOU 1983  C   LYS A1046     1580   1993   2511    642   1057    471       C  
ATOM   1984  O   LYS A1046     -48.038  61.687   6.560  1.00 21.25           O  
ANISOU 1984  O   LYS A1046     2174   2717   3181    783   1126    490       O  
ATOM   1985  CB  LYS A1046     -46.700  58.657   6.905  1.00 14.03           C  
ANISOU 1985  CB  LYS A1046     1241   1817   2271    433   1090    535       C  
ATOM   1986  CG  LYS A1046     -46.146  57.574   7.810  1.00 15.20           C  
ANISOU 1986  CG  LYS A1046     1453   1958   2363    351   1115    539       C  
ATOM   1987  CD  LYS A1046     -44.636  57.531   7.776  1.00 21.27           C  
ANISOU 1987  CD  LYS A1046     2372   2632   3074    308   1031    468       C  
ATOM   1988  CE  LYS A1046     -44.037  56.536   8.754  1.00 22.22           C  
ANISOU 1988  CE  LYS A1046     2578   2736   3129    253   1047    462       C  
ATOM   1989  NZ  LYS A1046     -44.015  57.082  10.131  1.00 20.88           N  
ANISOU 1989  NZ  LYS A1046     2505   2551   2876    333   1147    443       N  
ATOM   1990  N   GLY A1047     -46.280  61.218   5.203  1.00 12.18           N  
ANISOU 1990  N   GLY A1047     1119   1451   2057    559    937    453       N  
ATOM   1991  CA  GLY A1047     -46.570  62.363   4.318  1.00 12.15           C  
ANISOU 1991  CA  GLY A1047     1134   1403   2079    625    867    440       C  
ATOM   1992  C   GLY A1047     -47.228  62.033   3.019  1.00 12.04           C  
ANISOU 1992  C   GLY A1047      966   1437   2169    575    809    485       C  
ATOM   1993  O   GLY A1047     -46.886  62.683   2.062  1.00 11.68           O  
ANISOU 1993  O   GLY A1047      970   1332   2133    551    709    468       O  
ATOM   1994  N   VAL A1048     -48.160  61.089   3.024  1.00 12.49           N  
ANISOU 1994  N   VAL A1048      853   1599   2293    549    863    549       N  
ATOM   1995  CA  VAL A1048     -48.847  60.654   1.794  1.00 12.50           C  
ANISOU 1995  CA  VAL A1048      706   1646   2395    484    796    603       C  
ATOM   1996  C   VAL A1048     -49.606  61.838   1.219  1.00 13.39           C  
ANISOU 1996  C   VAL A1048      790   1754   2540    610    770    601       C  
ATOM   1997  O   VAL A1048     -49.771  61.914   0.015  1.00 13.12           O  
ANISOU 1997  O   VAL A1048      710   1705   2569    562    675    617       O  
ATOM   1998  CB  VAL A1048     -49.776  59.462   2.064  1.00 13.18           C  
ANISOU 1998  CB  VAL A1048      626   1850   2531    418    852    688       C  
ATOM   1999  CG1 VAL A1048     -50.924  59.833   2.981  1.00 14.85           C  
ANISOU 1999  CG1 VAL A1048      728   2182   2732    547    979    729       C  
ATOM   2000  CG2 VAL A1048     -50.292  58.872   0.765  1.00 13.08           C  
ANISOU 2000  CG2 VAL A1048      496   1862   2612    315    754    744       C  
ATOM   2001  N   ASP A1049     -50.118  62.691   2.083  1.00 14.59           N  
ANISOU 2001  N   ASP A1049      973   1924   2643    781    850    582       N  
ATOM   2002  CA  ASP A1049     -50.827  63.888   1.632  1.00 15.68           C  
ANISOU 2002  CA  ASP A1049     1117   2047   2793    941    815    567       C  
ATOM   2003  C   ASP A1049     -49.957  64.734   0.729  1.00 14.86           C  
ANISOU 2003  C   ASP A1049     1186   1790   2670    898    675    518       C  
ATOM   2004  O   ASP A1049     -50.457  65.193  -0.329  1.00 15.19           O  
ANISOU 2004  O   ASP A1049     1184   1817   2767    919    589    533       O  
ATOM   2005  CB  ASP A1049     -51.369  64.681   2.812  1.00 17.25           C  
ANISOU 2005  CB  ASP A1049     1365   2277   2909   1162    918    537       C  
ATOM   2006  CG  ASP A1049     -50.366  64.788   3.929  1.00 16.76           C  
ANISOU 2006  CG  ASP A1049     1498   2130   2740   1158    960    482       C  
ATOM   2007  OD1 ASP A1049     -49.432  63.951   3.961  1.00 15.35           O  
ANISOU 2007  OD1 ASP A1049     1348   1920   2561    980    942    484       O  
ATOM   2008  OD2 ASP A1049     -50.526  65.724   4.738  1.00 21.13           O  
ANISOU 2008  OD2 ASP A1049     2180   2645   3201   1345   1000    433       O  
ATOM   2009  N   VAL A1050     -48.688  64.858   1.084  1.00 13.90           N  
ANISOU 2009  N   VAL A1050     1239   1572   2468    817    645    472       N  
ATOM   2010  CA  VAL A1050     -47.715  65.649   0.290  1.00 13.25           C  
ANISOU 2010  CA  VAL A1050     1322   1367   2343    738    508    440       C  
ATOM   2011  C   VAL A1050     -47.419  64.956  -1.026  1.00 12.18           C  
ANISOU 2011  C   VAL A1050     1088   1262   2275    575    428    472       C  
ATOM   2012  O   VAL A1050     -47.352  65.683  -2.057  1.00 12.24           O  
ANISOU 2012  O   VAL A1050     1149   1210   2289    551    317    472       O  
ATOM   2013  CB  VAL A1050     -46.422  65.874   1.084  1.00 12.69           C  
ANISOU 2013  CB  VAL A1050     1437   1222   2160    675    500    398       C  
ATOM   2014  CG1 VAL A1050     -45.486  66.791   0.325  1.00 12.41           C  
ANISOU 2014  CG1 VAL A1050     1565   1083   2063    579    355    383       C  
ATOM   2015  CG2 VAL A1050     -46.687  66.400   2.491  1.00 13.75           C  
ANISOU 2015  CG2 VAL A1050     1683   1324   2217    835    586    364       C  
ATOM   2016  N   LEU A1051     -47.208  63.631  -1.039  1.00 11.34           N  
ANISOU 2016  N   LEU A1051      868   1234   2205    470    466    495       N  
ATOM   2017  CA  LEU A1051     -47.030  62.950  -2.337  1.00 10.56           C  
ANISOU 2017  CA  LEU A1051      688   1161   2160    344    382    521       C  
ATOM   2018  C   LEU A1051     -48.191  63.213  -3.279  1.00 11.27           C  
ANISOU 2018  C   LEU A1051      670   1267   2344    388    337    562       C  
ATOM   2019  O   LEU A1051     -47.972  63.509  -4.447  1.00 10.96           O  
ANISOU 2019  O   LEU A1051      652   1194   2317    326    233    564       O  
ATOM   2020  CB  LEU A1051     -46.937  61.446  -2.106  1.00  9.99           C  
ANISOU 2020  CB  LEU A1051      525   1159   2113    264    424    542       C  
ATOM   2021  CG  LEU A1051     -46.673  60.634  -3.373  1.00  9.30           C  
ANISOU 2021  CG  LEU A1051      387   1088   2059    152    331    558       C  
ATOM   2022  CD1 LEU A1051     -45.429  61.136  -4.082  1.00  8.57           C  
ANISOU 2022  CD1 LEU A1051      398    968   1890     90    249    517       C  
ATOM   2023  CD2 LEU A1051     -46.518  59.153  -3.044  1.00  8.96           C  
ANISOU 2023  CD2 LEU A1051      304   1083   2014     86    351    572       C  
ATOM   2024  N   LEU A1052     -49.399  63.100  -2.752  1.00 12.34           N  
ANISOU 2024  N   LEU A1052      684   1471   2534    490    415    598       N  
ATOM   2025  CA  LEU A1052     -50.630  63.291  -3.545  1.00 13.29           C  
ANISOU 2025  CA  LEU A1052      667   1636   2744    544    378    647       C  
ATOM   2026  C   LEU A1052     -50.692  64.706  -4.096  1.00 13.84           C  
ANISOU 2026  C   LEU A1052      851   1614   2793    642    294    613       C  
ATOM   2027  O   LEU A1052     -51.095  64.893  -5.247  1.00 13.98           O  
ANISOU 2027  O   LEU A1052      824   1616   2868    617    199    637       O  
ATOM   2028  CB  LEU A1052     -51.864  63.003  -2.683  1.00 14.66           C  
ANISOU 2028  CB  LEU A1052      675   1940   2954    650    492    697       C  
ATOM   2029  CG  LEU A1052     -52.094  61.531  -2.362  1.00 14.48           C  
ANISOU 2029  CG  LEU A1052      519   2014   2966    521    544    760       C  
ATOM   2030  CD1 LEU A1052     -53.337  61.348  -1.514  1.00 16.13           C  
ANISOU 2030  CD1 LEU A1052      549   2383   3194    610    658    826       C  
ATOM   2031  CD2 LEU A1052     -52.190  60.710  -3.629  1.00 13.93           C  
ANISOU 2031  CD2 LEU A1052      382   1939   2970    369    432    807       C  
ATOM   2032  N   LYS A1053     -50.283  65.665  -3.294  1.00 14.24           N  
ANISOU 2032  N   LYS A1053     1065   1589   2753    745    315    560       N  
ATOM   2033  CA  LYS A1053     -50.199  67.066  -3.719  1.00 18.16           C  
ANISOU 2033  CA  LYS A1053     1735   1963   3202    828    211    524       C  
ATOM   2034  C   LYS A1053     -49.183  67.174  -4.859  1.00 15.10           C  
ANISOU 2034  C   LYS A1053     1443   1499   2793    643     82    524       C  
ATOM   2035  O   LYS A1053     -49.469  67.793  -5.910  1.00 16.09           O  
ANISOU 2035  O   LYS A1053     1601   1570   2941    641    -30    535       O  
ATOM   2036  CB  LYS A1053     -49.863  67.917  -2.499  1.00 27.51           C  
ANISOU 2036  CB  LYS A1053     3105   3071   4274    955    252    469       C  
ATOM   2037  CG  LYS A1053     -50.491  69.297  -2.447  1.00 50.19           C  
ANISOU 2037  CG  LYS A1053     6119   5850   7099   1164    189    435       C  
ATOM   2038  CD  LYS A1053     -50.631  69.728  -0.989  1.00 68.30           C  
ANISOU 2038  CD  LYS A1053     8516   8134   9300   1350    285    389       C  
ATOM   2039  CE  LYS A1053     -51.100  71.151  -0.787  1.00 80.02           C  
ANISOU 2039  CE  LYS A1053    10206   9497  10700   1585    210    337       C  
ATOM   2040  NZ  LYS A1053     -51.153  71.475   0.657  1.00 96.78           N  
ANISOU 2040  NZ  LYS A1053    12443  11611  12716   1766    307    287       N  
ATOM   2041  N   ALA A1054     -48.021  66.583  -4.648  1.00 12.58           N  
ANISOU 2041  N   ALA A1054     1165   1192   2422    499     97    512       N  
ATOM   2042  CA  ALA A1054     -46.934  66.635  -5.638  1.00 11.68           C  
ANISOU 2042  CA  ALA A1054     1124   1051   2262    326     -7    515       C  
ATOM   2043  C   ALA A1054     -47.313  65.946  -6.931  1.00 11.27           C  
ANISOU 2043  C   ALA A1054      935   1053   2293    249    -59    552       C  
ATOM   2044  O   ALA A1054     -46.930  66.417  -8.000  1.00 11.16           O  
ANISOU 2044  O   ALA A1054      983   1004   2253    163   -168    561       O  
ATOM   2045  CB  ALA A1054     -45.698  66.041  -5.040  1.00 10.72           C  
ANISOU 2045  CB  ALA A1054     1038    970   2064    221     35    495       C  
ATOM   2046  N   ILE A1055     -48.083  64.879  -6.834  1.00 11.21           N  
ANISOU 2046  N   ILE A1055      756   1127   2374    272      7    579       N  
ATOM   2047  CA  ILE A1055     -48.539  64.126  -8.029  1.00 10.97           C  
ANISOU 2047  CA  ILE A1055      606   1138   2423    198    -52    619       C  
ATOM   2048  C   ILE A1055     -49.475  65.009  -8.833  1.00 11.92           C  
ANISOU 2048  C   ILE A1055      717   1212   2599    267   -134    642       C  
ATOM   2049  O   ILE A1055     -49.421  64.975 -10.066  1.00 11.70           O  
ANISOU 2049  O   ILE A1055      687   1167   2589    185   -234    660       O  
ATOM   2050  CB  ILE A1055     -49.236  62.823  -7.614  1.00 11.00           C  
ANISOU 2050  CB  ILE A1055      451   1228   2501    194     20    656       C  
ATOM   2051  CG1 ILE A1055     -48.205  61.793  -7.175  1.00 10.00           C  
ANISOU 2051  CG1 ILE A1055      356   1129   2314    106     58    632       C  
ATOM   2052  CG2 ILE A1055     -50.091  62.270  -8.732  1.00 11.30           C  
ANISOU 2052  CG2 ILE A1055      370   1290   2630    147    -54    711       C  
ATOM   2053  CD1 ILE A1055     -48.783  60.432  -6.977  1.00 10.09           C  
ANISOU 2053  CD1 ILE A1055      252   1197   2381     65     89    675       C  
ATOM   2054  N   GLU A1056     -50.334  65.751  -8.147  1.00 13.08           N  
ANISOU 2054  N   GLU A1056      858   1347   2765    428    -94    638       N  
ATOM   2055  CA  GLU A1056     -51.316  66.610  -8.830  1.00 14.25           C  
ANISOU 2055  CA  GLU A1056      994   1458   2962    533   -175    655       C  
ATOM   2056  C   GLU A1056     -50.600  67.780  -9.484  1.00 14.27           C  
ANISOU 2056  C   GLU A1056     1211   1326   2883    497   -302    626       C  
ATOM   2057  O   GLU A1056     -51.038  68.245 -10.574  1.00 16.29           O  
ANISOU 2057  O   GLU A1056     1479   1535   3172    492   -416    646       O  
ATOM   2058  CB  GLU A1056     -52.429  67.072  -7.891  1.00 15.77           C  
ANISOU 2058  CB  GLU A1056     1116   1697   3176    750    -96    654       C  
ATOM   2059  CG  GLU A1056     -53.537  66.049  -7.795  1.00 17.25           C  
ANISOU 2059  CG  GLU A1056     1044   2043   3467    763    -23    721       C  
ATOM   2060  CD  GLU A1056     -54.724  66.494  -6.971  1.00 23.26           C  
ANISOU 2060  CD  GLU A1056     1690   2904   4241    986     59    732       C  
ATOM   2061  OE1 GLU A1056     -55.777  65.817  -7.036  1.00 27.25           O  
ANISOU 2061  OE1 GLU A1056     1961   3562   4829    994     98    805       O  
ATOM   2062  OE2 GLU A1056     -54.592  67.519  -6.278  1.00 28.70           O  
ANISOU 2062  OE2 GLU A1056     2528   3528   4848   1151     78    673       O  
ATOM   2063  N   ILE A1057     -49.535  68.250  -8.851  1.00 13.90           N  
ANISOU 2063  N   ILE A1057     1334   1219   2726    457   -294    587       N  
ATOM   2064  CA  ILE A1057     -48.682  69.293  -9.476  1.00 13.97           C  
ANISOU 2064  CA  ILE A1057     1558   1112   2637    363   -428    578       C  
ATOM   2065  C   ILE A1057     -48.177  68.764 -10.809  1.00 13.09           C  
ANISOU 2065  C   ILE A1057     1395   1043   2535    180   -501    610       C  
ATOM   2066  O   ILE A1057     -48.325  69.396 -11.830  1.00 14.02           O  
ANISOU 2066  O   ILE A1057     1582   1097   2646    142   -622    629       O  
ATOM   2067  CB  ILE A1057     -47.492  69.623  -8.577  1.00 13.63           C  
ANISOU 2067  CB  ILE A1057     1673   1033   2472    298   -406    549       C  
ATOM   2068  CG1 ILE A1057     -47.990  70.305  -7.305  1.00 14.73           C  
ANISOU 2068  CG1 ILE A1057     1910   1104   2579    494   -354    510       C  
ATOM   2069  CG2 ILE A1057     -46.487  70.460  -9.352  1.00 13.67           C  
ANISOU 2069  CG2 ILE A1057     1863    962   2368    130   -549    565       C  
ATOM   2070  CD1 ILE A1057     -46.930  70.666  -6.309  1.00 14.59           C  
ANISOU 2070  CD1 ILE A1057     2064   1036   2441    444   -339    483       C  
ATOM   2071  N   LEU A1058     -47.557  67.601 -10.753  1.00 11.95           N  
ANISOU 2071  N   LEU A1058     1143   1004   2392     80   -429    613       N  
ATOM   2072  CA  LEU A1058     -46.904  67.013 -11.933  1.00 11.18           C  
ANISOU 2072  CA  LEU A1058     1010    966   2272    -75   -487    633       C  
ATOM   2073  C   LEU A1058     -47.883  66.699 -13.047  1.00 11.46           C  
ANISOU 2073  C   LEU A1058      945   1000   2406    -63   -550    665       C  
ATOM   2074  O   LEU A1058     -47.492  66.783 -14.203  1.00 11.31           O  
ANISOU 2074  O   LEU A1058      962    982   2350   -170   -641    682       O  
ATOM   2075  CB  LEU A1058     -46.124  65.754 -11.541  1.00 10.14           C  
ANISOU 2075  CB  LEU A1058      792    945   2114   -137   -398    617       C  
ATOM   2076  CG  LEU A1058     -44.959  65.987 -10.581  1.00  9.82           C  
ANISOU 2076  CG  LEU A1058      843    925   1962   -178   -351    590       C  
ATOM   2077  CD1 LEU A1058     -44.236  64.686 -10.274  1.00  8.92           C  
ANISOU 2077  CD1 LEU A1058      641    923   1822   -217   -276    570       C  
ATOM   2078  CD2 LEU A1058     -43.995  67.015 -11.138  1.00 10.10           C  
ANISOU 2078  CD2 LEU A1058     1020    941   1876   -302   -451    604       C  
ATOM   2079  N   SER A1059     -49.107  66.340 -12.692  1.00 11.96           N  
ANISOU 2079  N   SER A1059      883   1078   2583     55   -503    680       N  
ATOM   2080  CA  SER A1059     -50.120  65.871 -13.667  1.00 15.59           C  
ANISOU 2080  CA  SER A1059     1220   1555   3147     58   -562    723       C  
ATOM   2081  C   SER A1059     -50.324  66.901 -14.762  1.00 17.60           C  
ANISOU 2081  C   SER A1059     1574   1722   3391     47   -700    735       C  
ATOM   2082  O   SER A1059     -50.704  66.494 -15.903  1.00 14.78           O  
ANISOU 2082  O   SER A1059     1160   1371   3082    -12   -780    768       O  
ATOM   2083  CB  SER A1059     -51.423  65.564 -12.968  1.00 20.73           C  
ANISOU 2083  CB  SER A1059     1715   2255   3904    189   -493    750       C  
ATOM   2084  OG  SER A1059     -52.039  66.750 -12.471  1.00 26.74           O  
ANISOU 2084  OG  SER A1059     2527   2967   4665    352   -496    735       O  
ATOM   2085  N   SER A1060     -50.054  68.173 -14.443  1.00 20.29           N  
ANISOU 2085  N   SER A1060     2080   1969   3659     96   -742    712       N  
ATOM   2086  CA  SER A1060     -50.277  69.241 -15.446  1.00 23.15           C  
ANISOU 2086  CA  SER A1060     2570   2224   3999     86   -893    726       C  
ATOM   2087  C   SER A1060     -49.068  69.420 -16.355  1.00 22.90           C  
ANISOU 2087  C   SER A1060     2661   2185   3854   -113   -974    737       C  
ATOM   2088  O   SER A1060     -49.104  70.279 -17.232  1.00 26.85           O  
ANISOU 2088  O   SER A1060     3287   2599   4316   -159  -1107    757       O  
ATOM   2089  CB  SER A1060     -50.669  70.537 -14.783  1.00 25.15           C  
ANISOU 2089  CB  SER A1060     2973   2364   4218    240   -932    700       C  
ATOM   2090  OG  SER A1060     -49.650  70.985 -13.898  1.00 22.32           O  
ANISOU 2090  OG  SER A1060     2766   1968   3743    200   -899    670       O  
ATOM   2091  N   LYS A1061     -48.034  68.595 -16.165  1.00 23.74           N  
ANISOU 2091  N   LYS A1061     2723   2394   3900   -225   -898    728       N  
ATOM   2092  CA  LYS A1061     -46.778  68.716 -16.916  1.00 24.43           C  
ANISOU 2092  CA  LYS A1061     2894   2529   3856   -409   -952    742       C  
ATOM   2093  C   LYS A1061     -46.527  67.486 -17.780  1.00 25.14           C  
ANISOU 2093  C   LYS A1061     2859   2736   3954   -480   -934    749       C  
ATOM   2094  O   LYS A1061     -46.890  66.359 -17.407  1.00 18.13           O  
ANISOU 2094  O   LYS A1061     1839   1903   3143   -417   -851    734       O  
ATOM   2095  CB  LYS A1061     -45.626  68.956 -15.933  1.00 25.85           C  
ANISOU 2095  CB  LYS A1061     3150   2748   3922   -467   -893    725       C  
ATOM   2096  CG  LYS A1061     -45.857  70.136 -14.998  1.00 32.77           C  
ANISOU 2096  CG  LYS A1061     4184   3490   4775   -385   -921    712       C  
ATOM   2097  CD  LYS A1061     -44.756  70.388 -13.997  1.00 33.69           C  
ANISOU 2097  CD  LYS A1061     4389   3631   4779   -451   -877    700       C  
ATOM   2098  CE  LYS A1061     -45.070  71.589 -13.127  1.00 42.75           C  
ANISOU 2098  CE  LYS A1061     5730   4616   5894   -355   -927    684       C  
ATOM   2099  NZ  LYS A1061     -43.922  71.977 -12.273  1.00 43.44           N  
ANISOU 2099  NZ  LYS A1061     5942   4709   5852   -457   -923    685       N  
ATOM   2100  N   LYS A1062     -45.785  67.710 -18.852  1.00 37.51           N  
ANISOU 2100  N   LYS A1062     4488   4346   5416   -618  -1012    772       N  
ATOM   2101  CA  LYS A1062     -45.559  66.725 -19.944  1.00 43.60           C  
ANISOU 2101  CA  LYS A1062     5182   5216   6167   -676  -1027    777       C  
ATOM   2102  C   LYS A1062     -44.700  65.551 -19.492  1.00 25.84           C  
ANISOU 2102  C   LYS A1062     2844   3110   3861   -674   -921    742       C  
ATOM   2103  O   LYS A1062     -45.012  64.366 -19.861  1.00 23.28           O  
ANISOU 2103  O   LYS A1062     2438   2823   3584   -630   -905    726       O  
ATOM   2104  CB  LYS A1062     -44.904  67.392 -21.165  1.00 56.58           C  
ANISOU 2104  CB  LYS A1062     6922   6891   7682   -823  -1132    815       C  
ATOM   2105  CG  LYS A1062     -43.508  67.980 -20.963  1.00 73.53           C  
ANISOU 2105  CG  LYS A1062     9141   9143   9654   -962  -1124    832       C  
ATOM   2106  CD  LYS A1062     -43.106  68.997 -22.025  1.00 79.75           C  
ANISOU 2106  CD  LYS A1062    10053   9925  10321  -1125  -1251    891       C  
ATOM   2107  CE  LYS A1062     -41.749  69.627 -21.774  1.00 75.44           C  
ANISOU 2107  CE  LYS A1062     9570   9500   9594  -1295  -1255    930       C  
ATOM   2108  NZ  LYS A1062     -41.663  71.016 -22.290  1.00 76.60           N  
ANISOU 2108  NZ  LYS A1062     9904   9547   9653  -1449  -1404    998       N  
ATOM   2109  N   GLU A1063     -43.678  65.857 -18.687  1.00 13.36           N  
ANISOU 2109  N   GLU A1063     1295   1598   2180   -717   -863    730       N  
ATOM   2110  CA  GLU A1063     -42.724  64.873 -18.140  1.00 10.40           C  
ANISOU 2110  CA  GLU A1063      848   1368   1733   -706   -767    693       C  
ATOM   2111  C   GLU A1063     -43.477  63.822 -17.320  1.00  9.13           C  
ANISOU 2111  C   GLU A1063      605   1163   1698   -577   -690    660       C  
ATOM   2112  O   GLU A1063     -42.927  62.702 -17.092  1.00  8.67           O  
ANISOU 2112  O   GLU A1063      493   1201   1598   -544   -634    624       O  
ATOM   2113  CB  GLU A1063     -41.644  65.529 -17.285  1.00 12.31           C  
ANISOU 2113  CB  GLU A1063     1139   1674   1862   -775   -730    697       C  
ATOM   2114  CG  GLU A1063     -40.768  66.495 -18.062  1.00 19.91           C  
ANISOU 2114  CG  GLU A1063     2178   2712   2674   -943   -813    748       C  
ATOM   2115  CD  GLU A1063     -41.327  67.904 -18.186  1.00 33.70           C  
ANISOU 2115  CD  GLU A1063     4073   4288   4441  -1000   -918    792       C  
ATOM   2116  OE1 GLU A1063     -42.491  68.128 -17.758  1.00 26.02           O  
ANISOU 2116  OE1 GLU A1063     3129   3147   3608   -878   -924    774       O  
ATOM   2117  OE2 GLU A1063     -40.599  68.780 -18.713  1.00 49.86           O  
ANISOU 2117  OE2 GLU A1063     6209   6380   6354  -1166  -1001    846       O  
ATOM   2118  N   PHE A1064     -44.684  64.134 -16.877  1.00  9.35           N  
ANISOU 2118  N   PHE A1064      625   1064   1863   -502   -691    673       N  
ATOM   2119  CA  PHE A1064     -45.472  63.188 -16.063  1.00  9.09           C  
ANISOU 2119  CA  PHE A1064      503   1008   1943   -405   -619    660       C  
ATOM   2120  C   PHE A1064     -45.789  61.906 -16.817  1.00  8.94           C  
ANISOU 2120  C   PHE A1064      424   1016   1956   -404   -652    661       C  
ATOM   2121  O   PHE A1064     -46.105  60.894 -16.195  1.00  8.74           O  
ANISOU 2121  O   PHE A1064      345    995   1981   -360   -604    653       O  
ATOM   2122  CB  PHE A1064     -46.751  63.925 -15.651  1.00  9.73           C  
ANISOU 2122  CB  PHE A1064      569    981   2145   -325   -627    686       C  
ATOM   2123  CG  PHE A1064     -47.654  63.186 -14.706  1.00  9.79           C  
ANISOU 2123  CG  PHE A1064      471    987   2260   -236   -547    692       C  
ATOM   2124  CD1 PHE A1064     -47.291  62.986 -13.391  1.00  9.50           C  
ANISOU 2124  CD1 PHE A1064      431    977   2200   -194   -440    666       C  
ATOM   2125  CD2 PHE A1064     -48.872  62.701 -15.136  1.00 10.28           C  
ANISOU 2125  CD2 PHE A1064      434   1032   2439   -209   -584    733       C  
ATOM   2126  CE1 PHE A1064     -48.126  62.289 -12.538  1.00  9.70           C  
ANISOU 2126  CE1 PHE A1064      357   1017   2312   -129   -366    682       C  
ATOM   2127  CE2 PHE A1064     -49.712  62.017 -14.277  1.00 10.57           C  
ANISOU 2127  CE2 PHE A1064      360   1095   2561   -155   -514    757       C  
ATOM   2128  CZ  PHE A1064     -49.337  61.814 -12.979  1.00 10.29           C  
ANISOU 2128  CZ  PHE A1064      323   1090   2495   -116   -402    732       C  
ATOM   2129  N   GLN A1065     -45.684  61.938 -18.129  1.00  9.15           N  
ANISOU 2129  N   GLN A1065      480   1054   1942   -459   -743    673       N  
ATOM   2130  CA  GLN A1065     -45.989  60.781 -18.980  1.00 11.52           C  
ANISOU 2130  CA  GLN A1065      760   1361   2257   -457   -800    673       C  
ATOM   2131  C   GLN A1065     -44.887  59.733 -18.889  1.00  8.82           C  
ANISOU 2131  C   GLN A1065      435   1123   1791   -439   -763    622       C  
ATOM   2132  O   GLN A1065     -45.143  58.558 -19.223  1.00  8.91           O  
ANISOU 2132  O   GLN A1065      455   1119   1811   -409   -803    610       O  
ATOM   2133  CB  GLN A1065     -46.239  61.246 -20.416  1.00 24.67           C  
ANISOU 2133  CB  GLN A1065     2466   2998   3906   -513   -913    701       C  
ATOM   2134  CG  GLN A1065     -47.522  62.065 -20.545  1.00 47.10           C  
ANISOU 2134  CG  GLN A1065     5285   5726   6885   -501   -969    750       C  
ATOM   2135  CD  GLN A1065     -47.662  62.753 -21.885  1.00 80.30           C  
ANISOU 2135  CD  GLN A1065     9553   9894  11062   -562  -1086    778       C  
ATOM   2136  OE1 GLN A1065     -46.767  62.705 -22.730  1.00 73.74           O  
ANISOU 2136  OE1 GLN A1065     8782   9134  10100   -626  -1117    765       O  
ATOM   2137  NE2 GLN A1065     -48.803  63.395 -22.096  1.00 75.50           N  
ANISOU 2137  NE2 GLN A1065     8927   9188  10568   -536  -1152    818       N  
ATOM   2138  N   GLU A1066     -43.724  60.131 -18.400  1.00  8.56           N  
ANISOU 2138  N   GLU A1066      416   1191   1643   -451   -699    593       N  
ATOM   2139  CA  GLU A1066     -42.562  59.228 -18.285  1.00  8.37           C  
ANISOU 2139  CA  GLU A1066      397   1300   1483   -412   -661    540       C  
ATOM   2140  C   GLU A1066     -42.459  58.642 -16.878  1.00  7.96           C  
ANISOU 2140  C   GLU A1066      325   1236   1462   -351   -576    512       C  
ATOM   2141  O   GLU A1066     -41.444  57.976 -16.574  1.00  7.85           O  
ANISOU 2141  O   GLU A1066      318   1331   1334   -304   -540    463       O  
ATOM   2142  CB  GLU A1066     -41.291  60.038 -18.542  1.00 10.33           C  
ANISOU 2142  CB  GLU A1066      649   1701   1574   -476   -643    538       C  
ATOM   2143  CG  GLU A1066     -41.304  60.852 -19.817  1.00 13.42           C  
ANISOU 2143  CG  GLU A1066     1068   2112   1916   -567   -722    579       C  
ATOM   2144  CD  GLU A1066     -39.983  61.570 -20.043  1.00 24.12           C  
ANISOU 2144  CD  GLU A1066     2417   3652   3095   -659   -707    594       C  
ATOM   2145  OE1 GLU A1066     -40.026  62.740 -20.490  1.00 51.11           O  
ANISOU 2145  OE1 GLU A1066     5878   7047   6495   -776   -759    649       O  
ATOM   2146  OE2 GLU A1066     -38.913  60.955 -19.757  1.00 16.30           O  
ANISOU 2146  OE2 GLU A1066     1380   2836   1978   -616   -650    557       O  
ATOM   2147  N   MET A1067     -43.432  58.944 -16.024  1.00  7.87           N  
ANISOU 2147  N   MET A1067      288   1112   1587   -345   -542    542       N  
ATOM   2148  CA  MET A1067     -43.401  58.515 -14.616  1.00  7.57           C  
ANISOU 2148  CA  MET A1067      234   1061   1578   -298   -455    524       C  
ATOM   2149  C   MET A1067     -44.421  57.416 -14.345  1.00  7.74           C  
ANISOU 2149  C   MET A1067      237   1001   1702   -270   -471    542       C  
ATOM   2150  O   MET A1067     -45.475  57.358 -14.999  1.00  8.15           O  
ANISOU 2150  O   MET A1067      262    984   1847   -294   -537    588       O  
ATOM   2151  CB  MET A1067     -43.663  59.698 -13.690  1.00  7.55           C  
ANISOU 2151  CB  MET A1067      225   1015   1628   -305   -394    545       C  
ATOM   2152  CG  MET A1067     -42.709  60.820 -13.942  1.00  7.60           C  
ANISOU 2152  CG  MET A1067      276   1082   1528   -366   -405    543       C  
ATOM   2153  SD  MET A1067     -43.185  62.289 -13.032  1.00  7.90           S  
ANISOU 2153  SD  MET A1067      362   1020   1620   -364   -377    568       S  
ATOM   2154  CE  MET A1067     -41.645  63.201 -13.203  1.00  8.02           C  
ANISOU 2154  CE  MET A1067      450   1135   1460   -476   -403    569       C  
ATOM   2155  N   ARG A1068     -44.133  56.621 -13.310  1.00  7.55           N  
ANISOU 2155  N   ARG A1068      225    985   1658   -232   -415    517       N  
ATOM   2156  CA  ARG A1068     -45.007  55.550 -12.813  1.00  7.86           C  
ANISOU 2156  CA  ARG A1068      259    953   1774   -231   -428    546       C  
ATOM   2157  C   ARG A1068     -45.039  55.613 -11.283  1.00  7.71           C  
ANISOU 2157  C   ARG A1068      216    932   1779   -210   -320    547       C  
ATOM   2158  O   ARG A1068     -43.985  55.614 -10.628  1.00  7.30           O  
ANISOU 2158  O   ARG A1068      203    932   1635   -175   -265    496       O  
ATOM   2159  CB  ARG A1068     -44.523  54.182 -13.297  1.00  8.05           C  
ANISOU 2159  CB  ARG A1068      373    972   1710   -205   -510    507       C  
ATOM   2160  CG  ARG A1068     -44.191  54.101 -14.776  1.00  8.25           C  
ANISOU 2160  CG  ARG A1068      444   1023   1665   -198   -607    485       C  
ATOM   2161  CD  ARG A1068     -45.451  54.077 -15.588  1.00  8.76           C  
ANISOU 2161  CD  ARG A1068      488    997   1840   -262   -697    552       C  
ATOM   2162  NE  ARG A1068     -45.228  53.981 -17.022  1.00  9.03           N  
ANISOU 2162  NE  ARG A1068      581   1042   1809   -258   -797    535       N  
ATOM   2163  CZ  ARG A1068     -45.083  55.019 -17.841  1.00  8.94           C  
ANISOU 2163  CZ  ARG A1068      536   1074   1785   -283   -802    542       C  
ATOM   2164  NH1 ARG A1068     -45.091  56.263 -17.376  1.00  8.60           N  
ANISOU 2164  NH1 ARG A1068      422   1059   1787   -309   -724    562       N  
ATOM   2165  NH2 ARG A1068     -44.912  54.797 -19.135  1.00  9.32           N  
ANISOU 2165  NH2 ARG A1068      645   1131   1762   -279   -896    528       N  
ATOM   2166  N   PHE A1069     -46.229  55.659 -10.720  1.00  8.16           N  
ANISOU 2166  N   PHE A1069      202    947   1950   -230   -289    609       N  
ATOM   2167  CA  PHE A1069     -46.386  55.718  -9.253  1.00  8.20           C  
ANISOU 2167  CA  PHE A1069      181    959   1973   -206   -180    617       C  
ATOM   2168  C   PHE A1069     -47.071  54.488  -8.687  1.00  8.75           C  
ANISOU 2168  C   PHE A1069      243   1002   2078   -249   -190    664       C  
ATOM   2169  O   PHE A1069     -48.020  53.955  -9.272  1.00  9.42           O  
ANISOU 2169  O   PHE A1069      288   1060   2229   -310   -268    728       O  
ATOM   2170  CB  PHE A1069     -47.158  56.964  -8.859  1.00  8.54           C  
ANISOU 2170  CB  PHE A1069      145   1005   2092   -174   -113    650       C  
ATOM   2171  CG  PHE A1069     -46.396  58.215  -9.157  1.00  8.13           C  
ANISOU 2171  CG  PHE A1069      143    960   1986   -147   -109    608       C  
ATOM   2172  CD1 PHE A1069     -46.358  58.727 -10.437  1.00  8.14           C  
ANISOU 2172  CD1 PHE A1069      154    951   1986   -175   -196    611       C  
ATOM   2173  CD2 PHE A1069     -45.702  58.866  -8.156  1.00  7.87           C  
ANISOU 2173  CD2 PHE A1069      161    937   1893   -110    -30    571       C  
ATOM   2174  CE1 PHE A1069     -45.639  59.878 -10.708  1.00  7.95           C  
ANISOU 2174  CE1 PHE A1069      190    933   1897   -179   -206    586       C  
ATOM   2175  CE2 PHE A1069     -44.992  60.026  -8.421  1.00  7.71           C  
ANISOU 2175  CE2 PHE A1069      205    914   1810   -115    -48    546       C  
ATOM   2176  CZ  PHE A1069     -44.956  60.526  -9.699  1.00  7.78           C  
ANISOU 2176  CZ  PHE A1069      223    918   1813   -157   -138    557       C  
ATOM   2177  N   ILE A1070     -46.598  54.086  -7.517  1.00  8.59           N  
ANISOU 2177  N   ILE A1070      265    989   2008   -229   -120    640       N  
ATOM   2178  CA  ILE A1070     -47.172  52.959  -6.750  1.00  9.23           C  
ANISOU 2178  CA  ILE A1070      356   1046   2104   -285   -123    691       C  
ATOM   2179  C   ILE A1070     -47.356  53.415  -5.316  1.00  9.35           C  
ANISOU 2179  C   ILE A1070      324   1099   2129   -256     14    704       C  
ATOM   2180  O   ILE A1070     -46.389  53.473  -4.556  1.00  8.80           O  
ANISOU 2180  O   ILE A1070      329   1031   1981   -207     69    642       O  
ATOM   2181  CB  ILE A1070     -46.331  51.673  -6.861  1.00  9.13           C  
ANISOU 2181  CB  ILE A1070      492    982   1991   -288   -212    644       C  
ATOM   2182  CG1 ILE A1070     -45.969  51.338  -8.313  1.00  9.05           C  
ANISOU 2182  CG1 ILE A1070      550    947   1942   -276   -341    610       C  
ATOM   2183  CG2 ILE A1070     -47.072  50.530  -6.188  1.00 10.03           C  
ANISOU 2183  CG2 ILE A1070      639   1050   2122   -377   -246    715       C  
ATOM   2184  CD1 ILE A1070     -45.098  50.107  -8.485  1.00  9.17           C  
ANISOU 2184  CD1 ILE A1070      731    917   1835   -234   -439    547       C  
ATOM   2185  N   ILE A1071     -48.587  53.702  -4.956  1.00 10.21           N  
ANISOU 2185  N   ILE A1071      307   1249   2323   -281     66    786       N  
ATOM   2186  CA  ILE A1071     -48.920  54.147  -3.588  1.00 10.62           C  
ANISOU 2186  CA  ILE A1071      304   1355   2374   -237    205    804       C  
ATOM   2187  C   ILE A1071     -49.505  52.988  -2.815  1.00 11.50           C  
ANISOU 2187  C   ILE A1071      401   1485   2482   -333    211    880       C  
ATOM   2188  O   ILE A1071     -50.545  52.469  -3.175  1.00 12.50           O  
ANISOU 2188  O   ILE A1071      437   1644   2668   -428    158    976       O  
ATOM   2189  CB  ILE A1071     -49.835  55.378  -3.613  1.00 11.23           C  
ANISOU 2189  CB  ILE A1071      248   1495   2522   -163    272    836       C  
ATOM   2190  CG1 ILE A1071     -49.280  56.429  -4.570  1.00 10.50           C  
ANISOU 2190  CG1 ILE A1071      201   1360   2428   -101    224    773       C  
ATOM   2191  CG2 ILE A1071     -50.040  55.942  -2.216  1.00 11.71           C  
ANISOU 2191  CG2 ILE A1071      281   1611   2557    -79    417    834       C  
ATOM   2192  CD1 ILE A1071     -49.961  57.762  -4.449  1.00 11.12           C  
ANISOU 2192  CD1 ILE A1071      207   1470   2548      4    281    780       C  
ATOM   2193  N   ILE A1072     -48.839  52.620  -1.722  1.00 11.25           N  
ANISOU 2193  N   ILE A1072      462   1436   2374   -320    270    845       N  
ATOM   2194  CA  ILE A1072     -49.236  51.483  -0.865  1.00 12.12           C  
ANISOU 2194  CA  ILE A1072      596   1551   2456   -423    271    915       C  
ATOM   2195  C   ILE A1072     -49.480  51.962   0.555  1.00 12.58           C  
ANISOU 2195  C   ILE A1072      603   1685   2490   -375    430    930       C  
ATOM   2196  O   ILE A1072     -48.623  52.554   1.175  1.00 11.82           O  
ANISOU 2196  O   ILE A1072      582   1566   2340   -276    501    847       O  
ATOM   2197  CB  ILE A1072     -48.307  50.254  -0.842  1.00 11.75           C  
ANISOU 2197  CB  ILE A1072      742   1399   2323   -469    164    871       C  
ATOM   2198  CG1 ILE A1072     -48.027  49.681  -2.231  1.00 11.50           C  
ANISOU 2198  CG1 ILE A1072      789   1291   2289   -494      0    847       C  
ATOM   2199  CG2 ILE A1072     -48.912  49.197   0.070  1.00 12.94           C  
ANISOU 2199  CG2 ILE A1072      918   1550   2446   -597    157    964       C  
ATOM   2200  CD1 ILE A1072     -46.588  49.787  -2.647  1.00 10.35           C  
ANISOU 2200  CD1 ILE A1072      766   1102   2061   -381    -35    720       C  
ATOM   2201  N   GLY A1073     -50.664  51.675   1.065  1.00 14.00           N  
ANISOU 2201  N   GLY A1073      652   1965   2700   -453    480   1044       N  
ATOM   2202  CA  GLY A1073     -51.007  52.052   2.439  1.00 14.74           C  
ANISOU 2202  CA  GLY A1073      688   2156   2756   -404    638   1069       C  
ATOM   2203  C   GLY A1073     -52.474  52.005   2.775  1.00 16.58           C  
ANISOU 2203  C   GLY A1073      711   2562   3027   -464    707   1205       C  
ATOM   2204  O   GLY A1073     -53.324  51.944   1.874  1.00 17.28           O  
ANISOU 2204  O   GLY A1073      667   2707   3191   -526    639   1280       O  
ATOM   2205  N   LYS A1074     -52.737  52.087   4.069  1.00 18.04           N  
ANISOU 2205  N   LYS A1074      860   2843   3151   -438    844   1235       N  
ATOM   2206  CA  LYS A1074     -54.101  52.036   4.632  1.00 25.36           C  
ANISOU 2206  CA  LYS A1074     1565   3986   4082   -486    941   1371       C  
ATOM   2207  C   LYS A1074     -54.209  53.135   5.675  1.00 25.22           C  
ANISOU 2207  C   LYS A1074     1498   4072   4012   -283   1126   1323       C  
ATOM   2208  O   LYS A1074     -53.208  53.420   6.328  1.00 22.98           O  
ANISOU 2208  O   LYS A1074     1390   3677   3664   -195   1167   1218       O  
ATOM   2209  CB  LYS A1074     -54.350  50.644   5.222  1.00 33.97           C  
ANISOU 2209  CB  LYS A1074     2691   5099   5117   -713    897   1486       C  
ATOM   2210  CG  LYS A1074     -55.816  50.230   5.311  1.00 52.60           C  
ANISOU 2210  CG  LYS A1074     4806   7685   7493   -863    919   1670       C  
ATOM   2211  CD  LYS A1074     -56.050  49.023   6.203  1.00 70.33           C  
ANISOU 2211  CD  LYS A1074     7095   9972   9652  -1086    905   1791       C  
ATOM   2212  CE  LYS A1074     -55.214  47.818   5.826  1.00 83.11           C  
ANISOU 2212  CE  LYS A1074     8983  11349  11245  -1248    710   1769       C  
ATOM   2213  NZ  LYS A1074     -55.535  47.336   4.463  1.00123.28           N  
ANISOU 2213  NZ  LYS A1074    14065  16365  16408  -1370    522   1817       N  
ATOM   2214  N   GLY A1075     -55.394  53.721   5.832  1.00 27.80           N  
ANISOU 2214  N   GLY A1075     1595   4612   4355   -202   1227   1398       N  
ATOM   2215  CA  GLY A1075     -55.567  54.766   6.842  1.00 29.01           C  
ANISOU 2215  CA  GLY A1075     1715   4870   4438     21   1400   1348       C  
ATOM   2216  C   GLY A1075     -56.766  55.650   6.590  1.00 29.65           C  
ANISOU 2216  C   GLY A1075     1554   5158   4551    178   1474   1393       C  
ATOM   2217  O   GLY A1075     -57.890  55.178   6.268  1.00 35.28           O  
ANISOU 2217  O   GLY A1075     2029   6070   5304     70   1466   1533       O  
ATOM   2218  N   ASP A1076     -56.491  56.950   6.735  1.00 30.13           N  
ANISOU 2218  N   ASP A1076     1692   5169   4586    437   1532   1274       N  
ATOM   2219  CA  ASP A1076     -57.445  58.055   6.522  1.00 34.32           C  
ANISOU 2219  CA  ASP A1076     2057   5854   5128    669   1593   1272       C  
ATOM   2220  C   ASP A1076     -58.235  57.756   5.256  1.00 35.16           C  
