CNRS Nantes University UFIP UFIP
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***  BIBR stripped  ***

elNémo ID: 1909031731204319

Job options:

ID        	=	 1909031731204319
JOBID     	=	 BIBR stripped
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER BIBR stripped

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-JUL-15   5CQG              
TITLE     STRUCTURE OF TRIBOLIUM TELOMERASE IN COMPLEX WITH THE HIGHLY SPECIFIC 
TITLE    2 INHIBITOR BIBR1532                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TELOMERASE REVERSE TRANSCRIPTASE;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRIBOLIUM CASTANEUM;                            
SOURCE   3 ORGANISM_COMMON: RED FLOUR BEETLE;                                   
SOURCE   4 ORGANISM_TAXID: 7070;                                                
SOURCE   5 GENE: TERT, TCASGA2_TC010963;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TELOMERASE REVERSE TRANSCRIPTASE FOLD TERT BIBR15312, TELOMERASE      
KEYWDS   2 INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BRYAN,C.RICE,H.HOFFMAN,M.HARKISHEIMER,M.SWEENEY,E.SKORDALAKES       
REVDAT   3   10-OCT-18 5CQG    1       COMPND JRNL                              
REVDAT   2   13-SEP-17 5CQG    1       REMARK                                   
REVDAT   1   09-SEP-15 5CQG    0                                                
JRNL        AUTH   C.BRYAN,C.RICE,H.HOFFMAN,M.HARKISHEIMER,M.SWEENEY,           
JRNL        AUTH 2 E.SKORDALAKES                                                
JRNL        TITL   STRUCTURAL BASIS OF TELOMERASE INHIBITION BY THE HIGHLY      
JRNL        TITL 2 SPECIFIC BIBR1532.                                           
JRNL        REF    STRUCTURE                     V.  23  1934 2015              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   26365799                                                     
JRNL        DOI    10.1016/J.STR.2015.08.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 91683                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4857                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6464                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 333                          
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9964                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 409                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : 2.70000                                              
REMARK   3    B33 (A**2) : -2.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.01000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.252         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.216         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.859        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10282 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13860 ; 1.043 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1190 ; 6.511 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   470 ;34.082 ;22.979       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1922 ;18.885 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;15.695 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1494 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7650 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   596                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3100   5.6380 -50.5170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0957 T22:   0.2240                                     
REMARK   3      T33:   0.0165 T12:   0.0153                                     
REMARK   3      T13:   0.0044 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7366 L22:   0.2405                                     
REMARK   3      L33:   1.0439 L12:   0.0701                                     
REMARK   3      L13:  -0.6466 L23:   0.1246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:   0.2986 S13:  -0.0057                       
REMARK   3      S21:  -0.0183 S22:  -0.0141 S23:  -0.0267                       
REMARK   3      S31:  -0.0191 S32:  -0.3968 S33:  -0.0583                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   596                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7610  34.8410 -21.8880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1009 T22:   0.2408                                     
REMARK   3      T33:   0.0320 T12:  -0.0289                                     
REMARK   3      T13:   0.0170 T23:  -0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3753 L22:   0.1821                                     
REMARK   3      L33:   1.6145 L12:  -0.0942                                     
REMARK   3      L13:  -0.4253 L23:  -0.0243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0508 S12:   0.1994 S13:   0.0559                       
REMARK   3      S21:   0.0600 S22:  -0.0015 S23:   0.0022                       
REMARK   3      S31:   0.1212 S32:  -0.5267 S33:   0.0523                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5CQG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212034.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-11                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: 3DU6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M NANO3 100MM TRIS 8.5, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       42.45100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  45      148.26    -38.96                                   
REMARK 500    PHE A  83       -5.95     80.31                                   
REMARK 500    TRP A 102        0.84    -67.63                                   
REMARK 500    ILE A 126      -50.45   -127.46                                   
REMARK 500    LEU A 141       -9.30     78.46                                   
REMARK 500    LYS A 167       25.30    -78.07                                   
REMARK 500    MET A 168     -160.32   -127.14                                   
REMARK 500    ASP A 176      -12.67     77.11                                   
REMARK 500    GLU A 177       49.36    -93.35                                   
REMARK 500    VAL A 178      -36.38   -135.48                                   
REMARK 500    LYS A 179      105.04     71.39                                   
REMARK 500    GLN A 190      -84.43     53.49                                   
REMARK 500    ASN A 192     -134.74   -112.03                                   
REMARK 500    PRO A 201      -79.78    -93.68                                   
REMARK 500    ASP A 202      -93.04     56.23                                   
REMARK 500    SER A 203       92.20     46.21                                   
REMARK 500    ALA A 204      -89.10     56.58                                   
REMARK 500    GLU A 222      -71.53   -108.23                                   
REMARK 500    LYS A 225       24.89    -71.38                                   
REMARK 500    SER A 227      -83.53   -115.03                                   
REMARK 500    ASP A 254       74.56     25.35                                   
REMARK 500    PRO A 272       78.60   -117.63                                   
REMARK 500    LEU A 276      -53.31   -125.26                                   
REMARK 500    ASP A 277     -139.02     65.04                                   
REMARK 500    PHE A 295     -135.61   -141.60                                   
REMARK 500    ARG A 297      -18.09     66.11                                   
REMARK 500    ASN A 303       60.37   -116.82                                   
REMARK 500    PHE A 329       65.80   -116.89                                   
REMARK 500    ASP A 333      133.84    143.86                                   
REMARK 500    ARG A 399       -3.49     73.25                                   
REMARK 500    LYS A 406       10.43    119.32                                   
REMARK 500    LYS A 526      118.48   -178.36                                   
REMARK 500    SER B  25        0.39    -69.44                                   
REMARK 500    PHE B  83      -13.44     78.71                                   
REMARK 500    HIS B  92      -20.23   -143.71                                   
REMARK 500    LEU B 141       -3.98     73.87                                   
REMARK 500    LYS B 166      -74.55    -68.34                                   
REMARK 500    LYS B 167       31.55    -79.54                                   
REMARK 500    VAL B 174       81.73   -150.31                                   
REMARK 500    GLN B 175     -174.69     56.07                                   
REMARK 500    GLU B 177       18.23   -159.21                                   
REMARK 500    LYS B 179       81.17   -158.23                                   
REMARK 500    ARG B 181      -53.68     96.57                                   
REMARK 500    GLN B 190       94.03    -56.39                                   
REMARK 500    ASP B 191       -0.41     70.75                                   
REMARK 500    ASN B 192     -159.00   -138.82                                   
REMARK 500    ASP B 202       59.04     74.24                                   
REMARK 500    ARG B 205      141.82     74.62                                   
REMARK 500    ASP B 254       70.67     42.19                                   
REMARK 500    ILE B 271      116.66    -39.42                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  406     LEU B  407                  -41.10                    
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 55C A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 55C B 601                 
DBREF  5CQG A    1   596  UNP    Q0QHL8   Q0QHL8_TRICA     1    596             
DBREF  5CQG B    1   596  UNP    Q0QHL8   Q0QHL8_TRICA     1    596             
SEQRES   1 A  596  MET VAL HIS TYR TYR ARG LEU SER LEU LYS SER ARG GLN          
SEQRES   2 A  596  LYS ALA PRO LYS ILE VAL ASN SER LYS TYR ASN SER ILE          
SEQRES   3 A  596  LEU ASN ILE ALA LEU LYS ASN PHE ARG LEU CYS LYS LYS          
SEQRES   4 A  596  HIS LYS THR LYS LYS PRO VAL GLN ILE LEU ALA LEU LEU          
SEQRES   5 A  596  GLN GLU ILE ILE PRO LYS SER TYR PHE GLY THR THR THR          
SEQRES   6 A  596  ASN LEU LYS ARG PHE TYR LYS VAL VAL GLU LYS ILE LEU          
SEQRES   7 A  596  THR GLN SER SER PHE GLU CYS ILE HIS LEU SER VAL LEU          
SEQRES   8 A  596  HIS LYS CYS TYR ASP TYR ASP ALA ILE PRO TRP LEU GLN          
SEQRES   9 A  596  ASN VAL GLU PRO ASN LEU ARG PRO LYS LEU LEU LEU LYS          
SEQRES  10 A  596  HIS ASN LEU PHE LEU LEU ASP ASN ILE VAL LYS PRO ILE          
SEQRES  11 A  596  ILE ALA PHE TYR TYR LYS PRO ILE LYS THR LEU ASN GLY          
SEQRES  12 A  596  HIS GLU ILE LYS PHE ILE ARG LYS GLU GLU TYR ILE SER          
SEQRES  13 A  596  PHE GLU SER LYS VAL PHE HIS LYS LEU LYS LYS MET LYS          
SEQRES  14 A  596  TYR LEU VAL GLU VAL GLN ASP GLU VAL LYS PRO ARG GLY          
SEQRES  15 A  596  VAL LEU ASN ILE ILE PRO LYS GLN ASP ASN PHE ARG ALA          
SEQRES  16 A  596  ILE VAL SER ILE PHE PRO ASP SER ALA ARG LYS PRO PHE          
SEQRES  17 A  596  PHE LYS LEU LEU THR SER LYS ILE TYR LYS VAL LEU GLU          
SEQRES  18 A  596  GLU LYS TYR LYS THR SER GLY SER LEU TYR THR CYS TRP          
SEQRES  19 A  596  SER GLU PHE THR GLN LYS THR GLN GLY GLN ILE TYR GLY          
SEQRES  20 A  596  ILE LYS VAL ASP ILE ARG ASP ALA TYR GLY ASN VAL LYS          
SEQRES  21 A  596  ILE PRO VAL LEU CYS LYS LEU ILE GLN SER ILE PRO THR          
SEQRES  22 A  596  HIS LEU LEU ASP SER GLU LYS LYS ASN PHE ILE VAL ASP          
SEQRES  23 A  596  HIS ILE SER ASN GLN PHE VAL ALA PHE ARG ARG LYS ILE          
SEQRES  24 A  596  TYR LYS TRP ASN HIS GLY LEU LEU GLN GLY ASP PRO LEU          
SEQRES  25 A  596  SER GLY CYS LEU CYS GLU LEU TYR MET ALA PHE MET ASP          
SEQRES  26 A  596  ARG LEU TYR PHE SER ASN LEU ASP LYS ASP ALA PHE ILE          
SEQRES  27 A  596  HIS ARG THR VAL ASP ASP TYR PHE PHE CYS SER PRO HIS          
SEQRES  28 A  596  PRO HIS LYS VAL TYR ASP PHE GLU LEU LEU ILE LYS GLY          
SEQRES  29 A  596  VAL TYR GLN VAL ASN PRO THR LYS THR ARG THR ASN LEU          
SEQRES  30 A  596  PRO THR HIS ARG HIS PRO GLN ASP GLU ILE PRO TYR CYS          
SEQRES  31 A  596  GLY LYS ILE PHE ASN LEU THR THR ARG GLN VAL ARG THR          
SEQRES  32 A  596  LEU TYR LYS LEU PRO PRO ASN TYR GLU ILE ARG HIS LYS          
SEQRES  33 A  596  PHE LYS LEU TRP ASN PHE ASN ASN GLN ILE SER ASP ASP          
SEQRES  34 A  596  ASN PRO ALA ARG PHE LEU GLN LYS ALA MET ASP PHE PRO          
SEQRES  35 A  596  PHE ILE CYS ASN SER PHE THR LYS PHE GLU PHE ASN THR          
SEQRES  36 A  596  VAL PHE ASN ASP GLN ARG THR VAL PHE ALA ASN PHE TYR          
SEQRES  37 A  596  ASP ALA MET ILE CYS VAL ALA TYR LYS PHE ASP ALA ALA          
SEQRES  38 A  596  MET MET ALA LEU ARG THR SER PHE LEU VAL ASN ASP PHE          
SEQRES  39 A  596  GLY PHE ILE TRP LEU VAL LEU SER SER THR VAL ARG ALA          
SEQRES  40 A  596  TYR ALA SER ARG ALA PHE LYS LYS ILE VAL THR TYR LYS          
SEQRES  41 A  596  GLY GLY LYS TYR ARG LYS VAL THR PHE GLN CYS LEU LYS          
SEQRES  42 A  596  SER ILE ALA TRP ARG ALA PHE LEU ALA VAL LEU LYS ARG          
SEQRES  43 A  596  ARG THR GLU ILE TYR LYS GLY LEU ILE ASP ARG ILE LYS          
SEQRES  44 A  596  SER ARG GLU LYS LEU THR MET LYS PHE HIS ASP GLY GLU          
SEQRES  45 A  596  VAL ASP ALA SER TYR PHE CYS LYS LEU PRO GLU LYS PHE          
SEQRES  46 A  596  ARG PHE VAL LYS ILE ASN ARG LYS ALA SER ILE                  
SEQRES   1 B  596  MET VAL HIS TYR TYR ARG LEU SER LEU LYS SER ARG GLN          
SEQRES   2 B  596  LYS ALA PRO LYS ILE VAL ASN SER LYS TYR ASN SER ILE          
SEQRES   3 B  596  LEU ASN ILE ALA LEU LYS ASN PHE ARG LEU CYS LYS LYS          
SEQRES   4 B  596  HIS LYS THR LYS LYS PRO VAL GLN ILE LEU ALA LEU LEU          
SEQRES   5 B  596  GLN GLU ILE ILE PRO LYS SER TYR PHE GLY THR THR THR          
SEQRES   6 B  596  ASN LEU LYS ARG PHE TYR LYS VAL VAL GLU LYS ILE LEU          
SEQRES   7 B  596  THR GLN SER SER PHE GLU CYS ILE HIS LEU SER VAL LEU          
SEQRES   8 B  596  HIS LYS CYS TYR ASP TYR ASP ALA ILE PRO TRP LEU GLN          
SEQRES   9 B  596  ASN VAL GLU PRO ASN LEU ARG PRO LYS LEU LEU LEU LYS          
SEQRES  10 B  596  HIS ASN LEU PHE LEU LEU ASP ASN ILE VAL LYS PRO ILE          
SEQRES  11 B  596  ILE ALA PHE TYR TYR LYS PRO ILE LYS THR LEU ASN GLY          
SEQRES  12 B  596  HIS GLU ILE LYS PHE ILE ARG LYS GLU GLU TYR ILE SER          
SEQRES  13 B  596  PHE GLU SER LYS VAL PHE HIS LYS LEU LYS LYS MET LYS          
SEQRES  14 B  596  TYR LEU VAL GLU VAL GLN ASP GLU VAL LYS PRO ARG GLY          
SEQRES  15 B  596  VAL LEU ASN ILE ILE PRO LYS GLN ASP ASN PHE ARG ALA          
SEQRES  16 B  596  ILE VAL SER ILE PHE PRO ASP SER ALA ARG LYS PRO PHE          
SEQRES  17 B  596  PHE LYS LEU LEU THR SER LYS ILE TYR LYS VAL LEU GLU          
SEQRES  18 B  596  GLU LYS TYR LYS THR SER GLY SER LEU TYR THR CYS TRP          
SEQRES  19 B  596  SER GLU PHE THR GLN LYS THR GLN GLY GLN ILE TYR GLY          
SEQRES  20 B  596  ILE LYS VAL ASP ILE ARG ASP ALA TYR GLY ASN VAL LYS          
SEQRES  21 B  596  ILE PRO VAL LEU CYS LYS LEU ILE GLN SER ILE PRO THR          
SEQRES  22 B  596  HIS LEU LEU ASP SER GLU LYS LYS ASN PHE ILE VAL ASP          
SEQRES  23 B  596  HIS ILE SER ASN GLN PHE VAL ALA PHE ARG ARG LYS ILE          
SEQRES  24 B  596  TYR LYS TRP ASN HIS GLY LEU LEU GLN GLY ASP PRO LEU          
SEQRES  25 B  596  SER GLY CYS LEU CYS GLU LEU TYR MET ALA PHE MET ASP          
SEQRES  26 B  596  ARG LEU TYR PHE SER ASN LEU ASP LYS ASP ALA PHE ILE          
SEQRES  27 B  596  HIS ARG THR VAL ASP ASP TYR PHE PHE CYS SER PRO HIS          
SEQRES  28 B  596  PRO HIS LYS VAL TYR ASP PHE GLU LEU LEU ILE LYS GLY          
SEQRES  29 B  596  VAL TYR GLN VAL ASN PRO THR LYS THR ARG THR ASN LEU          
SEQRES  30 B  596  PRO THR HIS ARG HIS PRO GLN ASP GLU ILE PRO TYR CYS          
SEQRES  31 B  596  GLY LYS ILE PHE ASN LEU THR THR ARG GLN VAL ARG THR          
SEQRES  32 B  596  LEU TYR LYS LEU PRO PRO ASN TYR GLU ILE ARG HIS LYS          
SEQRES  33 B  596  PHE LYS LEU TRP ASN PHE ASN ASN GLN ILE SER ASP ASP          
SEQRES  34 B  596  ASN PRO ALA ARG PHE LEU GLN LYS ALA MET ASP PHE PRO          
SEQRES  35 B  596  PHE ILE CYS ASN SER PHE THR LYS PHE GLU PHE ASN THR          
SEQRES  36 B  596  VAL PHE ASN ASP GLN ARG THR VAL PHE ALA ASN PHE TYR          
SEQRES  37 B  596  ASP ALA MET ILE CYS VAL ALA TYR LYS PHE ASP ALA ALA          
SEQRES  38 B  596  MET MET ALA LEU ARG THR SER PHE LEU VAL ASN ASP PHE          
SEQRES  39 B  596  GLY PHE ILE TRP LEU VAL LEU SER SER THR VAL ARG ALA          
SEQRES  40 B  596  TYR ALA SER ARG ALA PHE LYS LYS ILE VAL THR TYR LYS          
SEQRES  41 B  596  GLY GLY LYS TYR ARG LYS VAL THR PHE GLN CYS LEU LYS          
SEQRES  42 B  596  SER ILE ALA TRP ARG ALA PHE LEU ALA VAL LEU LYS ARG          
SEQRES  43 B  596  ARG THR GLU ILE TYR LYS GLY LEU ILE ASP ARG ILE LYS          
SEQRES  44 B  596  SER ARG GLU LYS LEU THR MET LYS PHE HIS ASP GLY GLU          
SEQRES  45 B  596  VAL ASP ALA SER TYR PHE CYS LYS LEU PRO GLU LYS PHE          
SEQRES  46 B  596  ARG PHE VAL LYS ILE ASN ARG LYS ALA SER ILE                  
HET    55C  A 601      25                                                       
HET    55C  B 601      25                                                       
HETNAM     55C 2-{[(2E)-3-(NAPHTHALEN-2-YL)BUT-2-ENOYL]AMINO}BENZOIC            
HETNAM   2 55C  ACID                                                            
HETSYN     55C BIBR 1532                                                        
FORMUL   3  55C    2(C21 H17 N O3)                                              
FORMUL   5  HOH   *409(H2 O)                                                    
HELIX    1 AA1 SER A    8  ARG A   12  5                                   5    
HELIX    2 AA2 SER A   25  HIS A   40  1                                  16    
HELIX    3 AA3 GLN A   47  ILE A   56  1                                  10    
HELIX    4 AA4 PRO A   57  PHE A   61  5                                   5    
HELIX    5 AA5 THR A   63  LEU A   78  1                                  16    
HELIX    6 AA6 SER A   89  HIS A   92  5                                   4    
HELIX    7 AA7 ASP A   96  GLN A  104  5                                   9    
HELIX    8 AA8 GLU A  107  ASN A  109  5                                   3    
HELIX    9 AA9 LEU A  110  ILE A  126  1                                  17    
HELIX   10 AB1 ILE A  126  TYR A  134  1                                   9    
HELIX   11 AB2 LYS A  151  LYS A  167  1                                  17    
HELIX   12 AB3 ARG A  205  GLU A  221  1                                  17    
HELIX   13 AB4 SER A  229  THR A  241  1                                  13    
HELIX   14 AB5 LYS A  260  SER A  270  1                                  11    
HELIX   15 AB6 ASP A  277  SER A  289  1                                  13    
HELIX   16 AB7 LEU A  312  PHE A  329  1                                  18    
HELIX   17 AB8 HIS A  351  TYR A  366  1                                  16    
HELIX   18 AB9 GLU A  412  PHE A  417  5                                   6    
HELIX   19 AC1 ASN A  430  ASP A  440  1                                  11    
HELIX   20 AC2 PHE A  441  PHE A  448  5                                   8    
HELIX   21 AC3 THR A  449  ASN A  454  1                                   6    
HELIX   22 AC4 ASP A  459  SER A  488  1                                  30    
HELIX   23 AC5 PHE A  496  TYR A  519  1                                  24    
HELIX   24 AC6 THR A  528  LYS A  545  1                                  18    
HELIX   25 AC7 ARG A  547  GLU A  562  1                                  16    
HELIX   26 AC8 ASP A  574  LYS A  580  5                                   7    
HELIX   27 AC9 PRO A  582  PHE A  587  1                                   6    
HELIX   28 AD1 SER B    8  ARG B   12  5                                   5    
HELIX   29 AD2 SER B   25  HIS B   40  1                                  16    
HELIX   30 AD3 GLN B   47  ILE B   56  1                                  10    
HELIX   31 AD4 PRO B   57  PHE B   61  5                                   5    
HELIX   32 AD5 THR B   63  THR B   79  1                                  17    
HELIX   33 AD6 SER B   89  HIS B   92  5                                   4    
HELIX   34 AD7 ILE B  100  GLN B  104  5                                   5    
HELIX   35 AD8 GLU B  107  ASN B  109  5                                   3    
HELIX   36 AD9 LEU B  110  ILE B  126  1                                  17    
HELIX   37 AE1 ILE B  126  TYR B  134  1                                   9    
HELIX   38 AE2 LYS B  151  LYS B  167  1                                  17    
HELIX   39 AE3 LYS B  206  LEU B  220  1                                  15    
HELIX   40 AE4 SER B  229  THR B  241  1                                  13    
HELIX   41 AE5 LYS B  260  GLN B  269  1                                  10    
HELIX   42 AE6 GLU B  279  ASN B  290  1                                  12    
HELIX   43 AE7 LEU B  312  PHE B  329  1                                  18    
HELIX   44 AE8 HIS B  351  TYR B  366  1                                  16    
HELIX   45 AE9 ASN B  369  THR B  373  5                                   5    
HELIX   46 AF1 GLU B  412  PHE B  417  5                                   6    
HELIX   47 AF2 ASN B  430  ASP B  440  1                                  11    
HELIX   48 AF3 PHE B  441  PHE B  448  5                                   8    
HELIX   49 AF4 THR B  449  ASN B  454  1                                   6    
HELIX   50 AF5 ASP B  459  SER B  488  1                                  30    
HELIX   51 AF6 PHE B  496  TYR B  519  1                                  24    
HELIX   52 AF7 THR B  528  LYS B  545  1                                  18    
HELIX   53 AF8 ARG B  547  GLU B  562  1                                  16    
HELIX   54 AF9 ASP B  574  CYS B  579  5                                   6    
HELIX   55 AG1 PRO B  582  PHE B  587  1                                   6    
SHEET    1 AA1 2 TYR A   4  ARG A   6  0                                        
SHEET    2 AA1 2 CYS A  85  HIS A  87 -1  O  ILE A  86   N  TYR A   5           
SHEET    1 AA2 2 TYR A 135  LYS A 139  0                                        
SHEET    2 AA2 2 ILE A 146  ARG A 150 -1  O  LYS A 147   N  ILE A 138           
SHEET    1 AA3 3 LEU A 171  GLU A 173  0                                        
SHEET    2 AA3 3 ILE A 299  TRP A 302 -1  O  LYS A 301   N  VAL A 172           
SHEET    3 AA3 3 GLN A 291  ALA A 294 -1  N  GLN A 291   O  TRP A 302           
SHEET    1 AA4 2 VAL A 183  LYS A 189  0                                        
SHEET    2 AA4 2 ASN A 192  SER A 198 -1  O  ILE A 196   N  ASN A 185           
SHEET    1 AA5 4 PHE A 337  ARG A 340  0                                        
SHEET    2 AA5 4 ASP A 344  SER A 349 -1  O  CYS A 348   N  PHE A 337           
SHEET    3 AA5 4 TYR A 246  ASP A 251 -1  N  TYR A 246   O  SER A 349           
SHEET    4 AA5 4 ARG A 374  THR A 375 -1  O  ARG A 374   N  LYS A 249           
SHEET    1 AA6 3 GLU A 386  TYR A 389  0                                        
SHEET    2 AA6 3 LYS A 392  ASN A 395 -1  O  PHE A 394   N  ILE A 387           
SHEET    3 AA6 3 VAL A 401  THR A 403 -1  O  ARG A 402   N  ILE A 393           
SHEET    1 AA7 2 TYR B   4  ARG B   6  0                                        
SHEET    2 AA7 2 CYS B  85  HIS B  87 -1  O  ILE B  86   N  TYR B   5           
SHEET    1 AA8 2 TYR B 135  LYS B 139  0                                        
SHEET    2 AA8 2 ILE B 146  ARG B 150 -1  O  ILE B 149   N  LYS B 136           
SHEET    1 AA9 3 LEU B 171  GLU B 173  0                                        
SHEET    2 AA9 3 ILE B 299  TRP B 302 -1  O  LYS B 301   N  VAL B 172           
SHEET    3 AA9 3 GLN B 291  ALA B 294 -1  N  GLN B 291   O  TRP B 302           
SHEET    1 AB1 2 VAL B 183  PRO B 188  0                                        
SHEET    2 AB1 2 PHE B 193  SER B 198 -1  O  ILE B 196   N  ASN B 185           
SHEET    1 AB2 4 PHE B 337  ARG B 340  0                                        
SHEET    2 AB2 4 ASP B 344  SER B 349 -1  O  CYS B 348   N  PHE B 337           
SHEET    3 AB2 4 TYR B 246  ASP B 251 -1  N  VAL B 250   O  TYR B 345           
SHEET    4 AB2 4 ARG B 374  THR B 375 -1  O  ARG B 374   N  LYS B 249           
SHEET    1 AB3 3 GLU B 386  TYR B 389  0                                        
SHEET    2 AB3 3 LYS B 392  ASN B 395 -1  O  LYS B 392   N  TYR B 389           
SHEET    3 AB3 3 VAL B 401  THR B 403 -1  O  ARG B 402   N  ILE B 393           
CISPEP   1 PHE A  200    PRO A  201          0        -3.36                     
CISPEP   2 SER A  270    ILE A  271          0       -10.53                     
CISPEP   3 SER A  289    ASN A  290          0        20.56                     
CISPEP   4 TYR A  405    LYS A  406          0        11.85                     
CISPEP   5 ASP B  176    GLU B  177          0        -9.59                     
CISPEP   6 PHE B  200    PRO B  201          0        -0.23                     
SITE     1 AC1  8 MET A 483  ARG A 486  PHE A 494  ILE A 550                    
SITE     2 AC1  8 TYR A 551  LEU A 554  ARG A 557  HOH A 784                    
SITE     1 AC2 10 MET B 483  ARG B 486  PHE B 494  ILE B 550                    
SITE     2 AC2 10 TYR B 551  GLY B 553  LEU B 554  ARG B 557                    
SITE     3 AC2 10 HOH B 735  HOH B 841                                          
CRYST1  117.719   84.902  123.333  90.00 116.20  90.00 P 1 21 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      0.008495  0.000000  0.004180        0.00000                         
SCALE2      0.000000  0.011778  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009036        0.00000                         
ATOM      1  N   MET A   1      21.546  28.956 -51.201  1.00 70.61           N  
ANISOU    1  N   MET A   1    10060   7996   8772    392   1875     90       N  
ATOM      2  CA  MET A   1      20.194  28.325 -51.232  1.00 67.59           C  
ANISOU    2  CA  MET A   1     9630   7704   8345    488   1783    169       C  
ATOM      3  C   MET A   1      20.265  26.786 -51.302  1.00 61.73           C  
ANISOU    3  C   MET A   1     8784   7083   7588    460   1607    137       C  
ATOM      4  O   MET A   1      19.755  26.102 -50.407  1.00 62.98           O  
ANISOU    4  O   MET A   1     8894   7290   7743    440   1514    117       O  
ATOM      5  CB  MET A   1      19.352  28.895 -52.394  1.00 71.70           C  
ANISOU    5  CB  MET A   1    10190   8232   8821    626   1854    292       C  
ATOM      6  CG  MET A   1      17.917  28.361 -52.458  1.00 76.51           C  
ANISOU    6  CG  MET A   1    10748   8943   9378    727   1772    375       C  
ATOM      7  SD  MET A   1      16.845  29.111 -53.717  1.00 81.54           S  
ANISOU    7  SD  MET A   1    11422   9606   9951    901   1859    527       S  
ATOM      8  CE  MET A   1      17.455  28.369 -55.232  1.00 72.65           C  
ANISOU    8  CE  MET A   1    10249   8565   8789    910   1795    535       C  
ATOM      9  N   VAL A   2      20.912  26.250 -52.342  1.00 56.42           N  
ANISOU    9  N   VAL A   2     8080   6451   6905    457   1568    129       N  
ATOM     10  CA  VAL A   2      20.817  24.800 -52.661  1.00 50.54           C  
ANISOU   10  CA  VAL A   2     7243   5819   6138    453   1416    115       C  
ATOM     11  C   VAL A   2      21.791  23.909 -51.897  1.00 45.98           C  
ANISOU   11  C   VAL A   2     6613   5257   5598    343   1325     12       C  
ATOM     12  O   VAL A   2      23.007  24.066 -52.020  1.00 48.84           O  
ANISOU   12  O   VAL A   2     6982   5581   5993    275   1356    -51       O  
ATOM     13  CB  VAL A   2      20.948  24.530 -54.172  1.00 49.90           C  
ANISOU   13  CB  VAL A   2     7147   5787   6022    507   1410    159       C  
ATOM     14  CG1 VAL A   2      20.835  23.038 -54.459  1.00 48.57           C  
ANISOU   14  CG1 VAL A   2     6890   5729   5834    495   1263    137       C  
ATOM     15  CG2 VAL A   2      19.871  25.295 -54.935  1.00 52.76           C  
ANISOU   15  CG2 VAL A   2     7550   6160   6334    630   1485    273       C  
ATOM     16  N   HIS A   3      21.245  22.947 -51.145  1.00 41.25           N  
ANISOU   16  N   HIS A   3     5958   4721   4993    331   1212     -1       N  
ATOM     17  CA  HIS A   3      22.043  22.044 -50.310  1.00 37.63           C  
ANISOU   17  CA  HIS A   3     5448   4284   4566    241   1121    -87       C  
ATOM     18  C   HIS A   3      21.996  20.608 -50.768  1.00 34.11           C  
ANISOU   18  C   HIS A   3     4930   3926   4104    247    996    -92       C  
ATOM     19  O   HIS A   3      22.870  19.823 -50.420  1.00 30.51           O  
ANISOU   19  O   HIS A   3     4432   3487   3674    184    930   -158       O  
ATOM     20  CB  HIS A   3      21.581  22.108 -48.854  1.00 39.77           C  
ANISOU   20  CB  HIS A   3     5719   4543   4846    208   1102   -107       C  
ATOM     21  CG  HIS A   3      21.731  23.472 -48.223  1.00 42.36           C  
ANISOU   21  CG  HIS A   3     6118   4779   5195    182   1227   -121       C  
ATOM     22  ND1 HIS A   3      20.670  24.242 -47.900  1.00 43.03           N  
ANISOU   22  ND1 HIS A   3     6250   4832   5266    237   1292    -64       N  
ATOM     23  CD2 HIS A   3      22.864  24.200 -47.874  1.00 42.08           C  
ANISOU   23  CD2 HIS A   3     6115   4678   5195    101   1306   -192       C  
ATOM     24  CE1 HIS A   3      21.101  25.397 -47.367  1.00 43.39           C  
ANISOU   24  CE1 HIS A   3     6359   4786   5338    193   1411    -97       C  
ATOM     25  NE2 HIS A   3      22.444  25.373 -47.354  1.00 43.55           N  
ANISOU   25  NE2 HIS A   3     6370   4789   5388    105   1419   -178       N  
ATOM     26  N   TYR A   4      20.979  20.270 -51.560  1.00 32.27           N  
ANISOU   26  N   TYR A   4     4682   3751   3826    324    969    -24       N  
ATOM     27  CA  TYR A   4      20.626  18.887 -51.867  1.00 31.67           C  
ANISOU   27  CA  TYR A   4     4541   3762   3729    330    853    -27       C  
ATOM     28  C   TYR A   4      20.924  18.490 -53.320  1.00 33.12           C  
ANISOU   28  C   TYR A   4     4705   3988   3891    357    846    -14       C  
ATOM     29  O   TYR A   4      20.712  19.265 -54.254  1.00 32.78           O  
ANISOU   29  O   TYR A   4     4694   3940   3820    414    920     37       O  
ATOM     30  CB  TYR A   4      19.117  18.658 -51.653  1.00 30.41           C  
ANISOU   30  CB  TYR A   4     4367   3660   3526    387    818     32       C  
ATOM     31  CG  TYR A   4      18.585  18.713 -50.242  1.00 28.58           C  
ANISOU   31  CG  TYR A   4     4140   3411   3306    363    799     22       C  
ATOM     32  CD1 TYR A   4      19.439  18.799 -49.129  1.00 29.02           C  
ANISOU   32  CD1 TYR A   4     4205   3412   3408    287    798    -42       C  
ATOM     33  CD2 TYR A   4      17.218  18.611 -50.015  1.00 27.90           C  
ANISOU   33  CD2 TYR A   4     4042   3376   3182    413    778     74       C  
ATOM     34  CE1 TYR A   4      18.928  18.833 -47.831  1.00 28.23           C  
ANISOU   34  CE1 TYR A   4     4109   3303   3314    263    780    -51       C  
ATOM     35  CE2 TYR A   4      16.698  18.648 -48.734  1.00 28.18           C  
ANISOU   35  CE2 TYR A   4     4082   3397   3227    391    762     65       C  
ATOM     36  CZ  TYR A   4      17.553  18.761 -47.643  1.00 28.67           C  
ANISOU   36  CZ  TYR A   4     4158   3399   3333    316    763      3       C  
ATOM     37  OH  TYR A   4      17.021  18.798 -46.378  1.00 27.77           O  
ANISOU   37  OH  TYR A   4     4048   3277   3223    293    748     -5       O  
ATOM     38  N   TYR A   5      21.354  17.252 -53.497  1.00 33.53           N  
ANISOU   38  N   TYR A   5     4704   4084   3951    322    757    -59       N  
ATOM     39  CA  TYR A   5      21.326  16.601 -54.799  1.00 33.44           C  
ANISOU   39  CA  TYR A   5     4662   4134   3907    348    729    -47       C  
ATOM     40  C   TYR A   5      20.202  15.560 -54.760  1.00 33.09           C  
ANISOU   40  C   TYR A   5     4574   4173   3826    367    644    -29       C  
ATOM     41  O   TYR A   5      20.089  14.792 -53.812  1.00 34.18           O  
ANISOU   41  O   TYR A   5     4688   4313   3983    328    579    -61       O  
ATOM     42  CB  TYR A   5      22.683  15.945 -55.080  1.00 34.15           C  
ANISOU   42  CB  TYR A   5     4728   4208   4037    291    701   -118       C  
ATOM     43  CG  TYR A   5      22.758  15.140 -56.366  1.00 35.03           C  
ANISOU   43  CG  TYR A   5     4806   4381   4122    306    669   -120       C  
ATOM     44  CD1 TYR A   5      22.721  15.769 -57.624  1.00 34.73           C  
ANISOU   44  CD1 TYR A   5     4788   4360   4048    351    732    -79       C  
ATOM     45  CD2 TYR A   5      22.883  13.744 -56.329  1.00 34.81           C  
ANISOU   45  CD2 TYR A   5     4729   4392   4103    275    581   -163       C  
ATOM     46  CE1 TYR A   5      22.794  15.032 -58.799  1.00 34.05           C  
ANISOU   46  CE1 TYR A   5     4668   4335   3931    359    703    -86       C  
ATOM     47  CE2 TYR A   5      22.969  12.994 -57.505  1.00 35.44           C  
ANISOU   47  CE2 TYR A   5     4780   4525   4159    281    558   -173       C  
ATOM     48  CZ  TYR A   5      22.919  13.636 -58.730  1.00 36.19           C  
ANISOU   48  CZ  TYR A   5     4890   4644   4214    321    616   -137       C  
ATOM     49  OH  TYR A   5      22.993  12.880 -59.883  1.00 39.11           O  
ANISOU   49  OH  TYR A   5     5229   5074   4555    322    593   -151       O  
ATOM     50  N   ARG A   6      19.327  15.592 -55.735  1.00 31.39           N  
ANISOU   50  N   ARG A   6     4346   4028   3552    426    652     24       N  
ATOM     51  CA  ARG A   6      18.213  14.692 -55.737  1.00 32.27           C  
ANISOU   51  CA  ARG A   6     4413   4227   3621    438    581     38       C  
ATOM     52  C   ARG A   6      18.669  13.364 -56.285  1.00 32.65           C  
ANISOU   52  C   ARG A   6     4418   4314   3673    394    514    -16       C  
ATOM     53  O   ARG A   6      19.452  13.337 -57.236  1.00 32.92           O  
ANISOU   53  O   ARG A   6     4451   4346   3709    390    534    -33       O  
ATOM     54  CB  ARG A   6      17.111  15.249 -56.626  1.00 34.90           C  
ANISOU   54  CB  ARG A   6     4741   4638   3880    519    617    115       C  
ATOM     55  CG  ARG A   6      16.294  16.329 -55.974  1.00 35.77           C  
ANISOU   55  CG  ARG A   6     4886   4727   3978    573    672    177       C  
ATOM     56  CD  ARG A   6      15.366  16.976 -56.974  1.00 39.65           C  
ANISOU   56  CD  ARG A   6     5372   5296   4395    667    717    262       C  
ATOM     57  NE  ARG A   6      16.091  17.470 -58.140  1.00 45.49           N  
ANISOU   57  NE  ARG A   6     6135   6025   5124    692    775    279       N  
ATOM     58  CZ  ARG A   6      15.604  18.353 -59.008  1.00 46.67           C  
ANISOU   58  CZ  ARG A   6     6302   6210   5217    781    843    361       C  
ATOM     59  NH1 ARG A   6      14.382  18.850 -58.838  1.00 49.35           N  
ANISOU   59  NH1 ARG A   6     6636   6604   5509    858    862    434       N  
ATOM     60  NH2 ARG A   6      16.337  18.733 -60.045  1.00 45.56           N  
ANISOU   60  NH2 ARG A   6     6184   6056   5069    797    895    372       N  
ATOM     61  N   LEU A   7      18.202  12.264 -55.691  1.00 31.10           N  
ANISOU   61  N   LEU A   7     4189   4148   3478    359    439    -45       N  
ATOM     62  CA  LEU A   7      18.614  10.908 -56.148  1.00 30.92           C  
ANISOU   62  CA  LEU A   7     4130   4151   3464    314    381   -101       C  
ATOM     63  C   LEU A   7      17.840  10.391 -57.376  1.00 32.22           C  
ANISOU   63  C   LEU A   7     4259   4422   3562    334    367    -88       C  
ATOM     64  O   LEU A   7      18.259   9.411 -58.026  1.00 32.82           O  
ANISOU   64  O   LEU A   7     4310   4518   3640    300    338   -135       O  
ATOM     65  CB  LEU A   7      18.532   9.884 -55.013  1.00 28.52           C  
ANISOU   65  CB  LEU A   7     3815   3827   3195    266    316   -140       C  
ATOM     66  CG  LEU A   7      19.307  10.112 -53.696  1.00 28.42           C  
ANISOU   66  CG  LEU A   7     3826   3728   3243    236    312   -163       C  
ATOM     67  CD1 LEU A   7      19.167   8.882 -52.801  1.00 27.72           C  
ANISOU   67  CD1 LEU A   7     3720   3634   3176    195    244   -196       C  
ATOM     68  CD2 LEU A   7      20.785  10.452 -53.904  1.00 27.51           C  
ANISOU   68  CD2 LEU A   7     3722   3553   3175    219    342   -197       C  
ATOM     69  N   SER A   8      16.734  11.054 -57.702  1.00 33.12           N  
ANISOU   69  N   SER A   8     4366   4604   3612    390    391    -25       N  
ATOM     70  CA  SER A   8      15.867  10.626 -58.804  1.00 35.35           C  
ANISOU   70  CA  SER A   8     4603   5010   3816    410    376    -10       C  
ATOM     71  C   SER A   8      16.582  10.555 -60.160  1.00 36.58           C  
ANISOU   71  C   SER A   8     4752   5191   3953    412    399    -24       C  
ATOM     72  O   SER A   8      17.354  11.445 -60.532  1.00 34.04           O  
ANISOU   72  O   SER A   8     4465   4818   3650    440    455     -3       O  
ATOM     73  CB  SER A   8      14.650  11.547 -58.925  1.00 37.75           C  
ANISOU   73  CB  SER A   8     4901   5388   4053    485    407     69       C  
ATOM     74  OG  SER A   8      13.783  11.111 -59.961  1.00 40.65           O  
ANISOU   74  OG  SER A   8     5214   5894   4335    503    388     82       O  
ATOM     75  N   LEU A   9      16.294   9.488 -60.890  1.00 37.96           N  
ANISOU   75  N   LEU A   9     4882   5447   4091    379    359    -64       N  
ATOM     76  CA  LEU A   9      16.810   9.285 -62.228  1.00 40.42           C  
ANISOU   76  CA  LEU A   9     5180   5804   4374    376    376    -82       C  
ATOM     77  C   LEU A   9      16.289  10.367 -63.180  1.00 44.40           C  
ANISOU   77  C   LEU A   9     5680   6387   4801    455    427     -4       C  
ATOM     78  O   LEU A   9      16.988  10.778 -64.104  1.00 46.13           O  
ANISOU   78  O   LEU A   9     5913   6601   5011    473    468      3       O  
ATOM     79  CB  LEU A   9      16.400   7.897 -62.720  1.00 37.86           C  
ANISOU   79  CB  LEU A   9     4807   5560   4017    318    326   -143       C  
ATOM     80  CG  LEU A   9      17.456   6.793 -62.688  1.00 36.95           C  
ANISOU   80  CG  LEU A   9     4697   5371   3968    248    304   -227       C  
ATOM     81  CD1 LEU A   9      18.282   6.802 -61.404  1.00 33.58           C  
ANISOU   81  CD1 LEU A   9     4309   4812   3636    230    294   -244       C  
ATOM     82  CD2 LEU A   9      16.812   5.428 -62.946  1.00 35.22           C  
ANISOU   82  CD2 LEU A   9     4439   5223   3718    188    262   -285       C  
ATOM     83  N   LYS A  10      15.076  10.851 -62.909  1.00 47.39           N  
ANISOU   83  N   LYS A  10     6043   6837   5125    506    427     56       N  
ATOM     84  CA  LYS A  10      14.403  11.863 -63.733  1.00 49.73           C  
ANISOU   84  CA  LYS A  10     6332   7222   5339    596    475    143       C  
ATOM     85  C   LYS A  10      15.274  13.056 -64.100  1.00 48.83           C  
ANISOU   85  C   LYS A  10     6277   7025   5249    647    554    190       C  
ATOM     86  O   LYS A  10      15.064  13.691 -65.136  1.00 51.11           O  
ANISOU   86  O   LYS A  10     6563   7385   5471    712    597    250       O  
ATOM     87  CB  LYS A  10      13.119  12.347 -63.045  1.00 53.98           C  
ANISOU   87  CB  LYS A  10     6855   7813   5838    650    472    205       C  
ATOM     88  CG  LYS A  10      11.986  11.331 -63.079  1.00 59.34           C  
ANISOU   88  CG  LYS A  10     7463   8627   6456    617    407    175       C  
ATOM     89  CD  LYS A  10      10.774  11.797 -62.286  1.00 61.89           C  
ANISOU   89  CD  LYS A  10     7770   8995   6749    666    404    231       C  
ATOM     90  CE  LYS A  10       9.747  10.676 -62.168  1.00 66.37           C  
ANISOU   90  CE  LYS A  10     8268   9682   7267    611    338    184       C  
ATOM     91  NZ  LYS A  10       8.424  11.158 -61.670  1.00 69.56           N  
ANISOU   91  NZ  LYS A  10     8639  10172   7617    670    337    244       N  
ATOM     92  N   SER A  11      16.253  13.360 -63.260  1.00 47.23           N  
ANISOU   92  N   SER A  11     6128   6678   5139    616    575    162       N  
ATOM     93  CA  SER A  11      17.115  14.516 -63.501  1.00 48.49           C  
ANISOU   93  CA  SER A  11     6348   6747   5327    651    659    197       C  
ATOM     94  C   SER A  11      18.412  14.188 -64.253  1.00 47.04           C  
ANISOU   94  C   SER A  11     6173   6523   5176    604    671    141       C  
ATOM     95  O   SER A  11      19.265  15.063 -64.413  1.00 46.31           O  
ANISOU   95  O   SER A  11     6131   6348   5116    617    741    155       O  
ATOM     96  CB  SER A  11      17.431  15.230 -62.192  1.00 45.58           C  
ANISOU   96  CB  SER A  11     6033   6252   5032    645    691    200       C  
ATOM     97  OG  SER A  11      17.692  14.285 -61.173  1.00 45.96           O  
ANISOU   97  OG  SER A  11     6065   6259   5139    568    623    127       O  
ATOM     98  N   ARG A  12      18.556  12.946 -64.721  1.00 45.57           N  
ANISOU   98  N   ARG A  12     5939   6393   4981    548    609     75       N  
ATOM     99  CA  ARG A  12      19.778  12.544 -65.453  1.00 46.49           C  
ANISOU   99  CA  ARG A  12     6058   6476   5128    502    618     17       C  
ATOM    100  C   ARG A  12      19.947  13.361 -66.716  1.00 49.14           C  
ANISOU  100  C   ARG A  12     6409   6852   5407    557    685     70       C  
ATOM    101  O   ARG A  12      18.968  13.877 -67.270  1.00 51.59           O  
ANISOU  101  O   ARG A  12     6709   7257   5635    627    705    145       O  
ATOM    102  CB  ARG A  12      19.769  11.047 -65.809  1.00 42.91           C  
ANISOU  102  CB  ARG A  12     5552   6083   4668    438    549    -59       C  
ATOM    103  CG  ARG A  12      18.732  10.633 -66.843  1.00 41.15           C  
ANISOU  103  CG  ARG A  12     5278   6015   4343    457    528    -40       C  
ATOM    104  CD  ARG A  12      18.392   9.172 -66.676  1.00 41.95           C  
ANISOU  104  CD  ARG A  12     5333   6160   4446    386    459   -116       C  
ATOM    105  NE  ARG A  12      17.571   8.632 -67.763  1.00 42.68           N  
ANISOU  105  NE  ARG A  12     5370   6405   4440    382    441   -121       N  
ATOM    106  CZ  ARG A  12      16.246   8.520 -67.724  1.00 41.39           C  
ANISOU  106  CZ  ARG A  12     5164   6358   4202    401    414    -92       C  
ATOM    107  NH1 ARG A  12      15.560   8.928 -66.661  1.00 40.16           N  
ANISOU  107  NH1 ARG A  12     5017   6179   4059    430    403    -51       N  
ATOM    108  NH2 ARG A  12      15.606   8.001 -68.754  1.00 41.71           N  
ANISOU  108  NH2 ARG A  12     5148   6547   4151    387    399   -108       N  
ATOM    109  N   GLN A  13      21.185  13.462 -67.186  1.00 48.91           N  
ANISOU  109  N   GLN A  13     6404   6758   5418    527    721     32       N  
ATOM    110  CA  GLN A  13      21.450  14.130 -68.445  1.00 50.28           C  
ANISOU  110  CA  GLN A  13     6594   6968   5539    569    785     76       C  
ATOM    111  C   GLN A  13      21.881  13.158 -69.535  1.00 50.23           C  
ANISOU  111  C   GLN A  13     6546   7031   5507    526    755     16       C  
ATOM    112  O   GLN A  13      22.371  12.068 -69.247  1.00 46.85           O  
ANISOU  112  O   GLN A  13     6091   6580   5128    455    702    -68       O  
ATOM    113  CB  GLN A  13      22.467  15.258 -68.254  1.00 52.66           C  
ANISOU  113  CB  GLN A  13     6964   7145   5898    577    871     91       C  
ATOM    114  CG  GLN A  13      21.846  16.553 -67.722  1.00 57.31           C  
ANISOU  114  CG  GLN A  13     7605   7694   6476    649    937    180       C  
ATOM    115  CD  GLN A  13      22.826  17.404 -66.927  1.00 58.30           C  
ANISOU  115  CD  GLN A  13     7794   7671   6684    622   1004    161       C  
ATOM    116  OE1 GLN A  13      22.511  17.859 -65.824  1.00 58.04           O  
ANISOU  116  OE1 GLN A  13     7787   7579   6687    627   1013    175       O  
ATOM    117  NE2 GLN A  13      24.031  17.619 -67.482  1.00 55.71           N  
ANISOU  117  NE2 GLN A  13     7490   7288   6388    586   1053    124       N  
ATOM    118  N   LYS A  14      21.628  13.550 -70.786  1.00 54.12           N  
ANISOU  118  N   LYS A  14     7033   7614   5916    572    793     65       N  
ATOM    119  CA  LYS A  14      22.171  12.882 -71.962  1.00 55.79           C  
ANISOU  119  CA  LYS A  14     7215   7884   6097    536    787     16       C  
ATOM    120  C   LYS A  14      23.646  13.270 -72.109  1.00 55.34           C  
ANISOU  120  C   LYS A  14     7203   7710   6112    505    843    -19       C  
ATOM    121  O   LYS A  14      23.971  14.448 -72.263  1.00 58.59           O  
ANISOU  121  O   LYS A  14     7667   8068   6523    550    922     38       O  
ATOM    122  CB  LYS A  14      21.374  13.292 -73.210  1.00 58.91           C  
ANISOU  122  CB  LYS A  14     7589   8422   6370    603    812     90       C  
ATOM    123  CG  LYS A  14      21.901  12.707 -74.511  1.00 62.25           C  
ANISOU  123  CG  LYS A  14     7983   8916   6750    567    815     43       C  
ATOM    124  CD  LYS A  14      20.993  13.038 -75.680  1.00 66.22           C  
ANISOU  124  CD  LYS A  14     8455   9585   7120    633    830    117       C  
ATOM    125  CE  LYS A  14      21.509  12.422 -76.976  1.00 69.66           C  
ANISOU  125  CE  LYS A  14     8860  10098   7508    591    831     65       C  
ATOM    126  NZ  LYS A  14      20.550  12.642 -78.100  1.00 72.22           N  
ANISOU  126  NZ  LYS A  14     9141  10608   7689    651    836    133       N  
ATOM    127  N   ALA A  15      24.534  12.281 -72.028  1.00 53.07           N  
ANISOU  127  N   ALA A  15     6895   7383   5887    428    807   -117       N  
ATOM    128  CA  ALA A  15      25.988  12.538 -72.032  1.00 50.22           C  
ANISOU  128  CA  ALA A  15     6565   6915   5601    391    852   -163       C  
ATOM    129  C   ALA A  15      26.471  13.025 -73.379  1.00 49.39           C  
ANISOU  129  C   ALA A  15     6474   6845   5445    409    917   -143       C  
ATOM    130  O   ALA A  15      26.079  12.476 -74.404  1.00 49.58           O  
ANISOU  130  O   ALA A  15     6461   6978   5397    410    898   -148       O  
ATOM    131  CB  ALA A  15      26.755  11.281 -71.644  1.00 46.97           C  
ANISOU  131  CB  ALA A  15     6119   6464   5261    316    796   -267       C  
ATOM    132  N   PRO A  16      27.343  14.047 -73.383  1.00 48.73           N  
ANISOU  132  N   PRO A  16     6444   6671   5399    417    996   -125       N  
ATOM    133  CA  PRO A  16      28.066  14.414 -74.604  1.00 49.86           C  
ANISOU  133  CA  PRO A  16     6603   6827   5511    417   1061   -123       C  
ATOM    134  C   PRO A  16      29.022  13.295 -74.987  1.00 51.43           C  
ANISOU  134  C   PRO A  16     6762   7027   5751    344   1025   -228       C  
ATOM    135  O   PRO A  16      29.180  12.336 -74.212  1.00 47.72           O  
ANISOU  135  O   PRO A  16     6259   6531   5341    298    958   -296       O  
ATOM    136  CB  PRO A  16      28.869  15.647 -74.176  1.00 49.77           C  
ANISOU  136  CB  PRO A  16     6660   6694   5554    422   1150   -101       C  
ATOM    137  CG  PRO A  16      29.030  15.496 -72.690  1.00 48.64           C  
ANISOU  137  CG  PRO A  16     6517   6466   5497    388   1112   -141       C  
ATOM    138  CD  PRO A  16      27.755  14.861 -72.224  1.00 47.17           C  
ANISOU  138  CD  PRO A  16     6293   6352   5275    414   1032   -117       C  
ATOM    139  N   LYS A  17      29.653  13.410 -76.164  1.00 52.28           N  
ANISOU  139  N   LYS A  17     6874   7162   5828    336   1073   -239       N  
ATOM    140  CA  LYS A  17      30.721  12.488 -76.558  1.00 51.67           C  
ANISOU  140  CA  LYS A  17     6764   7071   5796    268   1057   -340       C  
ATOM    141  C   LYS A  17      32.004  12.759 -75.790  1.00 49.83           C  
ANISOU  141  C   LYS A  17     6551   6714   5667    225   1085   -393       C  
ATOM    142  O   LYS A  17      32.617  11.836 -75.265  1.00 49.81           O  
ANISOU  142  O   LYS A  17     6513   6678   5733    177   1037   -474       O  
ATOM    143  CB  LYS A  17      30.977  12.522 -78.074  1.00 55.49           C  
ANISOU  143  CB  LYS A  17     7244   7629   6209    270   1101   -337       C  
ATOM    144  CG  LYS A  17      29.879  11.881 -78.925  1.00 58.24           C  
ANISOU  144  CG  LYS A  17     7550   8123   6454    289   1058   -318       C  
ATOM    145  CD  LYS A  17      29.266  10.652 -78.253  1.00 57.60           C  
ANISOU  145  CD  LYS A  17     7418   8070   6393    255    966   -372       C  
ATOM    146  CE  LYS A  17      28.571   9.755 -79.266  1.00 58.99           C  
ANISOU  146  CE  LYS A  17     7544   8387   6480    239    931   -398       C  
ATOM    147  NZ  LYS A  17      29.565   8.987 -80.075  1.00 58.60           N  
ANISOU  147  NZ  LYS A  17     7476   8336   6452    178    944   -488       N  
ATOM    148  N   ILE A  18      32.414  14.021 -75.736  1.00 50.80           N  
ANISOU  148  N   ILE A  18     6729   6772   5799    244   1169   -349       N  
ATOM    149  CA  ILE A  18      33.549  14.436 -74.897  1.00 51.56           C  
ANISOU  149  CA  ILE A  18     6844   6758   5987    200   1202   -398       C  
ATOM    150  C   ILE A  18      33.156  15.660 -74.055  1.00 53.54           C  
ANISOU  150  C   ILE A  18     7153   6942   6248    232   1253   -331       C  
ATOM    151  O   ILE A  18      32.062  16.198 -74.220  1.00 52.25           O  
ANISOU  151  O   ILE A  18     7016   6814   6019    296   1267   -243       O  
ATOM    152  CB  ILE A  18      34.854  14.694 -75.725  1.00 53.58           C  
ANISOU  152  CB  ILE A  18     7108   6986   6262    160   1272   -446       C  
ATOM    153  CG1 ILE A  18      34.718  15.931 -76.638  1.00 53.54           C  
ANISOU  153  CG1 ILE A  18     7167   6982   6193    200   1375   -367       C  
ATOM    154  CG2 ILE A  18      35.265  13.443 -76.513  1.00 50.79           C  
ANISOU  154  CG2 ILE A  18     6697   6694   5905    127   1224   -519       C  
ATOM    155  CD1 ILE A  18      36.016  16.360 -77.316  1.00 52.67           C  
ANISOU  155  CD1 ILE A  18     7075   6829   6106    156   1457   -411       C  
ATOM    156  N   VAL A  19      34.026  16.075 -73.135  1.00 55.96           N  
ANISOU  156  N   VAL A  19     7474   7157   6631    188   1280   -376       N  
ATOM    157  CA  VAL A  19      33.716  17.212 -72.259  1.00 59.76           C  
ANISOU  157  CA  VAL A  19     8011   7566   7128    206   1334   -326       C  
ATOM    158  C   VAL A  19      34.286  18.530 -72.789  1.00 65.37           C  
ANISOU  158  C   VAL A  19     8792   8214   7830    207   1463   -295       C  
ATOM    159  O   VAL A  19      35.095  18.531 -73.725  1.00 70.83           O  
ANISOU  159  O   VAL A  19     9483   8914   8515    182   1506   -325       O  
ATOM    160  CB  VAL A  19      34.154  16.966 -70.792  1.00 57.94           C  
ANISOU  160  CB  VAL A  19     7758   7277   6978    157   1289   -387       C  
ATOM    161  CG1 VAL A  19      33.376  15.801 -70.197  1.00 57.32           C  
ANISOU  161  CG1 VAL A  19     7626   7251   6900    169   1173   -396       C  
ATOM    162  CG2 VAL A  19      35.652  16.722 -70.688  1.00 55.99           C  
ANISOU  162  CG2 VAL A  19     7481   6995   6796     84   1302   -485       C  
ATOM    163  N   ASN A  20      33.856  19.644 -72.194  1.00 69.80           N  
ANISOU  163  N   ASN A  20     9416   8711   8392    235   1530   -236       N  
ATOM    164  CA  ASN A  20      34.269  20.982 -72.645  1.00 78.91           C  
ANISOU  164  CA  ASN A  20    10652   9792   9536    240   1669   -197       C  
ATOM    165  C   ASN A  20      35.495  21.544 -71.905  1.00 81.45           C  
ANISOU  165  C   ASN A  20    10993  10016   9937    154   1733   -278       C  
ATOM    166  O   ASN A  20      36.254  20.796 -71.283  1.00 80.78           O  
ANISOU  166  O   ASN A  20    10847   9936   9910     87   1667   -372       O  
ATOM    167  CB  ASN A  20      33.088  21.963 -72.584  1.00 81.92           C  
ANISOU  167  CB  ASN A  20    11101  10156   9866    328   1728    -79       C  
ATOM    168  CG  ASN A  20      32.413  21.981 -71.228  1.00 82.92           C  
ANISOU  168  CG  ASN A  20    11225  10255  10026    335   1681    -73       C  
ATOM    169  OD1 ASN A  20      32.796  22.740 -70.342  1.00 84.46           O  
ANISOU  169  OD1 ASN A  20    11461  10355  10272    297   1743    -95       O  
ATOM    170  ND2 ASN A  20      31.395  21.143 -71.062  1.00 85.58           N  
ANISOU  170  ND2 ASN A  20    11509  10676  10329    377   1576    -47       N  
ATOM    171  N   SER A  21      35.685  22.860 -71.987  1.00 85.70           N  
ANISOU  171  N   SER A  21    11617  10470  10474    155   1866   -240       N  
ATOM    172  CA  SER A  21      36.839  23.518 -71.365  1.00 87.07           C  
ANISOU  172  CA  SER A  21    11814  10552  10713     64   1945   -320       C  
ATOM    173  C   SER A  21      36.878  23.351 -69.850  1.00 82.72           C  
ANISOU  173  C   SER A  21    11233   9974  10221     18   1891   -376       C  
ATOM    174  O   SER A  21      37.955  23.322 -69.253  1.00 83.26           O  
ANISOU  174  O   SER A  21    11272  10016  10346    -71   1898   -474       O  
ATOM    175  CB  SER A  21      36.867  25.008 -71.718  1.00 89.61           C  
ANISOU  175  CB  SER A  21    12246  10780  11019     79   2110   -261       C  
ATOM    176  OG  SER A  21      37.512  25.221 -72.959  1.00 94.37           O  
ANISOU  176  OG  SER A  21    12871  11387  11595     71   2182   -259       O  
ATOM    177  N   LYS A  22      35.700  23.234 -69.243  1.00 80.11           N  
ANISOU  177  N   LYS A  22    10905   9659   9871     78   1836   -314       N  
ATOM    178  CA  LYS A  22      35.561  23.217 -67.787  1.00 76.30           C  
ANISOU  178  CA  LYS A  22    10407   9147   9435     44   1795   -351       C  
ATOM    179  C   LYS A  22      36.137  21.956 -67.140  1.00 72.13           C  
ANISOU  179  C   LYS A  22     9780   8676   8950     -9   1667   -443       C  
ATOM    180  O   LYS A  22      36.823  22.030 -66.113  1.00 72.09           O  
ANISOU  180  O   LYS A  22     9753   8642   8996    -80   1663   -518       O  
ATOM    181  CB  LYS A  22      34.089  23.375 -67.399  1.00 78.57           C  
ANISOU  181  CB  LYS A  22    10722   9444   9686    130   1768   -256       C  
ATOM    182  CG  LYS A  22      33.531  24.784 -67.570  1.00 82.32           C  
ANISOU  182  CG  LYS A  22    11302   9840  10135    181   1906   -168       C  
ATOM    183  CD  LYS A  22      32.034  24.762 -67.859  1.00 81.07           C  
ANISOU  183  CD  LYS A  22    11157   9733   9912    297   1875    -52       C  
ATOM    184  CE  LYS A  22      31.259  24.023 -66.779  1.00 78.05           C  
ANISOU  184  CE  LYS A  22    10720   9392   9541    305   1758    -60       C  
ATOM    185  NZ  LYS A  22      29.999  23.438 -67.316  1.00 79.30           N  
ANISOU  185  NZ  LYS A  22    10847   9650   9631    398   1682     21       N  
ATOM    186  N   TYR A  23      35.864  20.807 -67.752  1.00 66.83           N  
ANISOU  186  N   TYR A  23     9050   8088   8254     24   1569   -438       N  
ATOM    187  CA  TYR A  23      36.139  19.513 -67.128  1.00 60.24           C  
ANISOU  187  CA  TYR A  23     8128   7305   7453     -4   1444   -504       C  
ATOM    188  C   TYR A  23      37.478  18.919 -67.526  1.00 58.31           C  
ANISOU  188  C   TYR A  23     7828   7082   7244    -64   1432   -594       C  
ATOM    189  O   TYR A  23      37.940  19.100 -68.656  1.00 58.65           O  
ANISOU  189  O   TYR A  23     7885   7131   7267    -65   1487   -595       O  
ATOM    190  CB  TYR A  23      35.041  18.521 -67.469  1.00 56.69           C  
ANISOU  190  CB  TYR A  23     7646   6930   6961     60   1347   -454       C  
ATOM    191  CG  TYR A  23      33.672  18.898 -66.970  1.00 56.55           C  
ANISOU  191  CG  TYR A  23     7664   6911   6910    121   1338   -372       C  
ATOM    192  CD1 TYR A  23      33.345  18.781 -65.621  1.00 54.84           C  
ANISOU  192  CD1 TYR A  23     7436   6675   6726    106   1289   -385       C  
ATOM    193  CD2 TYR A  23      32.685  19.332 -67.856  1.00 57.35           C  
ANISOU  193  CD2 TYR A  23     7805   7040   6942    196   1375   -278       C  
ATOM    194  CE1 TYR A  23      32.080  19.097 -65.163  1.00 54.77           C  
ANISOU  194  CE1 TYR A  23     7455   6668   6686    162   1281   -312       C  
ATOM    195  CE2 TYR A  23      31.417  19.657 -67.409  1.00 55.51           C  
ANISOU  195  CE2 TYR A  23     7598   6816   6677    258   1366   -201       C  
ATOM    196  CZ  TYR A  23      31.119  19.534 -66.063  1.00 56.75           C  
ANISOU  196  CZ  TYR A  23     7744   6947   6871    239   1319   -220       C  
ATOM    197  OH  TYR A  23      29.859  19.848 -65.611  1.00 59.89           O  
ANISOU  197  OH  TYR A  23     8164   7354   7237    299   1311   -146       O  
ATOM    198  N   ASN A  24      38.081  18.181 -66.596  1.00 52.89           N  
ANISOU  198  N   ASN A  24     7076   6412   6607   -107   1357   -667       N  
ATOM    199  CA  ASN A  24      39.291  17.439 -66.873  1.00 48.25           C  
ANISOU  199  CA  ASN A  24     6422   5857   6053   -152   1329   -751       C  
ATOM    200  C   ASN A  24      39.019  16.308 -67.854  1.00 50.31           C  
ANISOU  200  C   ASN A  24     6648   6178   6289   -111   1264   -740       C  
ATOM    201  O   ASN A  24      37.966  15.662 -67.797  1.00 48.27           O  
ANISOU  201  O   ASN A  24     6383   5951   6004    -61   1195   -693       O  
ATOM    202  CB  ASN A  24      39.889  16.895 -65.579  1.00 47.44           C  
ANISOU  202  CB  ASN A  24     6255   5766   6001   -194   1260   -819       C  
ATOM    203  CG  ASN A  24      41.246  16.262 -65.783  1.00 47.62           C  
ANISOU  203  CG  ASN A  24     6207   5824   6062   -238   1243   -906       C  
ATOM    204  OD1 ASN A  24      41.371  15.239 -66.454  1.00 49.00           O  
ANISOU  204  OD1 ASN A  24     6341   6039   6236   -212   1190   -917       O  
ATOM    205  ND2 ASN A  24      42.273  16.860 -65.195  1.00 46.11           N  
ANISOU  205  ND2 ASN A  24     5997   5619   5902   -306   1290   -972       N  
ATOM    206  N   SER A  25      39.987  16.076 -68.746  1.00 48.99           N  
ANISOU  206  N   SER A  25     6455   6028   6131   -137   1293   -789       N  
ATOM    207  CA  SER A  25      39.883  15.080 -69.806  1.00 46.96           C  
ANISOU  207  CA  SER A  25     6168   5825   5850   -109   1250   -791       C  
ATOM    208  C   SER A  25      39.624  13.662 -69.333  1.00 42.99           C  
ANISOU  208  C   SER A  25     5604   5362   5368    -91   1136   -814       C  
ATOM    209  O   SER A  25      39.164  12.826 -70.106  1.00 42.28           O  
ANISOU  209  O   SER A  25     5499   5314   5249    -62   1097   -803       O  
ATOM    210  CB  SER A  25      41.155  15.085 -70.653  1.00 47.82           C  
ANISOU  210  CB  SER A  25     6253   5939   5975   -152   1303   -855       C  
ATOM    211  OG  SER A  25      41.059  16.063 -71.657  1.00 52.28           O  
ANISOU  211  OG  SER A  25     6881   6485   6495   -146   1401   -813       O  
ATOM    212  N   ILE A  26      39.958  13.374 -68.084  1.00 41.48           N  
ANISOU  212  N   ILE A  26     5376   5158   5224   -111   1087   -850       N  
ATOM    213  CA  ILE A  26      39.720  12.040 -67.531  1.00 40.59           C  
ANISOU  213  CA  ILE A  26     5212   5074   5134    -91    985   -866       C  
ATOM    214  C   ILE A  26      38.247  11.591 -67.708  1.00 39.53           C  
ANISOU  214  C   ILE A  26     5103   4961   4953    -41    938   -800       C  
ATOM    215  O   ILE A  26      37.967  10.410 -67.914  1.00 40.52           O  
ANISOU  215  O   ILE A  26     5198   5117   5079    -24    876   -812       O  
ATOM    216  CB  ILE A  26      40.189  11.937 -66.065  1.00 38.88           C  
ANISOU  216  CB  ILE A  26     4960   4845   4967   -113    943   -900       C  
ATOM    217  CG1 ILE A  26      40.333  10.466 -65.645  1.00 39.52           C  
ANISOU  217  CG1 ILE A  26     4981   4953   5079    -92    851   -929       C  
ATOM    218  CG2 ILE A  26      39.258  12.722 -65.145  1.00 38.07           C  
ANISOU  218  CG2 ILE A  26     4903   4714   4847   -105    946   -846       C  
ATOM    219  CD1 ILE A  26      41.131  10.266 -64.367  1.00 41.02           C  
ANISOU  219  CD1 ILE A  26     5120   5147   5316   -112    813   -972       C  
ATOM    220  N   LEU A  27      37.327  12.550 -67.705  1.00 39.39           N  
ANISOU  220  N   LEU A  27     5142   4930   4894    -20    976   -732       N  
ATOM    221  CA  LEU A  27      35.912  12.257 -67.912  1.00 39.19           C  
ANISOU  221  CA  LEU A  27     5136   4937   4816     26    939   -667       C  
ATOM    222  C   LEU A  27      35.590  11.677 -69.293  1.00 39.52           C  
ANISOU  222  C   LEU A  27     5170   5036   4809     45    937   -659       C  
ATOM    223  O   LEU A  27      34.622  10.928 -69.442  1.00 40.60           O  
ANISOU  223  O   LEU A  27     5296   5218   4912     70    883   -637       O  
ATOM    224  CB  LEU A  27      35.060  13.487 -67.653  1.00 38.75           C  
ANISOU  224  CB  LEU A  27     5141   4858   4724     53    989   -593       C  
ATOM    225  CG  LEU A  27      35.068  14.054 -66.237  1.00 38.94           C  
ANISOU  225  CG  LEU A  27     5178   4832   4785     36    988   -593       C  
ATOM    226  CD1 LEU A  27      34.170  15.280 -66.188  1.00 38.54           C  
ANISOU  226  CD1 LEU A  27     5192   4754   4693     70   1053   -515       C  
ATOM    227  CD2 LEU A  27      34.634  13.017 -65.212  1.00 37.53           C  
ANISOU  227  CD2 LEU A  27     4958   4669   4629     39    889   -606       C  
ATOM    228  N   ASN A  28      36.389  12.027 -70.296  1.00 39.03           N  
ANISOU  228  N   ASN A  28     5114   4975   4739     29   1000   -682       N  
ATOM    229  CA  ASN A  28      36.253  11.421 -71.625  1.00 39.39           C  
ANISOU  229  CA  ASN A  28     5146   5079   4740     38   1000   -687       C  
ATOM    230  C   ASN A  28      36.443   9.884 -71.657  1.00 38.91           C  
ANISOU  230  C   ASN A  28     5030   5046   4707     24    927   -749       C  
ATOM    231  O   ASN A  28      35.790   9.200 -72.441  1.00 37.66           O  
ANISOU  231  O   ASN A  28     4862   4943   4502     36    904   -744       O  
ATOM    232  CB  ASN A  28      37.208  12.079 -72.615  1.00 41.41           C  
ANISOU  232  CB  ASN A  28     5417   5326   4988     17   1084   -707       C  
ATOM    233  CG  ASN A  28      36.870  13.535 -72.875  1.00 43.84           C  
ANISOU  233  CG  ASN A  28     5792   5610   5255     39   1170   -635       C  
ATOM    234  OD1 ASN A  28      35.774  14.002 -72.563  1.00 43.79           O  
ANISOU  234  OD1 ASN A  28     5817   5609   5209     81   1166   -562       O  
ATOM    235  ND2 ASN A  28      37.810  14.257 -73.469  1.00 45.24           N  
ANISOU  235  ND2 ASN A  28     5991   5759   5439     13   1254   -654       N  
ATOM    236  N   ILE A  29      37.358   9.363 -70.827  1.00 37.39           N  
ANISOU  236  N   ILE A  29     4802   4816   4588      0    898   -808       N  
ATOM    237  CA  ILE A  29      37.607   7.916 -70.744  1.00 35.60           C  
ANISOU  237  CA  ILE A  29     4529   4600   4396     -5    837   -863       C  
ATOM    238  C   ILE A  29      36.345   7.198 -70.282  1.00 34.20           C  
ANISOU  238  C   ILE A  29     4354   4443   4196     15    773   -831       C  
ATOM    239  O   ILE A  29      35.859   6.273 -70.957  1.00 33.10           O  
ANISOU  239  O   ILE A  29     4203   4342   4029     15    750   -846       O  
ATOM    240  CB  ILE A  29      38.797   7.588 -69.806  1.00 36.08           C  
ANISOU  240  CB  ILE A  29     4549   4621   4536    -23    818   -919       C  
ATOM    241  CG1 ILE A  29      40.079   8.253 -70.329  1.00 36.22           C  
ANISOU  241  CG1 ILE A  29     4557   4629   4574    -52    885   -961       C  
ATOM    242  CG2 ILE A  29      39.017   6.084 -69.719  1.00 35.67           C  
ANISOU  242  CG2 ILE A  29     4457   4573   4522    -17    764   -966       C  
ATOM    243  CD1 ILE A  29      41.194   8.308 -69.312  1.00 36.88           C  
ANISOU  243  CD1 ILE A  29     4600   4689   4723    -72    876  -1007       C  
ATOM    244  N   ALA A  30      35.792   7.678 -69.167  1.00 33.23           N  
ANISOU  244  N   ALA A  30     4249   4296   4080     28    749   -790       N  
ATOM    245  CA  ALA A  30      34.552   7.165 -68.602  1.00 33.21           C  
ANISOU  245  CA  ALA A  30     4252   4311   4055     46    693   -755       C  
ATOM    246  C   ALA A  30      33.369   7.248 -69.578  1.00 33.97           C  
ANISOU  246  C   ALA A  30     4365   4473   4067     64    701   -711       C  
ATOM    247  O   ALA A  30      32.609   6.295 -69.711  1.00 36.89           O  
ANISOU  247  O   ALA A  30     4721   4880   4415     62    659   -718       O  
ATOM    248  CB  ALA A  30      34.231   7.886 -67.292  1.00 31.57           C  
ANISOU  248  CB  ALA A  30     4062   4067   3863     55    680   -716       C  
ATOM    249  N   LEU A  31      33.224   8.378 -70.261  1.00 33.82           N  
ANISOU  249  N   LEU A  31     4376   4473   4000     80    760   -665       N  
ATOM    250  CA  LEU A  31      32.196   8.525 -71.299  1.00 34.44           C  
ANISOU  250  CA  LEU A  31     4464   4630   3990    104    773   -620       C  
ATOM    251  C   LEU A  31      32.344   7.428 -72.348  1.00 34.48           C  
ANISOU  251  C   LEU A  31     4438   4688   3975     79    761   -674       C  
ATOM    252  O   LEU A  31      31.347   6.857 -72.815  1.00 34.00           O  
ANISOU  252  O   LEU A  31     4364   4700   3855     82    733   -665       O  
ATOM    253  CB  LEU A  31      32.295   9.913 -71.988  1.00 34.23           C  
ANISOU  253  CB  LEU A  31     4478   4608   3920    129    853   -564       C  
ATOM    254  CG  LEU A  31      31.695  11.134 -71.258  1.00 35.94           C  
ANISOU  254  CG  LEU A  31     4738   4793   4124    166    882   -488       C  
ATOM    255  CD1 LEU A  31      32.030  12.445 -71.980  1.00 35.35           C  
ANISOU  255  CD1 LEU A  31     4710   4703   4019    187    976   -442       C  
ATOM    256  CD2 LEU A  31      30.180  10.980 -71.065  1.00 34.30           C  
ANISOU  256  CD2 LEU A  31     4526   4647   3855    204    838   -430       C  
ATOM    257  N   LYS A  32      33.599   7.171 -72.723  1.00 35.18           N  
ANISOU  257  N   LYS A  32     4513   4743   4111     53    786   -735       N  
ATOM    258  CA  LYS A  32      33.976   6.175 -73.717  1.00 36.96           C  
ANISOU  258  CA  LYS A  32     4710   5003   4329     26    787   -797       C  
ATOM    259  C   LYS A  32      33.548   4.779 -73.259  1.00 36.28           C  
ANISOU  259  C   LYS A  32     4599   4918   4267      9    726   -839       C  
ATOM    260  O   LYS A  32      32.723   4.124 -73.908  1.00 35.78           O  
ANISOU  260  O   LYS A  32     4526   4921   4148     -2    711   -848       O  
ATOM    261  CB  LYS A  32      35.501   6.256 -73.935  1.00 40.47           C  
ANISOU  261  CB  LYS A  32     5144   5398   4835      4    827   -852       C  
ATOM    262  CG  LYS A  32      36.145   5.105 -74.687  1.00 42.43           C  
ANISOU  262  CG  LYS A  32     5360   5657   5103    -23    827   -930       C  
ATOM    263  CD  LYS A  32      35.934   5.247 -76.174  1.00 45.24           C  
ANISOU  263  CD  LYS A  32     5719   6086   5381    -32    869   -930       C  
ATOM    264  CE  LYS A  32      36.628   4.126 -76.932  1.00 47.65           C  
ANISOU  264  CE  LYS A  32     5995   6398   5709    -64    877  -1014       C  
ATOM    265  NZ  LYS A  32      36.283   4.192 -78.382  1.00 51.97           N  
ANISOU  265  NZ  LYS A  32     6543   7030   6170    -77    913  -1015       N  
ATOM    266  N   ASN A  33      34.067   4.372 -72.102  1.00 36.19           N  
ANISOU  266  N   ASN A  33     4579   4835   4335      7    694   -862       N  
ATOM    267  CA  ASN A  33      33.701   3.112 -71.456  1.00 35.57           C  
ANISOU  267  CA  ASN A  33     4486   4738   4288     -1    641   -893       C  
ATOM    268  C   ASN A  33      32.200   2.977 -71.231  1.00 36.03           C  
ANISOU  268  C   ASN A  33     4555   4845   4288      2    606   -851       C  
ATOM    269  O   ASN A  33      31.665   1.870 -71.293  1.00 36.62           O  
ANISOU  269  O   ASN A  33     4620   4936   4357    -18    580   -884       O  
ATOM    270  CB  ASN A  33      34.455   2.936 -70.128  1.00 34.84           C  
ANISOU  270  CB  ASN A  33     4386   4569   4281      8    614   -904       C  
ATOM    271  CG  ASN A  33      35.970   3.090 -70.280  1.00 36.10           C  
ANISOU  271  CG  ASN A  33     4526   4693   4497      3    646   -948       C  
ATOM    272  OD1 ASN A  33      36.541   2.805 -71.336  1.00 37.03           O  
ANISOU  272  OD1 ASN A  33     4631   4828   4609    -10    681   -990       O  
ATOM    273  ND2 ASN A  33      36.621   3.546 -69.224  1.00 35.69           N  
ANISOU  273  ND2 ASN A  33     4466   4598   4495     13    636   -941       N  
ATOM    274  N   PHE A  34      31.518   4.097 -70.990  1.00 34.48           N  
ANISOU  274  N   PHE A  34     4378   4673   4048     29    612   -781       N  
ATOM    275  CA  PHE A  34      30.048   4.087 -70.911  1.00 35.05           C  
ANISOU  275  CA  PHE A  34     4454   4810   4053     38    584   -737       C  
ATOM    276  C   PHE A  34      29.406   3.657 -72.235  1.00 34.38           C  
ANISOU  276  C   PHE A  34     4351   4824   3885     21    595   -752       C  
ATOM    277  O   PHE A  34      28.575   2.747 -72.270  1.00 34.70           O  
ANISOU  277  O   PHE A  34     4376   4909   3898     -3    564   -776       O  
ATOM    278  CB  PHE A  34      29.498   5.450 -70.440  1.00 35.52           C  
ANISOU  278  CB  PHE A  34     4539   4874   4082     79    597   -654       C  
ATOM    279  CG  PHE A  34      27.990   5.499 -70.327  1.00 36.91           C  
ANISOU  279  CG  PHE A  34     4712   5122   4187     96    569   -604       C  
ATOM    280  CD1 PHE A  34      27.267   4.396 -69.885  1.00 38.11           C  
ANISOU  280  CD1 PHE A  34     4846   5292   4339     71    519   -633       C  
ATOM    281  CD2 PHE A  34      27.298   6.663 -70.626  1.00 37.85           C  
ANISOU  281  CD2 PHE A  34     4848   5291   4240    141    597   -527       C  
ATOM    282  CE1 PHE A  34      25.877   4.450 -69.780  1.00 37.90           C  
ANISOU  282  CE1 PHE A  34     4812   5343   4246     82    494   -592       C  
ATOM    283  CE2 PHE A  34      25.917   6.723 -70.524  1.00 35.84           C  
ANISOU  283  CE2 PHE A  34     4584   5114   3918    163    572   -480       C  
ATOM    284  CZ  PHE A  34      25.208   5.624 -70.104  1.00 36.76           C  
ANISOU  284  CZ  PHE A  34     4675   5257   4033    131    518   -515       C  
ATOM    285  N   ARG A  35      29.807   4.302 -73.320  1.00 34.22           N  
ANISOU  285  N   ARG A  35     4334   4842   3824     29    643   -743       N  
ATOM    286  CA  ARG A  35      29.348   3.910 -74.652  1.00 36.33           C  
ANISOU  286  CA  ARG A  35     4580   5213   4010      9    658   -763       C  
ATOM    287  C   ARG A  35      29.723   2.451 -75.017  1.00 35.60           C  
ANISOU  287  C   ARG A  35     4465   5112   3948    -45    648   -859       C  