ANISOU 2220  C   ASP A1076     1970   6035   5351    560   1482   1364       C  
ATOM   2221  O   ASP A1076     -57.705  57.898   4.139  1.00 36.94           O  
ANISOU 2221  O   ASP A1076     2301   6075   5657    518   1340   1309       O  
ATOM   2222  CB  ASP A1076     -56.792  59.437   6.429  1.00 36.30           C  
ANISOU 2222  CB  ASP A1076     2504   5936   5353    917   1583   1117       C  
ATOM   2223  CG  ASP A1076     -57.796  60.581   6.500  1.00 43.32           C  
ANISOU 2223  CG  ASP A1076     3258   6987   6214   1203   1659   1106       C  
ATOM   2224  OD1 ASP A1076     -58.945  60.392   6.015  1.00 67.81           O  
ANISOU 2224  OD1 ASP A1076     6089  10303   9370   1193   1664   1211       O  
ATOM   2225  OD2 ASP A1076     -57.429  61.655   7.018  1.00 39.50           O  
ANISOU 2225  OD2 ASP A1076     2946   6414   5647   1437   1700    993       O  
ATOM   2226  N   PRO A1077     -59.556  57.470   5.410  1.00 34.32           N  
ANISOU 2226  N   PRO A1077     1569   6224   5247    536   1550   1504       N  
ATOM   2227  CA  PRO A1077     -60.414  57.183   4.267  1.00 33.91           C  
ANISOU 2227  CA  PRO A1077     1311   6270   5301    426   1442   1608       C  
ATOM   2228  C   PRO A1077     -60.370  58.249   3.164  1.00 32.54           C  
ANISOU 2228  C   PRO A1077     1178   5979   5204    603   1350   1515       C  
ATOM   2229  O   PRO A1077     -60.579  57.938   1.990  1.00 31.57           O  
ANISOU 2229  O   PRO A1077     1004   5807   5181    473   1208   1561       O  
ATOM   2230  CB  PRO A1077     -61.813  57.175   4.897  1.00 37.81           C  
ANISOU 2230  CB  PRO A1077     1473   7146   5747    481   1577   1747       C  
ATOM   2231  CG  PRO A1077     -61.586  56.858   6.351  1.00 37.24           C  
ANISOU 2231  CG  PRO A1077     1448   7155   5545    480   1730   1755       C  
ATOM   2232  CD  PRO A1077     -60.301  57.575   6.677  1.00 34.39           C  
ANISOU 2232  CD  PRO A1077     1417   6504   5145    646   1737   1565       C  
ATOM   2233  N   GLU A1078     -60.143  59.492   3.570  1.00 34.07           N  
ANISOU 2233  N   GLU A1078     1476   6129   5339    894   1423   1392       N  
ATOM   2234  CA  GLU A1078     -60.111  60.629   2.641  1.00 37.30           C  
ANISOU 2234  CA  GLU A1078     1954   6420   5797   1082   1334   1301       C  
ATOM   2235  C   GLU A1078     -58.865  60.540   1.776  1.00 31.27           C  
ANISOU 2235  C   GLU A1078     1451   5343   5086    947   1184   1215       C  
ATOM   2236  O   GLU A1078     -58.901  60.918   0.595  1.00 34.37           O  
ANISOU 2236  O   GLU A1078     1858   5644   5557    948   1057   1197       O  
ATOM   2237  CB  GLU A1078     -60.163  61.976   3.373  1.00 48.00           C  
ANISOU 2237  CB  GLU A1078     3397   7786   7051   1430   1433   1191       C  
ATOM   2238  CG  GLU A1078     -61.427  62.202   4.199  1.00 66.07           C  
ANISOU 2238  CG  GLU A1078     5418  10417   9266   1627   1591   1262       C  
ATOM   2239  CD  GLU A1078     -62.652  62.672   3.424  1.00 85.24           C  
ANISOU 2239  CD  GLU A1078     7589  13048  11751   1767   1557   1323       C  
ATOM   2240  OE1 GLU A1078     -62.831  62.241   2.260  1.00 86.94           O  
ANISOU 2240  OE1 GLU A1078     7722  13221  12088   1583   1418   1385       O  
ATOM   2241  OE2 GLU A1078     -63.434  63.484   3.986  1.00 99.54           O  
ANISOU 2241  OE2 GLU A1078     9283  15061  13474   2078   1663   1303       O  
ATOM   2242  N   LEU A1079     -57.773  60.063   2.353  1.00 26.98           N  
ANISOU 2242  N   LEU A1079     1106   4653   4492    840   1198   1164       N  
ATOM   2243  CA  LEU A1079     -56.512  59.973   1.604  1.00 24.32           C  
ANISOU 2243  CA  LEU A1079     1003   4055   4183    726   1068   1081       C  
ATOM   2244  C   LEU A1079     -56.504  58.732   0.709  1.00 23.12           C  
ANISOU 2244  C   LEU A1079      795   3878   4110    463    950   1162       C  
ATOM   2245  O   LEU A1079     -55.890  58.759  -0.348  1.00 21.52           O  
ANISOU 2245  O   LEU A1079      703   3520   3953    398    821   1118       O  
ATOM   2246  CB  LEU A1079     -55.328  60.021   2.575  1.00 25.26           C  
ANISOU 2246  CB  LEU A1079     1349   4040   4205    740   1123    991       C  
ATOM   2247  CG  LEU A1079     -55.077  61.366   3.266  1.00 24.11           C  
ANISOU 2247  CG  LEU A1079     1345   3841   3972    991   1189    889       C  
ATOM   2248  CD1 LEU A1079     -53.996  61.231   4.337  1.00 23.22           C  
ANISOU 2248  CD1 LEU A1079     1435   3624   3763    971   1245    823       C  
ATOM   2249  CD2 LEU A1079     -54.697  62.443   2.262  1.00 21.58           C  
ANISOU 2249  CD2 LEU A1079     1157   3363   3679   1077   1067    811       C  
ATOM   2250  N   GLU A1080     -57.185  57.678   1.123  1.00 24.89           N  
ANISOU 2250  N   GLU A1080      863   4255   4338    314    985   1283       N  
ATOM   2251  CA  GLU A1080     -57.394  56.521   0.245  1.00 24.22           C  
ANISOU 2251  CA  GLU A1080      727   4153   4322     69    851   1377       C  
ATOM   2252  C   GLU A1080     -58.219  56.961  -0.964  1.00 25.34           C  
ANISOU 2252  C   GLU A1080      722   4345   4558     96    759   1419       C  
ATOM   2253  O   GLU A1080     -57.891  56.618  -2.107  1.00 22.75           O  
ANISOU 2253  O   GLU A1080      471   3882   4287    -16    610   1411       O  
ATOM   2254  CB  GLU A1080     -58.081  55.376   0.986  1.00 25.94           C  
ANISOU 2254  CB  GLU A1080      807   4536   4510   -111    896   1518       C  
ATOM   2255  CG  GLU A1080     -57.286  54.814   2.136  1.00 25.86           C  
ANISOU 2255  CG  GLU A1080      954   4464   4406   -162    968   1486       C  
ATOM   2256  CD  GLU A1080     -57.821  53.484   2.642  1.00 32.98           C  
ANISOU 2256  CD  GLU A1080     1776   5475   5278   -405    956   1633       C  
ATOM   2257  OE1 GLU A1080     -58.649  52.883   1.932  1.00 54.07           O  
ANISOU 2257  OE1 GLU A1080     4304   8230   8006   -570    857   1758       O  
ATOM   2258  OE2 GLU A1080     -57.413  53.045   3.744  1.00 31.47           O  
ANISOU 2258  OE2 GLU A1080     1676   5281   4999   -442   1034   1630       O  
ATOM   2259  N   GLY A1081     -59.246  57.753  -0.691  1.00 26.96           N  
ANISOU 2259  N   GLY A1081      730   4746   4768    268    847   1455       N  
ATOM   2260  CA  GLY A1081     -60.109  58.281  -1.751  1.00 27.96           C  
ANISOU 2260  CA  GLY A1081      702   4941   4978    330    765   1494       C  
ATOM   2261  C   GLY A1081     -59.331  59.150  -2.706  1.00 25.01           C  
ANISOU 2261  C   GLY A1081      528   4340   4633    427    662   1368       C  
ATOM   2262  O   GLY A1081     -59.456  59.040  -3.896  1.00 25.60           O  
ANISOU 2262  O   GLY A1081      595   4347   4782    343    525   1389       O  
ATOM   2263  N   TRP A1082     -58.564  60.076  -2.153  1.00 22.59           N  
ANISOU 2263  N   TRP A1082      403   3923   4257    605    726   1244       N  
ATOM   2264  CA  TRP A1082     -57.720  60.984  -2.953  1.00 21.18           C  
ANISOU 2264  CA  TRP A1082      436   3527   4081    681    629   1129       C  
ATOM   2265  C   TRP A1082     -56.782  60.174  -3.849  1.00 19.27           C  
ANISOU 2265  C   TRP A1082      332   3120   3870    461    502   1116       C  
ATOM   2266  O   TRP A1082     -56.602  60.478  -5.020  1.00 18.65           O  
ANISOU 2266  O   TRP A1082      310   2939   3835    435    379   1093       O  
ATOM   2267  CB  TRP A1082     -56.920  61.898  -2.023  1.00 20.73           C  
ANISOU 2267  CB  TRP A1082      578   3374   3922    851    711   1014       C  
ATOM   2268  CG  TRP A1082     -56.240  63.026  -2.739  1.00 19.88           C  
ANISOU 2268  CG  TRP A1082      675   3076   3800    941    611    915       C  
ATOM   2269  CD1 TRP A1082     -56.138  63.222  -4.087  1.00 19.25           C  
ANISOU 2269  CD1 TRP A1082      630   2900   3783    873    466    913       C  
ATOM   2270  CD2 TRP A1082     -55.510  64.098  -2.130  1.00 19.65           C  
ANISOU 2270  CD2 TRP A1082      867   2922   3675   1092    634    811       C  
ATOM   2271  NE1 TRP A1082     -55.417  64.351  -4.355  1.00 18.72           N  
ANISOU 2271  NE1 TRP A1082      780   2667   3662    963    402    821       N  
ATOM   2272  CE2 TRP A1082     -55.016  64.909  -3.174  1.00 18.97           C  
ANISOU 2272  CE2 TRP A1082      937   2673   3597   1092    495    759       C  
ATOM   2273  CE3 TRP A1082     -55.238  64.452  -0.807  1.00 20.08           C  
ANISOU 2273  CE3 TRP A1082     1016   2983   3629   1217    750    762       C  
ATOM   2274  CZ2 TRP A1082     -54.269  66.059  -2.933  1.00 18.80           C  
ANISOU 2274  CZ2 TRP A1082     1164   2494   3485   1197    457    669       C  
ATOM   2275  CZ3 TRP A1082     -54.513  65.598  -0.568  1.00 19.89           C  
ANISOU 2275  CZ3 TRP A1082     1243   2795   3518   1338    712    665       C  
ATOM   2276  CH2 TRP A1082     -54.022  66.379  -1.618  1.00 19.27           C  
ANISOU 2276  CH2 TRP A1082     1320   2553   3448   1316    562    623       C  
ATOM   2277  N   ALA A1083     -56.116  59.200  -3.268  1.00 18.42           N  
ANISOU 2277  N   ALA A1083      297   2981   3721    323    533   1119       N  
ATOM   2278  CA  ALA A1083     -55.149  58.364  -4.000  1.00 16.80           C  
ANISOU 2278  CA  ALA A1083      236   2628   3517    148    420   1095       C  
ATOM   2279  C   ALA A1083     -55.871  57.593  -5.092  1.00 17.30           C  
ANISOU 2279  C   ALA A1083      188   2721   3663      1    295   1189       C  
ATOM   2280  O   ALA A1083     -55.409  57.592  -6.254  1.00 17.96           O  
ANISOU 2280  O   ALA A1083      366   2687   3770    -50    170   1155       O  
ATOM   2281  CB  ALA A1083     -54.486  57.412  -3.043  1.00 16.24           C  
ANISOU 2281  CB  ALA A1083      249   2541   3381     54    476   1090       C  
ATOM   2282  N   ARG A1084     -56.979  56.968  -4.721  1.00 19.15           N  
ANISOU 2282  N   ARG A1084      227   3118   3930    -71    325   1310       N  
ATOM   2283  CA  ARG A1084     -57.738  56.161  -5.695  1.00 19.63           C  
ANISOU 2283  CA  ARG A1084      183   3211   4064   -241    190   1419       C  
ATOM   2284  C   ARG A1084     -58.333  57.079  -6.748  1.00 20.08           C  
ANISOU 2284  C   ARG A1084      155   3280   4193   -144    120   1418       C  
ATOM   2285  O   ARG A1084     -58.475  56.627  -7.934  1.00 19.92           O  
ANISOU 2285  O   ARG A1084      151   3191   4226   -267    -32   1455       O  
ATOM   2286  CB  ARG A1084     -58.777  55.255  -5.035  1.00 21.46           C  
ANISOU 2286  CB  ARG A1084      221   3630   4301   -379    224   1571       C  
ATOM   2287  CG  ARG A1084     -58.153  54.210  -4.129  1.00 21.03           C  
ANISOU 2287  CG  ARG A1084      288   3530   4170   -509    257   1578       C  
ATOM   2288  CD  ARG A1084     -59.120  53.132  -3.671  1.00 25.79           C  
ANISOU 2288  CD  ARG A1084      737   4290   4770   -715    242   1748       C  
ATOM   2289  NE  ARG A1084     -58.396  51.955  -3.199  1.00 27.37           N  
ANISOU 2289  NE  ARG A1084     1128   4370   4900   -878    196   1750       N  
ATOM   2290  CZ  ARG A1084     -57.812  51.034  -3.982  1.00 29.56           C  
ANISOU 2290  CZ  ARG A1084     1603   4457   5169  -1018     23   1735       C  
ATOM   2291  NH1 ARG A1084     -57.873  51.117  -5.306  1.00 32.05           N  
ANISOU 2291  NH1 ARG A1084     1947   4686   5544  -1035   -117   1723       N  
ATOM   2292  NH2 ARG A1084     -57.166  50.017  -3.432  1.00 27.01           N  
ANISOU 2292  NH2 ARG A1084     1464   4030   4767  -1131    -15   1729       N  
ATOM   2293  N   SER A1085     -58.636  58.320  -6.363  1.00 21.43           N  
ANISOU 2293  N   SER A1085      267   3518   4358     75    212   1372       N  
ATOM   2294  CA  SER A1085     -59.158  59.345  -7.298  1.00 23.36           C  
ANISOU 2294  CA  SER A1085      460   3756   4657    204    140   1356       C  
ATOM   2295  C   SER A1085     -58.163  59.579  -8.429  1.00 19.69           C  
ANISOU 2295  C   SER A1085      214   3072   4193    159     13   1269       C  
ATOM   2296  O   SER A1085     -58.548  59.547  -9.605  1.00 20.22           O  
ANISOU 2296  O   SER A1085      250   3107   4323    100   -117   1304       O  
ATOM   2297  CB  SER A1085     -59.461  60.637  -6.567  1.00 25.02           C  
ANISOU 2297  CB  SER A1085      638   4038   4828    472    253   1298       C  
ATOM   2298  OG  SER A1085     -59.819  61.694  -7.448  1.00 30.81           O  
ANISOU 2298  OG  SER A1085     1378   4727   5598    613    168   1264       O  
ATOM   2299  N   LEU A1086     -56.905  59.763  -8.071  1.00 17.91           N  
ANISOU 2299  N   LEU A1086      196   2715   3892    176     49   1166       N  
ATOM   2300  CA  LEU A1086     -55.826  60.018  -9.043  1.00 16.35           C  
ANISOU 2300  CA  LEU A1086      199   2344   3668    133    -53   1085       C  
ATOM   2301  C   LEU A1086     -55.538  58.779  -9.867  1.00 15.69           C  
ANISOU 2301  C   LEU A1086      153   2206   3599    -59   -163   1121       C  
ATOM   2302  O   LEU A1086     -55.057  58.873 -10.997  1.00 14.94           O  
ANISOU 2302  O   LEU A1086      161   2012   3502   -104   -274   1087       O  
ATOM   2303  CB  LEU A1086     -54.580  60.408  -8.255  1.00 15.17           C  
ANISOU 2303  CB  LEU A1086      229   2113   3421    185     24    986       C  
ATOM   2304  CG  LEU A1086     -54.676  61.748  -7.545  1.00 15.78           C  
ANISOU 2304  CG  LEU A1086      343   2192   3460    381    101    933       C  
ATOM   2305  CD1 LEU A1086     -53.367  62.083  -6.858  1.00 14.63           C  
ANISOU 2305  CD1 LEU A1086      392   1952   3212    395    150    844       C  
ATOM   2306  CD2 LEU A1086     -55.049  62.830  -8.535  1.00 16.28           C  
ANISOU 2306  CD2 LEU A1086      432   2199   3554    468      1    918       C  
ATOM   2307  N   GLU A1087     -55.825  57.630  -9.289  1.00 16.10           N  
ANISOU 2307  N   GLU A1087      141   2322   3653   -170   -138   1188       N  
ATOM   2308  CA  GLU A1087     -55.602  56.319  -9.947  1.00 15.80           C  
ANISOU 2308  CA  GLU A1087      170   2219   3612   -350   -258   1224       C  
ATOM   2309  C   GLU A1087     -56.502  56.198 -11.146  1.00 18.94           C  
ANISOU 2309  C   GLU A1087      480   2624   4089   -422   -396   1301       C  
ATOM   2310  O   GLU A1087     -56.045  55.714 -12.213  1.00 19.40           O  
ANISOU 2310  O   GLU A1087      665   2571   4134   -505   -528   1281       O  
ATOM   2311  CB  GLU A1087     -55.887  55.162  -8.992  1.00 16.43           C  
ANISOU 2311  CB  GLU A1087      206   2363   3671   -464   -219   1298       C  
ATOM   2312  CG  GLU A1087     -55.676  53.816  -9.672  1.00 16.32           C  
ANISOU 2312  CG  GLU A1087      305   2255   3639   -640   -370   1333       C  
ATOM   2313  CD  GLU A1087     -55.715  52.614  -8.747  1.00 21.29           C  
ANISOU 2313  CD  GLU A1087      964   2901   4222   -766   -359   1394       C  
ATOM   2314  OE1 GLU A1087     -56.213  52.763  -7.608  1.00 28.61           O  
ANISOU 2314  OE1 GLU A1087     1763   3956   5150   -748   -230   1444       O  
ATOM   2315  OE2 GLU A1087     -55.250  51.528  -9.160  1.00 22.25           O  
ANISOU 2315  OE2 GLU A1087     1251   2907   4295   -876   -485   1390       O  
ATOM   2316  N   GLU A1088     -57.765  56.588 -10.972  1.00 23.07           N  
ANISOU 2316  N   GLU A1088      788   3289   4685   -387   -370   1391       N  
ATOM   2317  CA  GLU A1088     -58.762  56.518 -12.059  1.00 25.80           C  
ANISOU 2317  CA  GLU A1088     1019   3668   5116   -455   -504   1480       C  
ATOM   2318  C   GLU A1088     -58.481  57.628 -13.050  1.00 23.74           C  
ANISOU 2318  C   GLU A1088      837   3313   4870   -339   -563   1402       C  
ATOM   2319  O   GLU A1088     -58.522  57.391 -14.274  1.00 23.34           O  
ANISOU 2319  O   GLU A1088      844   3178   4845   -422   -711   1416       O  
ATOM   2320  CB  GLU A1088     -60.197  56.454 -11.534  1.00 34.86           C  
ANISOU 2320  CB  GLU A1088     1887   5032   6325   -467   -462   1615       C  
ATOM   2321  CG  GLU A1088     -60.760  57.766 -11.018  1.00 55.56           C  
ANISOU 2321  CG  GLU A1088     4362   7784   8964   -234   -344   1592       C  
ATOM   2322  CD  GLU A1088     -62.276  57.767 -10.801  1.00 76.42           C  
ANISOU 2322  CD  GLU A1088     6692  10676  11665   -226   -327   1732       C  
ATOM   2323  OE1 GLU A1088     -62.860  56.679 -10.549  1.00 75.33           O  
ANISOU 2323  OE1 GLU A1088     6428  10654  11538   -422   -352   1863       O  
ATOM   2324  OE2 GLU A1088     -62.885  58.861 -10.877  1.00 72.00           O  
ANISOU 2324  OE2 GLU A1088     6015  10208  11132    -23   -295   1715       O  
ATOM   2325  N   LYS A1089     -58.206  58.815 -12.530  1.00 26.42           N  
ANISOU 2325  N   LYS A1089     1197   3659   5183   -155   -461   1323       N  
ATOM   2326  CA  LYS A1089     -58.033  60.036 -13.340  1.00 26.63           C  
ANISOU 2326  CA  LYS A1089     1304   3600   5214    -38   -518   1258       C  
ATOM   2327  C   LYS A1089     -56.835  59.948 -14.275  1.00 24.05           C  
ANISOU 2327  C   LYS A1089     1198   3109   4829   -117   -607   1182       C  
ATOM   2328  O   LYS A1089     -56.987  60.466 -15.433  1.00 24.35           O  
ANISOU 2328  O   LYS A1089     1276   3082   4892   -115   -724   1179       O  
ATOM   2329  CB  LYS A1089     -57.897  61.236 -12.396  1.00 26.84           C  
ANISOU 2329  CB  LYS A1089     1350   3649   5197    166   -396   1189       C  
ATOM   2330  CG  LYS A1089     -57.820  62.592 -13.073  1.00 32.03           C  
ANISOU 2330  CG  LYS A1089     2109   4214   5847    298   -465   1129       C  
ATOM   2331  CD  LYS A1089     -57.594  63.732 -12.104  1.00 48.58           C  
ANISOU 2331  CD  LYS A1089     4280   6298   7877    495   -367   1055       C  
ATOM   2332  CE  LYS A1089     -57.429  65.078 -12.783  1.00 64.17           C  
ANISOU 2332  CE  LYS A1089     6408   8147   9825    608   -463    996       C  
ATOM   2333  NZ  LYS A1089     -56.901  66.106 -11.852  1.00 66.74           N  
ANISOU 2333  NZ  LYS A1089     6888   8410  10057    763   -394    914       N  
ATOM   2334  N   HIS A1090     -55.727  59.294 -13.848  1.00 20.52           N  
ANISOU 2334  N   HIS A1090      880   2613   4302   -181   -561   1128       N  
ATOM   2335  CA  HIS A1090     -54.479  59.350 -14.659  1.00 17.28           C  
ANISOU 2335  CA  HIS A1090      665   2088   3811   -223   -624   1048       C  
ATOM   2336  C   HIS A1090     -54.052  58.015 -15.260  1.00 16.89           C  
ANISOU 2336  C   HIS A1090      691   1996   3728   -358   -710   1058       C  
ATOM   2337  O   HIS A1090     -54.114  57.946 -16.491  1.00 30.73           O  
ANISOU 2337  O   HIS A1090     2493   3695   5488   -409   -834   1066       O  
ATOM   2338  CB  HIS A1090     -53.310  59.986 -13.904  1.00 14.17           C  
ANISOU 2338  CB  HIS A1090      392   1668   3322   -154   -524    958       C  
ATOM   2339  CG  HIS A1090     -53.568  61.415 -13.574  1.00 13.71           C  
ANISOU 2339  CG  HIS A1090      335   1604   3269    -19   -486    934       C  
ATOM   2340  ND1 HIS A1090     -53.930  61.815 -12.307  1.00 14.80           N  
ANISOU 2340  ND1 HIS A1090      412   1800   3411     93   -366    931       N  
ATOM   2341  CD2 HIS A1090     -53.581  62.522 -14.344  1.00 13.69           C  
ANISOU 2341  CD2 HIS A1090      402   1536   3261     27   -563    914       C  
ATOM   2342  CE1 HIS A1090     -54.122  63.116 -12.299  1.00 14.73           C  
ANISOU 2342  CE1 HIS A1090      450   1755   3392    220   -375    902       C  
ATOM   2343  NE2 HIS A1090     -53.935  63.572 -13.538  1.00 14.43           N  
ANISOU 2343  NE2 HIS A1090      494   1636   3352    176   -500    894       N  
ATOM   2344  N   GLY A1091     -53.754  57.026 -14.436  1.00 13.28           N  
ANISOU 2344  N   GLY A1091      250   1559   3236   -405   -657   1060       N  
ATOM   2345  CA  GLY A1091     -53.503  55.682 -14.959  1.00 13.21           C  
ANISOU 2345  CA  GLY A1091      332   1495   3189   -517   -761   1074       C  
ATOM   2346  C   GLY A1091     -52.025  55.354 -15.147  1.00 13.11           C  
ANISOU 2346  C   GLY A1091      499   1430   3049   -497   -761    972       C  
ATOM   2347  O   GLY A1091     -51.722  54.183 -15.396  1.00 20.03           O  
ANISOU 2347  O   GLY A1091     1478   2261   3872   -555   -840    967       O  
ATOM   2348  N   ASN A1092     -51.120  56.326 -15.015  1.00 11.18           N  
ANISOU 2348  N   ASN A1092      300   1200   2745   -416   -686    895       N  
ATOM   2349  CA  ASN A1092     -49.718  56.044 -14.601  1.00 10.24           C  
ANISOU 2349  CA  ASN A1092      296   1090   2502   -383   -632    809       C  
ATOM   2350  C   ASN A1092     -49.589  55.982 -13.080  1.00 10.09           C  
ANISOU 2350  C   ASN A1092      244   1108   2480   -348   -504    802       C  
ATOM   2351  O   ASN A1092     -48.473  55.894 -12.568  1.00  9.39           O  
ANISOU 2351  O   ASN A1092      233   1036   2296   -313   -448    735       O  
ATOM   2352  CB  ASN A1092     -48.769  57.076 -15.209  1.00  9.61           C  
ANISOU 2352  CB  ASN A1092      279   1027   2346   -347   -627    749       C  
ATOM   2353  CG  ASN A1092     -49.059  58.486 -14.743  1.00  9.71           C  
ANISOU 2353  CG  ASN A1092      239   1046   2402   -300   -560    756       C  
ATOM   2354  OD1 ASN A1092     -50.191  58.796 -14.381  1.00 10.41           O  
ANISOU 2354  OD1 ASN A1092      228   1130   2594   -276   -543    810       O  
ATOM   2355  ND2 ASN A1092     -48.050  59.342 -14.751  1.00  9.20           N  
ANISOU 2355  ND2 ASN A1092      246   1000   2249   -286   -532    707       N  
ATOM   2356  N   VAL A1093     -50.712  55.954 -12.382  1.00 10.88           N  
ANISOU 2356  N   VAL A1093      225   1234   2673   -360   -461    875       N  
ATOM   2357  CA  VAL A1093     -50.770  55.838 -10.907  1.00 10.99           C  
ANISOU 2357  CA  VAL A1093      198   1292   2684   -331   -337    881       C  
ATOM   2358  C   VAL A1093     -51.492  54.559 -10.499  1.00 11.81           C  
ANISOU 2358  C   VAL A1093      263   1405   2817   -428   -369    960       C  
ATOM   2359  O   VAL A1093     -52.552  54.232 -11.035  1.00 13.00           O  
ANISOU 2359  O   VAL A1093      326   1567   3043   -503   -448   1047       O  
ATOM   2360  CB  VAL A1093     -51.526  57.032 -10.322  1.00 11.56           C  
ANISOU 2360  CB  VAL A1093      153   1418   2819   -246   -245    906       C  
ATOM   2361  CG1 VAL A1093     -51.651  56.918  -8.819  1.00 11.84           C  
ANISOU 2361  CG1 VAL A1093      146   1511   2841   -208   -114    915       C  
ATOM   2362  CG2 VAL A1093     -50.871  58.332 -10.726  1.00 10.98           C  
ANISOU 2362  CG2 VAL A1093      151   1312   2708   -170   -242    840       C  
ATOM   2363  N   LYS A1094     -50.906  53.847  -9.554  1.00 11.54           N  
ANISOU 2363  N   LYS A1094      301   1365   2717   -437   -319    935       N  
ATOM   2364  CA  LYS A1094     -51.502  52.618  -9.009  1.00 12.44           C  
ANISOU 2364  CA  LYS A1094      408   1478   2838   -547   -352   1014       C  
ATOM   2365  C   LYS A1094     -51.564  52.736  -7.509  1.00 12.62           C  
ANISOU 2365  C   LYS A1094      380   1567   2847   -519   -208   1025       C  
ATOM   2366  O   LYS A1094     -50.591  53.153  -6.897  1.00 11.71           O  
ANISOU 2366  O   LYS A1094      338   1443   2668   -430   -124    939       O  
ATOM   2367  CB  LYS A1094     -50.704  51.375  -9.386  1.00 12.17           C  
ANISOU 2367  CB  LYS A1094      565   1344   2712   -593   -471    972       C  
ATOM   2368  CG  LYS A1094     -51.229  50.080  -8.776  1.00 13.22           C  
ANISOU 2368  CG  LYS A1094      741   1447   2831   -721   -530   1054       C  
ATOM   2369  CD  LYS A1094     -51.853  49.158  -9.798  1.00 18.61           C  
ANISOU 2369  CD  LYS A1094     1488   2054   3529   -847   -719   1125       C  
ATOM   2370  CE  LYS A1094     -52.345  47.858  -9.200  1.00 21.77           C  
ANISOU 2370  CE  LYS A1094     1963   2407   3898  -1003   -806   1218       C  
ATOM   2371  NZ  LYS A1094     -53.643  48.061  -8.519  1.00 26.46           N  
ANISOU 2371  NZ  LYS A1094     2339   3132   4582  -1118   -737   1360       N  
ATOM   2372  N   VAL A1095     -52.687  52.352  -6.944  1.00 13.91           N  
ANISOU 2372  N   VAL A1095      416   1807   3062   -602   -185   1137       N  
ATOM   2373  CA  VAL A1095     -52.889  52.411  -5.475  1.00 14.38           C  
ANISOU 2373  CA  VAL A1095      412   1952   3100   -583    -40   1163       C  
ATOM   2374  C   VAL A1095     -53.235  51.027  -4.959  1.00 15.35           C  
ANISOU 2374  C   VAL A1095      572   2067   3190   -747    -98   1252       C  
ATOM   2375  O   VAL A1095     -54.141  50.388  -5.492  1.00 18.08           O  
ANISOU 2375  O   VAL A1095      856   2433   3580   -888   -205   1362       O  
ATOM   2376  CB  VAL A1095     -53.969  53.429  -5.064  1.00 15.41           C  
ANISOU 2376  CB  VAL A1095      326   2229   3297   -507     73   1222       C  
ATOM   2377  CG1 VAL A1095     -54.118  53.463  -3.555  1.00 15.98           C  
ANISOU 2377  CG1 VAL A1095      348   2398   3326   -472    226   1242       C  
ATOM   2378  CG2 VAL A1095     -53.710  54.825  -5.602  1.00 14.71           C  
ANISOU 2378  CG2 VAL A1095      231   2124   3233   -349    102   1140       C  
ATOM   2379  N   ILE A1096     -52.548  50.635  -3.903  1.00 14.99           N  
ANISOU 2379  N   ILE A1096      632   1996   3065   -734    -32   1212       N  
ATOM   2380  CA  ILE A1096     -52.781  49.356  -3.211  1.00 15.97           C  
ANISOU 2380  CA  ILE A1096      824   2103   3139   -889    -81   1293       C  
ATOM   2381  C   ILE A1096     -53.148  49.648  -1.769  1.00 16.63           C  
ANISOU 2381  C   ILE A1096      803   2312   3202   -872     88   1336       C  
ATOM   2382  O   ILE A1096     -52.322  50.148  -0.983  1.00 16.33           O  
ANISOU 2382  O   ILE A1096      832   2259   3113   -746    199   1240       O  
ATOM   2383  CB  ILE A1096     -51.542  48.450  -3.331  1.00 15.08           C  
ANISOU 2383  CB  ILE A1096      975   1826   2928   -884   -188   1199       C  
ATOM   2384  CG1 ILE A1096     -51.152  48.201  -4.788  1.00 14.57           C  
ANISOU 2384  CG1 ILE A1096     1017   1655   2864   -870   -348   1148       C  
ATOM   2385  CG2 ILE A1096     -51.753  47.143  -2.594  1.00 16.21           C  
ANISOU 2385  CG2 ILE A1096     1228   1923   3006  -1041   -259   1279       C  
ATOM   2386  CD1 ILE A1096     -49.914  47.344  -4.953  1.00 13.92           C  
ANISOU 2386  CD1 ILE A1096     1185   1436   2667   -820   -451   1044       C  
ATOM   2387  N   THR A1097     -54.329  49.169  -1.361  1.00 21.26           N  
ANISOU 2387  N   THR A1097     1245   3023   3809  -1021     95   1488       N  
ATOM   2388  CA  THR A1097     -54.813  49.356   0.019  1.00 22.38           C  
ANISOU 2388  CA  THR A1097     1267   3320   3916  -1018    260   1548       C  
ATOM   2389  C   THR A1097     -54.817  48.046   0.795  1.00 23.30           C  
ANISOU 2389  C   THR A1097     1498   3402   3950  -1210    204   1631       C  
ATOM   2390  O   THR A1097     -55.001  48.083   2.005  1.00 28.54           O  
ANISOU 2390  O   THR A1097     2110   4172   4562  -1213    336   1669       O  
ATOM   2391  CB  THR A1097     -56.183  50.046   0.095  1.00 26.69           C  
ANISOU 2391  CB  THR A1097     1514   4100   4527  -1005    358   1660       C  
ATOM   2392  OG1 THR A1097     -57.075  49.367  -0.787  1.00 32.27           O  
ANISOU 2392  OG1 THR A1097     2133   4841   5288  -1194    209   1792       O  
ATOM   2393  CG2 THR A1097     -56.124  51.521  -0.242  1.00 26.11           C  
ANISOU 2393  CG2 THR A1097     1351   4062   4505   -766    452   1563       C  
ATOM   2394  N   GLU A1098     -54.550  46.959   0.093  1.00 25.15           N  
ANISOU 2394  N   GLU A1098     1912   3479   4164  -1351      4   1648       N  
ATOM   2395  CA  GLU A1098     -54.628  45.599   0.652  1.00 30.88           C  
ANISOU 2395  CA  GLU A1098     2789   4138   4804  -1563   -104   1741       C  
ATOM   2396  C   GLU A1098     -53.350  45.296   1.414  1.00 29.43           C  
ANISOU 2396  C   GLU A1098     2844   3814   4525  -1467    -83   1615       C  
ATOM   2397  O   GLU A1098     -52.321  45.929   1.123  1.00 27.12           O  
ANISOU 2397  O   GLU A1098     2627   3442   4233  -1265    -46   1457       O  
ATOM   2398  CB  GLU A1098     -54.881  44.583  -0.469  1.00 47.74           C  
ANISOU 2398  CB  GLU A1098     5055   6138   6944  -1737   -354   1805       C  
ATOM   2399  CG  GLU A1098     -53.698  44.362  -1.411  1.00 62.79           C  
ANISOU 2399  CG  GLU A1098     7212   7822   8822  -1607   -487   1646       C  
ATOM   2400  CD  GLU A1098     -54.029  44.267  -2.902  1.00 73.35           C  
ANISOU 2400  CD  GLU A1098     8558   9094  10216  -1643   -650   1660       C  
ATOM   2401  OE1 GLU A1098     -54.596  45.246  -3.455  1.00 55.11           O  
ANISOU 2401  OE1 GLU A1098     6025   6906   8007  -1581   -574   1675       O  
ATOM   2402  OE2 GLU A1098     -53.703  43.222  -3.523  1.00 62.45           O  
ANISOU 2402  OE2 GLU A1098     7425   7531   8772  -1721   -863   1651       O  
ATOM   2403  N   MET A1099     -53.397  44.318   2.316  1.00 33.30           N  
ANISOU 2403  N   MET A1099     3454   4271   4925  -1620   -123   1689       N  
ATOM   2404  CA  MET A1099     -52.201  43.917   3.093  1.00 33.92           C  
ANISOU 2404  CA  MET A1099     3773   4210   4902  -1536   -122   1576       C  
ATOM   2405  C   MET A1099     -51.280  43.065   2.221  1.00 31.25           C  
ANISOU 2405  C   MET A1099     3719   3641   4514  -1509   -339   1482       C  
ATOM   2406  O   MET A1099     -51.775  42.165   1.509  1.00 39.38           O  
ANISOU 2406  O   MET A1099     4843   4585   5534  -1675   -534   1567       O  
ATOM   2407  CB  MET A1099     -52.603  43.133   4.347  1.00 40.74           C  
ANISOU 2407  CB  MET A1099     4687   5113   5679  -1717   -105   1695       C  
ATOM   2408  CG  MET A1099     -53.419  43.948   5.351  1.00 54.17           C  
ANISOU 2408  CG  MET A1099     6118   7064   7398  -1712    127   1777       C  
ATOM   2409  SD  MET A1099     -54.707  42.982   6.227  1.00106.86           S  
ANISOU 2409  SD  MET A1099    12705  13894  14002  -2046    108   2027       S  
ATOM   2410  CE  MET A1099     -55.318  44.181   7.412  1.00 85.53           C  
ANISOU 2410  CE  MET A1099     9700  11497  11300  -1918    424   2057       C  
ATOM   2411  N   LEU A1100     -49.989  43.371   2.247  1.00 24.65           N  
ANISOU 2411  N   LEU A1100     3008   2718   3637  -1300   -310   1312       N  
ATOM   2412  CA  LEU A1100     -49.022  42.796   1.284  1.00 19.74           C  
ANISOU 2412  CA  LEU A1100     2613   1925   2963  -1204   -487   1196       C  
ATOM   2413  C   LEU A1100     -48.042  41.862   1.975  1.00 20.45           C  
ANISOU 2413  C   LEU A1100     2977   1870   2920  -1164   -575   1125       C  
ATOM   2414  O   LEU A1100     -47.601  42.138   3.108  1.00 18.43           O  
ANISOU 2414  O   LEU A1100     2717   1655   2627  -1108   -447   1092       O  
ATOM   2415  CB  LEU A1100     -48.252  43.924   0.600  1.00 15.77           C  
ANISOU 2415  CB  LEU A1100     2015   1469   2505   -984   -396   1059       C  
ATOM   2416  CG  LEU A1100     -49.052  44.790  -0.367  1.00 16.99           C  
ANISOU 2416  CG  LEU A1100     1954   1722   2779   -992   -358   1103       C  
ATOM   2417  CD1 LEU A1100     -48.129  45.753  -1.095  1.00 16.28           C  
ANISOU 2417  CD1 LEU A1100     1832   1649   2705   -793   -307    965       C  
ATOM   2418  CD2 LEU A1100     -49.816  43.951  -1.377  1.00 18.88           C  
ANISOU 2418  CD2 LEU A1100     2249   1887   3036  -1145   -552   1194       C  
ATOM   2419  N   SER A1101     -47.650  40.821   1.262  1.00 21.97           N  
ANISOU 2419  N   SER A1101     3418   1893   3035  -1165   -797   1090       N  
ATOM   2420  CA  SER A1101     -46.613  39.889   1.738  1.00 22.62           C  
ANISOU 2420  CA  SER A1101     3795   1823   2977  -1080   -915    998       C  
ATOM   2421  C   SER A1101     -45.304  40.647   1.896  1.00 16.60           C  
ANISOU 2421  C   SER A1101     2998   1118   2191   -820   -792    830       C  
ATOM   2422  O   SER A1101     -44.986  41.526   1.065  1.00 15.43           O  
ANISOU 2422  O   SER A1101     2706   1056   2101   -691   -722    759       O  
ATOM   2423  CB  SER A1101     -46.506  38.710   0.803  1.00 29.14           C  
ANISOU 2423  CB  SER A1101     4897   2456   3716  -1100  -1187    985       C  
ATOM   2424  OG  SER A1101     -45.505  37.813   1.245  1.00 46.13           O  
ANISOU 2424  OG  SER A1101     7346   4460   5722   -986  -1313    888       O  
ATOM   2425  N   ARG A1102     -44.575  40.325   2.960  1.00 18.34           N  
ANISOU 2425  N   ARG A1102     3346   1297   2322   -761   -770    779       N  
ATOM   2426  CA  ARG A1102     -43.263  40.943   3.218  1.00 15.25           C  
ANISOU 2426  CA  ARG A1102     2937    965   1891   -531   -674    630       C  
ATOM   2427  C   ARG A1102     -42.378  40.723   2.004  1.00 14.82           C  
ANISOU 2427  C   ARG A1102     2975    877   1778   -346   -797    507       C  
ATOM   2428  O   ARG A1102     -41.590  41.611   1.645  1.00 13.60           O  
ANISOU 2428  O   ARG A1102     2689    840   1636   -187   -698    413       O  
ATOM   2429  CB  ARG A1102     -42.605  40.341   4.464  1.00 16.20           C  
ANISOU 2429  CB  ARG A1102     3237   1014   1904   -502   -691    596       C  
ATOM   2430  CG  ARG A1102     -41.382  41.126   4.911  1.00 16.38           C  
ANISOU 2430  CG  ARG A1102     3194   1131   1899   -302   -566    470       C  
ATOM   2431  CD  ARG A1102     -40.749  40.688   6.217  1.00 16.03           C  
ANISOU 2431  CD  ARG A1102     3299   1032   1759   -272   -563    440       C  
ATOM   2432  NE  ARG A1102     -40.274  39.321   6.131  1.00 17.89           N  
ANISOU 2432  NE  ARG A1102     3833   1100   1863   -223   -786    396       N  
ATOM   2433  CZ  ARG A1102     -39.398  38.769   6.957  1.00 19.08           C  
ANISOU 2433  CZ  ARG A1102     4165   1183   1900   -124   -844    327       C  
ATOM   2434  NH1 ARG A1102     -38.870  39.477   7.945  1.00 18.48           N  
ANISOU 2434  NH1 ARG A1102     3994   1196   1828    -76   -691    296       N  
ATOM   2435  NH2 ARG A1102     -39.058  37.502   6.785  1.00 22.12           N  
ANISOU 2435  NH2 ARG A1102     4845   1399   2159    -69  -1069    288       N  
ATOM   2436  N   GLU A1103     -42.512  39.547   1.409  1.00 16.05           N  
ANISOU 2436  N   GLU A1103     3364    877   1856   -371  -1017    514       N  
ATOM   2437  CA  GLU A1103     -41.702  39.167   0.245  1.00 16.07           C  
ANISOU 2437  CA  GLU A1103     3493    839   1771   -176  -1156    394       C  
ATOM   2438  C   GLU A1103     -42.064  40.019  -0.953  1.00 15.30           C  
ANISOU 2438  C   GLU A1103     3192    846   1773   -170  -1097    402       C  
ATOM   2439  O   GLU A1103     -41.185  40.292  -1.801  1.00 14.72           O  
ANISOU 2439  O   GLU A1103     3102    842   1648     23  -1106    288       O  
ATOM   2440  CB  GLU A1103     -41.891  37.694  -0.112  1.00 24.41           C  
ANISOU 2440  CB  GLU A1103     4885   1676   2712   -210  -1427    407       C  
ATOM   2441  CG  GLU A1103     -41.248  36.739   0.877  1.00 38.00           C  
ANISOU 2441  CG  GLU A1103     6872   3269   4294   -150  -1532    361       C  
ATOM   2442  CD  GLU A1103     -42.037  36.497   2.152  1.00 46.09           C  
ANISOU 2442  CD  GLU A1103     7915   4243   5352   -396  -1495    497       C  
ATOM   2443  OE1 GLU A1103     -43.167  37.031   2.267  1.00 76.84           O  
ANISOU 2443  OE1 GLU A1103    11602   8216   9374   -616  -1386    636       O  
ATOM   2444  OE2 GLU A1103     -41.513  35.768   3.028  1.00 49.29           O  
ANISOU 2444  OE2 GLU A1103     8539   4542   5645   -357  -1576    465       O  
ATOM   2445  N   PHE A1104     -43.329  40.418  -1.044  1.00 15.44           N  
ANISOU 2445  N   PHE A1104     3055    889   1920   -377  -1044    536       N  
ATOM   2446  CA  PHE A1104     -43.811  41.213  -2.194  1.00 14.86           C  
ANISOU 2446  CA  PHE A1104     2797    901   1948   -388  -1004    556       C  
ATOM   2447  C   PHE A1104     -43.309  42.642  -2.080  1.00 13.28           C  
ANISOU 2447  C   PHE A1104     2351    880   1814   -284   -790    500       C  
ATOM   2448  O   PHE A1104     -42.994  43.275  -3.098  1.00 12.59           O  
ANISOU 2448  O   PHE A1104     2172    866   1745   -192   -773    447       O  
ATOM   2449  CB  PHE A1104     -45.333  41.193  -2.254  1.00 15.71           C  
ANISOU 2449  CB  PHE A1104     2803    997   2168   -635  -1017    722       C  
ATOM   2450  CG  PHE A1104     -45.878  41.906  -3.457  1.00 16.53           C  
ANISOU 2450  CG  PHE A1104     2741   1168   2370   -649  -1004    746       C  
ATOM   2451  CD1 PHE A1104     -45.421  41.586  -4.730  1.00 16.90           C  
ANISOU 2451  CD1 PHE A1104     2910   1153   2358   -539  -1143    669       C  
ATOM   2452  CD2 PHE A1104     -46.832  42.899  -3.310  1.00 18.43           C  
ANISOU 2452  CD2 PHE A1104     2714   1538   2750   -753   -856    842       C  
ATOM   2453  CE1 PHE A1104     -45.916  42.240  -5.844  1.00 17.36           C  
ANISOU 2453  CE1 PHE A1104     2827   1267   2502   -557  -1137    692       C  
ATOM   2454  CE2 PHE A1104     -47.337  43.550  -4.425  1.00 20.41           C  
ANISOU 2454  CE2 PHE A1104     2825   1840   3087   -760   -858    863       C  
ATOM   2455  CZ  PHE A1104     -46.872  43.223  -5.688  1.00 20.56           C  
ANISOU 2455  CZ  PHE A1104     2969   1786   3053   -672   -999    790       C  
ATOM   2456  N   VAL A1105     -43.211  43.126  -0.850  1.00 12.85           N  
ANISOU 2456  N   VAL A1105     2214    886   1780   -302   -642    514       N  