ATOM    288  O   ARG A  35      28.927   1.751 -75.647  1.00 35.96           O  
ANISOU  288  O   ARG A  35     4490   5241   3931    -76    638   -887       O  
ATOM    289  CB  ARG A  35      29.874   4.878 -75.729  1.00 36.39           C  
ANISOU  289  CB  ARG A  35     4598   5253   3973     29    716   -736       C  
ATOM    290  CG  ARG A  35      29.425   6.334 -75.566  1.00 35.80           C  
ANISOU  290  CG  ARG A  35     4554   5191   3858     87    743   -637       C  
ATOM    291  CD  ARG A  35      29.766   7.161 -76.806  1.00 37.26           C  
ANISOU  291  CD  ARG A  35     4751   5424   3981    107    806   -607       C  
ATOM    292  NE  ARG A  35      31.213   7.217 -77.087  1.00 37.02           N  
ANISOU  292  NE  ARG A  35     4729   5319   4014     81    848   -658       N  
ATOM    293  CZ  ARG A  35      32.051   8.128 -76.575  1.00 37.74           C  
ANISOU  293  CZ  ARG A  35     4853   5322   4163     94    887   -639       C  
ATOM    294  NH1 ARG A  35      31.606   9.075 -75.742  1.00 37.61           N  
ANISOU  294  NH1 ARG A  35     4867   5269   4150    133    894   -570       N  
ATOM    295  NH2 ARG A  35      33.338   8.094 -76.887  1.00 36.81           N  
ANISOU  295  NH2 ARG A  35     4734   5153   4097     65    924   -693       N  
ATOM    296  N   LEU A  36      30.926   2.014 -74.623  1.00 35.60           N  
ANISOU  296  N   LEU A  36     4469   5015   4042    -55    655   -908       N  
ATOM    297  CA  LEU A  36      31.404   0.645 -74.900  1.00 33.89           C  
ANISOU  297  CA  LEU A  36     4238   4771   3866    -98    656   -996       C  
ATOM    298  C   LEU A  36      30.530  -0.370 -74.184  1.00 32.74           C  
ANISOU  298  C   LEU A  36     4090   4617   3729   -119    615  -1014       C  
ATOM    299  O   LEU A  36      30.103  -1.348 -74.770  1.00 32.80           O  
ANISOU  299  O   LEU A  36     4087   4664   3708   -164    620  -1070       O  
ATOM    300  CB  LEU A  36      32.867   0.485 -74.470  1.00 32.80           C  
ANISOU  300  CB  LEU A  36     4100   4533   3829    -90    671  -1032       C  
ATOM    301  CG  LEU A  36      34.031   0.451 -75.474  1.00 35.22           C  
ANISOU  301  CG  LEU A  36     4396   4835   4152   -103    721  -1083       C  
ATOM    302  CD1 LEU A  36      33.675   0.840 -76.919  1.00 34.76           C  
ANISOU  302  CD1 LEU A  36     4332   4875   3998   -120    758  -1081       C  
ATOM    303  CD2 LEU A  36      35.241   1.239 -74.964  1.00 34.73           C  
ANISOU  303  CD2 LEU A  36     4334   4706   4154    -77    738  -1070       C  
ATOM    304  N   CYS A  37      30.255  -0.110 -72.911  1.00 33.18           N  
ANISOU  304  N   CYS A  37     4159   4622   3823    -93    578   -970       N  
ATOM    305  CA  CYS A  37      29.398  -0.969 -72.081  1.00 34.28           C  
ANISOU  305  CA  CYS A  37     4304   4747   3973   -110    539   -978       C  
ATOM    306  C   CYS A  37      27.990  -1.133 -72.692  1.00 35.09           C  
ANISOU  306  C   CYS A  37     4392   4963   3975   -139    531   -973       C  
ATOM    307  O   CYS A  37      27.424  -2.240 -72.699  1.00 33.01           O  
ANISOU  307  O   CYS A  37     4125   4712   3705   -185    523  -1024       O  
ATOM    308  CB  CYS A  37      29.284  -0.383 -70.660  1.00 34.19           C  
ANISOU  308  CB  CYS A  37     4308   4679   4003    -72    504   -918       C  
ATOM    309  SG  CYS A  37      28.313  -1.360 -69.487  1.00 39.03           S  
ANISOU  309  SG  CYS A  37     4931   5262   4635    -89    458   -920       S  
ATOM    310  N   LYS A  38      27.431  -0.025 -73.190  1.00 35.49           N  
ANISOU  310  N   LYS A  38     4435   5101   3947   -112    536   -912       N  
ATOM    311  CA  LYS A  38      26.103  -0.052 -73.787  1.00 37.54           C  
ANISOU  311  CA  LYS A  38     4671   5490   4101   -130    526   -900       C  
ATOM    312  C   LYS A  38      26.039  -0.912 -75.040  1.00 39.14           C  
ANISOU  312  C   LYS A  38     4849   5769   4252   -188    551   -975       C  
ATOM    313  O   LYS A  38      25.003  -1.516 -75.319  1.00 41.77           O  
ANISOU  313  O   LYS A  38     5158   6190   4519   -231    539  -1003       O  
ATOM    314  CB  LYS A  38      25.588   1.367 -74.059  1.00 39.30           C  
ANISOU  314  CB  LYS A  38     4891   5789   4251    -73    532   -809       C  
ATOM    315  CG  LYS A  38      25.095   2.076 -72.794  1.00 39.27           C  
ANISOU  315  CG  LYS A  38     4906   5742   4271    -29    503   -737       C  
ATOM    316  CD  LYS A  38      24.441   3.401 -73.115  1.00 39.48           C  
ANISOU  316  CD  LYS A  38     4933   5848   4220     29    518   -646       C  
ATOM    317  CE  LYS A  38      25.464   4.485 -73.403  1.00 39.61           C  
ANISOU  317  CE  LYS A  38     4978   5810   4261     70    564   -609       C  
ATOM    318  NZ  LYS A  38      24.768   5.773 -73.676  1.00 40.96           N  
ANISOU  318  NZ  LYS A  38     5157   6047   4356    134    587   -513       N  
ATOM    319  N   LYS A  39      27.153  -0.980 -75.778  1.00 39.19           N  
ANISOU  319  N   LYS A  39     4859   5742   4287   -195    589  -1015       N  
ATOM    320  CA  LYS A  39      27.222  -1.744 -77.033  1.00 40.03           C  
ANISOU  320  CA  LYS A  39     4945   5918   4347   -251    621  -1092       C  
ATOM    321  C   LYS A  39      27.459  -3.233 -76.818  1.00 39.69           C  
ANISOU  321  C   LYS A  39     4909   5804   4366   -311    629  -1185       C  
ATOM    322  O   LYS A  39      27.075  -4.041 -77.642  1.00 42.19           O  
ANISOU  322  O   LYS A  39     5208   6188   4632   -373    650  -1255       O  
ATOM    323  CB  LYS A  39      28.313  -1.195 -77.939  1.00 41.15           C  
ANISOU  323  CB  LYS A  39     5088   6053   4491   -235    664  -1096       C  
ATOM    324  CG  LYS A  39      28.023   0.173 -78.512  1.00 42.73           C  
ANISOU  324  CG  LYS A  39     5283   6341   4609   -186    675  -1012       C  
ATOM    325  CD  LYS A  39      29.209   0.685 -79.321  1.00 45.23           C  
ANISOU  325  CD  LYS A  39     5608   6634   4940   -174    724  -1020       C  
ATOM    326  CE  LYS A  39      28.932   2.067 -79.904  1.00 46.59           C  
ANISOU  326  CE  LYS A  39     5785   6884   5030   -121    745   -930       C  
ATOM    327  NZ  LYS A  39      30.204   2.771 -80.225  1.00 49.97           N  
ANISOU  327  NZ  LYS A  39     6236   7245   5503   -100    793   -923       N  
ATOM    328  N   HIS A  40      28.121  -3.581 -75.723  1.00 39.49           N  
ANISOU  328  N   HIS A  40     4911   5645   4449   -290    618  -1187       N  
ATOM    329  CA  HIS A  40      28.382  -4.966 -75.382  1.00 40.33           C  
ANISOU  329  CA  HIS A  40     5033   5667   4623   -331    631  -1263       C  
ATOM    330  C   HIS A  40      27.136  -5.705 -74.988  1.00 44.54           C  
ANISOU  330  C   HIS A  40     5566   6234   5121   -378    612  -1282       C  
ATOM    331  O   HIS A  40      26.566  -5.460 -73.924  1.00 45.92           O  
ANISOU  331  O   HIS A  40     5751   6386   5309   -353    572  -1229       O  
ATOM    332  CB  HIS A  40      29.402  -5.048 -74.253  1.00 37.01           C  
ANISOU  332  CB  HIS A  40     4637   5106   4320   -283    620  -1244       C  
ATOM    333  CG  HIS A  40      29.784  -6.463 -73.885  1.00 36.65           C  
ANISOU  333  CG  HIS A  40     4613   4962   4350   -309    641  -1312       C  
ATOM    334  ND1 HIS A  40      30.043  -6.841 -72.614  1.00 35.18           N  
ANISOU  334  ND1 HIS A  40     4449   4672   4245   -276    619  -1290       N  
ATOM    335  CD2 HIS A  40      29.913  -7.619 -74.673  1.00 35.49           C  
ANISOU  335  CD2 HIS A  40     4471   4806   4207   -366    690  -1402       C  
ATOM    336  CE1 HIS A  40      30.343  -8.155 -72.594  1.00 34.81           C  
ANISOU  336  CE1 HIS A  40     4423   4549   4252   -303    653  -1355       C  
ATOM    337  NE2 HIS A  40      30.255  -8.627 -73.852  1.00 34.59           N  
ANISOU  337  NE2 HIS A  40     4386   4575   4179   -360    699  -1426       N  
ATOM    338  N   LYS A  41      26.721  -6.647 -75.826  1.00 51.43           N  
ANISOU  338  N   LYS A  41     6429   7160   5949   -452    644  -1364       N  
ATOM    339  CA  LYS A  41      25.594  -7.513 -75.504  1.00 56.06           C  
ANISOU  339  CA  LYS A  41     7017   7775   6506   -514    638  -1402       C  
ATOM    340  C   LYS A  41      26.092  -8.762 -74.778  1.00 58.99           C  
ANISOU  340  C   LYS A  41     7433   7998   6983   -533    664  -1455       C  
ATOM    341  O   LYS A  41      26.724  -9.635 -75.373  1.00 63.99           O  
ANISOU  341  O   LYS A  41     8079   8584   7650   -570    716  -1533       O  
ATOM    342  CB  LYS A  41      24.802  -7.877 -76.770  1.00 59.38           C  
ANISOU  342  CB  LYS A  41     7401   8342   6815   -594    664  -1468       C  
ATOM    343  CG  LYS A  41      24.438  -6.684 -77.663  1.00 60.59           C  
ANISOU  343  CG  LYS A  41     7511   8651   6859   -566    648  -1414       C  
ATOM    344  CD  LYS A  41      23.451  -5.735 -76.981  1.00 62.20           C  
ANISOU  344  CD  LYS A  41     7698   8922   7012   -517    594  -1318       C  
ATOM    345  CE  LYS A  41      23.209  -4.477 -77.808  1.00 62.36           C  
ANISOU  345  CE  LYS A  41     7682   9076   6933   -469    585  -1249       C  
ATOM    346  NZ  LYS A  41      22.659  -3.358 -76.988  1.00 64.76           N  
ANISOU  346  NZ  LYS A  41     7986   9394   7223   -393    543  -1139       N  
ATOM    347  N   THR A  42      25.826  -8.811 -73.480  1.00 61.31           N  
ANISOU  347  N   THR A  42     7750   8217   7326   -503    630  -1408       N  
ATOM    348  CA  THR A  42      26.253  -9.907 -72.620  1.00 64.87           C  
ANISOU  348  CA  THR A  42     8246   8524   7876   -505    650  -1438       C  
ATOM    349  C   THR A  42      25.047 -10.732 -72.172  1.00 70.88           C  
ANISOU  349  C   THR A  42     9023   9297   8610   -571    653  -1469       C  
ATOM    350  O   THR A  42      23.968 -10.183 -71.909  1.00 65.76           O  
ANISOU  350  O   THR A  42     8351   8740   7892   -580    613  -1429       O  
ATOM    351  CB  THR A  42      27.005  -9.383 -71.367  1.00 66.02           C  
ANISOU  351  CB  THR A  42     8409   8567   8106   -416    611  -1359       C  
ATOM    352  OG1 THR A  42      26.592 -10.118 -70.208  1.00 63.27           O  
ANISOU  352  OG1 THR A  42     8097   8137   7805   -419    602  -1350       O  
ATOM    353  CG2 THR A  42      26.716  -7.901 -71.130  1.00 61.21           C  
ANISOU  353  CG2 THR A  42     7773   8033   7450   -366    559  -1272       C  
ATOM    354  N   LYS A  43      25.243 -12.047 -72.070  1.00 76.08           N  
ANISOU  354  N   LYS A  43     9723   9859   9325   -614    707  -1539       N  
ATOM    355  CA  LYS A  43      24.178 -12.968 -71.652  1.00 83.21           C  
ANISOU  355  CA  LYS A  43    10650  10754  10210   -688    725  -1581       C  
ATOM    356  C   LYS A  43      23.843 -12.868 -70.152  1.00 84.16           C  
ANISOU  356  C   LYS A  43    10797  10803  10375   -642    681  -1507       C  
ATOM    357  O   LYS A  43      22.669 -12.951 -69.767  1.00 83.05           O  
ANISOU  357  O   LYS A  43    10653  10718  10184   -688    664  -1505       O  
ATOM    358  CB  LYS A  43      24.544 -14.415 -72.015  1.00 85.29           C  
ANISOU  358  CB  LYS A  43    10959  10920  10525   -748    811  -1680       C  
ATOM    359  CG  LYS A  43      23.362 -15.262 -72.461  1.00 86.83           C  
ANISOU  359  CG  LYS A  43    11157  11182  10653   -869    854  -1768       C  
ATOM    360  CD  LYS A  43      23.781 -16.697 -72.747  1.00 88.56           C  
ANISOU  360  CD  LYS A  43    11433  11282  10933   -928    951  -1866       C  
ATOM    361  CE  LYS A  43      23.240 -17.185 -74.084  1.00 87.73           C  
ANISOU  361  CE  LYS A  43    11302  11287  10742  -1047   1008  -1981       C  
ATOM    362  NZ  LYS A  43      21.761 -17.056 -74.188  1.00 88.59           N  
ANISOU  362  NZ  LYS A  43    11373  11546  10741  -1134    985  -2004       N  
ATOM    363  N   LYS A  44      24.876 -12.673 -69.323  1.00 85.41           N  
ANISOU  363  N   LYS A  44    10978  10847  10623   -554    663  -1449       N  
ATOM    364  CA  LYS A  44      24.740 -12.749 -67.856  1.00 86.26           C  
ANISOU  364  CA  LYS A  44    11119  10871  10785   -509    630  -1386       C  
ATOM    365  C   LYS A  44      24.447 -11.407 -67.159  1.00 82.26           C  
ANISOU  365  C   LYS A  44    10581  10423  10249   -451    553  -1292       C  
ATOM    366  O   LYS A  44      25.109 -10.396 -67.435  1.00 73.76           O  
ANISOU  366  O   LYS A  44     9475   9380   9169   -398    528  -1252       O  
ATOM    367  CB  LYS A  44      25.958 -13.448 -67.225  1.00 88.60           C  
ANISOU  367  CB  LYS A  44    11458  11012  11192   -448    657  -1378       C  
ATOM    368  CG  LYS A  44      26.033 -14.948 -67.511  1.00 92.95           C  
ANISOU  368  CG  LYS A  44    12060  11471  11784   -501    740  -1459       C  
ATOM    369  CD  LYS A  44      25.064 -15.747 -66.646  1.00 94.74           C  
ANISOU  369  CD  LYS A  44    12333  11647  12014   -545    755  -1463       C  
ATOM    370  CE  LYS A  44      24.731 -17.103 -67.262  1.00 99.69           C  
ANISOU  370  CE  LYS A  44    13005  12225  12646   -637    849  -1565       C  
ATOM    371  NZ  LYS A  44      25.886 -18.047 -67.272  1.00101.31           N  
ANISOU  371  NZ  LYS A  44    13259  12285  12947   -593    917  -1589       N  
ATOM    372  N   PRO A  45      23.451 -11.411 -66.244  1.00 80.22           N  
ANISOU  372  N   PRO A  45    10333  10174   9970   -466    523  -1259       N  
ATOM    373  CA  PRO A  45      22.875 -10.261 -65.542  1.00 75.36           C  
ANISOU  373  CA  PRO A  45     9693   9620   9318   -427    459  -1178       C  
ATOM    374  C   PRO A  45      23.848  -9.168 -65.099  1.00 69.27           C  
ANISOU  374  C   PRO A  45     8909   8823   8585   -337    421  -1106       C  
ATOM    375  O   PRO A  45      24.994  -9.440 -64.733  1.00 67.06           O  
ANISOU  375  O   PRO A  45     8649   8446   8385   -291    430  -1101       O  
ATOM    376  CB  PRO A  45      22.202 -10.906 -64.333  1.00 79.73           C  
ANISOU  376  CB  PRO A  45    10284  10111   9896   -442    451  -1162       C  
ATOM    377  CG  PRO A  45      21.722 -12.219 -64.860  1.00 81.04           C  
ANISOU  377  CG  PRO A  45    10476  10261  10053   -531    513  -1251       C  
ATOM    378  CD  PRO A  45      22.725 -12.654 -65.905  1.00 82.30           C  
ANISOU  378  CD  PRO A  45    10638  10388  10241   -534    563  -1309       C  
ATOM    379  N   VAL A  46      23.340  -7.942 -65.092  1.00 64.56           N  
ANISOU  379  N   VAL A  46     8281   8316   7932   -314    381  -1052       N  
ATOM    380  CA  VAL A  46      24.148  -6.752 -64.926  1.00 61.21           C  
ANISOU  380  CA  VAL A  46     7841   7889   7526   -245    357   -994       C  
ATOM    381  C   VAL A  46      24.186  -6.297 -63.459  1.00 59.62           C  
ANISOU  381  C   VAL A  46     7656   7632   7365   -197    315   -927       C  
ATOM    382  O   VAL A  46      23.142  -6.013 -62.852  1.00 65.06           O  
ANISOU  382  O   VAL A  46     8343   8358   8015   -206    288   -893       O  
ATOM    383  CB  VAL A  46      23.652  -5.606 -65.864  1.00 59.16           C  
ANISOU  383  CB  VAL A  46     7542   7755   7179   -242    351   -971       C  
ATOM    384  CG1 VAL A  46      23.386  -6.138 -67.268  1.00 53.79           C  
ANISOU  384  CG1 VAL A  46     6843   7152   6443   -300    389  -1039       C  
ATOM    385  CG2 VAL A  46      22.400  -4.945 -65.320  1.00 55.06           C  
ANISOU  385  CG2 VAL A  46     7011   7309   6601   -239    316   -918       C  
ATOM    386  N   GLN A  47      25.383  -6.278 -62.882  1.00 53.22           N  
ANISOU  386  N   GLN A  47     6855   6735   6628   -148    311   -911       N  
ATOM    387  CA  GLN A  47      25.594  -5.645 -61.580  1.00 52.42           C  
ANISOU  387  CA  GLN A  47     6760   6597   6560   -101    271   -849       C  
ATOM    388  C   GLN A  47      26.147  -4.211 -61.753  1.00 45.76           C  
ANISOU  388  C   GLN A  47     5892   5790   5705    -62    261   -811       C  
ATOM    389  O   GLN A  47      27.285  -4.024 -62.190  1.00 43.13           O  
ANISOU  389  O   GLN A  47     5546   5435   5405    -40    279   -827       O  
ATOM    390  CB  GLN A  47      26.520  -6.503 -60.712  1.00 56.69           C  
ANISOU  390  CB  GLN A  47     7323   7033   7182    -70    271   -852       C  
ATOM    391  CG  GLN A  47      25.810  -7.581 -59.887  1.00 62.48           C  
ANISOU  391  CG  GLN A  47     8093   7715   7929    -92    269   -853       C  
ATOM    392  CD  GLN A  47      25.283  -7.066 -58.552  1.00 61.20           C  
ANISOU  392  CD  GLN A  47     7939   7551   7763    -72    224   -792       C  
ATOM    393  OE1 GLN A  47      25.076  -5.864 -58.371  1.00 64.01           O  
ANISOU  393  OE1 GLN A  47     8273   7960   8087    -57    197   -753       O  
ATOM    394  NE2 GLN A  47      25.069  -7.976 -57.610  1.00 60.60           N  
ANISOU  394  NE2 GLN A  47     7898   7409   7717    -72    222   -782       N  
ATOM    395  N   ILE A  48      25.327  -3.207 -61.449  1.00 41.64           N  
ANISOU  395  N   ILE A  48     5363   5323   5133    -55    240   -763       N  
ATOM    396  CA  ILE A  48      25.684  -1.820 -61.780  1.00 39.37           C  
ANISOU  396  CA  ILE A  48     5060   5073   4826    -25    246   -728       C  
ATOM    397  C   ILE A  48      27.004  -1.365 -61.114  1.00 37.86           C  
ANISOU  397  C   ILE A  48     4867   4818   4699     11    242   -717       C  
ATOM    398  O   ILE A  48      27.876  -0.792 -61.782  1.00 35.99           O  
ANISOU  398  O   ILE A  48     4617   4587   4471     23    267   -727       O  
ATOM    399  CB  ILE A  48      24.502  -0.824 -61.582  1.00 38.08           C  
ANISOU  399  CB  ILE A  48     4893   4977   4597    -18    232   -675       C  
ATOM    400  CG1 ILE A  48      23.710  -0.664 -62.878  1.00 40.86           C  
ANISOU  400  CG1 ILE A  48     5225   5428   4869    -37    253   -684       C  
ATOM    401  CG2 ILE A  48      25.002   0.580 -61.285  1.00 35.08           C  
ANISOU  401  CG2 ILE A  48     4514   4591   4223     21    239   -628       C  
ATOM    402  CD1 ILE A  48      23.066  -1.911 -63.399  1.00 43.49           C  
ANISOU  402  CD1 ILE A  48     5553   5793   5177    -90    257   -738       C  
ATOM    403  N   LEU A  49      27.163  -1.664 -59.826  1.00 37.35           N  
ANISOU  403  N   LEU A  49     4813   4699   4676     25    212   -699       N  
ATOM    404  CA  LEU A  49      28.395  -1.297 -59.090  1.00 37.45           C  
ANISOU  404  CA  LEU A  49     4816   4667   4744     57    204   -691       C  
ATOM    405  C   LEU A  49      29.610  -1.837 -59.816  1.00 36.62           C  
ANISOU  405  C   LEU A  49     4695   4537   4681     65    230   -737       C  
ATOM    406  O   LEU A  49      30.560  -1.106 -60.071  1.00 35.44           O  
ANISOU  406  O   LEU A  49     4525   4392   4546     78    245   -743       O  
ATOM    407  CB  LEU A  49      28.366  -1.822 -57.651  1.00 36.11           C  
ANISOU  407  CB  LEU A  49     4658   4451   4609     71    167   -669       C  
ATOM    408  CG  LEU A  49      28.007  -0.943 -56.435  1.00 36.74           C  
ANISOU  408  CG  LEU A  49     4742   4536   4679     81    139   -621       C  
ATOM    409  CD1 LEU A  49      27.436   0.421 -56.790  1.00 34.92           C  
ANISOU  409  CD1 LEU A  49     4512   4354   4401     76    154   -595       C  
ATOM    410  CD2 LEU A  49      27.076  -1.687 -55.469  1.00 36.62           C  
ANISOU  410  CD2 LEU A  49     4751   4502   4660     73    109   -600       C  
ATOM    411  N   ALA A  50      29.542  -3.113 -60.194  1.00 37.33           N  
ANISOU  411  N   ALA A  50     4795   4600   4788     52    240   -773       N  
ATOM    412  CA  ALA A  50      30.612  -3.774 -60.950  1.00 36.22           C  
ANISOU  412  CA  ALA A  50     4641   4432   4686     60    271   -822       C  
ATOM    413  C   ALA A  50      30.868  -3.179 -62.344  1.00 36.31           C  
ANISOU  413  C   ALA A  50     4637   4493   4666     43    307   -849       C  
ATOM    414  O   ALA A  50      32.018  -3.088 -62.771  1.00 38.95           O  
ANISOU  414  O   ALA A  50     4951   4815   5034     58    328   -875       O  
ATOM    415  CB  ALA A  50      30.341  -5.273 -61.051  1.00 37.16           C  
ANISOU  415  CB  ALA A  50     4785   4505   4828     46    285   -855       C  
ATOM    416  N   LEU A  51      29.814  -2.801 -63.066  1.00 34.69           N  
ANISOU  416  N   LEU A  51     4437   4349   4393     12    316   -844       N  
ATOM    417  CA  LEU A  51      30.010  -2.181 -64.386  1.00 34.36           C  
ANISOU  417  CA  LEU A  51     4380   4361   4312      1    350   -861       C  
ATOM    418  C   LEU A  51      30.668  -0.837 -64.221  1.00 32.26           C  
ANISOU  418  C   LEU A  51     4104   4102   4049     26    356   -828       C  
ATOM    419  O   LEU A  51      31.586  -0.479 -64.958  1.00 34.96           O  
ANISOU  419  O   LEU A  51     4431   4448   4402     30    387   -852       O  
ATOM    420  CB  LEU A  51      28.692  -2.006 -65.157  1.00 32.70           C  
ANISOU  420  CB  LEU A  51     4173   4231   4018    -29    356   -854       C  
ATOM    421  CG  LEU A  51      28.050  -3.221 -65.804  1.00 34.52           C  
ANISOU  421  CG  LEU A  51     4407   4481   4225    -74    369   -905       C  
ATOM    422  CD1 LEU A  51      26.739  -2.814 -66.488  1.00 33.92           C  
ANISOU  422  CD1 LEU A  51     4322   4511   4054   -101    368   -890       C  
ATOM    423  CD2 LEU A  51      29.023  -3.869 -66.790  1.00 35.41           C  
ANISOU  423  CD2 LEU A  51     4512   4573   4365    -87    409   -968       C  
ATOM    424  N   LEU A  52      30.184  -0.089 -63.249  1.00 32.45           N  
ANISOU  424  N   LEU A  52     4137   4126   4064     40    330   -778       N  
ATOM    425  CA  LEU A  52      30.591   1.297 -63.067  1.00 31.71           C  
ANISOU  425  CA  LEU A  52     4042   4041   3966     57    344   -746       C  
ATOM    426  C   LEU A  52      32.081   1.367 -62.709  1.00 31.04           C  
ANISOU  426  C   LEU A  52     3937   3913   3944     69    352   -773       C  
ATOM    427  O   LEU A  52      32.788   2.287 -63.124  1.00 28.42           O  
ANISOU  427  O   LEU A  52     3596   3588   3611     69    386   -776       O  
ATOM    428  CB  LEU A  52      29.739   1.925 -61.991  1.00 30.07           C  
ANISOU  428  CB  LEU A  52     3850   3834   3740     66    318   -693       C  
ATOM    429  CG  LEU A  52      28.957   3.215 -62.272  1.00 32.74           C  
ANISOU  429  CG  LEU A  52     4204   4216   4020     75    340   -643       C  
ATOM    430  CD1 LEU A  52      28.635   3.441 -63.737  1.00 30.76           C  
ANISOU  430  CD1 LEU A  52     3950   4025   3712     71    376   -646       C  
ATOM    431  CD2 LEU A  52      27.690   3.270 -61.400  1.00 30.15           C  
ANISOU  431  CD2 LEU A  52     3890   3902   3663     79    307   -601       C  
ATOM    432  N   GLN A  53      32.544   0.352 -61.984  1.00 30.93           N  
ANISOU  432  N   GLN A  53     3912   3856   3981     79    324   -792       N  
ATOM    433  CA  GLN A  53      33.934   0.259 -61.580  1.00 32.77           C  
ANISOU  433  CA  GLN A  53     4117   4062   4272     97    325   -817       C  
ATOM    434  C   GLN A  53      34.884  -0.061 -62.752  1.00 33.60           C  
ANISOU  434  C   GLN A  53     4200   4169   4394     94    365   -868       C  
ATOM    435  O   GLN A  53      36.089   0.191 -62.667  1.00 31.78           O  
ANISOU  435  O   GLN A  53     3940   3934   4200    105    377   -891       O  
ATOM    436  CB  GLN A  53      34.083  -0.714 -60.408  1.00 33.72           C  
ANISOU  436  CB  GLN A  53     4233   4144   4435    121    284   -811       C  
ATOM    437  CG  GLN A  53      33.940   0.004 -59.064  1.00 37.14           C  
ANISOU  437  CG  GLN A  53     4666   4578   4867    129    251   -771       C  
ATOM    438  CD  GLN A  53      33.388  -0.860 -57.953  1.00 38.67           C  
ANISOU  438  CD  GLN A  53     4874   4743   5074    145    209   -745       C  
ATOM    439  OE1 GLN A  53      33.747  -2.021 -57.810  1.00 41.88           O  
ANISOU  439  OE1 GLN A  53     5278   5117   5516    167    201   -758       O  
ATOM    440  NE2 GLN A  53      32.511  -0.282 -57.149  1.00 40.52           N  
ANISOU  440  NE2 GLN A  53     5127   4987   5280    135    186   -705       N  
ATOM    441  N   GLU A  54      34.321  -0.543 -63.861  1.00 32.67           N  
ANISOU  441  N   GLU A  54     4097   4070   4245     75    387   -888       N  
ATOM    442  CA  GLU A  54      35.062  -0.649 -65.111  1.00 34.45           C  
ANISOU  442  CA  GLU A  54     4307   4309   4473     65    430   -933       C  
ATOM    443  C   GLU A  54      34.951   0.615 -65.972  1.00 34.93           C  
ANISOU  443  C   GLU A  54     4373   4416   4482     49    466   -919       C  
ATOM    444  O   GLU A  54      35.843   0.931 -66.769  1.00 33.33           O  
ANISOU  444  O   GLU A  54     4153   4221   4286     43    505   -949       O  
ATOM    445  CB  GLU A  54      34.570  -1.843 -65.892  1.00 36.67           C  
ANISOU  445  CB  GLU A  54     4599   4587   4743     47    442   -969       C  
ATOM    446  CG  GLU A  54      34.658  -3.129 -65.097  1.00 39.03           C  
ANISOU  446  CG  GLU A  54     4905   4829   5095     65    421   -981       C  
ATOM    447  CD  GLU A  54      33.944  -4.245 -65.763  1.00 39.50           C  
ANISOU  447  CD  GLU A  54     4986   4883   5137     36    438  -1016       C  
ATOM    448  OE1 GLU A  54      33.229  -3.966 -66.735  1.00 42.01           O  
ANISOU  448  OE1 GLU A  54     5310   5257   5394      0    457  -1026       O  
ATOM    449  OE2 GLU A  54      34.089  -5.397 -65.310  1.00 43.08           O  
ANISOU  449  OE2 GLU A  54     5452   5279   5636     49    438  -1033       O  
ATOM    450  N   ILE A  55      33.842   1.326 -65.815  1.00 33.39           N  
ANISOU  450  N   ILE A  55     4201   4250   4233     45    457   -870       N  
ATOM    451  CA  ILE A  55      33.555   2.474 -66.642  1.00 32.56           C  
ANISOU  451  CA  ILE A  55     4109   4189   4073     40    494   -844       C  
ATOM    452  C   ILE A  55      34.335   3.693 -66.172  1.00 32.63           C  
ANISOU  452  C   ILE A  55     4117   4176   4102     47    518   -827       C  
ATOM    453  O   ILE A  55      34.985   4.355 -66.972  1.00 34.76           O  
ANISOU  453  O   ILE A  55     4386   4457   4363     39    566   -839       O  
ATOM    454  CB  ILE A  55      32.041   2.745 -66.686  1.00 32.73           C  
ANISOU  454  CB  ILE A  55     4152   4256   4026     41    480   -794       C  
ATOM    455  CG1 ILE A  55      31.361   1.717 -67.587  1.00 31.42           C  
ANISOU  455  CG1 ILE A  55     3981   4134   3822     20    477   -824       C  
ATOM    456  CG2 ILE A  55      31.746   4.179 -67.125  1.00 32.33           C  
ANISOU  456  CG2 ILE A  55     4120   4239   3924     54    518   -744       C  
ATOM    457  CD1 ILE A  55      29.941   1.431 -67.189  1.00 30.59           C  
ANISOU  457  CD1 ILE A  55     3886   4063   3673     15    443   -794       C  
ATOM    458  N   ILE A  56      34.272   3.978 -64.868  1.00 33.27           N  
ANISOU  458  N   ILE A  56     4201   4229   4209     55    488   -803       N  
ATOM    459  CA  ILE A  56      35.046   5.062 -64.260  1.00 31.73           C  
ANISOU  459  CA  ILE A  56     4003   4014   4037     52    510   -798       C  
ATOM    460  C   ILE A  56      36.406   4.534 -63.802  1.00 31.82           C  
ANISOU  460  C   ILE A  56     3973   4004   4112     50    499   -849       C  
ATOM    461  O   ILE A  56      36.496   3.733 -62.883  1.00 31.63           O  
ANISOU  461  O   ILE A  56     3931   3963   4122     63    452   -854       O  
ATOM    462  CB  ILE A  56      34.282   5.731 -63.084  1.00 31.15           C  
ANISOU  462  CB  ILE A  56     3953   3930   3953     58    489   -749       C  
ATOM    463  CG1 ILE A  56      32.824   5.994 -63.478  1.00 30.62           C  
ANISOU  463  CG1 ILE A  56     3918   3891   3822     70    490   -697       C  
ATOM    464  CG2 ILE A  56      34.969   7.035 -62.665  1.00 30.78           C  
ANISOU  464  CG2 ILE A  56     3912   3865   3918     43    532   -747       C  
ATOM    465  CD1 ILE A  56      31.963   6.636 -62.397  1.00 30.16           C  
ANISOU  465  CD1 ILE A  56     3883   3824   3750     79    473   -647       C  
ATOM    466  N   PRO A  57      37.476   4.986 -64.446  1.00 32.73           N  
ANISOU  466  N   PRO A  57     4070   4124   4242     35    545   -885       N  
ATOM    467  CA  PRO A  57      38.792   4.414 -64.154  1.00 33.02           C  
ANISOU  467  CA  PRO A  57     4056   4153   4334     38    537   -936       C  
ATOM    468  C   PRO A  57      39.221   4.777 -62.763  1.00 32.88           C  
ANISOU  468  C   PRO A  57     4016   4130   4344     37    509   -932       C  
ATOM    469  O   PRO A  57      38.884   5.875 -62.283  1.00 33.17           O  
ANISOU  469  O   PRO A  57     4077   4165   4360     19    526   -906       O  
ATOM    470  CB  PRO A  57      39.704   5.112 -65.173  1.00 33.73           C  
ANISOU  470  CB  PRO A  57     4136   4256   4421     14    601   -971       C  
ATOM    471  CG  PRO A  57      39.064   6.457 -65.374  1.00 33.01           C  
ANISOU  471  CG  PRO A  57     4092   4165   4283     -2    644   -929       C  
ATOM    472  CD  PRO A  57      37.568   6.232 -65.236  1.00 33.61           C  
ANISOU  472  CD  PRO A  57     4205   4244   4318     17    611   -874       C  
ATOM    473  N   LYS A  58      39.988   3.905 -62.120  1.00 33.58           N  
ANISOU  473  N   LYS A  58     4060   4220   4478     58    473   -958       N  
ATOM    474  CA  LYS A  58      40.345   4.133 -60.721  1.00 36.36           C  
ANISOU  474  CA  LYS A  58     4385   4581   4848     61    438   -952       C  
ATOM    475  C   LYS A  58      41.146   5.393 -60.508  1.00 37.71           C  
ANISOU  475  C   LYS A  58     4537   4774   5017     21    479   -978       C  
ATOM    476  O   LYS A  58      41.118   5.979 -59.417  1.00 40.35           O  
ANISOU  476  O   LYS A  58     4866   5117   5347      5    464   -968       O  
ATOM    477  CB  LYS A  58      41.095   2.959 -60.110  1.00 37.89           C  
ANISOU  477  CB  LYS A  58     4528   4782   5085    100    394   -970       C  
ATOM    478  CG  LYS A  58      40.915   2.935 -58.599  1.00 39.21           C  
ANISOU  478  CG  LYS A  58     4684   4958   5255    113    342   -941       C  
ATOM    479  CD  LYS A  58      41.922   2.052 -57.885  1.00 40.82           C  
ANISOU  479  CD  LYS A  58     4825   5186   5497    156    306   -957       C  
ATOM    480  CE  LYS A  58      41.821   2.267 -56.385  1.00 41.15           C  
ANISOU  480  CE  LYS A  58     4851   5253   5530    160    260   -930       C  
ATOM    481  NZ  LYS A  58      42.472   1.154 -55.655  1.00 42.89           N  
ANISOU  481  NZ  LYS A  58     5023   5491   5779    220    215   -924       N  
ATOM    482  N   SER A  59      41.864   5.805 -61.540  1.00 36.44           N  
ANISOU  482  N   SER A  59     4366   4621   4857     -1    535  -1015       N  
ATOM    483  CA  SER A  59      42.647   7.025 -61.485  1.00 37.70           C  
ANISOU  483  CA  SER A  59     4512   4796   5014    -48    589  -1047       C  
ATOM    484  C   SER A  59      41.790   8.275 -61.250  1.00 37.60           C  
ANISOU  484  C   SER A  59     4561   4758   4965    -78    625  -1009       C  
ATOM    485  O   SER A  59      42.319   9.324 -60.865  1.00 37.81           O  
ANISOU  485  O   SER A  59     4584   4790   4991   -123    669  -1032       O  
ATOM    486  CB  SER A  59      43.462   7.184 -62.763  1.00 36.92           C  
ANISOU  486  CB  SER A  59     4401   4705   4920    -67    648  -1090       C  
ATOM    487  OG  SER A  59      42.614   7.085 -63.882  1.00 37.30           O  
ANISOU  487  OG  SER A  59     4502   4730   4938    -55    670  -1060       O  
ATOM    488  N   TYR A  60      40.479   8.177 -61.491  1.00 36.29           N  
ANISOU  488  N   TYR A  60     4450   4568   4769    -54    612   -952       N  
ATOM    489  CA  TYR A  60      39.597   9.286 -61.157  1.00 35.73           C  
ANISOU  489  CA  TYR A  60     4435   4474   4665    -69    643   -908       C  
ATOM    490  C   TYR A  60      39.508   9.526 -59.647  1.00 35.12           C  
ANISOU  490  C   TYR A  60     4346   4398   4597    -80    608   -903       C  
ATOM    491  O   TYR A  60      39.415  10.672 -59.212  1.00 33.77           O  
ANISOU  491  O   TYR A  60     4203   4212   4414   -113    654   -898       O  
ATOM    492  CB  TYR A  60      38.196   9.153 -61.770  1.00 34.99           C  
ANISOU  492  CB  TYR A  60     4394   4368   4530    -37    637   -848       C  
ATOM    493  CG  TYR A  60      37.273  10.251 -61.290  1.00 34.33           C  
ANISOU  493  CG  TYR A  60     4364   4262   4415    -41    666   -797       C  
ATOM    494  CD1 TYR A  60      37.328  11.521 -61.852  1.00 34.94           C  
ANISOU  494  CD1 TYR A  60     4484   4319   4470    -60    751   -785       C  
ATOM    495  CD2 TYR A  60      36.400  10.042 -60.221  1.00 35.08           C  
ANISOU  495  CD2 TYR A  60     4469   4354   4506    -26    614   -763       C  
ATOM    496  CE1 TYR A  60      36.514  12.537 -61.399  1.00 35.13           C  
ANISOU  496  CE1 TYR A  60     4560   4316   4470    -57    787   -738       C  
ATOM    497  CE2 TYR A  60      35.590  11.066 -59.737  1.00 33.43           C  
ANISOU  497  CE2 TYR A  60     4307   4123   4270    -28    645   -719       C  
ATOM    498  CZ  TYR A  60      35.654  12.307 -60.334  1.00 33.97           C  
ANISOU  498  CZ  TYR A  60     4418   4168   4319    -42    733   -707       C  
ATOM    499  OH  TYR A  60      34.847  13.320 -59.904  1.00 35.38           O  
ANISOU  499  OH  TYR A  60     4648   4318   4474    -37    773   -660       O  
ATOM    500  N   PHE A  61      39.552   8.452 -58.859  1.00 34.90           N  
ANISOU  500  N   PHE A  61     4280   4389   4591    -54    533   -904       N  
ATOM    501  CA  PHE A  61      39.436   8.567 -57.392  1.00 35.97           C  
ANISOU  501  CA  PHE A  61     4402   4535   4730    -61    492   -896       C  
ATOM    502  C   PHE A  61      40.774   8.501 -56.665  1.00 38.21           C  
ANISOU  502  C   PHE A  61     4614   4864   5041    -82    479   -952       C  
ATOM    503  O   PHE A  61      40.850   8.849 -55.504  1.00 41.96           O  
ANISOU  503  O   PHE A  61     5073   5359   5512   -102    459   -956       O  
ATOM    504  CB  PHE A  61      38.549   7.464 -56.823  1.00 34.43           C  
ANISOU  504  CB  PHE A  61     4213   4334   4535    -17    418   -855       C  
ATOM    505  CG  PHE A  61      37.212   7.347 -57.484  1.00 33.02           C  
ANISOU  505  CG  PHE A  61     4092   4128   4326      3    421   -805       C  
ATOM    506  CD1 PHE A  61      36.180   8.202 -57.144  1.00 31.39           C  
ANISOU  506  CD1 PHE A  61     3933   3904   4087     -5    439   -763       C  
ATOM    507  CD2 PHE A  61      36.972   6.346 -58.412  1.00 31.70           C  
ANISOU  507  CD2 PHE A  61     3926   3958   4160     30    407   -804       C  
ATOM    508  CE1 PHE A  61      34.936   8.083 -57.734  1.00 30.80           C  
ANISOU  508  CE1 PHE A  61     3901   3821   3979     17    438   -717       C  
ATOM    509  CE2 PHE A  61      35.722   6.218 -59.001  1.00 31.96           C  
ANISOU  509  CE2 PHE A  61     4001   3982   4157     43    408   -764       C  
ATOM    510  CZ  PHE A  61      34.700   7.090 -58.659  1.00 30.82           C  
ANISOU  510  CZ  PHE A  61     3899   3832   3977     39    421   -718       C  
ATOM    511  N   GLY A  62      41.808   7.982 -57.319  1.00 39.79           N  
ANISOU  511  N   GLY A  62     4765   5087   5264    -74    485   -994       N  
ATOM    512  CA  GLY A  62      43.132   7.874 -56.698  1.00 40.22           C  
ANISOU  512  CA  GLY A  62     4739   5200   5340    -88    471  -1048       C  
ATOM    513  C   GLY A  62      43.298   6.714 -55.724  1.00 42.10           C  
ANISOU  513  C   GLY A  62     4929   5473   5595    -37    390  -1033       C  
ATOM    514  O   GLY A  62      44.262   5.963 -55.816  1.00 44.43           O  
ANISOU  514  O   GLY A  62     5160   5805   5914     -7    370  -1061       O  
ATOM    515  N   THR A  63      42.378   6.577 -54.769  1.00 42.38           N  
ANISOU  515  N   THR A  63     4993   5495   5615    -23    346   -987       N  
ATOM    516  CA  THR A  63      42.491   5.530 -53.730  1.00 41.37           C  
ANISOU  516  CA  THR A  63     4825   5397   5497     26    272   -965       C  
ATOM    517  C   THR A  63      41.196   4.762 -53.570  1.00 40.68           C  
ANISOU  517  C   THR A  63     4795   5257   5404     66    233   -903       C  
ATOM    518  O   THR A  63      40.117   5.242 -53.932  1.00 38.97           O  
ANISOU  518  O   THR A  63     4644   4996   5167     48    255   -875       O  
ATOM    519  CB  THR A  63      42.814   6.120 -52.340  1.00 42.42           C  
ANISOU  519  CB  THR A  63     4918   5587   5610     -4    249   -977       C  
ATOM    520  OG1 THR A  63      41.814   7.081 -51.997  1.00 44.11           O  
ANISOU  520  OG1 THR A  63     5195   5765   5797    -47    273   -955       O  
ATOM    521  CG2 THR A  63      44.190   6.786 -52.311  1.00 41.21           C  
ANISOU  521  CG2 THR A  63     4692   5505   5459    -49    282  -1047       C  
ATOM    522  N   THR A  64      41.304   3.576 -52.990  1.00 40.73           N  
ANISOU  522  N   THR A  64     4776   5271   5426    123    178   -880       N  
ATOM    523  CA  THR A  64      40.141   2.767 -52.675  1.00 40.92           C  
ANISOU  523  CA  THR A  64     4852   5249   5446    157    141   -825       C  
ATOM    524  C   THR A  64      39.177   3.519 -51.751  1.00 40.66           C  
ANISOU  524  C   THR A  64     4855   5211   5379    125    128   -794       C  
ATOM    525  O   THR A  64      37.960   3.452 -51.938  1.00 40.64           O  
ANISOU  525  O   THR A  64     4914   5165   5363    123    128   -759       O  
ATOM    526  CB  THR A  64      40.564   1.421 -52.054  1.00 42.26           C  
ANISOU  526  CB  THR A  64     4988   5428   5640    224     92   -805       C  
ATOM    527  OG1 THR A  64      41.589   0.833 -52.865  1.00 43.17           O  
ANISOU  527  OG1 THR A  64     5061   5552   5787    255    111   -838       O  
ATOM    528  CG2 THR A  64      39.391   0.456 -51.973  1.00 42.24           C  
ANISOU  528  CG2 THR A  64     5045   5364   5638    255     69   -756       C  
ATOM    529  N   THR A  65      39.722   4.269 -50.790  1.00 40.89           N  
ANISOU  529  N   THR A  65     4846   5293   5395     95    122   -813       N  
ATOM    530  CA  THR A  65      38.886   4.989 -49.819  1.00 39.46           C  
ANISOU  530  CA  THR A  65     4698   5110   5183     62    113   -788       C  
ATOM    531  C   THR A  65      38.062   6.084 -50.483  1.00 38.58           C  
ANISOU  531  C   THR A  65     4648   4955   5054     19    170   -786       C  
ATOM    532  O   THR A  65      36.863   6.183 -50.219  1.00 36.49           O  
ANISOU  532  O   THR A  65     4436   4657   4770     20    162   -744       O  
ATOM    533  CB  THR A  65      39.692   5.553 -48.629  1.00 41.53           C  
ANISOU  533  CB  THR A  65     4902   5446   5430     33     97   -816       C  
ATOM    534  OG1 THR A  65      40.573   4.539 -48.125  1.00 42.98           O  
ANISOU  534  OG1 THR A  65     5020   5683   5627     84     47   -816       O  
ATOM    535  CG2 THR A  65      38.749   5.983 -47.499  1.00 40.28           C  
ANISOU  535  CG2 THR A  65     4778   5284   5242     11     77   -785       C  
ATOM    536  N   ASN A  66      38.694   6.891 -51.347  1.00 36.29           N  
ANISOU  536  N   ASN A  66     4352   4667   4769    -15    230   -827       N  
ATOM    537  CA  ASN A  66      37.944   7.829 -52.196  1.00 36.79           C  
ANISOU  537  CA  ASN A  66     4478   4685   4816    -41    292   -816       C  
ATOM    538  C   ASN A  66      36.876   7.112 -53.059  1.00 37.86           C  
ANISOU  538  C   ASN A  66     4660   4779   4946     -1    281   -772       C  
ATOM    539  O   ASN A  66      35.700   7.506 -53.092  1.00 36.45           O  
ANISOU  539  O   ASN A  66     4534   4573   4742     -2    291   -731       O  
ATOM    540  CB  ASN A  66      38.887   8.625 -53.103  1.00 37.62           C  
ANISOU  540  CB  ASN A  66     4569   4795   4928    -78    361   -865       C  
ATOM    541  CG  ASN A  66      39.776   9.592 -52.333  1.00 40.58           C  
ANISOU  541  CG  ASN A  66     4908   5209   5300   -137    391   -916       C  
ATOM    542  OD1 ASN A  66      39.537   9.881 -51.150  1.00 41.97           O  
ANISOU  542  OD1 ASN A  66     5081   5404   5462   -156    369   -911       O  
ATOM    543  ND2 ASN A  66      40.802  10.117 -53.010  1.00 38.47           N  
ANISOU  543  ND2 ASN A  66     4615   4957   5044   -172    446   -969       N  
ATOM    544  N   LEU A  67      37.276   6.043 -53.737  1.00 36.98           N  
ANISOU  544  N   LEU A  67     4525   4668   4856     31    261   -782       N  
ATOM    545  CA  LEU A  67      36.336   5.330 -54.589  1.00 37.03           C  
ANISOU  545  CA  LEU A  67     4571   4644   4855     58    256   -752       C  
ATOM    546  C   LEU A  67      35.113   4.854 -53.767  1.00 37.18           C  
ANISOU  546  C   LEU A  67     4621   4647   4856     74    210   -704       C  
ATOM    547  O   LEU A  67      33.963   5.000 -54.197  1.00 36.47           O  
ANISOU  547  O   LEU A  67     4576   4542   4739     74    220   -673       O  
ATOM    548  CB  LEU A  67      37.042   4.170 -55.294  1.00 34.91           C  
ANISOU  548  CB  LEU A  67     4272   4376   4617     89    245   -778       C  
ATOM    549  CG  LEU A  67      36.237   3.195 -56.140  1.00 33.54           C  
ANISOU  549  CG  LEU A  67     4128   4174   4438    111    239   -762       C  
ATOM    550  CD1 LEU A  67      37.170   2.566 -57.151  1.00 33.71           C  
ANISOU  550  CD1 LEU A  67     4121   4197   4488    123    260   -804       C  
ATOM    551  CD2 LEU A  67      35.593   2.117 -55.276  1.00 33.91           C  
ANISOU  551  CD2 LEU A  67     4187   4203   4492    139    186   -731       C  
ATOM    552  N   LYS A  68      35.374   4.307 -52.584  1.00 38.69           N  
ANISOU  552  N   LYS A  68     4787   4851   5060     89    161   -697       N  
ATOM    553  CA  LYS A  68      34.313   3.742 -51.749  1.00 42.34           C  
ANISOU  553  CA  LYS A  68     5277   5298   5509    104    118   -654       C  
ATOM    554  C   LYS A  68      33.352   4.812 -51.236  1.00 40.17           C  
ANISOU  554  C   LYS A  68     5039   5020   5200     76    132   -627       C  
ATOM    555  O   LYS A  68      32.164   4.555 -51.021  1.00 40.81           O  
ANISOU  555  O   LYS A  68     5156   5086   5261     82    114   -590       O  
ATOM    556  CB  LYS A  68      34.902   2.932 -50.593  1.00 47.01           C  
ANISOU  556  CB  LYS A  68     5834   5908   6120    132     67   -648       C  
ATOM    557  CG  LYS A  68      34.868   1.431 -50.828  1.00 51.17           C  
ANISOU  557  CG  LYS A  68     6364   6407   6671    177     41   -637       C  
ATOM    558  CD  LYS A  68      35.987   0.712 -50.090  1.00 57.71           C  
ANISOU  558  CD  LYS A  68     7140   7260   7525    218      9   -641       C  
ATOM    559  CE  LYS A  68      35.694  -0.779 -49.981  1.00 57.84           C  
ANISOU  559  CE  LYS A  68     7178   7235   7562    267    -12   -613       C  
ATOM    560  NZ  LYS A  68      34.760  -1.047 -48.846  1.00 61.47           N  
ANISOU  560  NZ  LYS A  68     7670   7684   8001    270    -48   -566       N  
ATOM    561  N   ARG A  69      33.862   6.022 -51.113  1.00 39.01           N  
ANISOU  561  N   ARG A  69     4885   4888   5048     43    170   -649       N  
ATOM    562  CA  ARG A  69      33.070   7.143 -50.672  1.00 37.81           C  
ANISOU  562  CA  ARG A  69     4769   4726   4868     17    198   -628       C  
ATOM    563  C   ARG A  69      32.057   7.560 -51.750  1.00 36.81           C  
ANISOU  563  C   ARG A  69     4690   4576   4717     24    238   -600       C  
ATOM    564  O   ARG A  69      30.862   7.679 -51.457  1.00 37.83           O  
ANISOU  564  O   ARG A  69     4854   4698   4821     32    230   -559       O  
ATOM    565  CB  ARG A  69      33.988   8.304 -50.237  1.00 40.26           C  
ANISOU  565  CB  ARG A  69     5061   5054   5181    -26    240   -668       C  
ATOM    566  CG  ARG A  69      33.271   9.434 -49.516  1.00 46.04           C  
ANISOU  566  CG  ARG A  69     5831   5772   5889    -56    271   -651       C  
ATOM    567  CD  ARG A  69      34.235  10.467 -48.947  1.00 48.61           C  
ANISOU  567  CD  ARG A  69     6135   6116   6218   -110    314   -701       C  
ATOM    568  NE  ARG A  69      34.655  10.130 -47.587  1.00 55.63           N  
ANISOU  568  NE  ARG A  69     6981   7050   7105   -124    261   -717       N  
ATOM    569  CZ  ARG A  69      35.884   9.734 -47.256  1.00 58.11           C  
ANISOU  569  CZ  ARG A  69     7228   7418   7432   -133    234   -759       C  
ATOM    570  NH1 ARG A  69      36.836   9.633 -48.188  1.00 57.90           N  
ANISOU  570  NH1 ARG A  69     7171   7402   7426   -132    258   -795       N  
ATOM    571  NH2 ARG A  69      36.169   9.450 -45.989  1.00 56.70           N  
ANISOU  571  NH2 ARG A  69     7010   7290   7242   -140    185   -766       N  
ATOM    572  N   PHE A  70      32.524   7.745 -52.992  1.00 34.29           N  
ANISOU  572  N   PHE A  70     4370   4255   4403     25    280   -619       N  
ATOM    573  CA  PHE A  70      31.643   8.050 -54.131  1.00 33.11           C  
ANISOU  573  CA  PHE A  70     4258   4098   4223     38    316   -590       C  
ATOM    574  C   PHE A  70      30.545   6.987 -54.288  1.00 32.56           C  
ANISOU  574  C   PHE A  70     4198   4035   4136     64    270   -560       C  
ATOM    575  O   PHE A  70      29.388   7.333 -54.444  1.00 34.87           O  
ANISOU  575  O   PHE A  70     4521   4333   4393     73    280   -521       O  
ATOM    576  CB  PHE A  70      32.471   8.210 -55.440  1.00 32.10           C  
ANISOU  576  CB  PHE A  70     4119   3972   4103     35    362   -621       C  
ATOM    577  CG  PHE A  70      31.643   8.485 -56.693  1.00 30.32           C  
ANISOU  577  CG  PHE A  70     3927   3752   3839     53    399   -590       C  
ATOM    578  CD1 PHE A  70      31.304   9.790 -57.059  1.00 31.56           C  
ANISOU  578  CD1 PHE A  70     4121   3899   3969     51    464   -563       C  
ATOM    579  CD2 PHE A  70      31.263   7.444 -57.544  1.00 30.45           C  
ANISOU  579  CD2 PHE A  70     3935   3787   3845     70    373   -590       C  
ATOM    580  CE1 PHE A  70      30.573  10.040 -58.226  1.00 29.74           C  
ANISOU  580  CE1 PHE A  70     3916   3685   3696     76    497   -528       C  
ATOM    581  CE2 PHE A  70      30.540   7.690 -58.710  1.00 27.24           C  
ANISOU  581  CE2 PHE A  70     3551   3404   3396     84    405   -565       C  
ATOM    582  CZ  PHE A  70      30.207   8.979 -59.048  1.00 28.80           C  
ANISOU  582  CZ  PHE A  70     3780   3600   3562     91    463   -531       C  
ATOM    583  N   TYR A  71      30.917   5.705 -54.199  1.00 31.20           N  
ANISOU  583  N   TYR A  71     4000   3863   3989     74    225   -579       N  
ATOM    584  CA  TYR A  71      30.000   4.594 -54.518  1.00 30.88           C  
ANISOU  584  CA  TYR A  71     3971   3824   3935     88    194   -564       C  
ATOM    585  C   TYR A  71      28.923   4.351 -53.457  1.00 31.22           C  
ANISOU  585  C   TYR A  71     4033   3865   3962     90    156   -528       C  
ATOM    586  O   TYR A  71      27.895   3.742 -53.743  1.00 30.12           O  
ANISOU  586  O   TYR A  71     3909   3734   3798     92    142   -512       O  
ATOM    587  CB  TYR A  71      30.774   3.298 -54.839  1.00 30.08           C  
ANISOU  587  CB  TYR A  71     3846   3712   3871    100    173   -598       C  
ATOM    588  CG  TYR A  71      31.322   3.279 -56.262  1.00 32.33           C  
ANISOU  588  CG  TYR A  71     4120   4005   4157     98    212   -629       C  
ATOM    589  CD1 TYR A  71      30.509   2.921 -57.337  1.00 32.05           C  
ANISOU  589  CD1 TYR A  71     4102   3985   4090     95    226   -627       C  
ATOM    590  CD2 TYR A  71      32.646   3.676 -56.541  1.00 31.87           C  
ANISOU  590  CD2 TYR A  71     4033   3947   4126     95    238   -664       C  
ATOM    591  CE1 TYR A  71      30.999   2.947 -58.646  1.00 33.06           C  
ANISOU  591  CE1 TYR A  71     4220   4126   4212     91    264   -655       C  
ATOM    592  CE2 TYR A  71      33.140   3.697 -57.847  1.00 31.98           C  
ANISOU  592  CE2 TYR A  71     4040   3969   4140     91    277   -693       C  
ATOM    593  CZ  TYR A  71      32.304   3.330 -58.893  1.00 32.43           C  
ANISOU  593  CZ  TYR A  71     4117   4039   4164     91    289   -687       C  
ATOM    594  OH  TYR A  71      32.771   3.318 -60.190  1.00 34.74           O  
ANISOU  594  OH  TYR A  71     4402   4345   4451     85    328   -716       O  
ATOM    595  N   LYS A  72      29.142   4.850 -52.244  1.00 32.01           N  
ANISOU  595  N   LYS A  72     4131   3960   4071     83    142   -520       N  
ATOM    596  CA  LYS A  72      28.051   4.888 -51.250  1.00 33.78           C  
ANISOU  596  CA  LYS A  72     4376   4183   4272     80    116   -484       C  
ATOM    597  C   LYS A  72      26.900   5.750 -51.769  1.00 31.47           C  
ANISOU  597  C   LYS A  72     4113   3906   3937     81    150   -452       C  
ATOM    598  O   LYS A  72      25.740   5.434 -51.535  1.00 30.59           O  
ANISOU  598  O   LYS A  72     4017   3805   3799     85    130   -424       O  
ATOM    599  CB  LYS A  72      28.530   5.418 -49.895  1.00 35.74           C  
ANISOU  599  CB  LYS A  72     4615   4430   4532     68    102   -484       C  
ATOM    600  CG  LYS A  72      29.406   4.459 -49.098  1.00 39.47           C  
ANISOU  600  CG  LYS A  72     5057   4903   5036     78     57   -500       C  
ATOM    601  CD  LYS A  72      28.602   3.564 -48.169  1.00 43.39           C  
ANISOU  601  CD  LYS A  72     5568   5391   5524     87     10   -469       C  
ATOM    602  CE  LYS A  72      28.528   2.124 -48.672  1.00 49.65           C  
ANISOU  602  CE  LYS A  72     6364   6164   6334    109     -9   -470       C  
ATOM    603  NZ  LYS A  72      27.398   1.886 -49.629  1.00 53.02           N  
ANISOU  603  NZ  LYS A  72     6820   6588   6738    101      8   -463       N  
ATOM    604  N   VAL A  73      27.228   6.834 -52.477  1.00 29.09           N  
ANISOU  604  N   VAL A  73     3818   3606   3627     81    204   -454       N  
ATOM    605  CA  VAL A  73      26.209   7.632 -53.126  1.00 29.51           C  
ANISOU  605  CA  VAL A  73     3897   3676   3636     95    242   -417       C  
ATOM    606  C   VAL A  73      25.465   6.807 -54.200  1.00 29.24           C  
ANISOU  606  C   VAL A  73     3858   3677   3572    108    229   -411       C  
ATOM    607  O   VAL A  73      24.234   6.681 -54.165  1.00 29.42           O  
ANISOU  607  O   VAL A  73     3890   3730   3558    117    217   -380       O  
ATOM    608  CB  VAL A  73      26.824   8.878 -53.755  1.00 29.79           C  
ANISOU  608  CB  VAL A  73     3947   3701   3672     95    311   -420       C  
ATOM    609  CG1 VAL A  73      25.777   9.614 -54.574  1.00 28.14           C  
ANISOU  609  CG1 VAL A  73     3764   3514   3413    124    353   -373       C  
ATOM    610  CG2 VAL A  73      27.449   9.756 -52.663  1.00 28.66           C  
ANISOU  610  CG2 VAL A  73     3810   3527   3552     71    332   -434       C  
ATOM    611  N   VAL A  74      26.235   6.219 -55.109  1.00 26.90           N  
ANISOU  611  N   VAL A  74     3544   3383   3293    105    233   -445       N  
ATOM    612  CA  VAL A  74      25.719   5.344 -56.157  1.00 28.24           C  
ANISOU  612  CA  VAL A  74     3706   3586   3437    106    225   -454       C  
ATOM    613  C   VAL A  74      24.806   4.282 -55.574  1.00 29.06           C  
ANISOU  613  C   VAL A  74     3810   3698   3533     96    178   -450       C  
ATOM    614  O   VAL A  74      23.773   3.932 -56.157  1.00 30.75           O  
ANISOU  614  O   VAL A  74     4023   3957   3703     93    175   -441       O  
ATOM    615  CB  VAL A  74      26.886   4.655 -56.929  1.00 27.70           C  
ANISOU  615  CB  VAL A  74     3617   3504   3403     98    231   -503       C  
ATOM    616  CG1 VAL A  74      26.374   3.575 -57.871  1.00 27.96           C  
ANISOU  616  CG1 VAL A  74     3642   3566   3413     90    222   -523       C  
ATOM    617  CG2 VAL A  74      27.695   5.681 -57.700  1.00 27.19           C  
ANISOU  617  CG2 VAL A  74     3552   3438   3338    103    284   -510       C  
ATOM    618  N   GLU A  75      25.198   3.773 -54.421  1.00 28.90           N  
ANISOU  618  N   GLU A  75     3789   3639   3551     89    144   -458       N  
ATOM    619  CA  GLU A  75      24.459   2.765 -53.746  1.00 31.02           C  
ANISOU  619  CA  GLU A  75     4063   3902   3818     79    106   -454       C  
ATOM    620  C   GLU A  75      23.117   3.296 -53.196  1.00 30.26           C  
ANISOU  620  C   GLU A  75     3982   3836   3679     79     99   -413       C  
ATOM    621  O   GLU A  75      22.125   2.569 -53.168  1.00 29.76           O  
ANISOU  621  O   GLU A  75     3922   3795   3591     65     81   -409       O  
ATOM    622  CB  GLU A  75      25.334   2.163 -52.645  1.00 35.11           C  
ANISOU  622  CB  GLU A  75     4578   4373   4386     81     75   -465       C  
ATOM    623  CG  GLU A  75      24.647   1.121 -51.779  1.00 44.32           C  
ANISOU  623  CG  GLU A  75     5759   5523   5555     73     39   -455       C  
ATOM    624  CD  GLU A  75      25.523  -0.102 -51.520  1.00 54.06           C  
ANISOU  624  CD  GLU A  75     6990   6714   6836     82     22   -477       C  
ATOM    625  OE1 GLU A  75      26.767   0.074 -51.370  1.00 58.51           O  
ANISOU  625  OE1 GLU A  75     7532   7264   7434    100     22   -491       O  
ATOM    626  OE2 GLU A  75      24.964  -1.240 -51.470  1.00 54.63           O  
ANISOU  626  OE2 GLU A  75     7079   6767   6909     71     13   -482       O  
ATOM    627  N   LYS A  76      23.074   4.557 -52.768  1.00 28.57           N  
ANISOU  627  N   LYS A  76     3777   3622   3456     91    120   -384       N  
ATOM    628  CA  LYS A  76      21.791   5.152 -52.349  1.00 28.92           C  
ANISOU  628  CA  LYS A  76     3833   3696   3457     98    122   -343       C  
ATOM    629  C   LYS A  76      20.879   5.277 -53.539  1.00 29.47           C  
ANISOU  629  C   LYS A  76     3895   3829   3473    111    142   -328       C  
ATOM    630  O   LYS A  76      19.686   4.969 -53.465  1.00 27.86           O  
ANISOU  630  O   LYS A  76     3686   3670   3230    107    127   -311       O  
ATOM    631  CB  LYS A  76      21.991   6.526 -51.737  1.00 29.80           C  
ANISOU  631  CB  LYS A  76     3960   3788   3573    111    153   -319       C  
ATOM    632  CG  LYS A  76      22.530   6.469 -50.323  1.00 32.05           C  
ANISOU  632  CG  LYS A  76     4250   4034   3894     94    128   -328       C  
ATOM    633  CD  LYS A  76      22.423   7.817 -49.632  1.00 35.04           C  
ANISOU  633  CD  LYS A  76     4647   4398   4266     97    163   -306       C  
ATOM    634  CE  LYS A  76      22.528   7.639 -48.109  1.00 35.25           C  
ANISOU  634  CE  LYS A  76     4677   4405   4311     76    129   -311       C  
ATOM    635  NZ  LYS A  76      22.341   8.914 -47.359  1.00 34.47           N  
ANISOU  635  NZ  LYS A  76     4599   4292   4205     71    167   -296       N  
ATOM    636  N   ILE A  77      21.466   5.708 -54.658  1.00 29.60           N  
ANISOU  636  N   ILE A  77     3905   3856   3483    124    178   -336       N  
ATOM    637  CA  ILE A  77      20.718   5.929 -55.854  1.00 28.29           C  
ANISOU  637  CA  ILE A  77     3728   3759   3259    141    200   -318       C  
ATOM    638  C   ILE A  77      20.148   4.598 -56.268  1.00 29.46           C  
ANISOU  638  C   ILE A  77     3856   3948   3387    112    168   -349       C  
ATOM    639  O   ILE A  77      18.990   4.517 -56.732  1.00 32.27           O  
ANISOU  639  O   ILE A  77     4196   4380   3683    114    166   -333       O  
ATOM    640  CB  ILE A  77      21.625   6.541 -56.962  1.00 27.90           C  
ANISOU  640  CB  ILE A  77     3679   3708   3212    157    246   -325       C  
ATOM    641  CG1 ILE A  77      21.971   7.999 -56.599  1.00 26.90           C  
ANISOU  641  CG1 ILE A  77     3580   3545   3095    183    293   -290       C  
ATOM    642  CG2 ILE A  77      20.969   6.426 -58.332  1.00 25.24           C  
ANISOU  642  CG2 ILE A  77     3323   3453   2811    169    260   -316       C  
ATOM    643  CD1 ILE A  77      22.855   8.709 -57.606  1.00 27.12           C  
ANISOU  643  CD1 ILE A  77     3616   3563   3126    196    347   -294       C  
ATOM    644  N   LEU A  78      20.931   3.538 -56.071  1.00 27.42           N  
ANISOU  644  N   LEU A  78     3598   3641   3179     84    146   -395       N  
ATOM    645  CA  LEU A  78      20.466   2.194 -56.448  1.00 28.79           C  
ANISOU  645  CA  LEU A  78     3761   3837   3340     48    127   -433       C  
ATOM    646  C   LEU A  78      19.334   1.686 -55.550  1.00 29.57           C  
ANISOU  646  C   LEU A  78     3864   3949   3420     28     98   -421       C  
ATOM    647  O   LEU A  78      18.688   0.683 -55.877  1.00 30.01           O  
ANISOU  647  O   LEU A  78     3912   4035   3453     -7     90   -451       O  
ATOM    648  CB  LEU A  78      21.619   1.190 -56.473  1.00 26.75           C  
ANISOU  648  CB  LEU A  78     3507   3513   3142     32    122   -481       C  
ATOM    649  CG  LEU A  78      22.578   1.306 -57.653  1.00 26.58           C  
ANISOU  649  CG  LEU A  78     3474   3495   3130     38    152   -509       C  
ATOM    650  CD1 LEU A  78      23.789   0.395 -57.429  1.00 25.80           C  
ANISOU  650  CD1 LEU A  78     3378   3324   3098     32    146   -549       C  
ATOM    651  CD2 LEU A  78      21.837   0.917 -58.923  1.00 26.63           C  
ANISOU  651  CD2 LEU A  78     3463   3578   3077     17    167   -530       C  
ATOM    652  N   THR A  79      19.088   2.388 -54.441  1.00 28.69           N  
ANISOU  652  N   THR A  79     3766   3816   3317     46     87   -382       N  
ATOM    653  CA  THR A  79      18.131   1.934 -53.422  1.00 30.15           C  
ANISOU  653  CA  THR A  79     3959   4004   3492     26     60   -371       C  
ATOM    654  C   THR A  79      17.166   3.064 -52.992  1.00 30.49           C  
ANISOU  654  C   THR A  79     4000   4091   3493     52     66   -320       C  
ATOM    655  O   THR A  79      16.472   2.953 -51.969  1.00 28.15           O  
ANISOU  655  O   THR A  79     3712   3791   3193     42     47   -304       O  
ATOM    656  CB  THR A  79      18.874   1.432 -52.169  1.00 31.69           C  
ANISOU  656  CB  THR A  79     4176   4115   3747     19     35   -377       C  
ATOM    657  OG1 THR A  79      19.711   2.486 -51.663  1.00 33.04           O  
ANISOU  657  OG1 THR A  79     4354   4252   3946     47     44   -356       O  
ATOM    658  CG2 THR A  79      19.738   0.188 -52.491  1.00 29.60           C  
ANISOU  658  CG2 THR A  79     3917   3804   3526      1     31   -422       C  
ATOM    659  N   GLN A  80      17.099   4.121 -53.807  1.00 30.84           N  
ANISOU  659  N   GLN A  80     4034   4178   3504     89     99   -293       N  
ATOM    660  CA  GLN A  80      16.417   5.360 -53.438  1.00 31.10           C  
ANISOU  660  CA  GLN A  80     4072   4236   3507    128    120   -239       C  
ATOM    661  C   GLN A  80      14.944   5.174 -53.126  1.00 31.80           C  
ANISOU  661  C   GLN A  80     4143   4394   3543    123    103   -219       C  
ATOM    662  O   GLN A  80      14.326   4.199 -53.575  1.00 32.43           O  
ANISOU  662  O   GLN A  80     4199   4529   3593     90     84   -247       O  
ATOM    663  CB  GLN A  80      16.560   6.380 -54.544  1.00 30.58           C  
ANISOU  663  CB  GLN A  80     4001   4206   3410    172    165   -210       C  
ATOM    664  CG  GLN A  80      16.103   5.863 -55.902  1.00 33.44           C  
ANISOU  664  CG  GLN A  80     4330   4658   3717    168    166   -224       C  
ATOM    665  CD  GLN A  80      16.383   6.849 -57.013  1.00 34.38           C  
ANISOU  665  CD  GLN A  80     4447   4809   3805    215    212   -193       C  
ATOM    666  OE1 GLN A  80      15.701   7.864 -57.133  1.00 33.45           O  
ANISOU  666  OE1 GLN A  80     4330   4734   3645    267    242   -135       O  
ATOM    667  NE2 GLN A  80      17.413   6.562 -57.827  1.00 35.10           N  
ANISOU  667  NE2 GLN A  80     4540   4878   3919    202    224   -228       N  
ATOM    668  N   SER A  81      14.394   6.109 -52.349  1.00 29.73           N  
ANISOU  668  N   SER A  81     3892   4131   3272    153    115   -174       N  
ATOM    669  CA  SER A  81      12.941   6.286 -52.248  1.00 31.74           C  
ANISOU  669  CA  SER A  81     4123   4468   3465    167    112   -143       C  
ATOM    670  C   SER A  81      12.545   7.462 -53.146  1.00 33.53           C  
ANISOU  670  C   SER A  81     4338   4759   3643    233    157    -91       C  
ATOM    671  O   SER A  81      13.412   8.237 -53.550  1.00 36.86           O  
ANISOU  671  O   SER A  81     4782   5136   4087    263    193    -77       O  
ATOM    672  CB  SER A  81      12.553   6.605 -50.803  1.00 30.25           C  
ANISOU  672  CB  SER A  81     3956   4238   3297    164    103   -123       C  
ATOM    673  OG  SER A  81      12.558   5.460 -49.991  1.00 28.83           O  
ANISOU  673  OG  SER A  81     3782   4025   3144    109     62   -160       O  
ATOM    674  N   SER A  82      11.258   7.629 -53.444  1.00 32.69           N  
ANISOU  674  N   SER A  82     4196   4757   3467    259    158    -60       N  
ATOM    675  CA  SER A  82      10.819   8.845 -54.131  1.00 33.22           C  
ANISOU  675  CA  SER A  82     4254   4880   3484    338    204      4       C  
ATOM    676  C   SER A  82      11.169  10.024 -53.266  1.00 32.89           C  
ANISOU  676  C   SER A  82     4262   4749   3486    376    246     43       C  
ATOM    677  O   SER A  82      10.998   9.965 -52.058  1.00 34.66           O  
ANISOU  677  O   SER A  82     4504   4924   3741    352    231     36       O  
ATOM    678  CB  SER A  82       9.315   8.835 -54.356  1.00 34.56           C  
ANISOU  678  CB  SER A  82     4373   5183   3573    363    195     34       C  
ATOM    679  OG  SER A  82       8.958   7.894 -55.343  1.00 37.51           O  
ANISOU  679  OG  SER A  82     4697   5660   3895    329    168     -2       O  
ATOM    680  N   PHE A  83      11.677  11.088 -53.877  1.00 33.21           N  
ANISOU  680  N   PHE A  83     4327   4764   3526    431    303     82       N  
ATOM    681  CA  PHE A  83      11.910  12.369 -53.187  1.00 33.26           C  
ANISOU  681  CA  PHE A  83     4383   4689   3564    472    361    122       C  
ATOM    682  C   PHE A  83      13.192  12.421 -52.354  1.00 31.86           C  
ANISOU  682  C   PHE A  83     4250   4387   3467    421    365     77       C  
ATOM    683  O   PHE A  83      13.512  13.450 -51.786  1.00 31.40           O  
ANISOU  683  O   PHE A  83     4235   4258   3438    440    418     97       O  
ATOM    684  CB  PHE A  83      10.710  12.745 -52.288  1.00 37.45           C  
ANISOU  684  CB  PHE A  83     4908   5249   4070    499    364    159       C  
ATOM    685  CG  PHE A  83       9.455  13.113 -53.043  1.00 40.11           C  
ANISOU  685  CG  PHE A  83     5203   5709   4324    572    380    221       C  
ATOM    686  CD1 PHE A  83       9.394  14.278 -53.807  1.00 42.40           C  
ANISOU  686  CD1 PHE A  83     5511   6012   4585    660    451    289       C  
ATOM    687  CD2 PHE A  83       8.310  12.320 -52.945  1.00 41.95           C  
ANISOU  687  CD2 PHE A  83     5380   6050   4506    555    329    213       C  
ATOM    688  CE1 PHE A  83       8.225  14.628 -54.487  1.00 43.16           C  
ANISOU  688  CE1 PHE A  83     5563   6234   4598    738    465    353       C  
ATOM    689  CE2 PHE A  83       7.139  12.663 -53.624  1.00 42.91           C  
ANISOU  689  CE2 PHE A  83     5454   6304   4546    624    342    268       C  
ATOM    690  CZ  PHE A  83       7.099  13.816 -54.399  1.00 43.01           C  
ANISOU  690  CZ  PHE A  83     5478   6336   4525    720    408    342       C  
ATOM    691  N   GLU A  84      13.891  11.301 -52.233  1.00 30.06           N  
ANISOU  691  N   GLU A  84     4010   4137   3273    357    312     16       N  
ATOM    692  CA  GLU A  84      15.081  11.257 -51.411  1.00 30.79           C  
ANISOU  692  CA  GLU A  84     4133   4131   3435    312    307    -25       C  
ATOM    693  C   GLU A  84      16.197  12.083 -52.034  1.00 32.00           C  
ANISOU  693  C   GLU A  84     4313   4231   3613    326    364    -26       C  
ATOM    694  O   GLU A  84      16.376  12.092 -53.268  1.00 32.69           O  
ANISOU  694  O   GLU A  84     4388   4355   3675    349    382    -18       O  
ATOM    695  CB  GLU A  84      15.559   9.804 -51.208  1.00 31.61           C  
ANISOU  695  CB  GLU A  84     4214   4228   3565    251    240    -83       C  
ATOM    696  CG  GLU A  84      16.778   9.657 -50.312  1.00 29.07           C  
ANISOU  696  CG  GLU A  84     3914   3822   3309    210    228   -123       C  
ATOM    697  CD  GLU A  84      17.101   8.209 -50.011  1.00 30.43           C  
ANISOU  697  CD  GLU A  84     4069   3988   3505    165    165   -167       C  
ATOM    698  OE1 GLU A  84      16.616   7.316 -50.745  1.00 32.21           O  
ANISOU  698  OE1 GLU A  84     4270   4263   3703    157    141   -179       O  
ATOM    699  OE2 GLU A  84      17.847   7.958 -49.043  1.00 30.76           O  
ANISOU  699  OE2 GLU A  84     4121   3976   3590    136    144   -192       O  
ATOM    700  N   CYS A  85      16.939  12.769 -51.167  1.00 31.01           N  
ANISOU  700  N   CYS A  85     4222   4024   3534    308    395    -40       N  
ATOM    701  CA  CYS A  85      18.125  13.502 -51.543  1.00 29.95           C  
ANISOU  701  CA  CYS A  85     4115   3831   3432    303    450    -56       C  
ATOM    702  C   CYS A  85      19.253  13.068 -50.646  1.00 30.18           C  
ANISOU  702  C   CYS A  85     4143   3805   3517    241    419   -116       C  
ATOM    703  O   CYS A  85      19.028  12.383 -49.660  1.00 31.34           O  
ANISOU  703  O   CYS A  85     4277   3953   3675    211    365   -134       O  
ATOM    704  CB  CYS A  85      17.891  14.985 -51.340  1.00 29.57           C  
ANISOU  704  CB  CYS A  85     4113   3740   3379    341    538    -13       C  
ATOM    705  SG  CYS A  85      16.499  15.623 -52.297  1.00 30.08           S  
ANISOU  705  SG  CYS A  85     4179   3877   3373    434    581     73       S  
ATOM    706  N   ILE A  86      20.474  13.454 -51.008  1.00 31.33           N  
ANISOU  706  N   ILE A  86     4299   3908   3694    222    455   -147       N  
ATOM    707  CA  ILE A  86      21.580  13.587 -50.061  1.00 30.30           C  
ANISOU  707  CA  ILE A  86     4174   3726   3612    170    455   -197       C  
ATOM    708  C   ILE A  86      22.019  15.046 -50.121  1.00 31.64           C  
ANISOU  708  C   ILE A  86     4388   3842   3792    172    552   -192       C  
ATOM    709  O   ILE A  86      21.540  15.787 -50.978  1.00 32.64           O  
ANISOU  709  O   ILE A  86     4541   3969   3892    220    614   -146       O  
ATOM    710  CB  ILE A  86      22.767  12.709 -50.449  1.00 29.41           C  
ANISOU  710  CB  ILE A  86     4030   3614   3530    139    416   -249       C  
ATOM    711  CG1 ILE A  86      23.055  12.839 -51.940  1.00 29.85           C  
ANISOU  711  CG1 ILE A  86     4085   3684   3573    164    452   -242       C  
ATOM    712  CG2 ILE A  86      22.477  11.258 -50.139  1.00 31.41           C  
ANISOU  712  CG2 ILE A  86     4249   3901   3784    128    329   -262       C  
ATOM    713  CD1 ILE A  86      24.517  13.066 -52.262  1.00 28.47           C  
ANISOU  713  CD1 ILE A  86     3906   3476   3434    133    481   -290       C  
ATOM    714  N   HIS A  87      22.934  15.447 -49.231  1.00 32.49           N  
ANISOU  714  N   HIS A  87     4502   3906   3934    120    571   -239       N  
ATOM    715  CA  HIS A  87      23.628  16.747 -49.335  1.00 33.36           C  
ANISOU  715  CA  HIS A  87     4653   3959   4061    102    670   -254       C  
ATOM    716  C   HIS A  87      24.676  16.813 -50.427  1.00 34.69           C  
ANISOU  716  C   HIS A  87     4816   4119   4243     94    702   -280       C  
ATOM    717  O   HIS A  87      25.515  15.913 -50.552  1.00 33.76           O  
ANISOU  717  O   HIS A  87     4654   4025   4144     66    644   -324       O  
ATOM    718  CB  HIS A  87      24.285  17.117 -48.001  1.00 34.49           C  
ANISOU  718  CB  HIS A  87     4799   4073   4232     36    679   -308       C  
ATOM    719  CG  HIS A  87      23.296  17.475 -46.917  1.00 34.95           C  
ANISOU  719  CG  HIS A  87     4880   4123   4277     40    683   -284       C  
ATOM    720  ND1 HIS A  87      22.708  16.540 -46.128  1.00 34.87           N  
ANISOU  720  ND1 HIS A  87     4839   4152   4257     38    596   -278       N  
ATOM    721  CD2 HIS A  87      22.771  18.706 -46.530  1.00 33.42           C  
ANISOU  721  CD2 HIS A  87     4739   3879   4077     48    772   -262       C  
ATOM    722  CE1 HIS A  87      21.853  17.150 -45.286  1.00 34.93           C  
ANISOU  722  CE1 HIS A  87     4876   4143   4252     43    625   -255       C  
ATOM    723  NE2 HIS A  87      21.900  18.476 -45.524  1.00 34.24           N  
ANISOU  723  NE2 HIS A  87     4840   4001   4169     49    733   -247       N  
ATOM    724  N   LEU A  88      24.678  17.926 -51.168  1.00 34.37           N  
ANISOU  724  N   LEU A  88     4823   4040   4194    118    801   -253       N  
ATOM    725  CA  LEU A  88      25.682  18.210 -52.168  1.00 33.60           C  
ANISOU  725  CA  LEU A  88     4731   3925   4109    106    850   -276       C  
ATOM    726  C   LEU A  88      27.111  18.133 -51.592  1.00 35.67           C  
ANISOU  726  C   LEU A  88     4967   4171   4413     26    846   -362       C  
ATOM    727  O   LEU A  88      28.058  17.757 -52.302  1.00 35.80           O  
ANISOU  727  O   LEU A  88     4956   4200   4443      8    838   -397       O  
ATOM    728  CB  LEU A  88      25.427  19.585 -52.812  1.00 32.00           C  
ANISOU  728  CB  LEU A  88     4597   3668   3891    142    973   -230       C  
ATOM    729  CG  LEU A  88      24.422  19.684 -53.984  1.00 33.52           C  
ANISOU  729  CG  LEU A  88     4806   3893   4036    230    992   -146       C  
ATOM    730  CD1 LEU A  88      24.080  21.141 -54.277  1.00 33.26           C  
ANISOU  730  CD1 LEU A  88     4849   3797   3991    272   1121    -92       C  
ATOM    731  CD2 LEU A  88      24.942  19.012 -55.271  1.00 32.54           C  
ANISOU  731  CD2 LEU A  88     4650   3812   3900    240    964   -153       C  
ATOM    732  N   SER A  89      27.268  18.482 -50.316  1.00 34.75           N  
ANISOU  732  N   SER A  89     4855   4036   4313    -21    851   -396       N  
ATOM    733  CA  SER A  89      28.586  18.441 -49.665  1.00 34.91           C  
ANISOU  733  CA  SER A  89     4841   4059   4363    -99    844   -479       C  
ATOM    734  C   SER A  89      29.139  17.024 -49.444  1.00 34.39           C  
ANISOU  734  C   SER A  89     4702   4056   4309   -109    730   -511       C  
ATOM    735  O   SER A  89      30.340  16.858 -49.229  1.00 35.03           O  
ANISOU  735  O   SER A  89     4742   4154   4411   -159    720   -574       O  
ATOM    736  CB  SER A  89      28.555  19.192 -48.338  1.00 35.20           C  