ATOM   2457  CA  VAL A1105     -42.702  44.483  -0.617  1.00 11.53           C  
ANISOU 2457  CA  VAL A1105     1853    866   1660   -213   -458    465       C  
ATOM   2458  C   VAL A1105     -41.207  44.519  -0.946  1.00 10.92           C  
ANISOU 2458  C   VAL A1105     1840    835   1471    -13   -483    326       C  
ATOM   2459  O   VAL A1105     -40.682  45.528  -1.439  1.00 10.02           O  
ANISOU 2459  O   VAL A1105     1590    842   1375     62   -401    279       O  
ATOM   2460  CB  VAL A1105     -43.041  44.944   0.797  1.00 11.45           C  
ANISOU 2460  CB  VAL A1105     1765    897   1688   -282   -308    518       C  
ATOM   2461  CG1 VAL A1105     -42.388  46.274   1.108  1.00 10.28           C  
ANISOU 2461  CG1 VAL A1105     1475    867   1560   -182   -149    458       C  
ATOM   2462  CG2 VAL A1105     -44.551  45.021   0.946  1.00 12.25           C  
ANISOU 2462  CG2 VAL A1105     1750   1011   1893   -462   -271    661       C  
ATOM   2463  N   ARG A1106     -40.534  43.430  -0.675  1.00 11.57           N  
ANISOU 2463  N   ARG A1106     2130    834   1431     66   -602    267       N  
ATOM   2464  CA  ARG A1106     -39.109  43.287  -1.038  1.00 11.37           C  
ANISOU 2464  CA  ARG A1106     2167    876   1276    279   -646    135       C  
ATOM   2465  C   ARG A1106     -38.987  43.321  -2.546  1.00 11.43           C  
ANISOU 2465  C   ARG A1106     2156    923   1261    356   -723     96       C  
ATOM   2466  O   ARG A1106     -38.047  43.946  -3.051  1.00 10.88           O  
ANISOU 2466  O   ARG A1106     1985   1006   1140    485   -672     22       O  
ATOM   2467  CB  ARG A1106     -38.611  41.938  -0.513  1.00 12.45           C  
ANISOU 2467  CB  ARG A1106     2565    885   1277    360   -794     85       C  
ATOM   2468  CG  ARG A1106     -37.159  41.631  -0.861  1.00 12.62           C  
ANISOU 2468  CG  ARG A1106     2659    990   1144    611   -855    -53       C  
ATOM   2469  CD  ARG A1106     -36.630  40.344  -0.243  1.00 13.80           C  
ANISOU 2469  CD  ARG A1106     3080   1010   1151    720  -1006   -112       C  
ATOM   2470  NE  ARG A1106     -37.452  39.195  -0.622  1.00 15.09           N  
ANISOU 2470  NE  ARG A1106     3484    959   1288    643  -1197    -67       N  
ATOM   2471  CZ  ARG A1106     -37.293  37.962  -0.158  1.00 16.42           C  
ANISOU 2471  CZ  ARG A1106     3946    953   1338    689  -1372    -93       C  
ATOM   2472  NH1 ARG A1106     -36.328  37.703   0.714  1.00 16.59           N  
ANISOU 2472  NH1 ARG A1106     4045    996   1260    831  -1371   -170       N  
ATOM   2473  NH2 ARG A1106     -38.097  36.993  -0.570  1.00 17.71           N  
ANISOU 2473  NH2 ARG A1106     4337    914   1476    587  -1560    -37       N  
ATOM   2474  N   GLU A1107     -39.904  42.669  -3.247  1.00 12.21           N  
ANISOU 2474  N   GLU A1107     2350    898   1389    268   -848    153       N  
ATOM   2475  CA  GLU A1107     -39.922  42.673  -4.721  1.00 12.37           C  
ANISOU 2475  CA  GLU A1107     2371    938   1391    327   -932    124       C  
ATOM   2476  C   GLU A1107     -40.084  44.103  -5.226  1.00 11.23           C  
ANISOU 2476  C   GLU A1107     1967    944   1354    285   -782    150       C  
ATOM   2477  O   GLU A1107     -39.388  44.520  -6.165  1.00 10.95           O  
ANISOU 2477  O   GLU A1107     1873   1023   1261    400   -778     85       O  
ATOM   2478  CB  GLU A1107     -41.084  41.803  -5.184  1.00 13.47           C  
ANISOU 2478  CB  GLU A1107     2654    898   1564    185  -1090    211       C  
ATOM   2479  CG  GLU A1107     -40.991  41.459  -6.650  1.00 18.57           C  
ANISOU 2479  CG  GLU A1107     3390   1517   2147    274  -1227    164       C  
ATOM   2480  CD  GLU A1107     -40.326  40.125  -6.886  1.00 32.25           C  
ANISOU 2480  CD  GLU A1107     5430   3126   3695    440  -1427     72       C  
ATOM   2481  OE1 GLU A1107     -41.044  39.113  -6.761  1.00 63.08           O  
ANISOU 2481  OE1 GLU A1107     9552   6830   7583    326  -1595    134       O  
ATOM   2482  OE2 GLU A1107     -39.098  40.098  -7.167  1.00 61.11           O  
ANISOU 2482  OE2 GLU A1107     9110   6891   7215    680  -1421    -55       O  
ATOM   2483  N   LEU A1108     -41.004  44.833  -4.610  1.00 10.76           N  
ANISOU 2483  N   LEU A1108     1763    889   1436    125   -667    247       N  
ATOM   2484  CA  LEU A1108     -41.285  46.227  -5.001  1.00  9.85           C  
ANISOU 2484  CA  LEU A1108     1429    888   1425     82   -538    278       C  
ATOM   2485  C   LEU A1108     -40.044  47.070  -4.843  1.00  9.04           C  
ANISOU 2485  C   LEU A1108     1242    935   1257    197   -439    198       C  
ATOM   2486  O   LEU A1108     -39.608  47.700  -5.812  1.00  8.71           O  
ANISOU 2486  O   LEU A1108     1121    994   1193    246   -432    166       O  
ATOM   2487  CB  LEU A1108     -42.369  46.831  -4.109  1.00  9.72           C  
ANISOU 2487  CB  LEU A1108     1289    862   1542    -62   -424    381       C  
ATOM   2488  CG  LEU A1108     -43.758  46.227  -4.240  1.00 10.66           C  
ANISOU 2488  CG  LEU A1108     1423    885   1743   -217   -499    494       C  
ATOM   2489  CD1 LEU A1108     -44.694  46.804  -3.199  1.00 10.76           C  
ANISOU 2489  CD1 LEU A1108     1295    936   1856   -327   -365    588       C  
ATOM   2490  CD2 LEU A1108     -44.309  46.462  -5.623  1.00 10.77           C  
ANISOU 2490  CD2 LEU A1108     1382    898   1812   -247   -571    520       C  
ATOM   2491  N   TYR A1109     -39.520  47.107  -3.625  1.00  8.84           N  
ANISOU 2491  N   TYR A1109     1231    927   1198    221   -367    177       N  
ATOM   2492  CA  TYR A1109     -38.252  47.802  -3.316  1.00  8.28           C  
ANISOU 2492  CA  TYR A1109     1094   1000   1049    317   -291    109       C  
ATOM   2493  C   TYR A1109     -37.190  47.460  -4.355  1.00  8.58           C  
ANISOU 2493  C   TYR A1109     1159   1147    954    463   -372     23       C  
ATOM   2494  O   TYR A1109     -36.502  48.347  -4.878  1.00  8.21           O  
ANISOU 2494  O   TYR A1109      990   1257    872    490   -320      2       O  
ATOM   2495  CB  TYR A1109     -37.691  47.416  -1.948  1.00  8.36           C  
ANISOU 2495  CB  TYR A1109     1181    991   1002    352   -259     81       C  
ATOM   2496  CG  TYR A1109     -38.411  47.982  -0.751  1.00  8.06           C  
ANISOU 2496  CG  TYR A1109     1096    902   1061    238   -145    150       C  
ATOM   2497  CD1 TYR A1109     -38.886  49.285  -0.736  1.00  7.49           C  
ANISOU 2497  CD1 TYR A1109      882    878   1084    167    -34    197       C  
ATOM   2498  CD2 TYR A1109     -38.579  47.228   0.402  1.00  8.49           C  
ANISOU 2498  CD2 TYR A1109     1265    864   1096    215   -150    165       C  
ATOM   2499  CE1 TYR A1109     -39.517  49.816   0.379  1.00  7.42           C  
ANISOU 2499  CE1 TYR A1109      840    835   1141     98     72    250       C  
ATOM   2500  CE2 TYR A1109     -39.236  47.731   1.514  1.00  8.38           C  
ANISOU 2500  CE2 TYR A1109     1207    823   1153    123    -36    227       C  
ATOM   2501  CZ  TYR A1109     -39.706  49.031   1.502  1.00  7.87           C  
ANISOU 2501  CZ  TYR A1109      994    817   1176     77     78    266       C  
ATOM   2502  OH  TYR A1109     -40.352  49.535   2.588  1.00  7.96           O  
ANISOU 2502  OH  TYR A1109      970    813   1238     18    191    319       O  
ATOM   2503  N   GLY A1110     -37.070  46.179  -4.679  1.00  9.45           N  
ANISOU 2503  N   GLY A1110     1437   1177    975    557   -506    -21       N  
ATOM   2504  CA  GLY A1110     -36.015  45.715  -5.577  1.00 10.05           C  
ANISOU 2504  CA  GLY A1110     1557   1367    892    743   -587   -116       C  
ATOM   2505  C   GLY A1110     -36.337  45.855  -7.043  1.00 10.23           C  
ANISOU 2505  C   GLY A1110     1552   1417    917    747   -640   -111       C  
ATOM   2506  O   GLY A1110     -35.523  45.445  -7.879  1.00 10.91           O  
ANISOU 2506  O   GLY A1110     1677   1609    858    914   -707   -190       O  
ATOM   2507  N   SER A1111     -37.490  46.419  -7.354  1.00  9.77           N  
ANISOU 2507  N   SER A1111     1425   1277   1008    582   -613    -23       N  
ATOM   2508  CA  SER A1111     -37.920  46.613  -8.759  1.00  9.93           C  
ANISOU 2508  CA  SER A1111     1421   1306   1045    564   -669     -8       C  
ATOM   2509  C   SER A1111     -38.035  48.080  -9.145  1.00  9.08           C  
ANISOU 2509  C   SER A1111     1114   1314   1021    467   -556     38       C  
ATOM   2510  O   SER A1111     -37.505  48.482 -10.210  1.00  9.18           O  
ANISOU 2510  O   SER A1111     1069   1458    961    519   -565     10       O  
ATOM   2511  CB  SER A1111     -39.217  45.953  -9.058  1.00 10.42           C  
ANISOU 2511  CB  SER A1111     1590   1170   1197    457   -774     58       C  
ATOM   2512  OG  SER A1111     -39.055  44.556  -8.994  1.00 11.48           O  
ANISOU 2512  OG  SER A1111     1954   1184   1224    550   -921     11       O  
ATOM   2513  N   VAL A1112     -38.658  48.866  -8.282  1.00  8.42           N  
ANISOU 2513  N   VAL A1112      938   1190   1068    339   -456    106       N  
ATOM   2514  CA  VAL A1112     -38.876  50.305  -8.582  1.00  7.77           C  
ANISOU 2514  CA  VAL A1112      702   1182   1067    247   -367    154       C  
ATOM   2515  C   VAL A1112     -37.549  51.018  -8.603  1.00  7.56           C  
ANISOU 2515  C   VAL A1112      598   1346    927    301   -309    108       C  
ATOM   2516  O   VAL A1112     -36.637  50.521  -7.945  1.00  7.74           O  
ANISOU 2516  O   VAL A1112      658   1433    849    392   -302     54       O  
ATOM   2517  CB  VAL A1112     -39.786  51.024  -7.584  1.00  7.33           C  
ANISOU 2517  CB  VAL A1112      582   1049   1153    135   -274    226       C  
ATOM   2518  CG1 VAL A1112     -41.169  50.412  -7.603  1.00  7.75           C  
ANISOU 2518  CG1 VAL A1112      669    958   1318     57   -325    294       C  
ATOM   2519  CG2 VAL A1112     -39.187  51.046  -6.182  1.00  7.10           C  
ANISOU 2519  CG2 VAL A1112      569   1040   1089    160   -196    203       C  
ATOM   2520  N   ASP A1113     -37.532  52.192  -9.239  1.00  7.28           N  
ANISOU 2520  N   ASP A1113      460   1389    914    228   -273    142       N  
ATOM   2521  CA  ASP A1113     -36.321  53.014  -9.368  1.00  7.27           C  
ANISOU 2521  CA  ASP A1113      373   1586    802    231   -230    125       C  
ATOM   2522  C   ASP A1113     -36.101  53.827  -8.107  1.00  6.84           C  
ANISOU 2522  C   ASP A1113      287   1529    781    165   -144    150       C  
ATOM   2523  O   ASP A1113     -34.990  53.851  -7.596  1.00  7.00           O  
ANISOU 2523  O   ASP A1113      282   1682    692    203   -120    119       O  
ATOM   2524  CB  ASP A1113     -36.405  53.938 -10.583  1.00  7.34           C  
ANISOU 2524  CB  ASP A1113      312   1666    807    155   -247    163       C  
ATOM   2525  CG  ASP A1113     -36.480  53.201 -11.904  1.00  7.88           C  
ANISOU 2525  CG  ASP A1113      417   1760    815    227   -333    134       C  
ATOM   2526  OD1 ASP A1113     -35.702  52.254 -12.080  1.00  8.46           O  
ANISOU 2526  OD1 ASP A1113      531   1927    753    366   -369     66       O  
ATOM   2527  OD2 ASP A1113     -37.337  53.564 -12.732  1.00  7.82           O  
ANISOU 2527  OD2 ASP A1113      409   1672    890    158   -370    176       O  
ATOM   2528  N   PHE A1114     -37.149  54.496  -7.640  1.00  6.45           N  
ANISOU 2528  N   PHE A1114      238   1340    872     77   -103    205       N  
ATOM   2529  CA  PHE A1114     -37.065  55.364  -6.461  1.00  6.17           C  
ANISOU 2529  CA  PHE A1114      198   1279    867     23    -27    227       C  
ATOM   2530  C   PHE A1114     -38.141  55.036  -5.437  1.00  6.03           C  
ANISOU 2530  C   PHE A1114      223   1101    966     24     17    249       C  
ATOM   2531  O   PHE A1114     -39.214  54.522  -5.772  1.00  6.16           O  
ANISOU 2531  O   PHE A1114      245   1021   1072     18     -8    276       O  
ATOM   2532  CB  PHE A1114     -37.222  56.810  -6.903  1.00  6.14           C  
ANISOU 2532  CB  PHE A1114      156   1285    891    -75    -21    276       C  
ATOM   2533  CG  PHE A1114     -36.172  57.232  -7.892  1.00  6.46           C  
ANISOU 2533  CG  PHE A1114      144   1502    805   -110    -63    275       C  
ATOM   2534  CD1 PHE A1114     -34.927  57.665  -7.460  1.00  6.70           C  
ANISOU 2534  CD1 PHE A1114      148   1682    713   -143    -49    271       C  
ATOM   2535  CD2 PHE A1114     -36.428  57.166  -9.254  1.00  6.66           C  
ANISOU 2535  CD2 PHE A1114      143   1560    825   -119   -120    284       C  
ATOM   2536  CE1 PHE A1114     -33.966  58.046  -8.381  1.00  7.23           C  
ANISOU 2536  CE1 PHE A1114      144   1951    650   -193    -86    286       C  
ATOM   2537  CE2 PHE A1114     -35.464  57.532 -10.177  1.00  7.12           C  
ANISOU 2537  CE2 PHE A1114      145   1807    752   -155   -152    289       C  
ATOM   2538  CZ  PHE A1114     -34.240  57.980  -9.740  1.00  7.45           C  
ANISOU 2538  CZ  PHE A1114      142   2019    668   -197   -132    294       C  
ATOM   2539  N   VAL A1115     -37.832  55.329  -4.194  1.00  5.91           N  
ANISOU 2539  N   VAL A1115      235   1073    937     22     81    244       N  
ATOM   2540  CA  VAL A1115     -38.809  55.228  -3.094  1.00  5.93           C  
ANISOU 2540  CA  VAL A1115      268    952   1031     18    144    272       C  
ATOM   2541  C   VAL A1115     -38.965  56.584  -2.474  1.00  5.90           C  
ANISOU 2541  C   VAL A1115      265    923   1054    -17    207    298       C  
ATOM   2542  O   VAL A1115     -37.953  57.161  -2.035  1.00  5.85           O  
ANISOU 2542  O   VAL A1115      286    974    961    -31    214    278       O  
ATOM   2543  CB  VAL A1115     -38.418  54.149  -2.079  1.00  6.01           C  
ANISOU 2543  CB  VAL A1115      346    943    992     67    156    240       C  
ATOM   2544  CG1 VAL A1115     -39.108  54.374  -0.756  1.00  6.10           C  
ANISOU 2544  CG1 VAL A1115      385    870   1061     51    243    270       C  
ATOM   2545  CG2 VAL A1115     -38.754  52.767  -2.623  1.00  6.30           C  
ANISOU 2545  CG2 VAL A1115      424    940   1030     99     78    230       C  
ATOM   2546  N   ILE A1116     -40.213  57.033  -2.390  1.00  6.12           N  
ANISOU 2546  N   ILE A1116      270    867   1188    -23    242    341       N  
ATOM   2547  CA  ILE A1116     -40.562  58.339  -1.780  1.00  6.36           C  
ANISOU 2547  CA  ILE A1116      326    848   1239    -22    294    359       C  
ATOM   2548  C   ILE A1116     -40.895  58.117  -0.325  1.00  6.58           C  
ANISOU 2548  C   ILE A1116      394    830   1273     20    382    359       C  
ATOM   2549  O   ILE A1116     -41.732  57.266  -0.011  1.00  6.81           O  
ANISOU 2549  O   ILE A1116      387    839   1361     34    416    383       O  
ATOM   2550  CB  ILE A1116     -41.775  59.013  -2.450  1.00  6.73           C  
ANISOU 2550  CB  ILE A1116      323    848   1386    -15    285    401       C  
ATOM   2551  CG1 ILE A1116     -41.793  58.915  -3.977  1.00  6.60           C  
ANISOU 2551  CG1 ILE A1116      257    862   1386    -57    196    412       C  
ATOM   2552  CG2 ILE A1116     -41.907  60.455  -1.987  1.00  7.14           C  
ANISOU 2552  CG2 ILE A1116      440    846   1425      7    307    405       C  
ATOM   2553  CD1 ILE A1116     -40.739  59.731  -4.656  1.00  6.46           C  
ANISOU 2553  CD1 ILE A1116      274    899   1279   -112    137    398       C  
ATOM   2554  N   ILE A1117     -40.331  58.953   0.537  1.00  6.67           N  
ANISOU 2554  N   ILE A1117      485    823   1222     29    413    341       N  
ATOM   2555  CA  ILE A1117     -40.492  58.789   2.011  1.00  6.93           C  
ANISOU 2555  CA  ILE A1117      578    816   1237     74    499    334       C  
ATOM   2556  C   ILE A1117     -40.668  60.190   2.578  1.00  7.44           C  
ANISOU 2556  C   ILE A1117      726    818   1280    110    527    334       C  
ATOM   2557  O   ILE A1117     -39.796  60.714   3.274  1.00  7.47           O  
ANISOU 2557  O   ILE A1117      835    804   1197     96    519    311       O  
ATOM   2558  CB  ILE A1117     -39.256  58.116   2.646  1.00  6.58           C  
ANISOU 2558  CB  ILE A1117      590    809   1098     57    486    296       C  
ATOM   2559  CG1 ILE A1117     -38.698  56.965   1.807  1.00  6.20           C  
ANISOU 2559  CG1 ILE A1117      493    830   1031     41    417    277       C  
ATOM   2560  CG2 ILE A1117     -39.563  57.660   4.058  1.00  6.86           C  
ANISOU 2560  CG2 ILE A1117      682    800   1125     96    569    294       C  
ATOM   2561  CD1 ILE A1117     -37.529  56.257   2.439  1.00  6.06           C  
ANISOU 2561  CD1 ILE A1117      527    860    914     56    399    234       C  
ATOM   2562  N   PRO A1118     -41.806  60.841   2.304  1.00  8.01           N  
ANISOU 2562  N   PRO A1118      766    853   1421    165    548    360       N  
ATOM   2563  CA  PRO A1118     -42.017  62.251   2.657  1.00  8.71           C  
ANISOU 2563  CA  PRO A1118      963    867   1478    225    547    352       C  
ATOM   2564  C   PRO A1118     -42.563  62.487   4.076  1.00  9.48           C  
ANISOU 2564  C   PRO A1118     1128    925   1549    335    650    342       C  
ATOM   2565  O   PRO A1118     -43.484  63.289   4.305  1.00 10.44           O  
ANISOU 2565  O   PRO A1118     1273   1008   1683    450    685    345       O  
ATOM   2566  CB  PRO A1118     -43.056  62.648   1.620  1.00  9.09           C  
ANISOU 2566  CB  PRO A1118      928    911   1613    259    518    381       C  
ATOM   2567  CG  PRO A1118     -43.927  61.406   1.530  1.00  9.03           C  
ANISOU 2567  CG  PRO A1118      765    972   1693    265    576    414       C  
ATOM   2568  CD  PRO A1118     -42.973  60.234   1.664  1.00  8.20           C  
ANISOU 2568  CD  PRO A1118      658    906   1550    180    564    399       C  
ATOM   2569  N   SER A1119     -41.980  61.786   5.034  1.00  9.20           N  
ANISOU 2569  N   SER A1119     1128    903   1462    314    696    326       N  
ATOM   2570  CA  SER A1119     -42.401  61.860   6.453  1.00  9.94           C  
ANISOU 2570  CA  SER A1119     1289    971   1514    409    801    317       C  
ATOM   2571  C   SER A1119     -42.359  63.287   7.006  1.00 10.80           C  
ANISOU 2571  C   SER A1119     1572    984   1546    498    787    288       C  
ATOM   2572  O   SER A1119     -41.482  64.095   6.611  1.00 10.63           O  
ANISOU 2572  O   SER A1119     1668    901   1469    433    679    273       O  
ATOM   2573  CB  SER A1119     -41.582  60.928   7.278  1.00  9.43           C  
ANISOU 2573  CB  SER A1119     1262    924   1397    353    823    303       C  
ATOM   2574  OG  SER A1119     -41.695  59.621   6.768  1.00  8.89           O  
ANISOU 2574  OG  SER A1119     1068    921   1386    288    817    326       O  
ATOM   2575  N   TYR A1120     -43.222  63.544   7.993  1.00 11.86           N  
ANISOU 2575  N   TYR A1120     1738   1110   1658    639    890    283       N  
ATOM   2576  CA  TYR A1120     -43.052  64.679   8.939  1.00 12.85           C  
ANISOU 2576  CA  TYR A1120     2079   1129   1672    746    889    243       C  
ATOM   2577  C   TYR A1120     -42.236  64.180  10.119  1.00 12.59           C  
ANISOU 2577  C   TYR A1120     2143   1079   1558    703    926    224       C  
ATOM   2578  O   TYR A1120     -41.084  64.663  10.368  1.00 12.34           O  
ANISOU 2578  O   TYR A1120     2277    967   1443    625    834    201       O  
ATOM   2579  CB  TYR A1120     -44.427  65.136   9.426  1.00 14.35           C  
ANISOU 2579  CB  TYR A1120     2242   1346   1861    953    993    242       C  
ATOM   2580  CG  TYR A1120     -45.250  65.835   8.375  1.00 14.92           C  
ANISOU 2580  CG  TYR A1120     2252   1419   1995   1031    944    252       C  
ATOM   2581  CD1 TYR A1120     -45.032  67.172   8.107  1.00 15.59           C  
ANISOU 2581  CD1 TYR A1120     2537   1368   2017   1095    831    216       C  
ATOM   2582  CD2 TYR A1120     -46.226  65.177   7.641  1.00 14.90           C  
ANISOU 2582  CD2 TYR A1120     2010   1542   2108   1032    990    301       C  
ATOM   2583  CE1 TYR A1120     -45.756  67.851   7.148  1.00 16.21           C  
ANISOU 2583  CE1 TYR A1120     2583   1431   2144   1173    770    222       C  
ATOM   2584  CE2 TYR A1120     -46.955  65.843   6.669  1.00 15.48           C  
ANISOU 2584  CE2 TYR A1120     2031   1613   2236   1107    934    309       C  
ATOM   2585  CZ  TYR A1120     -46.716  67.184   6.421  1.00 16.11           C  
ANISOU 2585  CZ  TYR A1120     2316   1553   2252   1184    826    267       C  
ATOM   2586  OH  TYR A1120     -47.416  67.882   5.482  1.00 16.79           O  
ANISOU 2586  OH  TYR A1120     2376   1621   2382   1267    756    271       O  
ATOM   2587  N   PHE A1121     -42.715  63.071  10.699  1.00 12.54           N  
ANISOU 2587  N   PHE A1121     2018   1163   1582    711   1039    246       N  
ATOM   2588  CA  PHE A1121     -42.061  62.420  11.838  1.00 12.55           C  
ANISOU 2588  CA  PHE A1121     2098   1157   1513    672   1082    234       C  
ATOM   2589  C   PHE A1121     -41.670  60.993  11.480  1.00 12.47           C  
ANISOU 2589  C   PHE A1121     1957   1219   1560    540   1069    260       C  
ATOM   2590  O   PHE A1121     -42.524  60.162  11.278  1.00 12.89           O  
ANISOU 2590  O   PHE A1121     1862   1353   1682    533   1130    302       O  
ATOM   2591  CB  PHE A1121     -42.998  62.396  13.052  1.00 18.68           C  
ANISOU 2591  CB  PHE A1121     2892   1964   2240    811   1226    238       C  
ATOM   2592  CG  PHE A1121     -43.008  63.634  13.916  1.00 36.46           C  
ANISOU 2592  CG  PHE A1121     5358   4117   4376    959   1236    191       C  
ATOM   2593  CD1 PHE A1121     -43.631  64.803  13.497  1.00 40.45           C  
ANISOU 2593  CD1 PHE A1121     5916   4578   4872   1098   1209    172       C  
ATOM   2594  CD2 PHE A1121     -42.459  63.610  15.194  1.00 73.18           C  
ANISOU 2594  CD2 PHE A1121    10177   8710   8916    976   1268    164       C  
ATOM   2595  CE1 PHE A1121     -43.672  65.925  14.320  1.00 42.44           C  
ANISOU 2595  CE1 PHE A1121     6402   4721   4999   1256   1204    122       C  
ATOM   2596  CE2 PHE A1121     -42.499  64.733  16.016  1.00 72.74           C  
ANISOU 2596  CE2 PHE A1121    10346   8550   8739   1123   1269    117       C  
ATOM   2597  CZ  PHE A1121     -43.108  65.889  15.578  1.00 52.22           C  
ANISOU 2597  CZ  PHE A1121     7815   5899   6125   1269   1234     94       C  
ATOM   2598  N   GLU A1122     -40.370  60.740  11.447  1.00 10.99           N  
ANISOU 2598  N   GLU A1122     1839   1006   1330    440    981    236       N  
ATOM   2599  CA  GLU A1122     -39.810  59.392  11.231  1.00 10.81           C  
ANISOU 2599  CA  GLU A1122     1739   1039   1329    345    952    243       C  
ATOM   2600  C   GLU A1122     -38.583  59.231  12.116  1.00  9.37           C  
ANISOU 2600  C   GLU A1122     1689    822   1048    308    914    210       C  
ATOM   2601  O   GLU A1122     -37.504  59.646  11.733  1.00  8.98           O  
ANISOU 2601  O   GLU A1122     1680    773    956    249    816    191       O  
ATOM   2602  CB  GLU A1122     -39.441  59.228   9.752  1.00 20.88           C  
ANISOU 2602  CB  GLU A1122     2908   2362   2664    273    853    248       C  
ATOM   2603  CG  GLU A1122     -38.816  57.889   9.396  1.00 34.98           C  
ANISOU 2603  CG  GLU A1122     4633   4201   4454    208    803    243       C  
ATOM   2604  CD  GLU A1122     -39.741  56.702   9.584  1.00 64.32           C  
ANISOU 2604  CD  GLU A1122     8282   7934   8223    207    858    279       C  
ATOM   2605  OE1 GLU A1122     -40.326  56.254   8.567  1.00 43.00           O  
ANISOU 2605  OE1 GLU A1122     5471   5268   5599    181    829    307       O  
ATOM   2606  OE2 GLU A1122     -39.859  56.220  10.741  1.00 83.16           O  
ANISOU 2606  OE2 GLU A1122    10734  10297  10564    218    919    284       O  
ATOM   2607  N   PRO A1123     -38.711  58.672  13.331  1.00  9.78           N  
ANISOU 2607  N   PRO A1123     1809    853   1052    335    987    208       N  
ATOM   2608  CA  PRO A1123     -37.577  58.576  14.240  1.00  9.69           C  
ANISOU 2608  CA  PRO A1123     1935    803    944    307    946    177       C  
ATOM   2609  C   PRO A1123     -36.576  57.468  13.897  1.00  8.94           C  
ANISOU 2609  C   PRO A1123     1796    759    841    236    861    163       C  
ATOM   2610  O   PRO A1123     -35.466  57.456  14.452  1.00  8.87           O  
ANISOU 2610  O   PRO A1123     1876    741    751    211    802    136       O  
ATOM   2611  CB  PRO A1123     -38.282  58.327  15.585  1.00 10.54           C  
ANISOU 2611  CB  PRO A1123     2120    876   1006    371   1065    186       C  
ATOM   2612  CG  PRO A1123     -39.578  57.625  15.223  1.00 10.83           C  
ANISOU 2612  CG  PRO A1123     2005    981   1126    382   1149    236       C  
ATOM   2613  CD  PRO A1123     -39.988  58.212  13.892  1.00 10.54           C  
ANISOU 2613  CD  PRO A1123     1851    976   1176    389   1111    246       C  
ATOM   2614  N   PHE A1124     -36.981  56.560  13.019  1.00  8.69           N  
ANISOU 2614  N   PHE A1124     1637    782    884    217    848    181       N  
ATOM   2615  CA  PHE A1124     -36.200  55.346  12.687  1.00 18.04           C  
ANISOU 2615  CA  PHE A1124     2796   2008   2051    187    766    161       C  
ATOM   2616  C   PHE A1124     -35.762  55.323  11.210  1.00  7.54           C  
ANISOU 2616  C   PHE A1124     1350    758    757    166    677    151       C  
ATOM   2617  O   PHE A1124     -34.565  55.270  10.880  1.00  7.29           O  
ANISOU 2617  O   PHE A1124     1310    793    664    156    592    120       O  
ATOM   2618  CB  PHE A1124     -37.037  54.102  12.998  1.00 40.01           C  
ANISOU 2618  CB  PHE A1124     5570   4767   4863    181    805    191       C  
ATOM   2619  CG  PHE A1124     -37.834  54.160  14.278  1.00 74.33           C  
ANISOU 2619  CG  PHE A1124     9990   9067   9185    194    919    222       C  
ATOM   2620  CD1 PHE A1124     -37.199  54.272  15.508  1.00 50.44           C  
ANISOU 2620  CD1 PHE A1124     7104   5993   6066    210    934    196       C  
ATOM   2621  CD2 PHE A1124     -39.221  54.083  14.253  1.00 87.58           C  
ANISOU 2621  CD2 PHE A1124    11587  10766  10922    189   1010    282       C  
ATOM   2622  CE1 PHE A1124     -37.934  54.294  16.686  1.00 44.96           C  
ANISOU 2622  CE1 PHE A1124     6480   5267   5334    227   1044    224       C  
ATOM   2623  CE2 PHE A1124     -39.955  54.110  15.432  1.00 59.11           C  
ANISOU 2623  CE2 PHE A1124     8028   7155   7276    206   1125    316       C  
ATOM   2624  CZ  PHE A1124     -39.311  54.218  16.646  1.00 47.77           C  
ANISOU 2624  CZ  PHE A1124     6743   5665   5741    229   1145    285       C  
ATOM   2625  N   GLY A1125     -36.739  55.353  10.326  1.00  7.49           N  
ANISOU 2625  N   GLY A1125     1246    759    838    162    699    182       N  
ATOM   2626  CA  GLY A1125     -36.449  55.346   8.885  1.00  7.04           C  
ANISOU 2626  CA  GLY A1125     1085    773    814    144    621    177       C  
ATOM   2627  C   GLY A1125     -36.106  53.967   8.381  1.00  6.88           C  
ANISOU 2627  C   GLY A1125     1045    788    782    157    549    156       C  
ATOM   2628  O   GLY A1125     -35.277  53.845   7.473  1.00  6.63           O  
ANISOU 2628  O   GLY A1125      961    841    715    167    468    128       O  
ATOM   2629  N   LEU A1126     -36.780  52.955   8.920  1.00  7.22           N  
ANISOU 2629  N   LEU A1126     1133    769    842    157    571    176       N  
ATOM   2630  CA  LEU A1126     -36.547  51.553   8.535  1.00  7.33           C  
ANISOU 2630  CA  LEU A1126     1178    776    830    173    480    157       C  
ATOM   2631  C   LEU A1126     -36.889  51.333   7.057  1.00  7.16           C  
ANISOU 2631  C   LEU A1126     1066    789    863    169    418    164       C  
ATOM   2632  O   LEU A1126     -36.303  50.427   6.421  1.00  7.22           O  
ANISOU 2632  O   LEU A1126     1101    819    821    216    316    125       O  
ATOM   2633  CB  LEU A1126     -37.385  50.591   9.391  1.00  7.95           C  
ANISOU 2633  CB  LEU A1126     1339    765    916    136    506    199       C  
ATOM   2634  CG  LEU A1126     -37.128  50.577  10.893  1.00  8.28           C  
ANISOU 2634  CG  LEU A1126     1490    761    893    137    562    195       C  
ATOM   2635  CD1 LEU A1126     -38.040  49.567  11.588  1.00  9.07           C  
ANISOU 2635  CD1 LEU A1126     1661    789    994     74    579    253       C  
ATOM   2636  CD2 LEU A1126     -35.674  50.263  11.204  1.00  8.11           C  
ANISOU 2636  CD2 LEU A1126     1551    759    770    200    480    123       C  
ATOM   2637  N   VAL A1127     -37.770  52.162   6.522  1.00  7.05           N  
ANISOU 2637  N   VAL A1127      959    782    937    132    471    208       N  
ATOM   2638  CA  VAL A1127     -38.175  52.069   5.108  1.00  6.92           C  
ANISOU 2638  CA  VAL A1127      857    793    977    120    414    221       C  
ATOM   2639  C   VAL A1127     -36.993  52.422   4.225  1.00  6.51           C  
ANISOU 2639  C   VAL A1127      770    840    863    160    348    168       C  
ATOM   2640  O   VAL A1127     -36.786  51.766   3.188  1.00  6.54           O  
ANISOU 2640  O   VAL A1127      755    877    849    188    264    147       O  
ATOM   2641  CB  VAL A1127     -39.374  52.977   4.782  1.00  7.01           C  
ANISOU 2641  CB  VAL A1127      774    796   1092     81    484    280       C  
ATOM   2642  CG1 VAL A1127     -39.723  52.940   3.309  1.00  6.87           C  
ANISOU 2642  CG1 VAL A1127      676    804   1129     65    416    293       C  
ATOM   2643  CG2 VAL A1127     -40.596  52.613   5.598  1.00  7.68           C  
ANISOU 2643  CG2 VAL A1127      857    834   1228     43    557    345       C  
ATOM   2644  N   ALA A1128     -36.262  53.462   4.607  1.00  6.31           N  
ANISOU 2644  N   ALA A1128      737    866    795    155    380    154       N  
ATOM   2645  CA  ALA A1128     -35.098  53.921   3.840  1.00  6.16           C  
ANISOU 2645  CA  ALA A1128      662    975    701    163    322    124       C  
ATOM   2646  C   ALA A1128     -34.124  52.770   3.701  1.00  6.37           C  
ANISOU 2646  C   ALA A1128      711   1076    630    244    245     68       C  
ATOM   2647  O   ALA A1128     -33.631  52.489   2.589  1.00  6.46           O  
ANISOU 2647  O   ALA A1128      662   1193    597    285    180     43       O  
ATOM   2648  CB  ALA A1128     -34.462  55.080   4.553  1.00  6.17           C  
ANISOU 2648  CB  ALA A1128      685   1002    656    120    353    130       C  
ATOM   2649  N   LEU A1129     -33.826  52.143   4.819  1.00  6.57           N  
ANISOU 2649  N   LEU A1129      831   1054    612    280    250     45       N  
ATOM   2650  CA  LEU A1129     -32.875  51.012   4.874  1.00  6.97           C  
ANISOU 2650  CA  LEU A1129      931   1160    556    385    167    -15       C  
ATOM   2651  C   LEU A1129     -33.324  49.871   3.971  1.00  7.25           C  
ANISOU 2651  C   LEU A1129     1001   1154    598    446     88    -34       C  
ATOM   2652  O   LEU A1129     -32.590  49.482   3.056  1.00  7.54           O  
ANISOU 2652  O   LEU A1129     1001   1307    555    538     14    -82       O  
ATOM   2653  CB  LEU A1129     -32.762  50.536   6.322  1.00  7.19           C  
ANISOU 2653  CB  LEU A1129     1082   1097    553    397    185    -25       C  
ATOM   2654  CG  LEU A1129     -32.224  51.586   7.288  1.00  7.07           C  
ANISOU 2654  CG  LEU A1129     1065   1110    511    346    244    -13       C  
ATOM   2655  CD1 LEU A1129     -32.276  51.053   8.697  1.00  7.33           C  
ANISOU 2655  CD1 LEU A1129     1233   1034    518    357    264    -19       C  
ATOM   2656  CD2 LEU A1129     -30.806  52.033   6.935  1.00  7.25           C  
ANISOU 2656  CD2 LEU A1129     1002   1322    430    373    192    -41       C  
ATOM   2657  N   GLU A1130     -34.530  49.370   4.220  1.00  7.32           N  
ANISOU 2657  N   GLU A1130     1080   1010    691    390    101      7       N  
ATOM   2658  CA  GLU A1130     -35.086  48.248   3.438  1.00  7.77           C  
ANISOU 2658  CA  GLU A1130     1203    992    754    418      6      4       C  
ATOM   2659  C   GLU A1130     -35.062  48.588   1.954  1.00  7.60           C  
ANISOU 2659  C   GLU A1130     1081   1061    746    437    -28     -2       C  
ATOM   2660  O   GLU A1130     -34.781  47.714   1.126  1.00  8.08           O  
ANISOU 2660  O   GLU A1130     1197   1133    741    529   -133    -47       O  
ATOM   2661  CB  GLU A1130     -36.497  47.939   3.938  1.00  7.98           C  
ANISOU 2661  CB  GLU A1130     1278    872    880    303     39     83       C  
ATOM   2662  CG  GLU A1130     -36.576  47.528   5.399  1.00  8.31           C  
ANISOU 2662  CG  GLU A1130     1429    830    896    274     72     98       C  
ATOM   2663  CD  GLU A1130     -37.996  47.356   5.938  1.00  8.72           C  
ANISOU 2663  CD  GLU A1130     1491    786   1034    143    127    194       C  
ATOM   2664  OE1 GLU A1130     -38.952  47.457   5.125  1.00  8.81           O  
ANISOU 2664  OE1 GLU A1130     1425    791   1129     78    123    249       O  
ATOM   2665  OE2 GLU A1130     -38.155  47.119   7.176  1.00  9.08           O  
ANISOU 2665  OE2 GLU A1130     1615    778   1055    104    173    219       O  
ATOM   2666  N   ALA A1131     -35.359  49.835   1.629  1.00  7.06           N  
ANISOU 2666  N   ALA A1131      886   1046    750    359     51     38       N  
ATOM   2667  CA  ALA A1131     -35.350  50.299   0.238  1.00  6.92           C  
ANISOU 2667  CA  ALA A1131      771   1114    743    359     23     39       C  
ATOM   2668  C   ALA A1131     -33.926  50.334  -0.302  1.00  7.13           C  
ANISOU 2668  C   ALA A1131      748   1327    634    456    -18    -22       C  
ATOM   2669  O   ALA A1131     -33.666  49.839  -1.402  1.00  7.50           O  
ANISOU 2669  O   ALA A1131      784   1441    622    533    -91    -56       O  
ATOM   2670  CB  ALA A1131     -36.037  51.638   0.160  1.00  6.45           C  
ANISOU 2670  CB  ALA A1131      617   1047    786    252    108    101       C  
ATOM   2671  N   MET A1132     -33.023  50.899   0.487  1.00  7.07           N  
ANISOU 2671  N   MET A1132      708   1412    566    454     22    -33       N  
ATOM   2672  CA  MET A1132     -31.625  51.093   0.062  1.00  7.47           C  
ANISOU 2672  CA  MET A1132      670   1687    479    523     -7    -73       C  
ATOM   2673  C   MET A1132     -30.892  49.763  -0.070  1.00  8.24           C  
ANISOU 2673  C   MET A1132      832   1845    453    704    -94   -153       C  
ATOM   2674  O   MET A1132     -30.085  49.606  -1.000  1.00  8.82           O  
ANISOU 2674  O   MET A1132      827   2109    414    803   -138   -192       O  
ATOM   2675  CB  MET A1132     -30.885  52.029   1.015  1.00  7.38           C  
ANISOU 2675  CB  MET A1132      617   1752    434    452     44    -51       C  
ATOM   2676  CG  MET A1132     -31.298  53.478   0.856  1.00  6.96           C  
ANISOU 2676  CG  MET A1132      505   1685    453    298     98     17       C  
ATOM   2677  SD  MET A1132     -30.929  54.462   2.320  1.00  6.89           S  
ANISOU 2677  SD  MET A1132      542   1636    436    203    149     49       S  
ATOM   2678  CE  MET A1132     -29.156  54.259   2.370  1.00  7.65           C  
ANISOU 2678  CE  MET A1132      552   1996    356    254     92     19       C  
ATOM   2679  N   CYS A1133     -31.147  48.833   0.838  1.00  8.41           N  
ANISOU 2679  N   CYS A1133      999   1715    479    754   -123   -178       N  
ATOM   2680  CA  CYS A1133     -30.540  47.486   0.773  1.00  9.32           C  
ANISOU 2680  CA  CYS A1133     1227   1843    470    943   -230   -260       C  
ATOM   2681  C   CYS A1133     -30.895  46.823  -0.550  1.00  9.77           C  
ANISOU 2681  C   CYS A1133     1322   1887    503   1026   -313   -288       C  
ATOM   2682  O   CYS A1133     -30.096  46.058  -1.100  1.00 10.71           O  
ANISOU 2682  O   CYS A1133     1474   2116    479   1218   -399   -367       O  
ATOM   2683  CB  CYS A1133     -31.051  46.589   1.890  1.00  9.48           C  
ANISOU 2683  CB  CYS A1133     1436   1648    516    943   -264   -264       C  
ATOM   2684  SG  CYS A1133     -30.476  47.050   3.541  1.00  9.25           S  
ANISOU 2684  SG  CYS A1133     1414   1623    476    896   -194   -253       S  
ATOM   2685  N   LEU A1134     -32.078  47.119  -1.045  1.00  9.24           N  
ANISOU 2685  N   LEU A1134     1253   1692    564    896   -292   -227       N  
ATOM   2686  CA  LEU A1134     -32.587  46.483  -2.275  1.00  9.68           C  
ANISOU 2686  CA  LEU A1134     1369   1696    611    948   -382   -242       C  
ATOM   2687  C   LEU A1134     -32.378  47.374  -3.476  1.00  9.46           C  
ANISOU 2687  C   LEU A1134     1177   1839    578    925   -345   -228       C  
ATOM   2688  O   LEU A1134     -32.950  47.081  -4.521  1.00  9.67           O  
ANISOU 2688  O   LEU A1134     1238   1815    621    933   -404   -224       O  
ATOM   2689  CB  LEU A1134     -34.066  46.137  -2.092  1.00  9.46           C  
ANISOU 2689  CB  LEU A1134     1446   1426    723    810   -401   -172       C  
ATOM   2690  CG  LEU A1134     -34.290  45.090  -0.999  1.00  9.97           C  
ANISOU 2690  CG  LEU A1134     1699   1320    769    821   -461   -179       C  
ATOM   2691  CD1 LEU A1134     -35.754  44.950  -0.639  1.00  9.86           C  
ANISOU 2691  CD1 LEU A1134     1737   1114    892    639   -452    -82       C  
ATOM   2692  CD2 LEU A1134     -33.725  43.753  -1.437  1.00 11.16           C  
ANISOU 2692  CD2 LEU A1134     2037   1434    769   1013   -623   -267       C  
ATOM   2693  N   GLY A1135     -31.618  48.443  -3.296  1.00  9.14           N  
ANISOU 2693  N   GLY A1135      976   1983    512    878   -261   -210       N  
ATOM   2694  CA  GLY A1135     -31.184  49.282  -4.414  1.00  9.20           C  
ANISOU 2694  CA  GLY A1135      828   2191    474    853   -237   -194       C  
ATOM   2695  C   GLY A1135     -32.202  50.322  -4.835  1.00  8.40           C  
ANISOU 2695  C   GLY A1135      668   2000    520    668   -184   -111       C  
ATOM   2696  O   GLY A1135     -31.970  51.029  -5.832  1.00  8.48           O  
ANISOU 2696  O   GLY A1135      570   2149    500    627   -176    -89       O  
ATOM   2697  N   ALA A1136     -33.270  50.484  -4.071  1.00  7.77           N  
ANISOU 2697  N   ALA A1136      650   1714    587    561   -147    -63       N  
ATOM   2698  CA  ALA A1136     -34.205  51.590  -4.323  1.00  7.15           C  
ANISOU 2698  CA  ALA A1136      509   1565    642    406    -93     12       C  
ATOM   2699  C   ALA A1136     -33.564  52.873  -3.831  1.00  6.90           C  
ANISOU 2699  C   ALA A1136      389   1640    591    319    -24     43       C  
ATOM   2700  O   ALA A1136     -33.105  52.944  -2.688  1.00  6.85           O  
ANISOU 2700  O   ALA A1136      408   1633    560    319     11     35       O  
ATOM   2701  CB  ALA A1136     -35.525  51.374  -3.642  1.00  6.85           C  
ANISOU 2701  CB  ALA A1136      543   1312    745    338    -69     57       C  
ATOM   2702  N   ILE A1137     -33.586  53.886  -4.675  1.00  6.83           N  
ANISOU 2702  N   ILE A1137      298   1704    591    231    -18     84       N  
ATOM   2703  CA  ILE A1137     -32.985  55.196  -4.338  1.00  6.81           C  
ANISOU 2703  CA  ILE A1137      237   1792    556    119     17    127       C  
ATOM   2704  C   ILE A1137     -34.019  56.026  -3.594  1.00  6.33           C  
ANISOU 2704  C   ILE A1137      233   1542    630     29     68    175       C  
ATOM   2705  O   ILE A1137     -35.044  56.397  -4.143  1.00  6.15           O  
ANISOU 2705  O   ILE A1137      212   1415    708    -11     67    207       O  
ATOM   2706  CB  ILE A1137     -32.507  55.914  -5.607  1.00  7.18           C  
ANISOU 2706  CB  ILE A1137      190   2006    532     53    -14    157       C  
ATOM   2707  CG1 ILE A1137     -31.485  55.079  -6.390  1.00  7.90           C  
ANISOU 2707  CG1 ILE A1137      211   2322    468    171    -55    107       C  
ATOM   2708  CG2 ILE A1137     -31.969  57.282  -5.226  1.00  7.34           C  
ANISOU 2708  CG2 ILE A1137      182   2090    516    -95     -1    217       C  
ATOM   2709  CD1 ILE A1137     -31.154  55.624  -7.769  1.00  8.41           C  
ANISOU 2709  CD1 ILE A1137      180   2557    455    116    -84    139       C  
ATOM   2710  N   PRO A1138     -33.764  56.343  -2.322  1.00  6.26           N  
ANISOU 2710  N   PRO A1138      272   1491    616      9    110    177       N  
ATOM   2711  CA  PRO A1138     -34.741  57.086  -1.536  1.00  6.03           C  
ANISOU 2711  CA  PRO A1138      307   1290    692    -39    164    212       C  
ATOM   2712  C   PRO A1138     -34.825  58.571  -1.884  1.00  6.18           C  
ANISOU 2712  C   PRO A1138      330   1300    719   -146    151    261       C  
ATOM   2713  O   PRO A1138     -33.791  59.211  -1.978  1.00  6.52           O  
ANISOU 2713  O   PRO A1138      356   1462    658   -220    115    278       O  
ATOM   2714  CB  PRO A1138     -34.246  56.887  -0.100  1.00  6.06           C  
ANISOU 2714  CB  PRO A1138      376   1270    654    -15    202    191       C  
ATOM   2715  CG  PRO A1138     -32.753  56.767  -0.254  1.00  6.40           C  
ANISOU 2715  CG  PRO A1138      367   1509    555    -14    156    170       C  
ATOM   2716  CD  PRO A1138     -32.531  56.070  -1.584  1.00  6.56           C  
ANISOU 2716  CD  PRO A1138      304   1651    535     41    106    147       C  
ATOM   2717  N   ILE A1139     -36.055  59.049  -2.049  1.00  6.11           N  
ANISOU 2717  N   ILE A1139      344   1153    821   -150    170    288       N  
ATOM   2718  CA  ILE A1139     -36.362  60.484  -2.125  1.00  6.41           C  
ANISOU 2718  CA  ILE A1139      436   1123    874   -222    153    329       C  
ATOM   2719  C   ILE A1139     -37.141  60.805  -0.877  1.00  6.52           C  
ANISOU 2719  C   ILE A1139      534    992    947   -169    221    327       C  
ATOM   2720  O   ILE A1139     -38.286  60.467  -0.858  1.00  6.48           O  
ANISOU 2720  O   ILE A1139      506    912   1043   -106    263    331       O  
ATOM   2721  CB  ILE A1139     -37.119  60.900  -3.387  1.00  6.48           C  
ANISOU 2721  CB  ILE A1139      408   1106    947   -247    109    357       C  
ATOM   2722  CG1 ILE A1139     -36.405  60.425  -4.646  1.00  6.46           C  
ANISOU 2722  CG1 ILE A1139      319   1256    876   -281     52    355       C  
ATOM   2723  CG2 ILE A1139     -37.288  62.407  -3.387  1.00  6.98           C  
ANISOU 2723  CG2 ILE A1139      562   1089   1001   -314     70    394       C  
ATOM   2724  CD1 ILE A1139     -37.187  60.633  -5.885  1.00  6.51           C  
ANISOU 2724  CD1 ILE A1139      294   1230    947   -297      8    379       C  
ATOM   2725  N   ALA A1140     -36.439  61.199   0.162  1.00  6.71           N  
ANISOU 2725  N   ALA A1140      641   1010    897   -189    232    319       N  
ATOM   2726  CA  ALA A1140     -37.008  61.280   1.524  1.00  6.88           C  
ANISOU 2726  CA  ALA A1140      750    915    947   -119    307    306       C  
ATOM   2727  C   ALA A1140     -37.056  62.713   2.025  1.00  7.52           C  
ANISOU 2727  C   ALA A1140      971    896    990   -143    283    322       C  
ATOM   2728  O   ALA A1140     -36.240  63.532   1.639  1.00  7.83           O  
ANISOU 2728  O   ALA A1140     1060    967    948   -248    197    345       O  
ATOM   2729  CB  ALA A1140     -36.245  60.379   2.460  1.00  6.67           C  
ANISOU 2729  CB  ALA A1140      733    936    862    -98    338    275       C  
ATOM   2730  N   SER A1141     -37.964  62.974   2.952  1.00  7.90           N  
ANISOU 2730  N   SER A1141     1092    831   1077    -45    354    312       N  
ATOM   2731  CA  SER A1141     -37.939  64.212   3.753  1.00  8.70           C  
ANISOU 2731  CA  SER A1141     1373    816   1114    -31    333    311       C  
ATOM   2732  C   SER A1141     -36.787  64.125   4.738  1.00  8.71           C  
ANISOU 2732  C   SER A1141     1461    837   1012    -87    320    299       C  
ATOM   2733  O   SER A1141     -36.559  63.070   5.286  1.00  8.25           O  
ANISOU 2733  O   SER A1141     1341    834    959    -59    380    279       O  
ATOM   2734  CB  SER A1141     -39.239  64.471   4.450  1.00  9.30           C  
ANISOU 2734  CB  SER A1141     1493    795   1245    120    420    298       C  
ATOM   2735  OG  SER A1141     -40.252  64.791   3.508  1.00  9.54           O  
ANISOU 2735  OG  SER A1141     1455    810   1359    168    409    315       O  
ATOM   2736  N   ALA A1142     -36.093  65.249   4.934  1.00  9.38           N  
ANISOU 2736  N   ALA A1142     1698    866    997   -172    225    317       N  
ATOM   2737  CA  ALA A1142     -34.997  65.325   5.916  1.00  9.61           C  
ANISOU 2737  CA  ALA A1142     1827    905    919   -240    193    315       C  
ATOM   2738  C   ALA A1142     -35.568  65.504   7.322  1.00 10.10           C  
ANISOU 2738  C   ALA A1142     2039    830    968   -115    268    281       C  
ATOM   2739  O   ALA A1142     -35.786  66.653   7.720  1.00 11.05           O  
ANISOU 2739  O   ALA A1142     2355    811   1032    -94    216    282       O  
ATOM   2740  CB  ALA A1142     -34.034  66.439   5.564  1.00 10.35           C  
ANISOU 2740  CB  ALA A1142     2030    999    901   -410     46    364       C  
ATOM   2741  N   VAL A1143     -35.769  64.438   8.043  1.00  9.63           N  
ANISOU 2741  N   VAL A1143     1911    805    942    -36    373    252       N  
ATOM   2742  CA  VAL A1143     -36.324  64.513   9.417  1.00 10.18           C  
ANISOU 2742  CA  VAL A1143     2111    769    988     83    460    223       C  
ATOM   2743  C   VAL A1143     -35.826  63.321  10.189  1.00  9.65           C  
ANISOU 2743  C   VAL A1143     1990    768    909     81    518    206       C  
ATOM   2744  O   VAL A1143     -35.655  62.261   9.606  1.00  8.89           O  
ANISOU 2744  O   VAL A1143     1733    780    863     55    530    208       O  
ATOM   2745  CB  VAL A1143     -37.864  64.535   9.397  1.00 10.54           C  
ANISOU 2745  CB  VAL A1143     2112    771   1119    238    564    215       C  
ATOM   2746  CG1 VAL A1143     -38.427  65.827   8.834  1.00 11.36           C  
ANISOU 2746  CG1 VAL A1143     2313    782   1218    282    501    220       C  
ATOM   2747  CG2 VAL A1143     -38.440  63.361   8.633  1.00  9.75           C  
ANISOU 2747  CG2 VAL A1143     1788    782   1133    243    626    229       C  
ATOM   2748  N   GLY A1144     -35.653  63.439  11.503  1.00 10.16           N  
ANISOU 2748  N   GLY A1144     2202    756    899    122    550    187       N  
ATOM   2749  CA  GLY A1144     -35.344  62.296  12.365  1.00  9.80           C  
ANISOU 2749  CA  GLY A1144     2130    751    841    137    611    169       C  
ATOM   2750  C   GLY A1144     -34.238  61.407  11.844  1.00  9.06           C  
ANISOU 2750  C   GLY A1144     1916    787    738     44    545    171       C  
ATOM   2751  O   GLY A1144     -33.094  61.865  11.690  1.00  9.18           O  
ANISOU 2751  O   GLY A1144     1962    849    677    -58    439    184       O  
ATOM   2752  N   GLY A1145     -34.567  60.137  11.657  1.00  8.51           N  
ANISOU 2752  N   GLY A1145     1723    778    730     82    599    162       N  
ATOM   2753  CA  GLY A1145     -33.599  59.117  11.247  1.00  7.99           C  
ANISOU 2753  CA  GLY A1145     1559    831    644     43    541    149       C  
ATOM   2754  C   GLY A1145     -33.289  59.153   9.758  1.00  7.62           C  
ANISOU 2754  C   GLY A1145     1371    898    625     -5    472    162       C  
ATOM   2755  O   GLY A1145     -32.204  58.707   9.317  1.00  7.49           O  
ANISOU 2755  O   GLY A1145     1279   1013    552    -40    401    154       O  
ATOM   2756  N   LEU A1146     -34.016  59.974   9.021  1.00  7.69           N  
ANISOU 2756  N   LEU A1146     1360    871    689    -17    476    186       N  
ATOM   2757  CA  LEU A1146     -33.862  60.019   7.556  1.00  7.39           C  
ANISOU 2757  CA  LEU A1146     1193    933    679    -64    418    203       C  
ATOM   2758  C   LEU A1146     -32.704  60.908   7.133  1.00  7.73           C  
ANISOU 2758  C   LEU A1146     1244   1063    628   -182    314    229       C  
ATOM   2759  O   LEU A1146     -32.054  60.580   6.135  1.00 19.33           O  
ANISOU 2759  O   LEU A1146     2586   2684   2073   -225    261    236       O  
ATOM   2760  CB  LEU A1146     -35.167  60.459   6.884  1.00  7.40           C  
ANISOU 2760  CB  LEU A1146     1165    863    781    -29    456    222       C  
ATOM   2761  CG  LEU A1146     -36.340  59.484   7.014  1.00  7.21           C  
ANISOU 2761  CG  LEU A1146     1083    805    852     54    544    218       C  
ATOM   2762  CD1 LEU A1146     -37.608  60.093   6.444  1.00  7.47           C  
ANISOU 2762  CD1 LEU A1146     1079    785    973     90    578    244       C  
ATOM   2763  CD2 LEU A1146     -36.047  58.161   6.328  1.00  6.72           C  
ANISOU 2763  CD2 LEU A1146      914    832    806     53    514    205       C  
ATOM   2764  N   ARG A1147     -32.404  61.944   7.902  1.00  8.34           N  
ANISOU 2764  N   ARG A1147     1470   1058    640   -236    280    246       N  
ATOM   2765  CA  ARG A1147     -31.260  62.823   7.619  1.00  8.93           C  
ANISOU 2765  CA  ARG A1147     1569   1214    607   -386    163    290       C  
ATOM   2766  C   ARG A1147     -29.968  62.176   8.115  1.00  9.04           C  
ANISOU 2766  C   ARG A1147     1529   1374    530   -423    127    285       C  
ATOM   2767  O   ARG A1147     -28.875  62.470   7.609  1.00  9.51           O  
ANISOU 2767  O   ARG A1147     1512   1601    499   -546     36    327       O  
ATOM   2768  CB  ARG A1147     -31.511  64.240   8.150  1.00  9.76           C  
ANISOU 2768  CB  ARG A1147     1887   1151    669   -438    112    316       C  
ATOM   2769  CG  ARG A1147     -31.555  64.372   9.665  1.00 22.56           C  
ANISOU 2769  CG  ARG A1147     3687   2637   2247   -381    144    290       C  
ATOM   2770  CD  ARG A1147     -31.586  65.853  10.059  1.00 41.29           C  
ANISOU 2770  CD  ARG A1147     6298   4847   4541   -443     53    317       C  
ATOM   2771  NE  ARG A1147     -31.752  66.112  11.493  1.00 37.69           N  
ANISOU 2771  NE  ARG A1147     6049   4238   4033   -367     81    287       N  
ATOM   2772  CZ  ARG A1147     -32.918  66.280  12.132  1.00 46.55           C  
ANISOU 2772  CZ  ARG A1147     7281   5212   5191   -198    178    245       C  
ATOM   2773  NH1 ARG A1147     -34.073  66.226  11.488  1.00 53.04           N  
ANISOU 2773  NH1 ARG A1147     8019   6019   6112    -88    254    231       N  
ATOM   2774  NH2 ARG A1147     -32.927  66.506  13.433  1.00 69.45           N  
ANISOU 2774  NH2 ARG A1147    10372   7994   8020   -135    198    219       N  
ATOM   2775  N   ASP A1148     -30.119  61.288   9.080  1.00  8.75           N  
ANISOU 2775  N   ASP A1148     1525   1288    510   -318    194    239       N  
ATOM   2776  CA  ASP A1148     -28.992  60.499   9.629  1.00  9.30           C  
ANISOU 2776  CA  ASP A1148     1549   1483    499   -314    163    221       C  
ATOM   2777  C   ASP A1148     -28.536  59.456   8.618  1.00  8.56           C  
ANISOU 2777  C   ASP A1148     1261   1585    405   -264    151    201       C  
ATOM   2778  O   ASP A1148     -27.324  59.247   8.421  1.00  9.03           O  
ANISOU 2778  O   ASP A1148     1219   1843    365   -301     83    211       O  
ATOM   2779  CB  ASP A1148     -29.394  59.798  10.930  1.00 22.55           C  
ANISOU 2779  CB  ASP A1148     3339   3032   2196   -209    236    177       C  
ATOM   2780  CG  ASP A1148     -29.784  60.770  12.029  1.00 54.92           C  
ANISOU 2780  CG  ASP A1148     7645   6949   6272   -230    252    188       C  
ATOM   2781  OD1 ASP A1148     -29.493  61.993  11.874  1.00 67.50           O  
ANISOU 2781  OD1 ASP A1148     9316   8514   7813   -338    176    229       O  
ATOM   2782  OD2 ASP A1148     -30.386  60.304  13.021  1.00 45.33           O  
ANISOU 2782  OD2 ASP A1148     6524   5619   5079   -139    333    156       O  
ATOM   2783  N   ILE A1149     -29.515  58.825   7.996  1.00  7.95           N  
ANISOU 2783  N   ILE A1149     1135   1457    426   -175    211    175       N  
ATOM   2784  CA  ILE A1149     -29.323  57.637   7.122  1.00  7.69           C  
ANISOU 2784  CA  ILE A1149      966   1556    397    -87    203    139       C  
ATOM   2785  C   ILE A1149     -28.887  58.067   5.734  1.00  7.88           C  
ANISOU 2785  C   ILE A1149      851   1752    389   -151    150    170       C  
ATOM   2786  O   ILE A1149     -27.929  57.507   5.170  1.00  8.24           O  
ANISOU 2786  O   ILE A1149      772   2008    348   -118    104    156       O  
ATOM   2787  CB  ILE A1149     -30.613  56.796   7.075  1.00  7.14           C  
ANISOU 2787  CB  ILE A1149      927   1343    441      9    272    111       C  
ATOM   2788  CG1 ILE A1149     -30.841  56.060   8.392  1.00  7.14           C  
ANISOU 2788  CG1 ILE A1149     1043   1226    443     74    314     82       C  
ATOM   2789  CG2 ILE A1149     -30.582  55.829   5.906  1.00  6.99           C  
ANISOU 2789  CG2 ILE A1149      797   1428    429     81    241     84       C  
ATOM   2790  CD1 ILE A1149     -32.100  55.253   8.433  1.00  6.86           C  
ANISOU 2790  CD1 ILE A1149     1037   1066    504    132    375     76       C  
ATOM   2791  N   ILE A1150     -29.592  59.040   5.163  1.00  7.78           N  
ANISOU 2791  N   ILE A1150      859   1660    434   -231    155    211       N  
ATOM   2792  CA  ILE A1150     -29.356  59.465   3.767  1.00  7.96           C  
ANISOU 2792  CA  ILE A1150      765   1826    434   -302    108    246       C  
ATOM   2793  C   ILE A1150     -28.241  60.500   3.704  1.00  8.82           C  
ANISOU 2793  C   ILE A1150      852   2077    421   -466     26    311       C  
ATOM   2794  O   ILE A1150     -28.292  61.537   4.402  1.00 12.54           O  
ANISOU 2794  O   ILE A1150     1459   2425    878   -569     -1    350       O  
ATOM   2795  CB  ILE A1150     -30.618  59.964   3.039  1.00  7.58           C  
ANISOU 2795  CB  ILE A1150      744   1637    497   -311    134    263       C  
ATOM   2796  CG1 ILE A1150     -31.598  58.832   2.732  1.00  6.96           C  
ANISOU 2796  CG1 ILE A1150      635   1485    521   -178    190    218       C  
ATOM   2797  CG2 ILE A1150     -30.234  60.686   1.749  1.00  7.97           C  
ANISOU 2797  CG2 ILE A1150      706   1821    498   -424     68    314       C  
ATOM   2798  CD1 ILE A1150     -32.493  58.454   3.873  1.00  6.69           C  
ANISOU 2798  CD1 ILE A1150      706   1269    564   -106    263    196       C  
ATOM   2799  N   THR A1151     -27.290  60.210   2.822  1.00  9.31           N  
ANISOU 2799  N   THR A1151      748   2402    388   -489    -16    326       N  
ATOM   2800  CA  THR A1151     -26.128  61.053   2.488  1.00 10.40           C  
ANISOU 2800  CA  THR A1151      804   2758    388   -667   -100    407       C  
ATOM   2801  C   THR A1151     -26.382  61.774   1.170  1.00 10.62           C  
ANISOU 2801  C   THR A1151      779   2842    414   -779   -133    463       C  
ATOM   2802  O   THR A1151     -27.372  61.450   0.444  1.00 11.47           O  
ANISOU 2802  O   THR A1151      887   2846    624   -689    -89    427       O  
ATOM   2803  CB  THR A1151     -24.881  60.153   2.431  1.00 11.05           C  
ANISOU 2803  CB  THR A1151      711   3140    347   -594   -115    386       C  
ATOM   2804  OG1 THR A1151     -24.716  59.542   3.717  1.00 10.86           O  
ANISOU 2804  OG1 THR A1151      767   3027    330   -495    -96    335       O  
ATOM   2805  CG2 THR A1151     -23.601  60.857   2.018  1.00 15.44           C  
ANISOU 2805  CG2 THR A1151     1126   3998    742   -775   -197    480       C  
ATOM   2806  N   ASN A1152     -25.444  62.626   0.785  1.00 20.00           N  
ANISOU 2806  N   ASN A1152     1903   4221   1474   -975   -217    554       N  
ATOM   2807  CA  ASN A1152     -25.502  63.375  -0.494  1.00 41.76           C  
ANISOU 2807  CA  ASN A1152     4605   7064   4195  -1118   -266    624       C  
ATOM   2808  C   ASN A1152     -25.456  62.451  -1.715  1.00 32.03           C  
ANISOU 2808  C   ASN A1152     3186   6033   2948   -992   -220    585       C  
ATOM   2809  O   ASN A1152     -26.188  62.714  -2.719  1.00 19.50           O  
ANISOU 2809  O   ASN A1152     1611   4379   1418  -1009   -220    594       O  
ATOM   2810  CB  ASN A1152     -24.390  64.430  -0.546  1.00 48.74           C  
ANISOU 2810  CB  ASN A1152     5460   8137   4920  -1385   -377    747       C  
ATOM   2811  CG  ASN A1152     -24.523  65.378  -1.723  1.00 47.96           C  
ANISOU 2811  CG  ASN A1152     5362   8079   4780  -1571   -447    835       C  
ATOM   2812  OD1 ASN A1152     -25.627  65.788  -2.091  1.00 28.85           O  
ANISOU 2812  OD1 ASN A1152     3077   5414   2470  -1548   -442    817       O  
ATOM   2813  ND2 ASN A1152     -23.398  65.736  -2.321  1.00 67.02           N  
ANISOU 2813  ND2 ASN A1152     7619  10817   7027  -1760   -515    937       N  
ATOM   2814  N   GLU A1153     -24.596  61.440  -1.656  1.00 27.52           N  
ANISOU 2814  N   GLU A1153     2459   5706   2291   -866   -195    543       N  
ATOM   2815  CA  GLU A1153     -24.401  60.511  -2.780  1.00 29.80           C  
ANISOU 2815  CA  GLU A1153     2582   6211   2530   -718   -163    498       C  
ATOM   2816  C   GLU A1153     -25.369  59.342  -2.675  1.00 12.79           C  
ANISOU 2816  C   GLU A1153      505   3847    506   -477   -100    383       C  
ATOM   2817  O   GLU A1153     -25.294  58.415  -3.515  1.00 11.77           O  
ANISOU 2817  O   GLU A1153      283   3849    338   -318    -84    327       O  
ATOM   2818  CB  GLU A1153     -22.947  60.024  -2.810  1.00 54.24           C  
ANISOU 2818  CB  GLU A1153     5470   9697   5441   -680   -179    508       C  
ATOM   2819  CG  GLU A1153     -21.959  61.067  -3.317  1.00 68.75           C  
ANISOU 2819  CG  GLU A1153     7170  11829   7120   -935   -245    641       C  
ATOM   2820  CD  GLU A1153     -21.630  62.197  -2.352  1.00 92.61           C  
ANISOU 2820  CD  GLU A1153    10299  14763  10123  -1184   -318    738       C  
ATOM   2821  OE1 GLU A1153     -21.860  62.021  -1.132  1.00105.65           O  
ANISOU 2821  OE1 GLU A1153    12090  16200  11853  -1121   -309    690       O  
ATOM   2822  OE2 GLU A1153     -21.146  63.258  -2.825  1.00 45.74           O  
ANISOU 2822  OE2 GLU A1153     4322   8969   4086  -1448   -395    864       O  
ATOM   2823  N   THR A1154     -26.214  59.342  -1.657  1.00 10.47           N  
ANISOU 2823  N   THR A1154      380   3252    344   -448    -72    352       N  
ATOM   2824  CA  THR A1154     -27.083  58.206  -1.320  1.00  9.54           C  
ANISOU 2824  CA  THR A1154      344   2940    338   -250    -21    260       C  
ATOM   2825  C   THR A1154     -28.478  58.369  -1.902  1.00  8.72           C  
ANISOU 2825  C   THR A1154      321   2611    380   -250      1    258       C  
ATOM   2826  O   THR A1154     -28.981  57.496  -2.587  1.00  8.43           O  
ANISOU 2826  O   THR A1154      268   2553    382   -128     10    211       O  
ATOM   2827  CB  THR A1154     -27.119  57.991   0.199  1.00  9.22           C  
ANISOU 2827  CB  THR A1154      420   2746    335   -214      0    232       C  
ATOM   2828  OG1 THR A1154     -25.845  57.500   0.643  1.00 10.01           O  
ANISOU 2828  OG1 THR A1154      431   3069    300   -161    -25    215       O  
ATOM   2829  CG2 THR A1154     -28.253  57.076   0.621  1.00  8.33           C  
ANISOU 2829  CG2 THR A1154      420   2390    351    -74     50    167       C  
ATOM   2830  N   GLY A1155     -29.122  59.482  -1.603  1.00  8.49           N  
ANISOU 2830  N   GLY A1155      391   2407    425   -380      0    310       N  
ATOM   2831  CA  GLY A1155     -30.487  59.766  -2.052  1.00  7.88           C  
ANISOU 2831  CA  GLY A1155      386   2119    487   -376     20    314       C  
ATOM   2832  C   GLY A1155     -30.714  61.236  -2.260  1.00  8.21           C  
ANISOU 2832  C   GLY A1155      495   2087    534   -540    -22    386       C  
ATOM   2833  O   GLY A1155     -29.737  62.064  -2.215  1.00  9.00           O  
ANISOU 2833  O   GLY A1155      585   2316    517   -690    -81    445       O  
ATOM   2834  N   ILE A1156     -31.981  61.591  -2.426  1.00  7.78           N  
ANISOU 2834  N   ILE A1156      522   1828    606   -519     -5    387       N  
ATOM   2835  CA  ILE A1156     -32.428  62.994  -2.558  1.00  8.17           C  
ANISOU 2835  CA  ILE A1156      681   1750    673   -636    -55    442       C  
ATOM   2836  C   ILE A1156     -33.200  63.352  -1.306  1.00  8.03           C  
ANISOU 2836  C   ILE A1156      808   1511    730   -575    -12    423       C  
ATOM   2837  O   ILE A1156     -34.137  62.615  -0.964  1.00  7.47           O  
ANISOU 2837  O   ILE A1156      730   1340    765   -441     63    380       O  
ATOM   2838  CB  ILE A1156     -33.300  63.161  -3.806  1.00  8.04           C  
ANISOU 2838  CB  ILE A1156      636   1687    730   -632    -75    455       C  
ATOM   2839  CG1 ILE A1156     -32.733  62.361  -4.977  1.00  8.05           C  
ANISOU 2839  CG1 ILE A1156      485   1900    671   -622    -88    448       C  
ATOM   2840  CG2 ILE A1156     -33.460  64.633  -4.114  1.00  8.72           C  
ANISOU 2840  CG2 ILE A1156      838   1682    791   -769   -159    518       C  
ATOM   2841  CD1 ILE A1156     -33.460  62.558  -6.267  1.00  8.02           C  
ANISOU 2841  CD1 ILE A1156      460   1865    720   -637   -121    467       C  
ATOM   2842  N   LEU A1157     -32.840  64.479  -0.699  1.00  8.70           N  
ANISOU 2842  N   LEU A1157     1029   1527    749   -677    -68    461       N  
ATOM   2843  CA  LEU A1157     -33.477  64.939   0.543  1.00  8.82           C  
ANISOU 2843  CA  LEU A1157     1208   1339    804   -609    -35    439       C  
ATOM   2844  C   LEU A1157     -34.227  66.243   0.295  1.00  9.47           C  
ANISOU 2844  C   LEU A1157     1444   1248    905   -637    -98    468       C  
ATOM   2845  O   LEU A1157     -33.736  67.138  -0.416  1.00 10.15           O  
ANISOU 2845  O   LEU A1157     1580   1363    914   -790   -210    525       O  
ATOM   2846  CB  LEU A1157     -32.416  65.090   1.640  1.00  9.24           C  
ANISOU 2846  CB  LEU A1157     1332   1428    749   -674    -59    447       C  
ATOM   2847  CG  LEU A1157     -31.938  63.807   2.312  1.00  8.68           C  
ANISOU 2847  CG  LEU A1157     1164   1459    675   -586     14    400       C  
ATOM   2848  CD1 LEU A1157     -31.385  64.090   3.695  1.00  9.10           C  
ANISOU 2848  CD1 LEU A1157     1345   1452    658   -608      6    397       C  
ATOM   2849  CD2 LEU A1157     -33.048  62.790   2.419  1.00  7.90           C  
ANISOU 2849  CD2 LEU A1157     1017   1281    702   -419    119    345       C  
ATOM   2850  N   VAL A1158     -35.372  66.364   0.921  1.00  9.46           N  
ANISOU 2850  N   VAL A1158     1525   1078    989   -492    -35    432       N  
ATOM   2851  CA  VAL A1158     -36.318  67.472   0.651  1.00 10.16           C  
ANISOU 2851  CA  VAL A1158     1752   1000   1109   -452    -85    442       C  
ATOM   2852  C   VAL A1158     -36.921  67.935   1.960  1.00 10.73           C  
ANISOU 2852  C   VAL A1158     1992    907   1179   -320    -41    407       C  
ATOM   2853  O   VAL A1158     -36.916  67.153   2.924  1.00 10.32           O  
ANISOU 2853  O   VAL A1158     1900    878   1142   -241     58    373       O  
ATOM   2854  CB  VAL A1158     -37.376  66.936  -0.317  1.00  9.65           C  
ANISOU 2854  CB  VAL A1158     1543    953   1171   -363    -38    432       C  
ATOM   2855  CG1 VAL A1158     -38.479  67.953  -0.564  1.00 10.44           C  
ANISOU 2855  CG1 VAL A1158     1759    893   1314   -279    -79    435       C  
ATOM   2856  CG2 VAL A1158     -36.726  66.507  -1.624  1.00  9.23           C  
ANISOU 2856  CG2 VAL A1158     1346   1062   1099   -485    -87    463       C  
ATOM   2857  N   LYS A1159     -37.450  69.158   2.005  1.00 11.79           N  
ANISOU 2857  N   LYS A1159     2320    875   1283   -282   -118    411       N  
ATOM   2858  CA  LYS A1159     -38.012  69.703   3.246  1.00 12.63           C  
ANISOU 2858  CA  LYS A1159     2613    823   1360   -129    -85    370       C  
ATOM   2859  C   LYS A1159     -39.402  69.121   3.469  1.00 12.45           C  
ANISOU 2859  C   LYS A1159     2471    801   1458     89     58    330       C  
ATOM   2860  O   LYS A1159     -40.275  69.173   2.523  1.00 12.48           O  
ANISOU 2860  O   LYS A1159     2380    812   1547    146     55    338       O  
ATOM   2861  CB  LYS A1159     -38.073  71.223   3.175  1.00 14.08           C  
ANISOU 2861  CB  LYS A1159     3074    823   1449   -147   -239    384       C  
ATOM   2862  CG  LYS A1159     -38.613  71.905   4.420  1.00 19.04           C  
ANISOU 2862  CG  LYS A1159     3938   1276   2018     33   -225    335       C  
ATOM   2863  CD  LYS A1159     -37.994  73.275   4.628  1.00 28.31           C  
ANISOU 2863  CD  LYS A1159     5446   2271   3039    -68   -420    359       C  
ATOM   2864  CE  LYS A1159     -38.838  74.209   5.472  1.00 37.21           C  
ANISOU 2864  CE  LYS A1159     6849   3185   4102    164   -444    301       C  
ATOM   2865  NZ  LYS A1159     -40.062  74.631   4.745  1.00 38.88           N  
ANISOU 2865  NZ  LYS A1159     7049   3340   4381    344   -447    276       N  
ATOM   2866  N   ALA A1160     -39.628  68.644   4.693  1.00 12.48           N  
ANISOU 2866  N   ALA A1160     2483    799   1456    203    172    295       N  
ATOM   2867  CA  ALA A1160     -40.876  67.945   5.034  1.00 12.45           C  
ANISOU 2867  CA  ALA A1160     2337    840   1551    383    322    273       C  
ATOM   2868  C   ALA A1160     -42.061  68.911   4.905  1.00 13.73           C  
ANISOU 2868  C   ALA A1160     2584    906   1727    562    310    257       C  
ATOM   2869  O   ALA A1160     -42.011  70.094   5.327  1.00 14.95           O  
ANISOU 2869  O   ALA A1160     2986    912   1781    629    227    235       O  
ATOM   2870  CB  ALA A1160     -40.761  67.325   6.399  1.00 12.40           C  
ANISOU 2870  CB  ALA A1160     2348    852   1511    443    434    247       C  
ATOM   2871  N   GLY A1161     -43.115  68.428   4.271  1.00 13.63           N  
ANISOU 2871  N   GLY A1161     2374    974   1828    642    375    270       N  
ATOM   2872  CA  GLY A1161     -44.370  69.193   4.175  1.00 16.33           C  
ANISOU 2872  CA  GLY A1161     2746   1267   2191    847    383    255       C  
ATOM   2873  C   GLY A1161     -44.422  70.066   2.944  1.00 17.33           C  
ANISOU 2873  C   GLY A1161     2943   1315   2326    804    233    270       C  
ATOM   2874  O   GLY A1161     -45.468  70.710   2.710  1.00 21.38           O  
ANISOU 2874  O   GLY A1161     3475   1788   2859    982    220    256       O  
ATOM   2875  N   ASP A1162     -43.357  70.059   2.146  1.00 14.64           N  
ANISOU 2875  N   ASP A1162     2624    972   1966    582    125    300       N  
ATOM   2876  CA  ASP A1162     -43.290  70.896   0.929  1.00 14.76           C  
ANISOU 2876  CA  ASP A1162     2719    914   1972    503    -29    325       C  
ATOM   2877  C   ASP A1162     -43.512  70.023  -0.299  1.00 13.68           C  
ANISOU 2877  C   ASP A1162     2335    908   1953    412    -12    361       C  
ATOM   2878  O   ASP A1162     -42.608  69.312  -0.762  1.00 13.70           O  
ANISOU 2878  O   ASP A1162     2240   1009   1956    234    -20    386       O  
ATOM   2879  CB  ASP A1162     -42.007  71.733   0.873  1.00 15.52           C  
ANISOU 2879  CB  ASP A1162     3045    914   1934    314   -185    346       C  
ATOM   2880  CG  ASP A1162     -42.170  72.995   0.031  1.00 16.65           C  
ANISOU 2880  CG  ASP A1162     3385    914   2027    291   -362    364       C  
ATOM   2881  OD1 ASP A1162     -42.134  72.873  -1.208  1.00 15.89           O  
ANISOU 2881  OD1 ASP A1162     3181    875   1980    175   -420    403       O  
ATOM   2882  OD2 ASP A1162     -42.388  74.083   0.617  1.00 18.30           O  
ANISOU 2882  OD2 ASP A1162     3865    945   2141    404   -447    335       O  
ATOM   2883  N   PRO A1163     -44.722  70.117  -0.895  1.00 14.21           N  
ANISOU 2883  N   PRO A1163     2307    980   2111    543     -3    364       N  
ATOM   2884  CA  PRO A1163     -45.028  69.460  -2.168  1.00 13.45           C  
ANISOU 2884  CA  PRO A1163     2015    976   2118    462    -18    401       C  
ATOM   2885  C   PRO A1163     -44.280  70.031  -3.374  1.00 13.27           C  
ANISOU 2885  C   PRO A1163     2079    911   2050    284   -173    432       C  
ATOM   2886  O   PRO A1163     -44.164  69.360  -4.393  1.00 12.44           O  
ANISOU 2886  O   PRO A1163     1826    898   2002    177   -185    461       O  
ATOM   2887  CB  PRO A1163     -46.515  69.731  -2.415  1.00 14.50           C  
ANISOU 2887  CB  PRO A1163     2069   1102   2335    658      2    399       C  
ATOM   2888  CG  PRO A1163     -47.041  70.155  -1.067  1.00 15.65           C  
ANISOU 2888  CG  PRO A1163     2303   1211   2431    867     86    358       C  
ATOM   2889  CD  PRO A1163     -45.885  70.844  -0.376  1.00 15.74           C  
ANISOU 2889  CD  PRO A1163     2572   1102   2304    793     20    332       C  
ATOM   2890  N   GLY A1164     -43.785  71.241  -3.178  1.00 14.19           N  
ANISOU 2890  N   GLY A1164     2448    891   2052    254   -291    428       N  
ATOM   2891  CA  GLY A1164     -42.992  71.960  -4.173  1.00 14.37           C  
ANISOU 2891  CA  GLY A1164     2595    867   1997     58   -454    470       C  
ATOM   2892  C   GLY A1164     -41.670  71.291  -4.379  1.00 13.29           C  
ANISOU 2892  C   GLY A1164     2372    869   1808   -162   -446    503       C  
ATOM   2893  O   GLY A1164     -41.342  70.897  -5.525  1.00 12.70           O  
ANISOU 2893  O   GLY A1164     2178    898   1750   -294   -480    539       O  
ATOM   2894  N   GLU A1165     -40.910  71.178  -3.296  1.00 13.18           N  
ANISOU 2894  N   GLU A1165     2419    866   1719   -193   -404    489       N  
ATOM   2895  CA  GLU A1165     -39.582  70.534  -3.330  1.00 12.35           C  
ANISOU 2895  CA  GLU A1165     2225    915   1549   -381   -393    517       C  
ATOM   2896  C   GLU A1165     -39.738  69.075  -3.725  1.00 11.06           C  
ANISOU 2896  C   GLU A1165     1797    918   1488   -350   -273    503       C  
ATOM   2897  O   GLU A1165     -38.849  68.534  -4.401  1.00 10.50           O  
ANISOU 2897  O   GLU A1165     1616    996   1376   -488   -289    528       O  
ATOM   2898  CB  GLU A1165     -38.919  70.638  -1.953  1.00 12.55           C  
ANISOU 2898  CB  GLU A1165     2367    910   1492   -382   -365    498       C  
ATOM   2899  CG  GLU A1165     -38.607  72.047  -1.489  1.00 14.10           C  
ANISOU 2899  CG  GLU A1165     2864    929   1562   -435   -507    515       C  
ATOM   2900  CD  GLU A1165     -37.703  72.143  -0.266  1.00 16.19           C  
ANISOU 2900  CD  GLU A1165     3249   1180   1723   -493   -509    512       C  
ATOM   2901  OE1 GLU A1165     -37.857  73.134   0.487  1.00 32.96           O  
ANISOU 2901  OE1 GLU A1165     5638   3115   3767   -436   -587    498       O  
ATOM   2902  OE2 GLU A1165     -36.835  71.250  -0.064  1.00 13.33           O  
ANISOU 2902  OE2 GLU A1165     2729    985   1348   -585   -444    522       O  
ATOM   2903  N   LEU A1166     -40.810  68.441  -3.277  1.00 10.80           N  
ANISOU 2903  N   LEU A1166     1668    868   1567   -174   -161    466       N  
ATOM   2904  CA  LEU A1166     -41.052  67.018  -3.553  1.00  9.79           C  
ANISOU 2904  CA  LEU A1166     1321    867   1530   -147    -64    458       C  
ATOM   2905  C   LEU A1166     -41.343  66.779  -5.030  1.00  9.54           C  
ANISOU 2905  C   LEU A1166     1184    887   1551   -201   -120    484       C  
ATOM   2906  O   LEU A1166     -40.805  65.846  -5.621  1.00  8.82           O  
ANISOU 2906  O   LEU A1166      973    920   1456   -270   -109    488       O  
ATOM   2907  CB  LEU A1166     -42.184  66.448  -2.698  1.00  9.85           C  
ANISOU 2907  CB  LEU A1166     1257    852   1633     23     57    432       C  
ATOM   2908  CG  LEU A1166     -42.419  64.941  -2.855  1.00  9.01           C  
ANISOU 2908  CG  LEU A1166      962    855   1605     28    137    433       C  
ATOM   2909  CD1 LEU A1166     -41.173  64.128  -2.574  1.00  8.24           C  
ANISOU 2909  CD1 LEU A1166      844    851   1436    -60    151    418       C  
ATOM   2910  CD2 LEU A1166     -43.549  64.471  -1.954  1.00  9.37           C  
ANISOU 2910  CD2 LEU A1166      939    891   1727    165    249    428       C  
ATOM   2911  N   ALA A1167     -42.183  67.611  -5.610  1.00 10.25           N  
ANISOU 2911  N   ALA A1167     1331    880   1681   -155   -186    499       N  
ATOM   2912  CA  ALA A1167     -42.514  67.487  -7.048  1.00 10.13           C  
ANISOU 2912  CA  ALA A1167     1235    897   1714   -208   -253    527       C  
ATOM   2913  C   ALA A1167     -41.249  67.696  -7.862  1.00  9.98           C  
ANISOU 2913  C   ALA A1167     1247    962   1580   -397   -340    557       C  
ATOM   2914  O   ALA A1167     -41.025  66.980  -8.850  1.00  9.47           O  
ANISOU 2914  O   ALA A1167     1065   1007   1525   -457   -348    569       O  
ATOM   2915  CB  ALA A1167     -43.588  68.440  -7.501  1.00 11.08           C  
ANISOU 2915  CB  ALA A1167     1429    893   1886   -121   -325    537       C  
ATOM   2916  N   ASN A1168     -40.427  68.643  -7.429  1.00 10.56           N  
ANISOU 2916  N   ASN A1168     1480    996   1537   -492   -405    574       N  
ATOM   2917  CA  ASN A1168     -39.157  68.929  -8.119  1.00 10.72           C  
ANISOU 2917  CA  ASN A1168     1519   1130   1424   -699   -490    621       C  
ATOM   2918  C   ASN A1168     -38.208  67.740  -7.990  1.00  9.89           C  
ANISOU 2918  C   ASN A1168     1252   1226   1280   -735   -407    607       C  
ATOM   2919  O   ASN A1168     -37.529  67.380  -8.940  1.00  9.79           O  
ANISOU 2919  O   ASN A1168     1143   1370   1204   -836   -433    632       O  
ATOM   2920  CB  ASN A1168     -38.492  70.191  -7.582  1.00 11.76           C  
ANISOU 2920  CB  ASN A1168     1866   1172   1428   -815   -593    656       C  
ATOM   2921  CG  ASN A1168     -39.034  71.480  -8.164  1.00 12.89           C  
ANISOU 2921  CG  ASN A1168     2202   1144   1551   -846   -736    688       C  
ATOM   2922  OD1 ASN A1168     -39.271  71.588  -9.367  1.00 13.00           O  
ANISOU 2922  OD1 ASN A1168     2180   1180   1579   -904   -799    718       O  
ATOM   2923  ND2 ASN A1168     -39.189  72.481  -7.312  1.00 13.87           N  
ANISOU 2923  ND2 ASN A1168     2554   1089   1625   -807   -802    681       N  
ATOM   2924  N   ALA A1169     -38.107  67.185  -6.785  1.00  9.48           N  
ANISOU 2924  N   ALA A1169     1183   1172   1246   -648   -314    567       N  
ATOM   2925  CA  ALA A1169     -37.232  66.032  -6.534  1.00  8.82           C  
ANISOU 2925  CA  ALA A1169      967   1261   1121   -654   -243    545       C  
ATOM   2926  C   ALA A1169     -37.638  64.854  -7.413  1.00  8.18           C  
ANISOU 2926  C   ALA A1169      733   1262   1110   -585   -205    522       C  
ATOM   2927  O   ALA A1169     -36.768  64.100  -7.869  1.00  7.97           O  
ANISOU 2927  O   ALA A1169      607   1409   1010   -617   -199    515       O  
ATOM   2928  CB  ALA A1169     -37.293  65.692  -5.076  1.00  8.57           C  
ANISOU 2928  CB  ALA A1169      971   1173   1112   -558   -159    505       C  
ATOM   2929  N   ILE A1170     -38.931  64.719  -7.655  1.00  8.05           N  
ANISOU 2929  N   ILE A1170      704   1130   1224   -488   -189    513       N  
ATOM   2930  CA  ILE A1170     -39.438  63.636  -8.511  1.00  7.60           C  