ANISOU  736  CB  SER A  89     4898   4069   4405   -151    881   -509       C  
ATOM    737  OG  SER A  89      27.792  18.479 -47.372  1.00 35.76           O  
ANISOU  737  OG  SER A  89     4946   4175   4465   -138    796   -489       O  
ATOM    738  N   VAL A  90      28.275  16.008 -49.489  1.00 35.21           N  
ANISOU  738  N   VAL A  90     4787   4193   4397    -61    648   -468       N  
ATOM    739  CA  VAL A  90      28.738  14.597 -49.412  1.00 36.30           C  
ANISOU  739  CA  VAL A  90     4865   4379   4547    -61    550   -490       C  
ATOM    740  C   VAL A  90      29.693  14.290 -50.553  1.00 37.05           C  
ANISOU  740  C   VAL A  90     4936   4482   4657    -60    560   -518       C  
ATOM    741  O   VAL A  90      30.465  13.301 -50.514  1.00 40.20           O  
ANISOU  741  O   VAL A  90     5284   4913   5075    -68    499   -552       O  
ATOM    742  CB  VAL A  90      27.564  13.578 -49.480  1.00 38.02           C  
ANISOU  742  CB  VAL A  90     5077   4624   4744    -12    478   -440       C  
ATOM    743  CG1 VAL A  90      28.094  12.160 -49.401  1.00 36.97           C  
ANISOU  743  CG1 VAL A  90     4893   4524   4628    -12    393   -464       C  
ATOM    744  CG2 VAL A  90      26.554  13.815 -48.354  1.00 37.89           C  
ANISOU  744  CG2 VAL A  90     5081   4602   4711    -11    465   -411       C  
ATOM    745  N   LEU A  91      29.633  15.119 -51.587  1.00 34.78           N  
ANISOU  745  N   LEU A  91     4687   4166   4359    -46    639   -500       N  
ATOM    746  CA  LEU A  91      30.339  14.821 -52.815  1.00 34.62           C  
ANISOU  746  CA  LEU A  91     4651   4156   4347    -38    651   -516       C  
ATOM    747  C   LEU A  91      31.731  15.442 -52.812  1.00 37.82           C  
ANISOU  747  C   LEU A  91     5044   4546   4779    -95    706   -581       C  
ATOM    748  O   LEU A  91      32.504  15.259 -53.757  1.00 39.54           O  
ANISOU  748  O   LEU A  91     5244   4771   5006    -98    723   -606       O  
ATOM    749  CB  LEU A  91      29.507  15.261 -54.029  1.00 33.72           C  
ANISOU  749  CB  LEU A  91     4579   4031   4199     12    701   -457       C  
ATOM    750  CG  LEU A  91      28.140  14.557 -54.277  1.00 32.80           C  
ANISOU  750  CG  LEU A  91     4462   3950   4047     68    646   -397       C  
ATOM    751  CD1 LEU A  91      27.418  15.112 -55.492  1.00 29.70           C  
ANISOU  751  CD1 LEU A  91     4105   3564   3614    120    701   -340       C  
ATOM    752  CD2 LEU A  91      28.294  13.038 -54.423  1.00 31.83           C  
ANISOU  752  CD2 LEU A  91     4289   3871   3934     70    553   -420       C  
ATOM    753  N   HIS A  92      32.063  16.155 -51.735  1.00 39.46           N  
ANISOU  753  N   HIS A  92     5257   4738   4996   -145    736   -615       N  
ATOM    754  CA  HIS A  92      33.412  16.693 -51.581  1.00 41.01           C  
ANISOU  754  CA  HIS A  92     5431   4934   5214   -212    785   -689       C  
ATOM    755  C   HIS A  92      34.011  16.583 -50.205  1.00 42.80           C  
ANISOU  755  C   HIS A  92     5613   5197   5452   -267    747   -743       C  
ATOM    756  O   HIS A  92      35.236  16.531 -50.069  1.00 44.57           O  
ANISOU  756  O   HIS A  92     5787   5455   5691   -315    748   -810       O  
ATOM    757  CB  HIS A  92      33.512  18.119 -52.124  1.00 40.45           C  
ANISOU  757  CB  HIS A  92     5425   4801   5140   -236    913   -690       C  
ATOM    758  CG  HIS A  92      32.710  19.130 -51.357  1.00 39.45           C  
ANISOU  758  CG  HIS A  92     5359   4627   5003   -246    974   -666       C  
ATOM    759  ND1 HIS A  92      33.172  19.722 -50.238  1.00 40.69           N  
ANISOU  759  ND1 HIS A  92     5512   4778   5169   -316   1004   -722       N  
ATOM    760  CD2 HIS A  92      31.456  19.687 -51.605  1.00 39.36           C  
ANISOU  760  CD2 HIS A  92     5413   4572   4969   -190   1017   -590       C  
ATOM    761  CE1 HIS A  92      32.258  20.602 -49.785  1.00 38.07           C  
ANISOU  761  CE1 HIS A  92     5245   4392   4825   -308   1066   -686       C  
ATOM    762  NE2 HIS A  92      31.210  20.582 -50.620  1.00 38.05           N  
ANISOU  762  NE2 HIS A  92     5284   4366   4804   -226   1074   -602       N  
ATOM    763  N   LYS A  93      33.173  16.518 -49.174  1.00 44.09           N  
ANISOU  763  N   LYS A  93     5787   5361   5601   -260    711   -717       N  
ATOM    764  CA  LYS A  93      33.676  16.434 -47.794  1.00 47.52           C  
ANISOU  764  CA  LYS A  93     6180   5839   6038   -311    674   -765       C  
ATOM    765  C   LYS A  93      34.448  15.139 -47.542  1.00 47.99           C  
ANISOU  765  C   LYS A  93     6158   5969   6107   -300    574   -788       C  
ATOM    766  O   LYS A  93      33.990  14.055 -47.907  1.00 46.51           O  
ANISOU  766  O   LYS A  93     5958   5790   5921   -240    505   -745       O  
ATOM    767  CB  LYS A  93      32.528  16.536 -46.780  1.00 49.67           C  
ANISOU  767  CB  LYS A  93     6482   6099   6291   -299    651   -725       C  
ATOM    768  CG  LYS A  93      32.173  17.942 -46.319  1.00 53.77           C  
ANISOU  768  CG  LYS A  93     7062   6565   6802   -342    752   -735       C  
ATOM    769  CD  LYS A  93      30.967  17.897 -45.383  1.00 54.51           C  
ANISOU  769  CD  LYS A  93     7182   6652   6878   -321    721   -690       C  
ATOM    770  CE  LYS A  93      31.008  18.991 -44.324  1.00 56.97           C  
ANISOU  770  CE  LYS A  93     7521   6941   7183   -389    791   -732       C  
ATOM    771  NZ  LYS A  93      30.707  20.340 -44.877  1.00 57.66           N  
ANISOU  771  NZ  LYS A  93     7688   6945   7274   -397    923   -723       N  
ATOM    772  N   CYS A  94      35.618  15.268 -46.912  1.00 50.36           N  
ANISOU  772  N   CYS A  94     6401   6320   6411   -358    572   -858       N  
ATOM    773  CA  CYS A  94      36.391  14.123 -46.382  1.00 50.26           C  
ANISOU  773  CA  CYS A  94     6306   6387   6403   -345    479   -879       C  
ATOM    774  C   CYS A  94      37.082  13.239 -47.435  1.00 52.01           C  
ANISOU  774  C   CYS A  94     6487   6625   6646   -304    450   -882       C  
ATOM    775  O   CYS A  94      37.557  12.145 -47.109  1.00 55.07           O  
ANISOU  775  O   CYS A  94     6815   7067   7040   -272    372   -883       O  
ATOM    776  CB  CYS A  94      35.525  13.247 -45.462  1.00 53.71           C  
ANISOU  776  CB  CYS A  94     6740   6840   6826   -302    392   -827       C  
ATOM    777  SG  CYS A  94      34.815  14.095 -44.040  1.00 55.92           S  
ANISOU  777  SG  CYS A  94     7050   7117   7077   -350    411   -829       S  
ATOM    778  N   TYR A  95      37.132  13.693 -48.686  1.00 49.51           N  
ANISOU  778  N   TYR A  95     6207   6263   6341   -301    515   -882       N  
ATOM    779  CA  TYR A  95      37.925  13.004 -49.703  1.00 50.41           C  
ANISOU  779  CA  TYR A  95     6281   6395   6475   -276    502   -899       C  
ATOM    780  C   TYR A  95      39.416  13.229 -49.457  1.00 51.62           C  
ANISOU  780  C   TYR A  95     6362   6610   6637   -330    518   -978       C  
ATOM    781  O   TYR A  95      39.824  14.310 -49.038  1.00 51.78           O  
ANISOU  781  O   TYR A  95     6387   6636   6649   -402    582  -1027       O  
ATOM    782  CB  TYR A  95      37.560  13.492 -51.104  1.00 47.67           C  
ANISOU  782  CB  TYR A  95     5992   5988   6131   -261    572   -876       C  
ATOM    783  CG  TYR A  95      36.367  12.807 -51.697  1.00 46.58           C  
ANISOU  783  CG  TYR A  95     5894   5819   5984   -194    536   -805       C  
ATOM    784  CD1 TYR A  95      35.070  13.179 -51.326  1.00 46.33           C  
ANISOU  784  CD1 TYR A  95     5919   5753   5930   -177    541   -751       C  
ATOM    785  CD2 TYR A  95      36.519  11.800 -52.652  1.00 47.00           C  
ANISOU  785  CD2 TYR A  95     5927   5882   6049   -150    501   -796       C  
ATOM    786  CE1 TYR A  95      33.958  12.555 -51.878  1.00 43.89           C  
ANISOU  786  CE1 TYR A  95     5638   5428   5607   -120    509   -691       C  
ATOM    787  CE2 TYR A  95      35.409  11.163 -53.207  1.00 45.81           C  
ANISOU  787  CE2 TYR A  95     5809   5711   5885    -99    472   -740       C  
ATOM    788  CZ  TYR A  95      34.133  11.547 -52.818  1.00 45.53           C  
ANISOU  788  CZ  TYR A  95     5824   5651   5824    -85    474   -688       C  
ATOM    789  OH  TYR A  95      33.028  10.930 -53.361  1.00 44.69           O  
ANISOU  789  OH  TYR A  95     5742   5539   5699    -40    446   -638       O  
ATOM    790  N   ASP A  96      40.219  12.203 -49.722  1.00 51.54           N  
ANISOU  790  N   ASP A  96     6287   6651   6645   -296    464   -993       N  
ATOM    791  CA  ASP A  96      41.669  12.331 -49.684  1.00 52.39           C  
ANISOU  791  CA  ASP A  96     6317   6828   6760   -338    478  -1068       C  
ATOM    792  C   ASP A  96      42.108  13.098 -50.923  1.00 51.63           C  
ANISOU  792  C   ASP A  96     6248   6693   6675   -373    570  -1101       C  
ATOM    793  O   ASP A  96      42.242  12.525 -52.005  1.00 52.67           O  
ANISOU  793  O   ASP A  96     6380   6806   6824   -331    567  -1088       O  
ATOM    794  CB  ASP A  96      42.320  10.941 -49.637  1.00 55.08           C  
ANISOU  794  CB  ASP A  96     6582   7230   7116   -276    394  -1064       C  
ATOM    795  CG  ASP A  96      43.813  10.987 -49.315  1.00 57.61           C  
ANISOU  795  CG  ASP A  96     6803   7647   7436   -312    393  -1138       C  
ATOM    796  OD1 ASP A  96      44.383  12.095 -49.185  1.00 57.24           O  
ANISOU  796  OD1 ASP A  96     6746   7623   7378   -396    460  -1201       O  
ATOM    797  OD2 ASP A  96      44.419   9.896 -49.196  1.00 58.97           O  
ANISOU  797  OD2 ASP A  96     6909   7877   7621   -256    329  -1133       O  
ATOM    798  N   TYR A  97      42.306  14.401 -50.774  1.00 50.13           N  
ANISOU  798  N   TYR A  97     6086   6484   6474   -451    657  -1144       N  
ATOM    799  CA  TYR A  97      42.597  15.247 -51.928  1.00 52.52           C  
ANISOU  799  CA  TYR A  97     6433   6737   6786   -485    757  -1166       C  
ATOM    800  C   TYR A  97      44.022  15.099 -52.452  1.00 54.57           C  
ANISOU  800  C   TYR A  97     6618   7055   7060   -517    774  -1238       C  
ATOM    801  O   TYR A  97      44.258  15.254 -53.650  1.00 58.13           O  
ANISOU  801  O   TYR A  97     7093   7471   7522   -513    827  -1242       O  
ATOM    802  CB  TYR A  97      42.265  16.706 -51.641  1.00 50.77           C  
ANISOU  802  CB  TYR A  97     6280   6459   6551   -556    860  -1183       C  
ATOM    803  CG  TYR A  97      40.789  16.974 -51.669  1.00 51.32           C  
ANISOU  803  CG  TYR A  97     6440   6449   6608   -510    870  -1101       C  
ATOM    804  CD1 TYR A  97      40.129  17.179 -52.876  1.00 51.19           C  
ANISOU  804  CD1 TYR A  97     6494   6363   6592   -466    917  -1046       C  
ATOM    805  CD2 TYR A  97      40.040  16.999 -50.491  1.00 50.57           C  
ANISOU  805  CD2 TYR A  97     6356   6357   6498   -509    832  -1078       C  
ATOM    806  CE1 TYR A  97      38.771  17.420 -52.916  1.00 51.36           C  
ANISOU  806  CE1 TYR A  97     6589   6326   6597   -418    925   -969       C  
ATOM    807  CE2 TYR A  97      38.680  17.231 -50.517  1.00 50.50           C  
ANISOU  807  CE2 TYR A  97     6426   6283   6479   -465    841  -1003       C  
ATOM    808  CZ  TYR A  97      38.050  17.442 -51.736  1.00 53.36           C  
ANISOU  808  CZ  TYR A  97     6851   6582   6839   -418    887   -948       C  
ATOM    809  OH  TYR A  97      36.696  17.678 -51.786  1.00 54.13           O  
ANISOU  809  OH  TYR A  97     7018   6628   6921   -369    896   -873       O  
ATOM    810  N   ASP A  98      44.960  14.785 -51.561  1.00 54.20           N  
ANISOU  810  N   ASP A  98     6477   7105   7009   -545    729  -1294       N  
ATOM    811  CA  ASP A  98      46.362  14.600 -51.950  1.00 57.73           C  
ANISOU  811  CA  ASP A  98     6838   7627   7467   -573    739  -1366       C  
ATOM    812  C   ASP A  98      46.577  13.369 -52.841  1.00 57.24           C  
ANISOU  812  C   ASP A  98     6745   7572   7429   -487    683  -1336       C  
ATOM    813  O   ASP A  98      47.633  13.216 -53.456  1.00 58.58           O  
ANISOU  813  O   ASP A  98     6858   7786   7613   -500    703  -1387       O  
ATOM    814  CB  ASP A  98      47.256  14.507 -50.708  1.00 60.18           C  
ANISOU  814  CB  ASP A  98     7046   8058   7759   -615    695  -1428       C  
ATOM    815  CG  ASP A  98      47.557  15.868 -50.101  1.00 63.91           C  
ANISOU  815  CG  ASP A  98     7529   8543   8209   -732    781  -1500       C  
ATOM    816  OD1 ASP A  98      47.866  16.803 -50.870  1.00 63.99           O  
ANISOU  816  OD1 ASP A  98     7580   8504   8227   -796    887  -1542       O  
ATOM    817  OD2 ASP A  98      47.486  16.000 -48.855  1.00 64.83           O  
ANISOU  817  OD2 ASP A  98     7614   8717   8300   -763    748  -1516       O  
ATOM    818  N   ALA A  99      45.571  12.502 -52.905  1.00 54.10           N  
ANISOU  818  N   ALA A  99     6386   7131   7037   -405    619  -1257       N  
ATOM    819  CA  ALA A  99      45.706  11.219 -53.576  1.00 51.42           C  
ANISOU  819  CA  ALA A  99     6018   6797   6720   -325    563  -1229       C  
ATOM    820  C   ALA A  99      45.003  11.188 -54.930  1.00 49.79           C  
ANISOU  820  C   ALA A  99     5888   6507   6521   -296    602  -1189       C  
ATOM    821  O   ALA A  99      45.055  10.178 -55.628  1.00 51.49           O  
ANISOU  821  O   ALA A  99     6090   6717   6754   -237    568  -1171       O  
ATOM    822  CB  ALA A  99      45.198  10.099 -52.680  1.00 49.42           C  
ANISOU  822  CB  ALA A  99     5744   6566   6466   -255    463  -1176       C  
ATOM    823  N   ILE A 100      44.356  12.291 -55.297  1.00 46.62           N  
ANISOU  823  N   ILE A 100     5567   6042   6105   -335    676  -1174       N  
ATOM    824  CA  ILE A 100      43.652  12.374 -56.567  1.00 46.04           C  
ANISOU  824  CA  ILE A 100     5564   5900   6027   -307    717  -1132       C  
ATOM    825  C   ILE A 100      44.572  13.005 -57.610  1.00 48.02           C  
ANISOU  825  C   ILE A 100     5811   6149   6285   -352    802  -1183       C  
ATOM    826  O   ILE A 100      44.794  14.217 -57.588  1.00 49.18           O  
ANISOU  826  O   ILE A 100     5989   6273   6422   -418    886  -1213       O  
ATOM    827  CB  ILE A 100      42.309  13.152 -56.450  1.00 45.09           C  
ANISOU  827  CB  ILE A 100     5536   5712   5881   -305    749  -1071       C  
ATOM    828  CG1 ILE A 100      41.369  12.455 -55.452  1.00 44.25           C  
ANISOU  828  CG1 ILE A 100     5433   5611   5768   -261    664  -1021       C  
ATOM    829  CG2 ILE A 100      41.625  13.269 -57.809  1.00 42.98           C  
ANISOU  829  CG2 ILE A 100     5334   5393   5601   -273    792  -1025       C  
ATOM    830  CD1 ILE A 100      40.272  13.343 -54.903  1.00 43.06           C  
ANISOU  830  CD1 ILE A 100     5352   5413   5594   -274    694   -978       C  
ATOM    831  N   PRO A 101      45.119  12.172 -58.525  1.00 48.03           N  
ANISOU  831  N   PRO A 101     5776   6168   6303   -318    785  -1197       N  
ATOM    832  CA  PRO A 101      46.140  12.584 -59.491  1.00 48.69           C  
ANISOU  832  CA  PRO A 101     5841   6263   6396   -358    857  -1254       C  
ATOM    833  C   PRO A 101      45.726  13.779 -60.335  1.00 48.97           C  
ANISOU  833  C   PRO A 101     5963   6232   6410   -395    960  -1237       C  
ATOM    834  O   PRO A 101      46.499  14.737 -60.459  1.00 53.53           O  
ANISOU  834  O   PRO A 101     6539   6810   6988   -465   1043  -1291       O  
ATOM    835  CB  PRO A 101      46.312  11.338 -60.375  1.00 48.52           C  
ANISOU  835  CB  PRO A 101     5790   6254   6392   -296    812  -1245       C  
ATOM    836  CG  PRO A 101      45.929  10.206 -59.487  1.00 47.62           C  
ANISOU  836  CG  PRO A 101     5641   6162   6288   -237    712  -1214       C  
ATOM    837  CD  PRO A 101      44.797  10.739 -58.658  1.00 47.62           C  
ANISOU  837  CD  PRO A 101     5700   6128   6265   -242    700  -1163       C  
ATOM    838  N   TRP A 102      44.522  13.743 -60.903  1.00 47.91           N  
ANISOU  838  N   TRP A 102     5902   6044   6255   -347    960  -1163       N  
ATOM    839  CA  TRP A 102      44.106  14.799 -61.824  1.00 47.58           C  
ANISOU  839  CA  TRP A 102     5943   5944   6188   -363   1058  -1134       C  
ATOM    840  C   TRP A 102      43.919  16.136 -61.146  1.00 50.11           C  
ANISOU  840  C   TRP A 102     6316   6223   6499   -418   1133  -1136       C  
ATOM    841  O   TRP A 102      43.596  17.127 -61.800  1.00 49.32           O  
ANISOU  841  O   TRP A 102     6291   6066   6379   -430   1228  -1109       O  
ATOM    842  CB  TRP A 102      42.868  14.391 -62.621  1.00 47.37           C  
ANISOU  842  CB  TRP A 102     5972   5889   6135   -294   1036  -1053       C  
ATOM    843  CG  TRP A 102      41.606  14.192 -61.808  1.00 45.95           C  
ANISOU  843  CG  TRP A 102     5823   5696   5940   -253    978   -990       C  
ATOM    844  CD1 TRP A 102      41.163  13.018 -61.203  1.00 46.43           C  
ANISOU  844  CD1 TRP A 102     5845   5784   6010   -211    875   -973       C  
ATOM    845  CD2 TRP A 102      40.557  15.188 -61.522  1.00 46.92           C  
ANISOU  845  CD2 TRP A 102     6023   5770   6035   -248   1024   -931       C  
ATOM    846  NE1 TRP A 102      39.953  13.218 -60.570  1.00 45.95           N  
ANISOU  846  NE1 TRP A 102     5829   5700   5928   -186    852   -914       N  
ATOM    847  CE2 TRP A 102      39.543  14.500 -60.716  1.00 46.20           C  
ANISOU  847  CE2 TRP A 102     5928   5689   5938   -204    937   -887       C  
ATOM    848  CE3 TRP A 102      40.378  16.539 -61.822  1.00 46.43           C  
ANISOU  848  CE3 TRP A 102     6032   5655   5955   -272   1131   -911       C  
ATOM    849  CZ2 TRP A 102      38.405  15.147 -60.255  1.00 45.69           C  
ANISOU  849  CZ2 TRP A 102     5923   5590   5848   -186    953   -827       C  
ATOM    850  CZ3 TRP A 102      39.225  17.180 -61.356  1.00 46.14           C  
ANISOU  850  CZ3 TRP A 102     6058   5577   5894   -247   1150   -847       C  
ATOM    851  CH2 TRP A 102      38.262  16.500 -60.588  1.00 46.35           C  
ANISOU  851  CH2 TRP A 102     6073   5621   5914   -205   1061   -807       C  
ATOM    852  N   LEU A 103      44.168  16.183 -59.834  1.00 53.01           N  
ANISOU  852  N   LEU A 103     6642   6619   6877   -451   1098  -1170       N  
ATOM    853  CA  LEU A 103      43.937  17.393 -59.042  1.00 56.50           C  
ANISOU  853  CA  LEU A 103     7133   7023   7310   -507   1167  -1177       C  
ATOM    854  C   LEU A 103      45.209  18.042 -58.485  1.00 61.60           C  
ANISOU  854  C   LEU A 103     7730   7706   7969   -605   1221  -1276       C  
ATOM    855  O   LEU A 103      45.140  19.102 -57.857  1.00 59.72           O  
ANISOU  855  O   LEU A 103     7532   7433   7723   -666   1293  -1297       O  
ATOM    856  CB  LEU A 103      42.936  17.120 -57.904  1.00 54.37           C  
ANISOU  856  CB  LEU A 103     6872   6752   7031   -474   1095  -1131       C  
ATOM    857  CG  LEU A 103      41.435  17.204 -58.238  1.00 53.60           C  
ANISOU  857  CG  LEU A 103     6857   6597   6911   -406   1092  -1034       C  
ATOM    858  CD1 LEU A 103      40.572  16.847 -57.031  1.00 51.21           C  
ANISOU  858  CD1 LEU A 103     6551   6304   6602   -381   1017   -999       C  
ATOM    859  CD2 LEU A 103      41.052  18.574 -58.784  1.00 52.35           C  
ANISOU  859  CD2 LEU A 103     6793   6361   6735   -426   1218  -1006       C  
ATOM    860  N   GLN A 104      46.365  17.426 -58.739  1.00 68.00           N  
ANISOU  860  N   GLN A 104     8453   8585   8796   -621   1193  -1339       N  
ATOM    861  CA  GLN A 104      47.642  17.897 -58.166  1.00 72.28           C  
ANISOU  861  CA  GLN A 104     8927   9189   9346   -714   1231  -1441       C  
ATOM    862  C   GLN A 104      48.090  19.265 -58.679  1.00 72.89           C  
ANISOU  862  C   GLN A 104     9062   9213   9419   -802   1376  -1487       C  
ATOM    863  O   GLN A 104      48.681  20.043 -57.932  1.00 71.73           O  
ANISOU  863  O   GLN A 104     8897   9088   9269   -895   1432  -1559       O  
ATOM    864  CB  GLN A 104      48.759  16.865 -58.366  1.00 74.75           C  
ANISOU  864  CB  GLN A 104     9127   9596   9676   -699   1166  -1493       C  
ATOM    865  CG  GLN A 104      48.578  15.565 -57.584  1.00 80.55           C  
ANISOU  865  CG  GLN A 104     9791  10394  10417   -625   1031  -1464       C  
ATOM    866  CD  GLN A 104      48.467  15.773 -56.077  1.00 85.30           C  
ANISOU  866  CD  GLN A 104    10363  11040  11005   -657    992  -1480       C  
ATOM    867  OE1 GLN A 104      47.388  16.081 -55.550  1.00 86.75           O  
ANISOU  867  OE1 GLN A 104    10613  11169  11175   -644    987  -1426       O  
ATOM    868  NE2 GLN A 104      49.578  15.574 -55.370  1.00 86.53           N  
ANISOU  868  NE2 GLN A 104    10412  11303  11160   -696    963  -1553       N  
ATOM    869  N   ASN A 105      47.798  19.555 -59.946  1.00 75.44           N  
ANISOU  869  N   ASN A 105     9456   9467   9738   -777   1443  -1445       N  
ATOM    870  CA  ASN A 105      48.164  20.846 -60.559  1.00 80.35           C  
ANISOU  870  CA  ASN A 105    10148  10024  10354   -851   1592  -1476       C  
ATOM    871  C   ASN A 105      47.253  22.022 -60.164  1.00 79.32           C  
ANISOU  871  C   ASN A 105    10129   9798  10211   -871   1681  -1433       C  
ATOM    872  O   ASN A 105      47.395  23.132 -60.686  1.00 79.59           O  
ANISOU  872  O   ASN A 105    10241   9758  10240   -922   1816  -1444       O  
ATOM    873  CB  ASN A 105      48.255  20.722 -62.093  1.00 85.94           C  
ANISOU  873  CB  ASN A 105    10891  10701  11060   -814   1634  -1445       C  
ATOM    874  CG  ASN A 105      47.043  20.023 -62.711  1.00 90.90           C  
ANISOU  874  CG  ASN A 105    11562  11300  11672   -700   1567  -1337       C  
ATOM    875  OD1 ASN A 105      45.998  19.851 -62.069  1.00 86.10           O  
ANISOU  875  OD1 ASN A 105    10982  10675  11056   -651   1512  -1275       O  
ATOM    876  ND2 ASN A 105      47.184  19.614 -63.971  1.00 91.07           N  
ANISOU  876  ND2 ASN A 105    11589  11324  11689   -663   1575  -1318       N  
ATOM    877  N   VAL A 106      46.322  21.761 -59.248  1.00 77.04           N  
ANISOU  877  N   VAL A 106     9849   9506   9915   -828   1609  -1384       N  
ATOM    878  CA  VAL A 106      45.390  22.773 -58.743  1.00 75.20           C  
ANISOU  878  CA  VAL A 106     9714   9188   9671   -836   1682  -1342       C  
ATOM    879  C   VAL A 106      45.694  23.011 -57.264  1.00 75.69           C  
ANISOU  879  C   VAL A 106     9730   9292   9736   -911   1665  -1410       C  
ATOM    880  O   VAL A 106      45.790  22.054 -56.486  1.00 73.62           O  
ANISOU  880  O   VAL A 106     9380   9115   9475   -889   1541  -1423       O  
ATOM    881  CB  VAL A 106      43.916  22.306 -58.895  1.00 73.14           C  
ANISOU  881  CB  VAL A 106     9503   8890   9393   -722   1616  -1223       C  
ATOM    882  CG1 VAL A 106      42.948  23.410 -58.497  1.00 72.02           C  
ANISOU  882  CG1 VAL A 106     9467   8656   9239   -721   1703  -1173       C  
ATOM    883  CG2 VAL A 106      43.634  21.834 -60.316  1.00 69.66           C  
ANISOU  883  CG2 VAL A 106     9086   8439   8942   -645   1607  -1160       C  
ATOM    884  N   GLU A 107      45.849  24.275 -56.870  1.00 78.09           N  
ANISOU  884  N   GLU A 107    10094   9538  10039  -1000   1792  -1455       N  
ATOM    885  CA  GLU A 107      46.126  24.581 -55.462  1.00 82.32           C  
ANISOU  885  CA  GLU A 107    10588  10118  10571  -1082   1785  -1528       C  
ATOM    886  C   GLU A 107      44.943  24.226 -54.536  1.00 78.49           C  
ANISOU  886  C   GLU A 107    10119   9627  10076  -1017   1700  -1458       C  
ATOM    887  O   GLU A 107      43.777  24.481 -54.870  1.00 73.09           O  
ANISOU  887  O   GLU A 107     9527   8856   9386   -944   1723  -1363       O  
ATOM    888  CB  GLU A 107      46.629  26.028 -55.259  1.00 92.07           C  
ANISOU  888  CB  GLU A 107    11883  11290  11806  -1208   1953  -1607       C  
ATOM    889  CG  GLU A 107      45.554  27.102 -55.189  1.00 98.95           C  
ANISOU  889  CG  GLU A 107    12892  12027  12675  -1195   2064  -1544       C  
ATOM    890  CD  GLU A 107      45.218  27.687 -56.547  1.00105.51           C  
ANISOU  890  CD  GLU A 107    13830  12748  13508  -1148   2173  -1474       C  
ATOM    891  OE1 GLU A 107      44.829  26.913 -57.456  1.00108.24           O  
ANISOU  891  OE1 GLU A 107    14168  13106  13849  -1044   2100  -1395       O  
ATOM    892  OE2 GLU A 107      45.334  28.923 -56.703  1.00105.71           O  
ANISOU  892  OE2 GLU A 107    13949  12677  13538  -1215   2336  -1499       O  
ATOM    893  N   PRO A 108      45.256  23.604 -53.382  1.00 77.46           N  
ANISOU  893  N   PRO A 108     9895   9596   9939  -1041   1599  -1504       N  
ATOM    894  CA  PRO A 108      44.328  22.910 -52.485  1.00 76.16           C  
ANISOU  894  CA  PRO A 108     9714   9456   9764   -974   1486  -1445       C  
ATOM    895  C   PRO A 108      42.931  23.523 -52.343  1.00 76.44           C  
ANISOU  895  C   PRO A 108     9862   9387   9794   -929   1531  -1361       C  
ATOM    896  O   PRO A 108      41.946  22.783 -52.300  1.00 73.06           O  
ANISOU  896  O   PRO A 108     9441   8955   9360   -833   1440  -1276       O  
ATOM    897  CB  PRO A 108      45.065  22.943 -51.146  1.00 76.52           C  
ANISOU  897  CB  PRO A 108     9675   9601   9798  -1064   1455  -1539       C  
ATOM    898  CG  PRO A 108      46.509  22.877 -51.529  1.00 76.62           C  
ANISOU  898  CG  PRO A 108     9603   9692   9815  -1131   1475  -1633       C  
ATOM    899  CD  PRO A 108      46.648  23.514 -52.890  1.00 76.58           C  
ANISOU  899  CD  PRO A 108     9675   9595   9826  -1137   1590  -1622       C  
ATOM    900  N   ASN A 109      42.850  24.853 -52.279  1.00 78.93           N  
ANISOU  900  N   ASN A 109    10263   9616  10109   -997   1675  -1386       N  
ATOM    901  CA  ASN A 109      41.590  25.540 -51.949  1.00 79.67           C  
ANISOU  901  CA  ASN A 109    10459   9613  10196   -961   1730  -1316       C  
ATOM    902  C   ASN A 109      40.496  25.503 -53.035  1.00 75.35           C  
ANISOU  902  C   ASN A 109     9995   8986   9647   -843   1742  -1194       C  
ATOM    903  O   ASN A 109      39.315  25.694 -52.730  1.00 77.15           O  
ANISOU  903  O   ASN A 109    10283   9164   9866   -784   1741  -1118       O  
ATOM    904  CB  ASN A 109      41.848  26.982 -51.460  1.00 82.86           C  
ANISOU  904  CB  ASN A 109    10933   9945  10603  -1072   1889  -1384       C  
ATOM    905  CG  ASN A 109      42.639  27.814 -52.462  1.00 90.01           C  
ANISOU  905  CG  ASN A 109    11886  10790  11521  -1130   2030  -1426       C  
ATOM    906  OD1 ASN A 109      42.078  28.370 -53.411  1.00 90.83           O  
ANISOU  906  OD1 ASN A 109    12090  10792  11629  -1074   2120  -1352       O  
ATOM    907  ND2 ASN A 109      43.950  27.917 -52.245  1.00 91.43           N  
ANISOU  907  ND2 ASN A 109    11994  11040  11704  -1243   2054  -1545       N  
ATOM    908  N   LEU A 110      40.885  25.248 -54.286  1.00 69.31           N  
ANISOU  908  N   LEU A 110     9229   8219   8886   -811   1753  -1175       N  
ATOM    909  CA  LEU A 110      39.916  25.120 -55.384  1.00 63.75           C  
ANISOU  909  CA  LEU A 110     8588   7463   8170   -699   1756  -1062       C  
ATOM    910  C   LEU A 110      39.492  23.670 -55.642  1.00 61.50           C  
ANISOU  910  C   LEU A 110     8233   7254   7876   -609   1598  -1011       C  
ATOM    911  O   LEU A 110      38.560  23.418 -56.411  1.00 62.24           O  
ANISOU  911  O   LEU A 110     8368   7327   7954   -516   1579   -918       O  
ATOM    912  CB  LEU A 110      40.465  25.726 -56.684  1.00 64.88           C  
ANISOU  912  CB  LEU A 110     8781   7555   8315   -710   1868  -1063       C  
ATOM    913  CG  LEU A 110      40.634  27.244 -56.834  1.00 65.19           C  
ANISOU  913  CG  LEU A 110     8924   7485   8359   -772   2054  -1081       C  
ATOM    914  CD1 LEU A 110      40.482  27.632 -58.298  1.00 64.16           C  
ANISOU  914  CD1 LEU A 110     8866   7293   8216   -714   2138  -1013       C  
ATOM    915  CD2 LEU A 110      39.644  28.018 -55.982  1.00 64.75           C  
ANISOU  915  CD2 LEU A 110     8945   7356   8299   -761   2110  -1042       C  
ATOM    916  N   ARG A 111      40.175  22.723 -55.000  1.00 56.82           N  
ANISOU  916  N   ARG A 111     7538   6754   7294   -637   1490  -1070       N  
ATOM    917  CA  ARG A 111      39.963  21.304 -55.264  1.00 54.72           C  
ANISOU  917  CA  ARG A 111     7207   6557   7026   -562   1353  -1034       C  
ATOM    918  C   ARG A 111      38.534  20.828 -54.972  1.00 54.61           C  
ANISOU  918  C   ARG A 111     7221   6532   6996   -476   1281   -943       C  
ATOM    919  O   ARG A 111      37.890  20.243 -55.856  1.00 54.25           O  
ANISOU  919  O   ARG A 111     7187   6486   6937   -398   1242   -876       O  
ATOM    920  CB  ARG A 111      40.984  20.446 -54.514  1.00 53.56           C  
ANISOU  920  CB  ARG A 111     6948   6507   6893   -604   1261  -1112       C  
ATOM    921  CG  ARG A 111      42.340  20.416 -55.180  1.00 54.99           C  
ANISOU  921  CG  ARG A 111     7078   6725   7088   -654   1294  -1186       C  
ATOM    922  CD  ARG A 111      43.384  19.758 -54.304  1.00 55.93           C  
ANISOU  922  CD  ARG A 111     7084   6948   7216   -699   1218  -1265       C  
ATOM    923  NE  ARG A 111      44.727  19.964 -54.846  1.00 57.65           N  
ANISOU  923  NE  ARG A 111     7253   7204   7445   -763   1270  -1348       N  
ATOM    924  CZ  ARG A 111      45.834  19.437 -54.330  1.00 57.24           C  
ANISOU  924  CZ  ARG A 111     7093   7255   7398   -801   1217  -1423       C  
ATOM    925  NH1 ARG A 111      45.768  18.662 -53.252  1.00 59.34           N  
ANISOU  925  NH1 ARG A 111     7292   7595   7659   -778   1110  -1422       N  
ATOM    926  NH2 ARG A 111      47.005  19.689 -54.888  1.00 53.47           N  
ANISOU  926  NH2 ARG A 111     6573   6811   6930   -860   1272  -1498       N  
ATOM    927  N   PRO A 112      38.032  21.070 -53.736  1.00 50.68           N  
ANISOU  927  N   PRO A 112     6731   6031   6494   -495   1265   -944       N  
ATOM    928  CA  PRO A 112      36.700  20.579 -53.420  1.00 49.05           C  
ANISOU  928  CA  PRO A 112     6544   5820   6271   -418   1195   -863       C  
ATOM    929  C   PRO A 112      35.658  20.972 -54.451  1.00 48.21           C  
ANISOU  929  C   PRO A 112     6516   5657   6144   -343   1246   -772       C  
ATOM    930  O   PRO A 112      34.819  20.150 -54.796  1.00 49.74           O  
ANISOU  930  O   PRO A 112     6700   5877   6323   -268   1169   -710       O  
ATOM    931  CB  PRO A 112      36.405  21.219 -52.058  1.00 51.43           C  
ANISOU  931  CB  PRO A 112     6864   6105   6570   -466   1218   -885       C  
ATOM    932  CG  PRO A 112      37.748  21.295 -51.408  1.00 51.41           C  
ANISOU  932  CG  PRO A 112     6796   6153   6582   -562   1222   -990       C  
ATOM    933  CD  PRO A 112      38.720  21.589 -52.536  1.00 51.50           C  
ANISOU  933  CD  PRO A 112     6807   6155   6606   -589   1291  -1027       C  
ATOM    934  N   LYS A 113      35.729  22.197 -54.963  1.00 50.54           N  
ANISOU  934  N   LYS A 113     6886   5879   6438   -361   1379   -765       N  
ATOM    935  CA  LYS A 113      34.749  22.687 -55.941  1.00 51.81           C  
ANISOU  935  CA  LYS A 113     7122   5989   6572   -281   1439   -671       C  
ATOM    936  C   LYS A 113      34.807  21.900 -57.241  1.00 49.09           C  
ANISOU  936  C   LYS A 113     6752   5686   6214   -227   1393   -639       C  
ATOM    937  O   LYS A 113      33.772  21.614 -57.857  1.00 47.59           O  
ANISOU  937  O   LYS A 113     6581   5507   5992   -143   1365   -557       O  
ATOM    938  CB  LYS A 113      34.982  24.164 -56.244  1.00 57.49           C  
ANISOU  938  CB  LYS A 113     7931   6617   7296   -315   1603   -674       C  
ATOM    939  CG  LYS A 113      33.739  24.904 -56.712  1.00 63.47           C  
ANISOU  939  CG  LYS A 113     8777   7312   8024   -228   1675   -567       C  
ATOM    940  CD  LYS A 113      33.259  25.903 -55.657  1.00 68.99           C  
ANISOU  940  CD  LYS A 113     9539   7942   8732   -254   1755   -567       C  
ATOM    941  CE  LYS A 113      32.663  25.204 -54.438  1.00 70.87           C  
ANISOU  941  CE  LYS A 113     9725   8230   8970   -252   1642   -573       C  
ATOM    942  NZ  LYS A 113      32.772  26.041 -53.209  1.00 75.66           N  
ANISOU  942  NZ  LYS A 113    10363   8786   9594   -325   1710   -626       N  
ATOM    943  N   LEU A 114      36.020  21.570 -57.668  1.00 47.17           N  
ANISOU  943  N   LEU A 114     6461   5471   5990   -276   1389   -708       N  
ATOM    944  CA  LEU A 114      36.205  20.798 -58.884  1.00 45.82           C  
ANISOU  944  CA  LEU A 114     6261   5340   5808   -235   1350   -691       C  
ATOM    945  C   LEU A 114      35.721  19.359 -58.695  1.00 43.53           C  
ANISOU  945  C   LEU A 114     5905   5121   5513   -188   1208   -675       C  
ATOM    946  O   LEU A 114      34.944  18.851 -59.508  1.00 42.84           O  
ANISOU  946  O   LEU A 114     5824   5056   5397   -121   1173   -614       O  
ATOM    947  CB  LEU A 114      37.662  20.839 -59.331  1.00 47.05           C  
ANISOU  947  CB  LEU A 114     6380   5507   5987   -303   1387   -774       C  
ATOM    948  CG  LEU A 114      38.035  22.038 -60.204  1.00 50.08           C  
ANISOU  948  CG  LEU A 114     6837   5824   6364   -325   1532   -769       C  
ATOM    949  CD1 LEU A 114      39.541  22.132 -60.377  1.00 50.48           C  
ANISOU  949  CD1 LEU A 114     6846   5891   6443   -412   1571   -868       C  
ATOM    950  CD2 LEU A 114      37.342  21.968 -61.561  1.00 51.00           C  
ANISOU  950  CD2 LEU A 114     6996   5938   6444   -242   1549   -684       C  
ATOM    951  N   LEU A 115      36.154  18.716 -57.612  1.00 41.62           N  
ANISOU  951  N   LEU A 115     5601   4916   5296   -225   1130   -728       N  
ATOM    952  CA  LEU A 115      35.721  17.351 -57.326  1.00 41.04           C  
ANISOU  952  CA  LEU A 115     5472   4898   5222   -184   1005   -713       C  
ATOM    953  C   LEU A 115      34.195  17.253 -57.313  1.00 40.26           C  
ANISOU  953  C   LEU A 115     5413   4793   5091   -117    977   -628       C  
ATOM    954  O   LEU A 115      33.615  16.330 -57.909  1.00 44.23           O  
ANISOU  954  O   LEU A 115     5898   5332   5575    -66    914   -593       O  
ATOM    955  CB  LEU A 115      36.305  16.841 -56.010  1.00 40.73           C  
ANISOU  955  CB  LEU A 115     5371   4894   5208   -227    937   -770       C  
ATOM    956  CG  LEU A 115      35.980  15.374 -55.700  1.00 41.99           C  
ANISOU  956  CG  LEU A 115     5477   5105   5371   -184    815   -756       C  
ATOM    957  CD1 LEU A 115      36.532  14.402 -56.752  1.00 40.23           C  
ANISOU  957  CD1 LEU A 115     5213   4913   5157   -161    780   -772       C  
ATOM    958  CD2 LEU A 115      36.478  15.003 -54.313  1.00 42.37           C  
ANISOU  958  CD2 LEU A 115     5472   5188   5437   -219    756   -800       C  
ATOM    959  N   LEU A 116      33.550  18.226 -56.681  1.00 36.95           N  
ANISOU  959  N   LEU A 116     5047   4329   4661   -118   1032   -598       N  
ATOM    960  CA  LEU A 116      32.089  18.287 -56.633  1.00 37.07           C  
ANISOU  960  CA  LEU A 116     5100   4340   4643    -54   1018   -516       C  
ATOM    961  C   LEU A 116      31.531  18.385 -58.034  1.00 36.84           C  
ANISOU  961  C   LEU A 116     5101   4319   4577      7   1051   -454       C  
ATOM    962  O   LEU A 116      30.596  17.676 -58.395  1.00 35.66           O  
ANISOU  962  O   LEU A 116     4937   4213   4397     62    989   -406       O  
ATOM    963  CB  LEU A 116      31.601  19.484 -55.788  1.00 36.00           C  
ANISOU  963  CB  LEU A 116     5024   4146   4506    -66   1094   -497       C  
ATOM    964  CG  LEU A 116      30.088  19.793 -55.834  1.00 36.58           C  
ANISOU  964  CG  LEU A 116     5144   4212   4543      7   1103   -406       C  
ATOM    965  CD1 LEU A 116      29.321  18.725 -55.069  1.00 35.33           C  
ANISOU  965  CD1 LEU A 116     4940   4105   4378     27    987   -394       C  
ATOM    966  CD2 LEU A 116      29.736  21.195 -55.308  1.00 35.40           C  
ANISOU  966  CD2 LEU A 116     5068   3986   4393      1   1215   -384       C  
ATOM    967  N   LYS A 117      32.121  19.269 -58.823  1.00 39.14           N  
ANISOU  967  N   LYS A 117     5432   4571   4867     -4   1151   -458       N  
ATOM    968  CA  LYS A 117      31.655  19.520 -60.175  1.00 41.43           C  
ANISOU  968  CA  LYS A 117     5756   4869   5117     55   1196   -394       C  
ATOM    969  C   LYS A 117      31.792  18.263 -61.062  1.00 39.84           C  
ANISOU  969  C   LYS A 117     5496   4738   4902     73   1113   -406       C  
ATOM    970  O   LYS A 117      30.884  17.936 -61.833  1.00 38.84           O  
ANISOU  970  O   LYS A 117     5371   4656   4728    134   1090   -346       O  
ATOM    971  CB  LYS A 117      32.430  20.688 -60.759  1.00 43.63           C  
ANISOU  971  CB  LYS A 117     6090   5084   5401     27   1325   -405       C  
ATOM    972  CG  LYS A 117      31.893  21.214 -62.065  1.00 47.65           C  
ANISOU  972  CG  LYS A 117     6650   5591   5863     96   1394   -326       C  
ATOM    973  CD  LYS A 117      33.043  21.745 -62.912  1.00 49.56           C  
ANISOU  973  CD  LYS A 117     6914   5799   6117     54   1484   -364       C  
ATOM    974  CE  LYS A 117      32.602  22.929 -63.738  1.00 54.06           C  
ANISOU  974  CE  LYS A 117     7571   6318   6648    108   1609   -283       C  
ATOM    975  NZ  LYS A 117      33.764  23.793 -64.083  1.00 60.85           N  
ANISOU  975  NZ  LYS A 117     8474   7110   7535     45   1727   -331       N  
ATOM    976  N   HIS A 118      32.909  17.550 -60.921  1.00 39.04           N  
ANISOU  976  N   HIS A 118     5340   4653   4840     19   1071   -485       N  
ATOM    977  CA  HIS A 118      33.149  16.319 -61.704  1.00 40.03           C  
ANISOU  977  CA  HIS A 118     5411   4836   4960     31    999   -506       C  
ATOM    978  C   HIS A 118      32.356  15.144 -61.208  1.00 39.09           C  
ANISOU  978  C   HIS A 118     5253   4764   4836     56    891   -494       C  
ATOM    979  O   HIS A 118      31.798  14.381 -62.019  1.00 41.26           O  
ANISOU  979  O   HIS A 118     5511   5086   5079     91    851   -471       O  
ATOM    980  CB  HIS A 118      34.644  15.996 -61.785  1.00 40.57           C  
ANISOU  980  CB  HIS A 118     5436   4906   5073    -26   1000   -590       C  
ATOM    981  CG  HIS A 118      35.433  17.013 -62.573  1.00 43.36           C  
ANISOU  981  CG  HIS A 118     5825   5222   5425    -53   1110   -605       C  
ATOM    982  ND1 HIS A 118      36.200  16.681 -63.633  1.00 44.92           N  
ANISOU  982  ND1 HIS A 118     6001   5441   5623    -63   1125   -636       N  
ATOM    983  CD2 HIS A 118      35.515  18.404 -62.449  1.00 43.69           C  
ANISOU  983  CD2 HIS A 118     5931   5202   5465    -73   1219   -591       C  
ATOM    984  CE1 HIS A 118      36.757  17.799 -64.144  1.00 45.30           C  
ANISOU  984  CE1 HIS A 118     6096   5445   5669    -89   1235   -641       C  
ATOM    985  NE2 HIS A 118      36.329  18.850 -63.424  1.00 43.32           N  
ANISOU  985  NE2 HIS A 118     5901   5141   5417    -95   1295   -612       N  
ATOM    986  N   ASN A 119      32.269  14.993 -59.883  1.00 36.80           N  
ANISOU  986  N   ASN A 119     4949   4461   4571     35    848   -510       N  
ATOM    987  CA  ASN A 119      31.378  14.007 -59.307  1.00 34.99           C  
ANISOU  987  CA  ASN A 119     4695   4266   4334     60    757   -490       C  
ATOM    988  C   ASN A 119      29.964  14.208 -59.835  1.00 34.40           C  
ANISOU  988  C   ASN A 119     4651   4214   4203    117    764   -414       C  
ATOM    989  O   ASN A 119      29.317  13.250 -60.305  1.00 34.47           O  
ANISOU  989  O   ASN A 119     4634   4274   4186    141    705   -400       O  
ATOM    990  CB  ASN A 119      31.381  14.066 -57.768  1.00 35.40           C  
ANISOU  990  CB  ASN A 119     4738   4297   4413     32    725   -508       C  
ATOM    991  CG  ASN A 119      32.502  13.254 -57.141  1.00 34.30           C  
ANISOU  991  CG  ASN A 119     4542   4170   4318     -6    671   -576       C  
ATOM    992  OD1 ASN A 119      32.659  13.243 -55.914  1.00 38.66           O  
ANISOU  992  OD1 ASN A 119     5080   4719   4890    -31    642   -596       O  
ATOM    993  ND2 ASN A 119      33.288  12.597 -57.958  1.00 32.24           N  
ANISOU  993  ND2 ASN A 119     4248   3929   4071     -9    659   -611       N  
ATOM    994  N   LEU A 120      29.478  15.444 -59.780  1.00 31.65           N  
ANISOU  994  N   LEU A 120     4356   3833   3834    137    839   -365       N  
ATOM    995  CA  LEU A 120      28.160  15.734 -60.326  1.00 32.59           C  
ANISOU  995  CA  LEU A 120     4501   3984   3895    202    852   -286       C  
ATOM    996  C   LEU A 120      28.061  15.312 -61.806  1.00 34.35           C  
ANISOU  996  C   LEU A 120     4710   4265   4076    231    852   -269       C  
ATOM    997  O   LEU A 120      27.072  14.693 -62.224  1.00 37.00           O  
ANISOU  997  O   LEU A 120     5025   4667   4365    267    805   -235       O  
ATOM    998  CB  LEU A 120      27.785  17.212 -60.138  1.00 32.70           C  
ANISOU  998  CB  LEU A 120     4582   3946   3896    228    950   -233       C  
ATOM    999  CG  LEU A 120      27.321  17.678 -58.739  1.00 32.86           C  
ANISOU  999  CG  LEU A 120     4623   3926   3936    217    952   -226       C  
ATOM   1000  CD1 LEU A 120      27.166  19.201 -58.704  1.00 32.93           C  
ANISOU 1000  CD1 LEU A 120     4705   3867   3938    238   1072   -183       C  
ATOM   1001  CD2 LEU A 120      26.024  16.986 -58.310  1.00 30.55           C  
ANISOU 1001  CD2 LEU A 120     4305   3687   3612    255    873   -186       C  
ATOM   1002  N   PHE A 121      29.091  15.611 -62.594  1.00 34.02           N  
ANISOU 1002  N   PHE A 121     4676   4203   4046    210    905   -298       N  
ATOM   1003  CA  PHE A 121      29.055  15.221 -63.994  1.00 34.72           C  
ANISOU 1003  CA  PHE A 121     4750   4347   4092    234    908   -286       C  
ATOM   1004  C   PHE A 121      28.870  13.717 -64.107  1.00 33.78           C  
ANISOU 1004  C   PHE A 121     4572   4288   3973    221    811   -324       C  
ATOM   1005  O   PHE A 121      27.944  13.256 -64.781  1.00 34.48           O  
ANISOU 1005  O   PHE A 121     4647   4449   4006    254    782   -290       O  
ATOM   1006  CB  PHE A 121      30.304  15.685 -64.768  1.00 34.83           C  
ANISOU 1006  CB  PHE A 121     4778   4329   4126    204    978   -322       C  
ATOM   1007  CG  PHE A 121      30.309  15.251 -66.210  1.00 34.36           C  
ANISOU 1007  CG  PHE A 121     4703   4330   4021    224    981   -315       C  
ATOM   1008  CD1 PHE A 121      30.712  13.970 -66.564  1.00 33.08           C  
ANISOU 1008  CD1 PHE A 121     4486   4210   3872    197    913   -374       C  
ATOM   1009  CD2 PHE A 121      29.876  16.118 -67.216  1.00 34.86           C  
ANISOU 1009  CD2 PHE A 121     4807   4411   4024    274   1055   -246       C  
ATOM   1010  CE1 PHE A 121      30.702  13.572 -67.887  1.00 34.05           C  
ANISOU 1010  CE1 PHE A 121     4594   4392   3949    209    918   -372       C  
ATOM   1011  CE2 PHE A 121      29.842  15.714 -68.532  1.00 33.65           C  
ANISOU 1011  CE2 PHE A 121     4637   4326   3821    291   1055   -238       C  
ATOM   1012  CZ  PHE A 121      30.262  14.443 -68.869  1.00 33.61           C  
ANISOU 1012  CZ  PHE A 121     4575   4363   3830    254    986   -306       C  
ATOM   1013  N   LEU A 122      29.737  12.953 -63.439  1.00 33.99           N  
ANISOU 1013  N   LEU A 122     4565   4289   4058    173    764   -394       N  
ATOM   1014  CA  LEU A 122      29.625  11.478 -63.452  1.00 32.97           C  
ANISOU 1014  CA  LEU A 122     4387   4200   3937    160    680   -432       C  
ATOM   1015  C   LEU A 122      28.229  10.983 -63.090  1.00 33.67           C  
ANISOU 1015  C   LEU A 122     4471   4334   3989    186    625   -392       C  
ATOM   1016  O   LEU A 122      27.633  10.198 -63.825  1.00 35.56           O  
ANISOU 1016  O   LEU A 122     4688   4635   4188    195    594   -391       O  
ATOM   1017  CB  LEU A 122      30.665  10.831 -62.546  1.00 31.74           C  
ANISOU 1017  CB  LEU A 122     4201   4006   3851    119    640   -498       C  
ATOM   1018  CG  LEU A 122      32.119  10.974 -63.003  1.00 32.46           C  
ANISOU 1018  CG  LEU A 122     4278   4074   3980     88    679   -554       C  
ATOM   1019  CD1 LEU A 122      33.091  10.523 -61.914  1.00 30.67           C  
ANISOU 1019  CD1 LEU A 122     4017   3819   3815     55    642   -609       C  
ATOM   1020  CD2 LEU A 122      32.345  10.216 -64.311  1.00 32.00           C  
ANISOU 1020  CD2 LEU A 122     4198   4055   3903     91    676   -577       C  
ATOM   1021  N   LEU A 123      27.692  11.460 -61.973  1.00 34.78           N  
ANISOU 1021  N   LEU A 123     4630   4448   4138    194    618   -363       N  
ATOM   1022  CA  LEU A 123      26.383  10.999 -61.529  1.00 33.65           C  
ANISOU 1022  CA  LEU A 123     4478   4346   3961    214    568   -329       C  
ATOM   1023  C   LEU A 123      25.306  11.387 -62.522  1.00 34.21           C  
ANISOU 1023  C   LEU A 123     4556   4487   3954    262    593   -268       C  
ATOM   1024  O   LEU A 123      24.349  10.640 -62.704  1.00 35.20           O  
ANISOU 1024  O   LEU A 123     4655   4679   4039    270    546   -259       O  
ATOM   1025  CB  LEU A 123      26.020  11.560 -60.151  1.00 33.07           C  
ANISOU 1025  CB  LEU A 123     4425   4229   3908    215    564   -308       C  
ATOM   1026  CG  LEU A 123      26.873  11.234 -58.934  1.00 33.77           C  
ANISOU 1026  CG  LEU A 123     4503   4264   4062    172    532   -358       C  
ATOM   1027  CD1 LEU A 123      26.534  12.225 -57.827  1.00 33.14           C  
ANISOU 1027  CD1 LEU A 123     4456   4146   3990    175    559   -329       C  
ATOM   1028  CD2 LEU A 123      26.704   9.789 -58.460  1.00 31.85           C  
ANISOU 1028  CD2 LEU A 123     4224   4040   3835    155    450   -389       C  
ATOM   1029  N   ASP A 124      25.436  12.565 -63.137  1.00 34.08           N  
ANISOU 1029  N   ASP A 124     4575   4460   3913    294    669   -225       N  
ATOM   1030  CA  ASP A 124      24.363  13.075 -63.983  1.00 34.39           C  
ANISOU 1030  CA  ASP A 124     4621   4571   3872    354    698   -153       C  
ATOM   1031  C   ASP A 124      24.411  12.394 -65.332  1.00 34.04           C  
ANISOU 1031  C   ASP A 124     4545   4605   3783    353    686   -169       C  
ATOM   1032  O   ASP A 124      23.375  12.095 -65.905  1.00 34.82           O  
ANISOU 1032  O   ASP A 124     4618   4799   3811    382    663   -137       O  
ATOM   1033  CB  ASP A 124      24.443  14.607 -64.169  1.00 35.75           C  
ANISOU 1033  CB  ASP A 124     4851   4700   4033    399    795    -91       C  
ATOM   1034  CG  ASP A 124      23.944  15.404 -62.939  1.00 38.17           C  
ANISOU 1034  CG  ASP A 124     5192   4950   4360    416    816    -56       C  
ATOM   1035  OD1 ASP A 124      23.040  14.942 -62.185  1.00 37.15           O  
ANISOU 1035  OD1 ASP A 124     5042   4851   4222    421    759    -46       O  
ATOM   1036  OD2 ASP A 124      24.449  16.533 -62.755  1.00 38.72           O  
ANISOU 1036  OD2 ASP A 124     5314   4944   4454    422    899    -39       O  
ATOM   1037  N   ASN A 125      25.620  12.149 -65.836  1.00 33.27           N  
ANISOU 1037  N   ASN A 125     4444   4473   3721    316    702   -224       N  
ATOM   1038  CA  ASN A 125      25.805  11.667 -67.216  1.00 33.53           C  
ANISOU 1038  CA  ASN A 125     4454   4574   3711    313    707   -242       C  
ATOM   1039  C   ASN A 125      26.056  10.146 -67.386  1.00 33.22           C  
ANISOU 1039  C   ASN A 125     4367   4562   3691    262    641   -319       C  
ATOM   1040  O   ASN A 125      25.856   9.589 -68.460  1.00 34.51           O  
ANISOU 1040  O   ASN A 125     4505   4801   3805    257    635   -334       O  
ATOM   1041  CB  ASN A 125      26.899  12.483 -67.901  1.00 32.60           C  
ANISOU 1041  CB  ASN A 125     4367   4410   3608    312    784   -244       C  
ATOM   1042  CG  ASN A 125      26.531  13.952 -68.008  1.00 33.43           C  
ANISOU 1042  CG  ASN A 125     4526   4495   3680    369    865   -161       C  
ATOM   1043  OD1 ASN A 125      26.970  14.772 -67.206  1.00 34.99           O  
ANISOU 1043  OD1 ASN A 125     4763   4606   3926    363    908   -156       O  
ATOM   1044  ND2 ASN A 125      25.653  14.269 -68.933  1.00 32.15           N  
ANISOU 1044  ND2 ASN A 125     4363   4418   3432    426    885    -93       N  
ATOM   1045  N   ILE A 126      26.475   9.486 -66.322  1.00 32.41           N  
ANISOU 1045  N   ILE A 126     4256   4400   3658    225    597   -367       N  
ATOM   1046  CA  ILE A 126      26.950   8.110 -66.428  1.00 31.47           C  
ANISOU 1046  CA  ILE A 126     4103   4281   3571    181    551   -441       C  
ATOM   1047  C   ILE A 126      26.230   7.207 -65.437  1.00 30.56           C  
ANISOU 1047  C   ILE A 126     3973   4165   3472    165    486   -453       C  
ATOM   1048  O   ILE A 126      25.653   6.198 -65.825  1.00 32.04           O  
ANISOU 1048  O   ILE A 126     4136   4405   3631    146    453   -478       O  
ATOM   1049  CB  ILE A 126      28.486   8.057 -66.240  1.00 30.72           C  
ANISOU 1049  CB  ILE A 126     4009   4109   3553    152    569   -496       C  
ATOM   1050  CG1 ILE A 126      29.152   9.007 -67.251  1.00 29.62           C  
ANISOU 1050  CG1 ILE A 126     3888   3970   3394    163    641   -483       C  
ATOM   1051  CG2 ILE A 126      29.006   6.618 -66.315  1.00 29.44           C  
ANISOU 1051  CG2 ILE A 126     3814   3940   3430    117    527   -567       C  
ATOM   1052  CD1 ILE A 126      30.581   8.678 -67.609  1.00 30.05           C  
ANISOU 1052  CD1 ILE A 126     3927   3986   3501    130    659   -549       C  
ATOM   1053  N   VAL A 127      26.188   7.613 -64.173  1.00 29.16           N  
ANISOU 1053  N   VAL A 127     3812   3932   3333    171    473   -433       N  
ATOM   1054  CA  VAL A 127      25.585   6.749 -63.137  1.00 28.81           C  
ANISOU 1054  CA  VAL A 127     3758   3879   3308    154    413   -444       C  
ATOM   1055  C   VAL A 127      24.086   6.632 -63.288  1.00 27.45           C  
ANISOU 1055  C   VAL A 127     3577   3786   3066    169    393   -406       C  
ATOM   1056  O   VAL A 127      23.564   5.542 -63.436  1.00 27.91           O  
ANISOU 1056  O   VAL A 127     3613   3882   3108    143    357   -437       O  
ATOM   1057  CB  VAL A 127      25.977   7.164 -61.708  1.00 28.02           C  
ANISOU 1057  CB  VAL A 127     3675   3707   3264    153    403   -438       C  
ATOM   1058  CG1 VAL A 127      25.297   6.264 -60.694  1.00 26.72           C  
ANISOU 1058  CG1 VAL A 127     3503   3538   3112    138    344   -443       C  
ATOM   1059  CG2 VAL A 127      27.503   7.104 -61.550  1.00 27.84           C  
ANISOU 1059  CG2 VAL A 127     3646   3622   3306    132    415   -486       C  
ATOM   1060  N   LYS A 128      23.392   7.752 -63.300  1.00 27.71           N  
ANISOU 1060  N   LYS A 128     3626   3847   3054    211    422   -340       N  
ATOM   1061  CA  LYS A 128      21.954   7.708 -63.539  1.00 28.55           C  
ANISOU 1061  CA  LYS A 128     3715   4047   3085    233    406   -300       C  
ATOM   1062  C   LYS A 128      21.570   7.117 -64.913  1.00 30.05           C  
ANISOU 1062  C   LYS A 128     3871   4339   3207    224    405   -318       C  
ATOM   1063  O   LYS A 128      20.730   6.224 -64.970  1.00 30.50           O  
ANISOU 1063  O   LYS A 128     3898   4460   3229    198    367   -340       O  
ATOM   1064  CB  LYS A 128      21.314   9.057 -63.268  1.00 28.38           C  
ANISOU 1064  CB  LYS A 128     3717   4033   3030    291    444   -221       C  
ATOM   1065  CG  LYS A 128      21.191   9.322 -61.780  1.00 28.51           C  
ANISOU 1065  CG  LYS A 128     3756   3980   3095    287    427   -210       C  
ATOM   1066  CD  LYS A 128      20.947  10.780 -61.492  1.00 28.98           C  
ANISOU 1066  CD  LYS A 128     3852   4014   3143    340    484   -142       C  
ATOM   1067  CE  LYS A 128      20.685  10.965 -60.005  1.00 28.52           C  
ANISOU 1067  CE  LYS A 128     3812   3899   3125    331    466   -137       C  
ATOM   1068  NZ  LYS A 128      20.003  12.258 -59.735  1.00 28.78           N  
ANISOU 1068  NZ  LYS A 128     3876   3927   3130    387    519    -64       N  
ATOM   1069  N   PRO A 129      22.224   7.569 -66.015  1.00 30.79           N  
ANISOU 1069  N   PRO A 129     3969   4447   3281    238    450   -316       N  
ATOM   1070  CA  PRO A 129      21.885   6.939 -67.305  1.00 31.81           C  
ANISOU 1070  CA  PRO A 129     4063   4680   3343    222    447   -340       C  
ATOM   1071  C   PRO A 129      22.179   5.431 -67.417  1.00 32.49           C  
ANISOU 1071  C   PRO A 129     4125   4760   3459    155    411   -429       C  
ATOM   1072  O   PRO A 129      21.382   4.711 -68.047  1.00 32.55           O  
ANISOU 1072  O   PRO A 129     4099   4864   3404    129    392   -452       O  
ATOM   1073  CB  PRO A 129      22.707   7.746 -68.311  1.00 32.19           C  
ANISOU 1073  CB  PRO A 129     4128   4724   3378    248    505   -322       C  
ATOM   1074  CG  PRO A 129      22.733   9.118 -67.703  1.00 31.88           C  
ANISOU 1074  CG  PRO A 129     4130   4629   3354    302    546   -251       C  
ATOM   1075  CD  PRO A 129      22.907   8.863 -66.219  1.00 31.02           C  
ANISOU 1075  CD  PRO A 129     4034   4428   3322    277    512   -273       C  
ATOM   1076  N   ILE A 130      23.286   4.941 -66.830  1.00 31.82           N  
ANISOU 1076  N   ILE A 130     4057   4568   3464    126    404   -478       N  
ATOM   1077  CA  ILE A 130      23.513   3.483 -66.830  1.00 30.73           C  
ANISOU 1077  CA  ILE A 130     3904   4413   3359     70    376   -555       C  
ATOM   1078  C   ILE A 130      22.367   2.698 -66.192  1.00 30.73           C  
ANISOU 1078  C   ILE A 130     3891   4445   3339     44    335   -563       C  
ATOM   1079  O   ILE A 130      21.884   1.715 -66.760  1.00 31.47           O  
ANISOU 1079  O   ILE A 130     3962   4595   3398      0    326   -611       O  
ATOM   1080  CB  ILE A 130      24.865   3.043 -66.247  1.00 30.01           C  
ANISOU 1080  CB  ILE A 130     3828   4207   3366     55    375   -599       C  
ATOM   1081  CG1 ILE A 130      25.171   1.634 -66.737  1.00 29.93           C  
ANISOU 1081  CG1 ILE A 130     3804   4191   3375      7    369   -676       C  
ATOM   1082  CG2 ILE A 130      24.866   3.045 -64.721  1.00 28.63           C  
ANISOU 1082  CG2 ILE A 130     3670   3957   3248     62    343   -582       C  
ATOM   1083  CD1 ILE A 130      26.470   1.550 -67.485  1.00 31.64           C  
ANISOU 1083  CD1 ILE A 130     4018   4373   3629      3    403   -717       C  
ATOM   1084  N   ILE A 131      21.918   3.161 -65.033  1.00 30.57           N  
ANISOU 1084  N   ILE A 131     3886   4392   3336     67    314   -518       N  
ATOM   1085  CA  ILE A 131      20.777   2.566 -64.355  1.00 32.12           C  
ANISOU 1085  CA  ILE A 131     4072   4620   3510     45    278   -518       C  
ATOM   1086  C   ILE A 131      19.541   2.604 -65.263  1.00 33.74           C  
ANISOU 1086  C   ILE A 131     4240   4966   3611     43    279   -505       C  
ATOM   1087  O   ILE A 131      18.878   1.575 -65.450  1.00 35.36           O  
ANISOU 1087  O   ILE A 131     4423   5223   3787     -8    262   -552       O  
ATOM   1088  CB  ILE A 131      20.542   3.230 -62.967  1.00 32.78           C  
ANISOU 1088  CB  ILE A 131     4178   4647   3627     75    261   -467       C  
ATOM   1089  CG1 ILE A 131      21.781   3.020 -62.090  1.00 31.12           C  
ANISOU 1089  CG1 ILE A 131     3995   4316   3513     69    255   -490       C  
ATOM   1090  CG2 ILE A 131      19.330   2.640 -62.242  1.00 33.56           C  
ANISOU 1090  CG2 ILE A 131     4268   4781   3702     52    225   -465       C  
ATOM   1091  CD1 ILE A 131      21.767   3.848 -60.826  1.00 31.02           C  
ANISOU 1091  CD1 ILE A 131     4004   4249   3530     97    247   -444       C  
ATOM   1092  N   ALA A 132      19.290   3.753 -65.897  1.00 33.31           N  
ANISOU 1092  N   ALA A 132     4178   4977   3499     96    305   -444       N  
ATOM   1093  CA  ALA A 132      18.119   3.923 -66.762  1.00 34.42           C  
ANISOU 1093  CA  ALA A 132     4277   5270   3530    108    306   -419       C  
ATOM   1094  C   ALA A 132      18.196   3.037 -67.992  1.00 36.00           C  
ANISOU 1094  C   ALA A 132     4444   5547   3685     57    312   -485       C  
ATOM   1095  O   ALA A 132      17.169   2.632 -68.540  1.00 35.35           O  
ANISOU 1095  O   ALA A 132     4317   5594   3518     32    300   -499       O  
ATOM   1096  CB  ALA A 132      17.968   5.378 -67.179  1.00 34.72           C  
ANISOU 1096  CB  ALA A 132     4321   5350   3520    189    340   -331       C  
ATOM   1097  N   PHE A 133      19.424   2.753 -68.429  1.00 36.02           N  
ANISOU 1097  N   PHE A 133     4467   5476   3742     38    334   -529       N  
ATOM   1098  CA  PHE A 133      19.648   1.971 -69.626  1.00 36.47           C  
ANISOU 1098  CA  PHE A 133     4498   5594   3762    -10    348   -596       C  
ATOM   1099  C   PHE A 133      19.247   0.532 -69.390  1.00 36.50           C  
ANISOU 1099  C   PHE A 133     4490   5597   3778    -89    327   -677       C  
ATOM   1100  O   PHE A 133      18.686  -0.108 -70.272  1.00 39.62           O  
ANISOU 1100  O   PHE A 133     4849   6100   4104   -138    332   -725       O  
ATOM   1101  CB  PHE A 133      21.121   2.046 -70.070  1.00 37.49           C  
ANISOU 1101  CB  PHE A 133     4654   5634   3955     -8    381   -623       C  
ATOM   1102  CG  PHE A 133      21.393   1.339 -71.378  1.00 39.48           C  
ANISOU 1102  CG  PHE A 133     4881   5950   4166    -54    403   -689       C  
ATOM   1103  CD1 PHE A 133      20.962   1.890 -72.590  1.00 40.15           C  
ANISOU 1103  CD1 PHE A 133     4935   6169   4148    -36    423   -662       C  
ATOM   1104  CD2 PHE A 133      22.065   0.119 -71.401  1.00 39.56           C  
ANISOU 1104  CD2 PHE A 133     4900   5891   4239   -115    407   -777       C  
ATOM   1105  CE1 PHE A 133      21.209   1.241 -73.792  1.00 41.26           C  
ANISOU 1105  CE1 PHE A 133     5052   6375   4247    -84    444   -728       C  
ATOM   1106  CE2 PHE A 133      22.310  -0.537 -72.602  1.00 42.03           C  
ANISOU 1106  CE2 PHE A 133     5193   6261   4515   -162    433   -844       C  
ATOM   1107  CZ  PHE A 133      21.882   0.023 -73.799  1.00 41.35           C  
ANISOU 1107  CZ  PHE A 133     5073   6311   4324   -151    450   -822       C  
ATOM   1108  N   TYR A 134      19.533   0.030 -68.191  1.00 36.32           N  
ANISOU 1108  N   TYR A 134     4499   5457   3842   -103    308   -691       N  
ATOM   1109  CA  TYR A 134      19.248  -1.367 -67.843  1.00 35.53           C  
ANISOU 1109  CA  TYR A 134     4401   5328   3767   -176    298   -765       C  
ATOM   1110  C   TYR A 134      17.970  -1.582 -67.021  1.00 36.77           C  
ANISOU 1110  C   TYR A 134     4547   5529   3893   -194    268   -750       C  
ATOM   1111  O   TYR A 134      17.431  -2.693 -67.001  1.00 36.91           O  
ANISOU 1111  O   TYR A 134     4557   5564   3900   -264    267   -813       O  
ATOM   1112  CB  TYR A 134      20.458  -1.994 -67.132  1.00 33.82           C  
ANISOU 1112  CB  TYR A 134     4228   4954   3666   -182    302   -798       C  
ATOM   1113  CG  TYR A 134      21.705  -2.079 -68.014  1.00 33.77           C  
ANISOU 1113  CG  TYR A 134     4228   4910   3693   -180    336   -834       C  
ATOM   1114  CD1 TYR A 134      21.735  -2.916 -69.123  1.00 33.55           C  
ANISOU 1114  CD1 TYR A 134     4183   4932   3633   -235    363   -907       C  
ATOM   1115  CD2 TYR A 134      22.842  -1.318 -67.729  1.00 31.72           C  
ANISOU 1115  CD2 TYR A 134     3987   4569   3493   -128    343   -800       C  
ATOM   1116  CE1 TYR A 134      22.862  -3.013 -69.921  1.00 35.09           C  
ANISOU 1116  CE1 TYR A 134     4382   5093   3857   -234    396   -943       C  
ATOM   1117  CE2 TYR A 134      23.971  -1.391 -68.523  1.00 32.04           C  
ANISOU 1117  CE2 TYR A 134     4029   4580   3563   -128    375   -835       C  
ATOM   1118  CZ  TYR A 134      23.984  -2.252 -69.618  1.00 34.43           C  
ANISOU 1118  CZ  TYR A 134     4316   4929   3835   -179    400   -905       C  
ATOM   1119  OH  TYR A 134      25.089  -2.332 -70.439  1.00 33.29           O  
ANISOU 1119  OH  TYR A 134     4172   4759   3717   -180    435   -942       O  
ATOM   1120  N   TYR A 135      17.487  -0.537 -66.338  1.00 37.35           N  
ANISOU 1120  N   TYR A 135     4620   5616   3952   -135    249   -670       N  
ATOM   1121  CA  TYR A 135      16.310  -0.689 -65.449  1.00 38.00           C  
ANISOU 1121  CA  TYR A 135     4692   5732   4011   -148    220   -653       C  
ATOM   1122  C   TYR A 135      15.210   0.315 -65.660  1.00 39.20           C  
ANISOU 1122  C   TYR A 135     4805   6015   4071   -100    211   -585       C  
ATOM   1123  O   TYR A 135      15.460   1.465 -65.993  1.00 39.24           O  
ANISOU 1123  O   TYR A 135     4812   6038   4057    -30    226   -520       O  
ATOM   1124  CB  TYR A 135      16.720  -0.656 -63.982  1.00 35.43           C  
ANISOU 1124  CB  TYR A 135     4413   5271   3776   -129    202   -628       C  
ATOM   1125  CG  TYR A 135      17.623  -1.781 -63.612  1.00 36.99           C  
ANISOU 1125  CG  TYR A 135     4646   5348   4059   -171    207   -689       C  
ATOM   1126  CD1 TYR A 135      17.110  -2.972 -63.132  1.00 37.30           C  
ANISOU 1126  CD1 TYR A 135     4695   5365   4112   -234    201   -739       C  
ATOM   1127  CD2 TYR A 135      19.010  -1.661 -63.750  1.00 37.09           C  
ANISOU 1127  CD2 TYR A 135     4682   5268   4140   -146    223   -696       C  
ATOM   1128  CE1 TYR A 135      17.944  -4.015 -62.799  1.00 39.13           C  
ANISOU 1128  CE1 TYR A 135     4964   5481   4423   -263    214   -788       C  
ATOM   1129  CE2 TYR A 135      19.845  -2.699 -63.417  1.00 37.23           C  
ANISOU 1129  CE2 TYR A 135     4728   5180   4234   -174    230   -746       C  
ATOM   1130  CZ  TYR A 135      19.304  -3.871 -62.944  1.00 38.77           C  
ANISOU 1130  CZ  TYR A 135     4937   5350   4441   -228    227   -789       C  
ATOM   1131  OH  TYR A 135      20.131  -4.907 -62.605  1.00 42.53           O  
ANISOU 1131  OH  TYR A 135     5447   5716   4995   -245    241   -831       O  
ATOM   1132  N   LYS A 136      13.982  -0.139 -65.427  1.00 42.27           N  
ANISOU 1132  N   LYS A 136     5162   6495   4405   -138    192   -599       N  
ATOM   1133  CA  LYS A 136      12.832   0.738 -65.326  1.00 42.77           C  
ANISOU 1133  CA  LYS A 136     5186   6675   4389    -88    179   -531       C  
ATOM   1134  C   LYS A 136      12.523   0.955 -63.847  1.00 40.67           C  
ANISOU 1134  C   LYS A 136     4950   6325   4177    -70    158   -494       C  
ATOM   1135  O   LYS A 136      12.262  -0.004 -63.115  1.00 42.01           O  
ANISOU 1135  O   LYS A 136     5133   6449   4380   -133    143   -542       O  
ATOM   1136  CB  LYS A 136      11.635   0.121 -66.062  1.00 47.73           C  
ANISOU 1136  CB  LYS A 136     5746   7478   4910   -145    172   -575       C  
ATOM   1137  CG  LYS A 136      10.459   1.063 -66.321  1.00 53.26           C  
ANISOU 1137  CG  LYS A 136     6389   8342   5506    -83    163   -503       C  
ATOM   1138  CD  LYS A 136      10.850   2.263 -67.176  1.00 59.59           C  
ANISOU 1138  CD  LYS A 136     7185   9188   6267      9    185   -427       C  
ATOM   1139  CE  LYS A 136       9.716   2.697 -68.101  1.00 62.81           C  
ANISOU 1139  CE  LYS A 136     7512   9814   6536     43    182   -391       C  
ATOM   1140  NZ  LYS A 136       8.414   2.752 -67.382  1.00 65.90           N  
ANISOU 1140  NZ  LYS A 136     7863  10293   6882     48    157   -367       N  
ATOM   1141  N   PRO A 137      12.589   2.212 -63.388  1.00 39.33           N  
ANISOU 1141  N   PRO A 137     4798   6128   4017     13    163   -410       N  
ATOM   1142  CA  PRO A 137      12.163   2.509 -62.026  1.00 39.85           C  
ANISOU 1142  CA  PRO A 137     4886   6134   4120     31    145   -373       C  
ATOM   1143  C   PRO A 137      10.640   2.533 -61.913  1.00 43.26           C  
ANISOU 1143  C   PRO A 137     5265   6703   4467     29    128   -355       C  
ATOM   1144  O   PRO A 137       9.959   3.234 -62.664  1.00 46.28           O  
ANISOU 1144  O   PRO A 137     5601   7217   4762     79    137   -309       O  
ATOM   1145  CB  PRO A 137      12.749   3.895 -61.758  1.00 38.45           C  
ANISOU 1145  CB  PRO A 137     4742   5891   3973    117    168   -295       C  
ATOM   1146  CG  PRO A 137      12.933   4.508 -63.099  1.00 38.83           C  
ANISOU 1146  CG  PRO A 137     4769   6022   3962    159    197   -269       C  
ATOM   1147  CD  PRO A 137      13.125   3.394 -64.087  1.00 38.51           C  
ANISOU 1147  CD  PRO A 137     4701   6034   3896     90    192   -348       C  
ATOM   1148  N   ILE A 138      10.117   1.757 -60.982  1.00 45.38           N  
ANISOU 1148  N   ILE A 138     5538   6944   4758    -26    106   -389       N  
ATOM   1149  CA  ILE A 138       8.686   1.620 -60.811  1.00 46.98           C  
ANISOU 1149  CA  ILE A 138     5688   7275   4884    -43     90   -386       C  
ATOM   1150  C   ILE A 138       8.308   2.055 -59.391  1.00 46.77           C  
ANISOU 1150  C   ILE A 138     5690   7180   4899    -16     77   -341       C  
ATOM   1151  O   ILE A 138       8.831   1.511 -58.411  1.00 46.07           O  
ANISOU 1151  O   ILE A 138     5651   6960   4891    -53     67   -367       O  
ATOM   1152  CB  ILE A 138       8.239   0.159 -61.117  1.00 48.45           C  
ANISOU 1152  CB  ILE A 138     5849   7513   5045   -154     83   -484       C  
ATOM   1153  CG1 ILE A 138       7.541   0.081 -62.472  1.00 51.73           C  
ANISOU 1153  CG1 ILE A 138     6188   8118   5347   -170     89   -507       C  
ATOM   1154  CG2 ILE A 138       7.278  -0.368 -60.065  1.00 51.25           C  
ANISOU 1154  CG2 ILE A 138     6199   7874   5399   -202     66   -501       C  
ATOM   1155  CD1 ILE A 138       8.464   0.091 -63.658  1.00 50.56           C  
ANISOU 1155  CD1 ILE A 138     6043   7971   5194   -164    109   -526       C  
ATOM   1156  N   LYS A 139       7.444   3.065 -59.285  1.00 45.57           N  
ANISOU 1156  N   LYS A 139     5507   7116   4691     52     79   -271       N  
ATOM   1157  CA  LYS A 139       6.875   3.460 -57.990  1.00 46.33           C  
ANISOU 1157  CA  LYS A 139     5619   7171   4811     74     69   -232       C  
ATOM   1158  C   LYS A 139       5.764   2.496 -57.619  1.00 45.35           C  
ANISOU 1158  C   LYS A 139     5456   7127   4647     -2     47   -283       C  
ATOM   1159  O   LYS A 139       4.735   2.466 -58.280  1.00 45.50           O  
ANISOU 1159  O   LYS A 139     5404   7311   4571     -5     43   -286       O  
ATOM   1160  CB  LYS A 139       6.343   4.893 -58.030  1.00 47.82           C  
ANISOU 1160  CB  LYS A 139     5791   7421   4955    180     89   -138       C  
ATOM   1161  CG  LYS A 139       7.401   5.947 -58.324  1.00 49.80           C  
ANISOU 1161  CG  LYS A 139     6089   7585   5248    254    123    -86       C  
ATOM   1162  CD  LYS A 139       6.832   7.350 -58.166  1.00 55.61           C  
ANISOU 1162  CD  LYS A 139     6821   8356   5949    359    154      8       C  
ATOM   1163  CE  LYS A 139       7.699   8.397 -58.861  1.00 59.45           C  
ANISOU 1163  CE  LYS A 139     7342   8796   6447    433    201     61       C  
ATOM   1164  NZ  LYS A 139       9.022   8.582 -58.197  1.00 59.42           N  
ANISOU 1164  NZ  LYS A 139     7414   8614   6549    416    215     44       N  
ATOM   1165  N   THR A 140       5.993   1.685 -56.585  1.00 44.72           N  
ANISOU 1165  N   THR A 140     5421   6935   4635    -65     34   -324       N  
ATOM   1166  CA  THR A 140       5.014   0.688 -56.147  1.00 47.72           C  
ANISOU 1166  CA  THR A 140     5775   7369   4986   -148     20   -378       C  
ATOM   1167  C   THR A 140       3.787   1.374 -55.558  1.00 51.42           C  
ANISOU 1167  C   THR A 140     6204   7931   5403   -109     13   -328       C  
ATOM   1168  O   THR A 140       2.704   0.798 -55.531  1.00 52.97           O  
ANISOU 1168  O   THR A 140     6350   8235   5539   -165      5   -365       O  
ATOM   1169  CB  THR A 140       5.600  -0.304 -55.108  1.00 47.78           C  
ANISOU 1169  CB  THR A 140     5850   7220   5083   -215     14   -423       C  
ATOM   1170  OG1 THR A 140       5.982   0.401 -53.911  1.00 46.67           O  
ANISOU 1170  OG1 THR A 140     5758   6969   5005   -163      7   -366       O  
ATOM   1171  CG2 THR A 140       6.825  -1.038 -55.680  1.00 44.78           C  
ANISOU 1171  CG2 THR A 140     5509   6747   4758   -248     26   -472       C  
ATOM   1172  N   LEU A 141       3.978   2.619 -55.114  1.00 53.59           N  
ANISOU 1172  N   LEU A 141     6499   8163   5698    -15     21   -247       N  
ATOM   1173  CA  LEU A 141       2.930   3.445 -54.496  1.00 56.23           C  
ANISOU 1173  CA  LEU A 141     6805   8567   5993     40     21   -189       C  
ATOM   1174  C   LEU A 141       2.691   3.046 -53.041  1.00 57.38           C  
ANISOU 1174  C   LEU A 141     6989   8623   6191     -4      8   -203       C  
ATOM   1175  O   LEU A 141       1.990   3.741 -52.296  1.00 59.82           O  
ANISOU 1175  O   LEU A 141     7289   8953   6487     38     11   -155       O  
ATOM   1176  CB  LEU A 141       1.617   3.456 -55.317  1.00 58.26           C  
ANISOU 1176  CB  LEU A 141     6965   9036   6132     46     18   -188       C  
ATOM   1177  CG  LEU A 141       1.635   4.023 -56.756  1.00 58.76           C  
ANISOU 1177  CG  LEU A 141     6979   9224   6123    108     31   -156       C  
ATOM   1178  CD1 LEU A 141       0.243   3.974 -57.367  1.00 62.57           C  
ANISOU 1178  CD1 LEU A 141     7358   9930   6484    111     22   -157       C  
ATOM   1179  CD2 LEU A 141       2.185   5.443 -56.822  1.00 57.24           C  
ANISOU 1179  CD2 LEU A 141     6822   8973   5954    229     60    -62       C  
ATOM   1180  N   ASN A 142       3.295   1.937 -52.636  1.00 52.04           N  
ANISOU 1180  N   ASN A 142     6356   7842   5572    -87     -1   -265       N  
ATOM   1181  CA  ASN A 142       3.468   1.664 -51.229  1.00 52.53           C  
ANISOU 1181  CA  ASN A 142     6474   7784   5700   -115    -11   -266       C  
ATOM   1182  C   ASN A 142       4.497   2.617 -50.610  1.00 50.50           C  
ANISOU 1182  C   ASN A 142     6275   7399   5514    -47     -3   -213       C  
ATOM   1183  O   ASN A 142       5.714   2.356 -50.613  1.00 48.72           O  
ANISOU 1183  O   ASN A 142     6096   7061   5352    -56     -4   -229       O  
ATOM   1184  CB  ASN A 142       3.854   0.210 -50.995  1.00 54.87           C  
ANISOU 1184  CB  ASN A 142     6805   8004   6037   -213    -18   -340       C  