ANISOU 2930  CA  ILE A1170      529   1121   1238   -435   -175    500       C  
ATOM   2931  C   ILE A1170     -38.967  63.898  -9.921  1.00  7.85           C  
ANISOU 2931  C   ILE A1170      538   1244   1200   -537   -259    530       C  
ATOM   2932  O   ILE A1170     -38.604  62.950 -10.644  1.00  7.60           O  
ANISOU 2932  O   ILE A1170      419   1332   1136   -527   -259    513       O  
ATOM   2933  CB  ILE A1170     -40.967  63.518  -8.433  1.00  7.65           C  
ANISOU 2933  CB  ILE A1170      516    996   1394   -330   -150    501       C  
ATOM   2934  CG1 ILE A1170     -41.426  63.151  -7.023  1.00  7.56           C  
ANISOU 2934  CG1 ILE A1170      506    930   1434   -232    -53    478       C  
ATOM   2935  CG2 ILE A1170     -41.490  62.533  -9.472  1.00  7.40           C  
ANISOU 2935  CG2 ILE A1170      386    999   1424   -312   -171    503       C  
ATOM   2936  CD1 ILE A1170     -42.912  63.254  -6.833  1.00  7.97           C  
ANISOU 2936  CD1 ILE A1170      525    889   1611   -133    -22    493       C  
ATOM   2937  N   LEU A1171     -38.971  65.159 -10.316  1.00  8.48           N  
ANISOU 2937  N   LEU A1171      712   1266   1244   -628   -338    572       N  
ATOM   2938  CA  LEU A1171     -38.546  65.544 -11.684  1.00  8.90           C  
ANISOU 2938  CA  LEU A1171      757   1405   1218   -749   -427    614       C  
ATOM   2939  C   LEU A1171     -37.037  65.422 -11.808  1.00  9.13           C  
ANISOU 2939  C   LEU A1171      737   1652   1080   -863   -430    631       C  
ATOM   2940  O   LEU A1171     -36.552  65.076 -12.886  1.00  9.32           O  
ANISOU 2940  O   LEU A1171      682   1829   1027   -912   -455    645       O  
ATOM   2941  CB  LEU A1171     -38.966  66.991 -11.967  1.00  9.71           C  
ANISOU 2941  CB  LEU A1171     1005   1366   1316   -826   -528    660       C  
ATOM   2942  CG  LEU A1171     -40.459  67.279 -12.087  1.00  9.83           C  
ANISOU 2942  CG  LEU A1171     1059   1195   1478   -706   -546    650       C  
ATOM   2943  CD1 LEU A1171     -40.700  68.786 -12.039  1.00 10.84           C  
ANISOU 2943  CD1 LEU A1171     1377   1168   1572   -754   -653    683       C  
ATOM   2944  CD2 LEU A1171     -41.019  66.669 -13.363  1.00  9.62           C  
ANISOU 2944  CD2 LEU A1171      939   1202   1511   -692   -573    656       C  
ATOM   2945  N   LYS A1172     -36.318  65.724 -10.744  1.00  9.28           N  
ANISOU 2945  N   LYS A1172      796   1695   1034   -902   -409    635       N  
ATOM   2946  CA  LYS A1172     -34.866  65.537 -10.703  1.00  9.63           C  
ANISOU 2946  CA  LYS A1172      766   1975    919  -1001   -405    655       C  
ATOM   2947  C   LYS A1172     -34.579  64.060 -10.940  1.00  9.08           C  
ANISOU 2947  C   LYS A1172      548   2059    843   -872   -332    596       C  
ATOM   2948  O   LYS A1172     -33.724  63.710 -11.772  1.00  9.52           O  
ANISOU 2948  O   LYS A1172      501   2340    774   -911   -343    608       O  
ATOM   2949  CB  LYS A1172     -34.311  66.016  -9.355  1.00  9.85           C  
ANISOU 2949  CB  LYS A1172      872   1967    901  -1043   -396    663       C  
ATOM   2950  CG  LYS A1172     -32.841  65.718  -9.096  1.00 10.27           C  
ANISOU 2950  CG  LYS A1172      826   2274    798  -1126   -386    683       C  
ATOM   2951  CD  LYS A1172     -31.926  66.389 -10.111  1.00 11.37           C  
ANISOU 2951  CD  LYS A1172      922   2617    778  -1331   -471    770       C  
ATOM   2952  CE  LYS A1172     -30.448  66.282  -9.776  1.00 12.14           C  
ANISOU 2952  CE  LYS A1172      910   2994    706  -1437   -470    811       C  
ATOM   2953  NZ  LYS A1172     -29.630  67.233 -10.575  1.00 13.54           N  
ANISOU 2953  NZ  LYS A1172     1073   3351    719  -1691   -570    926       N  
ATOM   2954  N   ALA A1173     -35.294  63.213 -10.210  1.00  8.32           N  
ANISOU 2954  N   ALA A1173      451   1843    865   -716   -263    535       N  
ATOM   2955  CA  ALA A1173     -35.123  61.759 -10.299  1.00  7.91           C  
ANISOU 2955  CA  ALA A1173      308   1885    810   -582   -213    474       C  
ATOM   2956  C   ALA A1173     -35.408  61.280 -11.717  1.00  8.02           C  
ANISOU 2956  C   ALA A1173      273   1955    818   -557   -252    469       C  
ATOM   2957  O   ALA A1173     -34.779  60.338 -12.193  1.00  8.18           O  
ANISOU 2957  O   ALA A1173      223   2136    750   -483   -246    432       O  
ATOM   2958  CB  ALA A1173     -36.004  61.055  -9.319  1.00  7.26           C  
ANISOU 2958  CB  ALA A1173      260   1637    859   -458   -154    429       C  
ATOM   2959  N   LEU A1174     -36.345  61.924 -12.381  1.00  8.06           N  
ANISOU 2959  N   LEU A1174      325   1826    908   -603   -300    504       N  
ATOM   2960  CA  LEU A1174     -36.671  61.564 -13.774  1.00  8.23           C  
ANISOU 2960  CA  LEU A1174      317   1883    926   -592   -349    506       C  
ATOM   2961  C   LEU A1174     -35.504  61.873 -14.696  1.00  9.00           C  
ANISOU 2961  C   LEU A1174      358   2220    841   -688   -382    537       C  
ATOM   2962  O   LEU A1174     -35.149  61.058 -15.512  1.00  9.25           O  
ANISOU 2962  O   LEU A1174      330   2389    793   -620   -386    507       O  
ATOM   2963  CB  LEU A1174     -37.916  62.340 -14.186  1.00  8.23           C  
ANISOU 2963  CB  LEU A1174      384   1686   1054   -628   -400    543       C  
ATOM   2964  CG  LEU A1174     -38.374  62.043 -15.606  1.00  8.43           C  
ANISOU 2964  CG  LEU A1174      394   1719   1089   -626   -463    550       C  
ATOM   2965  CD1 LEU A1174     -39.359  60.889 -15.599  1.00  7.99           C  
ANISOU 2965  CD1 LEU A1174      324   1555   1156   -500   -453    512       C  
ATOM   2966  CD2 LEU A1174     -38.983  63.279 -16.247  1.00  8.85           C  
ANISOU 2966  CD2 LEU A1174      517   1664   1182   -727   -541    608       C  
ATOM   2967  N   GLU A1175     -34.926  63.048 -14.544  1.00  9.55           N  
ANISOU 2967  N   GLU A1175      454   2340    833   -847   -412    600       N  
ATOM   2968  CA  GLU A1175     -33.782  63.484 -15.368  1.00 10.56           C  
ANISOU 2968  CA  GLU A1175      515   2725    770   -983   -447    656       C  
ATOM   2969  C   GLU A1175     -32.584  62.582 -15.107  1.00 10.86           C  
ANISOU 2969  C   GLU A1175      423   3033    669   -905   -387    619       C  
ATOM   2970  O   GLU A1175     -31.819  62.280 -16.027  1.00 11.67           O  
ANISOU 2970  O   GLU A1175      424   3389    618   -909   -389    628       O  
ATOM   2971  CB  GLU A1175     -33.411  64.931 -15.019  1.00 20.61           C  
ANISOU 2971  CB  GLU A1175     1869   3974   1988  -1193   -508    743       C  
ATOM   2972  CG  GLU A1175     -32.544  65.605 -16.065  1.00 39.00           C  
ANISOU 2972  CG  GLU A1175     4153   6526   4136  -1387   -572    831       C  
ATOM   2973  CD  GLU A1175     -33.216  65.746 -17.424  1.00 45.07           C  
ANISOU 2973  CD  GLU A1175     4953   7245   4925  -1406   -628    848       C  
ATOM   2974  OE1 GLU A1175     -34.460  65.839 -17.446  1.00 40.16           O  
ANISOU 2974  OE1 GLU A1175     4432   6355   4472  -1330   -653    819       O  
ATOM   2975  OE2 GLU A1175     -32.500  65.742 -18.457  1.00 40.89           O  
ANISOU 2975  OE2 GLU A1175     4338   6959   4237  -1492   -646    892       O  
ATOM   2976  N   LEU A1176     -32.435  62.157 -13.864  1.00 10.35           N  
ANISOU 2976  N   LEU A1176      363   2922    648   -823   -333    576       N  
ATOM   2977  CA  LEU A1176     -31.323  61.279 -13.473  1.00 10.69           C  
ANISOU 2977  CA  LEU A1176      293   3204    564   -724   -283    533       C  
ATOM   2978  C   LEU A1176     -31.464  59.884 -14.067  1.00 10.57           C  
ANISOU 2978  C   LEU A1176      240   3238    536   -513   -263    447       C  
ATOM   2979  O   LEU A1176     -30.472  59.219 -14.316  1.00 11.31           O  
ANISOU 2979  O   LEU A1176      231   3591    474   -420   -243    415       O  
ATOM   2980  CB  LEU A1176     -31.242  61.220 -11.953  1.00 10.17           C  
ANISOU 2980  CB  LEU A1176      270   3033    558   -694   -243    510       C  
ATOM   2981  CG  LEU A1176     -30.790  62.531 -11.310  1.00 10.63           C  
ANISOU 2981  CG  LEU A1176      374   3086    576   -897   -277    592       C  
ATOM   2982  CD1 LEU A1176     -30.376  62.299  -9.872  1.00 10.37           C  
ANISOU 2982  CD1 LEU A1176      359   3028    551   -852   -237    564       C  
ATOM   2983  CD2 LEU A1176     -29.656  63.202 -12.075  1.00 11.96           C  
ANISOU 2983  CD2 LEU A1176      444   3548    552  -1077   -324    680       C  
ATOM   2984  N   SER A1177     -32.684  59.454 -14.297  1.00  9.83           N  
ANISOU 2984  N   SER A1177      235   2903    594   -435   -278    413       N  
ATOM   2985  CA  SER A1177     -32.968  58.104 -14.816  1.00  9.78           C  
ANISOU 2985  CA  SER A1177      243   2886    586   -245   -286    334       C  
ATOM   2986  C   SER A1177     -32.453  57.929 -16.237  1.00 10.73           C  
ANISOU 2986  C   SER A1177      303   3218    553   -221   -317    334       C  
ATOM   2987  O   SER A1177     -32.421  56.796 -16.730  1.00 11.03           O  
ANISOU 2987  O   SER A1177      360   3293    536    -45   -334    262       O  
ATOM   2988  CB  SER A1177     -34.441  57.848 -14.813  1.00  8.99           C  
ANISOU 2988  CB  SER A1177      246   2489    680   -219   -312    325       C  
ATOM   2989  OG  SER A1177     -34.914  57.916 -13.479  1.00  8.30           O  
ANISOU 2989  OG  SER A1177      202   2233    715   -221   -271    323       O  
ATOM   2990  N   ARG A1178     -32.063  59.025 -16.873  1.00 11.62           N  
ANISOU 2990  N   ARG A1178      363   3463    587   -394   -334    414       N  
ATOM   2991  CA  ARG A1178     -31.572  58.990 -18.260  1.00 14.81           C  
ANISOU 2991  CA  ARG A1178      703   4092    831   -396   -358    428       C  
ATOM   2992  C   ARG A1178     -30.098  58.616 -18.315  1.00 20.42           C  
ANISOU 2992  C   ARG A1178     1263   5184   1309   -326   -314    414       C  
ATOM   2993  O   ARG A1178     -29.579  58.288 -19.389  1.00 42.83           O  
ANISOU 2993  O   ARG A1178     4034   8257   3982   -258   -317    403       O  
ATOM   2994  CB  ARG A1178     -31.817  60.356 -18.909  1.00 14.68           C  
ANISOU 2994  CB  ARG A1178      705   4051    821   -633   -405    532       C  
ATOM   2995  CG  ARG A1178     -33.262  60.835 -18.841  1.00 14.10           C  
ANISOU 2995  CG  ARG A1178      767   3620    967   -687   -454    548       C  
ATOM   2996  CD  ARG A1178     -33.554  62.026 -19.742  1.00 18.15           C  
ANISOU 2996  CD  ARG A1178     1325   4101   1470   -881   -524    637       C  
ATOM   2997  NE  ARG A1178     -34.967  62.122 -20.119  1.00 19.92           N  
ANISOU 2997  NE  ARG A1178     1659   4034   1875   -861   -579    631       N  
ATOM   2998  CZ  ARG A1178     -35.811  63.080 -19.730  1.00 31.39           C  
ANISOU 2998  CZ  ARG A1178     3205   5254   3465   -954   -621    673       C  
ATOM   2999  NH1 ARG A1178     -35.412  64.051 -18.922  1.00 52.35           N  
ANISOU 2999  NH1 ARG A1178     5890   7900   6100  -1078   -623    722       N  
ATOM   3000  NH2 ARG A1178     -37.070  63.052 -20.144  1.00 17.76           N  
ANISOU 3000  NH2 ARG A1178     1549   3307   1891   -911   -670    666       N  
ATOM   3001  N   SER A1179     -29.437  58.672 -17.176  1.00 25.93           N  
ANISOU 3001  N   SER A1179     1907   5956   1987   -334   -274    415       N  
ATOM   3002  CA  SER A1179     -28.046  58.207 -17.035  1.00 36.82           C  
ANISOU 3002  CA  SER A1179     3129   7705   3156   -237   -232    394       C  
ATOM   3003  C   SER A1179     -28.044  56.786 -16.472  1.00 41.17           C  
ANISOU 3003  C   SER A1179     3726   8196   3719     46   -216    270       C  
ATOM   3004  O   SER A1179     -29.117  56.174 -16.326  1.00 51.03           O  
ANISOU 3004  O   SER A1179     5128   9133   5128    139   -243    212       O  
ATOM   3005  CB  SER A1179     -27.291  59.150 -16.132  1.00 66.65           C  
ANISOU 3005  CB  SER A1179     6827  11600   6895   -432   -217    480       C  
ATOM   3006  OG  SER A1179     -27.596  60.509 -16.439  1.00 94.99           O  
ANISOU 3006  OG  SER A1179    10457  15113  10522   -710   -262    594       O  
ATOM   3007  N   ASP A1180     -26.870  56.314 -16.097  1.00 37.23           N  
ANISOU 3007  N   ASP A1180     3101   7989   3053    167   -182    238       N  
ATOM   3008  CA  ASP A1180     -26.753  55.002 -15.435  1.00 29.80           C  
ANISOU 3008  CA  ASP A1180     2221   6992   2107    437   -181    120       C  
ATOM   3009  C   ASP A1180     -26.746  55.220 -13.928  1.00 20.19           C  
ANISOU 3009  C   ASP A1180     1034   5630   1004    366   -161    133       C  
ATOM   3010  O   ASP A1180     -25.802  55.806 -13.369  1.00 57.00           O  
ANISOU 3010  O   ASP A1180     5565  10513   5577    263   -134    188       O  
ATOM   3011  CB  ASP A1180     -25.557  54.227 -15.972  1.00 36.96           C  
ANISOU 3011  CB  ASP A1180     2995   8290   2757    668   -167     59       C  
ATOM   3012  CG  ASP A1180     -25.568  52.799 -15.478  1.00 38.44           C  
ANISOU 3012  CG  ASP A1180     3301   8373   2931    975   -196    -74       C  
ATOM   3013  OD1 ASP A1180     -25.046  52.567 -14.390  1.00 44.55           O  
ANISOU 3013  OD1 ASP A1180     4048   9181   3699   1027   -181    -96       O  
ATOM   3014  OD2 ASP A1180     -26.133  51.948 -16.170  1.00 76.07           O  
ANISOU 3014  OD2 ASP A1180     8207  13001   7693   1147   -248   -151       O  
ATOM   3015  N   LEU A1181     -27.783  54.711 -13.296  1.00 13.27           N  
ANISOU 3015  N   LEU A1181      330   4400    311    419   -179     85       N  
ATOM   3016  CA  LEU A1181     -28.008  54.871 -11.840  1.00 12.32           C  
ANISOU 3016  CA  LEU A1181      273   4089    319    358   -158     92       C  
ATOM   3017  C   LEU A1181     -27.333  53.765 -11.025  1.00 12.75           C  
ANISOU 3017  C   LEU A1181      338   4212    294    574   -158      4       C  
ATOM   3018  O   LEU A1181     -27.460  53.764  -9.795  1.00 12.08           O  
ANISOU 3018  O   LEU A1181      312   3978    297    545   -142      2       O  
ATOM   3019  CB  LEU A1181     -29.517  54.849 -11.586  1.00 10.97           C  
ANISOU 3019  CB  LEU A1181      267   3526    374    308   -173     93       C  
ATOM   3020  CG  LEU A1181     -30.312  55.976 -12.240  1.00 10.52           C  
ANISOU 3020  CG  LEU A1181      221   3357    417    108   -183    176       C  
ATOM   3021  CD1 LEU A1181     -31.693  56.112 -11.588  1.00  9.33           C  
ANISOU 3021  CD1 LEU A1181      199   2856    488     54   -181    188       C  
ATOM   3022  CD2 LEU A1181     -29.537  57.291 -12.176  1.00 11.01           C  
ANISOU 3022  CD2 LEU A1181      178   3602    400    -94   -167    268       C  
ATOM   3023  N   SER A1182     -26.647  52.852 -11.690  1.00 13.96           N  
ANISOU 3023  N   SER A1182      447   4581    274    798   -180    -69       N  
ATOM   3024  CA  SER A1182     -26.214  51.598 -11.030  1.00 15.55           C  
ANISOU 3024  CA  SER A1182      718   4782    404   1053   -208   -174       C  
ATOM   3025  C   SER A1182     -25.307  51.938  -9.849  1.00 15.02           C  
ANISOU 3025  C   SER A1182      551   4859    296   1008   -172   -150       C  
ATOM   3026  O   SER A1182     -25.464  51.369  -8.755  1.00 14.14           O  
ANISOU 3026  O   SER A1182      553   4567    252   1078   -186   -195       O  
ATOM   3027  CB  SER A1182     -25.515  50.696 -11.991  1.00 19.26           C  
ANISOU 3027  CB  SER A1182     1154   5499    664   1320   -243   -259       C  
ATOM   3028  OG  SER A1182     -24.390  51.373 -12.547  1.00 22.10           O  
ANISOU 3028  OG  SER A1182     1272   6283    842   1278   -195   -206       O  
ATOM   3029  N   LYS A1183     -24.377  52.859 -10.061  1.00 17.86           N  
ANISOU 3029  N   LYS A1183      706   5538    540    875   -136    -71       N  
ATOM   3030  CA  LYS A1183     -23.423  53.199  -8.984  1.00 21.57           C  
ANISOU 3030  CA  LYS A1183     1068   6174    950    819   -116    -38       C  
ATOM   3031  C   LYS A1183     -24.126  53.951  -7.872  1.00 15.64           C  
ANISOU 3031  C   LYS A1183      431   5115    394    601   -103     19       C  
ATOM   3032  O   LYS A1183     -23.690  53.843  -6.730  1.00 16.00           O  
ANISOU 3032  O   LYS A1183      488   5151    440    613   -101     10       O  
ATOM   3033  CB  LYS A1183     -22.207  53.934  -9.553  1.00 38.55           C  
ANISOU 3033  CB  LYS A1183     2960   8780   2903    721    -95     43       C  
ATOM   3034  CG  LYS A1183     -21.422  53.111 -10.570  1.00 66.70           C  
ANISOU 3034  CG  LYS A1183     6396  12700   6245    984    -96    -24       C  
ATOM   3035  CD  LYS A1183     -20.652  53.936 -11.587  1.00 83.06           C  
ANISOU 3035  CD  LYS A1183     8230  15185   8144    843    -67     76       C  
ATOM   3036  CE  LYS A1183     -20.457  53.234 -12.919  1.00 81.81           C  
ANISOU 3036  CE  LYS A1183     8017  15249   7818   1080    -64      9       C  
ATOM   3037  NZ  LYS A1183     -19.578  52.045 -12.812  1.00 77.93           N  
ANISOU 3037  NZ  LYS A1183     7460  15010   7137   1450    -72   -108       N  
ATOM   3038  N   PHE A1184     -25.204  54.643  -8.196  1.00 13.33           N  
ANISOU 3038  N   PHE A1184      230   4578    255    431    -98     70       N  
ATOM   3039  CA  PHE A1184     -26.023  55.348  -7.202  1.00 12.05           C  
ANISOU 3039  CA  PHE A1184      193   4109    274    259    -83    116       C  
ATOM   3040  C   PHE A1184     -26.605  54.312  -6.255  1.00 11.29           C  
ANISOU 3040  C   PHE A1184      253   3759    278    416    -84     33       C  
ATOM   3041  O   PHE A1184     -26.580  54.493  -5.004  1.00 10.86           O  
ANISOU 3041  O   PHE A1184      257   3589    278    366    -67     42       O  
ATOM   3042  CB  PHE A1184     -27.133  56.121  -7.920  1.00 11.29           C  
ANISOU 3042  CB  PHE A1184      163   3816    307    108    -86    170       C  
ATOM   3043  CG  PHE A1184     -27.705  57.298  -7.175  1.00 10.54           C  
ANISOU 3043  CG  PHE A1184      150   3514    338   -101    -77    244       C  
ATOM   3044  CD1 PHE A1184     -27.421  57.521  -5.832  1.00 10.34           C  
ANISOU 3044  CD1 PHE A1184      171   3423    334   -142    -63    252       C  
ATOM   3045  CD2 PHE A1184     -28.570  58.171  -7.820  1.00 10.13           C  
ANISOU 3045  CD2 PHE A1184      149   3320    379   -240    -91    300       C  
ATOM   3046  CE1 PHE A1184     -27.965  58.605  -5.165  1.00  9.84           C  
ANISOU 3046  CE1 PHE A1184      208   3160    369   -309    -62    311       C  
ATOM   3047  CE2 PHE A1184     -29.123  59.250  -7.143  1.00  9.65           C  
ANISOU 3047  CE2 PHE A1184      187   3059    420   -398    -94    357       C  
ATOM   3048  CZ  PHE A1184     -28.812  59.470  -5.818  1.00  9.54           C  
ANISOU 3048  CZ  PHE A1184      225   2985    414   -428    -79    361       C  
ATOM   3049  N   ARG A1185     -27.095  53.227  -6.838  1.00 11.30           N  
ANISOU 3049  N   ARG A1185      332   3673    286    596   -113    -42       N  
ATOM   3050  CA  ARG A1185     -27.738  52.138  -6.073  1.00 10.78           C  
ANISOU 3050  CA  ARG A1185      438   3352    304    730   -135   -112       C  
ATOM   3051  C   ARG A1185     -26.705  51.370  -5.266  1.00 11.56           C  
ANISOU 3051  C   ARG A1185      528   3583    278    895   -154   -176       C  
ATOM   3052  O   ARG A1185     -27.020  50.923  -4.156  1.00 11.07           O  
ANISOU 3052  O   ARG A1185      591   3326    288    918   -157   -200       O  
ATOM   3053  CB  ARG A1185     -28.476  51.149  -6.977  1.00 10.87           C  
ANISOU 3053  CB  ARG A1185      559   3237    333    866   -191   -169       C  
ATOM   3054  CG  ARG A1185     -29.507  51.794  -7.885  1.00 10.25           C  
ANISOU 3054  CG  ARG A1185      486   3037    370    725   -186   -111       C  
ATOM   3055  CD  ARG A1185     -30.343  50.737  -8.560  1.00 10.34           C  
ANISOU 3055  CD  ARG A1185      637   2875    415    842   -256   -161       C  
ATOM   3056  NE  ARG A1185     -31.117  51.325  -9.629  1.00 10.03           N  
ANISOU 3056  NE  ARG A1185      577   2783    450    731   -262   -110       N  
ATOM   3057  CZ  ARG A1185     -32.264  51.956  -9.466  1.00  9.11           C  
ANISOU 3057  CZ  ARG A1185      492   2457    511    569   -241    -44       C  
ATOM   3058  NH1 ARG A1185     -32.783  52.078  -8.257  1.00  8.43           N  
ANISOU 3058  NH1 ARG A1185      457   2202    543    501   -203    -21       N  
ATOM   3059  NH2 ARG A1185     -32.889  52.451 -10.519  1.00  9.00           N  
ANISOU 3059  NH2 ARG A1185      458   2413    548    488   -260     -4       N  
ATOM   3060  N   GLU A1186     -25.505  51.213  -5.808  1.00 12.86           N  
ANISOU 3060  N   GLU A1186      546   4087    253   1013   -167   -201       N  
ATOM   3061  CA  GLU A1186     -24.419  50.529  -5.089  1.00 13.86           C  
ANISOU 3061  CA  GLU A1186      638   4384    241   1190   -191   -262       C  
ATOM   3062  C   GLU A1186     -24.111  51.290  -3.800  1.00 13.38           C  
ANISOU 3062  C   GLU A1186      550   4299    235   1021   -156   -201       C  
ATOM   3063  O   GLU A1186     -23.918  50.695  -2.732  1.00 13.38           O  
ANISOU 3063  O   GLU A1186      640   4206    235   1111   -176   -246       O  
ATOM   3064  CB  GLU A1186     -23.144  50.484  -5.936  1.00 21.42           C  
ANISOU 3064  CB  GLU A1186     1385   5779    973   1319   -195   -276       C  
ATOM   3065  CG  GLU A1186     -22.841  49.146  -6.591  1.00 38.39           C  
ANISOU 3065  CG  GLU A1186     3594   8016   2977   1654   -258   -397       C  
ATOM   3066  CD  GLU A1186     -21.672  49.205  -7.573  1.00 53.36           C  
ANISOU 3066  CD  GLU A1186     5257  10378   4638   1786   -245   -404       C  
ATOM   3067  OE1 GLU A1186     -20.796  50.086  -7.402  1.00 47.93           O  
ANISOU 3067  OE1 GLU A1186     4343   9993   3873   1643   -199   -320       O  
ATOM   3068  OE2 GLU A1186     -21.649  48.391  -8.529  1.00 76.11           O  
ANISOU 3068  OE2 GLU A1186     8184  13329   7403   2025   -286   -487       O  
ATOM   3069  N   ASN A1187     -24.041  52.594  -3.918  1.00 13.14           N  
ANISOU 3069  N   ASN A1187      412   4344    233    779   -116    -98       N  
ATOM   3070  CA  ASN A1187     -23.802  53.509  -2.781  1.00 12.78           C  
ANISOU 3070  CA  ASN A1187      364   4257    234    586    -96    -28       C  
ATOM   3071  C   ASN A1187     -24.838  53.318  -1.685  1.00 11.50           C  
ANISOU 3071  C   ASN A1187      410   3716    242    561    -79    -47       C  
ATOM   3072  O   ASN A1187     -24.473  53.263  -0.499  1.00 11.50           O  
ANISOU 3072  O   ASN A1187      457   3673    238    559    -81    -53       O  
ATOM   3073  CB  ASN A1187     -23.850  54.953  -3.286  1.00 12.73           C  
ANISOU 3073  CB  ASN A1187      272   4318    245    319    -80     86       C  
ATOM   3074  CG  ASN A1187     -22.665  55.269  -4.169  1.00 14.27           C  
ANISOU 3074  CG  ASN A1187      238   4935    247    293    -95    133       C  
ATOM   3075  OD1 ASN A1187     -21.688  54.519  -4.196  1.00 15.45           O  
ANISOU 3075  OD1 ASN A1187      270   5356    245    475   -108     83       O  
ATOM   3076  ND2 ASN A1187     -22.750  56.370  -4.894  1.00 14.43           N  
ANISOU 3076  ND2 ASN A1187      194   5024    261     74    -96    230       N  
ATOM   3077  N   CYS A1188     -26.094  53.210  -2.079  1.00 10.57           N  
ANISOU 3077  N   CYS A1188      405   3347    262    543    -65    -53       N  
ATOM   3078  CA  CYS A1188     -27.219  53.036  -1.145  1.00  9.52           C  
ANISOU 3078  CA  CYS A1188      448   2879    289    512    -40    -59       C  
ATOM   3079  C   CYS A1188     -27.040  51.767  -0.319  1.00  9.75           C  
ANISOU 3079  C   CYS A1188      586   2830    285    688    -71   -137       C  
ATOM   3080  O   CYS A1188     -27.168  51.789   0.914  1.00  9.40           O  
ANISOU 3080  O   CYS A1188      635   2648    288    651    -51   -132       O  
ATOM   3081  CB  CYS A1188     -28.495  52.952  -1.961  1.00  8.87           C  
ANISOU 3081  CB  CYS A1188      428   2613    329    490    -34    -51       C  
ATOM   3082  SG  CYS A1188     -29.073  54.582  -2.490  1.00  8.38           S  
ANISOU 3082  SG  CYS A1188      312   2517    355    259      1     47       S  
ATOM   3083  N   LYS A1189     -26.780  50.665  -1.006  1.00 10.43           N  
ANISOU 3083  N   LYS A1189      685   2992    283    883   -129   -210       N  
ATOM   3084  CA  LYS A1189     -26.608  49.362  -0.340  1.00 10.88           C  
ANISOU 3084  CA  LYS A1189      881   2961    290   1071   -188   -292       C  
ATOM   3085  C   LYS A1189     -25.475  49.431   0.671  1.00 11.45           C  
ANISOU 3085  C   LYS A1189      904   3181    265   1108   -191   -304       C  
ATOM   3086  O   LYS A1189     -25.655  49.033   1.821  1.00 11.21           O  
ANISOU 3086  O   LYS A1189     1007   2979    273   1116   -198   -320       O  
ATOM   3087  CB  LYS A1189     -26.298  48.283  -1.372  1.00 11.89           C  
ANISOU 3087  CB  LYS A1189     1030   3188    297   1299   -268   -375       C  
ATOM   3088  CG  LYS A1189     -27.418  48.029  -2.368  1.00 11.48           C  
ANISOU 3088  CG  LYS A1189     1060   2971    331   1277   -290   -369       C  
ATOM   3089  CD  LYS A1189     -27.121  46.871  -3.292  1.00 12.65           C  
ANISOU 3089  CD  LYS A1189     1281   3180    343   1523   -388   -460       C  
ATOM   3090  CE  LYS A1189     -28.265  46.501  -4.207  1.00 12.37           C  
ANISOU 3090  CE  LYS A1189     1361   2947    389   1497   -434   -454       C  
ATOM   3091  NZ  LYS A1189     -27.890  45.338  -5.036  1.00 13.72           N  
ANISOU 3091  NZ  LYS A1189     1641   3166    403   1757   -548   -552       N  
ATOM   3092  N   LYS A1190     -24.333  49.937   0.232  1.00 12.32           N  
ANISOU 3092  N   LYS A1190      818   3617    244   1119   -190   -289       N  
ATOM   3093  CA  LYS A1190     -23.138  50.048   1.092  1.00 13.13           C  
ANISOU 3093  CA  LYS A1190      836   3915    235   1148   -204   -290       C  
ATOM   3094  C   LYS A1190     -23.456  50.928   2.289  1.00 12.23           C  
ANISOU 3094  C   LYS A1190      787   3629    232    934   -160   -220       C  
ATOM   3095  O   LYS A1190     -23.031  50.605   3.418  1.00 12.45           O  
ANISOU 3095  O   LYS A1190      883   3616    232    977   -181   -243       O  
ATOM   3096  CB  LYS A1190     -21.951  50.655   0.329  1.00 17.86           C  
ANISOU 3096  CB  LYS A1190     1177   4927    680   1134   -203   -250       C  
ATOM   3097  CG  LYS A1190     -21.363  49.812  -0.801  1.00 23.71           C  
ANISOU 3097  CG  LYS A1190     1823   5924   1262   1386   -242   -324       C  
ATOM   3098  CD  LYS A1190     -19.928  50.201  -1.158  1.00 31.85           C  
ANISOU 3098  CD  LYS A1190     2578   7425   2096   1414   -244   -291       C  
ATOM   3099  CE  LYS A1190     -19.552  49.863  -2.588  1.00 41.23           C  
ANISOU 3099  CE  LYS A1190     3628   8897   3138   1579   -247   -325       C  
ATOM   3100  NZ  LYS A1190     -20.058  50.874  -3.554  1.00 45.65           N  
ANISOU 3100  NZ  LYS A1190     4109   9477   3758   1349   -197   -233       N  
ATOM   3101  N   ARG A1191     -24.180  52.013   2.037  1.00 11.38           N  
ANISOU 3101  N   ARG A1191      669   3418    234    723   -106   -142       N  
ATOM   3102  CA  ARG A1191     -24.514  52.988   3.095  1.00 10.71           C  
ANISOU 3102  CA  ARG A1191      659   3169    238    528    -67    -77       C  
ATOM   3103  C   ARG A1191     -25.444  52.363   4.102  1.00  9.95           C  
ANISOU 3103  C   ARG A1191      765   2763    249    571    -46   -113       C  
ATOM   3104  O   ARG A1191     -25.191  52.538   5.320  1.00  9.95           O  
ANISOU 3104  O   ARG A1191      840   2692    245    530    -41   -105       O  
ATOM   3105  CB  ARG A1191     -25.177  54.230   2.487  1.00 10.14           C  
ANISOU 3105  CB  ARG A1191      561   3041    251    329    -30      2       C  
ATOM   3106  CG  ARG A1191     -25.681  55.251   3.502  1.00  9.58           C  
ANISOU 3106  CG  ARG A1191      604   2766    267    159      2     59       C  
ATOM   3107  CD  ARG A1191     -24.536  55.943   4.186  1.00 10.36           C  
ANISOU 3107  CD  ARG A1191      653   3023    260     52    -36    107       C  
ATOM   3108  NE  ARG A1191     -24.945  56.687   5.358  1.00  9.99           N  
ANISOU 3108  NE  ARG A1191      762   2758    275    -61    -18    139       N  
ATOM   3109  CZ  ARG A1191     -24.771  56.296   6.621  1.00  9.99           C  
ANISOU 3109  CZ  ARG A1191      869   2659    267    -12    -16    109       C  
ATOM   3110  NH1 ARG A1191     -24.196  55.139   6.920  1.00 10.34           N  
ANISOU 3110  NH1 ARG A1191      888   2789    249    149    -39     45       N  
ATOM   3111  NH2 ARG A1191     -25.175  57.086   7.600  1.00  9.78           N  
ANISOU 3111  NH2 ARG A1191      990   2439    284   -116      1    142       N  
ATOM   3112  N   ALA A1192     -26.510  51.706   3.614  1.00  9.42           N  
ANISOU 3112  N   ALA A1192      786   2522    272    632    -37   -142       N  
ATOM   3113  CA  ALA A1192     -27.555  51.105   4.462  1.00  8.85           C  
ANISOU 3113  CA  ALA A1192      895   2165    302    642    -15   -156       C  
ATOM   3114  C   ALA A1192     -26.942  50.061   5.388  1.00  9.43           C  
ANISOU 3114  C   ALA A1192     1067   2220    292    778    -68   -217       C  
ATOM   3115  O   ALA A1192     -27.109  50.086   6.676  1.00  9.23           O  
ANISOU 3115  O   ALA A1192     1157   2053    297    731    -43   -207       O  
ATOM   3116  CB  ALA A1192     -28.612  50.445   3.621  1.00  8.57           C  
ANISOU 3116  CB  ALA A1192      912   2000    343    683    -26   -168       C  
ATOM   3117  N   MET A1193     -26.051  49.265   4.821  1.00 10.32           N  
ANISOU 3117  N   MET A1193     1130   2511    278    953   -145   -281       N  
ATOM   3118  CA  MET A1193     -25.375  48.196   5.590  1.00 11.43           C  
ANISOU 3118  CA  MET A1193     1374   2650    319   1122   -219   -352       C  
ATOM   3119  C   MET A1193     -24.391  48.837   6.553  1.00 11.41           C  
ANISOU 3119  C   MET A1193     1304   2776    256   1067   -208   -329       C  
ATOM   3120  O   MET A1193     -24.346  48.349   7.742  1.00 11.51           O  
ANISOU 3120  O   MET A1193     1461   2650    261   1097   -231   -351       O  
ATOM   3121  CB  MET A1193     -24.649  47.219   4.651  1.00 19.00           C  
ANISOU 3121  CB  MET A1193     2295   3786   1138   1361   -311   -435       C  
ATOM   3122  CG  MET A1193     -25.571  46.444   3.707  1.00 25.41           C  
ANISOU 3122  CG  MET A1193     3214   4449   1989   1430   -352   -465       C  
ATOM   3123  SD  MET A1193     -24.658  45.402   2.500  1.00 57.75           S  
ANISOU 3123  SD  MET A1193     7278   8771   5890   1743   -465   -572       S  
ATOM   3124  CE  MET A1193     -25.942  45.063   1.295  1.00 73.10           C  
ANISOU 3124  CE  MET A1193     9320  10529   7924   1711   -486   -564       C  
ATOM   3125  N   SER A1194     -23.695  49.892   6.124  1.00 11.62           N  
ANISOU 3125  N   SER A1194     1138   3037    239    969   -184   -276       N  
ATOM   3126  CA  SER A1194     -22.720  50.585   6.970  1.00 12.53           C  
ANISOU 3126  CA  SER A1194     1183   3291    287    885   -191   -238       C  
ATOM   3127  C   SER A1194     -23.426  51.167   8.192  1.00 11.24           C  
ATOM   3128  O   SER A1194     -22.946  50.998   9.336  1.00 12.14           O  
ATOM   3129  CB  SER A1194     -21.990  51.667   6.211  1.00 14.83           C  
ANISOU 3129  CB  SER A1194     1255   3866    514    760   -184   -167       C  
ATOM   3130  OG  SER A1194     -21.377  52.579   7.120  1.00 20.29           O  
ANISOU 3130  OG  SER A1194     1924   4608   1177    598   -192   -101       O  
ATOM   3131  N   PHE A1195     -24.491  51.919   7.928  1.00 10.32           N  
ATOM   3132  CA  PHE A1195     -25.314  52.552   8.974  1.00  9.64           C  
ATOM   3133  C   PHE A1195     -25.736  51.540  10.019  1.00  9.56           C  
ATOM   3134  O   PHE A1195     -25.642  51.824  11.222  1.00  9.60           O  
ATOM   3135  CB  PHE A1195     -26.569  53.207   8.392  1.00  8.84           C  
ATOM   3136  CG  PHE A1195     -27.411  53.952   9.401  1.00  8.39           C  
ATOM   3137  CD1 PHE A1195     -28.377  53.293  10.160  1.00  8.08           C  
ATOM   3138  CD2 PHE A1195     -27.226  55.311   9.611  1.00  8.49           C  
ATOM   3139  CE1 PHE A1195     -29.130  53.974  11.110  1.00  7.90           C  
ATOM   3140  CE2 PHE A1195     -27.982  55.992  10.558  1.00  8.30           C  
ATOM   3141  CZ  PHE A1195     -28.932  55.325  11.309  1.00  8.01           C  
ATOM   3142  N   SER A1196     -26.237  50.409   9.567  1.00 11.16           N  
ATOM   3143  CA  SER A1196     -26.749  49.325  10.430  1.00 25.01           C  
ATOM   3144  C   SER A1196     -25.673  48.872  11.412  1.00 23.09           C  
ATOM   3145  O   SER A1196     -25.948  48.756  12.628  1.00 29.83           O  
ATOM   3146  CB  SER A1196     -27.230  48.154   9.609  1.00 48.27           C  
ATOM   3147  OG  SER A1196     -28.303  48.547   8.776  1.00 80.12           O  
ATOM   3148  N   GLU A 238     -24.467  48.712  10.895  1.00 20.88           N  
ANISOU 3148  N   GLU A 238     2928   3510   1495    928   -186   -308       N  
ATOM   3149  CA  GLU A 238     -23.342  48.163  11.659  1.00 30.95           C  
ANISOU 3149  CA  GLU A 238     4232   4878   2648   1047   -270   -355       C  
ATOM   3150  C   GLU A 238     -22.832  49.196  12.653  1.00 14.27           C  
ANISOU 3150  C   GLU A 238     2100   2797    524    903   -242   -300       C  
ATOM   3151  O   GLU A 238     -22.403  48.805  13.767  1.00 12.50           O  
ANISOU 3151  O   GLU A 238     1991   2510    247    943   -285   -322       O  
ATOM   3152  CB  GLU A 238     -22.240  47.657  10.721  1.00 60.07           C  
ANISOU 3152  CB  GLU A 238     7764   8854   6205   1236   -354   -411       C  
ATOM   3153  CG  GLU A 238     -22.553  46.311  10.076  1.00 86.16           C  
ANISOU 3153  CG  GLU A 238    11175  12086   9475   1441   -428   -492       C  
ATOM   3154  CD  GLU A 238     -22.919  45.183  11.033  1.00115.63           C  
ANISOU 3154  CD  GLU A 238    15172  15562  13197   1525   -496   -539       C  
ATOM   3155  OE1 GLU A 238     -22.002  44.471  11.503  1.00106.06           O  
ANISOU 3155  OE1 GLU A 238    14011  14424  11862   1699   -595   -603       O  
ATOM   3156  OE2 GLU A 238     -24.123  45.017  11.307  1.00111.93           O  
ANISOU 3156  OE2 GLU A 238    14856  14832  12837   1411   -455   -506       O  
ATOM   3157  N   GLN A 239     -22.829  50.467  12.244  1.00 11.69           N  
ANISOU 3157  N   GLN A 239     1646   2561    232    741   -189   -231       N  
ATOM   3158  CA  GLN A 239     -22.431  51.562  13.145  1.00 11.77           C  
ANISOU 3158  CA  GLN A 239     1673   2570    229    580   -178   -170       C  
ATOM   3159  C   GLN A 239     -23.285  51.521  14.399  1.00 11.25           C  
ANISOU 3159  C   GLN A 239     1833   2211    229    531   -125   -168       C  
ATOM   3160  O   GLN A 239     -22.756  51.611  15.521  1.00 13.16           O  
ANISOU 3160  O   GLN A 239     2166   2417    416    509   -158   -165       O  
ATOM   3161  CB  GLN A 239     -22.557  52.930  12.477  1.00 13.59           C  
ANISOU 3161  CB  GLN A 239     1792   2875    494    400   -141    -92       C  
ATOM   3162  CG  GLN A 239     -21.571  53.152  11.334  1.00 23.98           C  
ANISOU 3162  CG  GLN A 239     2867   4522   1719    405   -193    -72       C  
ATOM   3163  CD  GLN A 239     -21.627  54.559  10.782  1.00 35.00           C  
ANISOU 3163  CD  GLN A 239     4183   5979   3133    194   -177     17       C  
ATOM   3164  OE1 GLN A 239     -22.440  55.385  11.202  1.00 99.43           O  
ANISOU 3164  OE1 GLN A 239    12478  13920  11377     66   -131     55       O  
ATOM   3165  NE2 GLN A 239     -20.745  54.854   9.844  1.00 25.13           N  
ANISOU 3165  NE2 GLN A 239     2719   5036   1790    161   -222     55       N  
ATOM   3166  N   VAL A 240     -24.583  51.407  14.192  1.00 10.47           N  
ANISOU 3166  N   VAL A 240     1813   1923    239    511    -46   -163       N  
ATOM   3167  CA  VAL A 240     -25.586  51.410  15.281  1.00 10.09           C  
ANISOU 3167  CA  VAL A 240     1956   1621    254    460     27   -149       C  
ATOM   3168  C   VAL A 240     -25.355  50.227  16.199  1.00 10.56           C  
ANISOU 3168  C   VAL A 240     2161   1594    256    562    -23   -197       C  
ATOM   3169  O   VAL A 240     -25.442  50.370  17.420  1.00 10.70           O  
ANISOU 3169  O   VAL A 240     2323   1485    256    518     -1   -185       O  
ATOM   3170  CB  VAL A 240     -26.997  51.377  14.670  1.00  9.41           C  
ANISOU 3170  CB  VAL A 240     1877   1411    285    433    113   -129       C  
ATOM   3171  CG1 VAL A 240     -28.059  51.099  15.720  1.00  9.31           C  
ANISOU 3171  CG1 VAL A 240     2034   1182    319    405    190   -114       C  
ATOM   3172  CG2 VAL A 240     -27.303  52.666  13.922  1.00  9.01           C  
ANISOU 3172  CG2 VAL A 240     1719   1412    291    328    162    -80       C  
ATOM   3173  N   SER A 241     -25.073  49.080  15.610  1.00 11.23           N  
ANISOU 3173  N   SER A 241     2228   1736    302    703   -100   -251       N  
ATOM   3174  CA  SER A 241     -24.855  47.819  16.350  1.00 12.95           C  
ANISOU 3174  CA  SER A 241     2609   1857    453    819   -178   -303       C  
ATOM   3175  C   SER A 241     -23.680  47.995  17.296  1.00 12.22           C  
ANISOU 3175  C   SER A 241     2536   1844    260    842   -242   -317       C  
ATOM   3176  O   SER A 241     -23.753  47.558  18.463  1.00 12.51           O  
ANISOU 3176  O   SER A 241     2755   1729    267    843   -258   -325       O  