ATOM   1185  CG  ASN A 142       3.424  -0.280 -49.632  1.00 59.68           C  
ANISOU 1185  CG  ASN A 142     7447   8553   6676   -258    -27   -348       C  
ATOM   1186  OD1 ASN A 142       3.464   0.471 -48.649  1.00 59.38           O  
ANISOU 1186  OD1 ASN A 142     7433   8461   6665   -212    -32   -298       O  
ATOM   1187  ND2 ASN A 142       2.999  -1.540 -49.561  1.00 61.20           N  
ANISOU 1187  ND2 ASN A 142     7641   8753   6859   -351    -24   -412       N  
ATOM   1188  N   GLY A 143       3.995   3.724 -50.074  1.00 47.47           N  
ANISOU 1188  N   GLY A 143     5885   7034   5115     17      6   -152       N  
ATOM   1189  CA  GLY A 143       4.843   4.827 -49.670  1.00 45.66           C  
ANISOU 1189  CA  GLY A 143     5703   6707   4938     84     26   -102       C  
ATOM   1190  C   GLY A 143       5.684   5.327 -50.837  1.00 43.66           C  
ANISOU 1190  C   GLY A 143     5450   6452   4684    130     46    -88       C  
ATOM   1191  O   GLY A 143       5.210   5.437 -51.949  1.00 45.56           O  
ANISOU 1191  O   GLY A 143     5642   6807   4861    153     54    -81       O  
ATOM   1192  N   HIS A 144       6.943   5.614 -50.571  1.00 43.09           N  
ANISOU 1192  N   HIS A 144     5431   6258   4683    140     55    -86       N  
ATOM   1193  CA  HIS A 144       7.831   6.183 -51.569  1.00 43.21           C  
ANISOU 1193  CA  HIS A 144     5455   6258   4706    183     80    -72       C  
ATOM   1194  C   HIS A 144       8.739   5.132 -52.165  1.00 43.77           C  
ANISOU 1194  C   HIS A 144     5533   6291   4806    128     63   -132       C  
ATOM   1195  O   HIS A 144       9.703   5.449 -52.861  1.00 47.10           O  
ANISOU 1195  O   HIS A 144     5969   6676   5250    150     81   -131       O  
ATOM   1196  CB  HIS A 144       8.600   7.350 -50.965  1.00 40.19           C  
ANISOU 1196  CB  HIS A 144     5121   5774   4373    232    112    -31       C  
ATOM   1197  CG  HIS A 144       7.706   8.402 -50.350  1.00 39.29           C  
ANISOU 1197  CG  HIS A 144     5006   5686   4234    288    139     25       C  
ATOM   1198  ND1 HIS A 144       7.426   8.440 -49.027  1.00 40.69           N  
ANISOU 1198  ND1 HIS A 144     5205   5814   4438    268    130     25       N  
ATOM   1199  CD2 HIS A 144       6.976   9.439 -50.932  1.00 40.34           C  
ANISOU 1199  CD2 HIS A 144     5116   5897   4311    368    178     87       C  
ATOM   1200  CE1 HIS A 144       6.586   9.466 -48.775  1.00 39.80           C  
ANISOU 1200  CE1 HIS A 144     5087   5740   4295    329    164     80       C  
ATOM   1201  NE2 HIS A 144       6.311  10.076 -49.939  1.00 38.48           N  
ANISOU 1201  NE2 HIS A 144     4892   5649   4077    395    195    120       N  
ATOM   1202  N   GLU A 145       8.393   3.865 -51.940  1.00 43.36           N  
ANISOU 1202  N   GLU A 145     5471   6249   4752     55     34   -184       N  
ATOM   1203  CA  GLU A 145       9.170   2.748 -52.450  1.00 43.22           C  
ANISOU 1203  CA  GLU A 145     5464   6192   4765      0     25   -245       C  
ATOM   1204  C   GLU A 145       9.348   2.814 -53.962  1.00 43.47           C  
ANISOU 1204  C   GLU A 145     5462   6299   4754     14     41   -256       C  
ATOM   1205  O   GLU A 145       8.384   3.015 -54.696  1.00 43.20           O  
ANISOU 1205  O   GLU A 145     5376   6394   4641     26     46   -245       O  
ATOM   1206  CB  GLU A 145       8.533   1.412 -52.059  1.00 43.93           C  
ANISOU 1206  CB  GLU A 145     5548   6294   4847    -79      5   -297       C  
ATOM   1207  CG  GLU A 145       9.228   0.200 -52.679  1.00 45.90           C  
ANISOU 1207  CG  GLU A 145     5810   6504   5123   -137      6   -362       C  
ATOM   1208  CD  GLU A 145       8.542  -1.124 -52.362  1.00 48.53           C  
ANISOU 1208  CD  GLU A 145     6145   6847   5447   -221      1   -418       C  
ATOM   1209  OE1 GLU A 145       9.247  -2.073 -51.976  1.00 52.04           O  
ANISOU 1209  OE1 GLU A 145     6633   7189   5951   -258      2   -452       O  
ATOM   1210  OE2 GLU A 145       7.303  -1.230 -52.509  1.00 49.05           O  
ANISOU 1210  OE2 GLU A 145     6166   7023   5445   -249      0   -427       O  
ATOM   1211  N   ILE A 146      10.594   2.654 -54.415  1.00 41.80           N  
ANISOU 1211  N   ILE A 146     5277   6013   4591     13     49   -277       N  
ATOM   1212  CA  ILE A 146      10.873   2.435 -55.822  1.00 39.98           C  
ANISOU 1212  CA  ILE A 146     5020   5843   4327      8     63   -303       C  
ATOM   1213  C   ILE A 146      11.463   1.041 -56.020  1.00 40.90           C  
ANISOU 1213  C   ILE A 146     5150   5906   4481    -63     56   -378       C  
ATOM   1214  O   ILE A 146      12.311   0.599 -55.246  1.00 39.60           O  
ANISOU 1214  O   ILE A 146     5030   5623   4391    -77     48   -393       O  
ATOM   1215  CB  ILE A 146      11.806   3.518 -56.407  1.00 39.52           C  
ANISOU 1215  CB  ILE A 146     4977   5754   4285     73     91   -265       C  
ATOM   1216  CG1 ILE A 146      11.071   4.863 -56.469  1.00 35.97           C  
ANISOU 1216  CG1 ILE A 146     4510   5371   3783    148    112   -190       C  
ATOM   1217  CG2 ILE A 146      12.293   3.122 -57.810  1.00 39.24           C  
ANISOU 1217  CG2 ILE A 146     4920   5762   4225     58    104   -301       C  
ATOM   1218  CD1 ILE A 146      11.976   6.055 -56.612  1.00 33.28           C  
ANISOU 1218  CD1 ILE A 146     4204   4965   3475    210    149   -145       C  
ATOM   1219  N   LYS A 147      10.960   0.339 -57.030  1.00 40.93           N  
ANISOU 1219  N   LYS A 147     5117   6004   4429   -107     61   -424       N  
ATOM   1220  CA  LYS A 147      11.513  -0.940 -57.435  1.00 42.01           C  
ANISOU 1220  CA  LYS A 147     5268   6096   4596   -174     68   -499       C  
ATOM   1221  C   LYS A 147      12.156  -0.798 -58.820  1.00 40.80           C  
ANISOU 1221  C   LYS A 147     5097   5982   4422   -163     89   -517       C  
ATOM   1222  O   LYS A 147      11.644  -0.073 -59.695  1.00 37.63           O  
ANISOU 1222  O   LYS A 147     4651   5699   3946   -130     96   -490       O  
ATOM   1223  CB  LYS A 147      10.425  -2.009 -57.442  1.00 47.35           C  
ANISOU 1223  CB  LYS A 147     5921   6840   5227   -255     66   -554       C  
ATOM   1224  CG  LYS A 147      10.827  -3.313 -56.767  1.00 52.23           C  
ANISOU 1224  CG  LYS A 147     6588   7343   5913   -319     71   -607       C  
ATOM   1225  CD  LYS A 147       9.616  -4.000 -56.136  1.00 58.71           C  
ANISOU 1225  CD  LYS A 147     7401   8205   6701   -383     67   -633       C  
ATOM   1226  CE  LYS A 147      10.033  -4.976 -55.029  1.00 60.95           C  
ANISOU 1226  CE  LYS A 147     7749   8346   7062   -419     71   -652       C  
ATOM   1227  NZ  LYS A 147       9.153  -4.865 -53.826  1.00 58.67           N  
ANISOU 1227  NZ  LYS A 147     7466   8058   6764   -426     53   -622       N  
ATOM   1228  N   PHE A 148      13.312  -1.430 -58.992  1.00 38.06           N  
ANISOU 1228  N   PHE A 148     4783   5537   4141   -182    100   -557       N  
ATOM   1229  CA  PHE A 148      14.020  -1.364 -60.260  1.00 36.44           C  
ANISOU 1229  CA  PHE A 148     4565   5357   3923   -175    122   -581       C  
ATOM   1230  C   PHE A 148      13.875  -2.677 -60.976  1.00 37.51           C  
ANISOU 1230  C   PHE A 148     4689   5519   4041   -257    138   -665       C  
ATOM   1231  O   PHE A 148      14.400  -3.698 -60.522  1.00 36.70           O  
ANISOU 1231  O   PHE A 148     4626   5313   4004   -297    146   -710       O  
ATOM   1232  CB  PHE A 148      15.498  -1.022 -60.056  1.00 35.51           C  
ANISOU 1232  CB  PHE A 148     4486   5118   3888   -135    130   -567       C  
ATOM   1233  CG  PHE A 148      15.748   0.424 -59.688  1.00 33.90           C  
ANISOU 1233  CG  PHE A 148     4288   4900   3689    -59    130   -492       C  
ATOM   1234  CD1 PHE A 148      15.568   1.442 -60.628  1.00 32.87           C  
ANISOU 1234  CD1 PHE A 148     4133   4856   3500    -14    149   -453       C  
ATOM   1235  CD2 PHE A 148      16.178   0.763 -58.408  1.00 32.20           C  
ANISOU 1235  CD2 PHE A 148     4108   4587   3537    -36    116   -461       C  
ATOM   1236  CE1 PHE A 148      15.795   2.765 -60.289  1.00 32.82           C  
ANISOU 1236  CE1 PHE A 148     4141   4825   3501     52    161   -385       C  
ATOM   1237  CE2 PHE A 148      16.410   2.087 -58.063  1.00 31.30           C  
ANISOU 1237  CE2 PHE A 148     4005   4458   3429     23    125   -401       C  
ATOM   1238  CZ  PHE A 148      16.230   3.091 -59.009  1.00 31.87           C  
ANISOU 1238  CZ  PHE A 148     4057   4602   3447     67    151   -364       C  
ATOM   1239  N   ILE A 149      13.133  -2.644 -62.086  1.00 38.12           N  
ANISOU 1239  N   ILE A 149     4714   5740   4027   -279    148   -687       N  
ATOM   1240  CA  ILE A 149      12.845  -3.831 -62.881  1.00 41.45           C  
ANISOU 1240  CA  ILE A 149     5118   6213   4416   -368    169   -776       C  
ATOM   1241  C   ILE A 149      13.766  -3.835 -64.097  1.00 42.69           C  
ANISOU 1241  C   ILE A 149     5271   6377   4572   -364    195   -805       C  
ATOM   1242  O   ILE A 149      13.975  -2.792 -64.718  1.00 41.43           O  
ANISOU 1242  O   ILE A 149     5088   6274   4376   -301    194   -755       O  
ATOM   1243  CB  ILE A 149      11.364  -3.843 -63.350  1.00 42.07           C  
ANISOU 1243  CB  ILE A 149     5131   6472   4382   -407    162   -790       C  
ATOM   1244  CG1 ILE A 149      10.422  -3.588 -62.168  1.00 42.58           C  
ANISOU 1244  CG1 ILE A 149     5194   6544   4441   -396    136   -748       C  
ATOM   1245  CG2 ILE A 149      11.013  -5.155 -64.041  1.00 42.64           C  
ANISOU 1245  CG2 ILE A 149     5187   6594   4421   -517    190   -896       C  
ATOM   1246  CD1 ILE A 149      10.585  -4.563 -61.019  1.00 42.24           C  
ANISOU 1246  CD1 ILE A 149     5208   6363   4478   -446    138   -781       C  
ATOM   1247  N   ARG A 150      14.340  -4.996 -64.415  1.00 46.33           N  
ANISOU 1247  N   ARG A 150     5757   6771   5075   -427    223   -885       N  
ATOM   1248  CA  ARG A 150      15.169  -5.128 -65.617  1.00 50.92           C  
ANISOU 1248  CA  ARG A 150     6332   7363   5652   -434    252   -925       C  
ATOM   1249  C   ARG A 150      14.358  -4.699 -66.827  1.00 52.98           C  
ANISOU 1249  C   ARG A 150     6525   7811   5792   -447    254   -930       C  
ATOM   1250  O   ARG A 150      13.195  -5.086 -66.975  1.00 55.16           O  
ANISOU 1250  O   ARG A 150     6761   8204   5993   -503    250   -963       O  
ATOM   1251  CB  ARG A 150      15.685  -6.554 -65.783  1.00 54.88           C  
ANISOU 1251  CB  ARG A 150     6868   7776   6207   -509    289  -1017       C  
ATOM   1252  CG  ARG A 150      16.696  -6.962 -64.724  1.00 61.27           C  
ANISOU 1252  CG  ARG A 150     7742   8402   7136   -480    291  -1004       C  
ATOM   1253  CD  ARG A 150      17.620  -8.070 -65.206  1.00 70.15           C  
ANISOU 1253  CD  ARG A 150     8900   9434   8319   -520    337  -1080       C  
ATOM   1254  NE  ARG A 150      18.411  -7.659 -66.373  1.00 78.59           N  
ANISOU 1254  NE  ARG A 150     9948  10539   9373   -499    355  -1093       N  
ATOM   1255  CZ  ARG A 150      19.366  -8.397 -66.940  1.00 82.12           C  
ANISOU 1255  CZ  ARG A 150    10417  10914   9869   -519    396  -1151       C  
ATOM   1256  NH1 ARG A 150      19.675  -9.592 -66.451  1.00 84.48           N  
ANISOU 1256  NH1 ARG A 150    10763  11095  10237   -553    427  -1199       N  
ATOM   1257  NH2 ARG A 150      20.019  -7.935 -67.999  1.00 86.38           N  
ANISOU 1257  NH2 ARG A 150    10933  11496  10388   -500    410  -1160       N  
ATOM   1258  N   LYS A 151      14.957  -3.858 -67.662  1.00 53.15           N  
ANISOU 1258  N   LYS A 151     6532   7869   5792   -391    260   -896       N  
ATOM   1259  CA  LYS A 151      14.240  -3.196 -68.744  1.00 56.31           C  
ANISOU 1259  CA  LYS A 151     6868   8451   6073   -376    259   -874       C  
ATOM   1260  C   LYS A 151      13.606  -4.182 -69.734  1.00 58.85           C  
ANISOU 1260  C   LYS A 151     7145   8900   6314   -474    279   -969       C  
ATOM   1261  O   LYS A 151      12.485  -3.968 -70.180  1.00 61.04           O  
ANISOU 1261  O   LYS A 151     7358   9350   6482   -488    266   -964       O  
ATOM   1262  CB  LYS A 151      15.167  -2.219 -69.467  1.00 57.84           C  
ANISOU 1262  CB  LYS A 151     7069   8638   6269   -303    273   -824       C  
ATOM   1263  CG  LYS A 151      14.462  -1.090 -70.195  1.00 59.60           C  
ANISOU 1263  CG  LYS A 151     7240   9022   6382   -240    267   -752       C  
ATOM   1264  CD  LYS A 151      15.301   0.177 -70.124  1.00 60.81           C  
ANISOU 1264  CD  LYS A 151     7427   9103   6574   -142    277   -665       C  
ATOM   1265  CE  LYS A 151      14.960   1.152 -71.240  1.00 62.85           C  
ANISOU 1265  CE  LYS A 151     7645   9508   6726    -83    291   -605       C  
ATOM   1266  NZ  LYS A 151      15.468   2.513 -70.913  1.00 61.87           N  
ANISOU 1266  NZ  LYS A 151     7558   9313   6635     16    306   -506       N  
ATOM   1267  N   GLU A 152      14.312  -5.265 -70.055  1.00 60.44           N  
ANISOU 1267  N   GLU A 152     7377   9019   6567   -544    312  -1058       N  
ATOM   1268  CA  GLU A 152      13.782  -6.271 -70.993  1.00 64.85           C  
ANISOU 1268  CA  GLU A 152     7898   9686   7055   -651    342  -1163       C  
ATOM   1269  C   GLU A 152      12.565  -7.000 -70.422  1.00 63.60           C  
ANISOU 1269  C   GLU A 152     7720   9582   6861   -730    336  -1208       C  
ATOM   1270  O   GLU A 152      11.631  -7.326 -71.156  1.00 62.82           O  
ANISOU 1270  O   GLU A 152     7560   9652   6656   -800    343  -1263       O  
ATOM   1271  CB  GLU A 152      14.866  -7.265 -71.479  1.00 66.77           C  
ANISOU 1271  CB  GLU A 152     8186   9816   7368   -706    390  -1250       C  
ATOM   1272  CG  GLU A 152      15.841  -7.764 -70.410  1.00 75.06           C  
ANISOU 1272  CG  GLU A 152     9315  10645   8560   -686    400  -1247       C  
ATOM   1273  CD  GLU A 152      16.965  -6.773 -70.109  1.00 79.46           C  
ANISOU 1273  CD  GLU A 152     9900  11105   9186   -579    382  -1163       C  
ATOM   1274  OE1 GLU A 152      17.473  -6.127 -71.054  1.00 85.81           O  
ANISOU 1274  OE1 GLU A 152    10683  11965   9956   -544    390  -1147       O  
ATOM   1275  OE2 GLU A 152      17.345  -6.638 -68.924  1.00 80.18           O  
ANISOU 1275  OE2 GLU A 152    10034  11069   9361   -533    363  -1116       O  
ATOM   1276  N   GLU A 153      12.572  -7.232 -69.110  1.00 62.16           N  
ANISOU 1276  N   GLU A 153     7589   9266   6763   -719    324  -1184       N  
ATOM   1277  CA  GLU A 153      11.440  -7.866 -68.433  1.00 63.76           C  
ANISOU 1277  CA  GLU A 153     7780   9505   6939   -789    321  -1219       C  
ATOM   1278  C   GLU A 153      10.226  -6.956 -68.445  1.00 61.16           C  
ANISOU 1278  C   GLU A 153     7377   9356   6503   -754    280  -1159       C  
ATOM   1279  O   GLU A 153       9.098  -7.407 -68.673  1.00 61.32           O  
ANISOU 1279  O   GLU A 153     7343   9517   6438   -831    283  -1213       O  
ATOM   1280  CB  GLU A 153      11.799  -8.233 -66.996  1.00 66.80           C  
ANISOU 1280  CB  GLU A 153     8239   9701   7438   -773    316  -1195       C  
ATOM   1281  CG  GLU A 153      12.672  -9.468 -66.876  1.00 74.20           C  
ANISOU 1281  CG  GLU A 153     9246  10475   8469   -829    366  -1270       C  
ATOM   1282  CD  GLU A 153      13.143  -9.718 -65.456  1.00 79.71           C  
ANISOU 1282  CD  GLU A 153    10016  10991   9278   -792    358  -1229       C  
ATOM   1283  OE1 GLU A 153      12.365  -9.446 -64.509  1.00 84.26           O  
ANISOU 1283  OE1 GLU A 153    10588  11581   9844   -781    327  -1185       O  
ATOM   1284  OE2 GLU A 153      14.291 -10.194 -65.288  1.00 80.14           O  
ANISOU 1284  OE2 GLU A 153    10127  10895   9426   -772    382  -1239       O  
ATOM   1285  N   TYR A 154      10.464  -5.670 -68.211  1.00 57.23           N  
ANISOU 1285  N   TYR A 154     6876   8857   6010   -638    247  -1050       N  
ATOM   1286  CA  TYR A 154       9.392  -4.706 -68.183  1.00 55.30           C  
ANISOU 1286  CA  TYR A 154     6568   8771   5673   -583    214   -979       C  
ATOM   1287  C   TYR A 154       8.778  -4.536 -69.562  1.00 56.30           C  
ANISOU 1287  C   TYR A 154     6609   9117   5664   -603    218  -1002       C  
ATOM   1288  O   TYR A 154       7.554  -4.515 -69.698  1.00 57.42           O  
ANISOU 1288  O   TYR A 154     6679   9431   5705   -630    203  -1009       O  
ATOM   1289  CB  TYR A 154       9.859  -3.354 -67.644  1.00 53.29           C  
ANISOU 1289  CB  TYR A 154     6339   8448   5459   -453    191   -858       C  
ATOM   1290  CG  TYR A 154       8.831  -2.273 -67.855  1.00 54.76           C  
ANISOU 1290  CG  TYR A 154     6458   8805   5541   -382    167   -778       C  
ATOM   1291  CD1 TYR A 154       7.700  -2.196 -67.041  1.00 56.02           C  
ANISOU 1291  CD1 TYR A 154     6589   9024   5670   -385    144   -756       C  
ATOM   1292  CD2 TYR A 154       8.956  -1.360 -68.899  1.00 55.51           C  
ANISOU 1292  CD2 TYR A 154     6516   9008   5564   -311    172   -724       C  
ATOM   1293  CE1 TYR A 154       6.730  -1.230 -67.249  1.00 58.39           C  
ANISOU 1293  CE1 TYR A 154     6823   9488   5872   -314    126   -681       C  
ATOM   1294  CE2 TYR A 154       7.996  -0.384 -69.113  1.00 59.35           C  
ANISOU 1294  CE2 TYR A 154     6942   9655   5953   -236    156   -643       C  
ATOM   1295  CZ  TYR A 154       6.881  -0.324 -68.284  1.00 61.58           C  
ANISOU 1295  CZ  TYR A 154     7194   9996   6207   -235    133   -622       C  
ATOM   1296  OH  TYR A 154       5.917   0.645 -68.487  1.00 63.54           O  
ANISOU 1296  OH  TYR A 154     7378  10405   6357   -151    119   -539       O  
ATOM   1297  N   ILE A 155       9.624  -4.397 -70.579  1.00 56.31           N  
ANISOU 1297  N   ILE A 155     6613   9120   5659   -588    238  -1013       N  
ATOM   1298  CA  ILE A 155       9.142  -4.225 -71.945  1.00 58.16           C  
ANISOU 1298  CA  ILE A 155     6769   9568   5762   -604    243  -1033       C  
ATOM   1299  C   ILE A 155       8.320  -5.429 -72.409  1.00 60.63           C  
ANISOU 1299  C   ILE A 155     7031  10002   6002   -743    261  -1157       C  
ATOM   1300  O   ILE A 155       7.269  -5.270 -73.035  1.00 62.61           O  
ANISOU 1300  O   ILE A 155     7191  10475   6120   -763    248  -1165       O  
ATOM   1301  CB  ILE A 155      10.290  -3.917 -72.924  1.00 57.38           C  
ANISOU 1301  CB  ILE A 155     6691   9433   5677   -569    267  -1027       C  
ATOM   1302  CG1 ILE A 155      10.806  -2.496 -72.669  1.00 54.90           C  
ANISOU 1302  CG1 ILE A 155     6403   9062   5392   -429    252   -897       C  
ATOM   1303  CG2 ILE A 155       9.829  -4.091 -74.375  1.00 55.81           C  
ANISOU 1303  CG2 ILE A 155     6413   9450   5342   -617    279  -1078       C  
ATOM   1304  CD1 ILE A 155      12.045  -2.137 -73.454  1.00 55.16           C  
ANISOU 1304  CD1 ILE A 155     6469   9030   5458   -391    279   -886       C  
ATOM   1305  N   SER A 156       8.793  -6.626 -72.070  1.00 61.15           N  
ANISOU 1305  N   SER A 156     7155   9924   6153   -839    295  -1252       N  
ATOM   1306  CA  SER A 156       8.063  -7.856 -72.340  1.00 63.22           C  
ANISOU 1306  CA  SER A 156     7388  10266   6366   -984    325  -1379       C  
ATOM   1307  C   SER A 156       6.680  -7.810 -71.681  1.00 66.46           C  
ANISOU 1307  C   SER A 156     7744  10794   6711  -1008    298  -1369       C  
ATOM   1308  O   SER A 156       5.655  -8.014 -72.344  1.00 70.99           O  
ANISOU 1308  O   SER A 156     8229  11584   7158  -1076    297  -1422       O  
ATOM   1309  CB  SER A 156       8.880  -9.063 -71.861  1.00 62.80           C  
ANISOU 1309  CB  SER A 156     7427   9995   6438  -1061    374  -1462       C  
ATOM   1310  OG  SER A 156       8.054 -10.117 -71.407  1.00 65.92           O  
ANISOU 1310  OG  SER A 156     7823  10399   6824  -1179    400  -1552       O  
ATOM   1311  N   PHE A 157       6.661  -7.510 -70.382  1.00 67.42           N  
ANISOU 1311  N   PHE A 157     7915  10784   6916   -952    275  -1301       N  
ATOM   1312  CA  PHE A 157       5.422  -7.302 -69.637  1.00 64.89           C  
ANISOU 1312  CA  PHE A 157     7549  10559   6544   -954    246  -1274       C  
ATOM   1313  C   PHE A 157       4.553  -6.225 -70.302  1.00 65.53           C  
ANISOU 1313  C   PHE A 157     7525  10882   6488   -881    209  -1203       C  
ATOM   1314  O   PHE A 157       3.353  -6.420 -70.502  1.00 64.92           O  
ANISOU 1314  O   PHE A 157     7363  10997   6303   -938    200  -1241       O  
ATOM   1315  CB  PHE A 157       5.739  -6.933 -68.175  1.00 63.74           C  
ANISOU 1315  CB  PHE A 157     7478  10224   6515   -881    225  -1193       C  
ATOM   1316  CG  PHE A 157       4.579  -6.326 -67.431  1.00 63.26           C  
ANISOU 1316  CG  PHE A 157     7369  10263   6402   -843    188  -1132       C  
ATOM   1317  CD1 PHE A 157       4.342  -4.949 -67.478  1.00 62.77           C  
ANISOU 1317  CD1 PHE A 157     7267  10286   6294   -714    152  -1014       C  
ATOM   1318  CD2 PHE A 157       3.724  -7.122 -66.682  1.00 64.53           C  
ANISOU 1318  CD2 PHE A 157     7527  10428   6561   -935    197  -1190       C  
ATOM   1319  CE1 PHE A 157       3.269  -4.387 -66.809  1.00 61.55           C  
ANISOU 1319  CE1 PHE A 157     7067  10225   6092   -674    123   -958       C  
ATOM   1320  CE2 PHE A 157       2.652  -6.564 -66.004  1.00 65.21           C  
ANISOU 1320  CE2 PHE A 157     7566  10611   6600   -900    164  -1136       C  
ATOM   1321  CZ  PHE A 157       2.425  -5.196 -66.070  1.00 64.33           C  
ANISOU 1321  CZ  PHE A 157     7411  10588   6442   -767    127  -1020       C  
ATOM   1322  N   GLU A 158       5.174  -5.099 -70.653  1.00 65.39           N  
ANISOU 1322  N   GLU A 158     7514  10855   6474   -755    191  -1101       N  
ATOM   1323  CA  GLU A 158       4.462  -3.955 -71.226  1.00 66.50           C  
ANISOU 1323  CA  GLU A 158     7570  11201   6496   -658    162  -1011       C  
ATOM   1324  C   GLU A 158       3.810  -4.330 -72.558  1.00 69.13           C  
ANISOU 1324  C   GLU A 158     7802  11782   6680   -730    169  -1083       C  
ATOM   1325  O   GLU A 158       2.700  -3.893 -72.855  1.00 69.54           O  
ANISOU 1325  O   GLU A 158     7757  12056   6608   -706    145  -1053       O  
ATOM   1326  CB  GLU A 158       5.422  -2.774 -71.413  1.00 66.24           C  
ANISOU 1326  CB  GLU A 158     7580  11080   6505   -520    158   -898       C  
ATOM   1327  CG  GLU A 158       4.766  -1.451 -71.786  1.00 67.86           C  
ANISOU 1327  CG  GLU A 158     7720  11453   6609   -393    135   -779       C  
ATOM   1328  CD  GLU A 158       5.747  -0.465 -72.406  1.00 70.14           C  
ANISOU 1328  CD  GLU A 158     8045  11689   6915   -285    149   -695       C  
ATOM   1329  OE1 GLU A 158       5.350   0.682 -72.693  1.00 72.45           O  
ANISOU 1329  OE1 GLU A 158     8301  12088   7137   -168    141   -586       O  
ATOM   1330  OE2 GLU A 158       6.918  -0.836 -72.616  1.00 71.94           O  
ANISOU 1330  OE2 GLU A 158     8338  11768   7226   -315    173   -736       O  
ATOM   1331  N   SER A 159       4.506  -5.145 -73.348  1.00 68.86           N  
ANISOU 1331  N   SER A 159     7789  11715   6659   -818    204  -1179       N  
ATOM   1332  CA  SER A 159       3.992  -5.588 -74.637  1.00 71.73           C  
ANISOU 1332  CA  SER A 159     8062  12307   6884   -901    217  -1263       C  
ATOM   1333  C   SER A 159       2.862  -6.597 -74.471  1.00 72.48           C  
ANISOU 1333  C   SER A 159     8098  12525   6914  -1043    226  -1376       C  
ATOM   1334  O   SER A 159       1.845  -6.515 -75.160  1.00 71.31           O  
ANISOU 1334  O   SER A 159     7836  12639   6616  -1073    211  -1399       O  
ATOM   1335  CB  SER A 159       5.114  -6.172 -75.499  1.00 70.53           C  
ANISOU 1335  CB  SER A 159     7957  12070   6772   -956    259  -1337       C  
ATOM   1336  OG  SER A 159       5.908  -5.139 -76.058  1.00 71.33           O  
ANISOU 1336  OG  SER A 159     8073  12152   6874   -833    250  -1239       O  
ATOM   1337  N   LYS A 160       3.049  -7.534 -73.543  1.00 72.69           N  
ANISOU 1337  N   LYS A 160     8201  12365   7052  -1129    253  -1446       N  
ATOM   1338  CA  LYS A 160       2.074  -8.589 -73.269  1.00 75.23           C  
ANISOU 1338  CA  LYS A 160     8487  12763   7332  -1277    275  -1562       C  
ATOM   1339  C   LYS A 160       0.721  -8.022 -72.804  1.00 76.35           C  
ANISOU 1339  C   LYS A 160     8539  13090   7381  -1243    231  -1509       C  
ATOM   1340  O   LYS A 160      -0.328  -8.608 -73.067  1.00 80.27           O  
ANISOU 1340  O   LYS A 160     8951  13772   7773  -1355    240  -1599       O  
ATOM   1341  CB  LYS A 160       2.649  -9.572 -72.238  1.00 75.20           C  
ANISOU 1341  CB  LYS A 160     8602  12490   7481  -1347    315  -1620       C  
ATOM   1342  CG  LYS A 160       1.690 -10.643 -71.741  1.00 78.45           C  
ANISOU 1342  CG  LYS A 160     8999  12936   7872  -1495    346  -1730       C  
ATOM   1343  CD  LYS A 160       2.183 -11.233 -70.428  1.00 81.20           C  
ANISOU 1343  CD  LYS A 160     9467  13009   8374  -1508    371  -1729       C  
ATOM   1344  CE  LYS A 160       1.030 -11.521 -69.479  1.00 83.61           C  
ANISOU 1344  CE  LYS A 160     9749  13359   8658  -1566    365  -1748       C  
ATOM   1345  NZ  LYS A 160       1.438 -11.354 -68.055  1.00 80.54           N  
ANISOU 1345  NZ  LYS A 160     9457  12742   8402  -1493    352  -1666       N  
ATOM   1346  N   VAL A 161       0.756  -6.876 -72.129  1.00 76.19           N  
ANISOU 1346  N   VAL A 161     8533  13020   7395  -1091    188  -1367       N  
ATOM   1347  CA  VAL A 161      -0.462  -6.193 -71.680  1.00 75.41           C  
ANISOU 1347  CA  VAL A 161     8350  13087   7212  -1034    148  -1299       C  
ATOM   1348  C   VAL A 161      -1.042  -5.357 -72.825  1.00 77.09           C  
ANISOU 1348  C   VAL A 161     8443  13582   7265   -961    120  -1245       C  
ATOM   1349  O   VAL A 161      -2.265  -5.262 -72.985  1.00 78.37           O  
ANISOU 1349  O   VAL A 161     8492  13982   7300   -979     99  -1254       O  
ATOM   1350  CB  VAL A 161      -0.192  -5.309 -70.429  1.00 72.70           C  
ANISOU 1350  CB  VAL A 161     8078  12565   6977   -901    121  -1170       C  
ATOM   1351  CG1 VAL A 161      -1.358  -4.367 -70.145  1.00 69.99           C  
ANISOU 1351  CG1 VAL A 161     7645  12406   6540   -810     81  -1079       C  
ATOM   1352  CG2 VAL A 161       0.105  -6.177 -69.211  1.00 70.13           C  
ANISOU 1352  CG2 VAL A 161     7852  12008   6785   -979    143  -1223       C  
ATOM   1353  N   PHE A 162      -0.150  -4.770 -73.620  1.00 77.06           N  
ANISOU 1353  N   PHE A 162     8462  13552   7263   -878    122  -1189       N  
ATOM   1354  CA  PHE A 162      -0.521  -3.975 -74.792  1.00 81.07           C  
ANISOU 1354  CA  PHE A 162     8869  14309   7623   -800    103  -1130       C  
ATOM   1355  C   PHE A 162      -1.367  -4.771 -75.794  1.00 84.36           C  
ANISOU 1355  C   PHE A 162     9167  14997   7886   -934    110  -1253       C  
ATOM   1356  O   PHE A 162      -2.317  -4.237 -76.376  1.00 83.61           O  
ANISOU 1356  O   PHE A 162     8951  15178   7639   -888     82  -1213       O  
ATOM   1357  CB  PHE A 162       0.742  -3.425 -75.466  1.00 80.25           C  
ANISOU 1357  CB  PHE A 162     8830  14095   7566   -716    117  -1072       C  
ATOM   1358  CG  PHE A 162       0.498  -2.757 -76.792  1.00 82.65           C  
ANISOU 1358  CG  PHE A 162     9040  14643   7718   -650    106  -1023       C  
ATOM   1359  CD1 PHE A 162      -0.316  -1.633 -76.888  1.00 82.74           C  
ANISOU 1359  CD1 PHE A 162     8973  14835   7627   -513     74   -896       C  
ATOM   1360  CD2 PHE A 162       1.119  -3.233 -77.947  1.00 84.81           C  
ANISOU 1360  CD2 PHE A 162     9308  14961   7952   -718    132  -1098       C  
ATOM   1361  CE1 PHE A 162      -0.520  -1.011 -78.109  1.00 84.64           C  
ANISOU 1361  CE1 PHE A 162     9132  15302   7725   -442     67   -842       C  
ATOM   1362  CE2 PHE A 162       0.916  -2.616 -79.173  1.00 84.53           C  
ANISOU 1362  CE2 PHE A 162     9189  15155   7773   -655    123  -1050       C  
ATOM   1363  CZ  PHE A 162       0.099  -1.503 -79.254  1.00 85.79           C  
ANISOU 1363  CZ  PHE A 162     9271  15496   7828   -514     89   -918       C  
ATOM   1364  N   HIS A 163      -1.021  -6.044 -75.982  1.00 87.05           N  
ANISOU 1364  N   HIS A 163     9545  15264   8266  -1100    152  -1404       N  
ATOM   1365  CA  HIS A 163      -1.742  -6.914 -76.914  1.00 91.37           C  
ANISOU 1365  CA  HIS A 163     9989  16049   8675  -1252    171  -1543       C  
ATOM   1366  C   HIS A 163      -3.061  -7.380 -76.365  1.00 90.65           C  
ANISOU 1366  C   HIS A 163     9819  16105   8517  -1343    163  -1606       C  
ATOM   1367  O   HIS A 163      -4.010  -7.593 -77.121  1.00 92.20           O  
ANISOU 1367  O   HIS A 163     9886  16593   8553  -1415    156  -1671       O  
ATOM   1368  CB  HIS A 163      -0.876  -8.096 -77.341  1.00 93.87           C  
ANISOU 1368  CB  HIS A 163    10380  16225   9061  -1398    231  -1685       C  
ATOM   1369  CG  HIS A 163       0.270  -7.711 -78.249  1.00 97.56           C  
ANISOU 1369  CG  HIS A 163    10888  16633   9546  -1332    242  -1648       C  
ATOM   1370  ND1 HIS A 163       0.078  -7.205 -79.485  1.00100.14           N  
ANISOU 1370  ND1 HIS A 163    11120  17199   9727  -1296    226  -1626       N  
ATOM   1371  CD2 HIS A 163       1.652  -7.764 -78.057  1.00 97.31           C  
ANISOU 1371  CD2 HIS A 163    10984  16325   9665  -1295    268  -1629       C  
ATOM   1372  CE1 HIS A 163       1.272  -6.948 -80.054  1.00101.89           C  
ANISOU 1372  CE1 HIS A 163    11410  17297  10006  -1242    244  -1595       C  
ATOM   1373  NE2 HIS A 163       2.234  -7.290 -79.179  1.00100.98           N  
ANISOU 1373  NE2 HIS A 163    11428  16868  10072  -1243    269  -1599       N  
ATOM   1374  N   LYS A 164      -3.131  -7.535 -75.044  1.00 87.54           N  
ANISOU 1374  N   LYS A 164     9499  15519   8240  -1341    164  -1587       N  
ATOM   1375  CA  LYS A 164      -4.374  -7.886 -74.365  1.00 86.35           C  
ANISOU 1375  CA  LYS A 164     9283  15487   8040  -1415    156  -1633       C  
ATOM   1376  C   LYS A 164      -5.384  -6.743 -74.468  1.00 86.98           C  
ANISOU 1376  C   LYS A 164     9239  15818   7991  -1283     98  -1516       C  
ATOM   1377  O   LYS A 164      -6.565  -6.976 -74.713  1.00 91.33           O  
ANISOU 1377  O   LYS A 164     9664  16628   8406  -1353     88  -1574       O  
ATOM   1378  CB  LYS A 164      -4.102  -8.234 -72.901  1.00 85.22           C  
ANISOU 1378  CB  LYS A 164     9258  15060   8059  -1427    170  -1625       C  
ATOM   1379  CG  LYS A 164      -5.152  -9.131 -72.262  1.00 86.49           C  
ANISOU 1379  CG  LYS A 164     9384  15283   8194  -1573    192  -1733       C  
ATOM   1380  CD  LYS A 164      -4.719  -9.597 -70.879  1.00 85.84           C  
ANISOU 1380  CD  LYS A 164     9436  14898   8280  -1593    215  -1731       C  
ATOM   1381  CE  LYS A 164      -3.712 -10.736 -70.966  1.00 86.87           C  
ANISOU 1381  CE  LYS A 164     9682  14804   8519  -1708    281  -1838       C  
ATOM   1382  NZ  LYS A 164      -2.900 -10.856 -69.723  1.00 87.55           N  
ANISOU 1382  NZ  LYS A 164     9911  14569   8782  -1661    292  -1785       N  
ATOM   1383  N   LEU A 165      -4.904  -5.511 -74.301  1.00 86.64           N  
ANISOU 1383  N   LEU A 165     9231  15699   7988  -1092     67  -1353       N  
ATOM   1384  CA  LEU A 165      -5.735  -4.313 -74.479  1.00 86.62           C  
ANISOU 1384  CA  LEU A 165     9123  15918   7869   -940     20  -1222       C  
ATOM   1385  C   LEU A 165      -6.169  -4.153 -75.932  1.00 89.44           C  
ANISOU 1385  C   LEU A 165     9348  16591   8042   -941      9  -1239       C  
ATOM   1386  O   LEU A 165      -7.299  -3.750 -76.207  1.00 91.29           O  
ANISOU 1386  O   LEU A 165     9447  17108   8130   -902    -21  -1207       O  
ATOM   1387  CB  LEU A 165      -4.988  -3.054 -74.021  1.00 84.58           C  
ANISOU 1387  CB  LEU A 165     8951  15478   7706   -741      5  -1050       C  
ATOM   1388  CG  LEU A 165      -4.584  -2.921 -72.547  1.00 81.24           C  
ANISOU 1388  CG  LEU A 165     8648  14765   7452   -704      8  -1002       C  
ATOM   1389  CD1 LEU A 165      -3.714  -1.687 -72.351  1.00 75.98           C  
ANISOU 1389  CD1 LEU A 165     8064  13938   6867   -522      3   -848       C  
ATOM   1390  CD2 LEU A 165      -5.803  -2.875 -71.637  1.00 78.26           C  
ANISOU 1390  CD2 LEU A 165     8211  14482   7042   -709    -11   -993       C  
ATOM   1391  N   LYS A 166      -5.255  -4.460 -76.852  1.00 90.11           N  
ANISOU 1391  N   LYS A 166     9471  16632   8133   -980     34  -1285       N  
ATOM   1392  CA  LYS A 166      -5.557  -4.509 -78.281  1.00 92.74           C  
ANISOU 1392  CA  LYS A 166     9687  17254   8295  -1012     30  -1327       C  
ATOM   1393  C   LYS A 166      -6.630  -5.555 -78.581  1.00 94.38           C  
ANISOU 1393  C   LYS A 166     9777  17702   8380  -1199     39  -1489       C  
ATOM   1394  O   LYS A 166      -7.699  -5.229 -79.099  1.00 90.57           O  
ANISOU 1394  O   LYS A 166     9145  17542   7726  -1177      7  -1473       O  
ATOM   1395  CB  LYS A 166      -4.292  -4.832 -79.084  1.00 93.76           C  
ANISOU 1395  CB  LYS A 166     9897  17250   8478  -1048     64  -1371       C  
ATOM   1396  CG  LYS A 166      -3.630  -3.638 -79.752  1.00 95.67           C  
ANISOU 1396  CG  LYS A 166    10154  17498   8698   -868     49  -1221       C  
ATOM   1397  CD  LYS A 166      -2.509  -4.096 -80.677  1.00 98.55           C  
ANISOU 1397  CD  LYS A 166    10577  17778   9091   -931     85  -1290       C  
ATOM   1398  CE  LYS A 166      -2.246  -3.085 -81.783  1.00100.03           C  
ANISOU 1398  CE  LYS A 166    10719  18114   9172   -794     71  -1177       C  
ATOM   1399  NZ  LYS A 166      -1.463  -3.681 -82.899  1.00 98.76           N  
ANISOU 1399  NZ  LYS A 166    10571  17965   8986   -887    105  -1274       N  
ATOM   1400  N   LYS A 167      -6.337  -6.811 -78.246  1.00 97.05           N  
ANISOU 1400  N   LYS A 167    10185  17882   8804  -1382     86  -1643       N  
ATOM   1401  CA  LYS A 167      -7.247  -7.920 -78.525  1.00100.68           C  
ANISOU 1401  CA  LYS A 167    10552  18537   9162  -1585    112  -1818       C  
ATOM   1402  C   LYS A 167      -8.401  -7.988 -77.530  1.00101.81           C  
ANISOU 1402  C   LYS A 167    10640  18754   9288  -1611     94  -1824       C  
ATOM   1403  O   LYS A 167      -8.973  -9.051 -77.289  1.00105.30           O  
ANISOU 1403  O   LYS A 167    11059  19232   9714  -1795    130  -1974       O  
ATOM   1404  CB  LYS A 167      -6.485  -9.253 -78.607  1.00103.29           C  
ANISOU 1404  CB  LYS A 167    10985  18667   9591  -1772    183  -1984       C  
ATOM   1405  CG  LYS A 167      -6.368  -9.830 -80.020  1.00105.90           C  
ANISOU 1405  CG  LYS A 167    11248  19186   9801  -1892    213  -2107       C  
ATOM   1406  CD  LYS A 167      -6.180  -8.754 -81.090  1.00106.65           C  
ANISOU 1406  CD  LYS A 167    11269  19472   9781  -1740    168  -1988       C  
ATOM   1407  CE  LYS A 167      -4.714  -8.488 -81.390  1.00105.15           C  
ANISOU 1407  CE  LYS A 167    11206  19034   9709  -1660    187  -1931       C  
ATOM   1408  NZ  LYS A 167      -4.171  -9.473 -82.363  1.00104.94           N  
ANISOU 1408  NZ  LYS A 167    11194  19018   9661  -1820    244  -2087       N  
ATOM   1409  N   MET A 168      -8.720  -6.838 -76.945  1.00100.77           N  
ANISOU 1409  N   MET A 168    10492  18634   9162  -1426     44  -1658       N  
ATOM   1410  CA  MET A 168     -10.006  -6.613 -76.306  1.00 99.85           C  
ANISOU 1410  CA  MET A 168    10273  18691   8971  -1414     15  -1638       C  
ATOM   1411  C   MET A 168     -10.602  -5.338 -76.889  1.00 98.47           C  
ANISOU 1411  C   MET A 168     9973  18786   8652  -1227    -39  -1489       C  
ATOM   1412  O   MET A 168     -10.209  -4.899 -77.965  1.00 94.95           O  
ANISOU 1412  O   MET A 168     9493  18453   8128  -1159    -49  -1444       O  
ATOM   1413  CB  MET A 168      -9.848  -6.498 -74.789  1.00 98.98           C  
ANISOU 1413  CB  MET A 168    10281  18297   9029  -1369     17  -1580       C  
ATOM   1414  CG  MET A 168      -9.624  -7.825 -74.083  1.00 98.48           C  
ANISOU 1414  CG  MET A 168    10314  18022   9080  -1561     72  -1731       C  
ATOM   1415  SD  MET A 168      -9.182  -7.610 -72.350  1.00 99.92           S  
ANISOU 1415  SD  MET A 168    10652  17843   9468  -1486     73  -1644       S  
ATOM   1416  CE  MET A 168      -8.877  -9.305 -71.853  1.00 99.90           C  
ANISOU 1416  CE  MET A 168    10754  17629   9572  -1724    149  -1833       C  
ATOM   1417  N   LYS A 169     -11.551  -4.744 -76.182  1.00101.19           N  
ANISOU 1417  N   LYS A 169    10251  19233   8961  -1139    -72  -1408       N  
ATOM   1418  CA  LYS A 169     -12.163  -3.506 -76.644  1.00105.55           C  
ANISOU 1418  CA  LYS A 169    10687  20033   9381   -946   -119  -1255       C  
ATOM   1419  C   LYS A 169     -11.336  -2.308 -76.192  1.00102.13           C  
ANISOU 1419  C   LYS A 169    10371  19362   9068   -730   -127  -1067       C  
ATOM   1420  O   LYS A 169     -11.423  -1.228 -76.777  1.00102.26           O  
ANISOU 1420  O   LYS A 169    10334  19518   9000   -553   -151   -926       O  
ATOM   1421  CB  LYS A 169     -13.606  -3.375 -76.120  1.00110.30           C  
ANISOU 1421  CB  LYS A 169    11154  20870   9882   -942   -146  -1251       C  
ATOM   1422  CG  LYS A 169     -14.268  -4.688 -75.720  1.00111.35           C  
ANISOU 1422  CG  LYS A 169    11251  21051  10005  -1179   -120  -1444       C  
ATOM   1423  CD  LYS A 169     -15.721  -4.746 -76.164  1.00110.64           C  
ANISOU 1423  CD  LYS A 169    10951  21378   9708  -1223   -147  -1492       C  
ATOM   1424  CE  LYS A 169     -16.261  -6.158 -76.031  1.00109.26           C  
ANISOU 1424  CE  LYS A 169    10740  21264   9508  -1489   -108  -1710       C  
ATOM   1425  NZ  LYS A 169     -17.189  -6.497 -77.140  1.00112.83           N  
ANISOU 1425  NZ  LYS A 169    10994  22138   9736  -1588   -120  -1811       N  
ATOM   1426  N   TYR A 170     -10.509  -2.526 -75.169  1.00100.66           N  
ANISOU 1426  N   TYR A 170    10347  18820   9077   -749   -104  -1069       N  
ATOM   1427  CA  TYR A 170      -9.951  -1.444 -74.347  1.00 96.58           C  
ANISOU 1427  CA  TYR A 170     9939  18069   8686   -565   -110   -906       C  
ATOM   1428  C   TYR A 170      -9.109  -0.436 -75.126  1.00 93.60           C  
ANISOU 1428  C   TYR A 170     9600  17658   8304   -401   -110   -775       C  
ATOM   1429  O   TYR A 170      -9.222   0.772 -74.909  1.00 90.67           O  
ANISOU 1429  O   TYR A 170     9231  17287   7930   -212   -122   -614       O  
ATOM   1430  CB  TYR A 170      -9.156  -2.016 -73.158  1.00 96.53           C  
ANISOU 1430  CB  TYR A 170    10096  17698   8883   -640    -83   -953       C  
ATOM   1431  CG  TYR A 170      -9.946  -2.964 -72.256  1.00100.34           C  
ANISOU 1431  CG  TYR A 170    10560  18179   9386   -792    -75  -1069       C  
ATOM   1432  CD1 TYR A 170     -11.308  -3.207 -72.475  1.00102.04           C  
ANISOU 1432  CD1 TYR A 170    10617  18705   9448   -853    -92  -1125       C  
ATOM   1433  CD2 TYR A 170      -9.338  -3.587 -71.164  1.00100.05           C  
ANISOU 1433  CD2 TYR A 170    10661  17834   9519   -869    -49  -1118       C  
ATOM   1434  CE1 TYR A 170     -12.028  -4.064 -71.657  1.00102.20           C  
ANISOU 1434  CE1 TYR A 170    10623  18722   9486   -997    -79  -1234       C  
ATOM   1435  CE2 TYR A 170     -10.055  -4.440 -70.333  1.00102.04           C  
ANISOU 1435  CE2 TYR A 170    10903  18077   9789  -1005    -36  -1219       C  
ATOM   1436  CZ  TYR A 170     -11.399  -4.674 -70.587  1.00104.21           C  
ANISOU 1436  CZ  TYR A 170    11025  18657   9913  -1072    -49  -1278       C  
ATOM   1437  OH  TYR A 170     -12.121  -5.516 -69.776  1.00104.43           O  
ANISOU 1437  OH  TYR A 170    11042  18678   9956  -1213    -31  -1382       O  
ATOM   1438  N   LEU A 171      -8.281  -0.936 -76.038  1.00 94.47           N  
ANISOU 1438  N   LEU A 171     9742  17739   8412   -477    -91   -845       N  
ATOM   1439  CA  LEU A 171      -7.423  -0.084 -76.851  1.00 96.38           C  
ANISOU 1439  CA  LEU A 171    10024  17948   8648   -342    -85   -736       C  
ATOM   1440  C   LEU A 171      -7.657  -0.353 -78.338  1.00 98.39           C  
ANISOU 1440  C   LEU A 171    10161  18492   8727   -391    -90   -791       C  
ATOM   1441  O   LEU A 171      -7.350  -1.439 -78.833  1.00 99.11           O  
ANISOU 1441  O   LEU A 171    10254  18587   8813   -564    -70   -944       O  
ATOM   1442  CB  LEU A 171      -5.955  -0.328 -76.487  1.00 98.60           C  
ANISOU 1442  CB  LEU A 171    10477  17870   9114   -370    -52   -755       C  
ATOM   1443  CG  LEU A 171      -4.937   0.800 -76.680  1.00100.16           C  
ANISOU 1443  CG  LEU A 171    10767  17908   9379   -199    -40   -609       C  
ATOM   1444  CD1 LEU A 171      -5.293   2.021 -75.843  1.00 99.28           C  
ANISOU 1444  CD1 LEU A 171    10676  17744   9302    -19    -50   -448       C  
ATOM   1445  CD2 LEU A 171      -3.537   0.311 -76.332  1.00100.07           C  
ANISOU 1445  CD2 LEU A 171    10908  17568   9542   -264     -9   -663       C  
ATOM   1446  N   VAL A 172      -8.222   0.633 -79.037  1.00 99.61           N  
ANISOU 1446  N   VAL A 172    10213  18894   8737   -237   -113   -667       N  
ATOM   1447  CA  VAL A 172      -8.455   0.533 -80.485  1.00102.25           C  
ANISOU 1447  CA  VAL A 172    10429  19528   8890   -258   -122   -696       C  
ATOM   1448  C   VAL A 172      -7.502   1.457 -81.238  1.00104.21           C  
ANISOU 1448  C   VAL A 172    10742  19706   9146   -108   -107   -568       C  
ATOM   1449  O   VAL A 172      -7.369   2.635 -80.901  1.00104.17           O  
ANISOU 1449  O   VAL A 172    10784  19616   9179     84   -105   -399       O  
ATOM   1450  CB  VAL A 172      -9.917   0.879 -80.869  1.00102.39           C  
ANISOU 1450  CB  VAL A 172    10257  19942   8704   -202   -160   -657       C  
ATOM   1451  CG1 VAL A 172     -10.068   1.017 -82.380  1.00102.87           C  
ANISOU 1451  CG1 VAL A 172    10200  20311   8572   -182   -171   -651       C  
ATOM   1452  CG2 VAL A 172     -10.879  -0.173 -80.334  1.00102.44           C  
ANISOU 1452  CG2 VAL A 172    10182  20062   8678   -384   -170   -813       C  
ATOM   1453  N   GLU A 173      -6.847   0.912 -82.260  1.00107.08           N  
ANISOU 1453  N   GLU A 173    11110  20102   9472   -201    -90   -653       N  
ATOM   1454  CA  GLU A 173      -5.904   1.673 -83.070  1.00109.50           C  
ANISOU 1454  CA  GLU A 173    11476  20348   9778    -81    -71   -550       C  
ATOM   1455  C   GLU A 173      -6.610   2.792 -83.840  1.00113.70           C  
ANISOU 1455  C   GLU A 173    11895  21172  10134    104    -92   -392       C  
ATOM   1456  O   GLU A 173      -7.684   2.587 -84.413  1.00113.87           O  
ANISOU 1456  O   GLU A 173    11755  21537   9973     76   -122   -425       O  
ATOM   1457  CB  GLU A 173      -5.168   0.742 -84.030  1.00110.21           C  
ANISOU 1457  CB  GLU A 173    11580  20443   9852   -238    -48   -692       C  
ATOM   1458  CG  GLU A 173      -3.792   1.232 -84.446  1.00109.28           C  
ANISOU 1458  CG  GLU A 173    11588  20105   9827   -163    -15   -626       C  
ATOM   1459  CD  GLU A 173      -3.218   0.428 -85.594  1.00109.67           C  
ANISOU 1459  CD  GLU A 173    11622  20226   9819   -299      5   -753       C  
ATOM   1460  OE1 GLU A 173      -3.062  -0.804 -85.447  1.00109.10           O  
ANISOU 1460  OE1 GLU A 173    11568  20084   9800   -493     21   -927       O  
ATOM   1461  OE2 GLU A 173      -2.924   1.029 -86.647  1.00111.78           O  
ANISOU 1461  OE2 GLU A 173    11863  20618   9988   -211     10   -677       O  
ATOM   1462  N   VAL A 174      -6.002   3.976 -83.832  1.00116.75           N  
ANISOU 1462  N   VAL A 174    12366  21419  10573    295    -72   -222       N  
ATOM   1463  CA  VAL A 174      -6.556   5.148 -84.512  1.00119.85           C  
ANISOU 1463  CA  VAL A 174    12676  22045  10815    498    -80    -48       C  
ATOM   1464  C   VAL A 174      -5.713   5.528 -85.741  1.00124.24           C  
ANISOU 1464  C   VAL A 174    13260  22629  11313    552    -54      2       C  
ATOM   1465  O   VAL A 174      -4.550   5.135 -85.852  1.00121.42           O  
ANISOU 1465  O   VAL A 174    13019  22042  11074    469    -25    -65       O  
ATOM   1466  CB  VAL A 174      -6.730   6.333 -83.526  1.00117.12           C  
ANISOU 1466  CB  VAL A 174    12396  21549  10554    694    -67    125       C  
ATOM   1467  CG1 VAL A 174      -6.534   7.674 -84.214  1.00119.45           C  
ANISOU 1467  CG1 VAL A 174    12703  21900  10779    918    -41    323       C  
ATOM   1468  CG2 VAL A 174      -8.103   6.272 -82.873  1.00117.09           C  
ANISOU 1468  CG2 VAL A 174    12274  21735  10480    704   -104    125       C  
ATOM   1469  N   GLN A 175      -6.317   6.282 -86.659  1.00133.14           N  
ANISOU 1469  N   GLN A 175    14279  24049  12257    694    -65    122       N  
ATOM   1470  CA  GLN A 175      -5.722   6.576 -87.971  1.00138.92           C  
ANISOU 1470  CA  GLN A 175    15007  24883  12892    739    -45    165       C  
ATOM   1471  C   GLN A 175      -4.684   7.713 -87.949  1.00145.25           C  
ANISOU 1471  C   GLN A 175    15960  25427  13802    909      6    326       C  
ATOM   1472  O   GLN A 175      -4.214   8.152 -89.006  1.00146.59           O  
ANISOU 1472  O   GLN A 175    16133  25674  13889    978     28    392       O  
ATOM   1473  CB  GLN A 175      -6.825   6.890 -88.995  1.00137.15           C  
ANISOU 1473  CB  GLN A 175    14597  25100  12412    822    -78    229       C  
ATOM   1474  CG  GLN A 175      -7.847   5.772 -89.197  1.00135.86           C  
ANISOU 1474  CG  GLN A 175    14269  25235  12117    643   -126     61       C  
ATOM   1475  CD  GLN A 175      -8.972   5.780 -88.166  1.00131.92           C  
ANISOU 1475  CD  GLN A 175    13698  24805  11619    661   -157     68       C  
ATOM   1476  OE1 GLN A 175      -9.054   6.670 -87.315  1.00127.71           O  
ANISOU 1476  OE1 GLN A 175    13232  24115  11177    820   -144    209       O  
ATOM   1477  NE2 GLN A 175      -9.847   4.784 -88.243  1.00130.78           N  
ANISOU 1477  NE2 GLN A 175    13417  24899  11372    493   -192    -87       N  
ATOM   1478  N   ASP A 176      -4.329   8.171 -86.744  1.00149.55           N  
ANISOU 1478  N   ASP A 176    16628  25667  14526    968     29    383       N  
ATOM   1479  CA  ASP A 176      -3.389   9.295 -86.536  1.00150.26           C  
ANISOU 1479  CA  ASP A 176    16867  25490  14732   1125     85    531       C  
ATOM   1480  C   ASP A 176      -4.017  10.674 -86.787  1.00155.45           C  
ANISOU 1480  C   ASP A 176    17489  26290  15283   1371    106    748       C  
ATOM   1481  O   ASP A 176      -3.436  11.703 -86.425  1.00153.87           O  
ANISOU 1481  O   ASP A 176    17412  25868  15182   1514    160    883       O  
ATOM   1482  CB  ASP A 176      -2.105   9.122 -87.363  1.00146.35           C  
ANISOU 1482  CB  ASP A 176    16459  24869  14277   1068    120    490       C  
ATOM   1483  CG  ASP A 176      -1.390   7.814 -87.068  1.00144.45           C  
ANISOU 1483  CG  ASP A 176    16269  24456  14158    841    111    287       C  
ATOM   1484  OD1 ASP A 176      -0.896   7.643 -85.932  1.00141.09           O  
ANISOU 1484  OD1 ASP A 176    15950  23740  13915    796    121    249       O  
ATOM   1485  OD2 ASP A 176      -1.321   6.958 -87.976  1.00143.66           O  
ANISOU 1485  OD2 ASP A 176    16102  24513  13968    709     97    166       O  
ATOM   1486  N   GLU A 177      -5.204  10.680 -87.398  1.00160.07           N  
ANISOU 1486  N   GLU A 177    17906  27245  15666   1419     67    780       N  
ATOM   1487  CA  GLU A 177      -5.948  11.912 -87.675  1.00159.30           C  
ANISOU 1487  CA  GLU A 177    17754  27326  15447   1659     84    986       C  
ATOM   1488  C   GLU A 177      -6.943  12.219 -86.543  1.00161.93           C  
ANISOU 1488  C   GLU A 177    18049  27668  15809   1732     67   1037       C  
ATOM   1489  O   GLU A 177      -8.127  12.480 -86.792  1.00163.57           O  
ANISOU 1489  O   GLU A 177    18110  28183  15854   1827     38   1105       O  
ATOM   1490  CB  GLU A 177      -6.668  11.802 -89.032  1.00157.05           C  
ANISOU 1490  CB  GLU A 177    17297  27462  14910   1687     51   1005       C  
ATOM   1491  CG  GLU A 177      -7.263  13.104 -89.561  1.00155.32           C  
ANISOU 1491  CG  GLU A 177    17029  27435  14550   1951     77   1234       C  
ATOM   1492  CD  GLU A 177      -6.258  13.962 -90.307  1.00152.49           C  
ANISOU 1492  CD  GLU A 177    16787  26945  14205   2075    145   1361       C  
ATOM   1493  OE1 GLU A 177      -5.269  14.415 -89.686  1.00152.25           O  
ANISOU 1493  OE1 GLU A 177    16933  26550  14364   2098    202   1395       O  
ATOM   1494  OE2 GLU A 177      -6.469  14.198 -91.517  1.00149.90           O  
ANISOU 1494  OE2 GLU A 177    16372  26889  13692   2148    142   1429       O  
ATOM   1495  N   VAL A 178      -6.452  12.176 -85.302  1.00159.89           N  
ANISOU 1495  N   VAL A 178    17918  27075  15755   1685     86   1000       N  
ATOM   1496  CA  VAL A 178      -7.271  12.472 -84.114  1.00154.91           C  
ANISOU 1496  CA  VAL A 178    17274  26404  15178   1745     77   1042       C  
ATOM   1497  C   VAL A 178      -6.529  13.386 -83.118  1.00148.10           C  
ANISOU 1497  C   VAL A 178    16590  25170  14509   1849    141   1143       C  
ATOM   1498  O   VAL A 178      -7.145  14.254 -82.488  1.00145.74           O  
ANISOU 1498  O   VAL A 178    16294  24861  14218   2005    164   1270       O  
ATOM   1499  CB  VAL A 178      -7.776  11.176 -83.420  1.00154.83           C  
ANISOU 1499  CB  VAL A 178    17198  26428  15201   1532     19    849       C  
ATOM   1500  CG1 VAL A 178      -8.363  11.482 -82.054  1.00151.94           C  
ANISOU 1500  CG1 VAL A 178    16856  25942  14932   1580     19    885       C  
ATOM   1501  CG2 VAL A 178      -8.819  10.471 -84.279  1.00156.43           C  
ANISOU 1501  CG2 VAL A 178    17201  27042  15191   1458    -38    772       C  
ATOM   1502  N   LYS A 179      -5.213  13.187 -82.996  1.00139.25           N  
ANISOU 1502  N   LYS A 179    15615  23755  13539   1762    172   1082       N  
ATOM   1503  CA  LYS A 179      -4.335  14.040 -82.169  1.00132.98           C  
ANISOU 1503  CA  LYS A 179    14994  22605  12924   1844    239   1165       C  
ATOM   1504  C   LYS A 179      -4.547  13.846 -80.657  1.00131.99           C  
ANISOU 1504  C   LYS A 179    14918  22285  12946   1791    228   1114       C  
ATOM   1505  O   LYS A 179      -5.532  14.336 -80.093  1.00132.61           O  
ANISOU 1505  O   LYS A 179    14943  22453  12988   1895    225   1194       O  
ATOM   1506  CB  LYS A 179      -4.468  15.522 -82.563  1.00132.37           C  
ANISOU 1506  CB  LYS A 179    14950  22555  12788   2091    306   1382       C  
ATOM   1507  CG  LYS A 179      -3.319  16.406 -82.101  1.00128.62           C  
ANISOU 1507  CG  LYS A 179    14662  21728  12479   2161    390   1459       C  
ATOM   1508  CD  LYS A 179      -3.346  17.756 -82.803  1.00125.68           C  
ANISOU 1508  CD  LYS A 179    14321  21404  12025   2388    467   1663       C  
ATOM   1509  CE  LYS A 179      -2.178  18.628 -82.372  1.00121.33           C  
ANISOU 1509  CE  LYS A 179    13960  20501  11638   2444    560   1729       C  
ATOM   1510  NZ  LYS A 179      -2.114  19.900 -83.142  1.00118.05           N  
ANISOU 1510  NZ  LYS A 179    13588  20120  11145   2654    646   1922       N  
ATOM   1511  N   PRO A 180      -3.601  13.145 -79.996  1.00127.66           N  
ANISOU 1511  N   PRO A 180    14472  21468  12563   1634    225    986       N  
ATOM   1512  CA  PRO A 180      -3.747  12.700 -78.606  1.00121.75           C  
ANISOU 1512  CA  PRO A 180    13762  20547  11947   1546    205    908       C  
ATOM   1513  C   PRO A 180      -3.584  13.832 -77.600  1.00117.65           C  
ANISOU 1513  C   PRO A 180    13354  19801  11544   1684    261   1031       C  
ATOM   1514  O   PRO A 180      -3.056  14.889 -77.941  1.00119.60           O  
ANISOU 1514  O   PRO A 180    13680  19956  11805   1822    326   1158       O  
ATOM   1515  CB  PRO A 180      -2.610  11.693 -78.447  1.00119.92           C  
ANISOU 1515  CB  PRO A 180    13614  20107  11843   1357    194    752       C  
ATOM   1516  CG  PRO A 180      -1.556  12.175 -79.382  1.00121.80           C  
ANISOU 1516  CG  PRO A 180    13923  20270  12082   1406    240    803       C  
ATOM   1517  CD  PRO A 180      -2.266  12.824 -80.539  1.00124.70           C  
ANISOU 1517  CD  PRO A 180    14190  20928  12260   1546    247    921       C  
ATOM   1518  N   ARG A 181      -4.039  13.605 -76.370  1.00114.45           N  
ANISOU 1518  N   ARG A 181    12956  19307  11221   1641    242    990       N  
ATOM   1519  CA  ARG A 181      -3.886  14.590 -75.298  1.00112.98           C  
ANISOU 1519  CA  ARG A 181    12877  18895  11155   1750    296   1087       C  
ATOM   1520  C   ARG A 181      -3.348  13.962 -74.003  1.00107.64           C  
ANISOU 1520  C   ARG A 181    12288  17959  10651   1609    281    973       C  
ATOM   1521  O   ARG A 181      -3.822  14.264 -72.905  1.00108.11           O  
ANISOU 1521  O   ARG A 181    12367  17937  10772   1642    287    998       O  
ATOM   1522  CB  ARG A 181      -5.201  15.347 -75.057  1.00116.17           C  
ANISOU 1522  CB  ARG A 181    13196  19478  11462   1907    303   1208       C  
ATOM   1523  CG  ARG A 181      -5.538  16.352 -76.154  1.00119.55           C  
ANISOU 1523  CG  ARG A 181    13581  20090  11750   2100    344   1369       C  
ATOM   1524  CD  ARG A 181      -6.868  17.053 -75.912  1.00122.09           C  
ANISOU 1524  CD  ARG A 181    13811  20601  11975   2262    351   1490       C  
ATOM   1525  NE  ARG A 181      -7.153  18.036 -76.961  1.00124.52           N  
ANISOU 1525  NE  ARG A 181    14084  21079  12149   2460    397   1656       N  
ATOM   1526  CZ  ARG A 181      -8.237  18.809 -77.010  1.00124.70           C  
ANISOU 1526  CZ  ARG A 181    14026  21287  12065   2641    416   1793       C  
ATOM   1527  NH1 ARG A 181      -9.169  18.731 -76.066  1.00122.78           N  
ANISOU 1527  NH1 ARG A 181    13727  21090  11833   2647    392   1781       N  
ATOM   1528  NH2 ARG A 181      -8.388  19.667 -78.010  1.00126.05           N  
ANISOU 1528  NH2 ARG A 181    14174  21601  12116   2821    462   1946       N  
ATOM   1529  N   GLY A 182      -2.339  13.103 -74.156  1.00101.76           N  
ANISOU 1529  N   GLY A 182    11595  17086   9981   1459    264    851       N  
ATOM   1530  CA  GLY A 182      -1.691  12.411 -73.038  1.00 95.19           C  
ANISOU 1530  CA  GLY A 182    10848  16011   9309   1321    249    739       C  
ATOM   1531  C   GLY A 182      -1.110  11.081 -73.493  1.00 92.32           C  
ANISOU 1531  C   GLY A 182    10469  15648   8958   1140    209    584       C  
ATOM   1532  O   GLY A 182      -1.573  10.508 -74.479  1.00 93.75           O  
ANISOU 1532  O   GLY A 182    10547  16060   9011   1096    178    539       O  
ATOM   1533  N   VAL A 183      -0.101  10.584 -72.779  1.00 89.32           N  
ANISOU 1533  N   VAL A 183    10191  15016   8729   1037    212    501       N  
ATOM   1534  CA  VAL A 183       0.562   9.323 -73.159  1.00 89.91           C  
ANISOU 1534  CA  VAL A 183    10268  15061   8833    870    184    355       C  
ATOM   1535  C   VAL A 183       0.171   8.144 -72.248  1.00 89.51           C  
ANISOU 1535  C   VAL A 183    10197  14978   8833    723    140    228       C  
ATOM   1536  O   VAL A 183       0.197   8.260 -71.016  1.00 88.98           O  
ANISOU 1536  O   VAL A 183    10189  14746   8870    721    141    234       O  
ATOM   1537  CB  VAL A 183       2.111   9.484 -73.258  1.00 89.21           C  
ANISOU 1537  CB  VAL A 183    10301  14730   8863    854    222    344       C  
ATOM   1538  CG1 VAL A 183       2.723   9.850 -71.910  1.00 88.38           C  
ANISOU 1538  CG1 VAL A 183    10308  14355   8918    862    243    359       C  
ATOM   1539  CG2 VAL A 183       2.761   8.230 -73.831  1.00 88.16           C  
ANISOU 1539  CG2 VAL A 183    10162  14591   8744    699    200    204       C  
ATOM   1540  N   LEU A 184      -0.203   7.020 -72.865  1.00 87.74           N  
ANISOU 1540  N   LEU A 184     9891  14912   8532    597    106    115       N  
ATOM   1541  CA  LEU A 184      -0.611   5.824 -72.121  1.00 85.34           C  
ANISOU 1541  CA  LEU A 184     9567  14591   8265    448     73    -11       C  
ATOM   1542  C   LEU A 184       0.564   5.167 -71.407  1.00 82.31           C  
ANISOU 1542  C   LEU A 184     9300  13928   8046    350     82    -92       C  
ATOM   1543  O   LEU A 184       1.549   4.779 -72.037  1.00 86.08           O  
ANISOU 1543  O   LEU A 184     9820  14329   8557    299     97   -142       O  
ATOM   1544  CB  LEU A 184      -1.303   4.804 -73.037  1.00 86.14           C  
ANISOU 1544  CB  LEU A 184     9552  14939   8236    333     45   -118       C  
ATOM   1545  CG  LEU A 184      -1.609   3.423 -72.426  1.00 85.68           C  
ANISOU 1545  CG  LEU A 184     9482  14853   8217    155     24   -268       C  
ATOM   1546  CD1 LEU A 184      -2.786   3.475 -71.461  1.00 84.58           C  
ANISOU 1546  CD1 LEU A 184     9291  14786   8057    163      3   -253       C  
ATOM   1547  CD2 LEU A 184      -1.860   2.391 -73.512  1.00 88.39           C  
ANISOU 1547  CD2 LEU A 184     9740  15387   8453     24     16   -390       C  
ATOM   1548  N   ASN A 185       0.446   5.031 -70.092  1.00 78.66           N  
ANISOU 1548  N   ASN A 185     8886  13319   7680    327     75   -102       N  
ATOM   1549  CA  ASN A 185       1.481   4.399 -69.297  1.00 73.53           C  
ANISOU 1549  CA  ASN A 185     8340  12414   7181    241     81   -172       C  
ATOM   1550  C   ASN A 185       0.975   3.109 -68.674  1.00 70.64           C  
ANISOU 1550  C   ASN A 185     7953  12051   6834     96     56   -292       C  
ATOM   1551  O   ASN A 185      -0.070   3.094 -68.016  1.00 73.00           O  
ANISOU 1551  O   ASN A 185     8205  12431   7099     94     38   -285       O  
ATOM   1552  CB  ASN A 185       1.971   5.357 -68.212  1.00 74.54           C  
ANISOU 1552  CB  ASN A 185     8561  12339   7421    336     99    -82       C  
ATOM   1553  CG  ASN A 185       3.478   5.379 -68.097  1.00 76.68           C  
ANISOU 1553  CG  ASN A 185     8939  12380   7815    324    123    -95       C  
ATOM   1554  OD1 ASN A 185       4.185   5.623 -69.078  1.00 74.90           O  
ANISOU 1554  OD1 ASN A 185     8724  12162   7571    349    144    -83       O  
ATOM   1555  ND2 ASN A 185       3.982   5.125 -66.895  1.00 77.60           N  
ANISOU 1555  ND2 ASN A 185     9132  12297   8056    286    120   -121       N  
ATOM   1556  N   ILE A 186       1.706   2.024 -68.895  1.00 65.60           N  
ANISOU 1556  N   ILE A 186     7352  11324   6249    -24     62   -402       N  
ATOM   1557  CA  ILE A 186       1.357   0.739 -68.302  1.00 64.56           C  
ANISOU 1557  CA  ILE A 186     7219  11162   6148   -167     52   -519       C  
ATOM   1558  C   ILE A 186       2.225   0.484 -67.069  1.00 64.84           C  
ANISOU 1558  C   ILE A 186     7368  10925   6343   -187     59   -528       C  
ATOM   1559  O   ILE A 186       3.451   0.462 -67.159  1.00 65.39           O  
ANISOU 1559  O   ILE A 186     7514  10830   6499   -181     76   -532       O  
ATOM   1560  CB  ILE A 186       1.473  -0.416 -69.327  1.00 61.77           C  
ANISOU 1560  CB  ILE A 186     6828  10899   5742   -297     62   -644       C  
ATOM   1561  CG1 ILE A 186       0.476  -0.204 -70.467  1.00 62.16           C  
ANISOU 1561  CG1 ILE A 186     6750  11247   5619   -286     51   -640       C  
ATOM   1562  CG2 ILE A 186       1.229  -1.766 -68.663  1.00 60.62           C  
ANISOU 1562  CG2 ILE A 186     6701  10685   5644   -448     67   -766       C  
ATOM   1563  CD1 ILE A 186       0.762  -1.028 -71.704  1.00 61.98           C  
ANISOU 1563  CD1 ILE A 186     6692  11324   5533   -387     66   -742       C  
ATOM   1564  N   ILE A 187       1.573   0.332 -65.916  1.00 67.90           N  
ANISOU 1564  N   ILE A 187     7762  11274   6762   -206     45   -528       N  
ATOM   1565  CA  ILE A 187       2.257   0.119 -64.633  1.00 67.35           C  
ANISOU 1565  CA  ILE A 187     7792  10965   6831   -221     48   -529       C  
ATOM   1566  C   ILE A 187       1.981  -1.298 -64.149  1.00 66.69           C  
ANISOU 1566  C   ILE A 187     7719  10843   6775   -365     50   -644       C  
ATOM   1567  O   ILE A 187       0.830  -1.705 -64.097  1.00 68.40           O  
ANISOU 1567  O   ILE A 187     7867  11207   6915   -422     41   -684       O  
ATOM   1568  CB  ILE A 187       1.751   1.099 -63.533  1.00 69.58           C  
ANISOU 1568  CB  ILE A 187     8086  11212   7136   -126     37   -433       C  
ATOM   1569  CG1 ILE A 187       1.703   2.550 -64.039  1.00 69.28           C  
ANISOU 1569  CG1 ILE A 187     8026  11248   7048     20     45   -314       C  
ATOM   1570  CG2 ILE A 187       2.582   0.971 -62.251  1.00 67.99           C  
ANISOU 1570  CG2 ILE A 187     7989  10768   7074   -135     39   -429       C  
ATOM   1571  CD1 ILE A 187       3.045   3.128 -64.430  1.00 71.22           C  
ANISOU 1571  CD1 ILE A 187     8343  11355   7360     79     68   -274       C  
ATOM   1572  N   PRO A 188       3.031  -2.045 -63.765  1.00 68.54           N  
ANISOU 1572  N   PRO A 188     8040  10879   7120   -421     65   -696       N  
ATOM   1573  CA  PRO A 188       2.791  -3.348 -63.140  1.00 71.69           C  
ANISOU 1573  CA  PRO A 188     8466  11213   7558   -546     76   -792       C  
ATOM   1574  C   PRO A 188       2.171  -3.181 -61.751  1.00 75.95           C  
ANISOU 1574  C   PRO A 188     9025  11697   8133   -533     60   -754       C  
ATOM   1575  O   PRO A 188       2.699  -2.431 -60.927  1.00 76.43           O  
ANISOU 1575  O   PRO A 188     9142  11629   8269   -448     49   -675       O  
ATOM   1576  CB  PRO A 188       4.199  -3.963 -63.030  1.00 69.30           C  
ANISOU 1576  CB  PRO A 188     8258  10700   7372   -572     98   -827       C  
ATOM   1577  CG  PRO A 188       5.088  -3.098 -63.865  1.00 67.89           C  
ANISOU 1577  CG  PRO A 188     8084  10517   7194   -483     99   -772       C  
ATOM   1578  CD  PRO A 188       4.466  -1.737 -63.858  1.00 67.41           C  
ANISOU 1578  CD  PRO A 188     7974  10566   7069   -370     77   -667       C  
ATOM   1579  N   LYS A 189       1.036  -3.841 -61.520  1.00 83.31           N  
ANISOU 1579  N   LYS A 189     9908  12738   9007   -619     60   -813       N  
ATOM   1580  CA  LYS A 189       0.359  -3.809 -60.221  1.00 86.82           C  
ANISOU 1580  CA  LYS A 189    10367  13140   9478   -623     49   -789       C  
ATOM   1581  C   LYS A 189       0.283  -5.201 -59.610  1.00 92.51           C  
ANISOU 1581  C   LYS A 189    11136  13765  10249   -755     74   -886       C  
ATOM   1582  O   LYS A 189      -0.656  -5.955 -59.882  1.00 93.12           O  
ANISOU 1582  O   LYS A 189    11158  13969  10254   -859     88   -967       O  
ATOM   1583  CB  LYS A 189      -1.052  -3.208 -60.338  1.00 86.41           C  
ANISOU 1583  CB  LYS A 189    10210  13310   9311   -594     29   -758       C  
ATOM   1584  CG  LYS A 189      -1.110  -1.686 -60.271  1.00 86.47           C  
ANISOU 1584  CG  LYS A 189    10197  13355   9300   -439      9   -632       C  
ATOM   1585  CD  LYS A 189      -0.580  -1.140 -58.951  1.00 80.87           C  
ANISOU 1585  CD  LYS A 189     9576  12451   8700   -374      4   -563       C  
ATOM   1586  CE  LYS A 189      -0.271   0.346 -59.059  1.00 79.93           C  
ANISOU 1586  CE  LYS A 189     9460  12328   8582   -225      1   -446       C  
ATOM   1587  NZ  LYS A 189       0.519   0.823 -57.894  1.00 76.71           N  
ANISOU 1587  NZ  LYS A 189     9147  11712   8288   -175      2   -394       N  
ATOM   1588  N   GLN A 190       1.290  -5.532 -58.798  1.00 96.50           N  
ANISOU 1588  N   GLN A 190    11744  14048  10874   -750     83   -877       N  
ATOM   1589  CA  GLN A 190       1.328  -6.777 -58.016  1.00100.54           C  
ANISOU 1589  CA  GLN A 190    12320  14431  11447   -854    111   -947       C  
ATOM   1590  C   GLN A 190       1.120  -8.038 -58.866  1.00102.64           C  
ANISOU 1590  C   GLN A 190    12571  14751  11675   -988    154  -1069       C  
ATOM   1591  O   GLN A 190       2.088  -8.674 -59.287  1.00106.44           O  
ANISOU 1591  O   GLN A 190    13108  15121  12213  -1016    183  -1112       O  
ATOM   1592  CB  GLN A 190       0.333  -6.714 -56.847  1.00105.57           C  
ANISOU 1592  CB  GLN A 190    12951  15085  12075   -868     99   -926       C  
ATOM   1593  CG  GLN A 190       0.587  -5.553 -55.888  1.00110.84           C  
ANISOU 1593  CG  GLN A 190    13645  15678  12790   -747     65   -814       C  
ATOM   1594  CD  GLN A 190      -0.692  -4.942 -55.330  1.00112.60           C  
ANISOU 1594  CD  GLN A 190    13805  16029  12947   -726     45   -777       C  
ATOM   1595  OE1 GLN A 190      -1.799  -5.328 -55.706  1.00117.19           O  
ANISOU 1595  OE1 GLN A 190    14312  16773  13440   -796     52   -832       O  
ATOM   1596  NE2 GLN A 190      -0.539  -3.970 -54.438  1.00112.37           N  
ANISOU 1596  NE2 GLN A 190    13803  15932  12959   -629     23   -687       N  
ATOM   1597  N   ASP A 191      -0.139  -8.389 -59.116  1.00103.06           N  
ANISOU 1597  N   ASP A 191    12549  14977  11632  -1072    162  -1129       N  
ATOM   1598  CA  ASP A 191      -0.470  -9.540 -59.953  1.00103.94           C  
ANISOU 1598  CA  ASP A 191    12636  15164  11693  -1212    209  -1256       C  
ATOM   1599  C   ASP A 191      -0.937  -9.107 -61.345  1.00103.64           C  
ANISOU 1599  C   ASP A 191    12486  15361  11531  -1211    196  -1277       C  
ATOM   1600  O   ASP A 191      -0.757  -9.837 -62.324  1.00107.43           O  
ANISOU 1600  O   ASP A 191    12952  15886  11978  -1298    232  -1369       O  
ATOM   1601  CB  ASP A 191      -1.540 -10.406 -59.277  1.00105.33           C  
ANISOU 1601  CB  ASP A 191    12805  15371  11844  -1333    238  -1328       C  
ATOM   1602  CG  ASP A 191      -1.666 -11.785 -59.909  1.00107.24           C  
ANISOU 1602  CG  ASP A 191    13057  15620  12066  -1494    305  -1469       C  
ATOM   1603  OD1 ASP A 191      -0.703 -12.580 -59.821  1.00108.03           O  
ANISOU 1603  OD1 ASP A 191    13256  15530  12260  -1525    349  -1502       O  
ATOM   1604  OD2 ASP A 191      -2.733 -12.078 -60.485  1.00106.12           O  
ANISOU 1604  OD2 ASP A 191    12825  15679  11815  -1589    319  -1547       O  
ATOM   1605  N   ASN A 192      -1.540  -7.922 -61.425  1.00 99.11           N  
ANISOU 1605  N   ASN A 192    11834  14937  10886  -1110    149  -1191       N  
ATOM   1606  CA  ASN A 192      -2.047  -7.395 -62.692  1.00 95.82           C  
ANISOU 1606  CA  ASN A 192    11304  14760  10341  -1089    133  -1193       C  
ATOM   1607  C   ASN A 192      -1.274  -6.173 -63.191  1.00 87.62           C  
ANISOU 1607  C   ASN A 192    10267  13713   9311   -937    103  -1083       C  
ATOM   1608  O   ASN A 192      -0.042  -6.166 -63.184  1.00 83.98           O  
ANISOU 1608  O   ASN A 192     9890  13071   8945   -900    113  -1063       O  
ATOM   1609  CB  ASN A 192      -3.548  -7.090 -62.590  1.00100.44           C  
ANISOU 1609  CB  ASN A 192    11778  15575  10810  -1102    112  -1192       C  
ATOM   1610  CG  ASN A 192      -4.411  -8.214 -63.133  1.00104.56           C  
ANISOU 1610  CG  ASN A 192    12234  16250  11244  -1271    146  -1332       C  
ATOM   1611  OD1 ASN A 192      -3.905  -9.190 -63.689  1.00106.73           O  
ANISOU 1611  OD1 ASN A 192    12545  16467  11538  -1376    189  -1431       O  
ATOM   1612  ND2 ASN A 192      -5.726  -8.080 -62.980  1.00108.16           N  
ANISOU 1612  ND2 ASN A 192    12589  16905  11599  -1299    131  -1345       N  
ATOM   1613  N   PHE A 193      -2.007  -5.153 -63.634  1.00 80.24           N  
ANISOU 1613  N   PHE A 193     9237  12975   8274   -849     72  -1013       N  
ATOM   1614  CA  PHE A 193      -1.416  -3.926 -64.156  1.00 76.49           C  
ANISOU 1614  CA  PHE A 193     8759  12510   7793   -703     52   -904       C  
ATOM   1615  C   PHE A 193      -2.362  -2.741 -63.978  1.00 76.01           C  
ANISOU 1615  C   PHE A 193     8622  12604   7654   -587     21   -801       C  
ATOM   1616  O   PHE A 193      -3.512  -2.910 -63.590  1.00 77.51           O  
ANISOU 1616  O   PHE A 193     8747  12921   7782   -626     12   -822       O  
ATOM   1617  CB  PHE A 193      -1.078  -4.085 -65.640  1.00 72.32           C  
ANISOU 1617  CB  PHE A 193     8186  12101   7192   -725     63   -947       C  
ATOM   1618  CG  PHE A 193      -2.283  -4.115 -66.530  1.00 69.06           C  
ANISOU 1618  CG  PHE A 193     7638  11984   6617   -763     53   -984       C  
ATOM   1619  CD1 PHE A 193      -2.834  -2.934 -67.020  1.00 68.37           C  
ANISOU 1619  CD1 PHE A 193     7467  12078   6431   -636     26   -882       C  
ATOM   1620  CD2 PHE A 193      -2.875  -5.323 -66.873  1.00 69.05           C  
ANISOU 1620  CD2 PHE A 193     7591  12083   6559   -925     76  -1121       C  
ATOM   1621  CE1 PHE A 193      -3.950  -2.957 -67.838  1.00 69.24           C  
ANISOU 1621  CE1 PHE A 193     7443  12479   6383   -664     14   -912       C  
ATOM   1622  CE2 PHE A 193      -3.990  -5.355 -67.695  1.00 70.25           C  
ANISOU 1622  CE2 PHE A 193     7610  12527   6554   -966     66  -1161       C  
ATOM   1623  CZ  PHE A 193      -4.528  -4.170 -68.178  1.00 70.72           C  
ANISOU 1623  CZ  PHE A 193     7579  12779   6511   -832     31  -1054       C  
ATOM   1624  N   ARG A 194      -1.873  -1.548 -64.297  1.00 77.82           N  
ANISOU 1624  N   ARG A 194     8860  12822   7885   -445     12   -691       N  
ATOM   1625  CA  ARG A 194      -2.687  -0.344 -64.259  1.00 79.81           C  
ANISOU 1625  CA  ARG A 194     9045  13216   8062   -318     -6   -583       C  
ATOM   1626  C   ARG A 194      -2.363   0.520 -65.470  1.00 79.00           C  
ANISOU 1626  C   ARG A 194     8905  13221   7890   -214     -4   -513       C  
ATOM   1627  O   ARG A 194      -1.207   0.891 -65.689  1.00 78.29           O  
ANISOU 1627  O   ARG A 194     8892  12983   7872   -164      9   -477       O  
ATOM   1628  CB  ARG A 194      -2.427   0.428 -62.966  1.00 85.04           C  
ANISOU 1628  CB  ARG A 194     9784  13698   8826   -229     -8   -494       C  
ATOM   1629  CG  ARG A 194      -3.553   1.353 -62.560  1.00 93.65           C  
ANISOU 1629  CG  ARG A 194    10808  14924   9850   -133    -21   -409       C  
ATOM   1630  CD  ARG A 194      -3.155   2.207 -61.371  1.00100.44           C  
ANISOU 1630  CD  ARG A 194    11753  15595  10813    -41    -16   -320       C  
ATOM   1631  NE  ARG A 194      -4.070   3.331 -61.200  1.00109.57           N  
ANISOU 1631  NE  ARG A 194    12850  16875  11904     82    -17   -219       N  
ATOM   1632  CZ  ARG A 194      -3.787   4.442 -60.524  1.00114.76           C  
ANISOU 1632  CZ  ARG A 194    13566  17415  12622    200     -2   -117       C  
ATOM   1633  NH1 ARG A 194      -2.600   4.597 -59.944  1.00119.22           N  
ANISOU 1633  NH1 ARG A 194    14243  17744  13309    206     11   -106       N  
ATOM   1634  NH2 ARG A 194      -4.694   5.408 -60.437  1.00117.81           N  
ANISOU 1634  NH2 ARG A 194    13895  17926  12942    312      2    -29       N  
ATOM   1635  N   ALA A 195      -3.383   0.818 -66.268  1.00 76.87           N  
ANISOU 1635  N   ALA A 195     8516  13216   7476   -185    -17   -496       N  
ATOM   1636  CA  ALA A 195      -3.203   1.607 -67.476  1.00 77.40           C  
ANISOU 1636  CA  ALA A 195     8537  13414   7457    -85    -14   -427       C  
ATOM   1637  C   ALA A 195      -3.668   3.042 -67.270  1.00 79.01           C  
ANISOU 1637  C   ALA A 195     8717  13675   7625     91    -15   -277       C  
ATOM   1638  O   ALA A 195      -4.840   3.364 -67.466  1.00 79.78           O  
ANISOU 1638  O   ALA A 195     8708  13996   7606    135    -30   -243       O  
ATOM   1639  CB  ALA A 195      -3.933   0.966 -68.643  1.00 78.89           C  
ANISOU 1639  CB  ALA A 195     8604  13871   7497   -167    -23   -507       C  
ATOM   1640  N   ILE A 196      -2.733   3.900 -66.873  1.00 81.96           N  
ANISOU 1640  N   ILE A 196     9193  13847   8100    191      4   -190       N  
ATOM   1641  CA  ILE A 196      -3.030   5.304 -66.584  1.00 82.66           C  
ANISOU 1641  CA  ILE A 196     9284  13943   8177    360     18    -47       C  
ATOM   1642  C   ILE A 196      -2.437   6.226 -67.651  1.00 84.96           C  
ANISOU 1642  C   ILE A 196     9586  14266   8428    477     43     42       C  
ATOM   1643  O   ILE A 196      -1.581   5.807 -68.436  1.00 83.97           O  
ANISOU 1643  O   ILE A 196     9487  14104   8314    425     50     -5       O  
ATOM   1644  CB  ILE A 196      -2.520   5.720 -65.180  1.00 81.57           C  
ANISOU 1644  CB  ILE A 196     9257  13551   8183    390     32     -9       C  
ATOM   1645  CG1 ILE A 196      -0.997   5.546 -65.072  1.00 82.34           C  
ANISOU 1645  CG1 ILE A 196     9472  13404   8407    355     50    -36       C  
ATOM   1646  CG2 ILE A 196      -3.231   4.919 -64.098  1.00 82.50           C  
ANISOU 1646  CG2 ILE A 196     9362  13655   8329    290      9    -81       C  
ATOM   1647  CD1 ILE A 196      -0.386   6.150 -63.821  1.00 80.72           C  
ANISOU 1647  CD1 ILE A 196     9373  12965   8332    402     68     13       C  
ATOM   1648  N   VAL A 197      -2.896   7.477 -67.676  1.00 85.71           N  
ANISOU 1648  N   VAL A 197     9663  14424   8477    636     63    175       N  
ATOM   1649  CA  VAL A 197      -2.382   8.466 -68.623  1.00 85.10           C  
ANISOU 1649  CA  VAL A 197     9603  14368   8362    762     97    276       C  
ATOM   1650  C   VAL A 197      -1.664   9.624 -67.950  1.00 88.55           C  
ANISOU 1650  C   VAL A 197    10154  14582   8906    877    145    380       C  
ATOM   1651  O   VAL A 197      -2.140  10.182 -66.958  1.00 88.00           O  
ANISOU 1651  O   VAL A 197    10104  14454   8875    936    156    433       O  
ATOM   1652  CB  VAL A 197      -3.484   9.027 -69.545  1.00 82.57           C  
ANISOU 1652  CB  VAL A 197     9159  14341   7872    870     93    357       C  
ATOM   1653  CG1 VAL A 197      -3.981   7.945 -70.479  1.00 83.39           C  
ANISOU 1653  CG1 VAL A 197     9151  14675   7858    753     53    251       C  
ATOM   1654  CG2 VAL A 197      -4.627   9.623 -68.737  1.00 80.51           C  
ANISOU 1654  CG2 VAL A 197     8851  14157   7581    958     92    430       C  
ATOM   1655  N   SER A 198      -0.513   9.980 -68.503  1.00 94.87           N  
ANISOU 1655  N   SER A 198    11030  15261   9754    902    178    402       N  
ATOM   1656  CA  SER A 198       0.196  11.173 -68.085  1.00101.68           C  
ANISOU 1656  CA  SER A 198    11996  15935  10701   1013    235    502       C  
ATOM   1657  C   SER A 198      -0.094  12.295 -69.075  1.00108.17           C  
ANISOU 1657  C   SER A 198    12789  16887  11420   1171    277    632       C  
ATOM   1658  O   SER A 198       0.169  12.161 -70.274  1.00107.77           O  
ANISOU 1658  O   SER A 198    12705  16946  11294   1173    277    630       O  
ATOM   1659  CB  SER A 198       1.699  10.899 -67.998  1.00101.75           C  
ANISOU 1659  CB  SER A 198    12110  15715  10832    940    251    444       C  
ATOM   1660  OG  SER A 198       1.974   9.852 -67.078  1.00 96.38           O  
ANISOU 1660  OG  SER A 198    11458  14916  10244    805    214    332       O  
ATOM   1661  N   ILE A 199      -0.664  13.387 -68.572  1.00113.87           N  
ANISOU 1661  N   ILE A 199    13525  17602  12137   1307    316    747       N  
ATOM   1662  CA  ILE A 199      -1.004  14.539 -69.407  1.00122.15           C  
ANISOU 1662  CA  ILE A 199    14555  18765  13092   1477    367    888       C  
ATOM   1663  C   ILE A 199       0.236  15.420 -69.617  1.00128.36           C  
ANISOU 1663  C   ILE A 199    15466  19345  13960   1537    440    949       C  
ATOM   1664  O   ILE A 199       1.269  15.203 -68.978  1.00127.37           O  
ANISOU 1664  O   ILE A 199    15434  18995  13964   1452    449    884       O  
ATOM   1665  CB  ILE A 199      -2.163  15.375 -68.799  1.00121.69           C  
ANISOU 1665  CB  ILE A 199    14459  18783  12991   1608    389    993       C  
ATOM   1666  CG1 ILE A 199      -3.006  14.541 -67.813  1.00118.69           C  
ANISOU 1666  CG1 ILE A 199    14020  18452  12625   1512    329    907       C  
ATOM   1667  CG2 ILE A 199      -3.020  15.992 -69.901  1.00122.82           C  
ANISOU 1667  CG2 ILE A 199    14509  19183  12974   1754    403   1106       C  
ATOM   1668  CD1 ILE A 199      -3.981  13.573 -68.459  1.00118.67           C  
ANISOU 1668  CD1 ILE A 199    13870  18729  12488   1443    261    840       C  
ATOM   1669  N   PHE A 200       0.128  16.408 -70.508  1.00137.33           N  
ANISOU 1669  N   PHE A 200    16601  20564  15015   1683    495   1073       N  
ATOM   1670  CA  PHE A 200       1.273  17.252 -70.899  1.00145.67           C  
ANISOU 1670  CA  PHE A 200    17769  21448  16130   1740    573   1132       C  
ATOM   1671  C   PHE A 200       1.865  18.182 -69.814  1.00151.10           C  
ANISOU 1671  C   PHE A 200    18586  21870  16955   1784    646   1176       C  
ATOM   1672  O   PHE A 200       3.087  18.327 -69.744  1.00144.46           O  
ANISOU 1672  O   PHE A 200    17843  20832  16210   1735    683   1144       O  
ATOM   1673  CB  PHE A 200       0.966  18.038 -72.182  1.00149.86           C  
ANISOU 1673  CB  PHE A 200    18265  22145  16530   1887    617   1258       C  
ATOM   1674  CG  PHE A 200       0.863  17.177 -73.412  1.00153.42           C  
ANISOU 1674  CG  PHE A 200    18617  22811  16863   1826    560   1202       C  
ATOM   1675  CD1 PHE A 200       2.007  16.761 -74.087  1.00154.97           C  
ANISOU 1675  CD1 PHE A 200    18858  22928  17093   1739    563   1136       C  
ATOM   1676  CD2 PHE A 200      -0.378  16.787 -73.902  1.00155.88           C  
ANISOU 1676  CD2 PHE A 200    18787  23412  17028   1851    505   1212       C  
ATOM   1677  CE1 PHE A 200       1.914  15.969 -75.224  1.00155.10           C  
ANISOU 1677  CE1 PHE A 200    18786  23143  17001   1678    515   1079       C  
ATOM   1678  CE2 PHE A 200      -0.476  15.997 -75.039  1.00155.61           C  
ANISOU 1678  CE2 PHE A 200    18659  23584  16880   1785    456   1153       C  
ATOM   1679  CZ  PHE A 200       0.670  15.587 -75.700  1.00154.69           C  
ANISOU 1679  CZ  PHE A 200    18594  23379  16800   1698    462   1086       C  
ATOM   1680  N   PRO A 201       1.014  18.832 -68.981  1.00161.97           N  
ANISOU 1680  N   PRO A 201    19962  23243  18335   1873    671   1247       N  
ATOM   1681  CA  PRO A 201      -0.448  18.856 -68.969  1.00169.02           C  
ANISOU 1681  CA  PRO A 201    20743  24356  19117   1952    641   1301       C  
ATOM   1682  C   PRO A 201      -1.032  20.039 -69.753  1.00174.85           C  
ANISOU 1682  C   PRO A 201    21466  25216  19751   2152    712   1467       C  
ATOM   1683  O   PRO A 201      -1.452  19.866 -70.900  1.00180.13           O  
ANISOU 1683  O   PRO A 201    22045  26107  20287   2197    688   1501       O  
ATOM   1684  CB  PRO A 201      -0.784  18.977 -67.470  1.00167.75           C  
ANISOU 1684  CB  PRO A 201    20620  24064  19053   1930    644   1280       C  
ATOM   1685  CG  PRO A 201       0.472  19.469 -66.802  1.00163.66           C  
ANISOU 1685  CG  PRO A 201    20247  23254  18683   1896    706   1263       C  
ATOM   1686  CD  PRO A 201       1.560  19.581 -67.836  1.00161.78           C  
ANISOU 1686  CD  PRO A 201    20057  22966  18445   1887    737   1265       C  
ATOM   1687  N   ASP A 202      -1.046  21.222 -69.133  1.00174.41           N  
ANISOU 1687  N   ASP A 202    21498  25014  19754   2272    803   1569       N  
ATOM   1688  CA  ASP A 202      -1.629  22.436 -69.721  1.00175.55           C  
ANISOU 1688  CA  ASP A 202    21643  25245  19812   2479    886   1739       C  
ATOM   1689  C   ASP A 202      -3.102  22.252 -70.120  1.00184.28           C  
ANISOU 1689  C   ASP A 202    22596  26656  20763   2567    835   1794       C  
ATOM   1690  O   ASP A 202      -3.995  22.428 -69.287  1.00186.84           O  
ANISOU 1690  O   ASP A 202    22886  27013  21091   2611    832   1817       O  
ATOM   1691  CB  ASP A 202      -0.785  22.942 -70.904  1.00167.47           C  
ANISOU 1691  CB  ASP A 202    20676  24196  18756   2536    947   1802       C  
ATOM   1692  CG  ASP A 202      -1.149  24.358 -71.322  1.00162.74           C  
ANISOU 1692  CG  ASP A 202    20122  23607  18103   2754   1061   1987       C  
ATOM   1693  OD1 ASP A 202      -1.445  25.190 -70.437  1.00158.58           O  
ANISOU 1693  OD1 ASP A 202    19659  22954  17639   2838   1132   2051       O  
ATOM   1694  OD2 ASP A 202      -1.129  24.642 -72.538  1.00159.89           O  
ANISOU 1694  OD2 ASP A 202    19736  23377  17637   2843   1084   2068       O  
ATOM   1695  N   SER A 203      -3.333  21.877 -71.384  1.00189.34           N  
ANISOU 1695  N   SER A 203    23142  27528  21270   2585    795   1809       N  
ATOM   1696  CA  SER A 203      -4.685  21.691 -71.956  1.00190.30           C  
ANISOU 1696  CA  SER A 203    23103  27977  21224   2668    744   1861       C  
ATOM   1697  C   SER A 203      -5.653  22.834 -71.625  1.00190.76           C  
ANISOU 1697  C   SER A 203    23153  28087  21240   2874    813   2019       C  
ATOM   1698  O   SER A 203      -6.345  22.803 -70.601  1.00188.89           O  
ANISOU 1698  O   SER A 203    22892  27836  21040   2871    800   2002       O  
ATOM   1699  CB  SER A 203      -5.276  20.326 -71.569  1.00189.36           C  
ANISOU 1699  CB  SER A 203    22867  27998  21080   2501    628   1710       C  
ATOM   1700  OG  SER A 203      -5.265  20.133 -70.166  1.00187.78           O  
ANISOU 1700  OG  SER A 203    22721  27615  21009   2420    621   1641       O  
ATOM   1701  N   ALA A 204      -5.709  23.822 -72.521  1.00191.46           N  
ANISOU 1701  N   ALA A 204    23259  28241  21247   3056    890   2174       N  
ATOM   1702  CA  ALA A 204      -6.359  25.110 -72.253  1.00191.37           C  
ANISOU 1702  CA  ALA A 204    23280  28212  21217   3273    989   2344       C  
ATOM   1703  C   ALA A 204      -5.746  25.765 -71.012  1.00191.21           C  
ANISOU 1703  C   ALA A 204    23420  27855  21376   3259   1074   2338       C  
ATOM   1704  O   ALA A 204      -4.779  26.522 -71.120  1.00194.19           O  
ANISOU 1704  O   ALA A 204    23938  28012  21833   3295   1171   2386       O  
ATOM   1705  CB  ALA A 204      -7.871  24.949 -72.110  1.00189.30           C  
ANISOU 1705  CB  ALA A 204    22860  28227  20835   3354    936   2383       C  
ATOM   1706  N   ARG A 205      -6.303  25.454 -69.842  1.00186.54           N  
ANISOU 1706  N   ARG A 205    22803  27228  20844   3200   1038   2273       N  
ATOM   1707  CA  ARG A 205      -5.727  25.861 -68.560  1.00178.80           C  
ANISOU 1707  CA  ARG A 205    21960  25943  20033   3148   1099   2235       C  
ATOM   1708  C   ARG A 205      -6.007  24.809 -67.492  1.00172.82           C  
ANISOU 1708  C   ARG A 205    21150  25177  19335   2976   1001   2084       C  
ATOM   1709  O   ARG A 205      -7.039  24.137 -67.530  1.00170.90           O  
ANISOU 1709  O   ARG A 205    20765  25169  18997   2959    917   2054       O  
ATOM   1710  CB  ARG A 205      -6.276  27.224 -68.125  1.00179.77           C  
ANISOU 1710  CB  ARG A 205    22144  25991  20168   3350   1222   2390       C  
ATOM   1711  CG  ARG A 205      -5.446  28.407 -68.598  1.00181.20           C  
ANISOU 1711  CG  ARG A 205    22471  25985  20389   3467   1361   2504       C  
ATOM   1712  CD  ARG A 205      -6.299  29.651 -68.776  1.00183.44           C  
ANISOU 1712  CD  ARG A 205    22763  26327  20606   3717   1472   2695       C  
ATOM   1713  NE  ARG A 205      -5.584  30.702 -69.502  1.00184.70           N  
ANISOU 1713  NE  ARG A 205    23047  26356  20774   3838   1603   2815       N  
ATOM   1714  CZ  ARG A 205      -6.163  31.773 -70.043  1.00185.30           C  
ANISOU 1714  CZ  ARG A 205    23136  26499  20770   4071   1707   3000       C  
ATOM   1715  NH1 ARG A 205      -7.478  31.946 -69.953  1.00185.79           N  
ANISOU 1715  NH1 ARG A 205    23086  26768  20735   4213   1692   3088       N  
ATOM   1716  NH2 ARG A 205      -5.425  32.671 -70.682  1.00183.39           N  
ANISOU 1716  NH2 ARG A 205    23017  26118  20542   4164   1831   3100       N  
ATOM   1717  N   LYS A 206      -5.081  24.666 -66.548  1.00168.57           N  
ANISOU 1717  N   LYS A 206    20725  24372  18949   2846   1014   1988       N  
ATOM   1718  CA  LYS A 206      -5.247  23.720 -65.446  1.00165.68           C  
ANISOU 1718  CA  LYS A 206    20330  23968  18652   2684    932   1850       C  
ATOM   1719  C   LYS A 206      -6.267  24.184 -64.388  1.00168.05           C  
ANISOU 1719  C   LYS A 206    20611  24272  18966   2760    958   1894       C  
ATOM   1720  O   LYS A 206      -6.943  23.348 -63.785  1.00169.71           O  
ANISOU 1720  O   LYS A 206    20736  24581  19164   2668    876   1810       O  
ATOM   1721  CB  LYS A 206      -3.900  23.384 -64.797  1.00161.61           C  
ANISOU 1721  CB  LYS A 206    19935  23181  18287   2523    934   1736       C  
ATOM   1722  CG  LYS A 206      -3.914  22.089 -64.001  1.00159.79           C  
ANISOU 1722  CG  LYS A 206    19658  22948  18104   2333    828   1579       C  
ATOM   1723  CD  LYS A 206      -2.588  21.838 -63.308  1.00158.27           C  
ANISOU 1723  CD  LYS A 206    19584  22491  18058   2193    835   1480       C  
ATOM   1724  CE  LYS A 206      -2.654  20.585 -62.451  1.00156.27           C  
ANISOU 1724  CE  LYS A 206    19291  22231  17853   2020    737   1337       C  
ATOM   1725  NZ  LYS A 206      -1.349  20.290 -61.799  1.00154.89           N  
ANISOU 1725  NZ  LYS A 206    19220  21816  17812   1889    739   1243       N  
ATOM   1726  N   PRO A 207      -6.377  25.516 -64.155  1.00170.59           N  
ANISOU 1726  N   PRO A 207    21018  24483  19316   2925   1080   2024       N  
ATOM   1727  CA  PRO A 207      -7.421  26.038 -63.254  1.00166.67           C  
ANISOU 1727  CA  PRO A 207    20498  24008  18820   3019   1115   2080       C  
ATOM   1728  C   PRO A 207      -8.840  25.864 -63.801  1.00161.45           C  
ANISOU 1728  C   PRO A 207    19671  23670  18003   3129   1065   2147       C  
ATOM   1729  O   PRO A 207      -9.799  25.842 -63.026  1.00156.43           O  
ANISOU 1729  O   PRO A 207    18975  23103  17356   3154   1050   2147       O  
ATOM   1730  CB  PRO A 207      -7.080  27.532 -63.143  1.00170.30           C  
ANISOU 1730  CB  PRO A 207    21095  24274  19337   3178   1271   2211       C  
ATOM   1731  CG  PRO A 207      -6.241  27.829 -64.341  1.00173.25           C  
ANISOU 1731  CG  PRO A 207    21517  24629  19679   3218   1311   2262       C  
ATOM   1732  CD  PRO A 207      -5.443  26.582 -64.565  1.00172.65           C  
ANISOU 1732  CD  PRO A 207    21416  24556  19628   3012   1200   2110       C  
ATOM   1733  N   PHE A 208      -8.962  25.757 -65.125  1.00159.01           N  
ANISOU 1733  N   PHE A 208    19285  23562  17569   3194   1041   2202       N  
ATOM   1734  CA  PHE A 208     -10.243  25.471 -65.774  1.00153.92           C  
ANISOU 1734  CA  PHE A 208    18466  23257  16759   3282    980   2252       C  
ATOM   1735  C   PHE A 208     -10.780  24.116 -65.330  1.00148.42           C  
ANISOU 1735  C   PHE A 208    17649  22703  16040   3103    851   2100       C  
ATOM   1736  O   PHE A 208     -11.973  23.975 -65.063  1.00146.92           O  
ANISOU 1736  O   PHE A 208    17340  22709  15773   3149    817   2115       O  
ATOM   1737  CB  PHE A 208     -10.098  25.516 -67.302  1.00156.42           C  
ANISOU 1737  CB  PHE A 208    18728  23754  16948   3358    973   2323       C  
ATOM   1738  CG  PHE A 208     -11.327  25.062 -68.047  1.00155.87           C  
ANISOU 1738  CG  PHE A 208    18465  24060  16698   3418    896   2352       C  
ATOM   1739  CD1 PHE A 208     -12.454  25.876 -68.122  1.00158.52           C  
ANISOU 1739  CD1 PHE A 208    18727  24562  16938   3629    943   2498       C  
ATOM   1740  CD2 PHE A 208     -11.354  23.825 -68.683  1.00153.90           C  
ANISOU 1740  CD2 PHE A 208    18101  24002  16369   3265    781   2231       C  
ATOM   1741  CE1 PHE A 208     -13.586  25.462 -68.810  1.00159.26           C  
ANISOU 1741  CE1 PHE A 208    18631  25020  16858   3684    870   2523       C  
ATOM   1742  CE2 PHE A 208     -12.482  23.406 -69.372  1.00156.05           C  
ANISOU 1742  CE2 PHE A 208    18189  24632  16468   3310    712   2249       C  
ATOM   1743  CZ  PHE A 208     -13.600  24.225 -69.436  1.00158.32           C  
ANISOU 1743  CZ  PHE A 208    18398  25096  16658   3519    753   2395       C  
ATOM   1744  N   PHE A 209      -9.889  23.128 -65.252  1.00141.35           N  
ANISOU 1744  N   PHE A 209    16788  21705  15212   2900    786   1954       N  
ATOM   1745  CA  PHE A 209     -10.242  21.794 -64.770  1.00136.33           C  
ANISOU 1745  CA  PHE A 209    16064  21159  14575   2712    676   1798       C  
ATOM   1746  C   PHE A 209     -10.579  21.788 -63.278  1.00133.97           C  
ANISOU 1746  C   PHE A 209    15802  20722  14376   2662    682   1752       C  
ATOM   1747  O   PHE A 209     -11.552  21.157 -62.865  1.00133.93           O  
ANISOU 1747  O   PHE A 209    15686  20878  14320   2612    619   1697       O  
ATOM   1748  CB  PHE A 209      -9.115  20.792 -65.054  1.00131.99           C  
ANISOU 1748  CB  PHE A 209    15558  20508  14082   2519    619   1663       C  
ATOM   1749  CG  PHE A 209      -9.067  20.309 -66.480  1.00131.09           C  
ANISOU 1749  CG  PHE A 209    15356  20606  13843   2511    573   1658       C  
ATOM   1750  CD1 PHE A 209     -10.211  19.828 -67.111  1.00131.21           C  
ANISOU 1750  CD1 PHE A 209    15202  20950  13702   2532    511   1659       C  
ATOM   1751  CD2 PHE A 209      -7.867  20.302 -67.183  1.00130.66           C  
ANISOU 1751  CD2 PHE A 209    15384  20431  13826   2471    593   1644       C  
ATOM   1752  CE1 PHE A 209     -10.163  19.374 -68.421  1.00128.99           C  
ANISOU 1752  CE1 PHE A 209    14837  20873  13301   2516    469   1648       C  
ATOM   1753  CE2 PHE A 209      -7.815  19.847 -68.492  1.00129.06           C  
ANISOU 1753  CE2 PHE A 209    15102  20425  13508   2458    553   1635       C  
ATOM   1754  CZ  PHE A 209      -8.963  19.382 -69.111  1.00127.10           C  
ANISOU 1754  CZ  PHE A 209    14686  20504  13101   2479    491   1636       C  
ATOM   1755  N   LYS A 210      -9.777  22.494 -62.480  1.00131.46           N  
ANISOU 1755  N   LYS A 210    15637  20112  14196   2672    760   1770       N  
ATOM   1756  CA  LYS A 210      -9.936  22.493 -61.020  1.00128.81           C  
ANISOU 1756  CA  LYS A 210    15352  19621  13967   2611    770   1717       C  
ATOM   1757  C   LYS A 210     -11.250  23.134 -60.569  1.00130.62           C  
ANISOU 1757  C   LYS A 210    15512  19976  14139   2755    805   1808       C  
ATOM   1758  O   LYS A 210     -11.859  22.690 -59.593  1.00127.33           O  
ANISOU 1758  O   LYS A 210    15057  19573  13747   2684    767   1742       O  
ATOM   1759  CB  LYS A 210      -8.738  23.156 -60.327  1.00125.03           C  
ANISOU 1759  CB  LYS A 210    15051  18813  13640   2588    851   1714       C  
ATOM   1760  CG  LYS A 210      -8.641  22.851 -58.837  1.00121.13           C  
ANISOU 1760  CG  LYS A 210    14611  18150  13262   2470    839   1621       C  
ATOM   1761  CD  LYS A 210      -7.199  22.824 -58.358  1.00117.62           C  
ANISOU 1761  CD  LYS A 210    14308  17427  12953   2355    863   1549       C  
ATOM   1762  CE  LYS A 210      -7.114  22.374 -56.909  1.00114.51           C  
ANISOU 1762  CE  LYS A 210    13955  16894  12660   2225    836   1450       C  
ATOM   1763  NZ  LYS A 210      -5.743  21.916 -56.554  1.00110.40           N  
ANISOU 1763  NZ  LYS A 210    13531  16165  12249   2077    819   1350       N  
ATOM   1764  N   LEU A 211     -11.681  24.174 -61.280  1.00135.04           N  
ANISOU 1764  N   LEU A 211    16057  20628  14622   2962    879   1962       N  
ATOM   1765  CA  LEU A 211     -12.985  24.788 -61.019  1.00138.09           C  
ANISOU 1765  CA  LEU A 211    16362  21169  14936   3122    913   2062       C  
ATOM   1766  C   LEU A 211     -14.094  24.209 -61.911  1.00137.31           C  
ANISOU 1766  C   LEU A 211    16069  21438  14663   3161    831   2076       C  
ATOM   1767  O   LEU A 211     -15.240  24.666 -61.870  1.00140.70           O  
ANISOU 1767  O   LEU A 211    16405  22046  15009   3304    850   2164       O  
ATOM   1768  CB  LEU A 211     -12.914  26.322 -61.129  1.00141.36           C  
ANISOU 1768  CB  LEU A 211    16875  21465  15371   3341   1055   2230       C  
ATOM   1769  CG  LEU A 211     -12.551  27.094 -59.847  1.00138.39           C  
ANISOU 1769  CG  LEU A 211    16644  20794  15142   3347   1152   2234       C  
ATOM   1770  CD1 LEU A 211     -11.045  27.278 -59.716  1.00134.41           C  
ANISOU 1770  CD1 LEU A 211    16305  19997  14766   3250   1200   2185       C  
ATOM   1771  CD2 LEU A 211     -13.260  28.442 -59.803  1.00137.17           C  
ANISOU 1771  CD2 LEU A 211    16513  20644  14961   3586   1277   2402       C  
ATOM   1772  N   LEU A 212     -13.744  23.199 -62.707  1.00131.42           N  
ANISOU 1772  N   LEU A 212    15262  20809  13862   3031    742   1985       N  
ATOM   1773  CA  LEU A 212     -14.732  22.404 -63.434  1.00125.72           C  
ANISOU 1773  CA  LEU A 212    14351  20433  12981   3011    651   1955       C  
ATOM   1774  C   LEU A 212     -15.160  21.223 -62.569  1.00121.97           C  
ANISOU 1774  C   LEU A 212    13813  19997  12533   2815    562   1796       C  
ATOM   1775  O   LEU A 212     -16.350  20.936 -62.438  1.00119.58           O  
ANISOU 1775  O   LEU A 212    13370  19926  12137   2832    522   1789       O  
ATOM   1776  CB  LEU A 212     -14.156  21.914 -64.770  1.00122.86           C  
ANISOU 1776  CB  LEU A 212    13955  20183  12540   2966    607   1933       C  
ATOM   1777  CG  LEU A 212     -15.087  21.510 -65.924  1.00121.96           C  
ANISOU 1777  CG  LEU A 212    13654  20453  12232   3013    544   1956       C  
ATOM   1778  CD1 LEU A 212     -15.521  20.056 -65.820  1.00119.80           C  
ANISOU 1778  CD1 LEU A 212    13261  20343  11914   2803    432   1785       C  
ATOM   1779  CD2 LEU A 212     -16.291  22.439 -66.044  1.00124.52           C  
ANISOU 1779  CD2 LEU A 212    13883  20979  12447   3241    589   2111       C  
ATOM   1780  N   THR A 213     -14.179  20.548 -61.972  1.00121.92           N  
ANISOU 1780  N   THR A 213    13909  19760  12653   2630    537   1671       N  
ATOM   1781  CA  THR A 213     -14.449  19.468 -61.022  1.00122.24           C  
ANISOU 1781  CA  THR A 213    13919  19785  12741   2443    467   1524       C  
ATOM   1782  C   THR A 213     -15.081  19.997 -59.736  1.00120.39           C  
ANISOU 1782  C   THR A 213    13710  19463  12568   2495    509   1553       C  
ATOM   1783  O   THR A 213     -15.860  19.298 -59.086  1.00121.41           O  
ANISOU 1783  O   THR A 213    13759  19690  12679   2402    457   1472       O  
ATOM   1784  CB  THR A 213     -13.181  18.636 -60.694  1.00121.15           C  
ANISOU 1784  CB  THR A 213    13891  19413  12724   2245    435   1393       C  
ATOM   1785  OG1 THR A 213     -13.482  17.687 -59.663  1.00121.01           O  
ANISOU 1785  OG1 THR A 213    13857  19364  12758   2082    381   1267       O  
ATOM   1786  CG2 THR A 213     -12.036  19.524 -60.225  1.00120.92           C  
ANISOU 1786  CG2 THR A 213    14039  19069  12834   2292    518   1444       C  
ATOM   1787  N   SER A 214     -14.747  21.237 -59.383  1.00119.97           N  
ANISOU 1787  N   SER A 214    13769  19225  12586   2639    609   1666       N  
ATOM   1788  CA  SER A 214     -15.336  21.900 -58.224  1.00120.29           C  
ANISOU 1788  CA  SER A 214    13841  19178  12683   2711    665   1707       C  
ATOM   1789  C   SER A 214     -16.830  22.126 -58.434  1.00120.54           C  
ANISOU 1789  C   SER A 214    13715  19503  12582   2842    657   1780       C  
ATOM   1790  O   SER A 214     -17.614  22.084 -57.484  1.00119.17           O  
ANISOU 1790  O   SER A 214    13504  19351  12422   2832    655   1758       O  
ATOM   1791  CB  SER A 214     -14.633  23.229 -57.950  1.00120.99           C  
ANISOU 1791  CB  SER A 214    14086  19015  12868   2843    786   1816       C  
ATOM   1792  OG  SER A 214     -14.864  23.663 -56.622  1.00121.22           O  
ANISOU 1792  OG  SER A 214    14180  18885  12990   2847    836   1811       O  
ATOM   1793  N   LYS A 215     -17.217  22.357 -59.687  1.00119.94           N  
ANISOU 1793  N   LYS A 215    13542  19658  12371   2965    652   1867       N  
ATOM   1794  CA  LYS A 215     -18.625  22.461 -60.052  1.00122.74           C  
ANISOU 1794  CA  LYS A 215    13722  20335  12576   3085    632   1932       C  
ATOM   1795  C   LYS A 215     -19.341  21.113 -59.950  1.00121.03           C  
ANISOU 1795  C   LYS A 215    13359  20336  12288   2907    519   1787       C  
ATOM   1796  O   LYS A 215     -20.551  21.065 -59.713  1.00122.42           O  
ANISOU 1796  O   LYS A 215    13404  20728  12379   2955    500   1800       O  
ATOM   1797  CB  LYS A 215     -18.781  23.045 -61.459  1.00125.43           C  
ANISOU 1797  CB  LYS A 215    13998  20874  12786   3261    654   2064       C  
ATOM   1798  CG  LYS A 215     -18.816  24.565 -61.499  1.00127.65           C  
ANISOU 1798  CG  LYS A 215    14360  21056  13084   3511    780   2250       C  
ATOM   1799  CD  LYS A 215     -19.341  25.075 -62.833  1.00130.48           C  
ANISOU 1799  CD  LYS A 215    14611  21685  13279   3706    794   2391       C  
ATOM   1800  CE  LYS A 215     -19.822  26.515 -62.723  1.00129.45           C  
ANISOU 1800  CE  LYS A 215    14519  21522  13141   3973    917   2581       C  
ATOM   1801  NZ  LYS A 215     -20.384  27.019 -64.006  1.00131.59           N  
ANISOU 1801  NZ  LYS A 215    14681  22071  13245   4178    931   2730       N  
ATOM   1802  N   ILE A 216     -18.587  20.025 -60.115  1.00114.34           N  
ANISOU 1802  N   ILE A 216    12538  19427  11476   2701    451   1649       N  
ATOM   1803  CA  ILE A 216     -19.145  18.672 -60.033  1.00109.99           C  
ANISOU 1803  CA  ILE A 216    11867  19054  10867   2511    354   1499       C  
ATOM   1804  C   ILE A 216     -19.348  18.199 -58.587  1.00109.53           C  
ANISOU 1804  C   ILE A 216    11851  18851  10913   2380    343   1400       C  
ATOM   1805  O   ILE A 216     -20.399  17.646 -58.258  1.00111.26           O  
ANISOU 1805  O   ILE A 216    11946  19264  11064   2326    300   1343       O  
ATOM   1806  CB  ILE A 216     -18.303  17.653 -60.831  1.00105.86           C  
ANISOU 1806  CB  ILE A 216    11353  18531  10336   2345    293   1389       C  
ATOM   1807  CG1 ILE A 216     -18.382  17.968 -62.327  1.00107.35           C  
ANISOU 1807  CG1 ILE A 216    11458  18942  10386   2462    290   1474       C  
ATOM   1808  CG2 ILE A 216     -18.781  16.230 -60.570  1.00103.92           C  
ANISOU 1808  CG2 ILE A 216    11014  18412  10058   2128    208   1221       C  
ATOM   1809  CD1 ILE A 216     -17.246  17.391 -63.144  1.00107.63           C  
ANISOU 1809  CD1 ILE A 216    11553  18897  10442   2351    263   1409       C  
ATOM   1810  N   TYR A 217     -18.355  18.429 -57.726  1.00106.94           N  
ANISOU 1810  N   TYR A 217    11692  18194  10743   2331    383   1381       N  
ATOM   1811  CA  TYR A 217     -18.462  18.037 -56.315  1.00105.66           C  
ANISOU 1811  CA  TYR A 217    11583  17879  10683   2212    377   1295       C  
ATOM   1812  C   TYR A 217     -19.655  18.685 -55.618  1.00108.83           C  
ANISOU 1812  C   TYR A 217    11918  18381  11052   2333    413   1363       C  
ATOM   1813  O   TYR A 217     -20.187  18.142 -54.647  1.00108.80           O  
ANISOU 1813  O   TYR A 217    11888  18375  11075   2229    387   1281       O  
ATOM   1814  CB  TYR A 217     -17.167  18.324 -55.557  1.00104.06           C  
ANISOU 1814  CB  TYR A 217    11571  17318  10646   2162    420   1279       C  
ATOM   1815  CG  TYR A 217     -16.132  17.234 -55.708  1.00102.64           C  
ANISOU 1815  CG  TYR A 217    11449  17024  10525   1967    363   1153       C  
ATOM   1816  CD1 TYR A 217     -16.273  16.014 -55.046  1.00103.21           C  
ANISOU 1816  CD1 TYR A 217    11500  17092  10623   1773    299   1013       C  
ATOM   1817  CD2 TYR A 217     -15.013  17.416 -56.518  1.00103.98           C  
ANISOU 1817  CD2 TYR A 217    11697  17088  10722   1980    377   1176       C  
ATOM   1818  CE1 TYR A 217     -15.329  15.007 -55.187  1.00101.73           C  
ANISOU 1818  CE1 TYR A 217    11367  16796  10489   1604    253    903       C  
ATOM   1819  CE2 TYR A 217     -14.061  16.415 -56.664  1.00101.64           C  
ANISOU 1819  CE2 TYR A 217    11451  16688  10478   1808    328   1062       C  
ATOM   1820  CZ  TYR A 217     -14.225  15.214 -55.999  1.00 99.33           C  
ANISOU 1820  CZ  TYR A 217    11136  16391  10212   1625    267    928       C  
ATOM   1821  OH  TYR A 217     -13.286  14.220 -56.143  1.00 97.38           O  
ANISOU 1821  OH  TYR A 217    10941  16038  10018   1464    225    821       O  
ATOM   1822  N   LYS A 218     -20.069  19.846 -56.123  1.00113.22           N  
ANISOU 1822  N   LYS A 218    12447  19023  11548   2556    478   1515       N  
ATOM   1823  CA  LYS A 218     -21.345  20.440 -55.748  1.00114.84           C  
ANISOU 1823  CA  LYS A 218    12554  19393  11688   2695    509   1592       C  
ATOM   1824  C   LYS A 218     -22.466  19.465 -56.080  1.00115.33           C  
ANISOU 1824  C   LYS A 218    12421  19786  11613   2613    423   1514       C  
ATOM   1825  O   LYS A 218     -23.136  18.958 -55.182  1.00116.79           O  
ANISOU 1825  O   LYS A 218    12559  20005  11809   2519    397   1434       O  
ATOM   1826  CB  LYS A 218     -21.574  21.759 -56.491  1.00118.73           C  
ANISOU 1826  CB  LYS A 218    13037  19954  12118   2957    590   1776       C  
ATOM   1827  CG  LYS A 218     -20.639  22.890 -56.098  1.00122.15           C  
ANISOU 1827  CG  LYS A 218    13659  20069  12681   3059    698   1866       C  
ATOM   1828  CD  LYS A 218     -20.980  24.161 -56.862  1.00124.47           C  
ANISOU 1828  CD  LYS A 218    13938  20448  12904   3325    785   2052       C  
ATOM   1829  CE  LYS A 218     -19.912  25.226 -56.678  1.00123.65           C  
ANISOU 1829  CE  LYS A 218    14030  20027  12924   3410    898   2133       C  
ATOM   1830  NZ  LYS A 218     -20.249  26.469 -57.422  1.00125.50           N  
ANISOU 1830  NZ  LYS A 218    14260  20333  13090   3674    994   2320       N  
ATOM   1831  N   VAL A 219     -22.633  19.182 -57.375  1.00115.18           N  
ANISOU 1831  N   VAL A 219    12292  20008  11463   2639    380   1529       N  
ATOM   1832  CA  VAL A 219     -23.711  18.312 -57.877  1.00115.61           C  
ANISOU 1832  CA  VAL A 219    12145  20413  11365   2568    302   1457       C  
ATOM   1833  C   VAL A 219     -23.798  17.000 -57.098  1.00115.32           C  
ANISOU 1833  C   VAL A 219    12098  20343  11374   2315    238   1275       C  
ATOM   1834  O   VAL A 219     -24.893  16.488 -56.849  1.00115.50           O  
ANISOU 1834  O   VAL A 219    11982  20587  11315   2261    201   1216       O  
ATOM   1835  CB  VAL A 219     -23.544  17.994 -59.386  1.00113.61           C  
ANISOU 1835  CB  VAL A 219    11805  20376  10986   2577    258   1465       C  
ATOM   1836  CG1 VAL A 219     -24.751  17.231 -59.915  1.00112.43           C  
ANISOU 1836  CG1 VAL A 219    11436  20616  10665   2521    187   1401       C  
ATOM   1837  CG2 VAL A 219     -23.331  19.269 -60.189  1.00115.28           C  
ANISOU 1837  CG2 VAL A 219    12045  20597  11158   2824    326   1650       C  
ATOM   1838  N   LEU A 220     -22.639  16.472 -56.711  1.00114.52           N  
ANISOU 1838  N   LEU A 220    12144  19964  11401   2162    229   1188       N  
ATOM   1839  CA  LEU A 220     -22.564  15.227 -55.957  1.00113.71           C  
ANISOU 1839  CA  LEU A 220    12057  19789  11356   1924    178   1022       C  
ATOM   1840  C   LEU A 220     -23.327  15.333 -54.639  1.00114.51           C  
ANISOU 1840  C   LEU A 220    12154  19851  11503   1913    197   1006       C  
ATOM   1841  O   LEU A 220     -24.081  14.430 -54.280  1.00113.76           O  
ANISOU 1841  O   LEU A 220    11965  19894  11362   1777    153    898       O  
ATOM   1842  CB  LEU A 220     -21.105  14.850 -55.692  1.00111.89           C  
ANISOU 1842  CB  LEU A 220    12002  19241  11267   1802    179    961       C  
ATOM   1843  CG  LEU A 220     -20.678  13.398 -55.934  1.00111.79           C  
ANISOU 1843  CG  LEU A 220    11983  19231  11257   1570    113    801       C  
ATOM   1844  CD1 LEU A 220     -19.243  13.199 -55.468  1.00110.07           C  
ANISOU 1844  CD1 LEU A 220    11950  18676  11196   1480    125    760       C  
ATOM   1845  CD2 LEU A 220     -21.602  12.400 -55.249  1.00111.85           C  
ANISOU 1845  CD2 LEU A 220    11904  19359  11235   1414     73    680       C  
ATOM   1846  N   GLU A 221     -23.138  16.445 -53.931  1.00117.38           N  
ANISOU 1846  N   GLU A 221    12618  20026  11953   2054    269   1110       N  
ATOM   1847  CA  GLU A 221     -23.841  16.682 -52.666  1.00120.33           C  
ANISOU 1847  CA  GLU A 221    12994  20351  12372   2062    298   1106       C  
ATOM   1848  C   GLU A 221     -25.102  17.545 -52.828  1.00123.87           C  
ANISOU 1848  C   GLU A 221    13310  21039  12714   2261    332   1220       C  
ATOM   1849  O   GLU A 221     -25.570  18.159 -51.869  1.00127.66           O  
ANISOU 1849  O   GLU A 221    13815  21446  13242   2334    383   1263       O  
ATOM   1850  CB  GLU A 221     -22.891  17.261 -51.598  1.00121.36           C  
ANISOU 1850  CB  GLU A 221    13319  20118  12672   2065    357   1127       C  
ATOM   1851  CG  GLU A 221     -22.002  18.411 -52.064  1.00120.98           C  
ANISOU 1851  CG  GLU A 221    13386  19904  12675   2227    427   1252       C  
ATOM   1852  CD  GLU A 221     -22.590  19.779 -51.766  1.00121.00           C  
ANISOU 1852  CD  GLU A 221    13393  19906  12675   2449    517   1395       C  
ATOM   1853  OE1 GLU A 221     -22.927  20.045 -50.593  1.00117.57           O  
ANISOU 1853  OE1 GLU A 221    12998  19364  12307   2444    553   1386       O  
ATOM   1854  OE2 GLU A 221     -22.695  20.600 -52.702  1.00122.10           O  
ANISOU 1854  OE2 GLU A 221    13500  20145  12746   2631    557   1520       O  
ATOM   1855  N   GLU A 222     -25.653  17.567 -54.042  1.00126.45           N  
ANISOU 1855  N   GLU A 222    13493  21658  12893   2346    305   1267       N  
ATOM   1856  CA  GLU A 222     -26.894  18.292 -54.324  1.00126.22           C  
ANISOU 1856  CA  GLU A 222    13314  21900  12742   2538    329   1374       C  
ATOM   1857  C   GLU A 222     -28.053  17.327 -54.550  1.00125.69           C  
ANISOU 1857  C   GLU A 222    13046  22172  12537   2431    256   1275       C  
ATOM   1858  O   GLU A 222     -28.949  17.212 -53.711  1.00125.36           O  
ANISOU 1858  O   GLU A 222    12940  22204  12488   2407    258   1241       O  
ATOM   1859  CB  GLU A 222     -26.733  19.201 -55.551  1.00131.12           C  
ANISOU 1859  CB  GLU A 222    13911  22626  13282   2750    363   1526       C  
ATOM   1860  CG  GLU A 222     -25.787  20.380 -55.363  1.00131.84           C  
ANISOU 1860  CG  GLU A 222    14186  22414  13493   2897    456   1648       C  
ATOM   1861  CD  GLU A 222     -26.331  21.445 -54.428  1.00134.23           C  
ANISOU 1861  CD  GLU A 222    14526  22625  13848   3058    544   1748       C  
ATOM   1862  OE1 GLU A 222     -27.564  21.658 -54.407  1.00136.74           O  
ANISOU 1862  OE1 GLU A 222    14695  23193  14063   3162    545   1794       O  
ATOM   1863  OE2 GLU A 222     -25.517  22.078 -53.721  1.00131.37           O  
ANISOU 1863  OE2 GLU A 222    14340  21944  13628   3080    615   1779       O  
ATOM   1864  N   LYS A 223     -28.029  16.637 -55.689  1.00125.04           N  
ANISOU 1864  N   LYS A 223    12866  22298  12345   2361    195   1225       N  
ATOM   1865  CA  LYS A 223     -29.103  15.718 -56.063  1.00126.07           C  
ANISOU 1865  CA  LYS A 223    12796  22776  12329   2253    129   1125       C  
ATOM   1866  C   LYS A 223     -28.898  14.322 -55.465  1.00124.33           C  
ANISOU 1866  C   LYS A 223    12605  22468  12164   1966     78    930       C  
ATOM   1867  O   LYS A 223     -29.700  13.413 -55.698  1.00126.82           O  
ANISOU 1867  O   LYS A 223    12771  23039  12372   1834     28    820       O  
ATOM   1868  CB  LYS A 223     -29.260  15.648 -57.592  1.00126.59           C  
ANISOU 1868  CB  LYS A 223    12729  23135  12234   2314     91   1160       C  
ATOM   1869  CG  LYS A 223     -29.545  16.987 -58.272  1.00125.80           C  
ANISOU 1869  CG  LYS A 223    12585  23154  12058   2608    141   1360       C  
ATOM   1870  CD  LYS A 223     -30.754  17.698 -57.671  1.00126.61           C  
ANISOU 1870  CD  LYS A 223    12585  23406  12112   2767    177   1445       C  
ATOM   1871  CE  LYS A 223     -30.882  19.121 -58.197  1.00125.99           C  
ANISOU 1871  CE  LYS A 223    12506  23372  11991   3073    247   1658       C  
ATOM   1872  NZ  LYS A 223     -31.790  19.957 -57.362  1.00122.66           N  
ANISOU 1872  NZ  LYS A 223    12048  22977  11578   3237    306   1750       N  
ATOM   1873  N   TYR A 224     -27.821  14.166 -54.696  1.00121.81           N  
ANISOU 1873  N   TYR A 224    12478  21789  12011   1870     98    890       N  
ATOM   1874  CA  TYR A 224     -27.567  12.947 -53.921  1.00118.33           C  
ANISOU 1874  CA  TYR A 224    12096  21216  11648   1617     65    723       C  
ATOM   1875  C   TYR A 224     -27.464  13.310 -52.441  1.00116.10           C  
ANISOU 1875  C   TYR A 224    11936  20672  11504   1617    109    733       C  
ATOM   1876  O   TYR A 224     -26.477  13.909 -52.008  1.00113.00           O  
ANISOU 1876  O   TYR A 224    11711  19984  11240   1671    150    792       O  
ATOM   1877  CB  TYR A 224     -26.285  12.243 -54.402  1.00115.01           C  
ANISOU 1877  CB  TYR A 224    11790  20612  11294   1480     40    650       C  
ATOM   1878  CG  TYR A 224     -26.263  11.966 -55.894  1.00115.21           C  
ANISOU 1878  CG  TYR A 224    11710  20873  11190   1487      3    646       C  
ATOM   1879  CD1 TYR A 224     -25.747  12.903 -56.792  1.00113.42           C  
ANISOU 1879  CD1 TYR A 224    11510  20645  10940   1669     26    780       C  
ATOM   1880  CD2 TYR A 224     -26.777  10.776 -56.409  1.00115.70           C  
ANISOU 1880  CD2 TYR A 224    11647  21164  11149   1309    -50    507       C  
ATOM   1881  CE1 TYR A 224     -25.746  12.661 -58.158  1.00113.10           C  
ANISOU 1881  CE1 TYR A 224    11370  20829  10773   1678     -7    778       C  
ATOM   1882  CE2 TYR A 224     -26.776  10.524 -57.773  1.00113.29           C  
ANISOU 1882  CE2 TYR A 224    11241  21085  10718   1310    -82    498       C  
ATOM   1883  CZ  TYR A 224     -26.261  11.467 -58.642  1.00113.21           C  
ANISOU 1883  CZ  TYR A 224    11255  21074  10684   1496    -64    636       C  
ATOM   1884  OH  TYR A 224     -26.259  11.215 -59.994  1.00110.08           O  
ANISOU 1884  OH  TYR A 224    10758  20909  10158   1496    -96    627       O  
ATOM   1885  N   LYS A 225     -28.498  12.959 -51.677  1.00119.49           N  
ANISOU 1885  N   LYS A 225    12277  21220  11901   1554    103    674       N  
ATOM   1886  CA  LYS A 225     -28.604  13.342 -50.261  1.00121.12           C  
ANISOU 1886  CA  LYS A 225    12575  21223  12218   1564    146    686       C  
ATOM   1887  C   LYS A 225     -27.617  12.599 -49.353  1.00120.69           C  
ANISOU 1887  C   LYS A 225    12691  20852  12310   1375    140    584       C  
ATOM   1888  O   LYS A 225     -27.851  12.457 -48.147  1.00118.30           O  
ANISOU 1888  O   LYS A 225    12438  20431  12079   1308    157    543       O  
ATOM   1889  CB  LYS A 225     -30.040  13.154 -49.752  1.00120.17           C  
ANISOU 1889  CB  LYS A 225    12302  21342  12012   1549    141    650       C  
ATOM   1890  CG  LYS A 225     -30.977  14.307 -50.072  1.00121.02           C  
ANISOU 1890  CG  LYS A 225    12290  21665  12027   1792    177    791       C  
ATOM   1891  CD  LYS A 225     -32.288  14.176 -49.312  1.00121.06           C  
ANISOU 1891  CD  LYS A 225    12169  21849  11976   1774    181    753       C  
ATOM   1892  CE  LYS A 225     -33.233  15.321 -49.637  1.00119.73           C  
ANISOU 1892  CE  LYS A 225    11876  21901  11713   2028    220    898       C  
ATOM   1893  NZ  LYS A 225     -34.552  15.148 -48.972  1.00116.71           N  
ANISOU 1893  NZ  LYS A 225    11354  21723  11265   2008    220    855       N  
ATOM   1894  N   THR A 226     -26.510  12.142 -49.939  1.00119.74           N  
ANISOU 1894  N   THR A 226    12659  20602  12234   1297    117    549       N  
ATOM   1895  CA  THR A 226     -25.466  11.447 -49.198  1.00117.28           C  
ANISOU 1895  CA  THR A 226    12508  19995  12057   1133    111    462       C  
ATOM   1896  C   THR A 226     -24.703  12.420 -48.301  1.00116.80           C  
ANISOU 1896  C   THR A 226    12610  19635  12133   1232    166    548       C  
ATOM   1897  O   THR A 226     -24.379  13.540 -48.714  1.00113.42           O  
ANISOU 1897  O   THR A 226    12216  19164  11714   1413    207    671       O  
ATOM   1898  CB  THR A 226     -24.469  10.749 -50.148  1.00117.47           C  
ANISOU 1898  CB  THR A 226    12576  19969  12086   1037     75    408       C  
ATOM   1899  OG1 THR A 226     -25.157  10.270 -51.311  1.00117.13           O  
ANISOU 1899  OG1 THR A 226    12369  20239  11893   1015     37    372       O  
ATOM   1900  CG2 THR A 226     -23.768   9.579 -49.443  1.00116.14           C  
ANISOU 1900  CG2 THR A 226    12517  19593  12016    819     54    278       C  
ATOM   1901  N   SER A 227     -24.439  11.989 -47.070  1.00116.79           N  
ANISOU 1901  N   SER A 227    12708  19434  12234   1111    171    480       N  
ATOM   1902  CA  SER A 227     -23.566  12.720 -46.155  1.00115.88           C  
ANISOU 1902  CA  SER A 227    12756  19017  12253   1163    218    534       C  
ATOM   1903  C   SER A 227     -22.311  11.888 -45.856  1.00113.40           C  
ANISOU 1903  C   SER A 227    12580  18463  12044   1002    193    450       C  
ATOM   1904  O   SER A 227     -21.269  12.072 -46.494  1.00113.31           O  
ANISOU 1904  O   SER A 227    12642  18338  12070   1030    193    479       O  
ATOM   1905  CB  SER A 227     -24.313  13.085 -44.865  1.00116.79           C  
ANISOU 1905  CB  SER A 227    12875  19098  12401   1180    254    541       C  
ATOM   1906  OG  SER A 227     -24.877  11.936 -44.254  1.00117.73           O  
ANISOU 1906  OG  SER A 227    12950  19278  12503   1000    217    420       O  
ATOM   1907  N   GLY A 228     -22.422  10.970 -44.897  1.00107.41           N  
ANISOU 1907  N   GLY A 228    11852  17630  11326    838    173    349       N  
ATOM   1908  CA  GLY A 228     -21.375   9.989 -44.634  1.00 99.17           C  
ANISOU 1908  CA  GLY A 228    10918  16394  10365    676    145    262       C  
ATOM   1909  C   GLY A 228     -20.156  10.509 -43.886  1.00 92.88           C  
ANISOU 1909  C   GLY A 228    10291  15297   9702    700    173    299       C  
ATOM   1910  O   GLY A 228     -19.421  11.373 -44.380  1.00 95.89           O  
ANISOU 1910  O   GLY A 228    10726  15592  10114    817    198    379       O  
ATOM   1911  N   SER A 229     -19.960   9.987 -42.680  1.00 81.18           N  
ANISOU 1911  N   SER A 229     8888  13661   8294    585    172    239       N  
ATOM   1912  CA  SER A 229     -18.665  10.048 -42.001  1.00 74.28           C  
ANISOU 1912  CA  SER A 229     8170  12509   7542    550    181    238       C  
ATOM   1913  C   SER A 229     -18.412   8.714 -41.311  1.00 65.60           C  
ANISOU 1913  C   SER A 229     7119  11322   6481    362    147    130       C  
ATOM   1914  O   SER A 229     -19.179   8.310 -40.436  1.00 64.66           O  
ANISOU 1914  O   SER A 229     6977  11238   6352    291    149     87       O  
ATOM   1915  CB  SER A 229     -18.624  11.185 -40.982  1.00 73.97           C  
ANISOU 1915  CB  SER A 229     8201  12338   7566    650    235    308       C  
ATOM   1916  OG  SER A 229     -17.479  11.065 -40.158  1.00 71.33           O  
ANISOU 1916  OG  SER A 229     8005  11755   7340    585    238    286       O  
ATOM   1917  N   LEU A 230     -17.350   8.028 -41.723  1.00 59.50           N  
ANISOU 1917  N   LEU A 230     6413  10438   5752    284    121     89       N  
ATOM   1918  CA  LEU A 230     -17.064   6.671 -41.252  1.00 57.35           C  
ANISOU 1918  CA  LEU A 230     6188  10090   5512    110     93    -10       C  
ATOM   1919  C   LEU A 230     -17.164   6.564 -39.734  1.00 54.84           C  
ANISOU 1919  C   LEU A 230     5940   9642   5255     54    108    -27       C  
ATOM   1920  O   LEU A 230     -17.770   5.631 -39.208  1.00 54.78           O  
ANISOU 1920  O   LEU A 230     5911   9676   5227    -65     98    -98       O  
ATOM   1921  CB  LEU A 230     -15.670   6.233 -41.702  1.00 55.90           C  
ANISOU 1921  CB  LEU A 230     6095   9748   5393     70     76    -28       C  
ATOM   1922  CG  LEU A 230     -15.481   4.804 -42.220  1.00 56.25           C  
ANISOU 1922  CG  LEU A 230     6132   9817   5421    -77     46   -125       C  
ATOM   1923  CD1 LEU A 230     -14.016   4.412 -42.087  1.00 53.21           C  
ANISOU 1923  CD1 LEU A 230     5872   9213   5133   -119     37   -138       C  
ATOM   1924  CD2 LEU A 230     -16.386   3.787 -41.529  1.00 55.08           C  
ANISOU 1924  CD2 LEU A 230     5952   9732   5243   -212     43   -207       C  
ATOM   1925  N   TYR A 231     -16.575   7.536 -39.043  1.00 53.09           N  
ANISOU 1925  N   TYR A 231     5801   9266   5103    140    135     37       N  
ATOM   1926  CA  TYR A 231     -16.556   7.554 -37.594  1.00 51.60           C  
ANISOU 1926  CA  TYR A 231     5685   8946   4972     96    150     27       C  
ATOM   1927  C   TYR A 231     -17.955   7.685 -37.001  1.00 53.38           C  
ANISOU 1927  C   TYR A 231     5829   9312   5140     97    168     22       C  
ATOM   1928  O   TYR A 231     -18.317   6.950 -36.079  1.00 54.59           O  
ANISOU 1928  O   TYR A 231     5999   9438   5301    -12    163    -34       O  
ATOM   1929  CB  TYR A 231     -15.645   8.677 -37.080  1.00 49.35           C  
ANISOU 1929  CB  TYR A 231     5498   8485   4766    191    182     96       C  
ATOM   1930  CG  TYR A 231     -15.575   8.734 -35.578  1.00 47.14           C  
ANISOU 1930  CG  TYR A 231     5293   8074   4542    144    198     84       C  
ATOM   1931  CD1 TYR A 231     -14.644   7.961 -34.876  1.00 45.39           C  
ANISOU 1931  CD1 TYR A 231     5168   7691   4385     39    175     40       C  
ATOM   1932  CD2 TYR A 231     -16.452   9.536 -34.851  1.00 46.92           C  
ANISOU 1932  CD2 TYR A 231     5237   8090   4499    207    237    118       C  
ATOM   1933  CE1 TYR A 231     -14.578   7.999 -33.497  1.00 43.84           C  
ANISOU 1933  CE1 TYR A 231     5038   7387   4233     -2    188     31       C  
ATOM   1934  CE2 TYR A 231     -16.399   9.577 -33.466  1.00 47.13           C  
ANISOU 1934  CE2 TYR A 231     5331   8002   4571    159    253    104       C  
ATOM   1935  CZ  TYR A 231     -15.455   8.804 -32.795  1.00 46.27           C  
ANISOU 1935  CZ  TYR A 231     5317   7740   4522     52    226     61       C  
ATOM   1936  OH  TYR A 231     -15.393   8.831 -31.420  1.00 47.46           O  
ANISOU 1936  OH  TYR A 231     5532   7786   4711      4    240     48       O  
ATOM   1937  N   THR A 232     -18.731   8.631 -37.524  1.00 55.38           N  
ANISOU 1937  N   THR A 232     5994   9712   5335    226    192     83       N  
ATOM   1938  CA  THR A 232     -20.097   8.857 -37.053  1.00 57.08           C  
ANISOU 1938  CA  THR A 232     6118  10080   5490    246    212     84       C  
ATOM   1939  C   THR A 232     -20.969   7.631 -37.304  1.00 56.13           C  
ANISOU 1939  C   THR A 232     5905  10128   5295    115    180     -4       C  
ATOM   1940  O   THR A 232     -21.698   7.196 -36.418  1.00 57.09           O  
ANISOU 1940  O   THR A 232     6009  10276   5404     35    187    -49       O  
ATOM   1941  CB  THR A 232     -20.735  10.086 -37.726  1.00 58.90           C  
ANISOU 1941  CB  THR A 232     6263  10451   5664    424    245    175       C  
ATOM   1942  OG1 THR A 232     -19.843  11.202 -37.628  1.00 61.70           O  
ANISOU 1942  OG1 THR A 232     6712  10641   6090    540    283    254       O  
ATOM   1943  CG2 THR A 232     -22.045  10.442 -37.057  1.00 59.53           C  
ANISOU 1943  CG2 THR A 232     6262  10658   5695    458    273    184       C  
ATOM   1944  N   CYS A 233     -20.874   7.068 -38.506  1.00 55.66           N  
ANISOU 1944  N   CYS A 233     5788  10176   5183     86    151    -34       N  
ATOM   1945  CA  CYS A 233     -21.658   5.885 -38.864  1.00 57.53           C  
ANISOU 1945  CA  CYS A 233     5935  10578   5344    -47    127   -128       C  
ATOM   1946  C   CYS A 233     -21.387   4.729 -37.902  1.00 55.81           C  
ANISOU 1946  C   CYS A 233     5803  10221   5181   -219    121   -213       C  
ATOM   1947  O   CYS A 233     -22.305   4.231 -37.254  1.00 55.96           O  
ANISOU 1947  O   CYS A 233     5779  10316   5166   -303    131   -265       O  
ATOM   1948  CB  CYS A 233     -21.372   5.448 -40.307  1.00 60.86           C  
ANISOU 1948  CB  CYS A 233     6302  11108   5714    -60     99   -152       C  
ATOM   1949  SG  CYS A 233     -21.956   6.571 -41.603  1.00 63.40           S  
ANISOU 1949  SG  CYS A 233     6490  11661   5936    123    102    -63       S  
ATOM   1950  N   TRP A 234     -20.118   4.333 -37.789  1.00 53.96           N  
ANISOU 1950  N   TRP A 234     5691   9780   5029   -263    110   -222       N  
ATOM   1951  CA  TRP A 234     -19.728   3.211 -36.935  1.00 51.77           C  
ANISOU 1951  CA  TRP A 234     5505   9357   4805   -414    107   -292       C  
ATOM   1952  C   TRP A 234     -20.113   3.433 -35.505  1.00 51.62           C  
ANISOU 1952  C   TRP A 234     5530   9263   4820   -428    128   -282       C  
ATOM   1953  O   TRP A 234     -20.533   2.505 -34.809  1.00 52.54           O  
ANISOU 1953  O   TRP A 234     5662   9368   4932   -557    134   -348       O  
ATOM   1954  CB  TRP A 234     -18.229   2.955 -37.033  1.00 49.36           C  
ANISOU 1954  CB  TRP A 234     5323   8844   4587   -426     92   -283       C  
ATOM   1955  CG  TRP A 234     -17.781   1.740 -36.247  1.00 46.84           C  
ANISOU 1955  CG  TRP A 234     5098   8379   4319   -571     91   -349       C  
ATOM   1956  CD1 TRP A 234     -17.087   1.716 -35.035  1.00 44.16           C  
ANISOU 1956  CD1 TRP A 234     4875   7842   4060   -590     96   -331       C  
ATOM   1957  CD2 TRP A 234     -17.994   0.331 -36.600  1.00 46.63           C  
ANISOU 1957  CD2 TRP A 234     5060   8391   4264   -721     90   -443       C  
ATOM   1958  NE1 TRP A 234     -16.856   0.420 -34.632  1.00 43.86           N  
ANISOU 1958  NE1 TRP A 234     4899   7719   4045   -727     97   -397       N  
ATOM   1959  CE2 TRP A 234     -17.377  -0.459 -35.536  1.00 46.10           C  
ANISOU 1959  CE2 TRP A 234     5115   8130   4269   -813     97   -468       C  
ATOM   1960  CE3 TRP A 234     -18.615  -0.331 -37.663  1.00 47.29           C  
ANISOU 1960  CE3 TRP A 234     5049   8648   4270   -788     88   -510       C  
ATOM   1961  CZ2 TRP A 234     -17.396  -1.850 -35.547  1.00 46.21           C  
ANISOU 1961  CZ2 TRP A 234     5160   8114   4282   -960    109   -551       C  
ATOM   1962  CZ3 TRP A 234     -18.623  -1.732 -37.665  1.00 47.25           C  
ANISOU 1962  CZ3 TRP A 234     5075   8612   4264   -948    100   -603       C  
ATOM   1963  CH2 TRP A 234     -18.022  -2.473 -36.632  1.00 46.16           C  
ANISOU 1963  CH2 TRP A 234     5063   8273   4202  -1029    114   -621       C  
ATOM   1964  N   SER A 235     -19.979   4.672 -35.053  1.00 51.37           N  
ANISOU 1964  N   SER A 235     5520   9176   4819   -299    146   -201       N  
ATOM   1965  CA  SER A 235     -20.261   5.005 -33.672  1.00 52.68           C  
ANISOU 1965  CA  SER A 235     5734   9260   5019   -304    171   -188       C  
ATOM   1966  C   SER A 235     -21.753   4.889 -33.381  1.00 55.39           C  
ANISOU 1966  C   SER A 235     5969   9790   5285   -334    187   -219       C  
ATOM   1967  O   SER A 235     -22.162   4.196 -32.436  1.00 54.36           O  
ANISOU 1967  O   SER A 235     5862   9631   5159   -445    195   -271       O  
ATOM   1968  CB  SER A 235     -19.747   6.407 -33.347  1.00 51.66           C  
ANISOU 1968  CB  SER A 235     5654   9031   4940   -158    195    -98       C  
ATOM   1969  OG  SER A 235     -19.949   6.705 -31.988  1.00 51.94           O  
ANISOU 1969  OG  SER A 235     5742   8980   5012   -172    220    -92       O  
ATOM   1970  N   GLU A 236     -22.565   5.557 -34.198  1.00 57.24           N  
ANISOU 1970  N   GLU A 236     6081  10220   5446   -233    193   -186       N  
ATOM   1971  CA  GLU A 236     -24.016   5.502 -34.036  1.00 59.40           C  
ANISOU 1971  CA  GLU A 236     6233  10699   5637   -250    208   -214       C  
ATOM   1972  C   GLU A 236     -24.540   4.076 -34.204  1.00 57.60           C  
ANISOU 1972  C   GLU A 236     5959  10566   5358   -425    192   -322       C  
ATOM   1973  O   GLU A 236     -25.395   3.643 -33.436  1.00 58.08           O  
ANISOU 1973  O   GLU A 236     5990  10682   5392   -510    209   -372       O  
ATOM   1974  CB  GLU A 236     -24.717   6.479 -34.989  1.00 63.97           C  
ANISOU 1974  CB  GLU A 236     6683  11480   6140    -97    215   -151       C  
ATOM   1975  CG  GLU A 236     -24.829   7.899 -34.431  1.00 68.50           C  
ANISOU 1975  CG  GLU A 236     7276  12006   6745     64    256    -55       C  
ATOM   1976  CD  GLU A 236     -25.075   8.961 -35.500  1.00 72.12           C  
ANISOU 1976  CD  GLU A 236     7649  12599   7152    242    268     31       C  
ATOM   1977  OE1 GLU A 236     -24.735  10.139 -35.249  1.00 73.51           O  
ANISOU 1977  OE1 GLU A 236     7878  12676   7375    381    306    117       O  
ATOM   1978  OE2 GLU A 236     -25.614   8.630 -36.582  1.00 73.61           O  
ANISOU 1978  OE2 GLU A 236     7720  12996   7252    244    244     13       O  
ATOM   1979  N   PHE A 237     -23.983   3.342 -35.172  1.00 56.52           N  
ANISOU 1979  N   PHE A 237     5826  10435   5212   -485    166   -363       N  
ATOM   1980  CA  PHE A 237     -24.360   1.945 -35.414  1.00 56.18           C  
ANISOU 1980  CA  PHE A 237     5753  10464   5127   -661    161   -472       C  
ATOM   1981  C   PHE A 237     -24.071   1.007 -34.239  1.00 56.78           C  
ANISOU 1981  C   PHE A 237     5945  10363   5266   -802    176   -527       C  
ATOM   1982  O   PHE A 237     -24.968   0.302 -33.784  1.00 60.91           O  
ANISOU 1982  O   PHE A 237     6427  10970   5746   -918    195   -597       O  
ATOM   1983  CB  PHE A 237     -23.704   1.398 -36.688  1.00 55.30           C  
ANISOU 1983  CB  PHE A 237     5636  10373   5001   -690    136   -502       C  
ATOM   1984  CG  PHE A 237     -23.981  -0.067 -36.933  1.00 56.15           C  
ANISOU 1984  CG  PHE A 237     5731  10528   5075   -878    141   -620       C  
ATOM   1985  CD1 PHE A 237     -25.221  -0.488 -37.422  1.00 58.40           C  
ANISOU 1985  CD1 PHE A 237     5873  11064   5252   -950    149   -691       C  
ATOM   1986  CD2 PHE A 237     -23.014  -1.027 -36.664  1.00 54.96           C  
ANISOU 1986  CD2 PHE A 237     5709  10174   4998   -985    145   -662       C  
ATOM   1987  CE1 PHE A 237     -25.478  -1.834 -37.641  1.00 58.32           C  
ANISOU 1987  CE1 PHE A 237     5855  11091   5210  -1133    164   -808       C  
ATOM   1988  CE2 PHE A 237     -23.267  -2.375 -36.882  1.00 56.03           C  
ANISOU 1988  CE2 PHE A 237     5842  10339   5106  -1158    162   -771       C  
ATOM   1989  CZ  PHE A 237     -24.500  -2.779 -37.370  1.00 57.90           C  
ANISOU 1989  CZ  PHE A 237     5942  10818   5237  -1237    174   -848       C  
ATOM   1990  N   THR A 238     -22.824   0.984 -33.761  1.00 54.16           N  
ANISOU 1990  N   THR A 238     5754   9792   5029   -794    169   -494       N  
ATOM   1991  CA  THR A 238     -22.441   0.060 -32.689  1.00 52.60           C  
ANISOU 1991  CA  THR A 238     5672   9421   4889   -919    182   -536       C  
ATOM   1992  C   THR A 238     -23.222   0.312 -31.398  1.00 54.26           C  
ANISOU 1992  C   THR A 238     5885   9634   5097   -935    208   -531       C  
ATOM   1993  O   THR A 238     -23.592  -0.632 -30.701  1.00 53.06           O  
ANISOU 1993  O   THR A 238     5765   9453   4942  -1068    228   -594       O  
ATOM   1994  CB  THR A 238     -20.919   0.085 -32.376  1.00 50.80           C  
ANISOU 1994  CB  THR A 238     5589   8949   4761   -891    167   -492       C  
ATOM   1995  OG1 THR A 238     -20.515   1.401 -31.986  1.00 49.89           O  
ANISOU 1995  OG1 THR A 238     5501   8767   4686   -748    165   -403       O  
ATOM   1996  CG2 THR A 238     -20.115  -0.354 -33.561  1.00 48.59           C  
ANISOU 1996  CG2 THR A 238     5319   8652   4490   -898    146   -509       C  
ATOM   1997  N   GLN A 239     -23.477   1.583 -31.088  1.00 56.11           N  
ANISOU 1997  N   GLN A 239     6087   9897   5332   -800    213   -458       N  
ATOM   1998  CA  GLN A 239     -24.133   1.943 -29.828  1.00 58.99           C  
ANISOU 1998  CA  GLN A 239     6461  10250   5702   -802    240   -448       C  
ATOM   1999  C   GLN A 239     -25.605   1.525 -29.767  1.00 62.86           C  
ANISOU 1999  C   GLN A 239     6832  10945   6104   -878    261   -511       C  
ATOM   2000  O   GLN A 239     -26.107   1.179 -28.694  1.00 64.24           O  
ANISOU 2000  O   GLN A 239     7034  11092   6282   -958    285   -542       O  
ATOM   2001  CB  GLN A 239     -23.968   3.436 -29.511  1.00 59.83           C  
ANISOU 2001  CB  GLN A 239     6574  10320   5837   -637    251   -355       C  
ATOM   2002  CG  GLN A 239     -22.511   3.905 -29.372  1.00 63.00           C  
ANISOU 2002  CG  GLN A 239     7100  10510   6328   -573    238   -298       C  
ATOM   2003  CD  GLN A 239     -21.651   3.007 -28.480  1.00 63.12           C  
ANISOU 2003  CD  GLN A 239     7245  10330   6406   -685    231   -328       C  
ATOM   2004  OE1 GLN A 239     -21.851   2.948 -27.263  1.00 65.20           O  
ANISOU 2004  OE1 GLN A 239     7559  10525   6689   -730    249   -333       O  
ATOM   2005  NE2 GLN A 239     -20.677   2.316 -29.083  1.00 59.73           N  
ANISOU 2005  NE2 GLN A 239     6872   9812   6008   -727    205   -344       N  
ATOM   2006  N   LYS A 240     -26.289   1.525 -30.910  1.00 65.36           N  
ANISOU 2006  N   LYS A 240     7016  11474   6340   -859    252   -534       N  
ATOM   2007  CA  LYS A 240     -27.672   1.040 -30.946  1.00 68.66           C  
ANISOU 2007  CA  LYS A 240     7311  12108   6668   -945    269   -606       C  
ATOM   2008  C   LYS A 240     -27.795  -0.478 -31.118  1.00 69.72           C  
ANISOU 2008  C   LYS A 240     7457  12251   6779  -1140    277   -716       C  
ATOM   2009  O   LYS A 240     -28.796  -1.064 -30.722  1.00 77.51           O  
ANISOU 2009  O   LYS A 240     8387  13348   7713  -1250    304   -787       O  
ATOM   2010  CB  LYS A 240     -28.521   1.790 -31.985  1.00 69.34           C  
ANISOU 2010  CB  LYS A 240     7230  12452   6664   -833    261   -581       C  
ATOM   2011  CG  LYS A 240     -28.070   1.672 -33.430  1.00 68.66           C  
ANISOU 2011  CG  LYS A 240     7099  12442   6546   -803    230   -581       C  
ATOM   2012  CD  LYS A 240     -28.786   2.713 -34.277  1.00 71.69           C  
ANISOU 2012  CD  LYS A 240     7335  13053   6851   -646    223   -522       C  
ATOM   2013  CE  LYS A 240     -28.348   2.665 -35.732  1.00 73.89           C  
ANISOU 2013  CE  LYS A 240     7565  13419   7090   -607    193   -515       C  
ATOM   2014  NZ  LYS A 240     -29.035   3.704 -36.553  1.00 73.36           N  
ANISOU 2014  NZ  LYS A 240     7355  13576   6940   -442    188   -446       N  
ATOM   2015  N   THR A 241     -26.771  -1.110 -31.681  1.00 68.72           N  
ANISOU 2015  N   THR A 241     7411  12003   6694  -1184    261   -732       N  
ATOM   2016  CA  THR A 241     -26.811  -2.549 -31.939  1.00 68.72           C  
ANISOU 2016  CA  THR A 241     7432  11999   6677  -1364    277   -836       C  
ATOM   2017  C   THR A 241     -26.267  -3.352 -30.760  1.00 70.38           C  
ANISOU 2017  C   THR A 241     7796  11981   6963  -1470    302   -855       C  
ATOM   2018  O   THR A 241     -25.062  -3.355 -30.500  1.00 71.05           O  
ANISOU 2018  O   THR A 241     8007  11856   7131  -1435    288   -808       O  
ATOM   2019  CB  THR A 241     -26.027  -2.916 -33.210  1.00 68.98           C  
ANISOU 2019  CB  THR A 241     7470  12025   6712  -1366    254   -852       C  
ATOM   2020  OG1 THR A 241     -26.296  -1.954 -34.240  1.00 69.57           O  
ANISOU 2020  OG1 THR A 241     7424  12279   6730  -1230    226   -804       O  
ATOM   2021  CG2 THR A 241     -26.418  -4.303 -33.693  1.00 70.08           C  
ANISOU 2021  CG2 THR A 241     7586  12234   6805  -1551    281   -973       C  
ATOM   2022  N   GLN A 242     -27.160  -4.048 -30.064  1.00 72.75           N  
ANISOU 2022  N   GLN A 242     8082  12330   7229  -1599    341   -924       N  
ATOM   2023  CA  GLN A 242     -26.795  -4.787 -28.856  1.00 71.95           C  
ANISOU 2023  CA  GLN A 242     8119  12028   7188  -1696    372   -937       C  
ATOM   2024  C   GLN A 242     -26.323  -6.212 -29.154  1.00 68.27           C  
ANISOU 2024  C   GLN A 242     7736  11462   6742  -1847    399  -1012       C  
ATOM   2025  O   GLN A 242     -25.425  -6.725 -28.487  1.00 65.72           O  
ANISOU 2025  O   GLN A 242     7557  10920   6492  -1877    409   -990       O  
ATOM   2026  CB  GLN A 242     -27.964  -4.798 -27.871  1.00 77.90           C  
ANISOU 2026  CB  GLN A 242     8829  12867   7900  -1758    407   -967       C  
ATOM   2027  CG  GLN A 242     -28.357  -3.409 -27.390  1.00 83.22           C  
ANISOU 2027  CG  GLN A 242     9445  13605   8568  -1608    390   -888       C  
ATOM   2028  CD  GLN A 242     -29.489  -3.436 -26.385  1.00 91.75           C  
ANISOU 2028  CD  GLN A 242    10484  14765   9610  -1670    428   -920       C  
ATOM   2029  OE1 GLN A 242     -30.612  -3.834 -26.708  1.00 96.12           O  
ANISOU 2029  OE1 GLN A 242    10922  15516  10083  -1754    451   -997       O  
ATOM   2030  NE2 GLN A 242     -29.204  -3.001 -25.156  1.00 92.77           N  
ANISOU 2030  NE2 GLN A 242    10705  14750   9793  -1631    436   -865       N  
ATOM   2031  N   GLY A 243     -26.926  -6.838 -30.162  1.00 65.60           N  
ANISOU 2031  N   GLY A 243     7303  11287   6334  -1939    414  -1101       N  
ATOM   2032  CA  GLY A 243     -26.573  -8.202 -30.548  1.00 64.01           C  
ANISOU 2032  CA  GLY A 243     7171  11005   6144  -2090    452  -1184       C  
ATOM   2033  C   GLY A 243     -25.346  -8.304 -31.446  1.00 63.79           C  
ANISOU 2033  C   GLY A 243     7202  10870   6166  -2036    423  -1158       C  
ATOM   2034  O   GLY A 243     -24.733  -7.290 -31.811  1.00 62.30           O  
ANISOU 2034  O   GLY A 243     6998  10670   6001  -1881    372  -1073       O  
ATOM   2035  N   GLN A 244     -25.004  -9.540 -31.807  1.00 61.96           N  
ANISOU 2035  N   GLN A 244     7037  10556   5948  -2169    464  -1233       N  
ATOM   2036  CA  GLN A 244     -23.849  -9.841 -32.641  1.00 60.24           C  
ANISOU 2036  CA  GLN A 244     6883  10226   5778  -2142    449  -1223       C  
ATOM   2037  C   GLN A 244     -23.942  -9.129 -33.985  1.00 60.75           C  
ANISOU 2037  C   GLN A 244     6817  10477   5787  -2056    403  -1218       C  
ATOM   2038  O   GLN A 244     -24.936  -9.271 -34.703  1.00 66.14           O  
ANISOU 2038  O   GLN A 244     7367  11385   6376  -2121    414  -1294       O  
ATOM   2039  CB  GLN A 244     -23.734 -11.364 -32.842  1.00 59.32           C  
ANISOU 2039  CB  GLN A 244     6842  10023   5670  -2319    517  -1323       C  
ATOM   2040  CG  GLN A 244     -22.638 -11.814 -33.808  1.00 58.49           C  
ANISOU 2040  CG  GLN A 244     6795   9819   5607  -2311    512  -1331       C  
ATOM   2041  CD  GLN A 244     -21.230 -11.549 -33.291  1.00 55.81           C  
ANISOU 2041  CD  GLN A 244     6592   9238   5372  -2197    481  -1227       C  
ATOM   2042  OE1 GLN A 244     -20.916 -11.820 -32.132  1.00 54.09           O  
ANISOU 2042  OE1 GLN A 244     6487   8853   5210  -2206    501  -1188       O  
ATOM   2043  NE2 GLN A 244     -20.369 -11.037 -34.163  1.00 55.32           N  
ANISOU 2043  NE2 GLN A 244     6519   9164   5334  -2092    434  -1184       N  
ATOM   2044  N   ILE A 245     -22.909  -8.360 -34.321  1.00 57.29           N  
ANISOU 2044  N   ILE A 245     6413   9952   5400  -1911    353  -1129       N  
ATOM   2045  CA  ILE A 245     -22.856  -7.669 -35.606  1.00 55.21           C  
ANISOU 2045  CA  ILE A 245     6043   9843   5091  -1818    311  -1113       C  
ATOM   2046  C   ILE A 245     -22.354  -8.623 -36.689  1.00 56.37           C  
ANISOU 2046  C   ILE A 245     6206   9976   5233  -1908    329  -1188       C  
ATOM   2047  O   ILE A 245     -21.361  -9.320 -36.494  1.00 58.73           O  
ANISOU 2047  O   ILE A 245     6638  10065   5610  -1946    348  -1189       O  
ATOM   2048  CB  ILE A 245     -21.949  -6.417 -35.537  1.00 53.29           C  
ANISOU 2048  CB  ILE A 245     5833   9508   4905  -1628    259   -988       C  
ATOM   2049  CG1 ILE A 245     -22.609  -5.313 -34.710  1.00 52.91           C  
ANISOU 2049  CG1 ILE A 245     5737   9524   4843  -1528    245   -920       C  
ATOM   2050  CG2 ILE A 245     -21.607  -5.903 -36.932  1.00 53.23           C  
ANISOU 2050  CG2 ILE A 245     5749   9609   4865  -1541    223   -971       C  
ATOM   2051  CD1 ILE A 245     -21.646  -4.240 -34.230  1.00 51.00           C  
ANISOU 2051  CD1 ILE A 245     5569   9129   4677  -1371    212   -806       C  
ATOM   2052  N   TYR A 246     -23.059  -8.668 -37.817  1.00 55.93           N  
ANISOU 2052  N   TYR A 246     6015  10151   5083  -1945    327  -1253       N  
ATOM   2053  CA  TYR A 246     -22.568  -9.347 -39.016  1.00 55.70           C  
ANISOU 2053  CA  TYR A 246     5983  10138   5040  -2007    336  -1317       C  
ATOM   2054  C   TYR A 246     -22.248  -8.296 -40.050  1.00 55.15           C  
ANISOU 2054  C   TYR A 246     5830  10183   4941  -1854    278  -1250       C  
ATOM   2055  O   TYR A 246     -22.885  -7.245 -40.084  1.00 56.04           O  
ANISOU 2055  O   TYR A 246     5837  10455   5001  -1744    244  -1193       O  
ATOM   2056  CB  TYR A 246     -23.615 -10.334 -39.555  1.00 59.36           C  
ANISOU 2056  CB  TYR A 246     6358  10785   5411  -2189    387  -1458       C  
ATOM   2057  CG  TYR A 246     -23.811 -11.517 -38.642  1.00 59.90           C  
ANISOU 2057  CG  TYR A 246     6529  10714   5515  -2354    459  -1533       C  
ATOM   2058  CD1 TYR A 246     -22.946 -12.609 -38.696  1.00 60.90           C  
ANISOU 2058  CD1 TYR A 246     6792  10636   5711  -2448    507  -1577       C  
ATOM   2059  CD2 TYR A 246     -24.818 -11.521 -37.682  1.00 60.89           C  
ANISOU 2059  CD2 TYR A 246     6623  10901   5610  -2408    483  -1551       C  
ATOM   2060  CE1 TYR A 246     -23.093 -13.682 -37.836  1.00 62.52           C  
ANISOU 2060  CE1 TYR A 246     7102  10699   5952  -2589    581  -1634       C  
ATOM   2061  CE2 TYR A 246     -24.971 -12.588 -36.812  1.00 63.16           C  
ANISOU 2061  CE2 TYR A 246     7014  11050   5931  -2556    554  -1611       C  
ATOM   2062  CZ  TYR A 246     -24.107 -13.669 -36.899  1.00 63.71           C  
ANISOU 2062  CZ  TYR A 246     7222  10915   6069  -2645    605  -1651       C  
ATOM   2063  OH  TYR A 246     -24.252 -14.737 -36.044  1.00 67.57           O  
ANISOU 2063  OH  TYR A 246     7821  11259   6591  -2786    683  -1705       O  
ATOM   2064  N   GLY A 247     -21.250  -8.554 -40.884  1.00 54.38           N  
ANISOU 2064  N   GLY A 247     5782  10001   4878  -1842    270  -1252       N  
ATOM   2065  CA  GLY A 247     -20.825  -7.546 -41.841  1.00 53.79           C  
ANISOU 2065  CA  GLY A 247     5643  10010   4781  -1692    217  -1180       C  
ATOM   2066  C   GLY A 247     -19.931  -8.072 -42.926  1.00 54.79           C  
ANISOU 2066  C   GLY A 247     5803  10088   4924  -1721    219  -1217       C  
ATOM   2067  O   GLY A 247     -19.343  -9.146 -42.798  1.00 56.40           O  
ANISOU 2067  O   GLY A 247     6113  10129   5185  -1831    259  -1276       O  
ATOM   2068  N   ILE A 248     -19.823  -7.303 -43.999  1.00 54.02           N  
ANISOU 2068  N   ILE A 248     5617  10129   4776  -1616    180  -1177       N  
ATOM   2069  CA  ILE A 248     -19.025  -7.699 -45.135  1.00 55.65           C  
ANISOU 2069  CA  ILE A 248     5840  10316   4985  -1635    179  -1210       C  
ATOM   2070  C   ILE A 248     -18.298  -6.496 -45.722  1.00 53.90           C  
ANISOU 2070  C   ILE A 248     5606  10093   4779  -1451    128  -1098       C  
ATOM   2071  O   ILE A 248     -18.786  -5.374 -45.654  1.00 54.84           O  
ANISOU 2071  O   ILE A 248     5648  10329   4859  -1323     98  -1018       O  
ATOM   2072  CB  ILE A 248     -19.889  -8.422 -46.211  1.00 57.96           C  
ANISOU 2072  CB  ILE A 248     6009  10850   5161  -1768    202  -1334       C  
ATOM   2073  CG1 ILE A 248     -19.009  -9.032 -47.303  1.00 58.95           C  
ANISOU 2073  CG1 ILE A 248     6172  10927   5299  -1814    213  -1385       C  
ATOM   2074  CG2 ILE A 248     -20.951  -7.496 -46.801  1.00 57.47           C  
ANISOU 2074  CG2 ILE A 248     5769  11089   4975  -1686    165  -1307       C  
ATOM   2075  CD1 ILE A 248     -19.726 -10.071 -48.143  1.00 62.78           C  
ANISOU 2075  CD1 ILE A 248     6574  11588   5689  -1993    256  -1533       C  
ATOM   2076  N   LYS A 249     -17.109  -6.737 -46.250  1.00 53.59           N  
ANISOU 2076  N   LYS A 249     5649   9909   4802  -1436    126  -1091       N  
ATOM   2077  CA  LYS A 249     -16.420  -5.747 -47.055  1.00 55.58           C  
ANISOU 2077  CA  LYS A 249     5881  10179   5055  -1287     87  -1006       C  
ATOM   2078  C   LYS A 249     -16.230  -6.318 -48.448  1.00 55.94           C  
ANISOU 2078  C   LYS A 249     5877  10333   5044  -1351     93  -1081       C  
ATOM   2079  O   LYS A 249     -15.715  -7.420 -48.607  1.00 54.04           O  
ANISOU 2079  O   LYS A 249     5709   9980   4843  -1472    127  -1163       O  
ATOM   2080  CB  LYS A 249     -15.068  -5.375 -46.438  1.00 53.65           C  
ANISOU 2080  CB  LYS A 249     5779   9666   4938  -1197     76   -922       C  
ATOM   2081  CG  LYS A 249     -14.395  -4.147 -47.062  1.00 53.37           C  
ANISOU 2081  CG  LYS A 249     5730   9637   4911  -1027     40   -820       C  