ATOM   3177  CB  SER A 241     -24.549  46.672  15.407  1.00 16.15           C  
ANISOU 3177  CB  SER A 241     2992   2338    807    995   -279   -368       C  
ATOM   3178  OG  SER A 241     -25.689  46.290  14.658  1.00 25.14           O  
ANISOU 3178  OG  SER A 241     4160   3362   2029    972   -246   -355       O  
ATOM   3179  N   ALA A 242     -22.610  48.602  16.784  1.00 12.59           N  
ANISOU 3179  N   ALA A 242     2395   2139    248    852   -283   -313       N  
ATOM   3180  CA  ALA A 242     -21.379  48.828  17.567  1.00 15.59           C  
ANISOU 3180  CA  ALA A 242     2754   2646    524    863   -359   -314       C  
ATOM   3181  C   ALA A 242     -21.673  49.757  18.737  1.00 14.42           C  
ANISOU 3181  C   ALA A 242     2731   2341    405    693   -302   -258       C  
ATOM   3182  O   ALA A 242     -21.269  49.453  19.892  1.00 17.53           O  
ANISOU 3182  O   ALA A 242     3264   2656    739    712   -350   -273       O  
ATOM   3183  CB  ALA A 242     -20.290  49.422  16.703  1.00 17.25           C  
ANISOU 3183  CB  ALA A 242     2707   3179    664    864   -405   -294       C  
ATOM   3184  N   LYS A 243     -22.334  50.872  18.422  1.00 12.42           N  
ANISOU 3184  N   LYS A 243     2441   2047    231    543   -212   -200       N  
ATOM   3185  CA  LYS A 243     -22.647  51.917  19.419  1.00 12.28           C  
ANISOU 3185  CA  LYS A 243     2551   1883    228    395   -160   -149       C  
ATOM   3186  C   LYS A 243     -23.456  51.316  20.554  1.00 13.94           C  
ANISOU 3186  C   LYS A 243     2989   1847    458    420   -107   -168       C  
ATOM   3187  O   LYS A 243     -23.172  51.660  21.758  1.00 13.39           O  
ANISOU 3187  O   LYS A 243     3063   1686    335    369   -121   -156       O  
ATOM   3188  CB  LYS A 243     -23.412  53.084  18.782  1.00 11.65           C  
ANISOU 3188  CB  LYS A 243     2422   1773    231    271    -76    -96       C  
ATOM   3189  CG  LYS A 243     -22.593  53.893  17.789  1.00 13.44           C  
ANISOU 3189  CG  LYS A 243     2449   2234    423    194   -134    -55       C  
ATOM   3190  CD  LYS A 243     -23.248  55.160  17.314  1.00 16.49           C  
ANISOU 3190  CD  LYS A 243     2831   2564    870     57    -79      0       C  
ATOM   3191  CE  LYS A 243     -22.400  55.868  16.274  1.00 28.94           C  
ANISOU 3191  CE  LYS A 243     4210   4386   2399    -36   -149     51       C  
ATOM   3192  NZ  LYS A 243     -22.740  57.310  16.185  1.00 51.86           N  
ANISOU 3192  NZ  LYS A 243     7176   7209   5319   -206   -143    118       N  
ATOM   3193  N   ARG A 244     -24.368  50.416  20.198  1.00 14.26           N  
ANISOU 3193  N   ARG A 244     3067   1792    558    488    -63   -192       N  
ATOM   3194  CA  ARG A 244     -25.222  49.716  21.186  1.00 17.85           C  
ANISOU 3194  CA  ARG A 244     3725   2032   1022    495    -14   -197       C  
ATOM   3195  C   ARG A 244     -24.367  48.817  22.057  1.00 18.96           C  
ANISOU 3195  C   ARG A 244     3988   2153   1062    579   -122   -239       C  
ATOM   3196  O   ARG A 244     -24.514  48.824  23.286  1.00 16.77           O  
ANISOU 3196  O   ARG A 244     3886   1737    748    538   -102   -229       O  
ATOM   3197  CB  ARG A 244     -26.230  48.842  20.421  1.00 26.14           C  
ANISOU 3197  CB  ARG A 244     4766   3023   2144    535     18   -202       C  
ATOM   3198  CG  ARG A 244     -27.518  49.540  20.000  1.00 37.75           C  
ANISOU 3198  CG  ARG A 244     6187   4433   3721    444    151   -150       C  
ATOM   3199  CD  ARG A 244     -28.664  48.569  19.728  1.00 41.09           C  
ANISOU 3199  CD  ARG A 244     6659   4752   4199    447    183   -136       C  
ATOM   3200  NE  ARG A 244     -28.875  48.215  18.326  1.00 31.81           N  
ANISOU 3200  NE  ARG A 244     5353   3653   3078    487    149   -146       N  
ATOM   3201  CZ  ARG A 244     -29.929  48.579  17.586  1.00 45.65           C  
ANISOU 3201  CZ  ARG A 244     7018   5397   4929    429    231   -104       C  
ATOM   3202  NH1 ARG A 244     -30.904  49.320  18.095  1.00 40.39           N  
ANISOU 3202  NH1 ARG A 244     6366   4662   4317    343    358    -51       N  
ATOM   3203  NH2 ARG A 244     -30.002  48.195  16.320  1.00 52.72           N  
ANISOU 3203  NH2 ARG A 244     7810   6360   5860    471    182   -119       N  
ATOM   3204  N   LYS A 245     -23.506  48.032  21.410  1.00 18.77           N  
ANISOU 3204  N   LYS A 245     3878   2270    984    710   -239   -291       N  
ATOM   3205  CA  LYS A 245     -22.665  47.050  22.135  1.00 21.24           C  
ANISOU 3205  CA  LYS A 245     4308   2571   1191    829   -364   -343       C  
ATOM   3206  C   LYS A 245     -21.785  47.794  23.132  1.00 18.78           C  
ANISOU 3206  C   LYS A 245     4021   2301    812    769   -396   -324       C  
ATOM   3207  O   LYS A 245     -21.634  47.318  24.288  1.00 19.52           O  
ANISOU 3207  O   LYS A 245     4305   2264    846    784   -439   -338       O  
ATOM   3208  CB  LYS A 245     -21.806  46.247  21.155  1.00 31.46           C  
ANISOU 3208  CB  LYS A 245     5477   4053   2423   1013   -484   -407       C  
ATOM   3209  CG  LYS A 245     -22.584  45.465  20.102  1.00 55.64           C  
ANISOU 3209  CG  LYS A 245     8535   7070   5534   1085   -481   -431       C  
ATOM   3210  CD  LYS A 245     -23.546  44.457  20.694  1.00 67.01           C  
ANISOU 3210  CD  LYS A 245    10225   8248   6987   1075   -489   -433       C  
ATOM   3211  CE  LYS A 245     -22.838  43.284  21.343  1.00 85.38           C  
ANISOU 3211  CE  LYS A 245    12732  10514   9194   1228   -644   -498       C  
ATOM   3212  NZ  LYS A 245     -23.790  42.228  21.761  1.00117.39           N  
ANISOU 3212  NZ  LYS A 245    17039  14314  13248   1201   -675   -490       N  
ATOM   3213  N   VAL A 246     -21.263  48.946  22.716  1.00 16.92           N  
ANISOU 3213  N   VAL A 246     3616   2229    582    683   -384   -284       N  
ATOM   3214  CA  VAL A 246     -20.388  49.769  23.587  1.00 19.26           C  
ANISOU 3214  CA  VAL A 246     3934   2575    809    595   -434   -251       C  
ATOM   3215  C   VAL A 246     -21.130  50.255  24.817  1.00 18.71           C  
ANISOU 3215  C   VAL A 246     4094   2258    754    486   -356   -222       C  
ATOM   3216  O   VAL A 246     -20.658  49.974  25.976  1.00 21.03           O  
ANISOU 3216  O   VAL A 246     4546   2472    972    497   -418   -233       O  
ATOM   3217  CB  VAL A 246     -19.744  50.943  22.829  1.00 20.62           C  
ANISOU 3217  CB  VAL A 246     3892   2966    974    489   -451   -198       C  
ATOM   3218  CG1 VAL A 246     -19.150  51.974  23.779  1.00 20.10           C  
ANISOU 3218  CG1 VAL A 246     3900   2885    849    343   -496   -143       C  
ATOM   3219  CG2 VAL A 246     -18.678  50.438  21.864  1.00 26.36           C  
ANISOU 3219  CG2 VAL A 246     4382   3995   1637    611   -548   -225       C  
ATOM   3220  N   VAL A 247     -22.254  50.959  24.591  1.00 16.45           N  
ANISOU 3220  N   VAL A 247     3830   1864    554    396   -225   -186       N  
ATOM   3221  CA  VAL A 247     -23.033  51.515  25.720  1.00 19.69           C  
ANISOU 3221  CA  VAL A 247     4451   2063    966    315   -134   -159       C  
ATOM   3222  C   VAL A 247     -23.563  50.405  26.622  1.00 22.72           C  
ANISOU 3222  C   VAL A 247     5024   2282   1327    374   -111   -185       C  
ATOM   3223  O   VAL A 247     -23.653  50.625  27.833  1.00 48.58           O  
ANISOU 3223  O   VAL A 247     8488   5423   4545    334    -91   -175       O  
ATOM   3224  CB  VAL A 247     -24.160  52.476  25.306  1.00 20.77           C  
ANISOU 3224  CB  VAL A 247     4571   2133   1187    241      0   -122       C  
ATOM   3225  CG1 VAL A 247     -23.606  53.736  24.654  1.00 18.91           C  
ANISOU 3225  CG1 VAL A 247     4214   2018    950    150    -41    -85       C  
ATOM   3226  CG2 VAL A 247     -25.190  51.784  24.431  1.00 33.15           C  
ANISOU 3226  CG2 VAL A 247     6055   3691   2849    292     81   -130       C  
ATOM   3227  N   LYS A 248     -23.798  49.213  26.068  1.00 20.49           N  
ANISOU 3227  N   LYS A 248     4708   2009   1067    466   -137   -217       N  
ATOM   3228  CA  LYS A 248     -24.254  48.073  26.887  1.00 20.09           C  
ANISOU 3228  CA  LYS A 248     4856   1798    979    502   -145   -232       C  
ATOM   3229  C   LYS A 248     -23.197  47.793  27.954  1.00 19.47           C  
ANISOU 3229  C   LYS A 248     4911   1696    788    538   -263   -259       C  
ATOM   3230  O   LYS A 248     -23.485  47.681  29.162  1.00 19.22           O  
ANISOU 3230  O   LYS A 248     5087   1509    706    495   -236   -245       O  
ATOM   3231  CB  LYS A 248     -24.434  46.866  25.962  1.00 23.17           C  
ANISOU 3231  CB  LYS A 248     5196   2214   1393    599   -205   -266       C  
ATOM   3232  CG  LYS A 248     -24.372  45.500  26.637  1.00 32.04           C  
ANISOU 3232  CG  LYS A 248     6524   3207   2441    666   -303   -296       C  
ATOM   3233  CD  LYS A 248     -25.707  44.963  27.114  1.00 38.07           C  
ANISOU 3233  CD  LYS A 248     7446   3790   3227    576   -215   -248       C  
ATOM   3234  CE  LYS A 248     -25.715  43.447  27.195  1.00 49.52           C  
ANISOU 3234  CE  LYS A 248     9067   5131   4615    643   -348   -274       C  
ATOM   3235  NZ  LYS A 248     -27.068  42.897  27.465  1.00 56.26           N  
ANISOU 3235  NZ  LYS A 248    10044   5839   5491    521   -272   -207       N  
ATOM   3236  N   MET A 249     -21.980  47.637  27.464  1.00 19.49           N  
ANISOU 3236  N   MET A 249     4784   1872    748    624   -395   -295       N  
ATOM   3237  CA  MET A 249     -20.818  47.273  28.309  1.00 22.44           C  
ANISOU 3237  CA  MET A 249     5243   2271   1012    686   -536   -325       C  
ATOM   3238  C   MET A 249     -20.690  48.290  29.432  1.00 22.09           C  
ANISOU 3238  C   MET A 249     5317   2143    930    560   -504   -283       C  
ATOM   3239  O   MET A 249     -20.396  47.917  30.571  1.00 24.60           O  
ANISOU 3239  O   MET A 249     5828   2348   1170    568   -561   -293       O  
ATOM   3240  CB  MET A 249     -19.518  47.194  27.504  1.00 23.71           C  
ANISOU 3240  CB  MET A 249     5184   2697   1128    793   -666   -356       C  
ATOM   3241  CG  MET A 249     -18.407  46.497  28.263  1.00 25.70           C  
ANISOU 3241  CG  MET A 249     5516   2984   1263    905   -826   -399       C  
ATOM   3242  SD  MET A 249     -16.810  46.512  27.408  1.00 30.48           S  
ANISOU 3242  SD  MET A 249     5822   3965   1791   1038   -972   -424       S  
ATOM   3243  CE  MET A 249     -16.405  48.258  27.471  1.00 33.00           C  
ANISOU 3243  CE  MET A 249     5997   4415   2126    808   -929   -329       C  
ATOM   3244  N   MET A 250     -20.899  49.559  29.140  1.00 19.90           N  
ANISOU 3244  N   MET A 250     4954   1909    698    447   -426   -237       N  
ATOM   3245  CA  MET A 250     -20.774  50.606  30.165  1.00 21.36           C  
ANISOU 3245  CA  MET A 250     5280   2000    833    333   -413   -199       C  
ATOM   3246  C   MET A 250     -21.909  50.509  31.175  1.00 19.73           C  
ANISOU 3246  C   MET A 250     5314   1559    622    304   -289   -191       C  
ATOM   3247  O   MET A 250     -21.635  50.654  32.410  1.00 24.10           O  
ANISOU 3247  O   MET A 250     6070   1996   1089    273   -321   -187       O  
ATOM   3248  CB  MET A 250     -20.767  51.994  29.530  1.00 24.75           C  
ANISOU 3248  CB  MET A 250     5587   2515   1301    223   -379   -151       C  
ATOM   3249  CG  MET A 250     -19.503  52.253  28.749  1.00 31.67           C  
ANISOU 3249  CG  MET A 250     6236   3646   2149    210   -511   -138       C  
ATOM   3250  SD  MET A 250     -18.021  52.005  29.772  1.00 37.44           S  
ANISOU 3250  SD  MET A 250     7028   4449   2748    216   -695   -140       S  
ATOM   3251  CE  MET A 250     -16.799  51.870  28.467  1.00 45.02           C  
ANISOU 3251  CE  MET A 250     7632   5784   3687    263   -812   -132       C  
ATOM   3252  N   ILE A 251     -23.082  50.128  30.708  1.00 17.68           N  
ANISOU 3252  N   ILE A 251     5034   1245    439    320   -165   -187       N  
ATOM   3253  CA  ILE A 251     -24.218  49.933  31.626  1.00 20.39           C  
ANISOU 3253  CA  ILE A 251     5573   1409    766    292    -37   -168       C  
ATOM   3254  C   ILE A 251     -23.901  48.787  32.545  1.00 22.73           C  
ANISOU 3254  C   ILE A 251     6048   1609    978    331   -120   -190       C  
ATOM   3255  O   ILE A 251     -24.132  48.924  33.735  1.00 29.17           O  
ANISOU 3255  O   ILE A 251     7068   2295   1719    293    -80   -175       O  
ATOM   3256  CB  ILE A 251     -25.510  49.661  30.854  1.00 23.17           C  
ANISOU 3256  CB  ILE A 251     5831   1758   1213    291     95   -146       C  
ATOM   3257  CG1 ILE A 251     -26.015  50.925  30.153  1.00 26.45           C  
ANISOU 3257  CG1 ILE A 251     6117   2231   1701    252    194   -121       C  
ATOM   3258  CG2 ILE A 251     -26.554  49.059  31.781  1.00 24.54           C  
ANISOU 3258  CG2 ILE A 251     6182   1791   1348    264    198   -119       C  
ATOM   3259  CD1 ILE A 251     -27.195  50.685  29.230  1.00 26.45           C  
ANISOU 3259  CD1 ILE A 251     5986   2258   1802    255    307    -99       C  
ATOM   3260  N   VAL A 252     -23.398  47.681  31.990  1.00 21.50           N  
ANISOU 3260  N   VAL A 252     5832   1513    824    416   -237   -226       N  
ATOM   3261  CA  VAL A 252     -23.037  46.502  32.801  1.00 24.60           C  
ANISOU 3261  CA  VAL A 252     6415   1803   1128    468   -347   -253       C  
ATOM   3262  C   VAL A 252     -22.099  46.911  33.954  1.00 26.17           C  
ANISOU 3262  C   VAL A 252     6753   1962   1226    454   -432   -261       C  
ATOM   3263  O   VAL A 252     -22.317  46.511  35.120  1.00 22.22           O  
ANISOU 3263  O   VAL A 252     6489   1305    646    427   -430   -252       O  
ATOM   3264  CB  VAL A 252     -22.360  45.402  31.958  1.00 27.35           C  
ANISOU 3264  CB  VAL A 252     6677   2240   1472    602   -500   -308       C  
ATOM   3265  CG1 VAL A 252     -21.938  44.226  32.831  1.00 27.31           C  
ANISOU 3265  CG1 VAL A 252     6901   2111   1362    669   -638   -340       C  
ATOM   3266  CG2 VAL A 252     -23.234  44.916  30.808  1.00 26.12           C  
ANISOU 3266  CG2 VAL A 252     6412   2107   1405    617   -443   -302       C  
ATOM   3267  N   VAL A 253     -21.046  47.641  33.629  1.00 27.81           N  
ANISOU 3267  N   VAL A 253     6819   2319   1427    464   -517   -270       N  
ATOM   3268  CA  VAL A 253     -20.022  47.988  34.643  1.00 37.30           C  
ANISOU 3268  CA  VAL A 253     8136   3506   2530    445   -631   -271       C  
ATOM   3269  C   VAL A 253     -20.615  48.955  35.656  1.00 39.84           C  
ANISOU 3269  C   VAL A 253     8643   3673   2818    330   -522   -231       C  
ATOM   3270  O   VAL A 253     -20.156  48.989  36.793  1.00 42.62           O  
ANISOU 3270  O   VAL A 253     9189   3927   3074    308   -589   -231       O  
ATOM   3271  CB  VAL A 253     -18.710  48.549  34.058  1.00 39.82           C  
ANISOU 3271  CB  VAL A 253     8242   4051   2837    457   -763   -272       C  
ATOM   3272  CG1 VAL A 253     -18.129  47.652  32.976  1.00 45.44           C  
ANISOU 3272  CG1 VAL A 253     8747   4950   3566    602   -858   -318       C  
ATOM   3273  CG2 VAL A 253     -18.848  49.984  33.581  1.00 38.85           C  
ANISOU 3273  CG2 VAL A 253     7999   3998   2761    335   -691   -222       C  
ATOM   3274  N   VAL A 254     -21.598  49.744  35.254  1.00 39.14           N  
ANISOU 3274  N   VAL A 254     8506   3567   2798    273   -364   -201       N  
ATOM   3275  CA  VAL A 254     -22.279  50.641  36.215  1.00 48.38           C  
ANISOU 3275  CA  VAL A 254     9872   4590   3919    203   -249   -172       C  
ATOM   3276  C   VAL A 254     -23.187  49.800  37.096  1.00 39.21           C  
ANISOU 3276  C   VAL A 254     8906   3279   2711    214   -154   -168       C  
ATOM   3277  O   VAL A 254     -23.241  50.029  38.318  1.00 38.21           O  
ANISOU 3277  O   VAL A 254     9011   3023   2483    186   -137   -160       O  
ATOM   3278  CB  VAL A 254     -23.076  51.756  35.509  1.00 71.60           C  
ANISOU 3278  CB  VAL A 254    12706   7562   6934    165   -116   -146       C  
ATOM   3279  CG1 VAL A 254     -24.030  52.455  36.464  1.00 74.54           C  
ANISOU 3279  CG1 VAL A 254    13288   7784   7247    145     26   -128       C  
ATOM   3280  CG2 VAL A 254     -22.165  52.770  34.827  1.00 89.17           C  
ANISOU 3280  CG2 VAL A 254    14790   9912   9177    114   -220   -134       C  
ATOM   3281  N   CYS A 255     -23.881  48.847  36.504  1.00 30.90           N  
ANISOU 3281  N   CYS A 255     7775   2244   1718    242   -103   -166       N  
ATOM   3282  CA  CYS A 255     -24.777  47.948  37.265  1.00 38.21           C  
ANISOU 3282  CA  CYS A 255     8876   3047   2593    221    -25   -143       C  
ATOM   3283  C   CYS A 255     -23.973  47.141  38.265  1.00 44.90           C  
ANISOU 3283  C   CYS A 255     9931   3796   3330    238   -172   -166       C  
ATOM   3284  O   CYS A 255     -24.520  46.915  39.334  1.00 58.24           O  
ANISOU 3284  O   CYS A 255    11831   5363   4932    192   -105   -139       O  
ATOM   3285  CB  CYS A 255     -25.593  47.060  36.333  1.00 47.25           C  
ANISOU 3285  CB  CYS A 255     9897   4234   3821    226     21   -127       C  
ATOM   3286  SG  CYS A 255     -26.837  47.980  35.383  1.00 41.54           S  
ANISOU 3286  SG  CYS A 255     8966   3603   3215    196    223    -88       S  
ATOM   3287  N   THR A 256     -22.741  46.800  38.000  1.00 45.28           N  
ANISOU 3287  N   THR A 256     9927   3907   3368    303   -357   -209       N  
ATOM   3288  CA  THR A 256     -21.892  46.117  38.972  1.00 48.72           C  
ANISOU 3288  CA  THR A 256    10561   4256   3695    335   -513   -235       C  
ATOM   3289  C   THR A 256     -21.816  46.899  40.283  1.00 46.05           C  
ANISOU 3289  C   THR A 256    10434   3804   3258    267   -479   -214       C  
ATOM   3290  O   THR A 256     -22.110  46.366  41.384  1.00 35.72           O  
ANISOU 3290  O   THR A 256     9372   2348   1852    238   -470   -202       O  
ATOM   3291  CB  THR A 256     -20.492  45.820  38.412  1.00 48.75           C  
ANISOU 3291  CB  THR A 256    10428   4395   3698    438   -718   -285       C  
ATOM   3292  OG1 THR A 256     -20.653  44.730  37.502  1.00 44.58           O  
ANISOU 3292  OG1 THR A 256     9812   3910   3215    526   -767   -314       O  
ATOM   3293  CG2 THR A 256     -19.462  45.480  39.470  1.00 49.48           C  
ANISOU 3293  CG2 THR A 256    10701   4423   3674    470   -886   -309       C  
ATOM   3294  N   PHE A 257     -21.392  48.141  40.171  1.00 52.54           N  
ANISOU 3294  N   PHE A 257    11178   4690   4094    238   -474   -209       N  
ATOM   3295  CA  PHE A 257     -21.157  48.976  41.379  1.00 57.08           C  
ANISOU 3295  CA  PHE A 257    11972   5151   4563    182   -478   -195       C  
ATOM   3296  C   PHE A 257     -22.488  49.106  42.091  1.00 54.89           C  
ANISOU 3296  C   PHE A 257    11865   4748   4240    148   -277   -166       C  
ATOM   3297  O   PHE A 257     -22.545  49.034  43.313  1.00 78.09           O  
ANISOU 3297  O   PHE A 257    15056   7554   7061    126   -272   -159       O  
ATOM   3298  CB  PHE A 257     -20.587  50.349  41.014  1.00 64.09           C  
ANISOU 3298  CB  PHE A 257    12759   6119   5471    138   -515   -184       C  
ATOM   3299  CG  PHE A 257     -19.082  50.380  40.997  1.00 89.31           C  
ANISOU 3299  CG  PHE A 257    15888   9410   8633    135   -737   -194       C  
ATOM   3300  CD1 PHE A 257     -18.365  49.676  40.037  1.00112.06           C  
ANISOU 3300  CD1 PHE A 257    18532  12471  11574    205   -848   -217       C  
ATOM   3301  CD2 PHE A 257     -18.377  51.080  41.964  1.00111.98           C  
ANISOU 3301  CD2 PHE A 257    18939  12207  11402     70   -840   -178       C  
ATOM   3302  CE1 PHE A 257     -16.977  49.689  40.033  1.00119.46           C  
ANISOU 3302  CE1 PHE A 257    19380  13540  12468    215  -1047   -220       C  
ATOM   3303  CE2 PHE A 257     -16.988  51.089  41.961  1.00153.12           C  
ANISOU 3303  CE2 PHE A 257    24067  17533  16577     56  -1052   -174       C  
ATOM   3304  CZ  PHE A 257     -16.289  50.395  40.996  1.00127.70           C  
ANISOU 3304  CZ  PHE A 257    20581  14522  13416    131  -1150   -193       C  
ATOM   3305  N   ALA A 258     -23.541  49.402  41.335  1.00 59.08           N  
ANISOU 3305  N   ALA A 258    12252   5340   4857    146   -110   -146       N  
ATOM   3306  CA  ALA A 258     -24.920  49.443  41.826  1.00 71.79           C  
ANISOU 3306  CA  ALA A 258    13956   6891   6430    127     98   -110       C  
ATOM   3307  C   ALA A 258     -25.239  48.219  42.698  1.00 64.36           C  
ANISOU 3307  C   ALA A 258    13200   5854   5399     99     97    -89       C  
ATOM   3308  O   ALA A 258     -25.952  48.337  43.736  1.00 69.07           O  
ANISOU 3308  O   ALA A 258    13986   6372   5886     70    221    -59       O  
ATOM   3309  CB  ALA A 258     -25.890  49.577  40.679  1.00109.28           C  
ANISOU 3309  CB  ALA A 258    18470  11750  11299    136    236    -89       C  
ATOM   3310  N   ILE A 259     -24.779  47.048  42.287  1.00 48.05           N  
ANISOU 3310  N   ILE A 259    11093   3797   3366    109    -39   -103       N  
ATOM   3311  CA  ILE A 259     -25.088  45.835  43.091  1.00 51.43           C  
ANISOU 3311  CA  ILE A 259    11726   4114   3700     65    -66    -77       C  
ATOM   3312  C   ILE A 259     -24.227  45.765  44.335  1.00 51.82           C  
ANISOU 3312  C   ILE A 259    12033   4038   3617     67   -190    -98       C  
ATOM   3313  O   ILE A 259     -24.798  45.725  45.420  1.00 60.86           O  
ANISOU 3313  O   ILE A 259    13388   5088   4645     11    -98    -62       O  
ATOM   3314  CB  ILE A 259     -24.935  44.565  42.231  1.00 58.96           C  
ANISOU 3314  CB  ILE A 259    12595   5091   4716     88   -191    -88       C  
ATOM   3315  CG1 ILE A 259     -25.933  44.549  41.069  1.00 60.52           C  
ANISOU 3315  CG1 ILE A 259    12565   5395   5033     67    -64    -55       C  
ATOM   3316  CG2 ILE A 259     -25.058  43.315  43.099  1.00 55.81           C  
ANISOU 3316  CG2 ILE A 259    12453   4549   4202     37   -273    -63       C  
ATOM   3317  CD1 ILE A 259     -25.663  43.485  40.031  1.00 68.55           C  
ANISOU 3317  CD1 ILE A 259    13484   6440   6118    112   -205    -79       C  
ATOM   3318  N   CYS A 260     -22.931  45.597  44.133  1.00 49.17           N  
ANISOU 3318  N   CYS A 260    11670   3718   3293    129   -398   -150       N  
ATOM   3319  CA  CYS A 260     -21.991  45.189  45.199  1.00 60.08           C  
ANISOU 3319  CA  CYS A 260    13286   4986   4556    141   -569   -173       C  
ATOM   3320  C   CYS A 260     -22.020  46.121  46.398  1.00 64.64           C  
ANISOU 3320  C   CYS A 260    14069   5468   5023     93   -504   -157       C  
ATOM   3321  O   CYS A 260     -21.905  45.619  47.529  1.00 97.47           O  
ANISOU 3321  O   CYS A 260    18489   9490   9054     65   -556   -149       O  
ATOM   3322  CB  CYS A 260     -20.596  45.080  44.610  1.00 60.94           C  
ANISOU 3322  CB  CYS A 260    13257   5191   4707    232   -787   -227       C  
ATOM   3323  SG  CYS A 260     -20.504  43.792  43.341  1.00 73.69           S  
ANISOU 3323  SG  CYS A 260    14696   6892   6408    330   -890   -260       S  
ATOM   3324  N   TRP A 261     -22.202  47.412  46.161  1.00 53.04           N  
ANISOU 3324  N   TRP A 261    12508   4055   3589     86   -401   -153       N  
ATOM   3325  CA  TRP A 261     -22.037  48.433  47.215  1.00 58.70           C  
ANISOU 3325  CA  TRP A 261    13434   4674   4192     61   -381   -150       C  
ATOM   3326  C   TRP A 261     -23.359  48.794  47.879  1.00 63.27           C  
ANISOU 3326  C   TRP A 261    14151   5195   4691     41   -145   -115       C  
ATOM   3327  O   TRP A 261     -23.367  49.625  48.784  1.00 92.32           O  
ANISOU 3327  O   TRP A 261    18033   8784   8258     41   -110   -117       O  
ATOM   3328  CB  TRP A 261     -21.386  49.692  46.633  1.00 66.18           C  
ANISOU 3328  CB  TRP A 261    14247   5700   5199     64   -439   -164       C  
ATOM   3329  CG  TRP A 261     -19.974  49.490  46.179  1.00 76.32           C  
ANISOU 3329  CG  TRP A 261    15403   7069   6523     74   -674   -187       C  
ATOM   3330  CD1 TRP A 261     -19.573  49.101  44.937  1.00112.31           C  
ANISOU 3330  CD1 TRP A 261    19675  11795  11203    115   -740   -201       C  
ATOM   3331  CD2 TRP A 261     -18.771  49.673  46.947  1.00 89.63           C  
ANISOU 3331  CD2 TRP A 261    17228   8706   8119     52   -875   -194       C  
ATOM   3332  NE1 TRP A 261     -18.209  49.031  44.875  1.00116.48           N  
ANISOU 3332  NE1 TRP A 261    20137  12403  11716    129   -958   -216       N  
ATOM   3333  CE2 TRP A 261     -17.688  49.377  46.091  1.00103.58           C  
ANISOU 3333  CE2 TRP A 261    18754  10642   9959     83  -1049   -209       C  
ATOM   3334  CE3 TRP A 261     -18.497  50.055  48.265  1.00110.12           C  
ANISOU 3334  CE3 TRP A 261    20125  11142  10573     11   -928   -188       C  
ATOM   3335  CZ2 TRP A 261     -16.361  49.443  46.511  1.00131.04           C  
ANISOU 3335  CZ2 TRP A 261    22260  14152  13375     71  -1272   -210       C  
ATOM   3336  CZ3 TRP A 261     -17.184  50.131  48.678  1.00124.73           C  
ANISOU 3336  CZ3 TRP A 261    22024  12998  12369    -12  -1158   -191       C  
ATOM   3337  CH2 TRP A 261     -16.131  49.825  47.813  1.00127.42           C  
ANISOU 3337  CH2 TRP A 261    22100  13526  12787     14  -1327   -199       C  
ATOM   3338  N   LEU A 262     -24.463  48.239  47.421  1.00 61.17           N  
ANISOU 3338  N   LEU A 262    13774   4993   4474     29     10    -81       N  
ATOM   3339  CA  LEU A 262     -25.752  48.523  48.083  1.00 88.59           C  
ANISOU 3339  CA  LEU A 262    17351   8455   7853     15    244    -38       C  
ATOM   3340  C   LEU A 262     -25.773  47.909  49.471  1.00133.20           C  
ANISOU 3340  C   LEU A 262    23301  13976  13330    -30    231    -16       C  
ATOM   3341  O   LEU A 262     -26.013  48.633  50.430  1.00169.31           O  
ANISOU 3341  O   LEU A 262    28069  18487  17771     -9    319    -15       O  
ATOM   3342  CB  LEU A 262     -26.939  48.042  47.236  1.00 80.70           C  
ANISOU 3342  CB  LEU A 262    16135   7582   6943     -6    406      8       C  
ATOM   3343  CG  LEU A 262     -28.319  48.259  47.867  1.00 69.15           C  
ANISOU 3343  CG  LEU A 262    14732   6164   5378    -19    656     66       C  
ATOM   3344  CD1 LEU A 262     -28.649  49.739  47.958  1.00 63.84           C  
ANISOU 3344  CD1 LEU A 262    14060   5520   4677     79    785     38       C  
ATOM   3345  CD2 LEU A 262     -29.405  47.517  47.105  1.00 62.90           C  
ANISOU 3345  CD2 LEU A 262    13732   5501   4664    -79    777    132       C  
ATOM   3346  N   PRO A 263     -25.501  46.596  49.624  1.00112.56           N  
ANISOU 3346  N   PRO A 263    20755  11311  10701    -86    110      0       N  
ATOM   3347  CA  PRO A 263     -25.512  46.013  50.954  1.00106.25           C  
ANISOU 3347  CA  PRO A 263    20259  10381   9729   -142     87     26       C  
ATOM   3348  C   PRO A 263     -24.511  46.671  51.912  1.00112.80           C  
ANISOU 3348  C   PRO A 263    21317  11084  10454   -107    -37    -19       C  
ATOM   3349  O   PRO A 263     -24.784  46.753  53.105  1.00 93.27           O  
ANISOU 3349  O   PRO A 263    19101   8519   7817   -132     24      1       O  
ATOM   3350  CB  PRO A 263     -25.130  44.542  50.719  1.00 94.35           C  
ANISOU 3350  CB  PRO A 263    18777   8824   8245   -189    -87     35       C  
ATOM   3351  CG  PRO A 263     -25.453  44.293  49.262  1.00 83.01           C  
ANISOU 3351  CG  PRO A 263    17037   7520   6982   -172    -67     36       C  
ATOM   3352  CD  PRO A 263     -25.163  45.612  48.580  1.00 86.42           C  
ANISOU 3352  CD  PRO A 263    17269   8048   7516    -89    -21     -8       C  
ATOM   3353  N   PHE A 264     -23.402  47.161  51.375  1.00104.65           N  
ANISOU 3353  N   PHE A 264    20180  10066   9514    -57   -212    -73       N  
ATOM   3354  CA  PHE A 264     -22.330  47.749  52.183  1.00 93.59           C  
ANISOU 3354  CA  PHE A 264    18976   8558   8025    -44   -365   -106       C  
ATOM   3355  C   PHE A 264     -22.801  49.018  52.871  1.00 91.60           C  
ANISOU 3355  C   PHE A 264    18879   8256   7665    -27   -215   -103       C  
ATOM   3356  O   PHE A 264     -22.603  49.213  54.066  1.00 78.80           O  
ANISOU 3356  O   PHE A 264    17547   6504   5889    -38   -245   -104       O  
ATOM   3357  CB  PHE A 264     -21.021  47.947  51.411  1.00114.58           C  
ANISOU 3357  CB  PHE A 264    21459  11281  10793    -15   -585   -146       C  
ATOM   3358  CG  PHE A 264     -19.776  47.918  52.271  1.00132.25           C  
ANISOU 3358  CG  PHE A 264    23895  13414  12937    -24   -814   -167       C  
ATOM   3359  CD1 PHE A 264     -19.687  47.097  53.389  1.00159.90           C  
ANISOU 3359  CD1 PHE A 264    27672  16774  16307    -46   -876   -160       C  
ATOM   3360  CD2 PHE A 264     -18.673  48.690  51.945  1.00142.39           C  
ANISOU 3360  CD2 PHE A 264    25084  14753  14261    -22   -982   -185       C  
ATOM   3361  CE1 PHE A 264     -18.535  47.060  54.160  1.00173.86           C  
ANISOU 3361  CE1 PHE A 264    29618  18448  17990    -50  -1096   -179       C  
ATOM   3362  CE2 PHE A 264     -17.523  48.653  52.717  1.00108.60           C  
ANISOU 3362  CE2 PHE A 264    20969  10398   9895    -39  -1202   -195       C  
ATOM   3363  CZ  PHE A 264     -17.455  47.841  53.824  1.00139.95           C  
ANISOU 3363  CZ  PHE A 264    25214  14220  13741    -45  -1259   -196       C  
ATOM   3364  N   HIS A 265     -23.573  49.835  52.131  1.00117.42           N  
ANISOU 3364  N   HIS A 265    21975  11628  11010     13    -58   -101       N  
ATOM   3365  CA  HIS A 265     -24.039  51.148  52.633  1.00127.69           C  
ANISOU 3365  CA  HIS A 265    23419  12886  12212     67     65   -112       C  
ATOM   3366  C   HIS A 265     -25.250  51.009  53.541  1.00131.79           C  
ANISOU 3366  C   HIS A 265    24103  13393  12578     92    294    -80       C  
ATOM   3367  O   HIS A 265     -25.257  51.615  54.636  1.00123.87           O  
ANISOU 3367  O   HIS A 265    23385  12276  11401    128    318    -94       O  
ATOM   3368  CB  HIS A 265     -24.353  52.071  51.442  1.00123.12           C  
ANISOU 3368  CB  HIS A 265    22589  12422  11766    114    135   -124       C  
ATOM   3369  CG  HIS A 265     -23.132  52.613  50.786  1.00120.76           C  
ANISOU 3369  CG  HIS A 265    22191  12130  11562     85    -82   -148       C  
ATOM   3370  ND1 HIS A 265     -22.414  51.892  49.861  1.00132.09           N  
ANISOU 3370  ND1 HIS A 265    23382  13664  13138     48   -220   -149       N  
ATOM   3371  CD2 HIS A 265     -22.486  53.787  50.940  1.00133.76           C  
ANISOU 3371  CD2 HIS A 265    23952  13703  13164     79   -196   -165       C  
ATOM   3372  CE1 HIS A 265     -21.383  52.607  49.456  1.00139.53           C  
ANISOU 3372  CE1 HIS A 265    24264  14627  14123     18   -396   -159       C  
ATOM   3373  NE2 HIS A 265     -21.408  53.775  50.101  1.00128.64           N  
ANISOU 3373  NE2 HIS A 265    23106  13136  12634     20   -392   -164       N  
ATOM   3374  N   ILE A 266     -26.234  50.228  53.116  1.00138.14           N  
ANISOU 3374  N   ILE A 266    24736  14320  13430     67    452    -34       N  
ATOM   3375  CA  ILE A 266     -27.483  50.019  53.890  1.00152.75           C  
ANISOU 3375  CA  ILE A 266    26686  16218  15131     72    689     16       C  
ATOM   3376  C   ILE A 266     -27.142  49.312  55.194  1.00164.69           C  
ANISOU 3376  C   ILE A 266    28505  17597  16473      5    616     35       C  
ATOM   3377  O   ILE A 266     -27.864  49.433  56.185  1.00201.18           O  
ANISOU 3377  O   ILE A 266    33309  22219  20912     22    776     64       O  
ATOM   3378  CB  ILE A 266     -28.511  49.209  53.070  1.00138.05           C  
ANISOU 3378  CB  ILE A 266    24553  14529  13369     17    834     80       C  
ATOM   3379  CG1 ILE A 266     -29.915  49.258  53.684  1.00134.08           C  
ANISOU 3379  CG1 ILE A 266    24076  14148  12721     32   1110    143       C  
ATOM   3380  CG2 ILE A 266     -28.039  47.772  52.883  1.00126.55           C  
ANISOU 3380  CG2 ILE A 266    23082  13030  11969   -104    671    110       C  
ATOM   3381  CD1 ILE A 266     -30.503  50.646  53.804  1.00122.77           C  
ANISOU 3381  CD1 ILE A 266    22651  12774  11220    195   1281    107       C  
ATOM   3382  N   PHE A 267     -26.056  48.546  55.159  1.00140.33           N  
ANISOU 3382  N   PHE A 267    25465  14411  13440    -62    375     19       N  
ATOM   3383  CA  PHE A 267     -25.509  47.866  56.348  1.00122.94           C  
ANISOU 3383  CA  PHE A 267    23569  12055  11088   -123    249     28       C  
ATOM   3384  C   PHE A 267     -25.057  48.907  57.373  1.00 90.32           C  
ANISOU 3384  C   PHE A 267    19718   7793   6804    -62    217    -12       C  
ATOM   3385  O   PHE A 267     -25.400  48.805  58.554  1.00 72.23           O  
ANISOU 3385  O   PHE A 267    17695   5428   4320    -74    292      9       O  
ATOM   3386  CB  PHE A 267     -24.360  46.953  55.926  1.00129.48           C  
ANISOU 3386  CB  PHE A 267    24355  12819  12020   -168    -22      5       C  
ATOM   3387  CG  PHE A 267     -23.661  46.234  57.046  1.00122.48           C  
ANISOU 3387  CG  PHE A 267    23774  11766  10996   -219   -193      6       C  
ATOM   3388  CD1 PHE A 267     -24.144  45.019  57.499  1.00116.06           C  
ANISOU 3388  CD1 PHE A 267    23079  10917  10100   -311   -178     63       C  
ATOM   3389  CD2 PHE A 267     -22.509  46.752  57.611  1.00103.89           C  
ANISOU 3389  CD2 PHE A 267    21591   9290   8593   -188   -385    -42       C  
ATOM   3390  CE1 PHE A 267     -23.487  44.333  58.507  1.00103.19           C  
ANISOU 3390  CE1 PHE A 267    21744   9121   8341   -358   -351     64       C  
ATOM   3391  CE2 PHE A 267     -21.857  46.070  58.624  1.00120.54           C  
ANISOU 3391  CE2 PHE A 267    23978  11243  10577   -231   -553    -41       C  
ATOM   3392  CZ  PHE A 267     -22.354  44.869  59.077  1.00111.14           C  
ANISOU 3392  CZ  PHE A 267    22913  10009   9304   -308   -532      7       C  
ATOM   3393  N   PHE A 268     -24.304  49.900  56.917  1.00 82.32           N  
ANISOU 3393  N   PHE A 268    18654   6753   5870     -6    102    -65       N  
ATOM   3394  CA  PHE A 268     -23.797  50.982  57.779  1.00 75.55           C  
ANISOU 3394  CA  PHE A 268    18074   5754   4875     42     33   -103       C  
ATOM   3395  C   PHE A 268     -24.866  52.013  58.113  1.00 80.83           C  
ANISOU 3395  C   PHE A 268    18832   6454   5425    151    272   -110       C  
ATOM   3396  O   PHE A 268     -24.725  52.724  59.102  1.00101.08           O  
ANISOU 3396  O   PHE A 268    21703   8887   7814    203    257   -136       O  
ATOM   3397  CB  PHE A 268     -22.581  51.652  57.134  1.00 68.54           C  
ANISOU 3397  CB  PHE A 268    17098   4836   4106     32   -200   -141       C  
ATOM   3398  CG  PHE A 268     -21.270  50.937  57.362  1.00 64.76           C  
ANISOU 3398  CG  PHE A 268    16673   4282   3650    -41   -476   -146       C  
ATOM   3399  CD1 PHE A 268     -21.001  49.726  56.744  1.00 65.39           C  
ANISOU 3399  CD1 PHE A 268    16555   4440   3848    -76   -555   -135       C  
ATOM   3400  CD2 PHE A 268     -20.300  51.475  58.190  1.00 63.91           C  
ANISOU 3400  CD2 PHE A 268    16821   4026   3435    -65   -670   -163       C  
ATOM   3401  CE1 PHE A 268     -19.793  49.073  56.944  1.00 66.95           C  
ANISOU 3401  CE1 PHE A 268    16799   4583   4055   -110   -814   -148       C  
ATOM   3402  CE2 PHE A 268     -19.090  50.826  58.388  1.00 64.49           C  
ANISOU 3402  CE2 PHE A 268    16922   4054   3526   -122   -928   -166       C  
ATOM   3403  CZ  PHE A 268     -18.841  49.621  57.772  1.00 65.83           C  
ANISOU 3403  CZ  PHE A 268    16884   4316   3811   -132   -996   -161       C  
ATOM   3404  N   LEU A 269     -25.914  52.059  57.294  1.00 95.81           N  
ANISOU 3404  N   LEU A 269    20469   8525   7408    197    479    -90       N  
ATOM   3405  CA  LEU A 269     -26.980  53.084  57.395  1.00122.65           C  
ANISOU 3405  CA  LEU A 269    23893  11995  10713    338    711   -103       C  
ATOM   3406  C   LEU A 269     -28.069  52.652  58.374  1.00127.65           C  
ANISOU 3406  C   LEU A 269    24654  12696  11150    366    944    -58       C  
ATOM   3407  O   LEU A 269     -28.901  53.530  58.763  1.00167.04           O  
ANISOU 3407  O   LEU A 269    29733  17735  15997    517   1135    -77       O  
ATOM   3408  CB  LEU A 269     -27.653  53.254  56.017  1.00149.14           C  
ANISOU 3408  CB  LEU A 269    26877  15535  14255    373    830    -93       C  
ATOM   3409  CG  LEU A 269     -27.280  54.462  55.147  1.00159.86           C  
ANISOU 3409  CG  LEU A 269    28145  16874  15720    444    749   -144       C  
ATOM   3410  CD1 LEU A 269     -25.886  54.318  54.544  1.00156.39           C  
ANISOU 3410  CD1 LEU A 269    27628  16363  15428    333    465   -158       C  
ATOM   3411  CD2 LEU A 269     -28.300  54.655  54.036  1.00153.45           C  
ANISOU 3411  CD2 LEU A 269    27014  16254  15035    508    934   -129       C  
ATOM   3412  N   LEU A 270     -28.098  51.369  58.725  1.00111.02           N  
ANISOU 3412  N   LEU A 270    22553  10604   9025    233    930      0       N  
ATOM   3413  CA  LEU A 270     -29.273  50.785  59.417  1.00121.70           C  
ANISOU 3413  CA  LEU A 270    23938  12085  10215    213   1170     73       C  
ATOM   3414  C   LEU A 270     -29.348  51.222  60.886  1.00163.81           C  
ANISOU 3414  C   LEU A 270    29646  17318  15273    285   1229     58       C  
ATOM   3415  O   LEU A 270     -30.397  51.706  61.339  1.00167.05           O  
ANISOU 3415  O   LEU A 270    30087  17861  15523    402   1476     72       O  
ATOM   3416  CB  LEU A 270     -29.264  49.254  59.312  1.00111.77           C  
ANISOU 3416  CB  LEU A 270    22599  10855   9013     24   1107    150       C  
ATOM   3417  CG  LEU A 270     -30.429  48.542  60.007  1.00113.72           C  
ANISOU 3417  CG  LEU A 270    22875  11245   9088    -51   1328    251       C  
ATOM   3418  CD1 LEU A 270     -31.019  47.465  59.113  1.00108.10           C  
ANISOU 3418  CD1 LEU A 270    21876  10682   8513   -197   1364    337       C  
ATOM   3419  CD2 LEU A 270     -30.010  47.941  61.345  1.00132.56           C  
ANISOU 3419  CD2 LEU A 270    25614  13478  11273   -139   1242    274       C  
ATOM   3420  N   PRO A 271     -28.270  51.057  61.693  1.00179.88           N  
ANISOU 3420  N   PRO A 271    31980  19132  17235    227   1009     29       N  
ATOM   3421  CA  PRO A 271     -28.440  51.253  63.129  1.00156.70           C  
ANISOU 3421  CA  PRO A 271    29405  16110  14023    272   1077     29       C  
ATOM   3422  C   PRO A 271     -28.629  52.714  63.529  1.00147.49           C  
ANISOU 3422  C   PRO A 271    28427  14894  12716    480   1155    -44       C  
ATOM   3423  O   PRO A 271     -27.783  53.207  64.265  1.00164.44           O  
ANISOU 3423  O   PRO A 271    30893  16826  14760    503    983    -95       O  
ATOM   3424  CB  PRO A 271     -27.136  50.687  63.723  1.00154.87           C  
ANISOU 3424  CB  PRO A 271    29416  15645  13782    152    784     15       C  
ATOM   3425  CG  PRO A 271     -26.498  49.899  62.597  1.00156.11           C  
ANISOU 3425  CG  PRO A 271    29296  15820  14198     37    605     26       C  
ATOM   3426  CD  PRO A 271     -26.912  50.626  61.338  1.00175.97           C  
ANISOU 3426  CD  PRO A 271    31488  18481  16889    125    701      2       C  
ATOM   3427  N   TYR A 272     -29.693  53.340  63.044  1.00152.20           N  
ANISOU 3427  N   TYR A 272    28839  15682  13307    625   1391    -47       N  
ATOM   3428  CA  TYR A 272     -29.886  54.796  63.244  1.00165.11           C  
ANISOU 3428  CA  TYR A 272    30647  17263  14823    854   1445   -129       C  
ATOM   3429  C   TYR A 272     -31.345  55.122  63.564  1.00195.75           C  
ANISOU 3429  C   TYR A 272    34474  21380  18521   1037   1783   -111       C  
ATOM   3430  O   TYR A 272     -31.725  55.617  64.691  1.00197.36           O  
ANISOU 3430  O   TYR A 272    34979  21561  18445   1190   1899   -138       O  
ATOM   3431  CB  TYR A 272     -29.479  55.563  61.983  1.00138.44           C  
ANISOU 3431  CB  TYR A 272    27071  13859  11670    893   1324   -179       C  
ATOM   3432  CG  TYR A 272     -27.996  55.740  61.782  1.00132.72           C  
ANISOU 3432  CG  TYR A 272    26458  12904  11064    777    988   -214       C  
ATOM   3433  CD1 TYR A 272     -27.196  54.710  61.312  1.00123.44           C  
ANISOU 3433  CD1 TYR A 272    25116  11715  10071    581    813   -176       C  
ATOM   3434  CD2 TYR A 272     -27.396  56.960  62.041  1.00124.87           C  
ANISOU 3434  CD2 TYR A 272    25737  11716   9989    870    837   -283       C  
ATOM   3435  CE1 TYR A 272     -25.834  54.896  61.110  1.00114.63           C  
ANISOU 3435  CE1 TYR A 272    24068  10431   9054    487    510   -203       C  
ATOM   3436  CE2 TYR A 272     -26.039  57.161  61.848  1.00108.46           C  
ANISOU 3436  CE2 TYR A 272    23741   9458   8011    744    524   -299       C  
ATOM   3437  CZ  TYR A 272     -25.252  56.126  61.381  1.00102.48           C  
ANISOU 3437  CZ  TYR A 272    22778   8723   7435    556    368   -258       C  
ATOM   3438  OH  TYR A 272     -23.920  56.359  61.200  1.00 80.41           O  
ANISOU 3438  OH  TYR A 272    20039   5790   4724    444     67   -268       O  
ATOM   3439  N   ILE A 273     -32.187  54.924  62.556  1.00201.20           N  
ANISOU 3439  N   ILE A 273    34777  22312  19358   1044   1945    -69       N  
ATOM   3440  CA  ILE A 273     -33.659  55.064  62.775  1.00181.80           C  
ANISOU 3440  CA  ILE A 273    32187  20148  16739   1199   2282    -29       C  
ATOM   3441  C   ILE A 273     -34.158  53.784  63.438  1.00193.58           C  
ANISOU 3441  C   ILE A 273    33638  21790  18124   1019   2407     87       C  
ATOM   3442  O   ILE A 273     -35.189  53.794  64.170  1.00257.06           O  
ANISOU 3442  O   ILE A 273    41697  30045  25927   1118   2667    132       O  
ATOM   3443  CB  ILE A 273     -34.427  55.378  61.474  1.00141.96           C  
ANISOU 3443  CB  ILE A 273    26742  15317  11876   1277   2409    -21       C  
ATOM   3444  CG1 ILE A 273     -35.831  55.921  61.766  1.00119.57           C  
ANISOU 3444  CG1 ILE A 273    23824  12765   8842   1519   2732    -12       C  
ATOM   3445  CG2 ILE A 273     -34.478  54.165  60.555  1.00132.72           C  
ANISOU 3445  CG2 ILE A 273    25217  14265  10943   1027   2378     73       C  
ATOM   3446  CD1 ILE A 273     -35.853  57.223  62.537  1.00110.67           C  
ANISOU 3446  CD1 ILE A 273    23049  11522   7476   1820   2760   -123       C  
ATOM   3447  N   ASN A 274     -33.434  52.711  63.156  1.00164.29           N  
ANISOU 3447  N   ASN A 274    29870  17975  14575    762   2216    137       N  
ATOM   3448  CA  ASN A 274     -33.752  51.354  63.645  1.00166.27           C  
ANISOU 3448  CA  ASN A 274    30096  18321  14758    538   2267    257       C  
ATOM   3449  C   ASN A 274     -32.577  50.860  64.467  1.00175.49           C  
ANISOU 3449  C   ASN A 274    31605  19201  15871    409   2016    237       C  
ATOM   3450  O   ASN A 274     -31.550  50.523  63.907  1.00160.93           O  
ANISOU 3450  O   ASN A 274    29740  17178  14225    302   1758    208       O  
ATOM   3451  CB  ASN A 274     -34.078  50.362  62.529  1.00159.14           C  
ANISOU 3451  CB  ASN A 274    28818  17564  14082    346   2261    345       C  
ATOM   3452  CG  ASN A 274     -34.407  48.983  63.068  1.00158.62           C  
ANISOU 3452  CG  ASN A 274    28773  17570  13923    100   2287    476       C  
ATOM   3453  OD1 ASN A 274     -33.517  48.176  63.328  1.00147.98           O  
ANISOU 3453  OD1 ASN A 274    27598  16014  12612    -64   2059    483       O  
ATOM   3454  ND2 ASN A 274     -35.689  48.698  63.229  1.00161.66           N  
ANISOU 3454  ND2 ASN A 274    28982  18259  14180     69   2554    585       N  
ATOM   3455  N   PRO A 275     -32.714  50.753  65.807  1.00197.25           N  
ANISOU 3455  N   PRO A 275    34671  21922  18351    417   2085    259       N  
ATOM   3456  CA  PRO A 275     -31.625  50.232  66.640  1.00185.96           C  
ANISOU 3456  CA  PRO A 275    33577  20219  16859    289   1842    246       C  
ATOM   3457  C   PRO A 275     -31.185  48.818  66.247  1.00189.27           C  
ANISOU 3457  C   PRO A 275    33889  20589  17434     24   1669    322       C  
ATOM   3458  O   PRO A 275     -32.012  48.000  65.845  1.00180.88           O  
ANISOU 3458  O   PRO A 275    32587  19731  16406   -105   1800    426       O  
ATOM   3459  CB  PRO A 275     -32.212  50.260  68.061  1.00173.99           C  
ANISOU 3459  CB  PRO A 275    32346  18758  15001    337   2021    282       C  
ATOM   3460  CG  PRO A 275     -33.711  50.237  67.852  1.00172.51           C  
ANISOU 3460  CG  PRO A 275    31874  18945  14727    391   2364    365       C  
ATOM   3461  CD  PRO A 275     -33.940  51.019  66.576  1.00187.10           C  
ANISOU 3461  CD  PRO A 275    33410  20883  16794    538   2401    306       C  
ATOM   3462  N   ASP A 276     -29.878  48.582  66.331  1.00187.18           N  
ANISOU 3462  N   ASP A 276    33804  20057  17259    -43   1364    269       N  
ATOM   3463  CA  ASP A 276     -29.260  47.340  65.815  1.00185.86           C  
ANISOU 3463  CA  ASP A 276    33546  19809  17261   -243   1147    311       C  
ATOM   3464  C   ASP A 276     -29.838  46.120  66.520  1.00181.28           C  
ANISOU 3464  C   ASP A 276    33065  19287  16523   -434   1214    431       C  
ATOM   3465  O   ASP A 276     -29.985  46.118  67.766  1.00131.56           O  
ANISOU 3465  O   ASP A 276    27068  12945   9973   -443   1277    455       O  
ATOM   3466  CB  ASP A 276     -27.737  47.354  65.977  1.00192.30           C  
ANISOU 3466  CB  ASP A 276    34567  20345  18151   -254    812    232       C  
ATOM   3467  CG  ASP A 276     -27.017  46.302  65.147  1.00174.56           C  
ANISOU 3467  CG  ASP A 276    32166  18040  16119   -383    577    243       C  
ATOM   3468  OD1 ASP A 276     -27.670  45.331  64.725  1.00163.23           O  
ANISOU 3468  OD1 ASP A 276    30567  16724  14727   -506    646    326       O  
ATOM   3469  OD2 ASP A 276     -25.802  46.461  64.931  1.00157.96           O  
ANISOU 3469  OD2 ASP A 276    30112  15777  14126   -357    319    172       O  
ATOM   3470  N   LEU A 277     -30.071  45.066  65.754  1.00184.75           N  
ANISOU 3470  N   LEU A 277    33290  19801  17103   -596   1169    505       N  
ATOM   3471  CA  LEU A 277     -30.509  43.777  66.323  1.00195.51           C  
ANISOU 3471  CA  LEU A 277    34766  21187  18332   -822   1172    631       C  
ATOM   3472  C   LEU A 277     -29.299  42.871  66.505  1.00181.22           C  
ANISOU 3472  C   LEU A 277    33180  19099  16575   -928    829    604       C  
ATOM   3473  O   LEU A 277     -28.800  42.333  65.516  1.00162.97           O  
ANISOU 3473  O   LEU A 277    30706  16736  14479   -964    647    583       O  
ATOM   3474  CB  LEU A 277     -31.558  43.173  65.379  1.00181.49           C  
ANISOU 3474  CB  LEU A 277    32644  19655  16658   -943   1316    737       C  
ATOM   3475  CG  LEU A 277     -32.708  42.412  66.041  1.00164.10           C  
ANISOU 3475  CG  LEU A 277    30469  17644  14237  -1139   1508    900       C  
ATOM   3476  CD1 LEU A 277     -33.638  43.358  66.789  1.00155.39           C  
ANISOU 3476  CD1 LEU A 277    29364  16765  12911  -1003   1832    918       C  
ATOM   3477  CD2 LEU A 277     -33.492  41.601  65.018  1.00137.19           C  
ANISOU 3477  CD2 LEU A 277    26748  14416  10960  -1311   1551   1012       C  
ATOM   3478  N   TYR A 278     -28.864  42.675  67.743  1.00181.87           N  
ANISOU 3478  N   TYR A 278    33630  19015  16454   -968    742    606       N  
ATOM   3479  CA  TYR A 278     -27.750  41.757  68.024  1.00171.69           C  
ANISOU 3479  CA  TYR A 278    32580  17465  15188  -1062    411    586       C  
ATOM   3480  C   TYR A 278     -28.273  40.403  68.468  1.00210.33           C  
ANISOU 3480  C   TYR A 278    37609  22358  19948  -1303    390    719       C  
ATOM   3481  O   TYR A 278     -27.437  39.547  68.774  1.00231.91           O  
ANISOU 3481  O   TYR A 278    40575  24869  22671  -1383    113    710       O  
ATOM   3482  CB  TYR A 278     -26.779  42.372  69.036  1.00167.39           C  
ANISOU 3482  CB  TYR A 278    32368  16705  14525   -961    272    499       C  
ATOM   3483  CG  TYR A 278     -25.844  43.401  68.452  1.00153.95           C  
ANISOU 3483  CG  TYR A 278    30566  14929  12998   -779    146    372       C  
ATOM   3484  CD1 TYR A 278     -25.271  43.218  67.203  1.00124.39           C  
ANISOU 3484  CD1 TYR A 278    26549  11194   9519   -752    -10    327       C  
ATOM   3485  CD2 TYR A 278     -25.516  44.550  69.156  1.00148.06           C  
ANISOU 3485  CD2 TYR A 278    30012  14103  12139   -644    171    303       C  
ATOM   3486  CE1 TYR A 278     -24.402  44.151  66.663  1.00120.77           C  
ANISOU 3486  CE1 TYR A 278    25988  10690   9208   -613   -130    227       C  
ATOM   3487  CE2 TYR A 278     -24.650  45.495  68.630  1.00141.41           C  
ANISOU 3487  CE2 TYR A 278    29093  13190  11444   -512     35    203       C  
ATOM   3488  CZ  TYR A 278     -24.092  45.294  67.380  1.00139.63           C  
ANISOU 3488  CZ  TYR A 278    28572  12997  11482   -506   -112    171       C  
ATOM   3489  OH  TYR A 278     -23.240  46.222  66.857  1.00154.81           O  
ANISOU 3489  OH  TYR A 278    30408  14874  13538   -402   -248     89       O  
ATOM   3490  N   LEU A 279     -29.552  40.160  68.200  1.00230.69           N  
ANISOU 3490  N   LEU A 279    39986  25186  22479  -1413    637    836       N  
ATOM   3491  CA  LEU A 279     -30.274  38.975  68.709  1.00241.20           C  
ANISOU 3491  CA  LEU A 279    41443  26565  23638  -1679    662    995       C  
ATOM   3492  C   LEU A 279     -29.742  37.698  68.084  1.00263.98           C  
ANISOU 3492  C   LEU A 279    44366  29280  26655  -1825    361   1017       C  
ATOM   3493  O   LEU A 279     -29.609  36.711  68.810  1.00287.92           O  
ANISOU 3493  O   LEU A 279    47697  32165  29532  -2007    211   1092       O  
ATOM   3494  CB  LEU A 279     -31.779  39.133  68.455  1.00207.89           C  
ANISOU 3494  CB  LEU A 279    36938  22699  19349  -1756   1004   1120       C  
ATOM   3495  CG  LEU A 279     -32.570  39.816  69.574  1.00174.79           C  
ANISOU 3495  CG  LEU A 279    32843  18692  14877  -1713   1301   1169       C  
ATOM   3496  CD1 LEU A 279     -32.311  41.314  69.599  1.00153.33           C  
ANISOU 3496  CD1 LEU A 279    30076  15990  12190  -1401   1421   1023       C  
ATOM   3497  CD2 LEU A 279     -34.060  39.541  69.437  1.00166.70           C  
ANISOU 3497  CD2 LEU A 279    31563  18030  13743  -1868   1593   1339       C  
ATOM   3498  N   LYS A 280     -29.487  37.703  66.782  1.00260.75           N  
ANISOU 3498  N   LYS A 280    43676  28889  26506  -1747    275    958       N  
ATOM   3499  CA  LYS A 280     -29.038  36.499  66.070  1.00214.92           C  
ANISOU 3499  CA  LYS A 280    37895  22938  20825  -1853     -7    971       C  
ATOM   3500  C   LYS A 280     -27.574  36.203  66.376  1.00199.44           C  
ANISOU 3500  C   LYS A 280    36203  20678  18896  -1752   -346    855       C  
ATOM   3501  O   LYS A 280     -26.750  37.117  66.641  1.00174.56           O  
ANISOU 3501  O   LYS A 280    33086  17456  15781  -1560   -382    736       O  
ATOM   3502  CB  LYS A 280     -29.265  36.643  64.560  1.00187.13           C  
ANISOU 3502  CB  LYS A 280    33983  19555  17563  -1784     23    942       C  
ATOM   3503  CG  LYS A 280     -30.600  36.114  64.050  1.00170.40           C  
ANISOU 3503  CG  LYS A 280    31659  17656  15427  -1987    198   1097       C  
ATOM   3504  CD  LYS A 280     -31.802  36.848  64.615  1.00178.19           C  
ANISOU 3504  CD  LYS A 280    32522  18924  16256  -2025    568   1190       C  
ATOM   3505  CE  LYS A 280     -33.093  36.538  63.884  1.00158.56           C  
ANISOU 3505  CE  LYS A 280    29733  16712  13801  -2187    755   1331       C  
ATOM   3506  NZ  LYS A 280     -34.141  37.546  64.174  1.00164.28           N  
ANISOU 3506  NZ  LYS A 280    30239  17752  14424  -2118   1128   1377       N  
ATOM   3507  N   LYS A 281     -27.226  34.928  66.249  1.00204.95           N  
ANISOU 3507  N   LYS A 281    37078  21202  19589  -1873   -614    888       N  
ATOM   3508  CA  LYS A 281     -25.828  34.447  66.369  1.00205.58           C  
ANISOU 3508  CA  LYS A 281    37386  21010  19712  -1763   -974    779       C  
ATOM   3509  C   LYS A 281     -24.973  34.869  65.180  1.00234.75           C  
ANISOU 3509  C   LYS A 281    40803  24720  23669  -1536  -1096    642       C  
ATOM   3510  O   LYS A 281     -23.744  34.954  65.321  1.00258.76           O  
ANISOU 3510  O   LYS A 281    43952  27609  26754  -1383  -1329    531       O  
ATOM   3511  CB  LYS A 281     -25.817  32.926  66.568  1.00209.89           C  
ANISOU 3511  CB  LYS A 281    38224  21370  20152  -1951  -1224    859       C  
ATOM   3512  CG  LYS A 281     -26.518  32.451  67.836  1.00195.90           C  
ANISOU 3512  CG  LYS A 281    36770  19564  18097  -2197  -1144   1001       C  
ATOM   3513  CD  LYS A 281     -27.093  31.051  67.748  1.00177.26           C  
ANISOU 3513  CD  LYS A 281    34586  17125  15637  -2464  -1283   1140       C  
ATOM   3514  CE  LYS A 281     -26.050  29.958  67.849  1.00158.18           C  
ANISOU 3514  CE  LYS A 281    32512  14386  13202  -2438  -1702   1083       C  
ATOM   3515  NZ  LYS A 281     -25.393  29.950  69.176  1.00154.71           N  
ANISOU 3515  NZ  LYS A 281    32448  13755  12576  -2431  -1817   1058       N  
ATOM   3516  N   PHE A 282     -25.605  35.276  64.087  1.00220.23           N  
ANISOU 3516  N   PHE A 282    38598  23085  21993  -1507   -921    650       N  
ATOM   3517  CA  PHE A 282     -24.912  35.804  62.899  1.00165.33           C  
ANISOU 3517  CA  PHE A 282    31343  16190  15285  -1301   -992    531       C  
ATOM   3518  C   PHE A 282     -24.580  37.287  63.065  1.00154.62           C  
ANISOU 3518  C   PHE A 282    29854  14918  13973  -1139   -847    450       C  
ATOM   3519  O   PHE A 282     -25.461  38.173  62.854  1.00119.37           O  
ANISOU 3519  O   PHE A 282    25177  10647   9530  -1133   -558    480       O  
ATOM   3520  CB  PHE A 282     -25.781  35.581  61.658  1.00159.48           C  
ANISOU 3520  CB  PHE A 282    30286  15621  14687  -1354   -873    582       C  
ATOM   3521  CG  PHE A 282     -26.352  34.190  61.516  1.00172.58           C  
ANISOU 3521  CG  PHE A 282    32085  17210  16277  -1556   -985    691       C  
ATOM   3522  CD1 PHE A 282     -27.558  33.846  62.109  1.00160.64           C  
ANISOU 3522  CD1 PHE A 282    30659  15781  14595  -1800   -803    848       C  
ATOM   3523  CD2 PHE A 282     -25.690  33.223  60.774  1.00168.61           C  
ANISOU 3523  CD2 PHE A 282    31632  16567  15864  -1505  -1280    640       C  
ATOM   3524  CE1 PHE A 282     -28.083  32.569  61.970  1.00154.15           C  
ANISOU 3524  CE1 PHE A 282    29981  14888  13700  -2021   -928    963       C  
ATOM   3525  CE2 PHE A 282     -26.217  31.947  60.634  1.00142.40           C  
ANISOU 3525  CE2 PHE A 282    28481  13155  12468  -1696  -1410    741       C  
ATOM   3526  CZ  PHE A 282     -27.412  31.621  61.233  1.00146.21           C  
ANISOU 3526  CZ  PHE A 282    29058  13707  12785  -1971  -1241    908       C  
ATOM   3527  N   ILE A 283     -23.315  37.574  63.322  1.00170.54           N  
ANISOU 3527  N   ILE A 283    31974  16805  16018  -1001  -1058    347       N  
ATOM   3528  CA  ILE A 283     -22.862  38.973  63.526  1.00153.07           C  
ANISOU 3528  CA  ILE A 283    29685  14638  13834   -866   -975    273       C  
ATOM   3529  C   ILE A 283     -21.681  39.266  62.605  1.00122.16           C  
ANISOU 3529  C   ILE A 283    25566  10732  10117   -702  -1180    166       C  
ATOM   3530  O   ILE A 283     -21.822  40.101  61.702  1.00117.60           O  
ANISOU 3530  O   ILE A 283    24682  10310   9690   -624  -1059    135       O  
ATOM   3531  CB  ILE A 283     -22.523  39.237  65.010  1.00157.39           C  
ANISOU 3531  CB  ILE A 283    30598  15033  14170   -890  -1010    274       C  
ATOM   3532  CG1 ILE A 283     -23.680  38.901  65.959  1.00130.99           C  
ANISOU 3532  CG1 ILE A 283    27458  11705  10604  -1056   -804    388       C  
ATOM   3533  CG2 ILE A 283     -22.043  40.668  65.205  1.00155.42           C  
ANISOU 3533  CG2 ILE A 283    30305  14807  13940   -760   -954    201       C  
ATOM   3534  CD1 ILE A 283     -24.915  39.748  65.777  1.00135.52           C  
ANISOU 3534  CD1 ILE A 283    27825  12504  11161  -1061   -447    438       C  
ATOM   3535  N   GLN A 284     -20.554  38.611  62.849  1.00119.54           N  
ANISOU 3535  N   GLN A 284    25396  10249   9771   -651  -1481    115       N  
ATOM   3536  CA  GLN A 284     -19.288  39.013  62.192  1.00117.14           C  
ANISOU 3536  CA  GLN A 284    24912   9978   9616   -489  -1682     17       C  
ATOM   3537  C   GLN A 284     -19.273  38.455  60.775  1.00142.69           C  
ANISOU 3537  C   GLN A 284    27851  13330  13032   -422  -1738     -6       C  
ATOM   3538  O   GLN A 284     -18.684  39.048  59.873  1.00192.80           O  
ANISOU 3538  O   GLN A 284    33913  19806  19534   -305  -1775    -65       O  
ATOM   3539  CB  GLN A 284     -18.071  38.530  62.987  1.00118.32           C  
ANISOU 3539  CB  GLN A 284    25327   9954   9675   -438  -1987    -27       C  
ATOM   3540  CG  GLN A 284     -16.747  39.069  62.454  1.00112.49           C  
ANISOU 3540  CG  GLN A 284    24393   9287   9061   -285  -2183   -112       C  
ATOM   3541  CD  GLN A 284     -15.565  38.706  63.321  1.00105.80           C  
ANISOU 3541  CD  GLN A 284    23796   8289   8112   -234  -2474   -150       C  
ATOM   3542  OE1 GLN A 284     -15.719  38.156  64.409  1.00124.07           O  
ANISOU 3542  OE1 GLN A 284    26462  10422  10257   -314  -2525   -117       O  
ATOM   3543  NE2 GLN A 284     -14.367  39.002  62.838  1.00 82.59           N  
ANISOU 3543  NE2 GLN A 284    20670   5439   5270   -104  -2672   -213       N  
ATOM   3544  N   GLN A 285     -19.879  37.281  60.618  1.00147.93           N  
ANISOU 3544  N   GLN A 285    28608  13937  13659   -504  -1765     43       N  
ATOM   3545  CA  GLN A 285     -19.754  36.455  59.404  1.00126.26           C  
ANISOU 3545  CA  GLN A 285    25682  11242  11046   -434  -1890     16       C  
ATOM   3546  C   GLN A 285     -20.419  37.160  58.234  1.00106.14           C  
ANISOU 3546  C   GLN A 285    22752   8906   8666   -418  -1668     22       C  
ATOM   3547  O   GLN A 285     -19.872  37.152  57.077  1.00 84.79           O  
ANISOU 3547  O   GLN A 285    19785   6308   6120   -283  -1763    -42       O  
ATOM   3548  CB  GLN A 285     -20.401  35.075  59.551  1.00121.86           C  
ANISOU 3548  CB  GLN A 285    25356  10555  10390   -561  -1965     85       C  
ATOM   3549  CG  GLN A 285     -19.951  34.298  60.780  1.00137.62           C  
ANISOU 3549  CG  GLN A 285    27774  12319  12193   -613  -2170     98       C  
ATOM   3550  CD  GLN A 285     -20.791  34.633  61.987  1.00154.80           C  
ANISOU 3550  CD  GLN A 285    30165  14454  14196   -802  -1965    194       C  
ATOM   3551  OE1 GLN A 285     -21.782  35.356  61.886  1.00166.75           O  
ANISOU 3551  OE1 GLN A 285    31512  16119  15725   -887  -1669    254       O  
ATOM   3552  NE2 GLN A 285     -20.389  34.127  63.141  1.00138.26           N  
ANISOU 3552  NE2 GLN A 285    28441  12164  11925   -853  -2122    207       N  
ATOM   3553  N   VAL A 286     -21.502  37.853  58.535  1.00116.92           N  
ANISOU 3553  N   VAL A 286    24079  10349   9993   -532  -1382     92       N  
ATOM   3554  CA  VAL A 286     -22.297  38.599  57.533  1.00110.68           C  
ANISOU 3554  CA  VAL A 286    22946   9760   9345   -526  -1144    108       C  
ATOM   3555  C   VAL A 286     -21.547  39.843  57.087  1.00 95.23           C  
ANISOU 3555  C   VAL A 286    20771   7905   7506   -388  -1137     29       C  
ATOM   3556  O   VAL A 286     -21.514  40.128  55.881  1.00124.11           O  
ANISOU 3556  O   VAL A 286    24120  11703  11329   -316  -1111      0       O  
ATOM   3557  CB  VAL A 286     -23.710  38.925  58.064  1.00110.82           C  
ANISOU 3557  CB  VAL A 286    22998   9847   9261   -673   -843    210       C  
ATOM   3558  CG1 VAL A 286     -24.392  40.043  57.282  1.00 94.96           C  
ANISOU 3558  CG1 VAL A 286    20664   8040   7374   -627   -592    210       C  
ATOM   3559  CG2 VAL A 286     -24.590  37.680  58.089  1.00100.19           C  
ANISOU 3559  CG2 VAL A 286    21761   8465   7838   -841   -839    311       C  
ATOM   3560  N   TYR A 287     -20.967  40.564  58.046  1.00 81.00           N  
ANISOU 3560  N   TYR A 287    19138   6027   5609   -366  -1169      4       N  
ATOM   3561  CA  TYR A 287     -20.077  41.713  57.774  1.00 89.86           C  
ANISOU 3561  CA  TYR A 287    20112   7215   6814   -262  -1223    -60       C  
ATOM   3562  C   TYR A 287     -19.015  41.328  56.753  1.00 85.75           C  
ANISOU 3562  C   TYR A 287    19377   6767   6436   -147  -1448   -124       C  
ATOM   3563  O   TYR A 287     -18.707  42.102  55.837  1.00 98.21           O  
ANISOU 3563  O   TYR A 287    20671   8494   8149    -82  -1425   -155       O  
ATOM   3564  CB  TYR A 287     -19.435  42.203  59.077  1.00 99.65           C  
ANISOU 3564  CB  TYR A 287    21645   8314   7903   -271  -1310    -73       C  
ATOM   3565  CG  TYR A 287     -18.418  43.309  58.915  1.00101.34           C  
ANISOU 3565  CG  TYR A 287    21754   8573   8177   -198  -1415   -125       C  
ATOM   3566  CD1 TYR A 287     -18.790  44.566  58.459  1.00 93.21           C  
ANISOU 3566  CD1 TYR A 287    20553   7649   7212   -186  -1248   -126       C  
ATOM   3567  CD2 TYR A 287     -17.081  43.107  59.230  1.00112.81           C  
ANISOU 3567  CD2 TYR A 287    23286   9965   9610   -149  -1695   -166       C  
ATOM   3568  CE1 TYR A 287     -17.865  45.587  58.313  1.00105.14           C  
ANISOU 3568  CE1 TYR A 287    21990   9192   8764   -152  -1363   -159       C  
ATOM   3569  CE2 TYR A 287     -16.142  44.115  59.087  1.00106.37           C  
ANISOU 3569  CE2 TYR A 287    22366   9208   8839   -115  -1804   -194       C  
ATOM   3570  CZ  TYR A 287     -16.535  45.359  58.627  1.00114.34           C  
ANISOU 3570  CZ  TYR A 287    23221  10311   9910   -129  -1642   -186       C  
ATOM   3571  OH  TYR A 287     -15.610  46.352  58.498  1.00138.43           O  
ANISOU 3571  OH  TYR A 287    26194  13411  12992   -126  -1770   -200       O  
ATOM   3572  N   LEU A 288     -18.486  40.107  56.945  1.00 82.21           N  
ANISOU 3572  N   LEU A 288    19081   6214   5938   -118  -1668   -141       N  
ATOM   3573  CA  LEU A 288     -17.407  39.553  56.111  1.00 96.40           C  
ANISOU 3573  CA  LEU A 288    20720   8076   7831     26  -1911   -209       C  
ATOM   3574  C   LEU A 288     -17.926  39.287  54.696  1.00105.68           C  
ANISOU 3574  C   LEU A 288    21597   9397   9157     66  -1829   -214       C  
ATOM   3575  O   LEU A 288     -17.253  39.565  53.705  1.00 81.09           O  
ANISOU 3575  O   LEU A 288    18203   6440   6166    183  -1902   -264       O  
ATOM   3576  CB  LEU A 288     -16.838  38.269  56.722  1.00109.58           C  
ANISOU 3576  CB  LEU A 288    22670   9575   9386     65  -2165   -229       C  
ATOM   3577  CG  LEU A 288     -15.818  38.447  57.846  1.00103.90           C  
ANISOU 3577  CG  LEU A 288    22179   8746   8551     91  -2349   -254       C  
ATOM   3578  CD1 LEU A 288     -15.515  37.102  58.483  1.00102.93           C  
ANISOU 3578  CD1 LEU A 288    22375   8431   8302    114  -2575   -264       C  
ATOM   3579  CD2 LEU A 288     -14.533  39.104  57.355  1.00100.57           C  
ANISOU 3579  CD2 LEU A 288    21513   8480   8217    224  -2502   -315       C  
ATOM   3580  N   ALA A 289     -19.094  38.699  54.606  1.00134.94           N  
ANISOU 3580  N   ALA A 289    25366  13059  12843    -36  -1692   -154       N  
ATOM   3581  CA  ALA A 289     -19.711  38.301  53.340  1.00134.10           C  
ANISOU 3581  CA  ALA A 289    25027  13061  12861    -22  -1624   -146       C  
ATOM   3582  C   ALA A 289     -20.057  39.519  52.515  1.00103.86           C  
ANISOU 3582  C   ALA A 289    20867   9423   9170    -12  -1419   -147       C  
ATOM   3583  O   ALA A 289     -19.658  39.570  51.280  1.00 99.87           O  
ANISOU 3583  O   ALA A 289    20078   9060   8804     96  -1472   -194       O  
ATOM   3584  CB  ALA A 289     -20.932  37.453  53.595  1.00158.83           C  
ANISOU 3584  CB  ALA A 289    28329  16101  15917   -178  -1526    -60       C  
ATOM   3585  N   ILE A 290     -20.629  40.514  53.172  1.00 78.05           N  
ANISOU 3585  N   ILE A 290    17640   6159   5854    -97  -1218   -106       N  
ATOM   3586  CA  ILE A 290     -21.050  41.784  52.517  1.00 77.16           C  
ANISOU 3586  CA  ILE A 290    17262   6203   5851    -89  -1017   -103       C  
ATOM   3587  C   ILE A 290     -19.799  42.535  52.100  1.00 76.95           C  
ANISOU 3587  C   ILE A 290    17077   6260   5900     15  -1161   -169       C  
ATOM   3588  O   ILE A 290     -19.734  42.992  50.932  1.00116.76           O  
ANISOU 3588  O   ILE A 290    21819  11460  11083     67  -1124   -188       O  
ATOM   3589  CB  ILE A 290     -21.922  42.635  53.478  1.00 68.67           C  
ANISOU 3589  CB  ILE A 290    16330   5093   4668   -176   -789    -52       C  
ATOM   3590  CG1 ILE A 290     -23.217  41.921  53.884  1.00 77.44           C  
ANISOU 3590  CG1 ILE A 290    17559   6173   5689   -297   -627     31       C  
ATOM   3591  CG2 ILE A 290     -22.209  44.027  52.919  1.00 68.06           C  
ANISOU 3591  CG2 ILE A 290    16033   5145   4679   -140   -623    -63       C  
ATOM   3592  CD1 ILE A 290     -24.077  41.444  52.733  1.00 84.11           C  
ANISOU 3592  CD1 ILE A 290    18165   7137   6653   -329   -531     68       C  
ATOM   3593  N   MET A 291     -18.878  42.746  53.049  1.00 76.41           N  
ANISOU 3593  N   MET A 291    17201   6098   5732     29  -1311   -191       N  
ATOM   3594  CA  MET A 291     -17.640  43.478  52.764  1.00 82.29           C  
ANISOU 3594  CA  MET A 291    17802   6935   6527     98  -1465   -234       C  
ATOM   3595  C   MET A 291     -16.916  42.792  51.604  1.00 75.21           C  
ANISOU 3595  C   MET A 291    16655   6180   5741    217  -1626   -280       C  
ATOM   3596  O   MET A 291     -16.240  43.476  50.789  1.00 80.78           O  
ANISOU 3596  O   MET A 291    17092   7059   6540    266  -1673   -301       O  
ATOM   3597  CB  MET A 291     -16.757  43.458  54.015  1.00120.46           C  
ANISOU 3597  CB  MET A 291    22913  11631  11222     89  -1642   -245       C  
ATOM   3598  CG  MET A 291     -15.409  44.122  53.849  1.00143.90           C  
ANISOU 3598  CG  MET A 291    25752  14702  14221    137  -1834   -273       C  
ATOM   3599  SD  MET A 291     -14.587  44.279  55.448  1.00230.00           S  
ANISOU 3599  SD  MET A 291    37014  25424  24949     94  -2010   -269       S  
ATOM   3600  CE  MET A 291     -13.949  42.619  55.668  1.00228.91           C  
ANISOU 3600  CE  MET A 291    36996  25218  24758    200  -2248   -308       C  
ATOM   3601  N   TRP A 292     -17.006  41.455  51.572  1.00 80.50           N  
ANISOU 3601  N   TRP A 292    17432   6774   6379    264  -1725   -294       N  
ATOM   3602  CA  TRP A 292     -16.366  40.655  50.509  1.00 96.44           C  
ANISOU 3602  CA  TRP A 292    19257   8908   8475    412  -1888   -349       C  
ATOM   3603  C   TRP A 292     -16.999  40.967  49.182  1.00 90.93           C  
ANISOU 3603  C   TRP A 292    18255   8370   7922    419  -1734   -343       C  
ATOM   3604  O   TRP A 292     -16.218  41.193  48.217  1.00 84.16           O  
ANISOU 3604  O   TRP A 292    17121   7702   7151    529  -1819   -384       O  
ATOM   3605  CB  TRP A 292     -16.431  39.155  50.816  1.00114.94           C  
ANISOU 3605  CB  TRP A 292    21845  11094  10733    460  -2038   -365       C  
ATOM   3606  CG  TRP A 292     -15.878  38.302  49.715  1.00103.39           C  
ANISOU 3606  CG  TRP A 292    20218   9734   9329    639  -2203   -429       C  
ATOM   3607  CD1 TRP A 292     -14.605  37.817  49.608  1.00101.84           C  
ANISOU 3607  CD1 TRP A 292    19994   9601   9100    825  -2456   -500       C  
ATOM   3608  CD2 TRP A 292     -16.576  37.849  48.540  1.00104.13           C  
ANISOU 3608  CD2 TRP A 292    20152   9893   9517    666  -2128   -430       C  
ATOM   3609  NE1 TRP A 292     -14.472  37.081  48.462  1.00100.38           N  
ANISOU 3609  NE1 TRP A 292    19655   9514   8970    984  -2540   -552       N  
ATOM   3610  CE2 TRP A 292     -15.660  37.088  47.784  1.00111.68           C  
ANISOU 3610  CE2 TRP A 292    21011  10937  10482    883  -2346   -511       C  
ATOM   3611  CE3 TRP A 292     -17.881  38.006  48.057  1.00104.74           C  
ANISOU 3611  CE3 TRP A 292    20159   9971   9663    536  -1903   -371       C  
ATOM   3612  CZ2 TRP A 292     -16.009  36.488  46.574  1.00102.13           C  
ANISOU 3612  CZ2 TRP A 292    19662   9796   9345    971  -2350   -537       C  
ATOM   3613  CZ3 TRP A 292     -18.226  37.414  46.862  1.00103.00           C  
ANISOU 3613  CZ3 TRP A 292    19790   9818   9524    603  -1912   -389       C  
ATOM   3614  CH2 TRP A 292     -17.300  36.666  46.132  1.00 95.38           C  
ANISOU 3614  CH2 TRP A 292    18754   8919   8563    817  -2134   -473       C  
ATOM   3615  N   LEU A 293     -18.314  41.012  49.098  1.00 93.58           N  
ANISOU 3615  N   LEU A 293    18615   8658   8280    309  -1518   -290       N  
ATOM   3616  CA  LEU A 293     -19.049  41.365  47.881  1.00 81.92           C  
ANISOU 3616  CA  LEU A 293    16861   7324   6940    301  -1356   -276       C  
ATOM   3617  C   LEU A 293     -18.671  42.749  47.374  1.00 58.58           C  
ANISOU 3617  C   LEU A 293    13657   4530   4071    307  -1285   -283       C  
ATOM   3618  O   LEU A 293     -18.225  42.868  46.158  1.00 57.47           O  
ANISOU 3618  O   LEU A 293    13228   4567   4041    393  -1329   -315       O  
ATOM   3619  CB  LEU A 293     -20.556  41.305  48.173  1.00 72.70           C  
ANISOU 3619  CB  LEU A 293    15791   6078   5751    161  -1128   -203       C  
ATOM   3620  CG  LEU A 293     -21.481  41.877  47.097  1.00 60.88           C  
ANISOU 3620  CG  LEU A 293    14024   4722   4386    131   -925   -175       C  
ATOM   3621  CD1 LEU A 293     -21.378  41.082  45.800  1.00 70.57           C  
ANISOU 3621  CD1 LEU A 293    15065   6032   5714    215  -1017   -206       C  
ATOM   3622  CD2 LEU A 293     -22.917  41.908  47.595  1.00 54.95           C  
ANISOU 3622  CD2 LEU A 293    13372   3920   3585     -4   -699    -94       C  
ATOM   3623  N   ALA A 294     -18.806  43.750  48.244  1.00 59.34           N  
ANISOU 3623  N   ALA A 294    13872   4566   4106    223  -1192   -254       N  
ATOM   3624  CA  ALA A 294     -18.455  45.141  47.925  1.00 66.66           C  
ANISOU 3624  CA  ALA A 294    14634   5605   5088    204  -1148   -252       C  
ATOM   3625  C   ALA A 294     -17.024  45.239  47.407  1.00 63.14           C  
ANISOU 3625  C   ALA A 294    14008   5305   4677    282  -1364   -289       C  
ATOM   3626  O   ALA A 294     -16.792  45.941  46.392  1.00 77.63           O  
ANISOU 3626  O   ALA A 294    15568   7315   6612    291  -1343   -288       O  
ATOM   3627  CB  ALA A 294     -18.675  46.025  49.130  1.00 78.76           C  
ANISOU 3627  CB  ALA A 294    16408   7007   6510    122  -1072   -224       C  
ATOM   3628  N   MET A 295     -16.107  44.491  48.008  1.00 64.18           N  
ANISOU 3628  N   MET A 295    14271   5388   4726    344  -1570   -317       N  
ATOM   3629  CA  MET A 295     -14.696  44.538  47.581  1.00 76.24           C  
ANISOU 3629  CA  MET A 295    15610   7091   6267    431  -1785   -347       C  
ATOM   3630  C   MET A 295     -14.513  43.742  46.288  1.00 69.69           C  
ANISOU 3630  C   MET A 295    14522   6430   5524    571  -1835   -389       C  
ATOM   3631  O   MET A 295     -13.579  44.022  45.509  1.00 72.05           O  
ANISOU 3631  O   MET A 295    14550   6958   5867    642  -1939   -404       O  
ATOM   3632  CB  MET A 295     -13.787  43.940  48.663  1.00115.78           C  
ANISOU 3632  CB  MET A 295    20844  11998  11149    476  -1998   -368       C  
ATOM   3633  CG  MET A 295     -13.728  44.754  49.954  1.00130.43           C  
ANISOU 3633  CG  MET A 295    22956  13697  12901    349  -1991   -331       C  
ATOM   3634  SD  MET A 295     -13.086  46.429  49.734  1.00167.15           S  
ANISOU 3634  SD  MET A 295    27435  18491  17582    242  -2005   -287       S  
ATOM   3635  CE  MET A 295     -11.438  46.073  49.127  1.00128.87           C  
ANISOU 3635  CE  MET A 295    22305  13910  12747    351  -2279   -308       C  
ATOM   3636  N   SER A 296     -15.376  42.761  46.073  1.00 71.98           N  
ANISOU 3636  N   SER A 296    14903   6617   5827    606  -1771   -403       N  
ATOM   3637  CA  SER A 296     -15.263  41.882  44.879  1.00 69.38           C  
ANISOU 3637  CA  SER A 296    14387   6412   5563    754  -1836   -450       C  
ATOM   3638  C   SER A 296     -15.732  42.622  43.633  1.00 60.97           C  
ANISOU 3638  C   SER A 296    13015   5520   4631    725  -1679   -432       C  
ATOM   3639  O   SER A 296     -15.468  42.142  42.516  1.00 54.53           O  
ANISOU 3639  O   SER A 296    11990   4856   3871    852  -1734   -471       O  
ATOM   3640  CB  SER A 296     -15.998  40.585  45.090  1.00 71.88           C  
ANISOU 3640  CB  SER A 296    14937   6538   5832    779  -1853   -461       C  
ATOM   3641  OG  SER A 296     -17.402  40.794  45.128  1.00 77.81           O  
ANISOU 3641  OG  SER A 296    15753   7189   6622    629  -1628   -402       O  
ATOM   3642  N   SER A 297     -16.392  43.767  43.823  1.00 55.36           N  
ANISOU 3642  N   SER A 297    12290   4784   3957    576  -1498   -379       N  
ATOM   3643  CA  SER A 297     -16.854  44.599  42.692  1.00 47.04           C  
ANISOU 3643  CA  SER A 297    10964   3882   3025    538  -1352   -358       C  
ATOM   3644  C   SER A 297     -15.663  45.009  41.844  1.00 53.45           C  
ANISOU 3644  C   SER A 297    11486   4949   3873    609  -1480   -376       C  
ATOM   3645  O   SER A 297     -15.823  45.262  40.632  1.00 76.99           O  
ANISOU 3645  O   SER A 297    14207   8094   6951    632  -1416   -377       O  
ATOM   3646  CB  SER A 297     -17.585  45.810  43.197  1.00 38.14           C  
ANISOU 3646  CB  SER A 297     9914   2676   1902    392  -1176   -306       C  
ATOM   3647  OG  SER A 297     -16.683  46.699  43.830  1.00 36.87           O  
ANISOU 3647  OG  SER A 297     9796   2532   1679    340  -1274   -292       O  
ATOM   3648  N   THR A 298     -14.498  45.083  42.474  1.00 48.42           N  
ANISOU 3648  N   THR A 298    10886   4357   3153    634  -1656   -384       N  
ATOM   3649  CA  THR A 298     -13.291  45.636  41.849  1.00 55.80           C  
ANISOU 3649  CA  THR A 298    11539   5564   4096    664  -1782   -378       C  
ATOM   3650  C   THR A 298     -12.689  44.676  40.831  1.00 52.42           C  