ATOM   2082  CD  LYS A 249     -13.333  -4.510 -48.082  1.00 50.80           C  
ANISOU 2082  CD  LYS A 249     5443   9245   4610  -1036     39   -841       C  
ATOM   2083  CE  LYS A 249     -12.171  -5.238 -47.426  1.00 52.91           C  
ANISOU 2083  CE  LYS A 249     5860   9244   4997  -1084     56   -854       C  
ATOM   2084  NZ  LYS A 249     -11.053  -5.515 -48.373  1.00 53.05           N  
ANISOU 2084  NZ  LYS A 249     5920   9186   5049  -1078     56   -867       N  
ATOM   2085  N   VAL A 250     -16.673  -5.569 -49.451  1.00 59.20           N  
ANISOU 2085  N   VAL A 250     6166  10967   5361  -1269     65  -1052       N  
ATOM   2086  CA  VAL A 250     -16.584  -6.016 -50.835  1.00 64.66           C  
ANISOU 2086  CA  VAL A 250     6792  11794   5980  -1325     67  -1120       C  
ATOM   2087  C   VAL A 250     -15.682  -5.082 -51.637  1.00 67.44           C  
ANISOU 2087  C   VAL A 250     7152  12123   6346  -1172     34  -1026       C  
ATOM   2088  O   VAL A 250     -15.874  -3.861 -51.637  1.00 69.94           O  
ANISOU 2088  O   VAL A 250     7421  12513   6640  -1016      4   -918       O  
ATOM   2089  CB  VAL A 250     -17.979  -6.134 -51.500  1.00 66.29           C  
ANISOU 2089  CB  VAL A 250     6826  12327   6035  -1388     67  -1190       C  
ATOM   2090  CG1 VAL A 250     -17.848  -6.585 -52.942  1.00 68.85           C  
ANISOU 2090  CG1 VAL A 250     7082  12797   6279  -1448     70  -1263       C  
ATOM   2091  CG2 VAL A 250     -18.865  -7.107 -50.733  1.00 67.20           C  
ANISOU 2091  CG2 VAL A 250     6934  12464   6134  -1554    107  -1294       C  
ATOM   2092  N   ASP A 251     -14.690  -5.673 -52.302  1.00 68.81           N  
ANISOU 2092  N   ASP A 251     7392  12189   6563  -1218     46  -1067       N  
ATOM   2093  CA  ASP A 251     -13.734  -4.944 -53.114  1.00 71.19           C  
ANISOU 2093  CA  ASP A 251     7712  12454   6883  -1096     22   -993       C  
ATOM   2094  C   ASP A 251     -14.281  -4.801 -54.536  1.00 72.11           C  
ANISOU 2094  C   ASP A 251     7689  12845   6864  -1093      9  -1023       C  
ATOM   2095  O   ASP A 251     -14.525  -5.802 -55.211  1.00 75.24           O  
ANISOU 2095  O   ASP A 251     8046  13334   7205  -1236     33  -1141       O  
ATOM   2096  CB  ASP A 251     -12.425  -5.729 -53.158  1.00 75.46           C  
ANISOU 2096  CB  ASP A 251     8385  12756   7530  -1155     45  -1031       C  
ATOM   2097  CG  ASP A 251     -11.239  -4.913 -52.718  1.00 80.95           C  
ANISOU 2097  CG  ASP A 251     9185  13239   8334  -1018     26   -920       C  
ATOM   2098  OD1 ASP A 251     -11.270  -4.382 -51.581  1.00 83.73           O  
ANISOU 2098  OD1 ASP A 251     9584  13486   8743   -956     17   -852       O  
ATOM   2099  OD2 ASP A 251     -10.259  -4.828 -53.497  1.00 84.02           O  
ANISOU 2099  OD2 ASP A 251     9607  13565   8749   -981     22   -907       O  
ATOM   2100  N   ILE A 252     -14.466  -3.566 -54.994  1.00 69.13           N  
ANISOU 2100  N   ILE A 252     7238  12594   6431   -932    -22   -917       N  
ATOM   2101  CA  ILE A 252     -14.927  -3.332 -56.362  1.00 69.68           C  
ANISOU 2101  CA  ILE A 252     7176  12931   6367   -909    -37   -928       C  
ATOM   2102  C   ILE A 252     -13.780  -3.399 -57.367  1.00 69.38           C  
ANISOU 2102  C   ILE A 252     7187  12816   6354   -890    -37   -927       C  
ATOM   2103  O   ILE A 252     -12.832  -2.611 -57.290  1.00 67.11           O  
ANISOU 2103  O   ILE A 252     6980  12372   6145   -763    -47   -828       O  
ATOM   2104  CB  ILE A 252     -15.674  -1.989 -56.507  1.00 69.71           C  
ANISOU 2104  CB  ILE A 252     7073  13121   6288   -736    -66   -809       C  
ATOM   2105  CG1 ILE A 252     -16.763  -1.872 -55.439  1.00 67.42           C  
ANISOU 2105  CG1 ILE A 252     6741  12892   5983   -745    -64   -805       C  
ATOM   2106  CG2 ILE A 252     -16.282  -1.862 -57.904  1.00 68.67           C  
ANISOU 2106  CG2 ILE A 252     6790  13297   6001   -722    -82   -828       C  
ATOM   2107  CD1 ILE A 252     -17.334  -0.482 -55.304  1.00 67.23           C  
ANISOU 2107  CD1 ILE A 252     6648  12982   5914   -556    -83   -672       C  
ATOM   2108  N   ARG A 253     -13.879  -4.336 -58.311  1.00 72.55           N  
ANISOU 2108  N   ARG A 253     7540  13335   6689  -1023    -22  -1043       N  
ATOM   2109  CA  ARG A 253     -12.887  -4.464 -59.389  1.00 73.12           C  
ANISOU 2109  CA  ARG A 253     7643  13369   6768  -1017    -19  -1055       C  
ATOM   2110  C   ARG A 253     -13.034  -3.330 -60.407  1.00 71.62           C  
ANISOU 2110  C   ARG A 253     7356  13377   6480   -864    -52   -958       C  
ATOM   2111  O   ARG A 253     -14.144  -3.008 -60.836  1.00 71.17           O  
ANISOU 2111  O   ARG A 253     7156  13594   6289   -841    -69   -953       O  
ATOM   2112  CB  ARG A 253     -12.985  -5.836 -60.077  1.00 74.39           C  
ANISOU 2112  CB  ARG A 253     7782  13595   6884  -1213     14  -1216       C  
ATOM   2113  CG  ARG A 253     -11.871  -6.123 -61.076  1.00 77.12           C  
ANISOU 2113  CG  ARG A 253     8180  13865   7256  -1226     25  -1242       C  
ATOM   2114  CD  ARG A 253     -11.872  -7.581 -61.512  1.00 82.84           C  
ANISOU 2114  CD  ARG A 253     8915  14593   7967  -1432     74  -1408       C  
ATOM   2115  NE  ARG A 253     -11.198  -8.438 -60.540  1.00 86.34           N  
ANISOU 2115  NE  ARG A 253     9507  14745   8552  -1515    114  -1452       N  
ATOM   2116  CZ  ARG A 253     -11.037  -9.756 -60.665  1.00 90.73           C  
ANISOU 2116  CZ  ARG A 253    10112  15227   9132  -1688    171  -1586       C  
ATOM   2117  NH1 ARG A 253     -11.508 -10.397 -61.729  1.00 90.54           N  
ANISOU 2117  NH1 ARG A 253     9999  15401   8999  -1812    196  -1704       N  
ATOM   2118  NH2 ARG A 253     -10.400 -10.436 -59.715  1.00 92.52           N  
ANISOU 2118  NH2 ARG A 253    10479  15182   9492  -1737    208  -1604       N  
ATOM   2119  N   ASP A 254     -11.897  -2.721 -60.746  1.00 69.75           N  
ANISOU 2119  N   ASP A 254     7198  12994   6309   -756    -57   -878       N  
ATOM   2120  CA  ASP A 254     -11.793  -1.611 -61.701  1.00 66.35           C  
ANISOU 2120  CA  ASP A 254     6705  12697   5805   -600    -78   -773       C  
ATOM   2121  C   ASP A 254     -13.058  -0.768 -61.863  1.00 68.05           C  
ANISOU 2121  C   ASP A 254     6778  13185   5891   -498   -101   -703       C  
ATOM   2122  O   ASP A 254     -13.754  -0.877 -62.867  1.00 71.87           O  
ANISOU 2122  O   ASP A 254     7131  13943   6233   -519   -112   -738       O  
ATOM   2123  CB  ASP A 254     -11.304  -2.126 -63.054  1.00 66.49           C  
ANISOU 2123  CB  ASP A 254     6695  12802   5764   -662    -73   -840       C  
ATOM   2124  CG  ASP A 254     -10.687  -1.025 -63.917  1.00 68.80           C  
ANISOU 2124  CG  ASP A 254     6985  13123   6033   -498    -85   -723       C  
ATOM   2125  OD1 ASP A 254     -10.629   0.144 -63.463  1.00 67.48           O  
ANISOU 2125  OD1 ASP A 254     6841  12899   5897   -336    -94   -590       O  
ATOM   2126  OD2 ASP A 254     -10.261  -1.333 -65.057  1.00 69.76           O  
ANISOU 2126  OD2 ASP A 254     7083  13320   6103   -535    -81   -767       O  
ATOM   2127  N   ALA A 255     -13.349   0.073 -60.870  1.00 67.66           N  
ANISOU 2127  N   ALA A 255     6754  13065   5889   -386   -105   -605       N  
ATOM   2128  CA  ALA A 255     -14.510   0.959 -60.929  1.00 66.74           C  
ANISOU 2128  CA  ALA A 255     6511  13185   5661   -267   -121   -523       C  
ATOM   2129  C   ALA A 255     -14.392   1.966 -62.074  1.00 68.64           C  
ANISOU 2129  C   ALA A 255     6689  13574   5814   -108   -132   -417       C  
ATOM   2130  O   ALA A 255     -15.378   2.238 -62.774  1.00 70.52           O  
ANISOU 2130  O   ALA A 255     6780  14109   5904    -64   -148   -400       O  
ATOM   2131  CB  ALA A 255     -14.709   1.674 -59.610  1.00 64.42           C  
ANISOU 2131  CB  ALA A 255     6275  12751   5451   -177   -115   -439       C  
ATOM   2132  N   TYR A 256     -13.188   2.499 -62.272  1.00 67.36           N  
ANISOU 2132  N   TYR A 256     6639  13214   5740    -24   -120   -347       N  
ATOM   2133  CA  TYR A 256     -12.925   3.424 -63.375  1.00 71.39           C  
ANISOU 2133  CA  TYR A 256     7111  13833   6178    121   -121   -245       C  
ATOM   2134  C   TYR A 256     -13.242   2.794 -64.728  1.00 71.90           C  
ANISOU 2134  C   TYR A 256     7060  14154   6103     42   -137   -324       C  
ATOM   2135  O   TYR A 256     -13.933   3.392 -65.550  1.00 70.52           O  
ANISOU 2135  O   TYR A 256     6763  14239   5790    142   -150   -261       O  
ATOM   2136  CB  TYR A 256     -11.474   3.905 -63.358  1.00 72.70           C  
ANISOU 2136  CB  TYR A 256     7426  13725   6472    188   -101   -184       C  
ATOM   2137  CG  TYR A 256     -11.197   4.977 -62.329  1.00 79.83           C  
ANISOU 2137  CG  TYR A 256     8421  14434   7477    323    -81    -66       C  
ATOM   2138  CD1 TYR A 256     -11.224   4.685 -60.965  1.00 79.07           C  
ANISOU 2138  CD1 TYR A 256     8396  14161   7486    264    -77    -98       C  
ATOM   2139  CD2 TYR A 256     -10.892   6.282 -62.714  1.00 83.82           C  
ANISOU 2139  CD2 TYR A 256     8946  14927   7974    508    -61     74       C  
ATOM   2140  CE1 TYR A 256     -10.973   5.663 -60.016  1.00 81.88           C  
ANISOU 2140  CE1 TYR A 256     8834  14345   7932    379    -56      1       C  
ATOM   2141  CE2 TYR A 256     -10.625   7.266 -61.768  1.00 83.29           C  
ANISOU 2141  CE2 TYR A 256     8967  14675   8002    623    -33    173       C  
ATOM   2142  CZ  TYR A 256     -10.672   6.952 -60.422  1.00 83.36           C  
ANISOU 2142  CZ  TYR A 256     9040  14521   8110    556    -32    134       C  
ATOM   2143  OH  TYR A 256     -10.416   7.919 -59.470  1.00 85.42           O  
ANISOU 2143  OH  TYR A 256     9387  14605   8463    661     -2    225       O  
ATOM   2144  N   GLY A 257     -12.743   1.579 -64.939  1.00 72.88           N  
ANISOU 2144  N   GLY A 257     7222  14206   6261   -135   -132   -462       N  
ATOM   2145  CA  GLY A 257     -12.845   0.906 -66.230  1.00 74.11           C  
ANISOU 2145  CA  GLY A 257     7289  14567   6300   -229   -139   -552       C  
ATOM   2146  C   GLY A 257     -14.180   0.228 -66.471  1.00 77.41           C  
ANISOU 2146  C   GLY A 257     7551  15283   6576   -341   -153   -652       C  
ATOM   2147  O   GLY A 257     -14.489  -0.157 -67.601  1.00 77.87           O  
ANISOU 2147  O   GLY A 257     7504  15578   6505   -400   -161   -715       O  
ATOM   2148  N   ASN A 258     -14.966   0.068 -65.407  1.00 76.72           N  
ANISOU 2148  N   ASN A 258     7447  15190   6510   -377   -153   -672       N  
ATOM   2149  CA  ASN A 258     -16.300  -0.514 -65.520  1.00 76.42           C  
ANISOU 2149  CA  ASN A 258     7257  15438   6340   -482   -164   -764       C  
ATOM   2150  C   ASN A 258     -17.415   0.523 -65.604  1.00 76.89           C  
ANISOU 2150  C   ASN A 258     7178  15760   6277   -323   -189   -652       C  
ATOM   2151  O   ASN A 258     -18.599   0.174 -65.649  1.00 79.59           O  
ANISOU 2151  O   ASN A 258     7378  16360   6500   -390   -201   -716       O  
ATOM   2152  CB  ASN A 258     -16.559  -1.528 -64.401  1.00 74.72           C  
ANISOU 2152  CB  ASN A 258     7097  15085   6208   -652   -143   -881       C  
ATOM   2153  CG  ASN A 258     -15.834  -2.845 -64.635  1.00 75.49           C  
ANISOU 2153  CG  ASN A 258     7275  15042   6364   -849   -113  -1031       C  
ATOM   2154  OD1 ASN A 258     -15.277  -3.430 -63.705  1.00 72.87           O  
ANISOU 2154  OD1 ASN A 258     7074  14440   6171   -929    -88  -1074       O  
ATOM   2155  ND2 ASN A 258     -15.817  -3.305 -65.891  1.00 73.53           N  
ANISOU 2155  ND2 ASN A 258     6950  14976   6010   -923   -113  -1108       N  
ATOM   2156  N   VAL A 259     -17.034   1.797 -65.653  1.00 73.43           N  
ANISOU 2156  N   VAL A 259     6776  15257   5864   -111   -192   -486       N  
ATOM   2157  CA  VAL A 259     -17.980   2.844 -65.996  1.00 73.96           C  
ANISOU 2157  CA  VAL A 259     6710  15586   5802     64   -209   -365       C  
ATOM   2158  C   VAL A 259     -18.501   2.623 -67.421  1.00 75.16           C  
ANISOU 2158  C   VAL A 259     6702  16088   5766     41   -231   -404       C  
ATOM   2159  O   VAL A 259     -17.727   2.570 -68.387  1.00 74.54           O  
ANISOU 2159  O   VAL A 259     6650  16000   5670     42   -230   -406       O  
ATOM   2160  CB  VAL A 259     -17.366   4.248 -65.851  1.00 72.30           C  
ANISOU 2160  CB  VAL A 259     6589  15220   5662    294   -195   -180       C  
ATOM   2161  CG1 VAL A 259     -18.289   5.303 -66.433  1.00 74.14           C  
ANISOU 2161  CG1 VAL A 259     6681  15740   5746    485   -206    -49       C  
ATOM   2162  CG2 VAL A 259     -17.102   4.549 -64.393  1.00 74.28           C  
ANISOU 2162  CG2 VAL A 259     6967  15183   6071    321   -174   -141       C  
ATOM   2163  N   LYS A 260     -19.810   2.435 -67.531  1.00 76.45           N  
ANISOU 2163  N   LYS A 260     6696  16564   5788     10   -251   -445       N  
ATOM   2164  CA  LYS A 260     -20.473   2.403 -68.823  1.00 78.28           C  
ANISOU 2164  CA  LYS A 260     6750  17172   5818     17   -276   -462       C  
ATOM   2165  C   LYS A 260     -20.628   3.851 -69.273  1.00 77.10           C  
ANISOU 2165  C   LYS A 260     6554  17138   5601    285   -285   -261       C  
ATOM   2166  O   LYS A 260     -21.395   4.625 -68.686  1.00 75.07           O  
ANISOU 2166  O   LYS A 260     6245  16954   5323    423   -286   -159       O  
ATOM   2167  CB  LYS A 260     -21.827   1.696 -68.715  1.00 82.96           C  
ANISOU 2167  CB  LYS A 260     7174  18063   6283   -114   -292   -580       C  
ATOM   2168  CG  LYS A 260     -21.774   0.380 -67.940  1.00 86.72           C  
ANISOU 2168  CG  LYS A 260     7718  18379   6852   -362   -270   -761       C  
ATOM   2169  CD  LYS A 260     -22.848   0.329 -66.851  1.00 89.61           C  
ANISOU 2169  CD  LYS A 260     8026  18805   7218   -387   -270   -780       C  
ATOM   2170  CE  LYS A 260     -22.425  -0.516 -65.651  1.00 87.59           C  
ANISOU 2170  CE  LYS A 260     7921  18228   7131   -546   -238   -879       C  
ATOM   2171  NZ  LYS A 260     -22.906  -1.925 -65.726  1.00 88.39           N  
ANISOU 2171  NZ  LYS A 260     7967  18432   7182   -808   -220  -1084       N  
ATOM   2172  N   ILE A 261     -19.850   4.216 -70.290  1.00 78.48           N  
ANISOU 2172  N   ILE A 261     6759  17311   5749    360   -283   -201       N  
ATOM   2173  CA  ILE A 261     -19.725   5.607 -70.746  1.00 79.70           C  
ANISOU 2173  CA  ILE A 261     6911  17507   5865    619   -276     -1       C  
ATOM   2174  C   ILE A 261     -21.063   6.239 -71.180  1.00 80.26           C  
ANISOU 2174  C   ILE A 261     6782  17967   5745    759   -300     84       C  
ATOM   2175  O   ILE A 261     -21.396   7.346 -70.738  1.00 80.71           O  
ANISOU 2175  O   ILE A 261     6843  18008   5814    963   -285    242       O  
ATOM   2176  CB  ILE A 261     -18.655   5.739 -71.865  1.00 80.15           C  
ANISOU 2176  CB  ILE A 261     7027  17510   5913    647   -269     26       C  
ATOM   2177  CG1 ILE A 261     -17.275   5.315 -71.348  1.00 79.55           C  
ANISOU 2177  CG1 ILE A 261     7157  17029   6037    549   -242    -29       C  
ATOM   2178  CG2 ILE A 261     -18.613   7.153 -72.423  1.00 81.74           C  
ANISOU 2178  CG2 ILE A 261     7217  17784   6055    913   -256    233       C  
ATOM   2179  CD1 ILE A 261     -16.934   5.858 -69.971  1.00 78.65           C  
ANISOU 2179  CD1 ILE A 261     7184  16598   6099    621   -215     42       C  
ATOM   2180  N   PRO A 262     -21.835   5.535 -72.032  1.00 79.96           N  
ANISOU 2180  N   PRO A 262     6567  18283   5530    648   -333    -20       N  
ATOM   2181  CA  PRO A 262     -23.147   6.056 -72.426  1.00 82.67           C  
ANISOU 2181  CA  PRO A 262     6705  19022   5682    772   -359     51       C  
ATOM   2182  C   PRO A 262     -24.039   6.472 -71.235  1.00 82.62           C  
ANISOU 2182  C   PRO A 262     6670  19008   5714    845   -353    101       C  
ATOM   2183  O   PRO A 262     -24.644   7.550 -71.264  1.00 83.71           O  
ANISOU 2183  O   PRO A 262     6736  19287   5781   1068   -351    263       O  
ATOM   2184  CB  PRO A 262     -23.771   4.886 -73.186  1.00 84.03           C  
ANISOU 2184  CB  PRO A 262     6716  19513   5698    558   -391   -131       C  
ATOM   2185  CG  PRO A 262     -22.611   4.128 -73.750  1.00 82.50           C  
ANISOU 2185  CG  PRO A 262     6635  19137   5572    405   -379   -236       C  
ATOM   2186  CD  PRO A 262     -21.417   4.386 -72.863  1.00 80.15           C  
ANISOU 2186  CD  PRO A 262     6573  18369   5508    436   -343   -187       C  
ATOM   2187  N   VAL A 263     -24.106   5.630 -70.204  1.00 80.28           N  
ANISOU 2187  N   VAL A 263     6432  18542   5526    662   -347    -32       N  
ATOM   2188  CA  VAL A 263     -24.916   5.913 -69.015  1.00 79.34           C  
ANISOU 2188  CA  VAL A 263     6294  18399   5451    705   -340     -3       C  
ATOM   2189  C   VAL A 263     -24.438   7.175 -68.278  1.00 80.45           C  
ANISOU 2189  C   VAL A 263     6573  18267   5725    929   -305    181       C  
ATOM   2190  O   VAL A 263     -25.255   8.004 -67.858  1.00 79.42           O  
ANISOU 2190  O   VAL A 263     6373  18247   5554   1093   -298    294       O  
ATOM   2191  CB  VAL A 263     -24.952   4.695 -68.055  1.00 78.08           C  
ANISOU 2191  CB  VAL A 263     6192  18081   5394    452   -333   -188       C  
ATOM   2192  CG1 VAL A 263     -25.542   5.069 -66.701  1.00 75.96           C  
ANISOU 2192  CG1 VAL A 263     5948  17704   5207    505   -318   -145       C  
ATOM   2193  CG2 VAL A 263     -25.731   3.547 -68.683  1.00 77.60           C  
ANISOU 2193  CG2 VAL A 263     5966  18338   5181    241   -358   -368       C  
ATOM   2194  N   LEU A 264     -23.117   7.322 -68.139  1.00 81.05           N  
ANISOU 2194  N   LEU A 264     6843  17994   5956    934   -278    209       N  
ATOM   2195  CA  LEU A 264     -22.528   8.501 -67.488  1.00 81.15           C  
ANISOU 2195  CA  LEU A 264     7002  17728   6101   1129   -237    373       C  
ATOM   2196  C   LEU A 264     -22.847   9.806 -68.234  1.00 83.67           C  
ANISOU 2196  C   LEU A 264     7251  18228   6311   1397   -224    568       C  
ATOM   2197  O   LEU A 264     -23.129  10.829 -67.609  1.00 85.60           O  
ANISOU 2197  O   LEU A 264     7525  18400   6597   1579   -191    705       O  
ATOM   2198  CB  LEU A 264     -21.005   8.333 -67.305  1.00 79.33           C  
ANISOU 2198  CB  LEU A 264     6981  17115   6046   1066   -213    351       C  
ATOM   2199  CG  LEU A 264     -20.219   9.425 -66.557  1.00 76.45           C  
ANISOU 2199  CG  LEU A 264     6788  16419   5837   1227   -164    492       C  
ATOM   2200  CD1 LEU A 264     -20.871   9.809 -65.236  1.00 75.24           C  
ANISOU 2200  CD1 LEU A 264     6650  16183   5753   1275   -147    526       C  
ATOM   2201  CD2 LEU A 264     -18.776   8.996 -66.328  1.00 76.19           C  
ANISOU 2201  CD2 LEU A 264     6941  16037   5968   1117   -149    431       C  
ATOM   2202  N   CYS A 265     -22.815   9.762 -69.564  1.00 84.34           N  
ANISOU 2202  N   CYS A 265     7242  18546   6254   1422   -245    580       N  
ATOM   2203  CA  CYS A 265     -23.173  10.927 -70.378  1.00 87.97           C  
ANISOU 2203  CA  CYS A 265     7622  19212   6590   1675   -233    764       C  
ATOM   2204  C   CYS A 265     -24.588  11.423 -70.098  1.00 89.91           C  
ANISOU 2204  C   CYS A 265     7703  19742   6717   1804   -241    837       C  
ATOM   2205  O   CYS A 265     -24.783  12.597 -69.779  1.00 91.14           O  
ANISOU 2205  O   CYS A 265     7888  19848   6894   2031   -200   1009       O  
ATOM   2206  CB  CYS A 265     -23.006  10.624 -71.867  1.00 89.75           C  
ANISOU 2206  CB  CYS A 265     7754  19683   6663   1651   -261    743       C  
ATOM   2207  SG  CYS A 265     -21.306  10.259 -72.339  1.00 87.13           S  
ANISOU 2207  SG  CYS A 265     7614  19030   6461   1547   -243    691       S  
ATOM   2208  N   LYS A 266     -25.566  10.524 -70.204  1.00 91.32           N  
ANISOU 2208  N   LYS A 266     7710  20215   6773   1656   -288    703       N  
ATOM   2209  CA  LYS A 266     -26.969  10.865 -69.939  1.00 93.66           C  
ANISOU 2209  CA  LYS A 266     7828  20811   6946   1755   -301    750       C  
ATOM   2210  C   LYS A 266     -27.135  11.434 -68.534  1.00 94.62           C  
ANISOU 2210  C   LYS A 266     8048  20687   7214   1833   -261    813       C  
ATOM   2211  O   LYS A 266     -27.971  12.311 -68.298  1.00 97.38           O  
ANISOU 2211  O   LYS A 266     8316  21178   7504   2029   -245    943       O  
ATOM   2212  CB  LYS A 266     -27.880   9.643 -70.127  1.00 93.86           C  
ANISOU 2212  CB  LYS A 266     7675  21145   6842   1532   -353    560       C  
ATOM   2213  CG  LYS A 266     -27.744   8.943 -71.475  1.00 94.69           C  
ANISOU 2213  CG  LYS A 266     7678  21499   6800   1418   -391    468       C  
ATOM   2214  CD  LYS A 266     -28.284   9.787 -72.616  1.00 97.10           C  
ANISOU 2214  CD  LYS A 266     7826  22159   6906   1637   -406    619       C  
ATOM   2215  CE  LYS A 266     -27.990   9.131 -73.951  1.00 99.76           C  
ANISOU 2215  CE  LYS A 266     8085  22708   7110   1523   -439    530       C  
ATOM   2216  NZ  LYS A 266     -28.796   9.725 -75.051  1.00103.12           N  
ANISOU 2216  NZ  LYS A 266     8306  23572   7301   1699   -466    643       N  
ATOM   2217  N   LEU A 267     -26.323  10.929 -67.608  1.00 93.87           N  
ANISOU 2217  N   LEU A 267     8130  20227   7309   1683   -244    721       N  
ATOM   2218  CA  LEU A 267     -26.293  11.430 -66.245  1.00 93.53           C  
ANISOU 2218  CA  LEU A 267     8206  19909   7421   1739   -204    770       C  
ATOM   2219  C   LEU A 267     -25.807  12.878 -66.223  1.00 93.73           C  
ANISOU 2219  C   LEU A 267     8340  19764   7509   2004   -146    979       C  
ATOM   2220  O   LEU A 267     -26.357  13.720 -65.512  1.00 94.18           O  
ANISOU 2220  O   LEU A 267     8396  19794   7592   2160   -110   1087       O  
ATOM   2221  CB  LEU A 267     -25.368  10.558 -65.393  1.00 91.35           C  
ANISOU 2221  CB  LEU A 267     8102  19279   7328   1521   -199    631       C  
ATOM   2222  CG  LEU A 267     -25.725  10.271 -63.936  1.00 89.57           C  
ANISOU 2222  CG  LEU A 267     7927  18888   7215   1433   -187    566       C  
ATOM   2223  CD1 LEU A 267     -24.600   9.474 -63.295  1.00 89.35           C  
ANISOU 2223  CD1 LEU A 267     8083  18503   7362   1242   -181    450       C  
ATOM   2224  CD2 LEU A 267     -25.984  11.548 -63.154  1.00 91.01           C  
ANISOU 2224  CD2 LEU A 267     8160  18959   7459   1655   -139    730       C  
ATOM   2225  N   ILE A 268     -24.772  13.159 -67.007  1.00 94.35           N  
ANISOU 2225  N   ILE A 268     8515  19721   7612   2050   -131   1033       N  
ATOM   2226  CA  ILE A 268     -24.210  14.500 -67.073  1.00 96.08           C  
ANISOU 2226  CA  ILE A 268     8849  19763   7892   2287    -67   1224       C  
ATOM   2227  C   ILE A 268     -25.195  15.465 -67.731  1.00 99.90           C  
ANISOU 2227  C   ILE A 268     9182  20563   8209   2535    -54   1389       C  
ATOM   2228  O   ILE A 268     -25.472  16.537 -67.189  1.00100.25           O  
ANISOU 2228  O   ILE A 268     9268  20527   8296   2734      3   1534       O  
ATOM   2229  CB  ILE A 268     -22.846  14.510 -67.799  1.00 94.65           C  
ANISOU 2229  CB  ILE A 268     8804  19384   7773   2263    -53   1232       C  
ATOM   2230  CG1 ILE A 268     -21.778  13.844 -66.922  1.00 90.66           C  
ANISOU 2230  CG1 ILE A 268     8479  18502   7465   2071    -48   1108       C  
ATOM   2231  CG2 ILE A 268     -22.428  15.934 -68.148  1.00 95.44           C  
ANISOU 2231  CG2 ILE A 268     8989  19384   7890   2524     15   1439       C  
ATOM   2232  CD1 ILE A 268     -20.712  13.105 -67.704  1.00 90.37           C  
ANISOU 2232  CD1 ILE A 268     8505  18382   7448   1926    -70   1014       C  
ATOM   2233  N   GLN A 269     -25.746  15.058 -68.875  1.00102.61           N  
ANISOU 2233  N   GLN A 269     9350  21274   8363   2521   -105   1364       N  
ATOM   2234  CA  GLN A 269     -26.674  15.895 -69.639  1.00109.96           C  
ANISOU 2234  CA  GLN A 269    10120  22547   9113   2756    -99   1520       C  
ATOM   2235  C   GLN A 269     -27.741  16.519 -68.739  1.00113.61           C  
ANISOU 2235  C   GLN A 269    10515  23080   9569   2894    -73   1600       C  
ATOM   2236  O   GLN A 269     -27.898  17.741 -68.704  1.00115.61           O  
ANISOU 2236  O   GLN A 269    10798  23304   9823   3149    -12   1789       O  
ATOM   2237  CB  GLN A 269     -27.355  15.090 -70.760  1.00110.45           C  
ANISOU 2237  CB  GLN A 269     9964  23039   8960   2662   -173   1431       C  
ATOM   2238  CG  GLN A 269     -26.415  14.303 -71.667  1.00109.18           C  
ANISOU 2238  CG  GLN A 269     9847  22845   8789   2495   -204   1324       C  
ATOM   2239  CD  GLN A 269     -25.930  15.092 -72.870  1.00109.43           C  
ANISOU 2239  CD  GLN A 269     9890  22953   8736   2679   -182   1476       C  
ATOM   2240  OE1 GLN A 269     -26.086  16.311 -72.936  1.00109.95           O  
ANISOU 2240  OE1 GLN A 269     9976  23014   8785   2940   -130   1675       O  
ATOM   2241  NE2 GLN A 269     -25.331  14.393 -73.832  1.00108.59           N  
ANISOU 2241  NE2 GLN A 269     9774  22910   8574   2544   -215   1384       N  
ATOM   2242  N   SER A 270     -28.448  15.672 -67.995  1.00116.86           N  
ANISOU 2242  N   SER A 270    10845  23574   9983   2722   -113   1454       N  
ATOM   2243  CA  SER A 270     -29.628  16.094 -67.247  1.00122.44           C  
ANISOU 2243  CA  SER A 270    11445  24423  10651   2829   -100   1506       C  
ATOM   2244  C   SER A 270     -29.607  15.590 -65.801  1.00121.79           C  
ANISOU 2244  C   SER A 270    11459  24082  10731   2665    -93   1387       C  
ATOM   2245  O   SER A 270     -29.180  14.465 -65.548  1.00119.57           O  
ANISOU 2245  O   SER A 270    11223  23693  10513   2410   -129   1208       O  
ATOM   2246  CB  SER A 270     -30.899  15.598 -67.953  1.00125.96           C  
ANISOU 2246  CB  SER A 270    11622  25367  10869   2807   -164   1456       C  
ATOM   2247  OG  SER A 270     -31.351  16.529 -68.925  1.00126.61           O  
ANISOU 2247  OG  SER A 270    11590  25721  10794   3066   -152   1637       O  
ATOM   2248  N   ILE A 271     -30.045  16.420 -64.848  1.00125.23           N  
ANISOU 2248  N   ILE A 271    11932  24411  11237   2813    -40   1486       N  
ATOM   2249  CA  ILE A 271     -30.330  17.847 -65.077  1.00130.76           C  
ANISOU 2249  CA  ILE A 271    12627  25154  11898   3127     24   1711       C  
ATOM   2250  C   ILE A 271     -29.515  18.697 -64.088  1.00127.75           C  
ANISOU 2250  C   ILE A 271    12479  24334  11725   3214    109   1795       C  
ATOM   2251  O   ILE A 271     -29.912  18.871 -62.931  1.00123.25           O  
ANISOU 2251  O   ILE A 271    11944  23642  11243   3213    138   1784       O  
ATOM   2252  CB  ILE A 271     -31.851  18.199 -64.955  1.00134.12           C  
ANISOU 2252  CB  ILE A 271    12844  25934  12180   3268     18   1774       C  
ATOM   2253  CG1 ILE A 271     -32.703  17.378 -65.937  1.00135.39           C  
ANISOU 2253  CG1 ILE A 271    12760  26559  12123   3180    -65   1686       C  
ATOM   2254  CG2 ILE A 271     -32.083  19.690 -65.198  1.00135.16           C  
ANISOU 2254  CG2 ILE A 271    12986  26087  12280   3605     95   2015       C  
ATOM   2255  CD1 ILE A 271     -34.199  17.618 -65.835  1.00136.11           C  
ANISOU 2255  CD1 ILE A 271    12628  27023  12063   3297    -78   1731       C  
ATOM   2256  N   PRO A 272     -28.338  19.170 -64.522  1.00128.86           N  
ANISOU 2256  N   PRO A 272    12781  24231  11946   3268    149   1865       N  
ATOM   2257  CA  PRO A 272     -27.670  20.227 -63.788  1.00132.71           C  
ANISOU 2257  CA  PRO A 272    13467  24358  12596   3404    245   1981       C  
ATOM   2258  C   PRO A 272     -27.511  21.509 -64.628  1.00137.23           C  
ANISOU 2258  C   PRO A 272    14067  24959  13113   3687    317   2196       C  
ATOM   2259  O   PRO A 272     -26.428  21.775 -65.157  1.00139.24           O  
ANISOU 2259  O   PRO A 272    14453  25025  13424   3701    346   2235       O  
ATOM   2260  CB  PRO A 272     -26.296  19.604 -63.464  1.00129.72           C  
ANISOU 2260  CB  PRO A 272    13276  23628  12381   3195    236   1859       C  
ATOM   2261  CG  PRO A 272     -26.171  18.384 -64.351  1.00128.49           C  
ANISOU 2261  CG  PRO A 272    13022  23668  12128   2999    146   1717       C  
ATOM   2262  CD  PRO A 272     -27.365  18.362 -65.265  1.00128.69           C  
ANISOU 2262  CD  PRO A 272    12813  24150  11934   3095    104   1761       C  
ATOM   2263  N   THR A 273     -28.588  22.287 -64.749  1.00140.50           N  
ANISOU 2263  N   THR A 273    14356  25609  13416   3912    349   2334       N  
ATOM   2264  CA  THR A 273     -28.559  23.547 -65.510  1.00142.29           C  
ANISOU 2264  CA  THR A 273    14602  25877  13582   4203    428   2554       C  
ATOM   2265  C   THR A 273     -28.115  24.723 -64.633  1.00142.57           C  
ANISOU 2265  C   THR A 273    14834  25552  13783   4356    552   2675       C  
ATOM   2266  O   THR A 273     -27.292  25.542 -65.047  1.00140.80           O  
ANISOU 2266  O   THR A 273    14752  25134  13611   4483    629   2793       O  
ATOM   2267  CB  THR A 273     -29.926  23.870 -66.164  1.00143.36           C  
ANISOU 2267  CB  THR A 273    14504  26459  13506   4397    409   2663       C  
ATOM   2268  OG1 THR A 273     -30.931  24.009 -65.152  1.00143.39           O  
ANISOU 2268  OG1 THR A 273    14436  26521  13523   4435    423   2658       O  
ATOM   2269  CG2 THR A 273     -30.340  22.770 -67.140  1.00142.94           C  
ANISOU 2269  CG2 THR A 273    14252  26782  13275   4250    293   2547       C  
ATOM   2270  N   HIS A 274     -28.665  24.786 -63.421  1.00145.90           N  
ANISOU 2270  N   HIS A 274    15263  25886  14283   4335    573   2639       N  
ATOM   2271  CA  HIS A 274     -28.296  25.791 -62.417  1.00148.64           C  
ANISOU 2271  CA  HIS A 274    15795  25886  14796   4444    689   2723       C  
ATOM   2272  C   HIS A 274     -26.853  25.648 -62.005  1.00144.87           C  
ANISOU 2272  C   HIS A 274    15540  25003  14499   4288    714   2644       C  
ATOM   2273  O   HIS A 274     -26.260  26.568 -61.438  1.00144.02           O  
ANISOU 2273  O   HIS A 274    15610  24586  14526   4381    820   2724       O  
ATOM   2274  CB  HIS A 274     -29.221  25.659 -61.200  1.00154.26           C  
ANISOU 2274  CB  HIS A 274    16447  26619  15543   4409    688   2665       C  
ATOM   2275  CG  HIS A 274     -28.949  26.662 -60.094  1.00158.92           C  
ANISOU 2275  CG  HIS A 274    17214  26870  16297   4512    809   2740       C  
ATOM   2276  ND1 HIS A 274     -29.382  27.937 -60.145  1.00162.07           N  
ANISOU 2276  ND1 HIS A 274    17630  27271  16678   4792    919   2930       N  
ATOM   2277  CD2 HIS A 274     -28.288  26.521 -58.870  1.00157.75           C  
ANISOU 2277  CD2 HIS A 274    17231  26371  16332   4358    836   2639       C  
ATOM   2278  CE1 HIS A 274     -29.005  28.584 -59.023  1.00161.22           C  
ANISOU 2278  CE1 HIS A 274    17695  26825  16736   4809   1016   2944       C  
ATOM   2279  NE2 HIS A 274     -28.337  27.717 -58.245  1.00157.58           N  
ANISOU 2279  NE2 HIS A 274    17320  26155  16395   4542    962   2765       N  
ATOM   2280  N   LEU A 275     -26.267  24.496 -62.319  1.00141.36           N  
ANISOU 2280  N   LEU A 275    15088  24566  14057   4051    620   2486       N  
ATOM   2281  CA  LEU A 275     -24.947  24.140 -61.819  1.00139.43           C  
ANISOU 2281  CA  LEU A 275    15034  23958  13982   3868    625   2382       C  
ATOM   2282  C   LEU A 275     -23.887  24.140 -62.920  1.00142.67           C  
ANISOU 2282  C   LEU A 275    15516  24308  14381   3860    624   2406       C  
ATOM   2283  O   LEU A 275     -22.804  24.701 -62.743  1.00144.37           O  
ANISOU 2283  O   LEU A 275    15919  24209  14726   3876    695   2442       O  
ATOM   2284  CB  LEU A 275     -25.003  22.779 -61.124  1.00135.47           C  
ANISOU 2284  CB  LEU A 275    14495  23454  13522   3586    529   2171       C  
ATOM   2285  CG  LEU A 275     -26.175  22.597 -60.152  1.00134.65           C  
ANISOU 2285  CG  LEU A 275    14287  23470  13401   3571    515   2131       C  
ATOM   2286  CD1 LEU A 275     -26.610  21.142 -60.080  1.00134.62           C  
ANISOU 2286  CD1 LEU A 275    14156  23653  13340   3327    403   1944       C  
ATOM   2287  CD2 LEU A 275     -25.842  23.138 -58.768  1.00132.97           C  
ANISOU 2287  CD2 LEU A 275    14238  22920  13364   3570    591   2133       C  
ATOM   2288  N   LEU A 276     -24.204  23.514 -64.052  1.00144.61           N  
ANISOU 2288  N   LEU A 276    15611  24863  14469   3830    545   2381       N  
ATOM   2289  CA  LEU A 276     -23.279  23.445 -65.187  1.00146.87           C  
ANISOU 2289  CA  LEU A 276    15946  25133  14726   3819    537   2399       C  
ATOM   2290  C   LEU A 276     -23.919  23.972 -66.463  1.00150.28           C  
ANISOU 2290  C   LEU A 276    16238  25894  14966   4028    541   2547       C  
ATOM   2291  O   LEU A 276     -23.374  24.857 -67.128  1.00148.99           O  
ANISOU 2291  O   LEU A 276    16160  25648  14798   4193    614   2688       O  
ATOM   2292  CB  LEU A 276     -22.813  22.003 -65.419  1.00144.61           C  
ANISOU 2292  CB  LEU A 276    15625  24880  14437   3538    431   2199       C  
ATOM   2293  CG  LEU A 276     -21.816  21.364 -64.454  1.00141.41           C  
ANISOU 2293  CG  LEU A 276    15379  24130  14219   3316    421   2051       C  
ATOM   2294  CD1 LEU A 276     -21.827  19.855 -64.634  1.00141.48           C  
ANISOU 2294  CD1 LEU A 276    15300  24265  14188   3058    313   1857       C  
ATOM   2295  CD2 LEU A 276     -20.414  21.919 -64.660  1.00139.21           C  
ANISOU 2295  CD2 LEU A 276    15296  23538  14060   3340    486   2099       C  
ATOM   2296  N   ASP A 277     -25.085  23.419 -66.789  1.00153.98           N  
ANISOU 2296  N   ASP A 277    16490  26740  15273   4019    465   2512       N  
ATOM   2297  CA  ASP A 277     -25.746  23.638 -68.073  1.00159.07           C  
ANISOU 2297  CA  ASP A 277    16966  27763  15709   4175    442   2619       C  
ATOM   2298  C   ASP A 277     -24.928  23.061 -69.239  1.00158.69           C  
ANISOU 2298  C   ASP A 277    16922  27769  15603   4069    392   2565       C  
ATOM   2299  O   ASP A 277     -24.339  21.986 -69.113  1.00154.28           O  
ANISOU 2299  O   ASP A 277    16395  27117  15104   3815    328   2385       O  
ATOM   2300  CB  ASP A 277     -26.090  25.122 -68.289  1.00163.95           C  
ANISOU 2300  CB  ASP A 277    17611  28391  16291   4503    551   2860       C  
ATOM   2301  CG  ASP A 277     -27.360  25.318 -69.111  1.00168.18           C  
ANISOU 2301  CG  ASP A 277    17914  29385  16600   4682    519   2965       C  
ATOM   2302  OD1 ASP A 277     -28.286  24.485 -68.999  1.00168.28           O  
ANISOU 2302  OD1 ASP A 277    17741  29682  16513   4571    430   2854       O  
ATOM   2303  OD2 ASP A 277     -27.434  26.311 -69.865  1.00169.36           O  
ANISOU 2303  OD2 ASP A 277    18064  29614  16669   4934    587   3159       O  
ATOM   2304  N   SER A 278     -24.867  23.801 -70.347  1.00160.68           N  
ANISOU 2304  N   SER A 278    17151  28155  15743   4269    430   2725       N  
ATOM   2305  CA  SER A 278     -24.546  23.225 -71.656  1.00160.11           C  
ANISOU 2305  CA  SER A 278    17001  28291  15541   4201    367   2687       C  
ATOM   2306  C   SER A 278     -23.061  23.240 -72.038  1.00157.75           C  
ANISOU 2306  C   SER A 278    16892  27691  15355   4124    399   2667       C  
ATOM   2307  O   SER A 278     -22.482  22.190 -72.322  1.00154.14           O  
ANISOU 2307  O   SER A 278    16435  27219  14911   3895    329   2505       O  
ATOM   2308  CB  SER A 278     -25.389  23.891 -72.749  1.00162.92           C  
ANISOU 2308  CB  SER A 278    17196  29021  15682   4450    375   2863       C  
ATOM   2309  OG  SER A 278     -25.484  23.067 -73.896  1.00165.44           O  
ANISOU 2309  OG  SER A 278    17369  29652  15837   4346    286   2785       O  
ATOM   2310  N   GLU A 279     -22.460  24.430 -72.054  1.00160.13           N  
ANISOU 2310  N   GLU A 279    17350  27755  15734   4314    509   2832       N  
ATOM   2311  CA  GLU A 279     -21.075  24.604 -72.519  1.00158.96           C  
ANISOU 2311  CA  GLU A 279    17377  27341  15679   4273    552   2837       C  
ATOM   2312  C   GLU A 279     -20.136  23.647 -71.799  1.00152.98           C  
ANISOU 2312  C   GLU A 279    16733  26304  15088   3990    510   2634       C  
ATOM   2313  O   GLU A 279     -19.200  23.111 -72.396  1.00151.02           O  
ANISOU 2313  O   GLU A 279    16540  25980  14860   3857    482   2554       O  
ATOM   2314  CB  GLU A 279     -20.595  26.050 -72.321  1.00162.89           C  
ANISOU 2314  CB  GLU A 279    18050  27569  16270   4500    693   3027       C  
ATOM   2315  CG  GLU A 279     -21.703  27.073 -72.124  1.00169.46           C  
ANISOU 2315  CG  GLU A 279    18813  28545  17028   4770    760   3208       C  
ATOM   2316  CD  GLU A 279     -22.151  27.167 -70.675  1.00171.67           C  
ANISOU 2316  CD  GLU A 279    19129  28664  17433   4739    784   3162       C  
ATOM   2317  OE1 GLU A 279     -21.436  27.801 -69.873  1.00171.15           O  
ANISOU 2317  OE1 GLU A 279    19257  28228  17542   4754    877   3186       O  
ATOM   2318  OE2 GLU A 279     -23.215  26.604 -70.338  1.00173.88           O  
ANISOU 2318  OE2 GLU A 279    19242  29189  17633   4695    710   3097       O  
ATOM   2319  N   LYS A 280     -20.406  23.430 -70.515  1.00147.94           N  
ANISOU 2319  N   LYS A 280    16126  25518  14565   3904    507   2554       N  
ATOM   2320  CA  LYS A 280     -19.632  22.501 -69.709  1.00141.86           C  
ANISOU 2320  CA  LYS A 280    15453  24496  13948   3643    466   2366       C  
ATOM   2321  C   LYS A 280     -19.986  21.064 -70.080  1.00139.79           C  
ANISOU 2321  C   LYS A 280    15041  24477  13593   3423    346   2187       C  
ATOM   2322  O   LYS A 280     -19.099  20.266 -70.393  1.00138.89           O  
ANISOU 2322  O   LYS A 280    14981  24264  13525   3241    307   2064       O  
ATOM   2323  CB  LYS A 280     -19.882  22.735 -68.214  1.00140.16           C  
ANISOU 2323  CB  LYS A 280    15311  24067  13873   3627    502   2342       C  
ATOM   2324  CG  LYS A 280     -20.599  24.034 -67.875  1.00140.47           C  
ANISOU 2324  CG  LYS A 280    15355  24116  13897   3890    595   2527       C  
ATOM   2325  CD  LYS A 280     -19.660  25.228 -67.815  1.00137.92           C  
ANISOU 2325  CD  LYS A 280    15233  23479  13691   4033    719   2659       C  
ATOM   2326  CE  LYS A 280     -20.401  26.461 -67.327  1.00137.24           C  
ANISOU 2326  CE  LYS A 280    15161  23376  13605   4278    821   2828       C  
ATOM   2327  NZ  LYS A 280     -19.580  27.696 -67.438  1.00134.97           N  
ANISOU 2327  NZ  LYS A 280    15059  22816  13405   4439    956   2972       N  
ATOM   2328  N   LYS A 281     -21.285  20.748 -70.066  1.00137.65           N  
ANISOU 2328  N   LYS A 281    14581  24529  13188   3441    294   2172       N  
ATOM   2329  CA  LYS A 281     -21.754  19.380 -70.312  1.00134.65           C  
ANISOU 2329  CA  LYS A 281    14051  24390  12718   3223    189   1993       C  
ATOM   2330  C   LYS A 281     -21.255  18.835 -71.650  1.00131.88           C  
ANISOU 2330  C   LYS A 281    13652  24192  12261   3150    145   1949       C  
ATOM   2331  O   LYS A 281     -20.830  17.685 -71.733  1.00127.81           O  
ANISOU 2331  O   LYS A 281    13136  23654  11771   2915     86   1774       O  
ATOM   2332  CB  LYS A 281     -23.289  19.278 -70.208  1.00136.50           C  
ANISOU 2332  CB  LYS A 281    14075  24983  12803   3282    149   2003       C  
ATOM   2333  CG  LYS A 281     -24.044  19.459 -71.522  1.00142.49           C  
ANISOU 2333  CG  LYS A 281    14645  26163  13332   3416    119   2092       C  
ATOM   2334  CD  LYS A 281     -25.492  18.994 -71.424  1.00143.59           C  
ANISOU 2334  CD  LYS A 281    14557  26679  13321   3398     58   2042       C  
ATOM   2335  CE  LYS A 281     -26.455  20.160 -71.220  1.00146.59           C  
ANISOU 2335  CE  LYS A 281    14866  27196  13633   3680    112   2234       C  
ATOM   2336  NZ  LYS A 281     -27.871  19.770 -71.482  1.00145.03           N  
ANISOU 2336  NZ  LYS A 281    14414  27446  13243   3691     48   2206       N  
ATOM   2337  N   ASN A 282     -21.285  19.679 -72.680  1.00131.58           N  
ANISOU 2337  N   ASN A 282    13583  24300  12110   3355    180   2111       N  
ATOM   2338  CA  ASN A 282     -20.815  19.302 -74.007  1.00128.95           C  
ANISOU 2338  CA  ASN A 282    13207  24120  11667   3312    147   2091       C  
ATOM   2339  C   ASN A 282     -19.349  18.902 -73.996  1.00125.82           C  
ANISOU 2339  C   ASN A 282    12992  23389  11424   3155    159   1999       C  
ATOM   2340  O   ASN A 282     -18.962  17.929 -74.646  1.00125.01           O  
ANISOU 2340  O   ASN A 282    12850  23367  11278   2977    102   1866       O  
ATOM   2341  CB  ASN A 282     -21.039  20.443 -75.002  1.00132.31           C  
ANISOU 2341  CB  ASN A 282    13595  24716  11960   3588    198   2307       C  
ATOM   2342  CG  ASN A 282     -22.501  20.824 -75.137  1.00134.23           C  
ANISOU 2342  CG  ASN A 282    13640  25328  12031   3757    182   2406       C  
ATOM   2343  OD1 ASN A 282     -23.378  19.963 -75.203  1.00133.52           O  
ANISOU 2343  OD1 ASN A 282    13371  25532  11827   3639    101   2291       O  
ATOM   2344  ND2 ASN A 282     -22.769  22.123 -75.181  1.00135.04           N  
ANISOU 2344  ND2 ASN A 282    13775  25418  12113   4036    265   2620       N  
ATOM   2345  N   PHE A 283     -18.540  19.650 -73.244  1.00123.30           N  
ANISOU 2345  N   PHE A 283    12868  22698  11282   3219    238   2065       N  
ATOM   2346  CA  PHE A 283     -17.111  19.365 -73.128  1.00119.63           C  
ANISOU 2346  CA  PHE A 283    12581  21897  10974   3082    257   1986       C  
ATOM   2347  C   PHE A 283     -16.842  18.074 -72.366  1.00116.77           C  
ANISOU 2347  C   PHE A 283    12237  21417  10714   2809    194   1772       C  
ATOM   2348  O   PHE A 283     -15.913  17.336 -72.698  1.00116.50           O  
ANISOU 2348  O   PHE A 283    12263  21268  10731   2645    169   1658       O  
ATOM   2349  CB  PHE A 283     -16.359  20.526 -72.468  1.00118.58           C  
ANISOU 2349  CB  PHE A 283    12645  21409  11001   3217    362   2108       C  
ATOM   2350  CG  PHE A 283     -14.889  20.258 -72.279  1.00117.56           C  
ANISOU 2350  CG  PHE A 283    12693  20938  11034   3077    382   2024       C  
ATOM   2351  CD1 PHE A 283     -14.005  20.356 -73.352  1.00116.93           C  
ANISOU 2351  CD1 PHE A 283    12664  20837  10926   3086    399   2051       C  
ATOM   2352  CD2 PHE A 283     -14.391  19.879 -71.035  1.00115.60           C  
ANISOU 2352  CD2 PHE A 283    12557  20402  10963   2933    383   1916       C  
ATOM   2353  CE1 PHE A 283     -12.653  20.095 -73.184  1.00116.12           C  
ANISOU 2353  CE1 PHE A 283    12716  20431  10970   2957    417   1971       C  
ATOM   2354  CE2 PHE A 283     -13.040  19.616 -70.862  1.00113.30           C  
ANISOU 2354  CE2 PHE A 283    12419  19814  10815   2808    399   1839       C  
ATOM   2355  CZ  PHE A 283     -12.170  19.726 -71.937  1.00113.75           C  
ANISOU 2355  CZ  PHE A 283    12522  19853  10845   2819    416   1865       C  
ATOM   2356  N   ILE A 284     -17.642  17.815 -71.336  1.00112.18           N  
ANISOU 2356  N   ILE A 284    11606  20853  10162   2764    173   1720       N  
ATOM   2357  CA  ILE A 284     -17.514  16.581 -70.572  1.00108.60           C  
ANISOU 2357  CA  ILE A 284    11162  20304   9795   2513    117   1523       C  
ATOM   2358  C   ILE A 284     -18.029  15.387 -71.382  1.00109.85           C  
ANISOU 2358  C   ILE A 284    11155  20775   9807   2352     34   1387       C  
ATOM   2359  O   ILE A 284     -17.379  14.342 -71.426  1.00108.46           O  
ANISOU 2359  O   ILE A 284    11018  20503   9686   2142      0   1232       O  
ATOM   2360  CB  ILE A 284     -18.221  16.669 -69.201  1.00108.27           C  
ANISOU 2360  CB  ILE A 284    11121  20185   9829   2510    124   1509       C  
ATOM   2361  CG1 ILE A 284     -17.801  17.947 -68.463  1.00107.04           C  
ANISOU 2361  CG1 ILE A 284    11120  19749   9802   2683    216   1652       C  
ATOM   2362  CG2 ILE A 284     -17.892  15.448 -68.350  1.00106.08           C  
ANISOU 2362  CG2 ILE A 284    10890  19751   9664   2254     79   1316       C  
ATOM   2363  CD1 ILE A 284     -18.634  18.263 -67.237  1.00105.91           C  
ANISOU 2363  CD1 ILE A 284    10962  19570   9707   2729    234   1672       C  
ATOM   2364  N   VAL A 285     -19.173  15.562 -72.049  1.00110.69           N  
ANISOU 2364  N   VAL A 285    11076  21255   9723   2455      7   1446       N  
ATOM   2365  CA  VAL A 285     -19.784  14.495 -72.856  1.00110.70           C  
ANISOU 2365  CA  VAL A 285    10902  21594   9564   2310    -66   1319       C  
ATOM   2366  C   VAL A 285     -18.787  13.871 -73.835  1.00109.73           C  
ANISOU 2366  C   VAL A 285    10822  21437   9433   2185    -84   1237       C  
ATOM   2367  O   VAL A 285     -18.557  12.660 -73.814  1.00108.96           O  
ANISOU 2367  O   VAL A 285    10714  21327   9357   1952   -126   1055       O  
ATOM   2368  CB  VAL A 285     -21.048  14.985 -73.608  1.00113.81           C  
ANISOU 2368  CB  VAL A 285    11090  22412   9739   2479    -85   1426       C  
ATOM   2369  CG1 VAL A 285     -21.463  13.996 -74.689  1.00114.90           C  
ANISOU 2369  CG1 VAL A 285    11057  22900   9699   2338   -154   1305       C  
ATOM   2370  CG2 VAL A 285     -22.193  15.200 -72.633  1.00114.42           C  
ANISOU 2370  CG2 VAL A 285    11086  22581   9808   2536    -87   1448       C  
ATOM   2371  N   ASP A 286     -18.177  14.701 -74.673  1.00110.88           N  
ANISOU 2371  N   ASP A 286    11023  21554   9550   2340    -44   1371       N  
ATOM   2372  CA  ASP A 286     -17.229  14.197 -75.657  1.00111.09           C  
ANISOU 2372  CA  ASP A 286    11090  21556   9562   2238    -55   1305       C  
ATOM   2373  C   ASP A 286     -15.881  13.846 -75.027  1.00107.23           C  
ANISOU 2373  C   ASP A 286    10803  20654   9286   2103    -30   1220       C  
ATOM   2374  O   ASP A 286     -15.056  13.174 -75.643  1.00107.07           O  
ANISOU 2374  O   ASP A 286    10822  20578   9280   1969    -44   1124       O  
ATOM   2375  CB  ASP A 286     -17.066  15.177 -76.834  1.00115.35           C  
ANISOU 2375  CB  ASP A 286    11613  22230   9984   2447    -21   1478       C  
ATOM   2376  CG  ASP A 286     -16.382  16.479 -76.435  1.00116.23           C  
ANISOU 2376  CG  ASP A 286    11896  22043  10221   2643     65   1650       C  
ATOM   2377  OD1 ASP A 286     -16.238  16.743 -75.220  1.00115.87           O  
ANISOU 2377  OD1 ASP A 286    11959  21733  10333   2644     98   1653       O  
ATOM   2378  OD2 ASP A 286     -15.991  17.241 -77.348  1.00113.42           O  
ANISOU 2378  OD2 ASP A 286    11568  21722   9803   2794    106   1782       O  
ATOM   2379  N   HIS A 287     -15.666  14.290 -73.793  1.00108.38           N  
ANISOU 2379  N   HIS A 287    11070  20515   9592   2138      7   1254       N  
ATOM   2380  CA  HIS A 287     -14.422  13.983 -73.095  1.00106.55           C  
ANISOU 2380  CA  HIS A 287    11022  19899   9561   2016     30   1176       C  
ATOM   2381  C   HIS A 287     -14.363  12.549 -72.641  1.00103.73           C  
ANISOU 2381  C   HIS A 287    10650  19506   9254   1758    -23    970       C  
ATOM   2382  O   HIS A 287     -13.309  11.919 -72.725  1.00101.91           O  
ANISOU 2382  O   HIS A 287    10519  19082   9119   1620    -24    873       O  
ATOM   2383  CB  HIS A 287     -14.196  14.931 -71.927  1.00106.65           C  
ANISOU 2383  CB  HIS A 287    11169  19629   9724   2132     91   1275       C  
ATOM   2384  CG  HIS A 287     -12.744  15.260 -71.690  1.00107.59           C  
ANISOU 2384  CG  HIS A 287    11484  19386  10009   2118    142   1287       C  
ATOM   2385  ND1 HIS A 287     -12.090  14.892 -70.573  1.00106.70           N  
ANISOU 2385  ND1 HIS A 287    11494  18977  10069   1998    148   1201       N  
ATOM   2386  CD2 HIS A 287     -11.816  15.931 -72.487  1.00108.30           C  
ANISOU 2386  CD2 HIS A 287    11661  19378  10108   2212    190   1376       C  
ATOM   2387  CE1 HIS A 287     -10.815  15.315 -70.642  1.00106.45           C  
ANISOU 2387  CE1 HIS A 287    11614  18680  10151   2014    196   1231       C  
ATOM   2388  NE2 HIS A 287     -10.649  15.948 -71.814  1.00109.03           N  
ANISOU 2388  NE2 HIS A 287    11921  19125  10379   2141    223   1336       N  
ATOM   2389  N   ILE A 288     -15.500  12.022 -72.178  1.00102.22           N  
ANISOU 2389  N   ILE A 288    10335  19506   8998   1694    -62    902       N  
ATOM   2390  CA  ILE A 288     -15.599  10.628 -71.703  1.00101.18           C  
ANISOU 2390  CA  ILE A 288    10181  19358   8904   1446   -106    704       C  
ATOM   2391  C   ILE A 288     -15.431   9.638 -72.863  1.00 99.68           C  
ANISOU 2391  C   ILE A 288     9912  19354   8609   1297   -143    582       C  
ATOM   2392  O   ILE A 288     -14.797   8.592 -72.730  1.00 98.98           O  
ANISOU 2392  O   ILE A 288     9883  19124   8599   1100   -154    432       O  
ATOM   2393  CB  ILE A 288     -16.955  10.352 -70.993  1.00103.20           C  
ANISOU 2393  CB  ILE A 288    10310  19803   9098   1418   -134    666       C  
ATOM   2394  CG1 ILE A 288     -17.441  11.572 -70.198  1.00103.88           C  
ANISOU 2394  CG1 ILE A 288    10420  19827   9220   1624    -96    825       C  
ATOM   2395  CG2 ILE A 288     -16.853   9.134 -70.088  1.00101.68           C  
ANISOU 2395  CG2 ILE A 288    10160  19463   9009   1185   -155    487       C  
ATOM   2396  CD1 ILE A 288     -16.526  11.990 -69.063  1.00103.82           C  
ANISOU 2396  CD1 ILE A 288    10608  19415   9421   1638    -50    854       C  
ATOM   2397  N   SER A 289     -16.035   9.970 -73.990  1.00 99.15           N  
ANISOU 2397  N   SER A 289     9704  19610   8356   1393   -158    646       N  
ATOM   2398  CA  SER A 289     -15.773   9.288 -75.236  1.00101.06           C  
ANISOU 2398  CA  SER A 289     9879  20030   8488   1290   -183    562       C  
ATOM   2399  C   SER A 289     -15.816  10.380 -76.281  1.00104.38           C  
ANISOU 2399  C   SER A 289    10253  20619   8785   1509   -166    735       C  
ATOM   2400  O   SER A 289     -16.861  11.005 -76.476  1.00110.00           O  
ANISOU 2400  O   SER A 289    10836  21596   9362   1657   -174    839       O  
ATOM   2401  CB  SER A 289     -16.850   8.243 -75.508  1.00100.46           C  
ANISOU 2401  CB  SER A 289     9623  20277   8268   1131   -234    416       C  
ATOM   2402  OG  SER A 289     -18.142   8.808 -75.370  1.00 98.06           O  
ANISOU 2402  OG  SER A 289     9173  20244   7839   1261   -249    503       O  
ATOM   2403  N   ASN A 290     -14.699  10.617 -76.966  1.00101.62           N  
ANISOU 2403  N   ASN A 290    10007  20126   8476   1533   -138    769       N  
ATOM   2404  CA  ASN A 290     -13.612   9.655 -77.092  1.00 99.90           C  
ANISOU 2404  CA  ASN A 290     9888  19707   8360   1335   -140    621       C  
ATOM   2405  C   ASN A 290     -12.330  10.094 -76.392  1.00 98.25           C  
ANISOU 2405  C   ASN A 290     9891  19076   8362   1364    -92    663       C  
ATOM   2406  O   ASN A 290     -11.926  11.257 -76.472  1.00 98.62           O  
ANISOU 2406  O   ASN A 290    10015  19015   8440   1551    -46    823       O  
ATOM   2407  CB  ASN A 290     -13.323   9.431 -78.574  1.00101.76           C  
ANISOU 2407  CB  ASN A 290    10058  20147   8458   1314   -152    602       C  
ATOM   2408  CG  ASN A 290     -14.296  10.180 -79.475  1.00103.39           C  
ANISOU 2408  CG  ASN A 290    10104  20726   8452   1491   -165    734       C  
ATOM   2409  OD1 ASN A 290     -14.475  11.393 -79.344  1.00103.09           O  
ANISOU 2409  OD1 ASN A 290    10090  20670   8409   1716   -131    918       O  
ATOM   2410  ND2 ASN A 290     -14.933   9.459 -80.388  1.00102.99           N  
ANISOU 2410  ND2 ASN A 290     9889  21018   8223   1392   -209    640       N  
ATOM   2411  N   GLN A 291     -11.682   9.146 -75.728  1.00 94.81           N  
ANISOU 2411  N   GLN A 291     9547  18409   8067   1176    -97    517       N  
ATOM   2412  CA  GLN A 291     -10.432   9.407 -75.029  1.00 92.20           C  
ANISOU 2412  CA  GLN A 291     9408  17688   7935   1176    -57    534       C  
ATOM   2413  C   GLN A 291      -9.265   8.859 -75.841  1.00 92.56           C  
ANISOU 2413  C   GLN A 291     9520  17633   8013   1074    -50    457       C  
ATOM   2414  O   GLN A 291      -9.122   7.647 -75.993  1.00 92.68           O  
ANISOU 2414  O   GLN A 291     9514  17667   8032    880    -75    295       O  
ATOM   2415  CB  GLN A 291     -10.458   8.760 -73.645  1.00 88.85           C  
ANISOU 2415  CB  GLN A 291     9046  17059   7653   1050    -66    435       C  
ATOM   2416  CG  GLN A 291     -11.589   9.245 -72.755  1.00 87.84           C  
ANISOU 2416  CG  GLN A 291     8857  17012   7503   1137    -72    500       C  
ATOM   2417  CD  GLN A 291     -11.772   8.395 -71.508  1.00 85.56           C  
ANISOU 2417  CD  GLN A 291     8604  16581   7324    983    -88    379       C  
ATOM   2418  OE1 GLN A 291     -11.714   7.166 -71.563  1.00 84.47           O  
ANISOU 2418  OE1 GLN A 291     8444  16459   7189    788   -113    220       O  
ATOM   2419  NE2 GLN A 291     -12.013   9.051 -70.377  1.00 82.99           N  
ANISOU 2419  NE2 GLN A 291     8333  16112   7085   1071    -68    454       N  
ATOM   2420  N   PHE A 292      -8.436   9.755 -76.365  1.00 93.30           N  
ANISOU 2420  N   PHE A 292     9698  17620   8132   1204     -9    573       N  
ATOM   2421  CA  PHE A 292      -7.354   9.358 -77.263  1.00 94.67           C  
ANISOU 2421  CA  PHE A 292     9925  17725   8318   1128      1    515       C  
ATOM   2422  C   PHE A 292      -5.981   9.555 -76.633  1.00 93.79           C  
ANISOU 2422  C   PHE A 292     9998  17232   8406   1113     42    517       C  
ATOM   2423  O   PHE A 292      -5.707  10.594 -76.024  1.00 93.81           O  
ANISOU 2423  O   PHE A 292    10090  17059   8492   1251     82    639       O  
ATOM   2424  CB  PHE A 292      -7.453  10.102 -78.599  1.00100.03           C  
ANISOU 2424  CB  PHE A 292    10538  18623   8842   1268     15    631       C  
ATOM   2425  CG  PHE A 292      -8.071  11.471 -78.493  1.00104.23           C  
ANISOU 2425  CG  PHE A 292    11053  19228   9320   1504     44    826       C  
ATOM   2426  CD1 PHE A 292      -7.382  12.521 -77.884  1.00105.76           C  
ANISOU 2426  CD1 PHE A 292    11392  19143   9646   1635    105    947       C  
ATOM   2427  CD2 PHE A 292      -9.340  11.713 -79.006  1.00106.24           C  
ANISOU 2427  CD2 PHE A 292    11143  19833   9389   1595     17    888       C  
ATOM   2428  CE1 PHE A 292      -7.950  13.781 -77.787  1.00107.63           C  
ANISOU 2428  CE1 PHE A 292    11620  19435   9836   1853    144   1127       C  
ATOM   2429  CE2 PHE A 292      -9.912  12.974 -78.917  1.00108.83           C  
ANISOU 2429  CE2 PHE A 292    11456  20226   9667   1823     51   1075       C  
ATOM   2430  CZ  PHE A 292      -9.216  14.009 -78.307  1.00109.52           C  
ANISOU 2430  CZ  PHE A 292    11699  20019   9892   1953    117   1195       C  
ATOM   2431  N   VAL A 293      -5.121   8.550 -76.780  1.00 91.07           N  
ANISOU 2431  N   VAL A 293     9706  16763   8134    945     34    378       N  
ATOM   2432  CA  VAL A 293      -3.828   8.542 -76.098  1.00 88.53           C  
ANISOU 2432  CA  VAL A 293     9546  16089   8001    906     65    355       C  
ATOM   2433  C   VAL A 293      -2.644   8.210 -77.008  1.00 89.76           C  
ANISOU 2433  C   VAL A 293     9759  16164   8181    844     84    304       C  
ATOM   2434  O   VAL A 293      -2.736   7.361 -77.901  1.00 89.55           O  
ANISOU 2434  O   VAL A 293     9658  16303   8063    735     62    204       O  
ATOM   2435  CB  VAL A 293      -3.823   7.584 -74.886  1.00 86.50           C  
ANISOU 2435  CB  VAL A 293     9330  15669   7867    756     43    230       C  
ATOM   2436  CG1 VAL A 293      -4.751   8.098 -73.801  1.00 85.16           C  
ANISOU 2436  CG1 VAL A 293     9139  15504   7712    833     37    297       C  
ATOM   2437  CG2 VAL A 293      -4.209   6.172 -75.304  1.00 88.80           C  
ANISOU 2437  CG2 VAL A 293     9534  16112   8092    568      7     64       C  
ATOM   2438  N   ALA A 294      -1.529   8.892 -76.764  1.00 90.14           N  
ANISOU 2438  N   ALA A 294     9939  15957   8351    910    128    368       N  
ATOM   2439  CA  ALA A 294      -0.277   8.599 -77.441  1.00 91.23           C  
ANISOU 2439  CA  ALA A 294    10149  15972   8540    849    150    317       C  
ATOM   2440  C   ALA A 294       0.335   7.317 -76.892  1.00 91.04           C  
ANISOU 2440  C   ALA A 294    10173  15784   8633    662    132    153       C  
ATOM   2441  O   ALA A 294       0.204   7.008 -75.706  1.00 91.92           O  
ANISOU 2441  O   ALA A 294    10323  15757   8845    614    120    116       O  
ATOM   2442  CB  ALA A 294       0.693   9.760 -77.280  1.00 90.19           C  
ANISOU 2442  CB  ALA A 294    10142  15621   8504    977    208    436       C  
ATOM   2443  N   PHE A 295       0.988   6.564 -77.767  1.00 93.36           N  
ANISOU 2443  N   PHE A 295    10465  16097   8910    558    133     58       N  
ATOM   2444  CA  PHE A 295       1.741   5.393 -77.352  1.00 93.89           C  
ANISOU 2444  CA  PHE A 295    10592  15987   9095    395    129    -87       C  
ATOM   2445  C   PHE A 295       3.041   5.280 -78.168  1.00 99.50           C  
ANISOU 2445  C   PHE A 295    11368  16589   9848    366    160   -117       C  
ATOM   2446  O   PHE A 295       3.745   6.280 -78.367  1.00103.05           O  
ANISOU 2446  O   PHE A 295    11883  16938  10330    481    195    -13       O  
ATOM   2447  CB  PHE A 295       0.874   4.126 -77.448  1.00 89.65           C  
ANISOU 2447  CB  PHE A 295     9958  15621   8484    241     93   -226       C  
ATOM   2448  CG  PHE A 295       1.341   3.003 -76.561  1.00 85.64           C  
ANISOU 2448  CG  PHE A 295     9517  14908   8112     93     91   -355       C  
ATOM   2449  CD1 PHE A 295       1.571   3.216 -75.208  1.00 83.27           C  
ANISOU 2449  CD1 PHE A 295     9302  14385   7951    119     92   -324       C  
ATOM   2450  CD2 PHE A 295       1.553   1.731 -77.079  1.00 83.81           C  
ANISOU 2450  CD2 PHE A 295     9266  14708   7869    -69     93   -506       C  
ATOM   2451  CE1 PHE A 295       2.015   2.184 -74.393  1.00 82.13           C  
ANISOU 2451  CE1 PHE A 295     9220  14056   7927     -7     92   -434       C  
ATOM   2452  CE2 PHE A 295       1.992   0.697 -76.269  1.00 79.53           C  
ANISOU 2452  CE2 PHE A 295     8792  13971   7453   -195     99   -617       C  
ATOM   2453  CZ  PHE A 295       2.223   0.922 -74.926  1.00 80.68           C  
ANISOU 2453  CZ  PHE A 295     9020  13900   7732   -161     97   -577       C  
ATOM   2454  N   ARG A 296       3.359   4.074 -78.633  1.00 98.56           N  
ANISOU 2454  N   ARG A 296    11233  16486   9728    213    154   -261       N  
ATOM   2455  CA  ARG A 296       4.584   3.835 -79.394  1.00 93.97           C  
ANISOU 2455  CA  ARG A 296    10709  15804   9188    173    184   -306       C  
ATOM   2456  C   ARG A 296       4.477   4.415 -80.804  1.00 97.26           C  
ANISOU 2456  C   ARG A 296    11064  16432   9456    244    197   -243       C  
ATOM   2457  O   ARG A 296       4.143   3.707 -81.758  1.00 96.89           O  
ANISOU 2457  O   ARG A 296    10935  16582   9297    156    186   -328       O  
ATOM   2458  CB  ARG A 296       4.896   2.338 -79.436  1.00 87.13           C  
ANISOU 2458  CB  ARG A 296     9846  14890   8366    -10    181   -480       C  
ATOM   2459  CG  ARG A 296       5.104   1.735 -78.058  1.00 79.42           C  
ANISOU 2459  CG  ARG A 296     8941  13692   7541    -77    175   -536       C  
ATOM   2460  CD  ARG A 296       5.106   0.221 -78.105  1.00 75.02           C  
ANISOU 2460  CD  ARG A 296     8372  13128   7002   -255    176   -704       C  
ATOM   2461  NE  ARG A 296       5.512  -0.355 -76.826  1.00 69.86           N  
ANISOU 2461  NE  ARG A 296     7804  12235   6504   -310    178   -750       N  
ATOM   2462  CZ  ARG A 296       5.590  -1.661 -76.587  1.00 68.50           C  
ANISOU 2462  CZ  ARG A 296     7647  11999   6381   -455    188   -885       C  
ATOM   2463  NH1 ARG A 296       5.279  -2.532 -77.541  1.00 69.07           N  
ANISOU 2463  NH1 ARG A 296     7655  12226   6359   -570    201   -997       N  
ATOM   2464  NH2 ARG A 296       5.969  -2.098 -75.395  1.00 64.74           N  
ANISOU 2464  NH2 ARG A 296     7251  11304   6042   -486    191   -909       N  
ATOM   2465  N   ARG A 297       4.751   5.718 -80.910  1.00101.57           N  
ANISOU 2465  N   ARG A 297    11652  16938  10002    403    223    -94       N  
ATOM   2466  CA  ARG A 297       4.623   6.480 -82.164  1.00106.20           C  
ANISOU 2466  CA  ARG A 297    12189  17714  10446    504    241     -2       C  
ATOM   2467  C   ARG A 297       3.171   6.597 -82.646  1.00107.36           C  
ANISOU 2467  C   ARG A 297    12195  18187  10408    548    206     36       C  
ATOM   2468  O   ARG A 297       2.846   7.474 -83.450  1.00108.17           O  
ANISOU 2468  O   ARG A 297    12254  18455  10388    675    219    154       O  
ATOM   2469  CB  ARG A 297       5.534   5.911 -83.273  1.00107.16           C  
ANISOU 2469  CB  ARG A 297    12321  17843  10549    418    261    -86       C  
ATOM   2470  CG  ARG A 297       7.027   6.142 -83.051  1.00105.47           C  
ANISOU 2470  CG  ARG A 297    12240  17342  10492    421    305    -85       C  
ATOM   2471  CD  ARG A 297       7.838   5.860 -84.315  1.00107.55           C  
ANISOU 2471  CD  ARG A 297    12505  17650  10710    373    331   -135       C  
ATOM   2472  NE  ARG A 297       8.302   4.470 -84.395  1.00106.40           N  
ANISOU 2472  NE  ARG A 297    12361  17448  10618    199    323   -308       N  
ATOM   2473  CZ  ARG A 297       8.855   3.913 -85.476  1.00104.54           C  
ANISOU 2473  CZ  ARG A 297    12109  17274  10335    120    342   -389       C  
ATOM   2474  NH1 ARG A 297       9.014   4.614 -86.592  1.00105.07           N  
ANISOU 2474  NH1 ARG A 297    12155  17469  10295    198    365   -313       N  
ATOM   2475  NH2 ARG A 297       9.245   2.644 -85.445  1.00100.81           N  
ANISOU 2475  NH2 ARG A 297    11645  16734   9922    -34    342   -546       N  
ATOM   2476  N   LYS A 298       2.304   5.727 -82.127  1.00110.33           N  
ANISOU 2476  N   LYS A 298    12501  18652  10764    445    166    -58       N  
ATOM   2477  CA  LYS A 298       0.914   5.626 -82.585  1.00112.39           C  
ANISOU 2477  CA  LYS A 298    12614  19243  10846    453    129    -53       C  
ATOM   2478  C   LYS A 298      -0.080   6.258 -81.602  1.00111.70           C  
ANISOU 2478  C   LYS A 298    12498  19184  10757    555    110     40       C  
ATOM   2479  O   LYS A 298       0.226   6.437 -80.418  1.00108.49           O  
ANISOU 2479  O   LYS A 298    12183  18538  10498    569    119     57       O  
ATOM   2480  CB  LYS A 298       0.539   4.158 -82.838  1.00114.36           C  
ANISOU 2480  CB  LYS A 298    12787  19612  11049    252    102   -239       C  
ATOM   2481  CG  LYS A 298       1.332   3.477 -83.949  1.00117.01           C  
ANISOU 2481  CG  LYS A 298    13128  19973  11356    145    121   -341       C  
ATOM   2482  CD  LYS A 298       1.061   1.976 -84.002  1.00119.12           C  
ANISOU 2482  CD  LYS A 298    13346  20300  11611    -65    109   -536       C  
ATOM   2483  CE  LYS A 298       1.751   1.232 -82.862  1.00120.04           C  
ANISOU 2483  CE  LYS A 298    13578  20106  11925   -164    123   -625       C  
ATOM   2484  NZ  LYS A 298       1.483  -0.235 -82.891  1.00118.77           N  
ANISOU 2484  NZ  LYS A 298    13380  19986  11758   -368    124   -813       N  
ATOM   2485  N   ILE A 299      -1.270   6.582 -82.109  1.00110.86           N  
ANISOU 2485  N   ILE A 299    12260  19382  10478    625     85     98       N  
ATOM   2486  CA  ILE A 299      -2.344   7.185 -81.310  1.00109.42           C  
ANISOU 2486  CA  ILE A 299    12029  19275  10268    729     68    189       C  
ATOM   2487  C   ILE A 299      -3.522   6.205 -81.172  1.00107.48           C  
ANISOU 2487  C   ILE A 299    11651  19256   9929    603     19     72       C  
ATOM   2488  O   ILE A 299      -3.960   5.607 -82.161  1.00109.46           O  
ANISOU 2488  O   ILE A 299    11789  19765  10034    524      0     -3       O  
ATOM   2489  CB  ILE A 299      -2.823   8.521 -81.934  1.00110.53           C  
ANISOU 2489  CB  ILE A 299    12123  19587  10284    945     85    378       C  
ATOM   2490  CG1 ILE A 299      -1.642   9.484 -82.106  1.00110.93           C  
ANISOU 2490  CG1 ILE A 299    12311  19409  10427   1059    144    488       C  
ATOM   2491  CG2 ILE A 299      -3.907   9.167 -81.081  1.00108.88           C  
ANISOU 2491  CG2 ILE A 299    11869  19445  10056   1061     74    475       C  
ATOM   2492  CD1 ILE A 299      -1.765  10.409 -83.299  1.00114.94           C  
ANISOU 2492  CD1 ILE A 299    12776  20108  10788   1214    169    626       C  
ATOM   2493  N   TYR A 300      -4.017   6.041 -79.942  1.00100.25           N  
ANISOU 2493  N   TYR A 300    10750  18244   9096    579      5     53       N  
ATOM   2494  CA  TYR A 300      -5.082   5.073 -79.643  1.00 96.71           C  
ANISOU 2494  CA  TYR A 300    10191  17971   8581    446    -33    -67       C  
ATOM   2495  C   TYR A 300      -6.287   5.708 -78.943  1.00 93.28           C  
ANISOU 2495  C   TYR A 300     9683  17665   8094    556    -53     25       C  
ATOM   2496  O   TYR A 300      -6.145   6.674 -78.193  1.00 88.69           O  
ANISOU 2496  O   TYR A 300     9178  16920   7598    698    -33    152       O  
ATOM   2497  CB  TYR A 300      -4.541   3.935 -78.775  1.00 96.43           C  
ANISOU 2497  CB  TYR A 300    10243  17695   8701    264    -29   -219       C  
ATOM   2498  CG  TYR A 300      -3.653   2.948 -79.497  1.00 96.54           C  
ANISOU 2498  CG  TYR A 300    10293  17649   8739    112    -14   -355       C  
ATOM   2499  CD1 TYR A 300      -2.312   3.241 -79.753  1.00 96.57           C  
ANISOU 2499  CD1 TYR A 300    10417  17430   8845    146     18   -324       C  
ATOM   2500  CD2 TYR A 300      -4.141   1.708 -79.895  1.00 98.00           C  
ANISOU 2500  CD2 TYR A 300    10394  17992   8848    -71    -26   -520       C  
ATOM   2501  CE1 TYR A 300      -1.491   2.333 -80.404  1.00 96.50           C  
ANISOU 2501  CE1 TYR A 300    10439  17363   8861     10     35   -448       C  
ATOM   2502  CE2 TYR A 300      -3.328   0.792 -80.546  1.00 99.09           C  
ANISOU 2502  CE2 TYR A 300    10569  18067   9012   -212     -4   -648       C  
ATOM   2503  CZ  TYR A 300      -2.005   1.110 -80.800  1.00 97.28           C  
ANISOU 2503  CZ  TYR A 300    10456  17618   8884   -166     25   -609       C  
ATOM   2504  OH  TYR A 300      -1.198   0.206 -81.449  1.00 98.87           O  
ANISOU 2504  OH  TYR A 300    10694  17758   9113   -300     50   -735       O  
ATOM   2505  N   LYS A 301      -7.473   5.154 -79.199  1.00 94.00           N  
ANISOU 2505  N   LYS A 301     9622  18050   8041    486    -89    -42       N  
ATOM   2506  CA  LYS A 301      -8.674   5.506 -78.440  1.00 93.62           C  
ANISOU 2506  CA  LYS A 301     9493  18126   7949    554   -110     10       C  
ATOM   2507  C   LYS A 301      -8.898   4.526 -77.300  1.00 88.03           C  
ANISOU 2507  C   LYS A 301     8815  17283   7348    390   -121   -123       C  
ATOM   2508  O   LYS A 301      -8.867   3.306 -77.494  1.00 85.02           O  
ANISOU 2508  O   LYS A 301     8410  16932   6959    194   -128   -290       O  
ATOM   2509  CB  LYS A 301      -9.911   5.553 -79.338  1.00101.07           C  
ANISOU 2509  CB  LYS A 301    10242  19492   8665    585   -144     23       C  
ATOM   2510  CG  LYS A 301     -10.273   6.943 -79.830  1.00105.70           C  
ANISOU 2510  CG  LYS A 301    10783  20227   9149    831   -136    226       C  
ATOM   2511  CD  LYS A 301     -11.573   6.913 -80.612  1.00112.17           C  
ANISOU 2511  CD  LYS A 301    11397  21482   9740    858   -174    233       C  
ATOM   2512  CE  LYS A 301     -11.608   8.020 -81.656  1.00117.02           C  
ANISOU 2512  CE  LYS A 301    11965  22275  10221   1066   -162    406       C  
ATOM   2513  NZ  LYS A 301     -12.752   7.873 -82.602  1.00116.33           N  
ANISOU 2513  NZ  LYS A 301    11668  22637   9894   1077   -203    399       N  
ATOM   2514  N   TRP A 302      -9.108   5.074 -76.107  1.00 83.37           N  
ANISOU 2514  N   TRP A 302     8282  16536   6857    472   -115    -48       N  
ATOM   2515  CA  TRP A 302      -9.354   4.276 -74.923  1.00 80.19           C  
ANISOU 2515  CA  TRP A 302     7914  15996   6557    339   -122   -153       C  
ATOM   2516  C   TRP A 302     -10.822   4.052 -74.766  1.00 80.80           C  
ANISOU 2516  C   TRP A 302     7837  16356   6505    314   -153   -183       C  
ATOM   2517  O   TRP A 302     -11.581   4.988 -74.487  1.00 79.55           O  
ANISOU 2517  O   TRP A 302     7622  16309   6293    471   -160    -57       O  
ATOM   2518  CB  TRP A 302      -8.780   4.957 -73.685  1.00 78.11           C  
ANISOU 2518  CB  TRP A 302     7794  15413   6469    430   -100    -65       C  
ATOM   2519  CG  TRP A 302      -8.892   4.118 -72.435  1.00 76.28           C  
ANISOU 2519  CG  TRP A 302     7614  15014   6354    294   -104   -170       C  
ATOM   2520  CD1 TRP A 302      -9.860   4.204 -71.442  1.00 75.08           C  
ANISOU 2520  CD1 TRP A 302     7420  14900   6204    305   -117   -158       C  
ATOM   2521  CD2 TRP A 302      -8.008   3.025 -72.014  1.00 74.74           C  
ANISOU 2521  CD2 TRP A 302     7524  14581   6291    123    -93   -304       C  
ATOM   2522  NE1 TRP A 302      -9.636   3.267 -70.461  1.00 74.20           N  
ANISOU 2522  NE1 TRP A 302     7382  14596   6212    155   -114   -271       N  
ATOM   2523  CE2 TRP A 302      -8.543   2.527 -70.749  1.00 73.18           C  
ANISOU 2523  CE2 TRP A 302     7343  14296   6165     45    -99   -359       C  
ATOM   2524  CE3 TRP A 302      -6.867   2.433 -72.543  1.00 73.48           C  
ANISOU 2524  CE3 TRP A 302     7444  14280   6195     36    -75   -377       C  
ATOM   2525  CZ2 TRP A 302      -7.948   1.485 -70.057  1.00 73.28           C  
ANISOU 2525  CZ2 TRP A 302     7451  14087   6304   -108    -87   -477       C  
ATOM   2526  CZ3 TRP A 302      -6.274   1.378 -71.837  1.00 72.39           C  
ANISOU 2526  CZ3 TRP A 302     7398  13918   6186   -115    -63   -497       C  
ATOM   2527  CH2 TRP A 302      -6.806   0.914 -70.626  1.00 71.22           C  
ANISOU 2527  CH2 TRP A 302     7266  13689   6102   -184    -69   -543       C  
ATOM   2528  N   ASN A 303     -11.237   2.805 -74.965  1.00 82.24           N  
ANISOU 2528  N   ASN A 303     7948  16662   6634    114   -167   -353       N  
ATOM   2529  CA  ASN A 303     -12.642   2.430 -74.852  1.00 84.51           C  
ANISOU 2529  CA  ASN A 303     8080  17236   6792     56   -194   -410       C  
ATOM   2530  C   ASN A 303     -12.894   1.431 -73.732  1.00 82.99           C  
ANISOU 2530  C   ASN A 303     7927  16904   6699   -114   -189   -542       C  
ATOM   2531  O   ASN A 303     -13.349   0.310 -73.969  1.00 84.76           O  
ANISOU 2531  O   ASN A 303     8081  17260   6861   -303   -191   -702       O  
ATOM   2532  CB  ASN A 303     -13.169   1.901 -76.188  1.00 86.18           C  
ANISOU 2532  CB  ASN A 303     8138  17795   6811    -27   -212   -495       C  
ATOM   2533  CG  ASN A 303     -13.607   3.016 -77.118  1.00 90.17           C  
ANISOU 2533  CG  ASN A 303     8535  18566   7157    171   -230   -341       C  
ATOM   2534  OD1 ASN A 303     -14.364   3.908 -76.722  1.00 92.04           O  
ANISOU 2534  OD1 ASN A 303     8715  18904   7351    330   -241   -214       O  
ATOM   2535  ND2 ASN A 303     -13.132   2.976 -78.361  1.00 90.18           N  
ANISOU 2535  ND2 ASN A 303     8510  18682   7071    167   -228   -349       N  
ATOM   2536  N   HIS A 304     -12.568   1.842 -72.511  1.00 79.89           N  
ANISOU 2536  N   HIS A 304     7653  16240   6460    -51   -177   -477       N  
ATOM   2537  CA  HIS A 304     -12.888   1.063 -71.324  1.00 78.89           C  
ANISOU 2537  CA  HIS A 304     7565  15981   6425   -182   -172   -574       C  
ATOM   2538  C   HIS A 304     -13.143   1.957 -70.155  1.00 74.61           C  
ANISOU 2538  C   HIS A 304     7073  15310   5966    -44   -172   -452       C  
ATOM   2539  O   HIS A 304     -12.313   2.084 -69.258  1.00 71.89           O  
ANISOU 2539  O   HIS A 304     6876  14652   5786    -29   -153   -425       O  
ATOM   2540  CB  HIS A 304     -11.790   0.059 -71.006  1.00 79.94           C  
ANISOU 2540  CB  HIS A 304     7841  15824   6707   -338   -145   -690       C  
ATOM   2541  CG  HIS A 304     -12.148  -0.896 -69.895  1.00 82.90           C  
ANISOU 2541  CG  HIS A 304     8252  16084   7162   -492   -134   -803       C  
ATOM   2542  ND1 HIS A 304     -11.404  -1.023 -68.778  1.00 82.47           N  
ANISOU 2542  ND1 HIS A 304     8347  15702   7282   -503   -116   -795       N  
ATOM   2543  CD2 HIS A 304     -13.231  -1.765 -69.747  1.00 83.94           C  
ANISOU 2543  CD2 HIS A 304     8280  16402   7209   -641   -136   -926       C  
ATOM   2544  CE1 HIS A 304     -11.967  -1.939 -67.969  1.00 81.81           C  
ANISOU 2544  CE1 HIS A 304     8263  15591   7228   -649   -106   -903       C  
ATOM   2545  NE2 HIS A 304     -13.089  -2.385 -68.559  1.00 83.06           N  
ANISOU 2545  NE2 HIS A 304     8268  16059   7229   -735   -116   -985       N  
ATOM   2546  N   GLY A 305     -14.303   2.598 -70.168  1.00 73.92           N  
ANISOU 2546  N   GLY A 305     6856  15472   5759     59   -192   -378       N  
ATOM   2547  CA  GLY A 305     -14.698   3.488 -69.095  1.00 73.15           C  
ANISOU 2547  CA  GLY A 305     6787  15284   5722    196   -188   -262       C  
ATOM   2548  C   GLY A 305     -13.893   4.763 -69.091  1.00 71.92           C  
ANISOU 2548  C   GLY A 305     6732  14953   5638    398   -167    -94       C  
ATOM   2549  O   GLY A 305     -13.431   5.222 -70.133  1.00 72.05           O  
ANISOU 2549  O   GLY A 305     6741  15037   5598    480   -163    -33       O  
ATOM   2550  N   LEU A 306     -13.743   5.341 -67.907  1.00 73.19           N  
ANISOU 2550  N   LEU A 306     6990  14893   5924    473   -150    -22       N  
ATOM   2551  CA  LEU A 306     -12.898   6.504 -67.713  1.00 73.41           C  
ANISOU 2551  CA  LEU A 306     7136  14708   6046    643   -119    121       C  
ATOM   2552  C   LEU A 306     -11.428   6.105 -67.684  1.00 72.23           C  
ANISOU 2552  C   LEU A 306     7140  14268   6037    564   -101     71       C  
ATOM   2553  O   LEU A 306     -11.072   5.034 -67.176  1.00 70.11           O  
ANISOU 2553  O   LEU A 306     6925  13863   5850    395   -107    -57       O  
ATOM   2554  CB  LEU A 306     -13.264   7.202 -66.404  1.00 71.86           C  
ANISOU 2554  CB  LEU A 306     6990  14379   5935    734   -102    199       C  
ATOM   2555  CG  LEU A 306     -14.641   7.847 -66.325  1.00 72.13           C  
ANISOU 2555  CG  LEU A 306     6888  14668   5848    854   -109    279       C  
ATOM   2556  CD1 LEU A 306     -14.983   8.156 -64.878  1.00 71.54           C  
ANISOU 2556  CD1 LEU A 306     6869  14438   5874    878    -95    306       C  
ATOM   2557  CD2 LEU A 306     -14.686   9.110 -67.169  1.00 74.43           C  
ANISOU 2557  CD2 LEU A 306     7147  15077   6056   1072    -88    444       C  
ATOM   2558  N   LEU A 307     -10.582   6.970 -68.237  1.00 73.64           N  
ANISOU 2558  N   LEU A 307     7386  14354   6240    691    -76    174       N  
ATOM   2559  CA  LEU A 307      -9.132   6.811 -68.131  1.00 75.23           C  
ANISOU 2559  CA  LEU A 307     7737  14264   6582    646    -54    149       C  
ATOM   2560  C   LEU A 307      -8.628   7.251 -66.772  1.00 71.91           C  
ANISOU 2560  C   LEU A 307     7446  13552   6322    680    -31    191       C  
ATOM   2561  O   LEU A 307      -8.762   8.416 -66.407  1.00 71.56           O  
ANISOU 2561  O   LEU A 307     7430  13464   6295    838     -4    319       O  
ATOM   2562  CB  LEU A 307      -8.417   7.627 -69.205  1.00 76.87           C  
ANISOU 2562  CB  LEU A 307     7970  14481   6755    768    -30    246       C  
ATOM   2563  CG  LEU A 307      -7.938   6.914 -70.464  1.00 77.92           C  
ANISOU 2563  CG  LEU A 307     8069  14717   6820    676    -41    165       C  
ATOM   2564  CD1 LEU A 307      -7.428   7.943 -71.456  1.00 78.72           C  
ANISOU 2564  CD1 LEU A 307     8186  14852   6872    830    -14    290       C  
ATOM   2565  CD2 LEU A 307      -6.861   5.887 -70.144  1.00 77.00           C  
ANISOU 2565  CD2 LEU A 307     8058  14363   6834    512    -39     38       C  
ATOM   2566  N   GLN A 308      -8.049   6.320 -66.025  1.00 71.74           N  
ANISOU 2566  N   GLN A 308     7506  13334   6416    533    -37     82       N  
ATOM   2567  CA  GLN A 308      -7.277   6.676 -64.840  1.00 74.91           C  
ANISOU 2567  CA  GLN A 308     8045  13438   6978    554    -15    113       C  
ATOM   2568  C   GLN A 308      -6.140   7.612 -65.243  1.00 76.04           C  
ANISOU 2568  C   GLN A 308     8283  13428   7180    666     19    206       C  
ATOM   2569  O   GLN A 308      -5.403   7.329 -66.192  1.00 73.37           O  
ANISOU 2569  O   GLN A 308     7956  13091   6827    634     22    175       O  
ATOM   2570  CB  GLN A 308      -6.719   5.426 -64.164  1.00 74.22           C  
ANISOU 2570  CB  GLN A 308     8026  13178   6994    377    -28    -19       C  
ATOM   2571  CG  GLN A 308      -7.586   4.875 -63.045  1.00 74.93           C  
ANISOU 2571  CG  GLN A 308     8093  13275   7101    299    -43    -74       C  
ATOM   2572  CD  GLN A 308      -7.314   3.408 -62.769  1.00 74.89           C  
ANISOU 2572  CD  GLN A 308     8118  13190   7146    107    -54   -222       C  
ATOM   2573  OE1 GLN A 308      -7.407   2.570 -63.668  1.00 75.12           O  
ANISOU 2573  OE1 GLN A 308     8089  13347   7105      7    -62   -311       O  
ATOM   2574  NE2 GLN A 308      -6.979   3.089 -61.522  1.00 73.39           N  
ANISOU 2574  NE2 GLN A 308     8019  12788   7076     55    -49   -247       N  
ATOM   2575  N   GLY A 309      -6.023   8.737 -64.543  1.00 79.41           N  
ANISOU 2575  N   GLY A 309     8774  13728   7669    796     53    316       N  
ATOM   2576  CA  GLY A 309      -5.004   9.738 -64.864  1.00 84.73           C  
ANISOU 2576  CA  GLY A 309     9540  14254   8397    907     98    409       C  
ATOM   2577  C   GLY A 309      -5.566  11.046 -65.398  1.00 87.30           C  
ANISOU 2577  C   GLY A 309     9825  14709   8636   1096    133    556       C  
ATOM   2578  O   GLY A 309      -4.963  12.107 -65.217  1.00 90.13           O  
ANISOU 2578  O   GLY A 309    10272  14915   9056   1208    186    652       O  
ATOM   2579  N   ASP A 310      -6.712  10.972 -66.070  1.00 86.61           N  
ANISOU 2579  N   ASP A 310     9602  14906   8401   1132    110    573       N  
ATOM   2580  CA  ASP A 310      -7.428  12.172 -66.496  1.00 89.71           C  
ANISOU 2580  CA  ASP A 310     9940  15445   8698   1322    142    719       C  
ATOM   2581  C   ASP A 310      -7.981  12.897 -65.262  1.00 90.63           C  
ANISOU 2581  C   ASP A 310    10089  15472   8874   1404    170    786       C  
ATOM   2582  O   ASP A 310      -8.651  12.284 -64.429  1.00 90.16           O  
ANISOU 2582  O   ASP A 310     9990  15440   8826   1320    137    717       O  
ATOM   2583  CB  ASP A 310      -8.558  11.813 -67.473  1.00 89.17           C  
ANISOU 2583  CB  ASP A 310     9704  15724   8449   1330    103    712       C  
ATOM   2584  CG  ASP A 310      -9.112  13.026 -68.213  1.00 89.87           C  
ANISOU 2584  CG  ASP A 310     9738  15982   8426   1539    139    872       C  
ATOM   2585  OD1 ASP A 310      -9.424  14.044 -67.565  1.00 92.21           O  
ANISOU 2585  OD1 ASP A 310    10072  16208   8756   1678    183    983       O  
ATOM   2586  OD2 ASP A 310      -9.264  12.949 -69.448  1.00 92.02           O  
ANISOU 2586  OD2 ASP A 310     9927  16463   8571   1566    125    888       O  
ATOM   2587  N   PRO A 311      -7.677  14.201 -65.134  1.00 93.30           N  
ANISOU 2587  N   PRO A 311    10504  15694   9251   1564    236    918       N  
ATOM   2588  CA  PRO A 311      -8.093  15.043 -64.002  1.00 94.14           C  
ANISOU 2588  CA  PRO A 311    10656  15692   9419   1656    278    991       C  
ATOM   2589  C   PRO A 311      -9.574  14.925 -63.601  1.00 94.92           C  
ANISOU 2589  C   PRO A 311    10632  16002   9430   1684    250    998       C  
ATOM   2590  O   PRO A 311      -9.907  15.109 -62.428  1.00 95.30           O  
ANISOU 2590  O   PRO A 311    10713  15949   9548   1682    263    997       O  
ATOM   2591  CB  PRO A 311      -7.788  16.476 -64.493  1.00 95.60           C  
ANISOU 2591  CB  PRO A 311    10900  15826   9595   1850    360   1146       C  
ATOM   2592  CG  PRO A 311      -7.276  16.343 -65.902  1.00 95.49           C  
ANISOU 2592  CG  PRO A 311    10862  15912   9505   1858    354   1156       C  
ATOM   2593  CD  PRO A 311      -6.789  14.937 -66.047  1.00 94.12           C  
ANISOU 2593  CD  PRO A 311    10673  15735   9354   1656    285    998       C  
ATOM   2594  N   LEU A 312     -10.446  14.622 -64.560  1.00 95.26           N  
ANISOU 2594  N   LEU A 312    10531  16343   9319   1706    214   1003       N  
ATOM   2595  CA  LEU A 312     -11.885  14.580 -64.297  1.00 92.67           C  
ANISOU 2595  CA  LEU A 312    10071  16246   8891   1745    189   1017       C  
ATOM   2596  C   LEU A 312     -12.397  13.211 -63.853  1.00 88.92           C  
ANISOU 2596  C   LEU A 312     9523  15856   8405   1550    121    861       C  
ATOM   2597  O   LEU A 312     -13.483  13.106 -63.282  1.00 88.14           O  
ANISOU 2597  O   LEU A 312     9340  15886   8261   1552    105    852       O  
ATOM   2598  CB  LEU A 312     -12.671  15.065 -65.515  1.00 96.63           C  
ANISOU 2598  CB  LEU A 312    10442  17051   9220   1886    190   1115       C  
ATOM   2599  CG  LEU A 312     -12.766  16.580 -65.718  1.00100.18           C  
ANISOU 2599  CG  LEU A 312    10929  17480   9652   2124    267   1300       C  
ATOM   2600  CD1 LEU A 312     -13.584  16.893 -66.961  1.00102.80           C  
ANISOU 2600  CD1 LEU A 312    11117  18143   9799   2254    257   1388       C  
ATOM   2601  CD2 LEU A 312     -13.362  17.270 -64.497  1.00101.46           C  
ANISOU 2601  CD2 LEU A 312    11121  17549   9877   2209    308   1359       C  
ATOM   2602  N   SER A 313     -11.614  12.170 -64.110  1.00 84.85           N  
ANISOU 2602  N   SER A 313     9043  15264   7931   1383     88    739       N  
ATOM   2603  CA  SER A 313     -12.042  10.804 -63.833  1.00 82.90           C  
ANISOU 2603  CA  SER A 313     8733  15097   7667   1190     32    586       C  
ATOM   2604  C   SER A 313     -12.534  10.604 -62.399  1.00 81.17           C  
ANISOU 2604  C   SER A 313     8538  14775   7525   1137     30    548       C  
ATOM   2605  O   SER A 313     -13.636  10.103 -62.187  1.00 81.89           O  
ANISOU 2605  O   SER A 313     8518  15056   7540   1084      0    498       O  
ATOM   2606  CB  SER A 313     -10.934   9.807 -64.175  1.00 80.52           C  
ANISOU 2606  CB  SER A 313     8501  14661   7430   1030     14    470       C  
ATOM   2607  OG  SER A 313     -10.804   9.671 -65.580  1.00 82.76           O  
ANISOU 2607  OG  SER A 313     8718  15120   7606   1040      2    469       O  
ATOM   2608  N   GLY A 314     -11.728  11.027 -61.426  1.00 79.47           N  
ANISOU 2608  N   GLY A 314     8465  14271   7458   1151     63    573       N  
ATOM   2609  CA  GLY A 314     -12.044  10.839 -60.008  1.00 76.62           C  
ANISOU 2609  CA  GLY A 314     8145  13785   7182   1095     63    536       C  
ATOM   2610  C   GLY A 314     -13.432  11.313 -59.618  1.00 77.31           C  
ANISOU 2610  C   GLY A 314     8127  14058   7188   1183     67    592       C  
ATOM   2611  O   GLY A 314     -14.226  10.548 -59.070  1.00 78.26           O  
ANISOU 2611  O   GLY A 314     8181  14269   7283   1078     35    508       O  
ATOM   2612  N   CYS A 315     -13.724  12.578 -59.914  1.00 77.69           N  
ANISOU 2612  N   CYS A 315     8161  14162   7194   1378    110    734       N  
ATOM   2613  CA  CYS A 315     -14.993  13.203 -59.533  1.00 78.66           C  
ANISOU 2613  CA  CYS A 315     8193  14448   7247   1494    124    807       C  
ATOM   2614  C   CYS A 315     -16.174  12.687 -60.358  1.00 80.07           C  
ANISOU 2614  C   CYS A 315     8184  14981   7254   1480     79    778       C  
ATOM   2615  O   CYS A 315     -17.314  12.686 -59.889  1.00 80.79           O  
ANISOU 2615  O   CYS A 315     8180  15229   7288   1498     69    778       O  
ATOM   2616  CB  CYS A 315     -14.900  14.720 -59.679  1.00 80.37           C  
ANISOU 2616  CB  CYS A 315     8456  14611   7469   1716    195    974       C  
ATOM   2617  SG  CYS A 315     -14.852  15.291 -61.397  1.00 82.99           S  
ANISOU 2617  SG  CYS A 315     8717  15148   7666   1860    206   1077       S  
ATOM   2618  N   LEU A 316     -15.901  12.282 -61.595  1.00 77.65           N  
ANISOU 2618  N   LEU A 316     7826  14812   6864   1450     52    752       N  
ATOM   2619  CA  LEU A 316     -16.934  11.725 -62.449  1.00 78.76           C  
ANISOU 2619  CA  LEU A 316     7788  15300   6837   1418      7    710       C  
ATOM   2620  C   LEU A 316     -17.248  10.290 -62.056  1.00 79.00           C  
ANISOU 2620  C   LEU A 316     7774  15373   6868   1189    -40    535       C  
ATOM   2621  O   LEU A 316     -18.398   9.855 -62.143  1.00 81.89           O  
ANISOU 2621  O   LEU A 316     7994  15997   7120   1147    -69    488       O  
ATOM   2622  CB  LEU A 316     -16.538  11.816 -63.923  1.00 78.89           C  
ANISOU 2622  CB  LEU A 316     7763  15455   6757   1465      0    743       C  
ATOM   2623  CG  LEU A 316     -16.550  13.219 -64.538  1.00 79.42           C  
ANISOU 2623  CG  LEU A 316     7831  15572   6773   1708     48    926       C  
ATOM   2624  CD1 LEU A 316     -16.062  13.172 -65.974  1.00 79.39           C  
ANISOU 2624  CD1 LEU A 316     7794  15689   6679   1729     38    944       C  
ATOM   2625  CD2 LEU A 316     -17.927  13.857 -64.464  1.00 80.83           C  
ANISOU 2625  CD2 LEU A 316     7873  16002   6836   1855     54   1018       C  
ATOM   2626  N   CYS A 317     -16.229   9.564 -61.604  1.00 76.87           N  
ANISOU 2626  N   CYS A 317     7630  14850   6726   1043    -43    441       N  
ATOM   2627  CA  CYS A 317     -16.421   8.211 -61.096  1.00 75.84           C  
ANISOU 2627  CA  CYS A 317     7486  14709   6619    827    -75    280       C  
ATOM   2628  C   CYS A 317     -17.244   8.214 -59.809  1.00 76.18           C  
ANISOU 2628  C   CYS A 317     7518  14728   6697    810    -71    269       C  
ATOM   2629  O   CYS A 317     -18.090   7.346 -59.611  1.00 77.04           O  
ANISOU 2629  O   CYS A 317     7535  14989   6747    683    -96    166       O  
ATOM   2630  CB  CYS A 317     -15.082   7.514 -60.870  1.00 73.08           C  
ANISOU 2630  CB  CYS A 317     7284  14077   6404    698    -73    200       C  
ATOM   2631  SG  CYS A 317     -15.223   5.773 -60.402  1.00 70.80           S  
ANISOU 2631  SG  CYS A 317     6990  13768   6141    432   -101      3       S  
ATOM   2632  N   GLU A 318     -17.002   9.198 -58.945  1.00 75.93           N  
ANISOU 2632  N   GLU A 318     7580  14508   6760    933    -34    370       N  
ATOM   2633  CA  GLU A 318     -17.803   9.375 -57.731  1.00 76.59           C  
ANISOU 2633  CA  GLU A 318     7653  14573   6874    942    -24    376       C  
ATOM   2634  C   GLU A 318     -19.249   9.725 -58.079  1.00 76.59           C  
ANISOU 2634  C   GLU A 318     7477  14899   6723   1032    -33    420       C  
ATOM   2635  O   GLU A 318     -20.189   9.199 -57.484  1.00 77.59           O  
ANISOU 2635  O   GLU A 318     7526  15138   6814    950    -49    352       O  
ATOM   2636  CB  GLU A 318     -17.203  10.467 -56.843  1.00 79.54           C  
ANISOU 2636  CB  GLU A 318     8162  14686   7373   1067     25    482       C  
ATOM   2637  CG  GLU A 318     -15.936  10.058 -56.106  1.00 84.39           C  
ANISOU 2637  CG  GLU A 318     8942  14977   8144    961     31    425       C  
ATOM   2638  CD  GLU A 318     -15.564  11.032 -54.998  1.00 86.75           C  
ANISOU 2638  CD  GLU A 318     9357  15043   8558   1056     79    506       C  
ATOM   2639  OE1 GLU A 318     -14.420  11.541 -55.016  1.00 87.59           O  
ANISOU 2639  OE1 GLU A 318     9584  14938   8755   1100    107    550       O  
ATOM   2640  OE2 GLU A 318     -16.416  11.293 -54.116  1.00 86.62           O  
ANISOU 2640  OE2 GLU A 318     9310  15060   8540   1084     91    523       O  
ATOM   2641  N   LEU A 319     -19.405  10.626 -59.045  1.00 75.42           N  
ANISOU 2641  N   LEU A 319     7269  14903   6485   1205    -19    537       N  
ATOM   2642  CA  LEU A 319     -20.710  11.037 -59.549  1.00 75.05           C  
ANISOU 2642  CA  LEU A 319     7047  15188   6280   1316    -28    596       C  
ATOM   2643  C   LEU A 319     -21.482   9.833 -60.083  1.00 73.58           C  
ANISOU 2643  C   LEU A 319     6710  15276   5970   1151    -81    459       C  
ATOM   2644  O   LEU A 319     -22.619   9.589 -59.681  1.00 75.34           O  
ANISOU 2644  O   LEU A 319     6815  15685   6122   1121    -95    422       O  
ATOM   2645  CB  LEU A 319     -20.522  12.091 -60.648  1.00 76.92           C  
ANISOU 2645  CB  LEU A 319     7259  15523   6443   1520     -4    742       C  
ATOM   2646  CG  LEU A 319     -21.681  12.977 -61.114  1.00 78.01           C  
ANISOU 2646  CG  LEU A 319     7249  15951   6437   1717      6    867       C  
ATOM   2647  CD1 LEU A 319     -22.332  12.402 -62.360  1.00 79.05           C  
ANISOU 2647  CD1 LEU A 319     7202  16444   6387   1680    -43    822       C  
ATOM   2648  CD2 LEU A 319     -22.699  13.218 -60.008  1.00 79.03           C  
ANISOU 2648  CD2 LEU A 319     7331  16118   6576   1751     20    879       C  
ATOM   2649  N   TYR A 320     -20.844   9.082 -60.977  1.00 70.35           N  
ANISOU 2649  N   TYR A 320     6305  14886   5536   1038   -106    379       N  
ATOM   2650  CA  TYR A 320     -21.393   7.840 -61.508  1.00 70.62           C  
ANISOU 2650  CA  TYR A 320     6219  15145   5467    852   -148    229       C  
ATOM   2651  C   TYR A 320     -21.742   6.823 -60.408  1.00 72.47           C  
ANISOU 2651  C   TYR A 320     6474  15295   5766    658   -155     91       C  
ATOM   2652  O   TYR A 320     -22.855   6.278 -60.391  1.00 72.20           O  
ANISOU 2652  O   TYR A 320     6299  15505   5627    576   -174     15       O  
ATOM   2653  CB  TYR A 320     -20.413   7.241 -62.509  1.00 68.76           C  
ANISOU 2653  CB  TYR A 320     6028  14866   5231    760   -161    166       C  
ATOM   2654  CG  TYR A 320     -20.833   5.929 -63.133  1.00 70.35           C  
ANISOU 2654  CG  TYR A 320     6122  15274   5333    555   -194      1       C  
ATOM   2655  CD1 TYR A 320     -21.668   5.896 -64.255  1.00 70.98           C  
ANISOU 2655  CD1 TYR A 320     6020  15724   5224    579   -220     -3       C  
ATOM   2656  CD2 TYR A 320     -20.353   4.718 -62.634  1.00 69.79           C  
ANISOU 2656  CD2 TYR A 320     6135  15026   5354    337   -193   -149       C  
ATOM   2657  CE1 TYR A 320     -22.031   4.692 -64.842  1.00 71.82           C  
ANISOU 2657  CE1 TYR A 320     6029  16021   5237    379   -243   -164       C  
ATOM   2658  CE2 TYR A 320     -20.709   3.511 -63.211  1.00 70.39           C  
ANISOU 2658  CE2 TYR A 320     6124  15276   5345    143   -211   -306       C  
ATOM   2659  CZ  TYR A 320     -21.546   3.501 -64.313  1.00 72.10           C  
ANISOU 2659  CZ  TYR A 320     6158  15860   5374    159   -235   -318       C  
ATOM   2660  OH  TYR A 320     -21.887   2.297 -64.878  1.00 72.39           O  
ANISOU 2660  OH  TYR A 320     6110  16068   5324    -46   -246   -483       O  
ATOM   2661  N   MET A 321     -20.801   6.587 -59.489  1.00 71.07           N  
ANISOU 2661  N   MET A 321     6469  14777   5756    589   -136     63       N  
ATOM   2662  CA  MET A 321     -20.956   5.556 -58.452  1.00 70.66           C  
ANISOU 2662  CA  MET A 321     6460  14609   5777    400   -138    -65       C  
ATOM   2663  C   MET A 321     -22.067   5.882 -57.452  1.00 70.56           C  
ANISOU 2663  C   MET A 321     6386  14674   5749    438   -130    -42       C  
ATOM   2664  O   MET A 321     -22.689   4.977 -56.890  1.00 70.60           O  
ANISOU 2664  O   MET A 321     6351  14729   5743    281   -137   -157       O  
ATOM   2665  CB  MET A 321     -19.632   5.320 -57.706  1.00 73.28           C  
ANISOU 2665  CB  MET A 321     6992  14562   6289    340   -120    -83       C  
ATOM   2666  CG  MET A 321     -18.531   4.668 -58.536  1.00 75.01           C  
ANISOU 2666  CG  MET A 321     7277  14684   6537    250   -127   -145       C  
ATOM   2667  SD  MET A 321     -18.838   2.924 -58.878  1.00 78.94           S  
ANISOU 2667  SD  MET A 321     7717  15293   6982    -15   -143   -347       S  
ATOM   2668  CE  MET A 321     -18.264   2.191 -57.347  1.00 75.73           C  
ANISOU 2668  CE  MET A 321     7475  14549   6750   -147   -122   -417       C  
ATOM   2669  N   ALA A 322     -22.299   7.171 -57.215  1.00 69.14           N  
ANISOU 2669  N   ALA A 322     6204  14494   5572    646   -109    106       N  
ATOM   2670  CA  ALA A 322     -23.400   7.604 -56.359  1.00 70.17           C  
ANISOU 2670  CA  ALA A 322     6263  14720   5676    708    -98    141       C  
ATOM   2671  C   ALA A 322     -24.738   7.287 -57.028  1.00 73.30           C  
ANISOU 2671  C   ALA A 322     6446  15510   5891    687   -125     98       C  
ATOM   2672  O   ALA A 322     -25.708   6.927 -56.359  1.00 73.25           O  
ANISOU 2672  O   ALA A 322     6363  15615   5853    618   -128     39       O  
ATOM   2673  CB  ALA A 322     -23.291   9.090 -56.065  1.00 70.95           C  
ANISOU 2673  CB  ALA A 322     6412  14726   5816    943    -59    313       C  
ATOM   2674  N   PHE A 323     -24.769   7.419 -58.354  1.00 73.18           N  
ANISOU 2674  N   PHE A 323     6336  15710   5757    745   -145    126       N  
ATOM   2675  CA  PHE A 323     -25.950   7.122 -59.138  1.00 78.40           C  
ANISOU 2675  CA  PHE A 323     6786  16769   6233    726   -174     84       C  
ATOM   2676  C   PHE A 323     -26.271   5.630 -59.116  1.00 79.60           C  
ANISOU 2676  C   PHE A 323     6887  17006   6351    461   -196   -112       C  
ATOM   2677  O   PHE A 323     -27.442   5.249 -58.991  1.00 81.13           O  
ANISOU 2677  O   PHE A 323     6932  17452   6441    395   -208   -178       O  
ATOM   2678  CB  PHE A 323     -25.771   7.621 -60.579  1.00 81.13           C  
ANISOU 2678  CB  PHE A 323     7056  17307   6463    851   -189    164       C  
ATOM   2679  CG  PHE A 323     -26.944   7.343 -61.478  1.00 81.87           C  
ANISOU 2679  CG  PHE A 323     6921  17832   6351    838   -223    125       C  
ATOM   2680  CD1 PHE A 323     -28.204   7.859 -61.187  1.00 83.85           C  
ANISOU 2680  CD1 PHE A 323     7027  18326   6505    945   -224    181       C  
ATOM   2681  CD2 PHE A 323     -26.782   6.590 -62.633  1.00 83.50           C  
ANISOU 2681  CD2 PHE A 323     7055  18213   6456    723   -252     33       C  
ATOM   2682  CE1 PHE A 323     -29.282   7.611 -62.021  1.00 86.05           C  
ANISOU 2682  CE1 PHE A 323     7085  19022   6587    935   -257    144       C  
ATOM   2683  CE2 PHE A 323     -27.854   6.344 -63.477  1.00 86.04           C  
ANISOU 2683  CE2 PHE A 323     7161  18950   6580    707   -284     -7       C  
ATOM   2684  CZ  PHE A 323     -29.107   6.854 -63.170  1.00 87.42           C  
ANISOU 2684  CZ  PHE A 323     7185  19373   6657    813   -288     48       C  
ATOM   2685  N   MET A 324     -25.238   4.793 -59.232  1.00 77.79           N  
ANISOU 2685  N   MET A 324     6779  16566   6209    308   -195   -205       N  
ATOM   2686  CA  MET A 324     -25.414   3.341 -59.150  1.00 78.84           C  
ANISOU 2686  CA  MET A 324     6895  16729   6332     49   -201   -394       C  
ATOM   2687  C   MET A 324     -25.967   2.964 -57.777  1.00 79.56           C  
ANISOU 2687  C   MET A 324     7016  16718   6492    -42   -184   -451       C  
ATOM   2688  O   MET A 324     -26.743   2.011 -57.646  1.00 81.86           O  
ANISOU 2688  O   MET A 324     7221  17160   6720   -217   -185   -586       O  
ATOM   2689  CB  MET A 324     -24.095   2.604 -59.393  1.00 76.16           C  
ANISOU 2689  CB  MET A 324     6706  16132   6098    -73   -194   -465       C  
ATOM   2690  CG  MET A 324     -23.455   2.843 -60.747  1.00 77.23           C  
ANISOU 2690  CG  MET A 324     6824  16346   6172     -9   -208   -427       C  
ATOM   2691  SD  MET A 324     -24.139   1.836 -62.076  1.00 78.53           S  
ANISOU 2691  SD  MET A 324     6806  16884   6147   -170   -231   -573       S  
ATOM   2692  CE  MET A 324     -25.170   3.042 -62.906  1.00 81.75           C  
ANISOU 2692  CE  MET A 324     7014  17677   6369     58   -258   -431       C  
ATOM   2693  N   ASP A 325     -25.577   3.735 -56.765  1.00 77.18           N  
ANISOU 2693  N   ASP A 325     6838  16168   6318     73   -164   -348       N  
ATOM   2694  CA  ASP A 325     -26.012   3.503 -55.396  1.00 80.18           C  
ANISOU 2694  CA  ASP A 325     7262  16426   6774      6   -145   -385       C  
ATOM   2695  C   ASP A 325     -27.515   3.778 -55.197  1.00 80.74           C  
ANISOU 2695  C   ASP A 325     7155  16798   6721     48   -150   -379       C  
ATOM   2696  O   ASP A 325     -28.224   2.989 -54.564  1.00 79.43           O  
ANISOU 2696  O   ASP A 325     6948  16689   6542   -105   -143   -490       O  
ATOM   2697  CB  ASP A 325     -25.174   4.351 -54.437  1.00 81.33           C  
ANISOU 2697  CB  ASP A 325     7580  16243   7078    130   -121   -271       C  
ATOM   2698  CG  ASP A 325     -25.399   3.986 -52.994  1.00 85.45           C  
ANISOU 2698  CG  ASP A 325     8176  16595   7695     38   -101   -320       C  
ATOM   2699  OD1 ASP A 325     -26.449   4.372 -52.438  1.00 88.42           O  
ANISOU 2699  OD1 ASP A 325     8463  17109   8023     89    -94   -294       O  
ATOM   2700  OD2 ASP A 325     -24.518   3.326 -52.407  1.00 91.06           O  
ANISOU 2700  OD2 ASP A 325     9035  17035   8528    -79    -91   -379       O  
ATOM   2701  N   ARG A 326     -27.989   4.899 -55.729  1.00 80.81           N  
ANISOU 2701  N   ARG A 326     7063  16998   6643    260   -157   -246       N  
ATOM   2702  CA  ARG A 326     -29.408   5.246 -55.659  1.00 82.67           C  
ANISOU 2702  CA  ARG A 326     7115  17545   6750    326   -162   -226       C  
ATOM   2703  C   ARG A 326     -30.228   4.252 -56.487  1.00 81.90           C  
ANISOU 2703  C   ARG A 326     6840  17783   6493    163   -190   -366       C  
ATOM   2704  O   ARG A 326     -31.339   3.889 -56.117  1.00 81.20           O  
ANISOU 2704  O   ARG A 326     6626  17897   6326     87   -191   -437       O  
ATOM   2705  CB  ARG A 326     -29.617   6.671 -56.169  1.00 84.81           C  
ANISOU 2705  CB  ARG A 326     7325  17937   6961    603   -159    -42       C  
ATOM   2706  CG  ARG A 326     -30.923   7.322 -55.744  1.00 88.56           C  
ANISOU 2706  CG  ARG A 326     7657  18640   7352    725   -151     20       C  
ATOM   2707  CD  ARG A 326     -30.803   8.843 -55.738  1.00 90.86           C  
ANISOU 2707  CD  ARG A 326     7980  18877   7666   1010   -122    221       C  
ATOM   2708  NE  ARG A 326     -30.084   9.352 -56.908  1.00 90.51           N  
ANISOU 2708  NE  ARG A 326     7953  18850   7586   1131   -129    311       N  
ATOM   2709  CZ  ARG A 326     -30.654   9.960 -57.946  1.00 93.61           C  
ANISOU 2709  CZ  ARG A 326     8195  19543   7827   1291   -141    404       C  
ATOM   2710  NH1 ARG A 326     -31.971  10.156 -57.974  1.00 94.43           N  
ANISOU 2710  NH1 ARG A 326     8110  19969   7798   1357   -150    420       N  
ATOM   2711  NH2 ARG A 326     -29.901  10.377 -58.960  1.00 91.87           N  
ANISOU 2711  NH2 ARG A 326     8011  19308   7587   1390   -143    482       N  
ATOM   2712  N   LEU A 327     -29.630   3.796 -57.586  1.00 82.69           N  
ANISOU 2712  N   LEU A 327     6937  17930   6548    101   -208   -412       N  
ATOM   2713  CA  LEU A 327     -30.241   2.854 -58.524  1.00 82.73           C  
ANISOU 2713  CA  LEU A 327     6785  18245   6401    -59   -230   -550       C  
ATOM   2714  C   LEU A 327     -30.458   1.458 -57.927  1.00 83.06           C  
ANISOU 2714  C   LEU A 327     6852  18229   6476   -338   -213   -744       C  
ATOM   2715  O   LEU A 327     -31.570   0.933 -57.957  1.00 84.14           O  
ANISOU 2715  O   LEU A 327     6833  18639   6496   -448   -216   -844       O  
ATOM   2716  CB  LEU A 327     -29.355   2.746 -59.767  1.00 81.79           C  
ANISOU 2716  CB  LEU A 327     6692  18131   6253    -55   -246   -547       C  
ATOM   2717  CG  LEU A 327     -29.963   2.545 -61.152  1.00 82.30           C  
ANISOU 2717  CG  LEU A 327     6559  18593   6116    -71   -277   -589       C  
ATOM   2718  CD1 LEU A 327     -31.095   3.530 -61.423  1.00 83.28           C  
ANISOU 2718  CD1 LEU A 327     6496  19052   6094    127   -296   -471       C  
ATOM   2719  CD2 LEU A 327     -28.866   2.681 -62.193  1.00 79.52           C  
ANISOU 2719  CD2 LEU A 327     6279  18159   5775    -25   -286   -548       C  
ATOM   2720  N   TYR A 328     -29.392   0.871 -57.376  1.00 82.91           N  
ANISOU 2720  N   TYR A 328     7030  17855   6617   -449   -190   -794       N  
ATOM   2721  CA  TYR A 328     -29.407  -0.538 -56.966  1.00 80.30           C  
ANISOU 2721  CA  TYR A 328     6745  17440   6323   -717   -165   -977       C  
ATOM   2722  C   TYR A 328     -29.315  -0.783 -55.454  1.00 80.21           C  
ANISOU 2722  C   TYR A 328     6870  17148   6456   -780   -134   -994       C  
ATOM   2723  O   TYR A 328     -29.543  -1.905 -54.989  1.00 78.85           O  
ANISOU 2723  O   TYR A 328     6723  16931   6304   -995   -106  -1139       O  
ATOM   2724  CB  TYR A 328     -28.299  -1.311 -57.675  1.00 78.03           C  
ANISOU 2724  CB  TYR A 328     6562  17002   6084   -836   -158  -1053       C  
ATOM   2725  CG  TYR A 328     -28.295  -1.179 -59.180  1.00 76.72           C  
ANISOU 2725  CG  TYR A 328     6274  17095   5778   -796   -186  -1050       C  
ATOM   2726  CD1 TYR A 328     -29.345  -1.688 -59.956  1.00 76.39           C  
ANISOU 2726  CD1 TYR A 328     6033  17434   5556   -901   -197  -1157       C  
ATOM   2727  CD2 TYR A 328     -27.228  -0.573 -59.831  1.00 74.04           C  
ANISOU 2727  CD2 TYR A 328     6020  16625   5484   -662   -199   -946       C  
ATOM   2728  CE1 TYR A 328     -29.333  -1.578 -61.337  1.00 75.71           C  
ANISOU 2728  CE1 TYR A 328     5833  17596   5335   -868   -224  -1156       C  
ATOM   2729  CE2 TYR A 328     -27.203  -0.460 -61.210  1.00 75.17           C  
ANISOU 2729  CE2 TYR A 328     6057  17005   5499   -626   -223   -942       C  
ATOM   2730  CZ  TYR A 328     -28.257  -0.962 -61.960  1.00 77.05           C  
ANISOU 2730  CZ  TYR A 328     6096  17624   5555   -727   -237  -1045       C  
ATOM   2731  OH  TYR A 328     -28.217  -0.844 -63.332  1.00 77.42           O  
ANISOU 2731  OH  TYR A 328     6035  17913   5468   -692   -262  -1040       O  
ATOM   2732  N   PHE A 329     -28.977   0.256 -54.695  1.00 81.37           N  
ANISOU 2732  N   PHE A 329     7108  17106   6701   -598   -133   -848       N  
ATOM   2733  CA  PHE A 329     -28.869   0.133 -53.245  1.00 83.24           C  
ANISOU 2733  CA  PHE A 329     7472  17082   7071   -640   -105   -851       C  
ATOM   2734  C   PHE A 329     -29.897   1.027 -52.570  1.00 90.08           C  
ANISOU 2734  C   PHE A 329     8245  18082   7898   -505   -105   -765       C  
ATOM   2735  O   PHE A 329     -29.553   1.992 -51.872  1.00 94.02           O  
ANISOU 2735  O   PHE A 329     8834  18401   8489   -343    -97   -638       O  
ATOM   2736  CB  PHE A 329     -27.446   0.454 -52.774  1.00 80.64           C  
ANISOU 2736  CB  PHE A 329     7356  16368   6913   -574    -96   -772       C  
ATOM   2737  CG  PHE A 329     -26.403  -0.460 -53.348  1.00 77.87           C  
ANISOU 2737  CG  PHE A 329     7105  15868   6613   -707    -92   -856       C  
ATOM   2738  CD1 PHE A 329     -26.155  -1.700 -52.774  1.00 77.05           C  
ANISOU 2738  CD1 PHE A 329     7094  15601   6579   -918    -63   -988       C  
ATOM   2739  CD2 PHE A 329     -25.685  -0.092 -54.476  1.00 77.09           C  
ANISOU 2739  CD2 PHE A 329     7006  15794   6488   -619   -112   -804       C  
ATOM   2740  CE1 PHE A 329     -25.209  -2.553 -53.313  1.00 74.95           C  
ANISOU 2740  CE1 PHE A 329     6919  15198   6359  -1036    -53  -1065       C  
ATOM   2741  CE2 PHE A 329     -24.738  -0.939 -55.019  1.00 76.17           C  
ANISOU 2741  CE2 PHE A 329     6978  15545   6417   -742   -105   -885       C  
ATOM   2742  CZ  PHE A 329     -24.500  -2.170 -54.437  1.00 75.27           C  
ANISOU 2742  CZ  PHE A 329     6954  15267   6375   -948    -75  -1015       C  
ATOM   2743  N   SER A 330     -31.166   0.680 -52.781  1.00 93.27           N  
ANISOU 2743  N   SER A 330     8468  18808   8163   -578   -109   -843       N  
ATOM   2744  CA  SER A 330     -32.293   1.489 -52.334  1.00 95.09           C  
ANISOU 2744  CA  SER A 330     8571  19234   8324   -448   -111   -771       C  
ATOM   2745  C   SER A 330     -33.093   0.813 -51.224  1.00 95.65           C  
ANISOU 2745  C   SER A 330     8629  19301   8411   -604    -84   -875       C  
ATOM   2746  O   SER A 330     -33.720   1.491 -50.406  1.00 97.45           O  
ANISOU 2746  O   SER A 330     8828  19547   8650   -501    -74   -805       O  
ATOM   2747  CB  SER A 330     -33.211   1.824 -53.519  1.00 98.14           C  
ANISOU 2747  CB  SER A 330     8729  20040   8517   -369   -141   -755       C  
ATOM   2748  OG  SER A 330     -33.383   0.704 -54.375  1.00 98.02           O  
ANISOU 2748  OG  SER A 330     8631  20207   8405   -570   -150   -910       O  
ATOM   2749  N   ASN A 331     -33.068  -0.519 -51.197  1.00 96.85           N  
ANISOU 2749  N   ASN A 331     8806  19426   8565   -852    -66  -1041       N  
ATOM   2750  CA  ASN A 331     -33.833  -1.288 -50.208  1.00100.25           C  
ANISOU 2750  CA  ASN A 331     9226  19859   9004  -1025    -33  -1154       C  
ATOM   2751  C   ASN A 331     -32.971  -1.947 -49.138  1.00100.12           C  
ANISOU 2751  C   ASN A 331     9429  19455   9157  -1145      1  -1195       C  
ATOM   2752  O   ASN A 331     -33.309  -3.022 -48.629  1.00100.56           O  
ANISOU 2752  O   ASN A 331     9505  19481   9221  -1356     36  -1331       O  
ATOM   2753  CB  ASN A 331     -34.702  -2.332 -50.904  1.00102.31           C  
ANISOU 2753  CB  ASN A 331     9328  20422   9121  -1230    -27  -1324       C  
ATOM   2754  CG  ASN A 331     -35.651  -1.715 -51.902  1.00103.08           C  
ANISOU 2754  CG  ASN A 331     9192  20935   9037  -1116    -63  -1288       C  
ATOM   2755  OD1 ASN A 331     -35.527  -1.936 -53.104  1.00104.32           O  
ANISOU 2755  OD1 ASN A 331     9267  21269   9098  -1140    -85  -1324       O  
ATOM   2756  ND2 ASN A 331     -36.583  -0.907 -51.411  1.00102.06           N  
ANISOU 2756  ND2 ASN A 331     8953  20965   8859   -982    -69  -1210       N  
ATOM   2757  N   LEU A 332     -31.872  -1.281 -48.786  1.00 99.56           N  
ANISOU 2757  N   LEU A 332     9519  19092   9217  -1009     -5  -1075       N  
ATOM   2758  CA  LEU A 332     -30.910  -1.810 -47.824  1.00 97.38           C  
ANISOU 2758  CA  LEU A 332     9453  18443   9101  -1096     21  -1095       C  
ATOM   2759  C   LEU A 332     -31.468  -1.880 -46.396  1.00 94.62           C  
ANISOU 2759  C   LEU A 332     9145  17997   8806  -1142     51  -1107       C  
ATOM   2760  O   LEU A 332     -31.572  -2.969 -45.828  1.00 95.47           O  
ANISOU 2760  O   LEU A 332     9310  18016   8945  -1339     85  -1225       O  
ATOM   2761  CB  LEU A 332     -29.607  -0.997 -47.858  1.00 97.27           C  
ANISOU 2761  CB  LEU A 332     9585  18171   9202   -931      5   -962       C  
ATOM   2762  CG  LEU A 332     -28.782  -1.030 -49.150  1.00 98.13           C  
ANISOU 2762  CG  LEU A 332     9700  18296   9288   -902    -17   -952       C  
ATOM   2763  CD1 LEU A 332     -27.649  -0.017 -49.092  1.00 96.99           C  
ANISOU 2763  CD1 LEU A 332     9682  17921   9249   -714    -30   -807       C  
ATOM   2764  CD2 LEU A 332     -28.242  -2.426 -49.419  1.00 97.23           C  
ANISOU 2764  CD2 LEU A 332     9660  18078   9203  -1121      2  -1095       C  
ATOM   2765  N   ASP A 333     -31.830  -0.720 -45.838  1.00 91.07           N  
ANISOU 2765  N   ASP A 333     8669  17566   8367   -959     43   -985       N  
ATOM   2766  CA  ASP A 333     -32.296  -0.592 -44.444  1.00 89.53           C  
ANISOU 2766  CA  ASP A 333     8519  17266   8230   -972     71   -976       C  
ATOM   2767  C   ASP A 333     -31.790   0.722 -43.861  1.00 90.81           C  
ANISOU 2767  C   ASP A 333     8766  17256   8481   -753     66   -815       C  
ATOM   2768  O   ASP A 333     -30.613   1.059 -44.000  1.00 92.65           O  
ANISOU 2768  O   ASP A 333     9129  17268   8805   -677     56   -746       O  
ATOM   2769  CB  ASP A 333     -31.808  -1.766 -43.574  1.00 86.06           C  
ANISOU 2769  CB  ASP A 333     8234  16573   7890  -1175    105  -1077       C  
ATOM   2770  CG  ASP A 333     -32.448  -1.791 -42.182  1.00 86.57           C  
ANISOU 2770  CG  ASP A 333     8327  16572   7993  -1218    136  -1089       C  
ATOM   2771  OD1 ASP A 333     -32.953  -0.749 -41.710  1.00 86.33           O  
ANISOU 2771  OD1 ASP A 333     8245  16601   7954  -1065    131   -994       O  
ATOM   2772  OD2 ASP A 333     -32.433  -2.868 -41.549  1.00 85.72           O  
ANISOU 2772  OD2 ASP A 333     8297  16345   7925  -1407    170  -1192       O  
ATOM   2773  N   LYS A 334     -32.676   1.452 -43.195  1.00 93.16           N  
ANISOU 2773  N   LYS A 334     8991  17653   8752   -657     77   -761       N  
ATOM   2774  CA  LYS A 334     -32.292   2.690 -42.521  1.00 95.92           C  
ANISOU 2774  CA  LYS A 334     9422  17835   9186   -462     86   -619       C  
ATOM   2775  C   LYS A 334     -31.427   2.422 -41.270  1.00 94.45           C  
ANISOU 2775  C   LYS A 334     9438  17296   9151   -530    108   -623       C  
ATOM   2776  O   LYS A 334     -30.678   3.298 -40.821  1.00 93.31           O  
ANISOU 2776  O   LYS A 334     9405  16947   9100   -395    114   -517       O  
ATOM   2777  CB  LYS A 334     -33.536   3.508 -42.156  1.00 98.63           C  
ANISOU 2777  CB  LYS A 334     9626  18392   9455   -344     99   -566       C  
ATOM   2778  CG  LYS A 334     -33.264   4.988 -41.945  1.00 99.76           C  
ANISOU 2778  CG  LYS A 334     9808  18447   9647    -98    111   -405       C  
ATOM   2779  CD  LYS A 334     -34.103   5.536 -40.807  1.00101.92           C  
ANISOU 2779  CD  LYS A 334    10056  18734   9932    -44    144   -374       C  
ATOM   2780  CE  LYS A 334     -33.296   6.512 -39.964  1.00101.32           C  
ANISOU 2780  CE  LYS A 334    10140  18369   9987     89    172   -263       C  
ATOM   2781  NZ  LYS A 334     -34.059   6.969 -38.769  1.00100.26           N  
ANISOU 2781  NZ  LYS A 334     9996  18224   9873    123    210   -244       N  
ATOM   2782  N   ASP A 335     -31.524   1.204 -40.734  1.00 90.62           N  
ANISOU 2782  N   ASP A 335     8999  16746   8685   -741    124   -745       N  
ATOM   2783  CA  ASP A 335     -30.859   0.839 -39.482  1.00 85.86           C  
ANISOU 2783  CA  ASP A 335     8573  15840   8209   -818    146   -756       C  
ATOM   2784  C   ASP A 335     -29.557   0.049 -39.672  1.00 80.70           C  
ANISOU 2784  C   ASP A 335     8072  14948   7643   -913    140   -791       C  
ATOM   2785  O   ASP A 335     -28.838  -0.223 -38.704  1.00 80.68           O  
ANISOU 2785  O   ASP A 335     8223  14683   7748   -960    155   -787       O  
ATOM   2786  CB  ASP A 335     -31.823   0.068 -38.579  1.00 88.87           C  
ANISOU 2786  CB  ASP A 335     8921  16280   8563   -976    177   -854       C  
ATOM   2787  CG  ASP A 335     -32.997   0.913 -38.126  1.00 91.27           C  
ANISOU 2787  CG  ASP A 335     9101  16769   8805   -873    188   -809       C  
ATOM   2788  OD1 ASP A 335     -32.776   2.079 -37.726  1.00 92.40           O  
ANISOU 2788  OD1 ASP A 335     9280  16830   8997   -695    190   -690       O  
ATOM   2789  OD2 ASP A 335     -34.140   0.410 -38.166  1.00 92.59           O  
ANISOU 2789  OD2 ASP A 335     9137  17166   8877   -974    201   -895       O  
ATOM   2790  N   ALA A 336     -29.257  -0.316 -40.912  1.00 75.06           N  
ANISOU 2790  N   ALA A 336     7311  14330   6878   -938    120   -825       N  
ATOM   2791  CA  ALA A 336     -28.005  -0.987 -41.224  1.00 69.55           C  
ANISOU 2791  CA  ALA A 336     6747  13419   6258  -1009    115   -852       C  
ATOM   2792  C   ALA A 336     -26.845   0.004 -41.261  1.00 66.31           C  
ANISOU 2792  C   ALA A 336     6441  12814   5937   -838     96   -726       C  
ATOM   2793  O   ALA A 336     -27.050   1.216 -41.369  1.00 64.85           O  
ANISOU 2793  O   ALA A 336     6205  12699   5735   -660     88   -622       O  
ATOM   2794  CB  ALA A 336     -28.117  -1.723 -42.547  1.00 67.69           C  
ANISOU 2794  CB  ALA A 336     6422  13361   5934  -1101    104   -938       C  
ATOM   2795  N   PHE A 337     -25.629  -0.522 -41.146  1.00 63.35           N  
ANISOU 2795  N   PHE A 337     6215  12194   5660   -893     96   -738       N  
ATOM   2796  CA  PHE A 337     -24.420   0.260 -41.381  1.00 61.01           C  
ANISOU 2796  CA  PHE A 337     6014  11725   5442   -756     79   -639       C  
ATOM   2797  C   PHE A 337     -23.998   0.125 -42.836  1.00 59.18           C  
ANISOU 2797  C   PHE A 337     5733  11590   5161   -741     57   -651       C  
ATOM   2798  O   PHE A 337     -23.804  -0.987 -43.331  1.00 59.07           O  
ANISOU 2798  O   PHE A 337     5728  11581   5134   -886     60   -749       O  
ATOM   2799  CB  PHE A 337     -23.279  -0.213 -40.470  1.00 59.36           C  
ANISOU 2799  CB  PHE A 337     5986  11204   5362   -817     88   -642       C  
ATOM   2800  CG  PHE A 337     -21.954   0.430 -40.780  1.00 57.96           C  
ANISOU 2800  CG  PHE A 337     5906  10851   5264   -702     72   -559       C  
ATOM   2801  CD1 PHE A 337     -21.129  -0.087 -41.767  1.00 56.35           C  
ANISOU 2801  CD1 PHE A 337     5730  10611   5068   -737     58   -589       C  
ATOM   2802  CD2 PHE A 337     -21.537   1.561 -40.087  1.00 57.01           C  
ANISOU 2802  CD2 PHE A 337     5848  10602   5208   -563     75   -456       C  
ATOM   2803  CE1 PHE A 337     -19.925   0.516 -42.066  1.00 56.03           C  
ANISOU 2803  CE1 PHE A 337     5773  10417   5098   -634     45   -516       C  
ATOM   2804  CE2 PHE A 337     -20.328   2.164 -40.379  1.00 55.04           C  
ANISOU 2804  CE2 PHE A 337     5686  10198   5029   -466     65   -387       C  
ATOM   2805  CZ  PHE A 337     -19.520   1.642 -41.366  1.00 54.61           C  
ANISOU 2805  CZ  PHE A 337     5654  10114   4981   -501     48   -415       C  
ATOM   2806  N   ILE A 338     -23.857   1.256 -43.521  1.00 58.09           N  
ANISOU 2806  N   ILE A 338     5547  11526   4997   -566     40   -551       N  
ATOM   2807  CA  ILE A 338     -23.323   1.269 -44.885  1.00 57.82           C  
ANISOU 2807  CA  ILE A 338     5481  11565   4924   -530     19   -544       C  
ATOM   2808  C   ILE A 338     -22.291   2.383 -45.031  1.00 56.19           C  
ANISOU 2808  C   ILE A 338     5358  11202   4789   -359     14   -422       C  
ATOM   2809  O   ILE A 338     -22.496   3.498 -44.553  1.00 57.14           O  
ANISOU 2809  O   ILE A 338     5477  11307   4926   -215     25   -325       O  
ATOM   2810  CB  ILE A 338     -24.422   1.461 -45.966  1.00 58.93           C  
ANISOU 2810  CB  ILE A 338     5429  12047   4912   -495      5   -556       C  
ATOM   2811  CG1 ILE A 338     -25.628   0.548 -45.718  1.00 62.12           C  
ANISOU 2811  CG1 ILE A 338     5731  12637   5234   -653     16   -672       C  
ATOM   2812  CG2 ILE A 338     -23.861   1.172 -47.351  1.00 59.96           C  
ANISOU 2812  CG2 ILE A 338     5533  12250   4999   -506    -13   -578       C  
ATOM   2813  CD1 ILE A 338     -26.830   1.237 -45.091  1.00 63.23           C  
ANISOU 2813  CD1 ILE A 338     5768  12935   5319   -576     25   -631       C  
ATOM   2814  N   HIS A 339     -21.182   2.074 -45.688  1.00 54.04           N  
ANISOU 2814  N   HIS A 339     5160  10811   4561   -378      3   -431       N  
ATOM   2815  CA  HIS A 339     -20.213   3.089 -46.063  1.00 55.06           C  
ANISOU 2815  CA  HIS A 339     5353  10823   4743   -224      0   -324       C  
ATOM   2816  C   HIS A 339     -19.471   2.638 -47.274  1.00 55.38           C  
ANISOU 2816  C   HIS A 339     5396  10877   4766   -256    -16   -355       C  
ATOM   2817  O   HIS A 339     -19.237   1.439 -47.461  1.00 56.20           O  
ANISOU 2817  O   HIS A 339     5523  10953   4876   -412    -19   -459       O  
ATOM   2818  CB  HIS A 339     -19.240   3.387 -44.907  1.00 54.62           C  
ANISOU 2818  CB  HIS A 339     5457  10471   4824   -203     13   -282       C  
ATOM   2819  CG  HIS A 339     -18.501   4.704 -45.056  1.00 53.00           C  
ANISOU 2819  CG  HIS A 339     5306  10164   4667    -27     23   -162       C  
ATOM   2820  ND1 HIS A 339     -17.386   4.835 -45.822  1.00 52.10           N  
ANISOU 2820  ND1 HIS A 339     5251   9955   4590      8     15   -137       N  
ATOM   2821  CD2 HIS A 339     -18.764   5.971 -44.519  1.00 51.37           C  
ANISOU 2821  CD2 HIS A 339     5103   9939   4476    120     48    -62       C  
ATOM   2822  CE1 HIS A 339     -16.958   6.115 -45.771  1.00 52.13           C  
ANISOU 2822  CE1 HIS A 339     5295   9881   4630    167     35    -29       C  
ATOM   2823  NE2 HIS A 339     -17.804   6.809 -44.973  1.00 52.56           N  
ANISOU 2823  NE2 HIS A 339     5317   9979   4672    235     58     16       N  
ATOM   2824  N   ARG A 340     -19.090   3.592 -48.118  1.00 57.26           N  
ANISOU 2824  N   ARG A 340     5615  11156   4983   -107    -21   -265       N  
ATOM   2825  CA  ARG A 340     -18.474   3.267 -49.399  1.00 58.35           C  
ANISOU 2825  CA  ARG A 340     5739  11341   5089   -123    -36   -288       C  
ATOM   2826  C   ARG A 340     -17.374   4.252 -49.790  1.00 56.98           C  
ANISOU 2826  C   ARG A 340     5646  11028   4976     20    -31   -184       C  
ATOM   2827  O   ARG A 340     -17.368   5.402 -49.351  1.00 54.88           O  
ANISOU 2827  O   ARG A 340     5405  10707   4740    163    -13    -80       O  
ATOM   2828  CB  ARG A 340     -19.549   3.182 -50.507  1.00 61.57           C  
ANISOU 2828  CB  ARG A 340     5972  12079   5341   -119    -51   -313       C  
ATOM   2829  CG  ARG A 340     -20.383   4.448 -50.672  1.00 64.54           C  
ANISOU 2829  CG  ARG A 340     6248  12632   5642     63    -47   -200       C  
ATOM   2830  CD  ARG A 340     -21.433   4.304 -51.769  1.00 72.04           C  
ANISOU 2830  CD  ARG A 340     7015  13925   6429     65    -65   -227       C  
ATOM   2831  NE  ARG A 340     -21.427   5.458 -52.671  1.00 72.55           N  
ANISOU 2831  NE  ARG A 340     7024  14109   6433    259    -66   -104       N  
ATOM   2832  CZ  ARG A 340     -20.525   5.644 -53.630  1.00 73.16           C  
ANISOU 2832  CZ  ARG A 340     7140  14143   6515    306    -71    -71       C  
ATOM   2833  NH1 ARG A 340     -19.569   4.741 -53.831  1.00 74.50           N  
ANISOU 2833  NH1 ARG A 340     7398  14161   6748    172    -79   -155       N  
ATOM   2834  NH2 ARG A 340     -20.574   6.731 -54.390  1.00 74.26           N  
ANISOU 2834  NH2 ARG A 340     7231  14389   6596    490    -65     48       N  
ATOM   2835  N   THR A 341     -16.427   3.776 -50.593  1.00 58.27           N  
ANISOU 2835  N   THR A 341     5853  11124   5159    -25    -41   -217       N  
ATOM   2836  CA  THR A 341     -15.545   4.646 -51.354  1.00 61.58           C  
ANISOU 2836  CA  THR A 341     6311  11486   5598    104    -37   -130       C  
ATOM   2837  C   THR A 341     -15.690   4.215 -52.801  1.00 68.09           C  
ANISOU 2837  C   THR A 341     7040  12511   6318     75    -55   -170       C  
ATOM   2838  O   THR A 341     -16.546   3.389 -53.118  1.00 71.98           O  
ANISOU 2838  O   THR A 341     7433  13192   6723    -32    -68   -259       O  
ATOM   2839  CB  THR A 341     -14.063   4.508 -50.933  1.00 59.37           C  
ANISOU 2839  CB  THR A 341     6189  10912   5454     78    -30   -130       C  
ATOM   2840  OG1 THR A 341     -13.602   3.185 -51.221  1.00 60.55           O  
ANISOU 2840  OG1 THR A 341     6367  11018   5621    -80    -43   -242       O  
ATOM   2841  CG2 THR A 341     -13.873   4.801 -49.450  1.00 56.92           C  
ANISOU 2841  CG2 THR A 341     5975  10405   5244     85    -14   -105       C  
ATOM   2842  N   VAL A 342     -14.853   4.757 -53.681  1.00 72.64           N  
ANISOU 2842  N   VAL A 342     7647  13052   6902    163    -53   -112       N  
ATOM   2843  CA  VAL A 342     -14.878   4.348 -55.087  1.00 77.25           C  
ANISOU 2843  CA  VAL A 342     8147  13816   7387    134    -69   -151       C  
ATOM   2844  C   VAL A 342     -14.508   2.871 -55.255  1.00 79.59           C  
ANISOU 2844  C   VAL A 342     8470  14066   7704    -62    -79   -293       C  
ATOM   2845  O   VAL A 342     -15.011   2.196 -56.158  1.00 80.27           O  
ANISOU 2845  O   VAL A 342     8457  14353   7687   -145    -90   -369       O  
ATOM   2846  CB  VAL A 342     -13.977   5.237 -55.982  1.00 78.07           C  
ANISOU 2846  CB  VAL A 342     8288  13873   7499    268    -60    -57       C  
ATOM   2847  CG1 VAL A 342     -14.768   6.434 -56.490  1.00 77.98           C  
ANISOU 2847  CG1 VAL A 342     8179  14059   7389    447    -51     60       C  
ATOM   2848  CG2 VAL A 342     -12.718   5.680 -55.238  1.00 74.07           C  
ANISOU 2848  CG2 VAL A 342     7943  13057   7143    307    -39    -11       C  
ATOM   2849  N   ASP A 343     -13.645   2.375 -54.369  1.00 78.36           N  
ANISOU 2849  N   ASP A 343     8448  13648   7677   -137    -69   -328       N  
ATOM   2850  CA  ASP A 343     -13.173   0.990 -54.440  1.00 76.96           C  
ANISOU 2850  CA  ASP A 343     8318  13387   7536   -312    -68   -452       C  
ATOM   2851  C   ASP A 343     -13.949   0.045 -53.502  1.00 75.95           C  
ANISOU 2851  C   ASP A 343     8182  13262   7412   -453    -60   -543       C  
ATOM   2852  O   ASP A 343     -13.923  -1.175 -53.684  1.00 75.93           O  
ANISOU 2852  O   ASP A 343     8187  13256   7406   -610    -51   -658       O  
ATOM   2853  CB  ASP A 343     -11.664   0.902 -54.132  1.00 76.15           C  
ANISOU 2853  CB  ASP A 343     8366  12997   7569   -311    -59   -439       C  
ATOM   2854  CG  ASP A 343     -10.870   2.112 -54.643  1.00 77.27           C  
ANISOU 2854  CG  ASP A 343     8541  13083   7733   -150    -58   -326       C  
ATOM   2855  OD1 ASP A 343     -11.270   2.721 -55.658  1.00 79.63           O  
ANISOU 2855  OD1 ASP A 343     8749  13570   7935    -64    -63   -279       O  
ATOM   2856  OD2 ASP A 343      -9.830   2.443 -54.026  1.00 72.91           O  
ANISOU 2856  OD2 ASP A 343     8106  12299   7295   -111    -49   -284       O  
ATOM   2857  N   ASP A 344     -14.646   0.609 -52.515  1.00 72.98           N  
ANISOU 2857  N   ASP A 344     7792  12892   7042   -399    -58   -493       N  
ATOM   2858  CA  ASP A 344     -15.037  -0.156 -51.328  1.00 66.56           C  
ANISOU 2858  CA  ASP A 344     7021  11991   6276   -516    -46   -558       C  
ATOM   2859  C   ASP A 344     -16.489  -0.020 -50.967  1.00 64.80           C  
ANISOU 2859  C   ASP A 344     6684  11973   5964   -523    -46   -568       C  
ATOM   2860  O   ASP A 344     -17.037   1.075 -50.996  1.00 67.02           O  
ANISOU 2860  O   ASP A 344     6897  12367   6197   -383    -53   -476       O  
ATOM   2861  CB  ASP A 344     -14.226   0.301 -50.127  1.00 63.96           C  
ANISOU 2861  CB  ASP A 344     6828  11396   6078   -460    -39   -493       C  
ATOM   2862  CG  ASP A 344     -12.830  -0.228 -50.135  1.00 64.90           C  
ANISOU 2862  CG  ASP A 344     7073  11287   6300   -504    -35   -515       C  
ATOM   2863  OD1 ASP A 344     -12.649  -1.437 -50.397  1.00 64.51           O  
ANISOU 2863  OD1 ASP A 344     7041  11213   6253   -643    -26   -615       O  
ATOM   2864  OD2 ASP A 344     -11.908   0.568 -49.853  1.00 67.63           O  
ANISOU 2864  OD2 ASP A 344     7500  11473   6724   -399    -36   -433       O  
ATOM   2865  N   TYR A 345     -17.095  -1.138 -50.582  1.00 62.96           N  
ANISOU 2865  N   TYR A 345     6433  11778   5712   -687    -33   -679       N  
ATOM   2866  CA  TYR A 345     -18.369  -1.127 -49.881  1.00 62.43           C  
ANISOU 2866  CA  TYR A 345     6284  11845   5588   -715    -27   -698       C  
ATOM   2867  C   TYR A 345     -18.237  -1.883 -48.564  1.00 57.09           C  
ANISOU 2867  C   TYR A 345     5717  10969   5006   -828     -4   -748       C  
ATOM   2868  O   TYR A 345     -17.620  -2.946 -48.505  1.00 56.05           O  
ANISOU 2868  O   TYR A 345     5669  10698   4928   -956     12   -827       O  
ATOM   2869  CB  TYR A 345     -19.461  -1.761 -50.743  1.00 69.75           C  
ANISOU 2869  CB  TYR A 345     7060  13065   6376   -817    -28   -794       C  
ATOM   2870  CG  TYR A 345     -20.318  -0.776 -51.515  1.00 74.40           C  
ANISOU 2870  CG  TYR A 345     7493  13934   6840   -682    -50   -725       C  
ATOM   2871  CD1 TYR A 345     -21.583  -0.409 -51.051  1.00 76.90           C  
ANISOU 2871  CD1 TYR A 345     7701  14434   7083   -654    -50   -712       C  
ATOM   2872  CD2 TYR A 345     -19.880  -0.233 -52.723  1.00 77.08           C  
ANISOU 2872  CD2 TYR A 345     7793  14363   7131   -582    -68   -672       C  
ATOM   2873  CE1 TYR A 345     -22.376   0.484 -51.758  1.00 79.70           C  
ANISOU 2873  CE1 TYR A 345     7909  15053   7320   -521    -69   -643       C  
ATOM   2874  CE2 TYR A 345     -20.667   0.662 -53.439  1.00 78.99           C  
ANISOU 2874  CE2 TYR A 345     7892  14866   7253   -450    -86   -600       C  
ATOM   2875  CZ  TYR A 345     -21.912   1.016 -52.953  1.00 80.70           C  
ANISOU 2875  CZ  TYR A 345     8000  15261   7398   -416    -86   -584       C  
ATOM   2876  OH  TYR A 345     -22.697   1.903 -53.662  1.00 84.97           O  
ANISOU 2876  OH  TYR A 345     8398  16069   7818   -274   -102   -506       O  
ATOM   2877  N   PHE A 346     -18.820  -1.331 -47.510  1.00 53.95           N  
ANISOU 2877  N   PHE A 346     5317  10557   4623   -777     -1   -699       N  
ATOM   2878  CA  PHE A 346     -18.754  -1.940 -46.187  1.00 51.45           C  
ANISOU 2878  CA  PHE A 346     5100  10059   4388   -870     20   -734       C  
ATOM   2879  C   PHE A 346     -20.120  -1.883 -45.546  1.00 51.55           C  
ANISOU 2879  C   PHE A 346     5021  10230   4335   -900     30   -755       C  
ATOM   2880  O   PHE A 346     -20.666  -0.803 -45.330  1.00 53.17           O  
ANISOU 2880  O   PHE A 346     5165  10526   4509   -769     20   -672       O  
ATOM   2881  CB  PHE A 346     -17.711  -1.219 -45.316  1.00 49.83           C  
ANISOU 2881  CB  PHE A 346     5028   9599   4304   -765     16   -637       C  
ATOM   2882  CG  PHE A 346     -17.496  -1.845 -43.955  1.00 47.95           C  
ANISOU 2882  CG  PHE A 346     4901   9163   4151   -854     35   -665       C  
ATOM   2883  CD1 PHE A 346     -17.575  -3.225 -43.776  1.00 47.62           C  
ANISOU 2883  CD1 PHE A 346     4896   9078   4118  -1027     59   -773       C  
ATOM   2884  CD2 PHE A 346     -17.166  -1.048 -42.860  1.00 46.05           C  
ANISOU 2884  CD2 PHE A 346     4736   8775   3985   -763     34   -583       C  
ATOM   2885  CE1 PHE A 346     -17.362  -3.792 -42.524  1.00 48.26           C  
ANISOU 2885  CE1 PHE A 346     5084   8976   4274  -1099     79   -789       C  
ATOM   2886  CE2 PHE A 346     -16.939  -1.609 -41.608  1.00 46.68           C  
ANISOU 2886  CE2 PHE A 346     4918   8680   4138   -840     50   -603       C  
ATOM   2887  CZ  PHE A 346     -17.041  -2.981 -41.436  1.00 47.21           C  
ANISOU 2887  CZ  PHE A 346     5019   8708   4209  -1004     71   -702       C  
ATOM   2888  N   PHE A 347     -20.668  -3.053 -45.237  1.00 51.58           N  
ANISOU 2888  N   PHE A 347     5018  10260   4317  -1074     55   -868       N  
ATOM   2889  CA  PHE A 347     -22.060  -3.164 -44.822  1.00 52.23           C  
ANISOU 2889  CA  PHE A 347     4992  10533   4318  -1131     68   -912       C  
ATOM   2890  C   PHE A 347     -22.174  -4.060 -43.597  1.00 51.77           C  
ANISOU 2890  C   PHE A 347     5026  10320   4321  -1269    103   -975       C  
ATOM   2891  O   PHE A 347     -21.614  -5.155 -43.572  1.00 52.85           O  
ANISOU 2891  O   PHE A 347     5253  10321   4506  -1400    128  -1050       O  
ATOM   2892  CB  PHE A 347     -22.912  -3.719 -45.992  1.00 54.21           C  
ANISOU 2892  CB  PHE A 347     5092  11067   4436  -1222     69  -1008       C  
ATOM   2893  CG  PHE A 347     -24.364  -3.928 -45.650  1.00 55.50           C  
ANISOU 2893  CG  PHE A 347     5131  11450   4505  -1297     84  -1069       C  
ATOM   2894  CD1 PHE A 347     -24.796  -5.120 -45.062  1.00 56.69           C  
ANISOU 2894  CD1 PHE A 347     5311  11567   4660  -1491    126  -1187       C  
ATOM   2895  CD2 PHE A 347     -25.299  -2.940 -45.911  1.00 56.29           C  
ANISOU 2895  CD2 PHE A 347     5086  11790   4511  -1172     61  -1008       C  
ATOM   2896  CE1 PHE A 347     -26.130  -5.316 -44.742  1.00 57.86           C  
ANISOU 2896  CE1 PHE A 347     5342  11919   4720  -1567    143  -1249       C  
ATOM   2897  CE2 PHE A 347     -26.639  -3.136 -45.605  1.00 59.40           C  
ANISOU 2897  CE2 PHE A 347     5356  12397   4814  -1240     75  -1066       C  
ATOM   2898  CZ  PHE A 347     -27.054  -4.325 -45.018  1.00 59.37           C  
ANISOU 2898  CZ  PHE A 347     5380  12361   4816  -1442    115  -1190       C  
ATOM   2899  N   CYS A 348     -22.899  -3.592 -42.585  1.00 51.77           N  
ANISOU 2899  N   CYS A 348     5007  10341   4320  -1235    109   -941       N  
ATOM   2900  CA  CYS A 348     -23.124  -4.369 -41.371  1.00 52.71           C  
ANISOU 2900  CA  CYS A 348     5207  10332   4488  -1360    144   -993       C  
ATOM   2901  C   CYS A 348     -24.577  -4.297 -40.931  1.00 54.75           C  
ANISOU 2901  C   CYS A 348     5347  10794   4661  -1401    158  -1030       C  
ATOM   2902  O   CYS A 348     -25.257  -3.293 -41.169  1.00 54.91           O  
ANISOU 2902  O   CYS A 348     5250  10994   4616  -1278    137   -970       O  
ATOM   2903  CB  CYS A 348     -22.230  -3.881 -40.227  1.00 51.27           C  
ANISOU 2903  CB  CYS A 348     5169   9884   4424  -1278    139   -904       C  
ATOM   2904  SG  CYS A 348     -20.474  -3.863 -40.629  1.00 51.04           S  
ANISOU 2904  SG  CYS A 348     5278   9614   4500  -1218    121   -853       S  
ATOM   2905  N   SER A 349     -25.033  -5.370 -40.282  1.00 54.66           N  
ANISOU 2905  N   SER A 349     5368  10749   4652  -1572    200  -1126       N  
ATOM   2906  CA  SER A 349     -26.354  -5.449 -39.680  1.00 56.60           C  
ANISOU 2906  CA  SER A 349     5520  11154   4829  -1635    222  -1171       C  
ATOM   2907  C   SER A 349     -26.348  -6.585 -38.669  1.00 57.63           C  
ANISOU 2907  C   SER A 349     5764  11118   5014  -1804    273  -1247       C  
ATOM   2908  O   SER A 349     -25.610  -7.562 -38.838  1.00 57.06           O  
ANISOU 2908  O   SER A 349     5794  10893   4991  -1908    298  -1301       O  
ATOM   2909  CB  SER A 349     -27.427  -5.715 -40.752  1.00 58.52           C  
ANISOU 2909  CB  SER A 349     5584  11717   4934  -1703    224  -1258       C  
ATOM   2910  OG  SER A 349     -28.660  -6.119 -40.166  1.00 58.64           O  
ANISOU 2910  OG  SER A 349     5520  11874   4885  -1815    257  -1334       O  
ATOM   2911  N   PRO A 350     -27.171  -6.468 -37.612  1.00 59.28           N  
ANISOU 2911  N   PRO A 350     5957  11353   5213  -1829    294  -1248       N  
ATOM   2912  CA  PRO A 350     -27.366  -7.599 -36.696  1.00 61.33           C  
ANISOU 2912  CA  PRO A 350     6306  11490   5504  -2002    350  -1329       C  
ATOM   2913  C   PRO A 350     -28.123  -8.753 -37.367  1.00 64.49           C  
ANISOU 2913  C   PRO A 350     6631  12051   5821  -2196    396  -1476       C  
ATOM   2914  O   PRO A 350     -28.184  -9.853 -36.817  1.00 65.32           O  
ANISOU 2914  O   PRO A 350     6822  12045   5953  -2359    454  -1556       O  
ATOM   2915  CB  PRO A 350     -28.208  -6.997 -35.566  1.00 60.64           C  
ANISOU 2915  CB  PRO A 350     6186  11446   5406  -1963    356  -1291       C  
ATOM   2916  CG  PRO A 350     -28.891  -5.816 -36.178  1.00 59.77           C  
ANISOU 2916  CG  PRO A 350     5913  11578   5216  -1818    314  -1237       C  
ATOM   2917  CD  PRO A 350     -27.935  -5.274 -37.197  1.00 59.26           C  
ANISOU 2917  CD  PRO A 350     5859  11484   5173  -1693    271  -1172       C  
ATOM   2918  N   HIS A 351     -28.684  -8.490 -38.550  1.00 67.13           N  
ANISOU 2918  N   HIS A 351     6807  12646   6053  -2179    373  -1511       N  
ATOM   2919  CA  HIS A 351     -29.461  -9.489 -39.296  1.00 68.96           C  
ANISOU 2919  CA  HIS A 351     6943  13069   6188  -2363    414  -1658       C  
ATOM   2920  C   HIS A 351     -28.623 -10.126 -40.372  1.00 69.99           C  
ANISOU 2920  C   HIS A 351     7115  13145   6330  -2416    418  -1706       C  
ATOM   2921  O   HIS A 351     -28.377  -9.520 -41.423  1.00 70.86           O  
ANISOU 2921  O   HIS A 351     7146  13378   6398  -2311    371  -1668       O  
ATOM   2922  CB  HIS A 351     -30.741  -8.871 -39.870  1.00 69.45           C  
ANISOU 2922  CB  HIS A 351     6787  13486   6112  -2327    389  -1679       C  
ATOM   2923  CG  HIS A 351     -31.584  -8.152 -38.836  1.00 70.01           C  
ANISOU 2923  CG  HIS A 351     6808  13620   6171  -2258    385  -1626       C  
ATOM   2924  ND1 HIS A 351     -32.101  -8.779 -37.754  1.00 70.88           N  
ANISOU 2924  ND1 HIS A 351     6970  13659   6302  -2387    437  -1683       N  
ATOM   2925  CD2 HIS A 351     -31.969  -6.814 -38.736  1.00 70.01           C  
ANISOU 2925  CD2 HIS A 351     6714  13741   6143  -2065    337  -1515       C  
ATOM   2926  CE1 HIS A 351     -32.780  -7.889 -37.002  1.00 70.50           C  
ANISOU 2926  CE1 HIS A 351     6861  13687   6238  -2284    421  -1615       C  
ATOM   2927  NE2 HIS A 351     -32.701  -6.688 -37.604  1.00 71.21           N  
ANISOU 2927  NE2 HIS A 351     6862  13893   6299  -2085    362  -1513       N  
ATOM   2928  N   PRO A 352     -28.157 -11.364 -40.119  1.00 70.46           N  
ANISOU 2928  N   PRO A 352     7307  13015   6448  -2577    481  -1788       N  
ATOM   2929  CA  PRO A 352     -27.190 -12.026 -40.997  1.00 69.55           C  
ANISOU 2929  CA  PRO A 352     7265  12791   6367  -2624    495  -1827       C  
ATOM   2930  C   PRO A 352     -27.702 -12.148 -42.423  1.00 72.07           C  
ANISOU 2930  C   PRO A 352     7428  13387   6568  -2677    487  -1914       C  
ATOM   2931  O   PRO A 352     -26.923 -11.999 -43.365  1.00 70.46           O  
ANISOU 2931  O   PRO A 352     7230  13167   6372  -2615    458  -1891       O  
ATOM   2932  CB  PRO A 352     -27.029 -13.420 -40.372  1.00 70.49           C  
ANISOU 2932  CB  PRO A 352     7524  12712   6544  -2815    584  -1921       C  
ATOM   2933  CG  PRO A 352     -27.554 -13.299 -38.981  1.00 70.43           C  
ANISOU 2933  CG  PRO A 352     7558  12636   6565  -2821    602  -1888       C  
ATOM   2934  CD  PRO A 352     -28.617 -12.248 -39.033  1.00 70.79           C  
ANISOU 2934  CD  PRO A 352     7427  12952   6516  -2731    552  -1856       C  
ATOM   2935  N   HIS A 353     -29.006 -12.397 -42.580  1.00 74.08           N  
ANISOU 2935  N   HIS A 353     7536  13902   6706  -2790    511  -2013       N  
ATOM   2936  CA  HIS A 353     -29.591 -12.572 -43.910  1.00 77.01           C  
ANISOU 2936  CA  HIS A 353     7744  14565   6948  -2858    506  -2108       C  
ATOM   2937  C   HIS A 353     -29.458 -11.334 -44.760  1.00 76.88           C  
ANISOU 2937  C   HIS A 353     7613  14717   6880  -2654    421  -2002       C  
ATOM   2938  O   HIS A 353     -29.262 -11.433 -45.972  1.00 78.44           O  
ANISOU 2938  O   HIS A 353     7742  15043   7016  -2665    406  -2042       O  
ATOM   2939  CB  HIS A 353     -31.043 -13.071 -43.837  1.00 78.66           C  
ANISOU 2939  CB  HIS A 353     7813  15034   7040  -3023    551  -2238       C  
ATOM   2940  CG  HIS A 353     -32.061 -11.987 -43.545  1.00 80.30           C  
ANISOU 2940  CG  HIS A 353     7862  15479   7168  -2899    499  -2171       C  
ATOM   2941  ND1 HIS A 353     -32.511 -11.727 -42.296  1.00 81.88           N  
ANISOU 2941  ND1 HIS A 353     8095  15607   7407  -2877    510  -2128       N  
ATOM   2942  CD2 HIS A 353     -32.723 -11.097 -44.395  1.00 79.11           C  
ANISOU 2942  CD2 HIS A 353     7513  15649   6896  -2785    438  -2138       C  
ATOM   2943  CE1 HIS A 353     -33.406 -10.721 -42.344  1.00 82.02           C  
ANISOU 2943  CE1 HIS A 353     7947  15879   7336  -2755    461  -2072       C  
ATOM   2944  NE2 HIS A 353     -33.532 -10.335 -43.629  1.00 80.74           N  
ANISOU 2944  NE2 HIS A 353     7643  15956   7076  -2695    418  -2075       N  
ATOM   2945  N   LYS A 354     -29.528 -10.158 -44.133  1.00 75.19           N  
ANISOU 2945  N   LYS A 354     7384  14492   6692  -2467    369  -1865       N  
ATOM   2946  CA  LYS A 354     -29.320  -8.896 -44.855  1.00 75.89           C  
ANISOU 2946  CA  LYS A 354     7385  14703   6744  -2253    295  -1745       C  
ATOM   2947  C   LYS A 354     -27.888  -8.764 -45.402  1.00 74.85           C  
ANISOU 2947  C   LYS A 354     7374  14365   6700  -2167    272  -1680       C  
ATOM   2948  O   LYS A 354     -27.661  -8.094 -46.415  1.00 73.63           O  
ANISOU 2948  O   LYS A 354     7142  14338   6495  -2049    226  -1627       O  
ATOM   2949  CB  LYS A 354     -29.653  -7.692 -43.973  1.00 75.76           C  
ANISOU 2949  CB  LYS A 354     7349  14686   6751  -2075    260  -1614       C  
ATOM   2950  CG  LYS A 354     -31.126  -7.515 -43.665  1.00 76.25           C  
ANISOU 2950  CG  LYS A 354     7251  15016   6706  -2109    268  -1656       C  
ATOM   2951  CD  LYS A 354     -31.384  -6.150 -43.050  1.00 76.98           C  
ANISOU 2951  CD  LYS A 354     7307  15127   6811  -1897    229  -1512       C  
ATOM   2952  CE  LYS A 354     -32.443  -6.216 -41.960  1.00 80.30           C  
ANISOU 2952  CE  LYS A 354     7686  15611   7211  -1957    259  -1543       C  
ATOM   2953  NZ  LYS A 354     -33.802  -6.523 -42.490  1.00 84.43           N  
ANISOU 2953  NZ  LYS A 354     8008  16487   7583  -2056    270  -1648       N  
ATOM   2954  N   VAL A 355     -26.931  -9.405 -44.734  1.00 73.68           N  
ANISOU 2954  N   VAL A 355     7412  13903   6679  -2224    305  -1682       N  
ATOM   2955  CA  VAL A 355     -25.539  -9.382 -45.192  1.00 73.48           C  
ANISOU 2955  CA  VAL A 355     7506  13671   6741  -2156    288  -1630       C  
ATOM   2956  C   VAL A 355     -25.334 -10.284 -46.423  1.00 74.17           C  
ANISOU 2956  C   VAL A 355     7564  13838   6777  -2285    314  -1745       C  
ATOM   2957  O   VAL A 355     -24.434 -10.044 -47.223  1.00 74.12           O  
ANISOU 2957  O   VAL A 355     7588  13780   6795  -2209    287  -1705       O  
ATOM   2958  CB  VAL A 355     -24.539  -9.711 -44.055  1.00 70.02           C  
ANISOU 2958  CB  VAL A 355     7271  12879   6453  -2155    311  -1583       C  
ATOM   2959  CG1 VAL A 355     -23.108  -9.538 -44.529  1.00 67.58           C  
ANISOU 2959  CG1 VAL A 355     7070  12377   6230  -2063    287  -1518       C  
ATOM   2960  CG2 VAL A 355     -24.790  -8.811 -42.851  1.00 68.36           C  
ANISOU 2960  CG2 VAL A 355     7081  12607   6284  -2037    288  -1478       C  
ATOM   2961  N   TYR A 356     -26.187 -11.299 -46.579  1.00 78.30           N  
ANISOU 2961  N   TYR A 356     8027  14494   7226  -2485    370  -1893       N  
ATOM   2962  CA  TYR A 356     -26.252 -12.069 -47.833  1.00 80.31           C  
ANISOU 2962  CA  TYR A 356     8216  14895   7401  -2617    397  -2017       C  
ATOM   2963  C   TYR A 356     -26.955 -11.269 -48.914  1.00 79.31           C  
ANISOU 2963  C   TYR A 356     7887  15114   7132  -2533    341  -2003       C  
ATOM   2964  O   TYR A 356     -26.422 -11.096 -50.010  1.00 78.56           O  
ANISOU 2964  O   TYR A 356     7760  15080   7006  -2485    314  -1994       O  
ATOM   2965  CB  TYR A 356     -26.971 -13.411 -47.644  1.00 85.83           C  
ANISOU 2965  CB  TYR A 356     8916  15631   8063  -2870    485  -2189       C  
ATOM   2966  CG  TYR A 356     -26.287 -14.345 -46.680  1.00 90.01           C  
ANISOU 2966  CG  TYR A 356     9650  15824   8726  -2966    553  -2211       C  
ATOM   2967  CD1 TYR A 356     -25.198 -15.121 -47.078  1.00 92.64           C  
ANISOU 2967  CD1 TYR A 356    10117  15943   9138  -3022    593  -2246       C  
ATOM   2968  CD2 TYR A 356     -26.728 -14.452 -45.364  1.00 92.74           C  
ANISOU 2968  CD2 TYR A 356    10054  16066   9116  -2995    581  -2194       C  
ATOM   2969  CE1 TYR A 356     -24.562 -15.974 -46.183  1.00 94.83           C  
ANISOU 2969  CE1 TYR A 356    10582  15913   9535  -3097    658  -2256       C  
ATOM   2970  CE2 TYR A 356     -26.105 -15.301 -44.460  1.00 95.52           C  
ANISOU 2970  CE2 TYR A 356    10594  16114   9585  -3074    644  -2206       C  
ATOM   2971  CZ  TYR A 356     -25.024 -16.061 -44.868  1.00 96.04           C  
ANISOU 2971  CZ  TYR A 356    10790  15971   9726  -3121    683  -2234       C  
ATOM   2972  OH  TYR A 356     -24.413 -16.898 -43.955  1.00 95.52           O  
ANISOU 2972  OH  TYR A 356    10911  15608   9774  -3188    749  -2236       O  
ATOM   2973  N   ASP A 357     -28.156 -10.781 -48.602  1.00 79.57           N  
ANISOU 2973  N   ASP A 357     7779  15379   7074  -2512    324  -1999       N  
ATOM   2974  CA  ASP A 357     -28.914  -9.952 -49.542  1.00 79.95           C  
ANISOU 2974  CA  ASP A 357     7623  15774   6978  -2413    270  -1971       C  
ATOM   2975  C   ASP A 357     -28.033  -8.829 -50.082  1.00 76.94           C  
ANISOU 2975  C   ASP A 357     7262  15341   6631  -2185    204  -1819       C  
ATOM   2976  O   ASP A 357     -28.209  -8.389 -51.217  1.00 77.78           O  
ANISOU 2976  O   ASP A 357     7240  15680   6633  -2119    167  -1806       O  
ATOM   2977  CB  ASP A 357     -30.185  -9.382 -48.893  1.00 81.20           C  
ANISOU 2977  CB  ASP A 357     7651  16137   7063  -2373    256  -1949       C  
ATOM   2978  CG  ASP A 357     -31.147 -10.472 -48.412  1.00 82.97           C  
ANISOU 2978  CG  ASP A 357     7839  16443   7240  -2606    324  -2107       C  