ANISOU 3650  C   THR A 298    10891   5342   3684    866  -1892   -436       C  
ATOM   3651  O   THR A 298     -11.963  45.139  39.928  1.00 59.82           O  
ANISOU 3651  O   THR A 298    11518   6558   4651    894  -1936   -425       O  
ATOM   3652  CB  THR A 298     -12.266  46.039  42.917  1.00 74.51           C  
ANISOU 3652  CB  THR A 298    14024   7924   6362    611  -1943   -355       C  
ATOM   3653  OG1 THR A 298     -11.833  44.845  43.568  1.00 93.04           O  
ANISOU 3653  OG1 THR A 298    16542  10184   8623    749  -2091   -407       O  
ATOM   3654  CG2 THR A 298     -12.817  47.013  43.938  1.00 70.59           C  
ANISOU 3654  CG2 THR A 298    13774   7217   5830    429  -1849   -304       C  
ATOM   3655  N   MET A 299     -12.987  43.385  40.961  1.00 51.22           N  
ANISOU 3655  N   MET A 299    10902   5058   3500   1002  -1940   -493       N  
ATOM   3656  CA  MET A 299     -12.392  42.359  40.070  1.00 56.63           C  
ANISOU 3656  CA  MET A 299    11434   5910   4172   1236  -2072   -564       C  
ATOM   3657  C   MET A 299     -13.330  41.992  38.927  1.00 56.01           C  
ANISOU 3657  C   MET A 299    11259   5836   4186   1275  -1946   -582       C  
ATOM   3658  O   MET A 299     -12.890  41.310  37.983  1.00 61.19           O  
ANISOU 3658  O   MET A 299    11756   6656   4837   1471  -2034   -640       O  
ATOM   3659  CB  MET A 299     -11.988  41.082  40.824  1.00 59.44           C  
ANISOU 3659  CB  MET A 299    12047   6121   4414   1396  -2257   -626       C  
ATOM   3660  CG  MET A 299     -13.137  40.385  41.527  1.00 70.16           C  
ANISOU 3660  CG  MET A 299    13760   7142   5753   1321  -2189   -621       C  
ATOM   3661  SD  MET A 299     -12.808  38.629  41.863  1.00101.55           S  
ANISOU 3661  SD  MET A 299    18015  10960   9607   1547  -2425   -705       S  
ATOM   3662  CE  MET A 299     -13.344  37.862  40.334  1.00 77.32           C  
ANISOU 3662  CE  MET A 299    14809   7965   6604   1694  -2401   -754       C  
ATOM   3663  N   TYR A 300     -14.470  42.652  38.821  1.00 52.05           N  
ANISOU 3663  N   TYR A 300    10778   5226   3770   1100  -1742   -529       N  
ATOM   3664  CA  TYR A 300     -15.510  42.257  37.853  1.00 61.21           C  
ANISOU 3664  CA  TYR A 300    11883   6355   5016   1113  -1621   -535       C  
ATOM   3665  C   TYR A 300     -15.320  42.920  36.488  1.00 61.36           C  
ANISOU 3665  C   TYR A 300    11550   6638   5126   1135  -1560   -530       C  
ATOM   3666  O   TYR A 300     -15.539  42.274  35.440  1.00 51.45           O  
ANISOU 3666  O   TYR A 300    10186   5455   3907   1255  -1566   -570       O  
ATOM   3667  CB  TYR A 300     -16.892  42.572  38.433  1.00 67.04           C  
ANISOU 3667  CB  TYR A 300    12813   6866   5793    926  -1430   -477       C  
ATOM   3668  CG  TYR A 300     -17.301  41.726  39.611  1.00 60.49           C  
ANISOU 3668  CG  TYR A 300    12333   5779   4872    897  -1471   -474       C  
ATOM   3669  CD1 TYR A 300     -16.750  40.475  39.838  1.00 62.83           C  
ANISOU 3669  CD1 TYR A 300    12786   6006   5079   1046  -1668   -531       C  
ATOM   3670  CD2 TYR A 300     -18.278  42.171  40.487  1.00 73.82           C  
ANISOU 3670  CD2 TYR A 300    14202   7294   6550    725  -1313   -413       C  
ATOM   3671  CE1 TYR A 300     -17.142  39.699  40.917  1.00 79.84           C  
ANISOU 3671  CE1 TYR A 300    15279   7914   7140    999  -1715   -520       C  
ATOM   3672  CE2 TYR A 300     -18.683  41.408  41.569  1.00 83.46           C  
ANISOU 3672  CE2 TYR A 300    15739   8296   7674    678  -1342   -399       C  
ATOM   3673  CZ  TYR A 300     -18.115  40.166  41.783  1.00 97.41           C  
ANISOU 3673  CZ  TYR A 300    17670   9984   9357    802  -1548   -448       C  
ATOM   3674  OH  TYR A 300     -18.517  39.420  42.853  1.00102.28           O  
ANISOU 3674  OH  TYR A 300    18614  10377   9870    737  -1587   -426       O  
ATOM   3675  N   ASN A 301     -15.048  44.223  36.523  1.00 57.97           N  
ANISOU 3675  N   ASN A 301    10976   6322   4727    998  -1496   -475       N  
ATOM   3676  CA  ASN A 301     -14.964  45.072  35.317  1.00 53.46           C  
ANISOU 3676  CA  ASN A 301    10090   5983   4238    962  -1423   -449       C  
ATOM   3677  C   ASN A 301     -14.011  44.522  34.266  1.00 50.12           C  
ANISOU 3677  C   ASN A 301     9408   5841   3791   1156  -1546   -499       C  
ATOM   3678  O   ASN A 301     -14.347  44.567  33.087  1.00 55.25           O  
ANISOU 3678  O   ASN A 301     9867   6613   4511   1190  -1474   -505       O  
ATOM   3679  CB  ASN A 301     -14.568  46.505  35.675  1.00 60.51           C  
ANISOU 3679  CB  ASN A 301    10915   6946   5130    783  -1399   -378       C  
ATOM   3680  CG  ASN A 301     -15.651  47.257  36.417  1.00 64.46           C  
ANISOU 3680  CG  ASN A 301    11628   7203   5660    612  -1243   -332       C  
ATOM   3681  OD1 ASN A 301     -16.645  46.668  36.837  1.00 60.49           O  
ANISOU 3681  OD1 ASN A 301    11325   6490   5167    617  -1153   -346       O  
ATOM   3682  ND2 ASN A 301     -15.461  48.555  36.593  1.00 55.66           N  
ANISOU 3682  ND2 ASN A 301    10481   6121   4545    461  -1220   -274       N  
ATOM   3683  N   PRO A 302     -12.759  44.149  34.615  1.00 53.54           N  
ANISOU 3683  N   PRO A 302     9797   6422   4122   1282  -1728   -528       N  
ATOM   3684  CA  PRO A 302     -11.829  43.703  33.593  1.00 57.40           C  
ANISOU 3684  CA  PRO A 302    10010   7227   4570   1488  -1834   -575       C  
ATOM   3685  C   PRO A 302     -12.316  42.452  32.861  1.00 58.29           C  
ANISOU 3685  C   PRO A 302    10184   7276   4687   1700  -1850   -659       C  
ATOM   3686  O   PRO A 302     -11.971  42.263  31.680  1.00 51.85           O  
ANISOU 3686  O   PRO A 302     9123   6705   3871   1846  -1866   -692       O  
ATOM   3687  CB  PRO A 302     -10.531  43.433  34.376  1.00 69.81           C  
ANISOU 3687  CB  PRO A 302    11585   8920   6018   1591  -2030   -591       C  
ATOM   3688  CG  PRO A 302     -11.003  43.165  35.796  1.00 69.83           C  
ANISOU 3688  CG  PRO A 302    11968   8572   5993   1506  -2044   -590       C  
ATOM   3689  CD  PRO A 302     -12.196  44.081  35.975  1.00 64.55           C  
ANISOU 3689  CD  PRO A 302    11400   7701   5424   1255  -1842   -522       C  
ATOM   3690  N   ILE A 303     -13.090  41.626  33.573  1.00 58.46           N  
ANISOU 3690  N   ILE A 303    10539   6975   4699   1706  -1856   -687       N  
ATOM   3691  CA  ILE A 303     -13.716  40.439  32.968  1.00 51.56           C  
ANISOU 3691  CA  ILE A 303     9788   5976   3823   1861  -1883   -752       C  
ATOM   3692  C   ILE A 303     -14.846  40.864  32.049  1.00 46.49           C  
ANISOU 3692  C   ILE A 303     9050   5305   3308   1734  -1699   -713       C  
ATOM   3693  O   ILE A 303     -14.964  40.338  30.936  1.00 40.67           O  
ANISOU 3693  O   ILE A 303     8208   4658   2584   1875  -1715   -759       O  
ATOM   3694  CB  ILE A 303     -14.168  39.364  33.974  1.00 52.65           C  
ANISOU 3694  CB  ILE A 303    10321   5786   3895   1887  -1972   -781       C  
ATOM   3695  CG1 ILE A 303     -13.020  38.911  34.881  1.00 57.44           C  
ANISOU 3695  CG1 ILE A 303    11035   6416   4372   2029  -2171   -825       C  
ATOM   3696  CG2 ILE A 303     -14.789  38.184  33.234  1.00 46.88           C  
ANISOU 3696  CG2 ILE A 303     9719   4934   3156   2026  -2023   -837       C  
ATOM   3697  CD1 ILE A 303     -13.435  37.957  35.990  1.00 52.16           C  
ANISOU 3697  CD1 ILE A 303    10778   5412   3628   2022  -2264   -841       C  
ATOM   3698  N   ILE A 304     -15.649  41.795  32.525  1.00 53.51           N  
ANISOU 3698  N   ILE A 304     9984   6070   4277   1488  -1536   -634       N  
ATOM   3699  CA  ILE A 304     -16.794  42.325  31.763  1.00 60.79           C  
ANISOU 3699  CA  ILE A 304    10817   6958   5322   1354  -1352   -589       C  
ATOM   3700  C   ILE A 304     -16.298  42.938  30.459  1.00 56.55           C  
ANISOU 3700  C   ILE A 304     9934   6721   4829   1403  -1328   -590       C  
ATOM   3701  O   ILE A 304     -16.978  42.746  29.385  1.00 62.29           O  
ANISOU 3701  O   ILE A 304    10570   7469   5627   1427  -1257   -598       O  
ATOM   3702  CB  ILE A 304     -17.563  43.368  32.605  1.00 69.72           C  
ANISOU 3702  CB  ILE A 304    12043   7940   6505   1112  -1193   -509       C  
ATOM   3703  CG1 ILE A 304     -18.274  42.718  33.797  1.00 79.49           C  
ANISOU 3703  CG1 ILE A 304    13617   8888   7696   1051  -1184   -498       C  
ATOM   3704  CG2 ILE A 304     -18.526  44.168  31.737  1.00 52.84           C  
ANISOU 3704  CG2 ILE A 304     9751   5836   4489    993  -1013   -462       C  
ATOM   3705  CD1 ILE A 304     -18.821  43.706  34.810  1.00 76.42           C  
ANISOU 3705  CD1 ILE A 304    13344   8374   7318    858  -1050   -432       C  
ATOM   3706  N   TYR A 305     -15.124  43.551  30.511  1.00 52.39           N  
ANISOU 3706  N   TYR A 305     9224   6431   4251   1421  -1401   -580       N  
ATOM   3707  CA  TYR A 305     -14.532  44.230  29.328  1.00 55.46           C  
ANISOU 3707  CA  TYR A 305     9264   7147   4661   1439  -1384   -563       C  
ATOM   3708  C   TYR A 305     -14.220  43.233  28.225  1.00 45.47           C  
ANISOU 3708  C   TYR A 305     7878   6040   3356   1693  -1462   -643       C  
ATOM   3709  O   TYR A 305     -14.574  43.492  27.081  1.00 36.19           O  
ANISOU 3709  O   TYR A 305     6524   4982   2243   1689  -1380   -635       O  
ATOM   3710  CB  TYR A 305     -13.245  44.980  29.693  1.00 59.81           C  
ANISOU 3710  CB  TYR A 305     9644   7941   5137   1397  -1476   -523       C  
ATOM   3711  CG  TYR A 305     -13.408  46.223  30.535  1.00 59.67           C  
ANISOU 3711  CG  TYR A 305     9700   7821   5149   1134  -1411   -436       C  
ATOM   3712  CD1 TYR A 305     -14.654  46.761  30.838  1.00 50.02           C  
ANISOU 3712  CD1 TYR A 305     8647   6338   4017    966  -1256   -398       C  
ATOM   3713  CD2 TYR A 305     -12.288  46.877  31.024  1.00 66.84           C  
ANISOU 3713  CD2 TYR A 305    10508   8906   5982   1062  -1517   -387       C  
ATOM   3714  CE1 TYR A 305     -14.778  47.892  31.629  1.00 51.42           C  
ANISOU 3714  CE1 TYR A 305     8921   6414   4199    760  -1211   -329       C  
ATOM   3715  CE2 TYR A 305     -12.397  48.013  31.808  1.00 63.75           C  
ANISOU 3715  CE2 TYR A 305    10219   8402   5599    826  -1485   -309       C  
ATOM   3716  CZ  TYR A 305     -13.645  48.522  32.112  1.00 62.63           C  
ANISOU 3716  CZ  TYR A 305    10274   7982   5541    687  -1332   -286       C  
ATOM   3717  OH  TYR A 305     -13.744  49.635  32.893  1.00 77.43           O  
ANISOU 3717  OH  TYR A 305    12278   9736   7405    486  -1310   -219       O  
ATOM   3718  N   CYS A 306     -13.554  42.134  28.550  1.00 46.65           N  
ANISOU 3718  N   CYS A 306     8134   6193   3395   1921  -1624   -721       N  
ATOM   3719  CA  CYS A 306     -13.153  41.158  27.511  1.00 49.08           C  
ANISOU 3719  CA  CYS A 306     8348   6663   3636   2210  -1721   -811       C  
ATOM   3720  C   CYS A 306     -14.336  40.292  27.088  1.00 50.02           C  
ANISOU 3720  C   CYS A 306     8686   6513   3805   2246  -1690   -849       C  
ATOM   3721  O   CYS A 306     -14.351  39.800  25.930  1.00 44.22           O  
ANISOU 3721  O   CYS A 306     7849   5895   3056   2417  -1713   -902       O  
ATOM   3722  CB  CYS A 306     -12.010  40.280  28.000  1.00 48.34           C  
ANISOU 3722  CB  CYS A 306     8307   6668   3389   2472  -1924   -889       C  
ATOM   3723  SG  CYS A 306     -12.582  39.008  29.150  1.00 53.12           S  
ANISOU 3723  SG  CYS A 306     9397   6838   3945   2536  -2041   -945       S  
ATOM   3724  N   CYS A 307     -15.293  40.096  27.967  1.00 55.24           N  
ANISOU 3724  N   CYS A 307     9636   6839   4513   2089  -1645   -817       N  
ATOM   3725  CA  CYS A 307     -16.483  39.265  27.710  1.00 70.58           C  
ANISOU 3725  CA  CYS A 307    11807   8514   6496   2073  -1625   -828       C  
ATOM   3726  C   CYS A 307     -17.460  39.949  26.763  1.00 70.19           C  
ANISOU 3726  C   CYS A 307    11600   8488   6581   1917  -1448   -772       C  
ATOM   3727  O   CYS A 307     -18.147  39.235  25.992  1.00 79.54           O  
ANISOU 3727  O   CYS A 307    12857   9579   7785   1976  -1462   -797       O  
ATOM   3728  CB  CYS A 307     -17.167  38.949  29.038  1.00 72.04           C  
ANISOU 3728  CB  CYS A 307    12321   8374   6675   1921  -1622   -790       C  
ATOM   3729  SG  CYS A 307     -18.381  37.607  28.946  1.00 84.03           S  
ANISOU 3729  SG  CYS A 307    14177   9565   8185   1916  -1677   -800       S  
ATOM   3730  N   LEU A 308     -17.594  41.256  26.888  1.00 58.28           N  
ANISOU 3730  N   LEU A 308     9923   7065   5156   1716  -1300   -696       N  
ATOM   3731  CA  LEU A 308     -18.500  42.009  25.969  1.00 50.45           C  
ANISOU 3731  CA  LEU A 308     8771   6104   4290   1573  -1135   -642       C  
ATOM   3732  C   LEU A 308     -17.771  42.459  24.694  1.00 50.55           C  
ANISOU 3732  C   LEU A 308     8462   6443   4302   1673  -1139   -661       C  
ATOM   3733  O   LEU A 308     -18.170  42.062  23.532  1.00 55.33           O  
ANISOU 3733  O   LEU A 308     8994   7092   4937   1758  -1129   -689       O  
ATOM   3734  CB  LEU A 308     -19.100  43.213  26.707  1.00 46.64           C  
ANISOU 3734  CB  LEU A 308     8299   5532   3888   1319   -979   -554       C  
ATOM   3735  CG  LEU A 308     -20.497  42.994  27.287  1.00 50.46           C  
ANISOU 3735  CG  LEU A 308     9007   5733   4432   1174   -875   -509       C  
ATOM   3736  CD1 LEU A 308     -21.533  42.954  26.170  1.00 58.56           C  
ANISOU 3736  CD1 LEU A 308     9943   6748   5558   1135   -780   -489       C  
ATOM   3737  CD2 LEU A 308     -20.554  41.726  28.135  1.00 42.52           C  
ANISOU 3737  CD2 LEU A 308     8296   4521   3338   1245   -995   -543       C  
ATOM   3738  N   ASN A 309     -16.705  43.226  24.944  1.00 41.84           N  
ANISOU 3738  N   ASN A 309     7182   5563   3151   1657  -1166   -640       N  
ATOM   3739  CA  ASN A 309     -15.911  43.888  23.884  1.00 32.20           C  
ANISOU 3739  CA  ASN A 309     5625   4694   1913   1694  -1161   -628       C  
ATOM   3740  C   ASN A 309     -14.767  42.975  23.421  1.00 31.72           C  
ANISOU 3740  C   ASN A 309     5460   4876   1715   1993  -1317   -715       C  
ATOM   3741  O   ASN A 309     -14.000  42.437  24.215  1.00 30.30           O  
ANISOU 3741  O   ASN A 309     5371   4707   1435   2118  -1444   -755       O  
ATOM   3742  CB  ASN A 309     -15.374  45.230  24.377  1.00 30.99           C  
ANISOU 3742  CB  ASN A 309     5336   4668   1767   1489  -1122   -542       C  
ATOM   3743  CG  ASN A 309     -14.463  45.897  23.374  1.00 31.43           C  
ANISOU 3743  CG  ASN A 309     5048   5110   1784   1498  -1135   -512       C  
ATOM   3744  OD1 ASN A 309     -13.244  45.790  23.494  1.00 31.66           O  
ANISOU 3744  OD1 ASN A 309     4932   5397   1700   1602  -1248   -521       O  
ATOM   3745  ND2 ASN A 309     -15.044  46.551  22.376  1.00 29.10           N  
ANISOU 3745  ND2 ASN A 309     4614   4869   1572   1392  -1026   -471       N  
ATOM   3746  N   ASP A 310     -14.667  42.848  22.120  1.00 38.79           N  
ANISOU 3746  N   ASP A 310     6160   5975   2600   2113  -1305   -743       N  
ATOM   3747  CA  ASP A 310     -13.648  41.956  21.505  1.00 43.33           C  
ANISOU 3747  CA  ASP A 310     6623   6809   3029   2442  -1443   -836       C  
ATOM   3748  C   ASP A 310     -12.270  42.601  21.541  1.00 53.44           C  
ANISOU 3748  C   ASP A 310     7601   8489   4212   2466  -1489   -802       C  
ATOM   3749  O   ASP A 310     -11.307  41.869  21.503  1.00 64.20           O  
ANISOU 3749  O   ASP A 310     8904  10053   5435   2739  -1621   -875       O  
ATOM   3750  CB  ASP A 310     -14.042  41.557  20.085  1.00 43.60           C  
ANISOU 3750  CB  ASP A 310     6570   6925   3070   2578  -1415   -882       C  
ATOM   3751  CG  ASP A 310     -15.351  40.791  20.023  1.00 48.26           C  
ANISOU 3751  CG  ASP A 310     7463   7134   3739   2561  -1401   -911       C  
ATOM   3752  OD1 ASP A 310     -16.039  40.712  21.074  1.00 53.14           O  
ANISOU 3752  OD1 ASP A 310     8330   7441   4417   2405  -1384   -879       O  
ATOM   3753  OD2 ASP A 310     -15.668  40.265  18.928  1.00 45.20           O  
ANISOU 3753  OD2 ASP A 310     7061   6772   3338   2700  -1414   -960       O  
ATOM   3754  N   ARG A 311     -12.206  43.926  21.500  1.00 64.40           N  
ANISOU 3754  N   ARG A 311     8799  10005   5665   2194  -1391   -692       N  
ATOM   3755  CA  ARG A 311     -10.934  44.645  21.365  1.00 62.55           C  
ANISOU 3755  CA  ARG A 311     8242  10186   5336   2165  -1435   -632       C  
ATOM   3756  C   ARG A 311     -10.065  44.370  22.589  1.00 57.76           C  
ANISOU 3756  C   ARG A 311     7714   9593   4636   2224  -1566   -642       C  
ATOM   3757  O   ARG A 311      -8.853  44.143  22.454  1.00 56.93           O  
ANISOU 3757  O   ARG A 311     7388   9849   4393   2400  -1672   -658       O  
ATOM   3758  CB  ARG A 311     -11.152  46.152  21.165  1.00 77.76           C  
ANISOU 3758  CB  ARG A 311    10017  12177   7349   1818  -1324   -501       C  
ATOM   3759  CG  ARG A 311     -12.100  46.535  20.030  1.00101.77           C  
ANISOU 3759  CG  ARG A 311    13002  15170  10494   1730  -1193   -482       C  
ATOM   3760  CD  ARG A 311     -11.441  46.558  18.659  1.00112.31           C  
ANISOU 3760  CD  ARG A 311    14005  16920  11746   1853  -1193   -483       C  
ATOM   3761  NE  ARG A 311     -10.297  47.470  18.580  1.00136.04           N  
ANISOU 3761  NE  ARG A 311    16706  20320  14659   1719  -1231   -383       N  
ATOM   3762  CZ  ARG A 311      -9.388  47.496  17.600  1.00131.86           C  
ANISOU 3762  CZ  ARG A 311    15842  20250  14009   1829  -1255   -368       C  
ATOM   3763  NH1 ARG A 311      -9.470  46.661  16.576  1.00139.44           N  
ANISOU 3763  NH1 ARG A 311    16733  21327  14919   2102  -1242   -460       N  
ATOM   3764  NH2 ARG A 311      -8.390  48.365  17.648  1.00117.67           N  
ANISOU 3764  NH2 ARG A 311    13778  18803  12127   1658  -1297   -253       N  
ATOM   3765  N   PHE A 312     -10.688  44.375  23.760  1.00 60.55           N  
ANISOU 3765  N   PHE A 312     8373   9573   5057   2088  -1559   -632       N  
ATOM   3766  CA  PHE A 312     -10.011  44.038  25.024  1.00 65.37           C  
ANISOU 3766  CA  PHE A 312     9122  10125   5587   2138  -1687   -647       C  
ATOM   3767  C   PHE A 312      -9.612  42.569  25.005  1.00 55.33           C  
ANISOU 3767  C   PHE A 312     7959   8858   4203   2508  -1826   -776       C  
ATOM   3768  O   PHE A 312      -8.483  42.204  25.333  1.00 87.70           O  
ANISOU 3768  O   PHE A 312    11961  13187   8173   2689  -1964   -807       O  
ATOM   3769  CB  PHE A 312     -10.909  44.322  26.233  1.00 77.60           C  
ANISOU 3769  CB  PHE A 312    11003  11253   7229   1917  -1633   -612       C  
ATOM   3770  CG  PHE A 312     -11.033  45.785  26.565  1.00 90.53           C  
ANISOU 3770  CG  PHE A 312    12576  12888   8934   1586  -1547   -491       C  
ATOM   3771  CD1 PHE A 312      -9.962  46.472  27.115  1.00 88.90           C  
ANISOU 3771  CD1 PHE A 312    12236  12891   8651   1482  -1637   -422       C  
ATOM   3772  CD2 PHE A 312     -12.211  46.476  26.315  1.00 90.28           C  
ANISOU 3772  CD2 PHE A 312    12623  12646   9031   1385  -1391   -446       C  
ATOM   3773  CE1 PHE A 312     -10.067  47.821  27.416  1.00115.21           C  
ANISOU 3773  CE1 PHE A 312    15548  16196  12029   1173  -1585   -310       C  
ATOM   3774  CE2 PHE A 312     -12.316  47.823  26.619  1.00109.54           C  
ANISOU 3774  CE2 PHE A 312    15038  15066  11516   1105  -1332   -343       C  
ATOM   3775  CZ  PHE A 312     -11.244  48.492  27.169  1.00152.90           C  
ANISOU 3775  CZ  PHE A 312    20429  20742  16925    996  -1435   -276       C  
ATOM   3776  N   ARG A 313     -10.566  41.732  24.627  1.00 46.38           N  
ANISOU 3776  N   ARG A 313     7044   7463   3115   2616  -1800   -849       N  
ATOM   3777  CA  ARG A 313     -10.386  40.270  24.635  1.00 51.82           C  
ANISOU 3777  CA  ARG A 313     7930   8063   3697   2957  -1950   -976       C  
ATOM   3778  C   ARG A 313      -9.181  39.881  23.788  1.00 53.83           C  
ANISOU 3778  C   ARG A 313     7896   8756   3798   3279  -2050  -1041       C  
ATOM   3779  O   ARG A 313      -8.392  39.025  24.214  1.00 63.92           O  
ANISOU 3779  O   ARG A 313     9248  10098   4939   3556  -2216  -1123       O  
ATOM   3780  CB  ARG A 313     -11.621  39.501  24.153  1.00 56.25           C  
ANISOU 3780  CB  ARG A 313     8748   8301   4323   2993  -1914  -1027       C  
ATOM   3781  CG  ARG A 313     -11.591  38.016  24.496  1.00 61.60           C  
ANISOU 3781  CG  ARG A 313     9748   8765   4892   3276  -2094  -1142       C  
ATOM   3782  CD  ARG A 313     -12.803  37.232  24.021  1.00 64.24           C  
ANISOU 3782  CD  ARG A 313    10353   8777   5278   3283  -2085  -1177       C  
ATOM   3783  NE  ARG A 313     -12.971  37.275  22.572  1.00 66.91           N  
ANISOU 3783  NE  ARG A 313    10494   9298   5629   3381  -2027  -1200       N  
ATOM   3784  CZ  ARG A 313     -13.842  38.043  21.914  1.00 72.07           C  
ANISOU 3784  CZ  ARG A 313    11028   9931   6423   3148  -1855  -1126       C  
ATOM   3785  NH1 ARG A 313     -14.664  38.856  22.565  1.00 65.19           N  
ANISOU 3785  NH1 ARG A 313    10210   8867   5691   2812  -1716  -1024       N  
ATOM   3786  NH2 ARG A 313     -13.886  37.987  20.592  1.00 72.10           N  
ANISOU 3786  NH2 ARG A 313    10866  10112   6417   3269  -1826  -1157       N  
ATOM   3787  N   LEU A 314      -9.050  40.496  22.623  1.00 56.56           N  
ANISOU 3787  N   LEU A 314     7925   9407   4158   3250  -1953  -1004       N  
ATOM   3788  CA  LEU A 314      -7.928  40.220  21.721  1.00 70.44           C  
ANISOU 3788  CA  LEU A 314     9364  11639   5758   3549  -2022  -1054       C  
ATOM   3789  C   LEU A 314      -6.662  40.860  22.262  1.00 70.66           C  
ANISOU 3789  C   LEU A 314     9114  12034   5698   3501  -2079   -984       C  
ATOM   3790  O   LEU A 314      -5.543  40.362  21.975  1.00 73.26           O  
ANISOU 3790  O   LEU A 314     9235  12742   5857   3811  -2191  -1041       O  
ATOM   3791  CB  LEU A 314      -8.250  40.776  20.328  1.00 78.06           C  
ANISOU 3791  CB  LEU A 314    10078  12811   6768   3484  -1886  -1018       C  
ATOM   3792  CG  LEU A 314      -9.470  40.176  19.624  1.00 92.78           C  
ANISOU 3792  CG  LEU A 314    12178  14360   8714   3532  -1834  -1081       C  
ATOM   3793  CD1 LEU A 314      -9.476  40.549  18.149  1.00 97.71           C  
ANISOU 3793  CD1 LEU A 314    12519  15278   9329   3565  -1739  -1068       C  
ATOM   3794  CD2 LEU A 314      -9.534  38.661  19.790  1.00108.57           C  
ANISOU 3794  CD2 LEU A 314    14495  16143  10611   3884  -1995  -1225       C  
ATOM   3795  N   GLY A 315      -6.824  41.936  23.028  1.00 69.85           N  
ANISOU 3795  N   GLY A 315     9011  11833   5697   3129  -2015   -861       N  
ATOM   3796  CA  GLY A 315      -5.697  42.567  23.719  1.00 68.34           C  
ANISOU 3796  CA  GLY A 315     8612  11926   5428   3030  -2091   -779       C  
ATOM   3797  C   GLY A 315      -5.141  41.600  24.752  1.00 77.40           C  
ANISOU 3797  C   GLY A 315     9962  12971   6474   3271  -2264   -864       C  
ATOM   3798  O   GLY A 315      -3.935  41.429  24.901  1.00117.66           O  
ANISOU 3798  O   GLY A 315    14844  18432  11430   3448  -2385   -871       O  
ATOM   3799  N   PHE A 316      -6.050  40.861  25.384  1.00 84.63           N  
ANISOU 3799  N   PHE A 316    11297  13403   7452   3304  -2283   -937       N  
ATOM   3800  CA  PHE A 316      -5.667  39.738  26.264  1.00 83.90           C  
ANISOU 3800  CA  PHE A 316    11465  13154   7256   3570  -2461  -1039       C  
ATOM   3801  C   PHE A 316      -4.959  38.635  25.472  1.00 93.96           C  
ANISOU 3801  C   PHE A 316    12641  14694   8364   4040  -2586  -1170       C  
ATOM   3802  O   PHE A 316      -4.021  38.050  25.974  1.00100.26           O  
ANISOU 3802  O   PHE A 316    13431  15638   9023   4293  -2750  -1228       O  
ATOM   3803  CB  PHE A 316      -6.837  39.175  27.077  1.00 78.92           C  
ANISOU 3803  CB  PHE A 316    11314  11952   6716   3478  -2456  -1074       C  
ATOM   3804  CG  PHE A 316      -7.249  40.013  28.261  1.00 77.94           C  
ANISOU 3804  CG  PHE A 316    11345  11574   6693   3114  -2394   -971       C  
ATOM   3805  CD1 PHE A 316      -8.114  41.085  28.102  1.00 74.48           C  
ANISOU 3805  CD1 PHE A 316    10873  11021   6402   2771  -2210   -871       C  
ATOM   3806  CD2 PHE A 316      -6.791  39.726  29.537  1.00 85.26           C  
ANISOU 3806  CD2 PHE A 316    12468  12367   7558   3129  -2524   -980       C  
ATOM   3807  CE1 PHE A 316      -8.505  41.857  29.184  1.00 73.72           C  
ANISOU 3807  CE1 PHE A 316    10939  10689   6380   2467  -2156   -786       C  
ATOM   3808  CE2 PHE A 316      -7.180  40.499  30.621  1.00 80.39           C  
ANISOU 3808  CE2 PHE A 316    12010  11513   7019   2806  -2466   -890       C  
ATOM   3809  CZ  PHE A 316      -8.033  41.566  30.443  1.00 78.01           C  
ANISOU 3809  CZ  PHE A 316    11677  11108   6856   2484  -2281   -796       C  
ATOM   3810  N   LYS A 317      -5.461  38.345  24.282  1.00111.57           N  
ANISOU 3810  N   LYS A 317    14826  16958  10606   4161  -2514  -1221       N  
ATOM   3811  CA  LYS A 317      -4.891  37.334  23.382  1.00132.47           C  
ANISOU 3811  CA  LYS A 317    17394  19850  13087   4624  -2620  -1353       C  
ATOM   3812  C   LYS A 317      -3.461  37.673  23.069  1.00144.64           C  
ANISOU 3812  C   LYS A 317    18483  21997  14476   4791  -2667  -1329       C  
ATOM   3813  O   LYS A 317      -2.719  36.713  22.844  1.00194.21           O  
ANISOU 3813  O   LYS A 317    24742  28471  20574   5230  -2813  -1451       O  
ATOM   3814  CB  LYS A 317      -5.764  37.226  22.121  1.00136.04           C  
ANISOU 3814  CB  LYS A 317    17853  20237  13598   4641  -2506  -1382       C  
ATOM   3815  CG  LYS A 317      -5.596  35.967  21.276  1.00132.88           C  
ANISOU 3815  CG  LYS A 317    17555  19889  13042   5115  -2627  -1542       C  
ATOM   3816  CD  LYS A 317      -6.121  36.124  19.852  1.00115.01           C  
ANISOU 3816  CD  LYS A 317    15152  17735  10809   5131  -2505  -1548       C  
ATOM   3817  CE  LYS A 317      -6.926  34.941  19.349  1.00111.75           C  
ANISOU 3817  CE  LYS A 317    15120  16972  10367   5366  -2591  -1674       C  
ATOM   3818  NZ  LYS A 317      -6.160  33.673  19.398  1.00116.66           N  
ANISOU 3818  NZ  LYS A 317    15902  17654  10768   5873  -2815  -1833       N  
ATOM   3819  N   HIS A 318      -3.120  38.936  22.926  1.00136.87           N  
ANISOU 3819  N   HIS A 318    17147  21311  13545   4479  -2553  -1183       N  
ATOM   3820  CA  HIS A 318      -1.759  39.421  22.679  1.00127.48           C  
ANISOU 3820  CA  HIS A 318    15486  20734  12214   4551  -2590  -1120       C  
ATOM   3821  C   HIS A 318      -0.738  38.872  23.670  1.00112.23           C  
ANISOU 3821  C   HIS A 318    13572  18922  10146   4775  -2781  -1163       C  
ATOM   3822  O   HIS A 318       0.321  38.368  23.203  1.00149.39           O  
ANISOU 3822  O   HIS A 318    18005  24096  14658   5151  -2876  -1225       O  
ATOM   3823  CB  HIS A 318      -1.767  40.959  22.697  1.00120.33           C  
ANISOU 3823  CB  HIS A 318    14324  19976  11419   4059  -2459   -928       C  
ATOM   3824  CG  HIS A 318      -0.542  41.601  22.142  1.00119.92           C  
ANISOU 3824  CG  HIS A 318    13748  20583  11232   4054  -2465   -829       C  
ATOM   3825  ND1 HIS A 318       0.627  41.710  22.865  1.00111.21           N  
ANISOU 3825  ND1 HIS A 318    12447  19798  10009   4089  -2596   -778       N  
ATOM   3826  CD2 HIS A 318      -0.310  42.195  20.952  1.00129.52           C  
ANISOU 3826  CD2 HIS A 318    14592  22212  12408   3993  -2359   -759       C  
ATOM   3827  CE1 HIS A 318       1.536  42.328  22.137  1.00125.12           C  
ANISOU 3827  CE1 HIS A 318    13721  22160  11658   4048  -2571   -675       C  
ATOM   3828  NE2 HIS A 318       0.986  42.638  20.959  1.00128.80           N  
ANISOU 3828  NE2 HIS A 318    14075  22695  12168   3987  -2424   -662       N  
ATOM   3829  N   ALA A 319      -0.959  39.056  24.966  1.00102.11           N  
ANISOU 3829  N   ALA A 319    12556  17291   8948   4549  -2834  -1120       N  
ATOM   3830  CA  ALA A 319      -0.060  38.489  25.987  1.00116.35           C  
ANISOU 3830  CA  ALA A 319    14426  19152  10629   4755  -3029  -1165       C  
ATOM   3831  C   ALA A 319      -0.771  37.493  26.905  1.00117.68           C  
ANISOU 3831  C   ALA A 319    15144  18736  10831   4864  -3133  -1276       C  
ATOM   3832  O   ALA A 319      -0.502  36.263  26.831  1.00120.02           O  
ANISOU 3832  O   ALA A 319    15611  18998  10993   5302  -3285  -1428       O  
ATOM   3833  CB  ALA A 319       0.580  39.615  26.767  1.00108.75           C  
ANISOU 3833  CB  ALA A 319    13247  18379   9692   4399  -3035  -1001       C  
ATOM   3834  N   PHE A 320      -1.580  38.023  27.808  1.00119.02           N  
ANISOU 3834  N   PHE A 320    15585  18477  11156   4482  -3068  -1199       N  
ATOM   3835  CA  PHE A 320      -2.520  37.236  28.634  1.00114.71           C  
ANISOU 3835  CA  PHE A 320    15572  17340  10670   4480  -3121  -1272       C  
ATOM   3836  C   PHE A 320      -3.527  38.201  29.275  1.00110.18           C  
ANISOU 3836  C   PHE A 320    15167  16410  10285   3992  -2966  -1152       C  
ATOM   3837  O   PHE A 320      -3.229  38.938  30.220  1.00 89.55           O  
ANISOU 3837  O   PHE A 320    12543  13780   7701   3740  -2976  -1057       O  
ATOM   3838  CB  PHE A 320      -1.856  36.369  29.710  1.00109.07           C  
ANISOU 3838  CB  PHE A 320    15087  16524   9831   4720  -3344  -1350       C  
ATOM   3839  CG  PHE A 320      -2.820  35.439  30.417  1.00118.61           C  
ANISOU 3839  CG  PHE A 320    16848  17143  11073   4741  -3411  -1428       C  
ATOM   3840  CD1 PHE A 320      -3.690  35.912  31.392  1.00105.33           C  
ANISOU 3840  CD1 PHE A 320    15445  15048   9527   4358  -3329  -1345       C  
ATOM   3841  CD2 PHE A 320      -2.881  34.092  30.091  1.00136.10           C  
ANISOU 3841  CD2 PHE A 320    19317  19220  13172   5139  -3561  -1579       C  
ATOM   3842  CE1 PHE A 320      -4.585  35.064  32.028  1.00108.54           C  
ANISOU 3842  CE1 PHE A 320    16339  14947   9951   4353  -3385  -1399       C  
ATOM   3843  CE2 PHE A 320      -3.774  33.243  30.732  1.00141.64           C  
ANISOU 3843  CE2 PHE A 320    20538  19384  13895   5121  -3638  -1632       C  
ATOM   3844  CZ  PHE A 320      -4.624  33.730  31.699  1.00128.79           C  
ANISOU 3844  CZ  PHE A 320    19151  17378  12402   4718  -3544  -1537       C  
TER    3845      PHE A 320                                                      
HETATM 3846  F7  L76 A2001     -12.974  53.085  55.700  1.00 43.38           F  
HETATM 3847  C11 L76 A2001     -14.279  53.453  55.784  1.00 88.43           C  
HETATM 3848  C10 L76 A2001     -15.262  52.527  56.147  1.00 64.76           C  
HETATM 3849  C9  L76 A2001     -16.599  52.923  56.226  1.00 66.30           C  
HETATM 3850  C12 L76 A2001     -14.634  54.769  55.501  1.00 70.21           C  
HETATM 3851  C13 L76 A2001     -15.965  55.156  55.575  1.00 79.57           C  
HETATM 3852  C8  L76 A2001     -16.957  54.248  55.943  1.00 91.51           C  
HETATM 3853  C1  L76 A2001     -18.286  54.717  56.011  1.00136.57           C  
HETATM 3854  N1  L76 A2001     -19.183  54.174  57.053  1.00169.40           N  
HETATM 3855  C5  L76 A2001     -18.623  54.161  58.439  1.00190.76           C  
HETATM 3856  C6  L76 A2001     -17.875  55.428  58.849  1.00165.75           C  
HETATM 3857  C7  L76 A2001     -18.361  56.465  59.494  1.00110.98           C  
HETATM 3858  C24 L76 A2001     -19.785  56.671  60.013  1.00 99.84           C  
HETATM 3859  N5  L76 A2001     -19.792  56.637  61.492  1.00117.54           N  
HETATM 3860  C26 L76 A2001     -21.166  56.818  61.990  1.00110.42           C  
HETATM 3861  C25 L76 A2001     -19.191  55.390  62.020  1.00 80.86           C  
HETATM 3862  N4  L76 A2001     -17.358  57.309  59.644  1.00 95.56           N  
HETATM 3863  N3  L76 A2001     -16.334  56.779  59.099  1.00 95.33           N  
HETATM 3864  N2  L76 A2001     -16.590  55.676  58.628  1.00 96.99           N  
HETATM 3865  C4  L76 A2001     -20.516  54.829  56.980  1.00143.89           C  
HETATM 3866  C3  L76 A2001     -21.100  54.656  55.585  1.00134.32           C  
HETATM 3867  O1  L76 A2001     -20.189  55.205  54.676  1.00170.96           O  
HETATM 3868  C2  L76 A2001     -18.956  54.482  54.678  1.00171.24           C  
HETATM 3869  O2  L76 A2001     -19.205  53.061  54.522  1.00209.03           O  
HETATM 3870  C14 L76 A2001     -19.410  52.711  53.156  1.00158.29           C  
HETATM 3871  C21 L76 A2001     -20.146  51.376  53.070  1.00104.03           C  
HETATM 3872  C15 L76 A2001     -18.153  52.666  52.558  1.00135.69           C  
HETATM 3873  C20 L76 A2001     -17.886  53.554  51.527  1.00 90.97           C  
HETATM 3874  C19 L76 A2001     -16.635  53.552  50.935  1.00 85.52           C  
HETATM 3875  C23 L76 A2001     -16.377  54.442  49.922  1.00133.16           C  
HETATM 3876  F6  L76 A2001     -15.088  54.509  49.751  1.00 57.65           F  
HETATM 3877  F5  L76 A2001     -16.851  55.682  50.322  1.00 94.07           F  
HETATM 3878  F4  L76 A2001     -16.976  54.049  48.804  1.00288.58           F  
HETATM 3879  C18 L76 A2001     -15.645  52.682  51.375  1.00 60.76           C  
HETATM 3880  C17 L76 A2001     -15.903  51.795  52.410  1.00 97.57           C  
HETATM 3881  C16 L76 A2001     -17.161  51.798  53.014  1.00113.23           C  
HETATM 3882  C22 L76 A2001     -14.886  50.940  52.828  1.00132.65           C  
HETATM 3883  F1  L76 A2001     -14.632  50.025  51.859  1.00 47.96           F  
HETATM 3884  F2  L76 A2001     -13.795  51.643  53.055  1.00 99.08           F  
HETATM 3885  F3  L76 A2001     -15.238  50.331  53.958  1.00238.11           F  
CONECT  633 1224                                                                
CONECT 1224  633                                                                
CONECT 3846 3847                                                                
CONECT 3847 3846 3848 3850                                                      
CONECT 3848 3847 3849                                                           
CONECT 3849 3848 3852                                                           
CONECT 3850 3847 3851                                                           
CONECT 3851 3850 3852                                                           
CONECT 3852 3849 3851 3853                                                      
CONECT 3853 3852 3854 3868                                                      
CONECT 3854 3853 3855 3865                                                      
CONECT 3855 3854 3856                                                           
CONECT 3856 3855 3857 3864                                                      
CONECT 3857 3856 3858 3862                                                      
CONECT 3858 3857 3859                                                           
CONECT 3859 3858 3860 3861                                                      
CONECT 3860 3859                                                                
CONECT 3861 3859                                                                
CONECT 3862 3857 3863                                                           
CONECT 3863 3862 3864                                                           
CONECT 3864 3856 3863                                                           
CONECT 3865 3854 3866                                                           
CONECT 3866 3865 3867                                                           
CONECT 3867 3866 3868                                                           
CONECT 3868 3853 3867 3869                                                      
CONECT 3869 3868 3870                                                           
CONECT 3870 3869 3871 3872                                                      
CONECT 3871 3870                                                                
CONECT 3872 3870 3873 3881                                                      
CONECT 3873 3872 3874                                                           
CONECT 3874 3873 3875 3879                                                      
CONECT 3875 3874 3876 3877 3878                                                 
CONECT 3876 3875                                                                
CONECT 3877 3875                                                                
CONECT 3878 3875                                                                
CONECT 3879 3874 3880                                                           
CONECT 3880 3879 3881 3882                                                      
CONECT 3881 3872 3880                                                           
CONECT 3882 3880 3883 3884 3885                                                 
CONECT 3883 3882                                                                
CONECT 3884 3882                                                                
CONECT 3885 3882                                                                
MASTER      359    0    1   21    8    0    3    6 3884    1   42   42          
END