ATOM   2979  OD1 ASP A 357     -30.941 -11.655 -48.761  1.00 83.14           O  
ANISOU 2979  OD1 ASP A 357     7913  16409   7264  -2804    383  -2244       O  
ATOM   2980  OD2 ASP A 357     -32.106 -10.142 -47.673  1.00 82.12           O  
ANISOU 2980  OD2 ASP A 357     7656  16450   7095  -2593    324  -2096       O  
ATOM   2981  N   PHE A 358     -27.065  -8.391 -49.277  1.00 72.42           N  
ANISOU 2981  N   PHE A 358     6851  14463   6201  -2071    194  -1706       N  
ATOM   2982  CA  PHE A 358     -26.109  -7.392 -49.735  1.00 68.83           C  
ANISOU 2982  CA  PHE A 358     6438  13922   5792  -1870    143  -1569       C  
ATOM   2983  C   PHE A 358     -24.997  -7.976 -50.593  1.00 68.08           C  
ANISOU 2983  C   PHE A 358     6428  13699   5740  -1920    153  -1609       C  
ATOM   2984  O   PHE A 358     -24.679  -7.423 -51.643  1.00 68.61           O  
ANISOU 2984  O   PHE A 358     6434  13878   5755  -1820    116  -1562       O  
ATOM   2985  CB  PHE A 358     -25.506  -6.589 -48.584  1.00 66.03           C  
ANISOU 2985  CB  PHE A 358     6211  13311   5565  -1722    128  -1433       C  
ATOM   2986  CG  PHE A 358     -24.671  -5.433 -49.051  1.00 62.64           C  
ANISOU 2986  CG  PHE A 358     5804  12823   5169  -1511     80  -1292       C  
ATOM   2987  CD1 PHE A 358     -23.334  -5.610 -49.366  1.00 59.77           C  
ANISOU 2987  CD1 PHE A 358     5573  12236   4900  -1493     79  -1269       C  
ATOM   2988  CD2 PHE A 358     -25.244  -4.186 -49.244  1.00 61.65           C  
ANISOU 2988  CD2 PHE A 358     5565  12881   4977  -1332     43  -1184       C  
ATOM   2989  CE1 PHE A 358     -22.579  -4.556 -49.835  1.00 59.64           C  
ANISOU 2989  CE1 PHE A 358     5576  12174   4910  -1309     41  -1146       C  
ATOM   2990  CE2 PHE A 358     -24.493  -3.126 -49.701  1.00 59.93           C  
ANISOU 2990  CE2 PHE A 358     5374  12607   4788  -1142     10  -1056       C  
ATOM   2991  CZ  PHE A 358     -23.159  -3.311 -50.001  1.00 59.79           C  
ANISOU 2991  CZ  PHE A 358     5488  12363   4863  -1135      9  -1039       C  
ATOM   2992  N   GLU A 359     -24.389  -9.073 -50.142  1.00 69.20           N  
ANISOU 2992  N   GLU A 359     6714  13603   5975  -2067    205  -1689       N  
ATOM   2993  CA  GLU A 359     -23.347  -9.724 -50.936  1.00 73.06           C  
ANISOU 2993  CA  GLU A 359     7287  13965   6506  -2126    223  -1736       C  
ATOM   2994  C   GLU A 359     -23.839 -10.082 -52.345  1.00 75.58           C  
ANISOU 2994  C   GLU A 359     7460  14569   6686  -2213    225  -1838       C  
ATOM   2995  O   GLU A 359     -23.201  -9.720 -53.339  1.00 77.02           O  
ANISOU 2995  O   GLU A 359     7627  14786   6850  -2133    195  -1801       O  
ATOM   2996  CB  GLU A 359     -22.780 -10.963 -50.237  1.00 74.08           C  
ANISOU 2996  CB  GLU A 359     7582  13818   6744  -2284    292  -1818       C  
ATOM   2997  CG  GLU A 359     -21.585 -11.562 -50.980  1.00 75.70           C  
ANISOU 2997  CG  GLU A 359     7889  13863   7011  -2321    312  -1851       C  
ATOM   2998  CD  GLU A 359     -20.953 -12.747 -50.270  1.00 78.10           C  
ANISOU 2998  CD  GLU A 359     8366  13879   7429  -2454    384  -1916       C  
ATOM   2999  OE1 GLU A 359     -21.631 -13.382 -49.429  1.00 80.04           O  
ANISOU 2999  OE1 GLU A 359     8634  14099   7678  -2575    433  -1980       O  
ATOM   3000  OE2 GLU A 359     -19.770 -13.046 -50.563  1.00 79.27           O  
ANISOU 3000  OE2 GLU A 359     8628  13826   7662  -2435    394  -1901       O  
ATOM   3001  N   LEU A 360     -24.970 -10.782 -52.424  1.00 78.06           N  
ANISOU 3001  N   LEU A 360     7668  15092   6898  -2379    262  -1969       N  
ATOM   3002  CA  LEU A 360     -25.534 -11.182 -53.716  1.00 81.43           C  
ANISOU 3002  CA  LEU A 360     7944  15814   7180  -2483    268  -2082       C  
ATOM   3003  C   LEU A 360     -25.855  -9.967 -54.590  1.00 79.48           C  
ANISOU 3003  C   LEU A 360     7539  15838   6822  -2299    192  -1981       C  
ATOM   3004  O   LEU A 360     -25.466  -9.923 -55.749  1.00 79.76           O  
ANISOU 3004  O   LEU A 360     7529  15974   6801  -2282    175  -1993       O  
ATOM   3005  CB  LEU A 360     -26.773 -12.067 -53.530  1.00 86.42           C  
ANISOU 3005  CB  LEU A 360     8480  16637   7718  -2693    322  -2239       C  
ATOM   3006  CG  LEU A 360     -26.569 -13.563 -53.239  1.00 88.49           C  
ANISOU 3006  CG  LEU A 360     8863  16718   8039  -2934    418  -2394       C  
ATOM   3007  CD1 LEU A 360     -26.008 -13.811 -51.844  1.00 87.96           C  
ANISOU 3007  CD1 LEU A 360     8988  16298   8133  -2925    451  -2340       C  
ATOM   3008  CD2 LEU A 360     -27.882 -14.305 -53.405  1.00 91.20           C  
ANISOU 3008  CD2 LEU A 360     9068  17329   8252  -3139    468  -2558       C  
ATOM   3009  N   LEU A 361     -26.529  -8.973 -54.012  1.00 78.66           N  
ANISOU 3009  N   LEU A 361     7360  15837   6690  -2156    152  -1876       N  
ATOM   3010  CA  LEU A 361     -26.869  -7.737 -54.727  1.00 77.48           C  
ANISOU 3010  CA  LEU A 361     7067  15930   6440  -1959     86  -1761       C  
ATOM   3011  C   LEU A 361     -25.649  -7.026 -55.320  1.00 77.72           C  
ANISOU 3011  C   LEU A 361     7179  15815   6533  -1793     51  -1641       C  
ATOM   3012  O   LEU A 361     -25.670  -6.630 -56.489  1.00 78.68           O  
ANISOU 3012  O   LEU A 361     7196  16144   6554  -1726     19  -1621       O  
ATOM   3013  CB  LEU A 361     -27.646  -6.780 -53.811  1.00 77.40           C  
ANISOU 3013  CB  LEU A 361     7001  15983   6423  -1820     60  -1655       C  
ATOM   3014  CG  LEU A 361     -27.748  -5.291 -54.179  1.00 77.73           C  
ANISOU 3014  CG  LEU A 361     6956  16159   6416  -1562      1  -1486       C  
ATOM   3015  CD1 LEU A 361     -28.486  -5.079 -55.493  1.00 79.87           C  
ANISOU 3015  CD1 LEU A 361     7021  16819   6504  -1541    -27  -1511       C  
ATOM   3016  CD2 LEU A 361     -28.424  -4.509 -53.063  1.00 77.02           C  
ANISOU 3016  CD2 LEU A 361     6847  16066   6350  -1450     -5  -1396       C  
ATOM   3017  N   ILE A 362     -24.597  -6.860 -54.513  1.00 74.89           N  
ANISOU 3017  N   ILE A 362     7006  15111   6338  -1727     57  -1563       N  
ATOM   3018  CA  ILE A 362     -23.428  -6.088 -54.920  1.00 72.89           C  
ANISOU 3018  CA  ILE A 362     6837  14702   6156  -1561     26  -1441       C  
ATOM   3019  C   ILE A 362     -22.663  -6.800 -56.031  1.00 73.05           C  
ANISOU 3019  C   ILE A 362     6885  14705   6165  -1653     40  -1521       C  
ATOM   3020  O   ILE A 362     -22.027  -6.158 -56.863  1.00 73.37           O  
ANISOU 3020  O   ILE A 362     6920  14763   6193  -1528      9  -1444       O  
ATOM   3021  CB  ILE A 362     -22.502  -5.757 -53.705  1.00 73.25           C  
ANISOU 3021  CB  ILE A 362     7068  14388   6374  -1479     31  -1346       C  
ATOM   3022  CG1 ILE A 362     -21.899  -4.346 -53.823  1.00 71.61           C  
ANISOU 3022  CG1 ILE A 362     6883  14122   6203  -1240    -10  -1175       C  
ATOM   3023  CG2 ILE A 362     -21.433  -6.828 -53.494  1.00 71.42           C  
ANISOU 3023  CG2 ILE A 362     7001  13871   6261  -1610     71  -1421       C  
ATOM   3024  CD1 ILE A 362     -20.504  -4.294 -54.406  1.00 71.05           C  
ANISOU 3024  CD1 ILE A 362     6924  13860   6212  -1192    -16  -1138       C  
ATOM   3025  N   LYS A 363     -22.736  -8.129 -56.044  1.00 75.01           N  
ANISOU 3025  N   LYS A 363     7166  14915   6417  -1871     92  -1678       N  
ATOM   3026  CA  LYS A 363     -22.134  -8.920 -57.117  1.00 79.59           C  
ANISOU 3026  CA  LYS A 363     7763  15499   6976  -1983    116  -1776       C  
ATOM   3027  C   LYS A 363     -22.890  -8.751 -58.429  1.00 81.85           C  
ANISOU 3027  C   LYS A 363     7855  16160   7082  -1994     92  -1822       C  
ATOM   3028  O   LYS A 363     -22.303  -8.852 -59.510  1.00 85.78           O  
ANISOU 3028  O   LYS A 363     8344  16699   7547  -1995     87  -1842       O  
ATOM   3029  CB  LYS A 363     -22.070 -10.398 -56.734  1.00 81.85           C  
ANISOU 3029  CB  LYS A 363     8141  15642   7316  -2217    192  -1935       C  
ATOM   3030  CG  LYS A 363     -20.743 -10.821 -56.130  1.00 83.88           C  
ANISOU 3030  CG  LYS A 363     8610  15512   7749  -2218    222  -1908       C  
ATOM   3031  CD  LYS A 363     -20.870 -12.151 -55.408  1.00 85.87           C  
ANISOU 3031  CD  LYS A 363     8958  15609   8060  -2423    302  -2037       C  
ATOM   3032  CE  LYS A 363     -19.531 -12.602 -54.853  1.00 85.48           C  
ANISOU 3032  CE  LYS A 363     9113  15186   8178  -2415    332  -2006       C  
ATOM   3033  NZ  LYS A 363     -19.713 -13.519 -53.693  1.00 86.56           N  
ANISOU 3033  NZ  LYS A 363     9358  15138   8392  -2545    397  -2067       N  
ATOM   3034  N   GLY A 364     -24.196  -8.504 -58.326  1.00 83.52           N  
ANISOU 3034  N   GLY A 364     7908  16652   7172  -2002     77  -1840       N  
ATOM   3035  CA  GLY A 364     -25.039  -8.250 -59.494  1.00 83.63           C  
ANISOU 3035  CA  GLY A 364     7717  17060   6999  -1996     47  -1872       C  
ATOM   3036  C   GLY A 364     -24.762  -6.897 -60.125  1.00 83.78           C  
ANISOU 3036  C   GLY A 364     7679  17175   6977  -1749    -15  -1703       C  
ATOM   3037  O   GLY A 364     -24.817  -6.752 -61.346  1.00 86.67           O  
ANISOU 3037  O   GLY A 364     7937  17766   7224  -1729    -37  -1715       O  
ATOM   3038  N   VAL A 365     -24.453  -5.906 -59.291  1.00 80.12           N  
ANISOU 3038  N   VAL A 365     7293  16538   6609  -1564    -39  -1548       N  
ATOM   3039  CA  VAL A 365     -24.166  -4.554 -59.768  1.00 79.46           C  
ANISOU 3039  CA  VAL A 365     7176  16512   6503  -1319    -88  -1376       C  
ATOM   3040  C   VAL A 365     -22.759  -4.443 -60.360  1.00 80.77           C  
ANISOU 3040  C   VAL A 365     7469  16464   6753  -1263    -90  -1330       C  
ATOM   3041  O   VAL A 365     -22.583  -3.939 -61.468  1.00 85.09           O  
ANISOU 3041  O   VAL A 365     7945  17169   7216  -1171   -116  -1280       O  
ATOM   3042  CB  VAL A 365     -24.342  -3.507 -58.645  1.00 76.11           C  
ANISOU 3042  CB  VAL A 365     6794  15971   6153  -1144   -103  -1231       C  
ATOM   3043  CG1 VAL A 365     -24.014  -2.106 -59.149  1.00 74.10           C  
ANISOU 3043  CG1 VAL A 365     6517  15758   5879   -892   -139  -1053       C  
ATOM   3044  CG2 VAL A 365     -25.757  -3.562 -58.093  1.00 75.52           C  
ANISOU 3044  CG2 VAL A 365     6583  16120   5988  -1188   -101  -1272       C  
ATOM   3045  N   TYR A 366     -21.765  -4.926 -59.618  1.00 81.01           N  
ANISOU 3045  N   TYR A 366     7685  16145   6948  -1320    -60  -1346       N  
ATOM   3046  CA  TYR A 366     -20.359  -4.691 -59.952  1.00 79.09           C  
ANISOU 3046  CA  TYR A 366     7577  15662   6809  -1244    -63  -1283       C  
ATOM   3047  C   TYR A 366     -19.595  -5.988 -60.224  1.00 78.91           C  
ANISOU 3047  C   TYR A 366     7653  15479   6847  -1433    -20  -1421       C  
ATOM   3048  O   TYR A 366     -20.035  -7.077 -59.845  1.00 77.34           O  
ANISOU 3048  O   TYR A 366     7461  15275   6650  -1622     19  -1555       O  
ATOM   3049  CB  TYR A 366     -19.659  -3.939 -58.809  1.00 76.25           C  
ANISOU 3049  CB  TYR A 366     7363  15004   6604  -1106    -67  -1154       C  
ATOM   3050  CG  TYR A 366     -20.199  -2.553 -58.488  1.00 75.99           C  
ANISOU 3050  CG  TYR A 366     7265  15068   6537   -898    -98  -1001       C  
ATOM   3051  CD1 TYR A 366     -20.020  -1.488 -59.369  1.00 74.59           C  
ANISOU 3051  CD1 TYR A 366     7031  15009   6298   -720   -126   -884       C  
ATOM   3052  CD2 TYR A 366     -20.838  -2.296 -57.270  1.00 74.27           C  
ANISOU 3052  CD2 TYR A 366     7056  14804   6358   -876    -93   -970       C  
ATOM   3053  CE1 TYR A 366     -20.495  -0.219 -59.063  1.00 74.27           C  
ANISOU 3053  CE1 TYR A 366     6942  15042   6233   -524   -143   -741       C  
ATOM   3054  CE2 TYR A 366     -21.307  -1.027 -56.957  1.00 72.86           C  
ANISOU 3054  CE2 TYR A 366     6827  14700   6156   -684   -113   -832       C  
ATOM   3055  CZ  TYR A 366     -21.132   0.005 -57.858  1.00 72.91           C  
ANISOU 3055  CZ  TYR A 366     6778  14822   6101   -507   -136   -717       C  
ATOM   3056  OH  TYR A 366     -21.591   1.265 -57.558  1.00 74.17           O  
ANISOU 3056  OH  TYR A 366     6895  15046   6240   -311   -145   -577       O  
ATOM   3057  N   GLN A 367     -18.445  -5.860 -60.881  1.00 80.66           N  
ANISOU 3057  N   GLN A 367     7955  15569   7122  -1381    -23  -1386       N  
ATOM   3058  CA  GLN A 367     -17.435  -6.909 -60.852  1.00 83.77           C  
ANISOU 3058  CA  GLN A 367     8490  15714   7624  -1515     19  -1478       C  
ATOM   3059  C   GLN A 367     -16.591  -6.695 -59.603  1.00 84.80           C  
ANISOU 3059  C   GLN A 367     8790  15499   7929  -1447     25  -1397       C  
ATOM   3060  O   GLN A 367     -16.082  -5.591 -59.368  1.00 85.35           O  
ANISOU 3060  O   GLN A 367     8900  15476   8050  -1265     -6  -1255       O  
ATOM   3061  CB  GLN A 367     -16.555  -6.861 -62.101  1.00 84.46           C  
ANISOU 3061  CB  GLN A 367     8585  15815   7691  -1487     13  -1477       C  
ATOM   3062  CG  GLN A 367     -16.174  -8.232 -62.650  1.00 87.20           C  
ANISOU 3062  CG  GLN A 367     8973  16112   8045  -1691     66  -1640       C  
ATOM   3063  CD  GLN A 367     -17.267  -8.847 -63.522  1.00 89.68           C  
ANISOU 3063  CD  GLN A 367     9124  16759   8188  -1838     78  -1775       C  
ATOM   3064  OE1 GLN A 367     -18.350  -9.187 -63.039  1.00 89.73           O  
ANISOU 3064  OE1 GLN A 367     9054  16901   8135  -1929     90  -1839       O  
ATOM   3065  NE2 GLN A 367     -16.981  -8.998 -64.812  1.00 87.57           N  
ANISOU 3065  NE2 GLN A 367     8801  16630   7839  -1866     78  -1821       N  
ATOM   3066  N   VAL A 368     -16.469  -7.739 -58.786  1.00 85.05           N  
ANISOU 3066  N   VAL A 368     8919  15348   8046  -1594     70  -1488       N  
ATOM   3067  CA  VAL A 368     -15.814  -7.623 -57.481  1.00 82.52           C  
ANISOU 3067  CA  VAL A 368     8749  14723   7879  -1544     77  -1420       C  
ATOM   3068  C   VAL A 368     -14.745  -8.696 -57.263  1.00 83.77           C  
ANISOU 3068  C   VAL A 368     9062  14607   8159  -1654    125  -1491       C  
ATOM   3069  O   VAL A 368     -14.916  -9.839 -57.680  1.00 86.97           O  
ANISOU 3069  O   VAL A 368     9463  15046   8535  -1826    172  -1628       O  
ATOM   3070  CB  VAL A 368     -16.841  -7.654 -56.323  1.00 78.60           C  
ANISOU 3070  CB  VAL A 368     8227  14259   7377  -1579     83  -1425       C  
ATOM   3071  CG1 VAL A 368     -17.880  -6.557 -56.499  1.00 77.66           C  
ANISOU 3071  CG1 VAL A 368     7957  14406   7143  -1455     39  -1346       C  
ATOM   3072  CG2 VAL A 368     -17.508  -9.016 -56.214  1.00 78.37           C  
ANISOU 3072  CG2 VAL A 368     8182  14279   7312  -1802    139  -1588       C  
ATOM   3073  N   ASN A 369     -13.647  -8.321 -56.611  1.00 82.49           N  
ANISOU 3073  N   ASN A 369     9033  14177   8129  -1554    115  -1399       N  
ATOM   3074  CA  ASN A 369     -12.590  -9.278 -56.266  1.00 84.73           C  
ANISOU 3074  CA  ASN A 369     9468  14188   8537  -1635    159  -1449       C  
ATOM   3075  C   ASN A 369     -13.025 -10.208 -55.132  1.00 85.09           C  
ANISOU 3075  C   ASN A 369     9580  14118   8633  -1763    204  -1516       C  
ATOM   3076  O   ASN A 369     -12.890  -9.855 -53.962  1.00 81.18           O  
ANISOU 3076  O   ASN A 369     9155  13472   8216  -1698    193  -1440       O  
ATOM   3077  CB  ASN A 369     -11.304  -8.548 -55.863  1.00 83.36           C  
ANISOU 3077  CB  ASN A 369     9407  13780   8483  -1484    132  -1327       C  
ATOM   3078  CG  ASN A 369     -10.804  -7.601 -56.935  1.00 85.70           C  
ANISOU 3078  CG  ASN A 369     9653  14167   8739  -1355     94  -1255       C  
ATOM   3079  OD1 ASN A 369     -11.026  -7.820 -58.125  1.00 88.57           O  
ANISOU 3079  OD1 ASN A 369     9933  14709   9009  -1402     98  -1315       O  
ATOM   3080  ND2 ASN A 369     -10.115  -6.541 -56.515  1.00 83.76           N  
ANISOU 3080  ND2 ASN A 369     9460  13800   8563  -1195     62  -1127       N  
ATOM   3081  N   PRO A 370     -13.528 -11.414 -55.476  1.00 88.06           N  
ANISOU 3081  N   PRO A 370     9936  14558   8962  -1949    262  -1661       N  
ATOM   3082  CA  PRO A 370     -14.182 -12.277 -54.484  1.00 88.43           C  
ANISOU 3082  CA  PRO A 370    10025  14542   9032  -2082    313  -1733       C  
ATOM   3083  C   PRO A 370     -13.221 -12.913 -53.465  1.00 87.32           C  
ANISOU 3083  C   PRO A 370    10064  14070   9041  -2098    351  -1715       C  
ATOM   3084  O   PRO A 370     -13.667 -13.373 -52.408  1.00 90.22           O  
ANISOU 3084  O   PRO A 370    10481  14355   9443  -2164    383  -1733       O  
ATOM   3085  CB  PRO A 370     -14.851 -13.350 -55.344  1.00 87.90           C  
ANISOU 3085  CB  PRO A 370     9888  14639   8870  -2277    371  -1898       C  
ATOM   3086  CG  PRO A 370     -13.982 -13.447 -56.551  1.00 87.72           C  
ANISOU 3086  CG  PRO A 370     9871  14614   8843  -2264    372  -1919       C  
ATOM   3087  CD  PRO A 370     -13.400 -12.081 -56.788  1.00 86.60           C  
ANISOU 3087  CD  PRO A 370     9707  14483   8712  -2052    293  -1769       C  
ATOM   3088  N   THR A 371     -11.925 -12.936 -53.777  1.00 84.13           N  
ANISOU 3088  N   THR A 371     9753  13489   8724  -2035    350  -1677       N  
ATOM   3089  CA  THR A 371     -10.915 -13.412 -52.828  1.00 81.37           C  
ANISOU 3089  CA  THR A 371     9566  12834   8514  -2021    377  -1640       C  
ATOM   3090  C   THR A 371     -10.583 -12.317 -51.816  1.00 80.79           C  
ANISOU 3090  C   THR A 371     9528  12663   8503  -1857    317  -1495       C  
ATOM   3091  O   THR A 371     -10.090 -12.600 -50.720  1.00 80.80           O  
ANISOU 3091  O   THR A 371     9644  12452   8602  -1845    332  -1457       O  
ATOM   3092  CB  THR A 371      -9.608 -13.861 -53.527  1.00 82.33           C  
ANISOU 3092  CB  THR A 371     9772  12802   8706  -2012    400  -1655       C  
ATOM   3093  OG1 THR A 371      -8.791 -12.716 -53.823  1.00 80.06           O  
ANISOU 3093  OG1 THR A 371     9477  12497   8445  -1840    333  -1539       O  
ATOM   3094  CG2 THR A 371      -9.904 -14.644 -54.813  1.00 81.34           C  
ANISOU 3094  CG2 THR A 371     9585  12819   8499  -2148    447  -1789       C  
ATOM   3095  N   LYS A 372     -10.852 -11.068 -52.195  1.00 78.64           N  
ANISOU 3095  N   LYS A 372     9158  12548   8172  -1730    253  -1415       N  
ATOM   3096  CA  LYS A 372     -10.584  -9.919 -51.335  1.00 75.42           C  
ANISOU 3096  CA  LYS A 372     8775  12066   7814  -1573    201  -1282       C  
ATOM   3097  C   LYS A 372     -11.790  -9.549 -50.468  1.00 70.96           C  
ANISOU 3097  C   LYS A 372     8149  11609   7201  -1577    190  -1264       C  
ATOM   3098  O   LYS A 372     -11.771  -8.543 -49.747  1.00 69.43           O  
ANISOU 3098  O   LYS A 372     7961  11383   7035  -1453    152  -1160       O  
ATOM   3099  CB  LYS A 372     -10.104  -8.715 -52.158  1.00 80.38           C  
ANISOU 3099  CB  LYS A 372     9349  12772   8418  -1422    149  -1194       C  
ATOM   3100  CG  LYS A 372      -8.617  -8.749 -52.497  1.00 83.04           C  
ANISOU 3100  CG  LYS A 372     9781  12921   8846  -1367    148  -1163       C  
ATOM   3101  CD  LYS A 372      -7.979  -7.378 -52.337  1.00 83.33           C  
ANISOU 3101  CD  LYS A 372     9829  12912   8920  -1189     98  -1032       C  
ATOM   3102  CE  LYS A 372      -6.504  -7.500 -51.989  1.00 85.35           C  
ANISOU 3102  CE  LYS A 372    10211  12918   9299  -1144    102   -994       C  
ATOM   3103  NZ  LYS A 372      -5.962  -6.251 -51.382  1.00 82.87           N  
ANISOU 3103  NZ  LYS A 372     9927  12523   9036   -994     63   -872       N  
ATOM   3104  N   THR A 373     -12.828 -10.374 -50.526  1.00 65.81           N  
ANISOU 3104  N   THR A 373     7442  11082   6478  -1723    230  -1370       N  
ATOM   3105  CA  THR A 373     -13.980 -10.188 -49.663  1.00 65.08           C  
ANISOU 3105  CA  THR A 373     7298  11085   6344  -1747    228  -1368       C  
ATOM   3106  C   THR A 373     -13.669 -10.631 -48.235  1.00 63.49           C  
ANISOU 3106  C   THR A 373     7227  10650   6246  -1772    254  -1345       C  
ATOM   3107  O   THR A 373     -13.040 -11.669 -48.024  1.00 65.59           O  
ANISOU 3107  O   THR A 373     7603  10736   6581  -1860    303  -1396       O  
ATOM   3108  CB  THR A 373     -15.199 -10.949 -50.191  1.00 63.65           C  
ANISOU 3108  CB  THR A 373     7010  11123   6049  -1906    266  -1498       C  
ATOM   3109  OG1 THR A 373     -15.501 -10.486 -51.509  1.00 63.48           O  
ANISOU 3109  OG1 THR A 373     6858  11337   5921  -1875    237  -1512       O  
ATOM   3110  CG2 THR A 373     -16.390 -10.710 -49.298  1.00 61.71           C  
ANISOU 3110  CG2 THR A 373     6704  10983   5758  -1926    264  -1493       C  
ATOM   3111  N   ARG A 374     -14.095  -9.824 -47.264  1.00 59.42           N  
ANISOU 3111  N   ARG A 374     6700  10137   5738  -1689    224  -1265       N  
ATOM   3112  CA  ARG A 374     -13.934 -10.155 -45.852  1.00 58.20           C  
ANISOU 3112  CA  ARG A 374     6656   9789   5666  -1709    244  -1239       C  
ATOM   3113  C   ARG A 374     -15.271 -10.087 -45.129  1.00 56.86           C  
ANISOU 3113  C   ARG A 374     6419   9750   5435  -1761    254  -1261       C  
ATOM   3114  O   ARG A 374     -15.968  -9.072 -45.189  1.00 56.57           O  
ANISOU 3114  O   ARG A 374     6277   9880   5335  -1674    214  -1211       O  
ATOM   3115  CB  ARG A 374     -12.921  -9.217 -45.177  1.00 58.46           C  
ANISOU 3115  CB  ARG A 374     6768   9653   5789  -1551    201  -1111       C  
ATOM   3116  CG  ARG A 374     -11.521  -9.254 -45.780  1.00 59.37           C  
ANISOU 3116  CG  ARG A 374     6955   9627   5973  -1495    191  -1085       C  
ATOM   3117  CD  ARG A 374     -10.868 -10.620 -45.612  1.00 61.16           C  
ANISOU 3117  CD  ARG A 374     7296   9672   6267  -1607    246  -1152       C  
ATOM   3118  NE  ARG A 374      -9.474 -10.624 -46.058  1.00 62.07           N  
ANISOU 3118  NE  ARG A 374     7486   9641   6457  -1542    237  -1118       N  
ATOM   3119  CZ  ARG A 374      -9.069 -10.972 -47.280  1.00 62.26           C  
ANISOU 3119  CZ  ARG A 374     7487   9706   6461  -1570    249  -1170       C  
ATOM   3120  NH1 ARG A 374      -9.946 -11.353 -48.198  1.00 61.99           N  
ANISOU 3120  NH1 ARG A 374     7357   9861   6332  -1665    271  -1262       N  
ATOM   3121  NH2 ARG A 374      -7.779 -10.937 -47.583  1.00 61.91           N  
ANISOU 3121  NH2 ARG A 374     7512   9520   6489  -1505    241  -1134       N  
ATOM   3122  N   THR A 375     -15.616 -11.172 -44.440  1.00 56.04           N  
ANISOU 3122  N   THR A 375     6376   9564   5349  -1901    311  -1334       N  
ATOM   3123  CA  THR A 375     -16.907 -11.295 -43.762  1.00 56.59           C  
ANISOU 3123  CA  THR A 375     6387   9754   5360  -1979    331  -1374       C  
ATOM   3124  C   THR A 375     -16.787 -12.232 -42.567  1.00 56.82           C  
ANISOU 3124  C   THR A 375     6545   9581   5461  -2074    387  -1397       C  
ATOM   3125  O   THR A 375     -15.860 -13.036 -42.503  1.00 55.92           O  
ANISOU 3125  O   THR A 375     6553   9270   5424  -2113    422  -1411       O  
ATOM   3126  CB  THR A 375     -18.002 -11.829 -44.720  1.00 58.13           C  
ANISOU 3126  CB  THR A 375     6452  10198   5436  -2111    361  -1497       C  
ATOM   3127  OG1 THR A 375     -19.222 -12.016 -43.997  1.00 58.85           O  
ANISOU 3127  OG1 THR A 375     6490  10396   5474  -2196    386  -1541       O  
ATOM   3128  CG2 THR A 375     -17.585 -13.156 -45.335  1.00 58.81           C  
ANISOU 3128  CG2 THR A 375     6602  10203   5539  -2261    427  -1609       C  
ATOM   3129  N   ASN A 376     -17.722 -12.117 -41.621  1.00 57.99           N  
ANISOU 3129  N   ASN A 376     6669   9780   5582  -2105    396  -1395       N  
ATOM   3130  CA  ASN A 376     -17.808 -13.056 -40.495  1.00 59.53           C  
ANISOU 3130  CA  ASN A 376     6977   9812   5828  -2210    456  -1425       C  
ATOM   3131  C   ASN A 376     -18.972 -14.049 -40.628  1.00 62.72           C  
ANISOU 3131  C   ASN A 376     7329  10341   6157  -2401    527  -1559       C  
ATOM   3132  O   ASN A 376     -19.292 -14.771 -39.675  1.00 64.87           O  
ANISOU 3132  O   ASN A 376     7679  10513   6455  -2498    583  -1589       O  
ATOM   3133  CB  ASN A 376     -17.900 -12.310 -39.158  1.00 57.55           C  
ANISOU 3133  CB  ASN A 376     6761   9488   5615  -2118    425  -1327       C  
ATOM   3134  CG  ASN A 376     -19.146 -11.444 -39.051  1.00 56.97           C  
ANISOU 3134  CG  ASN A 376     6546   9644   5453  -2088    396  -1320       C  
ATOM   3135  OD1 ASN A 376     -19.678 -10.969 -40.059  1.00 57.76           O  
ANISOU 3135  OD1 ASN A 376     6514   9959   5472  -2065    370  -1344       O  
ATOM   3136  ND2 ASN A 376     -19.600 -11.209 -37.823  1.00 55.20           N  
ANISOU 3136  ND2 ASN A 376     6349   9378   5244  -2080    400  -1283       N  
ATOM   3137  N   LEU A 377     -19.607 -14.067 -41.801  1.00 65.32           N  
ANISOU 3137  N   LEU A 377     7528  10897   6391  -2456    526  -1640       N  
ATOM   3138  CA  LEU A 377     -20.704 -15.006 -42.083  1.00 68.02           C  
ANISOU 3138  CA  LEU A 377     7807  11385   6651  -2649    595  -1782       C  
ATOM   3139  C   LEU A 377     -20.223 -16.458 -42.018  1.00 69.86           C  
ANISOU 3139  C   LEU A 377     8177  11424   6943  -2802    690  -1870       C  
ATOM   3140  O   LEU A 377     -19.263 -16.826 -42.700  1.00 69.00           O  
ANISOU 3140  O   LEU A 377     8131  11205   6879  -2792    701  -1877       O  
ATOM   3141  CB  LEU A 377     -21.333 -14.712 -43.449  1.00 66.48           C  
ANISOU 3141  CB  LEU A 377     7442  11477   6338  -2669    571  -1848       C  
ATOM   3142  CG  LEU A 377     -22.166 -13.434 -43.565  1.00 65.53           C  
ANISOU 3142  CG  LEU A 377     7162  11603   6133  -2549    497  -1786       C  
ATOM   3143  CD1 LEU A 377     -22.390 -13.076 -45.022  1.00 64.41           C  
ANISOU 3143  CD1 LEU A 377     6875  11704   5891  -2527    463  -1821       C  
ATOM   3144  CD2 LEU A 377     -23.488 -13.556 -42.820  1.00 66.18           C  
ANISOU 3144  CD2 LEU A 377     7173  11820   6152  -2638    525  -1836       C  
ATOM   3145  N   PRO A 378     -20.891 -17.287 -41.191  1.00 73.30           N  
ANISOU 3145  N   PRO A 378     8662  11810   7377  -2942    765  -1935       N  
ATOM   3146  CA  PRO A 378     -20.436 -18.658 -40.932  1.00 76.41           C  
ANISOU 3146  CA  PRO A 378     9208  11986   7836  -3077    867  -2002       C  
ATOM   3147  C   PRO A 378     -20.505 -19.591 -42.148  1.00 80.05           C  
ANISOU 3147  C   PRO A 378     9644  12516   8253  -3226    935  -2143       C  
ATOM   3148  O   PRO A 378     -19.868 -20.647 -42.140  1.00 82.02           O  
ANISOU 3148  O   PRO A 378    10029  12564   8570  -3309   1018  -2186       O  
ATOM   3149  CB  PRO A 378     -21.385 -19.141 -39.824  1.00 77.05           C  
ANISOU 3149  CB  PRO A 378     9315  12056   7901  -3191    928  -2041       C  
ATOM   3150  CG  PRO A 378     -21.920 -17.891 -39.203  1.00 75.90           C  
ANISOU 3150  CG  PRO A 378     9076  12035   7724  -3062    841  -1947       C  
ATOM   3151  CD  PRO A 378     -22.045 -16.931 -40.349  1.00 75.22           C  
ANISOU 3151  CD  PRO A 378     8834  12177   7566  -2966    761  -1934       C  
ATOM   3152  N   THR A 379     -21.249 -19.197 -43.183  1.00 81.92           N  
ANISOU 3152  N   THR A 379     9712  13035   8379  -3256    904  -2210       N  
ATOM   3153  CA  THR A 379     -21.386 -20.021 -44.390  1.00 85.84           C  
ANISOU 3153  CA  THR A 379    10167  13630   8819  -3405    965  -2352       C  
ATOM   3154  C   THR A 379     -20.180 -19.934 -45.323  1.00 83.99           C  
ANISOU 3154  C   THR A 379     9973  13307   8631  -3318    938  -2319       C  
ATOM   3155  O   THR A 379     -20.008 -20.788 -46.196  1.00 84.42           O  
ANISOU 3155  O   THR A 379    10042  13361   8670  -3441   1005  -2431       O  
ATOM   3156  CB  THR A 379     -22.657 -19.675 -45.192  1.00 88.73           C  
ANISOU 3156  CB  THR A 379    10324  14355   9033  -3477    942  -2443       C  
ATOM   3157  OG1 THR A 379     -22.655 -18.277 -45.516  1.00 88.77           O  
ANISOU 3157  OG1 THR A 379    10209  14520   8998  -3286    823  -2332       O  
ATOM   3158  CG2 THR A 379     -23.918 -20.035 -44.394  1.00 88.94           C  
ANISOU 3158  CG2 THR A 379    10308  14478   9005  -3611    994  -2515       C  
ATOM   3159  N   HIS A 380     -19.360 -18.900 -45.145  1.00 82.59           N  
ANISOU 3159  N   HIS A 380     9813  13058   8510  -3113    844  -2172       N  
ATOM   3160  CA  HIS A 380     -18.153 -18.716 -45.961  1.00 83.75           C  
ANISOU 3160  CA  HIS A 380     9999  13113   8706  -3016    813  -2128       C  
ATOM   3161  C   HIS A 380     -17.076 -19.694 -45.597  1.00 83.78           C  
ANISOU 3161  C   HIS A 380    10190  12812   8829  -3047    884  -2127       C  
ATOM   3162  O   HIS A 380     -17.094 -20.278 -44.508  1.00 83.75           O  
ANISOU 3162  O   HIS A 380    10300  12636   8886  -3093    939  -2116       O  
ATOM   3163  CB  HIS A 380     -17.626 -17.291 -45.832  1.00 83.62           C  
ANISOU 3163  CB  HIS A 380     9946  13112   8714  -2792    698  -1973       C  
ATOM   3164  CG  HIS A 380     -18.274 -16.312 -46.782  1.00 85.92           C  
ANISOU 3164  CG  HIS A 380    10055  13700   8891  -2730    627  -1969       C  
ATOM   3165  ND1 HIS A 380     -17.587 -15.692 -47.764  1.00 85.58           N  
ANISOU 3165  ND1 HIS A 380     9972  13705   8840  -2621    572  -1924       N  
ATOM   3166  CD2 HIS A 380     -19.592 -15.852 -46.871  1.00 86.02           C  
ANISOU 3166  CD2 HIS A 380     9911  13984   8787  -2759    604  -2002       C  
ATOM   3167  CE1 HIS A 380     -18.420 -14.882 -48.449  1.00 86.38           C  
ANISOU 3167  CE1 HIS A 380     9903  14091   8825  -2579    519  -1924       C  
ATOM   3168  NE2 HIS A 380     -19.645 -14.980 -47.901  1.00 86.44           N  
ANISOU 3168  NE2 HIS A 380     9837  14238   8766  -2660    537  -1971       N  
ATOM   3169  N   ARG A 381     -16.131 -19.885 -46.517  1.00 86.39           N  
ANISOU 3169  N   ARG A 381    10552  13078   9191  -3019    887  -2137       N  
ATOM   3170  CA  ARG A 381     -14.976 -20.755 -46.293  1.00 88.94           C  
ANISOU 3170  CA  ARG A 381    11049  13114   9631  -3026    951  -2126       C  
ATOM   3171  C   ARG A 381     -14.282 -20.381 -44.992  1.00 89.19           C  
ANISOU 3171  C   ARG A 381    11192  12930   9762  -2889    915  -1984       C  
ATOM   3172  O   ARG A 381     -14.241 -21.175 -44.046  1.00 87.87           O  
ANISOU 3172  O   ARG A 381    11147  12585   9654  -2949    986  -1987       O  
ATOM   3173  CB  ARG A 381     -13.982 -20.637 -47.454  1.00 91.21           C  
ANISOU 3173  CB  ARG A 381    11332  13386   9936  -2963    928  -2124       C  
ATOM   3174  CG  ARG A 381     -14.438 -21.269 -48.760  1.00 96.64           C  
ANISOU 3174  CG  ARG A 381    11942  14237  10539  -3115    985  -2277       C  
ATOM   3175  CD  ARG A 381     -13.829 -20.540 -49.950  1.00 97.37           C  
ANISOU 3175  CD  ARG A 381    11955  14437  10603  -3012    913  -2248       C  
ATOM   3176  NE  ARG A 381     -13.874 -21.328 -51.181  1.00101.97           N  
ANISOU 3176  NE  ARG A 381    12507  15101  11135  -3151    980  -2388       N  
ATOM   3177  CZ  ARG A 381     -14.936 -21.431 -51.980  1.00104.59           C  
ANISOU 3177  CZ  ARG A 381    12700  15701  11338  -3277    994  -2506       C  
ATOM   3178  NH1 ARG A 381     -16.071 -20.809 -51.678  1.00104.90           N  
ANISOU 3178  NH1 ARG A 381    12613  15956  11286  -3278    946  -2498       N  
ATOM   3179  NH2 ARG A 381     -14.865 -22.169 -53.083  1.00104.36           N  
ANISOU 3179  NH2 ARG A 381    12653  15730  11267  -3404   1059  -2635       N  
ATOM   3180  N   HIS A 382     -13.761 -19.154 -44.948  1.00 88.36           N  
ANISOU 3180  N   HIS A 382    11044  12853   9673  -2707    809  -1862       N  
ATOM   3181  CA  HIS A 382     -13.005 -18.665 -43.801  1.00 85.62           C  
ANISOU 3181  CA  HIS A 382    10793  12322   9417  -2567    765  -1725       C  
ATOM   3182  C   HIS A 382     -13.575 -17.372 -43.270  1.00 80.97           C  
ANISOU 3182  C   HIS A 382    10108  11869   8786  -2458    675  -1639       C  
ATOM   3183  O   HIS A 382     -13.085 -16.284 -43.607  1.00 76.52           O  
ANISOU 3183  O   HIS A 382     9493  11355   8225  -2312    592  -1556       O  
ATOM   3184  CB  HIS A 382     -11.529 -18.505 -44.165  1.00 89.31           C  
ANISOU 3184  CB  HIS A 382    11333  12631   9969  -2447    736  -1655       C  
ATOM   3185  CG  HIS A 382     -10.904 -19.756 -44.744  1.00 95.97           C  
ANISOU 3185  CG  HIS A 382    12271  13335  10857  -2542    828  -1737       C  
ATOM   3186  ND1 HIS A 382     -10.627 -19.890 -46.059  1.00 98.55           N  
ANISOU 3186  ND1 HIS A 382    12549  13741  11155  -2570    835  -1803       N  
ATOM   3187  CD2 HIS A 382     -10.517 -20.953 -44.139  1.00 97.69           C  
ANISOU 3187  CD2 HIS A 382    12636  13333  11149  -2616    923  -1760       C  
ATOM   3188  CE1 HIS A 382     -10.086 -21.102 -46.283  1.00 98.51           C  
ANISOU 3188  CE1 HIS A 382    12653  13571  11205  -2659    932  -1870       C  
ATOM   3189  NE2 HIS A 382     -10.019 -21.752 -45.109  1.00100.85           N  
ANISOU 3189  NE2 HIS A 382    13071  13682  11565  -2684    988  -1841       N  
ATOM   3190  N   PRO A 383     -14.633 -17.471 -42.436  1.00 78.21           N  
ANISOU 3190  N   PRO A 383     9737  11580   8398  -2529    697  -1661       N  
ATOM   3191  CA  PRO A 383     -15.223 -16.305 -41.771  1.00 77.03           C  
ANISOU 3191  CA  PRO A 383     9509  11542   8215  -2430    623  -1579       C  
ATOM   3192  C   PRO A 383     -14.228 -15.594 -40.849  1.00 74.68           C  
ANISOU 3192  C   PRO A 383     9298  11068   8007  -2269    568  -1440       C  
ATOM   3193  O   PRO A 383     -13.337 -16.233 -40.281  1.00 74.03           O  
ANISOU 3193  O   PRO A 383     9352  10763   8012  -2264    601  -1410       O  
ATOM   3194  CB  PRO A 383     -16.376 -16.905 -40.954  1.00 78.20           C  
ANISOU 3194  CB  PRO A 383     9656  11730   8324  -2564    683  -1643       C  
ATOM   3195  CG  PRO A 383     -16.053 -18.355 -40.823  1.00 78.77           C  
ANISOU 3195  CG  PRO A 383     9858  11622   8446  -2701    787  -1719       C  
ATOM   3196  CD  PRO A 383     -15.347 -18.713 -42.093  1.00 78.77           C  
ANISOU 3196  CD  PRO A 383     9857  11617   8454  -2714    801  -1769       C  
ATOM   3197  N   GLN A 384     -14.408 -14.283 -40.693  1.00 72.84           N  
ANISOU 3197  N   GLN A 384     8983  10940   7750  -2139    488  -1356       N  
ATOM   3198  CA  GLN A 384     -13.414 -13.422 -40.063  1.00 69.04           C  
ANISOU 3198  CA  GLN A 384     8562  10325   7343  -1980    429  -1230       C  
ATOM   3199  C   GLN A 384     -14.083 -12.300 -39.280  1.00 66.07           C  
ANISOU 3199  C   GLN A 384     8122  10042   6937  -1897    379  -1161       C  
ATOM   3200  O   GLN A 384     -14.933 -11.593 -39.813  1.00 65.97           O  
ANISOU 3200  O   GLN A 384     7981  10237   6844  -1876    350  -1172       O  
ATOM   3201  CB  GLN A 384     -12.520 -12.817 -41.137  1.00 68.35           C  
ANISOU 3201  CB  GLN A 384     8445  10256   7268  -1877    382  -1196       C  
ATOM   3202  CG  GLN A 384     -11.054 -12.812 -40.779  1.00 72.18           C  
ANISOU 3202  CG  GLN A 384     9048  10520   7857  -1786    366  -1120       C  
ATOM   3203  CD  GLN A 384     -10.186 -12.315 -41.916  1.00 72.73           C  
ANISOU 3203  CD  GLN A 384     9087  10609   7936  -1701    330  -1100       C  
ATOM   3204  OE1 GLN A 384      -9.453 -13.087 -42.530  1.00 74.43           O  
ANISOU 3204  OE1 GLN A 384     9356  10735   8187  -1739    362  -1140       O  
ATOM   3205  NE2 GLN A 384     -10.267 -11.017 -42.204  1.00 71.41           N  
ANISOU 3205  NE2 GLN A 384     8837  10557   7738  -1584    267  -1036       N  
ATOM   3206  N   ASP A 385     -13.677 -12.122 -38.025  1.00 64.19           N  
ANISOU 3206  N   ASP A 385     7974   9652   6761  -1845    370  -1086       N  
ATOM   3207  CA  ASP A 385     -14.214 -11.047 -37.181  1.00 62.22           C  
ANISOU 3207  CA  ASP A 385     7679   9467   6493  -1763    328  -1016       C  
ATOM   3208  C   ASP A 385     -13.675  -9.655 -37.533  1.00 58.84           C  
ANISOU 3208  C   ASP A 385     7202   9079   6074  -1600    258   -928       C  
ATOM   3209  O   ASP A 385     -14.374  -8.648 -37.381  1.00 57.29           O  
ANISOU 3209  O   ASP A 385     6921   9012   5832  -1534    228   -892       O  
ATOM   3210  CB  ASP A 385     -13.959 -11.348 -35.706  1.00 62.96           C  
ANISOU 3210  CB  ASP A 385     7886   9389   6646  -1770    345   -971       C  
ATOM   3211  CG  ASP A 385     -15.041 -12.209 -35.094  1.00 65.33           C  
ANISOU 3211  CG  ASP A 385     8192   9720   6907  -1912    406  -1041       C  
ATOM   3212  OD1 ASP A 385     -16.028 -12.527 -35.798  1.00 67.55           O  
ANISOU 3212  OD1 ASP A 385     8382  10168   7114  -2007    433  -1130       O  
ATOM   3213  OD2 ASP A 385     -14.911 -12.557 -33.904  1.00 65.78           O  
ANISOU 3213  OD2 ASP A 385     8344   9645   7005  -1930    428  -1009       O  
ATOM   3214  N   GLU A 386     -12.438  -9.605 -38.006  1.00 55.52           N  
ANISOU 3214  N   GLU A 386     6837   8544   5712  -1535    240   -894       N  
ATOM   3215  CA  GLU A 386     -11.765  -8.336 -38.212  1.00 53.91           C  
ANISOU 3215  CA  GLU A 386     6611   8341   5530  -1384    183   -807       C  
ATOM   3216  C   GLU A 386     -11.809  -7.950 -39.674  1.00 53.21           C  
ANISOU 3216  C   GLU A 386     6429   8396   5392  -1351    165   -829       C  
ATOM   3217  O   GLU A 386     -11.397  -8.719 -40.551  1.00 55.12           O  
ANISOU 3217  O   GLU A 386     6683   8621   5636  -1409    186   -885       O  
ATOM   3218  CB  GLU A 386     -10.329  -8.390 -37.685  1.00 53.11           C  
ANISOU 3218  CB  GLU A 386     6628   8026   5525  -1322    170   -746       C  
ATOM   3219  CG  GLU A 386     -10.251  -8.930 -36.268  1.00 55.08           C  
ANISOU 3219  CG  GLU A 386     6974   8136   5817  -1362    192   -727       C  
ATOM   3220  CD  GLU A 386      -9.098  -8.370 -35.465  1.00 58.31           C  
ANISOU 3220  CD  GLU A 386     7461   8395   6299  -1259    158   -639       C  
ATOM   3221  OE1 GLU A 386      -7.945  -8.412 -35.964  1.00 59.88           O  
ANISOU 3221  OE1 GLU A 386     7699   8505   6546  -1209    144   -619       O  
ATOM   3222  OE2 GLU A 386      -9.349  -7.910 -34.320  1.00 55.86           O  
ANISOU 3222  OE2 GLU A 386     7169   8059   5993  -1234    149   -595       O  
ATOM   3223  N   ILE A 387     -12.333  -6.760 -39.935  1.00 49.28           N  
ANISOU 3223  N   ILE A 387     5837   8042   4845  -1258    131   -783       N  
ATOM   3224  CA  ILE A 387     -12.589  -6.325 -41.294  1.00 48.73           C  
ANISOU 3224  CA  ILE A 387     5663   8141   4708  -1223    115   -798       C  
ATOM   3225  C   ILE A 387     -11.755  -5.092 -41.601  1.00 47.18           C  
ANISOU 3225  C   ILE A 387     5469   7912   4545  -1068     75   -705       C  
ATOM   3226  O   ILE A 387     -11.930  -4.053 -40.969  1.00 48.80           O  
ANISOU 3226  O   ILE A 387     5663   8122   4755   -973     57   -633       O  
ATOM   3227  CB  ILE A 387     -14.089  -6.000 -41.502  1.00 49.08           C  
ANISOU 3227  CB  ILE A 387     5576   8423   4650  -1245    117   -827       C  
ATOM   3228  CG1 ILE A 387     -14.994  -7.168 -41.044  1.00 49.16           C  
ANISOU 3228  CG1 ILE A 387     5584   8466   4627  -1407    162   -923       C  
ATOM   3229  CG2 ILE A 387     -14.359  -5.580 -42.936  1.00 47.60           C  
ANISOU 3229  CG2 ILE A 387     5274   8426   4383  -1205     99   -840       C  
ATOM   3230  CD1 ILE A 387     -14.746  -8.499 -41.735  1.00 48.69           C  
ANISOU 3230  CD1 ILE A 387     5557   8375   4567  -1542    203  -1023       C  
ATOM   3231  N   PRO A 388     -10.835  -5.201 -42.567  1.00 46.55           N  
ANISOU 3231  N   PRO A 388     5407   7793   4487  -1044     68   -709       N  
ATOM   3232  CA  PRO A 388     -10.087  -4.017 -42.947  1.00 47.13           C  
ANISOU 3232  CA  PRO A 388     5477   7845   4583   -903     37   -625       C  
ATOM   3233  C   PRO A 388     -10.906  -3.135 -43.885  1.00 48.96           C  
ANISOU 3233  C   PRO A 388     5583   8294   4723   -834     23   -605       C  
ATOM   3234  O   PRO A 388     -11.483  -3.633 -44.858  1.00 52.48           O  
ANISOU 3234  O   PRO A 388     5950   8892   5095   -896     30   -669       O  
ATOM   3235  CB  PRO A 388      -8.853  -4.593 -43.665  1.00 46.94           C  
ANISOU 3235  CB  PRO A 388     5515   7708   4611   -917     39   -647       C  
ATOM   3236  CG  PRO A 388      -9.314  -5.895 -44.224  1.00 48.76           C  
ANISOU 3236  CG  PRO A 388     5726   7995   4802  -1057     71   -751       C  
ATOM   3237  CD  PRO A 388     -10.451  -6.387 -43.356  1.00 48.92           C  
ANISOU 3237  CD  PRO A 388     5730   8065   4789  -1146     93   -791       C  
ATOM   3238  N   TYR A 389     -10.969  -1.840 -43.582  1.00 48.16           N  
ANISOU 3238  N   TYR A 389     5463   8209   4624   -707      7   -517       N  
ATOM   3239  CA  TYR A 389     -11.669  -0.875 -44.427  1.00 47.28           C  
ANISOU 3239  CA  TYR A 389     5240   8291   4430   -614     -1   -478       C  
ATOM   3240  C   TYR A 389     -11.168   0.543 -44.143  1.00 46.65           C  
ANISOU 3240  C   TYR A 389     5189   8145   4390   -462     -8   -371       C  
ATOM   3241  O   TYR A 389     -11.148   0.985 -42.993  1.00 45.99           O  
ANISOU 3241  O   TYR A 389     5156   7963   4353   -432     -2   -332       O  
ATOM   3242  CB  TYR A 389     -13.179  -0.970 -44.193  1.00 48.09           C  
ANISOU 3242  CB  TYR A 389     5244   8581   4447   -657      6   -509       C  
ATOM   3243  CG  TYR A 389     -13.983   0.048 -44.948  1.00 49.39           C  
ANISOU 3243  CG  TYR A 389     5288   8955   4521   -549     -2   -459       C  
ATOM   3244  CD1 TYR A 389     -14.271  -0.126 -46.310  1.00 50.74           C  
ANISOU 3244  CD1 TYR A 389     5365   9305   4607   -557    -10   -491       C  
ATOM   3245  CD2 TYR A 389     -14.470   1.184 -44.311  1.00 48.75           C  
ANISOU 3245  CD2 TYR A 389     5186   8899   4436   -437      0   -379       C  
ATOM   3246  CE1 TYR A 389     -15.021   0.809 -47.012  1.00 50.29           C  
ANISOU 3246  CE1 TYR A 389     5194   9453   4460   -448    -17   -437       C  
ATOM   3247  CE2 TYR A 389     -15.218   2.125 -45.005  1.00 51.08           C  
ANISOU 3247  CE2 TYR A 389     5372   9388   4648   -325     -1   -324       C  
ATOM   3248  CZ  TYR A 389     -15.492   1.933 -46.353  1.00 51.82           C  
ANISOU 3248  CZ  TYR A 389     5371   9663   4655   -328    -12   -350       C  
ATOM   3249  OH  TYR A 389     -16.231   2.871 -47.033  1.00 52.84           O  
ANISOU 3249  OH  TYR A 389     5390   9990   4695   -207    -14   -287       O  
ATOM   3250  N   CYS A 390     -10.744   1.234 -45.195  1.00 47.56           N  
ANISOU 3250  N   CYS A 390     5275   8310   4485   -370    -14   -328       N  
ATOM   3251  CA  CYS A 390     -10.247   2.614 -45.103  1.00 49.24           C  
ANISOU 3251  CA  CYS A 390     5513   8463   4730   -225     -9   -229       C  
ATOM   3252  C   CYS A 390      -9.084   2.847 -44.121  1.00 46.46           C  
ANISOU 3252  C   CYS A 390     5284   7877   4489   -209     -6   -199       C  
ATOM   3253  O   CYS A 390      -9.103   3.798 -43.347  1.00 40.87           O  
ANISOU 3253  O   CYS A 390     4604   7114   3810   -132      6   -138       O  
ATOM   3254  CB  CYS A 390     -11.396   3.571 -44.802  1.00 52.69           C  
ANISOU 3254  CB  CYS A 390     5876   9034   5109   -139      2   -174       C  
ATOM   3255  SG  CYS A 390     -12.504   3.741 -46.203  1.00 61.59           S  
ANISOU 3255  SG  CYS A 390     6850  10451   6101    -99     -3   -175       S  
ATOM   3256  N   GLY A 391      -8.070   1.984 -44.185  1.00 47.35           N  
ANISOU 3256  N   GLY A 391     5469   7862   4660   -280    -15   -243       N  
ATOM   3257  CA  GLY A 391      -6.913   2.076 -43.289  1.00 44.94           C  
ANISOU 3257  CA  GLY A 391     5272   7348   4453   -272    -16   -221       C  
ATOM   3258  C   GLY A 391      -7.233   1.742 -41.840  1.00 46.06           C  
ANISOU 3258  C   GLY A 391     5460   7413   4627   -327    -13   -232       C  
ATOM   3259  O   GLY A 391      -6.494   2.118 -40.923  1.00 48.40           O  
ANISOU 3259  O   GLY A 391     5832   7567   4991   -301    -13   -199       O  
ATOM   3260  N   LYS A 392      -8.336   1.042 -41.624  1.00 43.90           N  
ANISOU 3260  N   LYS A 392     5138   7239   4301   -406    -10   -280       N  
ATOM   3261  CA  LYS A 392      -8.734   0.674 -40.283  1.00 43.80           C  
ANISOU 3261  CA  LYS A 392     5165   7166   4311   -464     -4   -293       C  
ATOM   3262  C   LYS A 392      -9.135  -0.799 -40.223  1.00 44.48           C  
ANISOU 3262  C   LYS A 392     5255   7264   4381   -602      1   -377       C  
ATOM   3263  O   LYS A 392      -9.544  -1.384 -41.231  1.00 47.27           O  
ANISOU 3263  O   LYS A 392     5549   7730   4681   -652      4   -430       O  
ATOM   3264  CB  LYS A 392      -9.881   1.568 -39.811  1.00 44.72           C  
ANISOU 3264  CB  LYS A 392     5219   7393   4379   -409      6   -256       C  
ATOM   3265  CG  LYS A 392      -9.460   2.724 -38.916  1.00 48.13           C  
ANISOU 3265  CG  LYS A 392     5702   7724   4861   -318     14   -185       C  
ATOM   3266  CD  LYS A 392      -8.796   3.883 -39.647  1.00 49.03           C  
ANISOU 3266  CD  LYS A 392     5815   7825   4989   -197     21   -122       C  
ATOM   3267  CE  LYS A 392      -8.252   4.883 -38.635  1.00 49.73           C  
ANISOU 3267  CE  LYS A 392     5970   7786   5136   -132     37    -68       C  
ATOM   3268  NZ  LYS A 392      -7.663   6.110 -39.241  1.00 49.23           N  
ANISOU 3268  NZ  LYS A 392     5914   7702   5089    -15     57     -6       N  
ATOM   3269  N   ILE A 393      -8.993  -1.398 -39.048  1.00 42.85           N  
ANISOU 3269  N   ILE A 393     5122   6939   4219   -664      7   -390       N  
ATOM   3270  CA  ILE A 393      -9.503  -2.739 -38.805  1.00 42.81           C  
ANISOU 3270  CA  ILE A 393     5129   6937   4198   -795     25   -464       C  
ATOM   3271  C   ILE A 393     -10.664  -2.669 -37.822  1.00 42.66           C  
ANISOU 3271  C   ILE A 393     5083   6981   4144   -830     38   -469       C  
ATOM   3272  O   ILE A 393     -10.500  -2.232 -36.683  1.00 41.65           O  
ANISOU 3272  O   ILE A 393     5006   6765   4054   -799     35   -425       O  
ATOM   3273  CB  ILE A 393      -8.415  -3.681 -38.258  1.00 43.15           C  
ANISOU 3273  CB  ILE A 393     5285   6791   4319   -847     30   -477       C  
ATOM   3274  CG1 ILE A 393      -7.268  -3.813 -39.265  1.00 44.31           C  
ANISOU 3274  CG1 ILE A 393     5455   6879   4500   -816     20   -478       C  
ATOM   3275  CG2 ILE A 393      -9.004  -5.052 -37.935  1.00 44.14           C  
ANISOU 3275  CG2 ILE A 393     5433   6907   4428   -982     62   -550       C  
ATOM   3276  CD1 ILE A 393      -5.941  -4.199 -38.643  1.00 43.89           C  
ANISOU 3276  CD1 ILE A 393     5508   6633   4532   -807     15   -455       C  
ATOM   3277  N   PHE A 394     -11.839  -3.081 -38.292  1.00 42.77           N  
ANISOU 3277  N   PHE A 394     5011   7158   4081   -897     52   -525       N  
ATOM   3278  CA  PHE A 394     -13.042  -3.141 -37.480  1.00 43.90           C  
ANISOU 3278  CA  PHE A 394     5116   7382   4181   -945     68   -544       C  
ATOM   3279  C   PHE A 394     -13.256  -4.581 -37.008  1.00 44.85           C  
ANISOU 3279  C   PHE A 394     5288   7443   4309  -1093     99   -619       C  
ATOM   3280  O   PHE A 394     -13.306  -5.506 -37.809  1.00 48.61           O  
ANISOU 3280  O   PHE A 394     5751   7954   4762  -1179    116   -689       O  
ATOM   3281  CB  PHE A 394     -14.266  -2.667 -38.291  1.00 42.68           C  
ANISOU 3281  CB  PHE A 394     4822   7464   3929   -925     68   -560       C  
ATOM   3282  CG  PHE A 394     -14.166  -1.244 -38.783  1.00 41.37           C  
ANISOU 3282  CG  PHE A 394     4604   7365   3749   -773     48   -480       C  
ATOM   3283  CD1 PHE A 394     -13.381  -0.925 -39.882  1.00 40.68           C  
ANISOU 3283  CD1 PHE A 394     4511   7277   3669   -708     33   -458       C  
ATOM   3284  CD2 PHE A 394     -14.871  -0.224 -38.149  1.00 41.30           C  
ANISOU 3284  CD2 PHE A 394     4554   7417   3719   -693     52   -426       C  
ATOM   3285  CE1 PHE A 394     -13.291   0.387 -40.330  1.00 41.00           C  
ANISOU 3285  CE1 PHE A 394     4511   7371   3697   -567     23   -380       C  
ATOM   3286  CE2 PHE A 394     -14.783   1.089 -38.592  1.00 40.46           C  
ANISOU 3286  CE2 PHE A 394     4408   7360   3603   -548     45   -349       C  
ATOM   3287  CZ  PHE A 394     -13.990   1.396 -39.680  1.00 39.96           C  
ANISOU 3287  CZ  PHE A 394     4344   7290   3546   -485     32   -324       C  
ATOM   3288  N   ASN A 395     -13.360  -4.774 -35.707  1.00 45.30           N  
ANISOU 3288  N   ASN A 395     5410   7403   4397  -1124    111   -606       N  
ATOM   3289  CA  ASN A 395     -13.745  -6.071 -35.190  1.00 46.12           C  
ANISOU 3289  CA  ASN A 395     5560   7462   4500  -1263    150   -673       C  
ATOM   3290  C   ASN A 395     -15.257  -6.085 -34.955  1.00 45.70           C  
ANISOU 3290  C   ASN A 395     5418   7577   4369  -1326    170   -716       C  
ATOM   3291  O   ASN A 395     -15.769  -5.344 -34.126  1.00 44.29           O  
ANISOU 3291  O   ASN A 395     5220   7427   4181  -1279    164   -675       O  
ATOM   3292  CB  ASN A 395     -12.967  -6.389 -33.913  1.00 44.93           C  
ANISOU 3292  CB  ASN A 395     5535   7112   4423  -1267    154   -633       C  
ATOM   3293  CG  ASN A 395     -13.274  -7.767 -33.374  1.00 45.14           C  
ANISOU 3293  CG  ASN A 395     5625   7071   4452  -1403    202   -693       C  
ATOM   3294  OD1 ASN A 395     -14.439  -8.137 -33.217  1.00 47.48           O  
ANISOU 3294  OD1 ASN A 395     5873   7474   4693  -1491    233   -748       O  
ATOM   3295  ND2 ASN A 395     -12.231  -8.523 -33.057  1.00 42.55           N  
ANISOU 3295  ND2 ASN A 395     5409   6566   4190  -1420    214   -681       N  
ATOM   3296  N   LEU A 396     -15.965  -6.907 -35.717  1.00 46.65           N  
ANISOU 3296  N   LEU A 396     5478   7814   4430  -1433    198   -804       N  
ATOM   3297  CA  LEU A 396     -17.424  -6.893 -35.705  1.00 48.53           C  
ANISOU 3297  CA  LEU A 396     5609   8247   4582  -1493    216   -855       C  
ATOM   3298  C   LEU A 396     -17.999  -7.378 -34.383  1.00 49.96           C  
ANISOU 3298  C   LEU A 396     5841   8369   4771  -1575    249   -871       C  
ATOM   3299  O   LEU A 396     -19.130  -7.036 -34.031  1.00 50.60           O  
ANISOU 3299  O   LEU A 396     5841   8589   4794  -1590    257   -885       O  
ATOM   3300  CB  LEU A 396     -17.976  -7.721 -36.863  1.00 49.37           C  
ANISOU 3300  CB  LEU A 396     5640   8497   4621  -1602    241   -956       C  
ATOM   3301  CG  LEU A 396     -17.591  -7.231 -38.265  1.00 49.83           C  
ANISOU 3301  CG  LEU A 396     5627   8653   4650  -1527    208   -946       C  
ATOM   3302  CD1 LEU A 396     -18.208  -8.125 -39.322  1.00 49.98           C  
ANISOU 3302  CD1 LEU A 396     5570   8824   4594  -1653    238  -1057       C  
ATOM   3303  CD2 LEU A 396     -17.988  -5.774 -38.492  1.00 48.78           C  
ANISOU 3303  CD2 LEU A 396     5395   8662   4477  -1378    166   -868       C  
ATOM   3304  N   THR A 397     -17.200  -8.144 -33.638  1.00 50.09           N  
ANISOU 3304  N   THR A 397     5991   8180   4859  -1620    270   -864       N  
ATOM   3305  CA  THR A 397     -17.648  -8.713 -32.368  1.00 50.18           C  
ANISOU 3305  CA  THR A 397     6067   8117   4881  -1703    308   -876       C  
ATOM   3306  C   THR A 397     -17.366  -7.751 -31.221  1.00 48.85           C  
ANISOU 3306  C   THR A 397     5938   7870   4750  -1599    278   -784       C  
ATOM   3307  O   THR A 397     -18.273  -7.406 -30.470  1.00 50.48           O  
ANISOU 3307  O   THR A 397     6107   8149   4923  -1611    287   -783       O  
ATOM   3308  CB  THR A 397     -17.012 -10.105 -32.102  1.00 51.32           C  
ANISOU 3308  CB  THR A 397     6338   8083   5076  -1808    356   -914       C  
ATOM   3309  OG1 THR A 397     -17.420 -11.029 -33.129  1.00 52.49           O  
ANISOU 3309  OG1 THR A 397     6448   8312   5183  -1924    397  -1014       O  
ATOM   3310  CG2 THR A 397     -17.437 -10.651 -30.738  1.00 49.08           C  
ANISOU 3310  CG2 THR A 397     6129   7715   4802  -1884    396   -915       C  
ATOM   3311  N   THR A 398     -16.118  -7.293 -31.112  1.00 47.28           N  
ANISOU 3311  N   THR A 398     5809   7533   4618  -1499    243   -713       N  
ATOM   3312  CA  THR A 398     -15.707  -6.423 -30.005  1.00 45.98           C  
ANISOU 3312  CA  THR A 398     5693   7283   4494  -1408    219   -631       C  
ATOM   3313  C   THR A 398     -15.986  -4.941 -30.270  1.00 45.16           C  
ANISOU 3313  C   THR A 398     5499   7291   4366  -1284    185   -581       C  
ATOM   3314  O   THR A 398     -16.005  -4.128 -29.336  1.00 44.52           O  
ANISOU 3314  O   THR A 398     5436   7179   4301  -1222    175   -528       O  
ATOM   3315  CB  THR A 398     -14.212  -6.606 -29.655  1.00 46.63           C  
ANISOU 3315  CB  THR A 398     5892   7166   4656  -1362    201   -578       C  
ATOM   3316  OG1 THR A 398     -13.402  -6.278 -30.795  1.00 45.13           O  
ANISOU 3316  OG1 THR A 398     5682   6977   4486  -1292    173   -566       O  
ATOM   3317  CG2 THR A 398     -13.924  -8.045 -29.217  1.00 45.81           C  
ANISOU 3317  CG2 THR A 398     5890   6935   4580  -1470    242   -613       C  
ATOM   3318  N   ARG A 399     -16.183  -4.599 -31.545  1.00 44.75           N  
ANISOU 3318  N   ARG A 399     5358   7368   4277  -1246    171   -597       N  
ATOM   3319  CA  ARG A 399     -16.468  -3.222 -31.991  1.00 44.64           C  
ANISOU 3319  CA  ARG A 399     5255   7469   4235  -1120    147   -547       C  
ATOM   3320  C   ARG A 399     -15.255  -2.304 -31.935  1.00 45.14           C  
ANISOU 3320  C   ARG A 399     5375   7411   4363   -998    118   -468       C  
ATOM   3321  O   ARG A 399     -15.330  -1.140 -32.338  1.00 47.42           O  
ANISOU 3321  O   ARG A 399     5608   7769   4639   -887    105   -420       O  
ATOM   3322  CB  ARG A 399     -17.640  -2.604 -31.224  1.00 44.80           C  
ANISOU 3322  CB  ARG A 399     5213   7595   4211  -1108    160   -537       C  
ATOM   3323  CG  ARG A 399     -18.977  -3.261 -31.491  1.00 46.37           C  
ANISOU 3323  CG  ARG A 399     5321   7965   4330  -1211    187   -615       C  
ATOM   3324  CD  ARG A 399     -19.348  -4.223 -30.373  1.00 47.43           C  
ANISOU 3324  CD  ARG A 399     5521   8026   4474  -1337    221   -658       C  
ATOM   3325  NE  ARG A 399     -20.548  -4.996 -30.688  1.00 49.82           N  
ANISOU 3325  NE  ARG A 399     5743   8483   4702  -1458    253   -746       N  
ATOM   3326  CZ  ARG A 399     -21.793  -4.539 -30.572  1.00 48.86           C  
ANISOU 3326  CZ  ARG A 399     5512   8538   4511  -1456    263   -763       C  
ATOM   3327  NH1 ARG A 399     -22.020  -3.299 -30.165  1.00 48.18           N  
ANISOU 3327  NH1 ARG A 399     5388   8492   4424  -1334    246   -694       N  
ATOM   3328  NH2 ARG A 399     -22.808  -5.324 -30.873  1.00 50.95           N  
ANISOU 3328  NH2 ARG A 399     5706   8944   4709  -1579    294   -852       N  
ATOM   3329  N   GLN A 400     -14.142  -2.834 -31.433  1.00 44.04           N  
ANISOU 3329  N   GLN A 400     5347   7093   4291  -1019    113   -455       N  
ATOM   3330  CA  GLN A 400     -12.869  -2.126 -31.394  1.00 41.79           C  
ANISOU 3330  CA  GLN A 400     5121   6688   4068   -922     87   -393       C  
ATOM   3331  C   GLN A 400     -12.405  -1.765 -32.787  1.00 41.00           C  
ANISOU 3331  C   GLN A 400     4974   6638   3963   -859     70   -387       C  
ATOM   3332  O   GLN A 400     -12.629  -2.517 -33.735  1.00 42.00           O  
ANISOU 3332  O   GLN A 400     5065   6832   4060   -917     76   -440       O  
ATOM   3333  CB  GLN A 400     -11.802  -2.995 -30.727  1.00 41.76           C  
ANISOU 3333  CB  GLN A 400     5234   6505   4127   -968     85   -390       C  
ATOM   3334  CG  GLN A 400     -12.157  -3.458 -29.325  1.00 41.29           C  
ANISOU 3334  CG  GLN A 400     5232   6384   4072  -1033    103   -391       C  
ATOM   3335  CD  GLN A 400     -12.612  -2.314 -28.445  1.00 43.44           C  
ANISOU 3335  CD  GLN A 400     5482   6688   4334   -972    101   -349       C  
ATOM   3336  OE1 GLN A 400     -13.816  -2.068 -28.287  1.00 47.11           O  
ANISOU 3336  OE1 GLN A 400     5880   7272   4747   -991    119   -368       O  
ATOM   3337  NE2 GLN A 400     -11.663  -1.600 -27.875  1.00 40.50           N  
ANISOU 3337  NE2 GLN A 400     5163   6214   4008   -900     83   -295       N  
ATOM   3338  N   VAL A 401     -11.753  -0.613 -32.912  1.00 39.84           N  
ANISOU 3338  N   VAL A 401     4832   6459   3845   -745     54   -326       N  
ATOM   3339  CA  VAL A 401     -11.133  -0.233 -34.176  1.00 38.39           C  
ANISOU 3339  CA  VAL A 401     4621   6299   3665   -679     40   -312       C  
ATOM   3340  C   VAL A 401      -9.643   0.056 -33.988  1.00 38.14           C  
ANISOU 3340  C   VAL A 401     4675   6106   3709   -627     24   -272       C  
ATOM   3341  O   VAL A 401      -9.256   0.840 -33.120  1.00 37.31           O  
ANISOU 3341  O   VAL A 401     4612   5927   3638   -574     24   -226       O  
ATOM   3342  CB  VAL A 401     -11.848   0.958 -34.845  1.00 37.75           C  
ANISOU 3342  CB  VAL A 401     4444   6365   3533   -580     44   -277       C  
ATOM   3343  CG1 VAL A 401     -11.182   1.306 -36.170  1.00 36.46           C  
ANISOU 3343  CG1 VAL A 401     4257   6226   3370   -515     32   -260       C  
ATOM   3344  CG2 VAL A 401     -13.324   0.645 -35.060  1.00 38.61           C  
ANISOU 3344  CG2 VAL A 401     4455   6653   3560   -631     57   -319       C  
ATOM   3345  N   ARG A 402      -8.825  -0.591 -34.814  1.00 38.54           N  
ANISOU 3345  N   ARG A 402     4749   6111   3782   -647     13   -294       N  
ATOM   3346  CA  ARG A 402      -7.371  -0.426 -34.795  1.00 39.64           C  
ANISOU 3346  CA  ARG A 402     4960   6110   3989   -603     -1   -263       C  
ATOM   3347  C   ARG A 402      -6.908   0.156 -36.137  1.00 39.89           C  
ANISOU 3347  C   ARG A 402     4950   6189   4015   -532     -9   -249       C  
ATOM   3348  O   ARG A 402      -7.592   0.013 -37.158  1.00 39.45           O  
ANISOU 3348  O   ARG A 402     4822   6262   3905   -542     -5   -276       O  
ATOM   3349  CB  ARG A 402      -6.679  -1.787 -34.554  1.00 39.00           C  
ANISOU 3349  CB  ARG A 402     4953   5916   3946   -686     -3   -298       C  
ATOM   3350  CG  ARG A 402      -7.055  -2.501 -33.254  1.00 40.49           C  
ANISOU 3350  CG  ARG A 402     5194   6048   4141   -759      8   -309       C  
ATOM   3351  CD  ARG A 402      -6.321  -1.922 -32.029  1.00 42.52           C  
ANISOU 3351  CD  ARG A 402     5515   6195   4443   -714     -4   -257       C  
ATOM   3352  NE  ARG A 402      -4.862  -1.976 -32.167  1.00 42.24           N  
ANISOU 3352  NE  ARG A 402     5536   6046   4466   -675    -23   -234       N  
ATOM   3353  CZ  ARG A 402      -4.113  -3.021 -31.813  1.00 42.25           C  
ANISOU 3353  CZ  ARG A 402     5607   5942   4504   -717    -25   -241       C  
ATOM   3354  NH1 ARG A 402      -4.677  -4.086 -31.261  1.00 44.71           N  
ANISOU 3354  NH1 ARG A 402     5950   6234   4801   -800     -4   -268       N  
ATOM   3355  NH2 ARG A 402      -2.797  -2.989 -31.981  1.00 38.98           N  
ANISOU 3355  NH2 ARG A 402     5232   5439   4138   -672    -43   -220       N  
ATOM   3356  N   THR A 403      -5.752   0.813 -36.141  1.00 40.51           N  
ANISOU 3356  N   THR A 403     5074   6171   4146   -463    -18   -209       N  
ATOM   3357  CA  THR A 403      -5.139   1.250 -37.403  1.00 41.72           C  
ANISOU 3357  CA  THR A 403     5202   6347   4301   -403    -23   -197       C  
ATOM   3358  C   THR A 403      -4.583   0.046 -38.155  1.00 41.30           C  
ANISOU 3358  C   THR A 403     5166   6263   4261   -468    -31   -247       C  
ATOM   3359  O   THR A 403      -4.054  -0.869 -37.545  1.00 41.11           O  
ANISOU 3359  O   THR A 403     5206   6135   4277   -527    -34   -268       O  
ATOM   3360  CB  THR A 403      -4.002   2.237 -37.147  1.00 41.58           C  
ANISOU 3360  CB  THR A 403     5232   6226   4339   -324    -25   -148       C  
ATOM   3361  OG1 THR A 403      -4.486   3.320 -36.352  1.00 44.88           O  
ANISOU 3361  OG1 THR A 403     5645   6657   4750   -272     -8   -107       O  
ATOM   3362  CG2 THR A 403      -3.417   2.767 -38.457  1.00 40.95           C  
ANISOU 3362  CG2 THR A 403     5126   6172   4258   -260    -23   -133       C  
ATOM   3363  N   LEU A 404      -4.727   0.045 -39.475  1.00 43.58           N  
ANISOU 3363  N   LEU A 404     5398   6645   4513   -455    -30   -264       N  
ATOM   3364  CA  LEU A 404      -4.187  -1.029 -40.301  1.00 44.45           C  
ANISOU 3364  CA  LEU A 404     5523   6731   4634   -514    -31   -315       C  
ATOM   3365  C   LEU A 404      -2.770  -0.715 -40.778  1.00 44.62           C  
ANISOU 3365  C   LEU A 404     5587   6654   4711   -457    -41   -291       C  
ATOM   3366  O   LEU A 404      -2.484   0.388 -41.236  1.00 43.22           O  
ANISOU 3366  O   LEU A 404     5387   6501   4532   -370    -42   -247       O  
ATOM   3367  CB  LEU A 404      -5.105  -1.291 -41.492  1.00 45.81           C  
ANISOU 3367  CB  LEU A 404     5608   7069   4730   -543    -23   -357       C  
ATOM   3368  CG  LEU A 404      -4.638  -2.154 -42.677  1.00 46.25           C  
ANISOU 3368  CG  LEU A 404     5657   7135   4779   -591    -19   -411       C  
ATOM   3369  CD1 LEU A 404      -4.581  -3.627 -42.311  1.00 45.50           C  
ANISOU 3369  CD1 LEU A 404     5614   6963   4708   -707     -2   -477       C  
ATOM   3370  CD2 LEU A 404      -5.547  -1.944 -43.886  1.00 45.26           C  
ANISOU 3370  CD2 LEU A 404     5427   7203   4565   -588    -17   -434       C  
ATOM   3371  N   TYR A 405      -1.888  -1.698 -40.630  1.00 48.26           N  
ANISOU 3371  N   TYR A 405     6111   7001   5224   -505    -43   -318       N  
ATOM   3372  CA  TYR A 405      -0.553  -1.692 -41.230  1.00 49.36           C  
ANISOU 3372  CA  TYR A 405     6284   7056   5412   -469    -50   -312       C  
ATOM   3373  C   TYR A 405      -0.303  -3.129 -41.771  1.00 54.48           C  
ANISOU 3373  C   TYR A 405     6956   7672   6071   -552    -38   -375       C  
ATOM   3374  O   TYR A 405      -0.335  -4.079 -40.977  1.00 62.13           O  
ANISOU 3374  O   TYR A 405     7976   8567   7064   -614    -28   -395       O  
ATOM   3375  CB  TYR A 405       0.520  -1.367 -40.164  1.00 43.76           C  
ANISOU 3375  CB  TYR A 405     5644   6209   4770   -432    -63   -270       C  
ATOM   3376  CG  TYR A 405       0.244  -0.215 -39.194  1.00 40.29           C  
ANISOU 3376  CG  TYR A 405     5205   5771   4330   -380    -66   -220       C  
ATOM   3377  CD1 TYR A 405       0.756   1.063 -39.434  1.00 39.42           C  
ANISOU 3377  CD1 TYR A 405     5086   5658   4232   -296    -64   -178       C  
ATOM   3378  CD2 TYR A 405      -0.437  -0.430 -37.982  1.00 38.72           C  
ANISOU 3378  CD2 TYR A 405     5024   5562   4122   -417    -65   -217       C  
ATOM   3379  CE1 TYR A 405       0.561   2.107 -38.530  1.00 37.00           C  
ANISOU 3379  CE1 TYR A 405     4787   5341   3929   -253    -57   -137       C  
ATOM   3380  CE2 TYR A 405      -0.643   0.613 -37.077  1.00 37.48           C  
ANISOU 3380  CE2 TYR A 405     4871   5401   3966   -373    -64   -175       C  
ATOM   3381  CZ  TYR A 405      -0.143   1.884 -37.362  1.00 37.90           C  
ANISOU 3381  CZ  TYR A 405     4914   5451   4032   -292    -58   -137       C  
ATOM   3382  OH  TYR A 405      -0.332   2.935 -36.477  1.00 37.91           O  
ANISOU 3382  OH  TYR A 405     4924   5442   4036   -252    -47   -101       O  
ATOM   3383  N   LYS A 406      -0.044  -3.339 -43.072  1.00 60.28           N  
ANISOU 3383  N   LYS A 406     7660   8453   6790   -555    -32   -406       N  
ATOM   3384  CA  LYS A 406       0.284  -2.331 -44.108  1.00 65.17           C  
ANISOU 3384  CA  LYS A 406     8233   9136   7391   -477    -39   -378       C  
ATOM   3385  C   LYS A 406       1.688  -2.603 -44.711  1.00 62.75           C  
ANISOU 3385  C   LYS A 406     7967   8732   7140   -458    -40   -385       C  
ATOM   3386  O   LYS A 406       2.251  -1.761 -45.440  1.00 61.15           O  
ANISOU 3386  O   LYS A 406     7746   8547   6939   -390    -45   -357       O  
ATOM   3387  CB  LYS A 406       0.199  -0.900 -43.561  1.00 63.83           C  
ANISOU 3387  CB  LYS A 406     8053   8978   7221   -387    -49   -308       C  
ATOM   3388  CG  LYS A 406      -0.277   0.130 -44.565  1.00 65.05           C  
ANISOU 3388  CG  LYS A 406     8137   9260   7319   -320    -44   -280       C  
ATOM   3389  CD  LYS A 406      -0.042   1.536 -44.040  1.00 66.91           C  
ANISOU 3389  CD  LYS A 406     8383   9464   7572   -226    -41   -210       C  
ATOM   3390  CE  LYS A 406       1.408   1.743 -43.651  1.00 62.59           C  
ANISOU 3390  CE  LYS A 406     7906   8769   7104   -199    -46   -192       C  
ATOM   3391  NZ  LYS A 406       1.685   3.171 -43.338  1.00 66.98           N  
ANISOU 3391  NZ  LYS A 406     8471   9301   7674   -113    -32   -133       N  
ATOM   3392  N   LEU A 407       2.259  -3.764 -44.388  1.00 57.81           N  
ANISOU 3392  N   LEU A 407     7401   8002   6562   -515    -32   -420       N  
ATOM   3393  CA  LEU A 407       3.657  -4.023 -44.724  1.00 60.22           C  
ANISOU 3393  CA  LEU A 407     7750   8202   6929   -490    -33   -420       C  
ATOM   3394  C   LEU A 407       3.855  -5.374 -45.394  1.00 62.51           C  
ANISOU 3394  C   LEU A 407     8059   8462   7227   -563     -6   -486       C  
ATOM   3395  O   LEU A 407       3.744  -6.417 -44.745  1.00 61.98           O  
ANISOU 3395  O   LEU A 407     8041   8325   7183   -622     10   -511       O  
ATOM   3396  CB  LEU A 407       4.577  -3.912 -43.483  1.00 61.57           C  
ANISOU 3396  CB  LEU A 407     7985   8241   7165   -455    -48   -377       C  
ATOM   3397  CG  LEU A 407       4.860  -2.591 -42.728  1.00 58.23           C  
ANISOU 3397  CG  LEU A 407     7562   7806   6755   -381    -69   -315       C  
ATOM   3398  CD1 LEU A 407       5.113  -1.412 -43.656  1.00 60.23           C  
ANISOU 3398  CD1 LEU A 407     7774   8118   6993   -314    -69   -292       C  
ATOM   3399  CD2 LEU A 407       3.774  -2.263 -41.715  1.00 57.46           C  
ANISOU 3399  CD2 LEU A 407     7456   7749   6626   -394    -72   -295       C  
ATOM   3400  N   PRO A 408       4.167  -5.358 -46.703  1.00 62.91           N  
ANISOU 3400  N   PRO A 408     8078   8563   7262   -558      1   -515       N  
ATOM   3401  CA  PRO A 408       4.640  -6.551 -47.394  1.00 62.66           C  
ANISOU 3401  CA  PRO A 408     8073   8483   7252   -616     30   -577       C  
ATOM   3402  C   PRO A 408       5.869  -7.128 -46.686  1.00 65.57           C  
ANISOU 3402  C   PRO A 408     8521   8686   7705   -596     33   -560       C  
ATOM   3403  O   PRO A 408       6.593  -6.382 -46.012  1.00 62.48           O  
ANISOU 3403  O   PRO A 408     8148   8238   7352   -524      6   -501       O  
ATOM   3404  CB  PRO A 408       5.050  -6.015 -48.767  1.00 62.12           C  
ANISOU 3404  CB  PRO A 408     7957   8485   7159   -580     28   -586       C  
ATOM   3405  CG  PRO A 408       4.234  -4.793 -48.960  1.00 62.48           C  
ANISOU 3405  CG  PRO A 408     7936   8662   7141   -533      7   -546       C  
ATOM   3406  CD  PRO A 408       4.103  -4.187 -47.595  1.00 62.29           C  
ANISOU 3406  CD  PRO A 408     7938   8586   7142   -493    -11   -487       C  
ATOM   3407  N   PRO A 409       6.107  -8.452 -46.830  1.00 69.51           N  
ANISOU 3407  N   PRO A 409     9066   9110   8233   -659     71   -611       N  
ATOM   3408  CA  PRO A 409       7.370  -9.028 -46.350  1.00 67.74           C  
ANISOU 3408  CA  PRO A 409     8911   8737   8087   -626     78   -592       C  
ATOM   3409  C   PRO A 409       8.550  -8.410 -47.103  1.00 66.16           C  
ANISOU 3409  C   PRO A 409     8695   8524   7917   -555     61   -575       C  
ATOM   3410  O   PRO A 409       8.420  -8.084 -48.284  1.00 66.31           O  
ANISOU 3410  O   PRO A 409     8665   8627   7899   -561     66   -605       O  
ATOM   3411  CB  PRO A 409       7.232 -10.520 -46.694  1.00 70.37           C  
ANISOU 3411  CB  PRO A 409     9288   9015   8433   -710    135   -660       C  
ATOM   3412  CG  PRO A 409       6.200 -10.584 -47.778  1.00 69.40           C  
ANISOU 3412  CG  PRO A 409     9104   9025   8237   -783    155   -727       C  
ATOM   3413  CD  PRO A 409       5.254  -9.456 -47.502  1.00 69.37           C  
ANISOU 3413  CD  PRO A 409     9036   9145   8173   -760    115   -691       C  
ATOM   3414  N   ASN A 410       9.673  -8.213 -46.416  1.00 65.31           N  
ANISOU 3414  N   ASN A 410     8623   8320   7869   -490     42   -528       N  
ATOM   3415  CA  ASN A 410      10.867  -7.628 -47.039  1.00 64.12           C  
ANISOU 3415  CA  ASN A 410     8459   8152   7750   -426     28   -514       C  
ATOM   3416  C   ASN A 410      10.739  -6.135 -47.354  1.00 62.35           C  
ANISOU 3416  C   ASN A 410     8180   8017   7492   -376     -1   -480       C  
ATOM   3417  O   ASN A 410      11.597  -5.571 -48.062  1.00 62.87           O  
ANISOU 3417  O   ASN A 410     8228   8084   7572   -331     -5   -475       O  
ATOM   3418  CB  ASN A 410      11.239  -8.367 -48.342  1.00 68.49           C  
ANISOU 3418  CB  ASN A 410     9010   8703   8310   -457     64   -574       C  
ATOM   3419  CG  ASN A 410      11.448  -9.849 -48.144  1.00 72.48           C  
ANISOU 3419  CG  ASN A 410     9575   9107   8854   -503    108   -610       C  
ATOM   3420  OD1 ASN A 410      11.880 -10.299 -47.079  1.00 76.60           O  
ANISOU 3420  OD1 ASN A 410    10149   9533   9421   -480    106   -575       O  
ATOM   3421  ND2 ASN A 410      11.148 -10.623 -49.179  1.00 77.13           N  
ANISOU 3421  ND2 ASN A 410    10162   9718   9426   -567    151   -680       N  
ATOM   3422  N   TYR A 411       9.670  -5.497 -46.874  1.00 54.46           N  
ANISOU 3422  N   TYR A 411     7155   7090   6445   -383    -15   -458       N  
ATOM   3423  CA  TYR A 411       9.495  -4.071 -47.126  1.00 47.80           C  
ANISOU 3423  CA  TYR A 411     6266   6323   5569   -329    -33   -420       C  
ATOM   3424  C   TYR A 411      10.467  -3.275 -46.267  1.00 45.79           C  
ANISOU 3424  C   TYR A 411     6035   5999   5362   -267    -54   -370       C  
ATOM   3425  O   TYR A 411      10.606  -3.539 -45.075  1.00 46.52           O  
ANISOU 3425  O   TYR A 411     6163   6029   5482   -268    -66   -349       O  
ATOM   3426  CB  TYR A 411       8.063  -3.632 -46.865  1.00 44.19           C  
ANISOU 3426  CB  TYR A 411     5775   5965   5050   -349    -36   -410       C  
ATOM   3427  CG  TYR A 411       7.776  -2.185 -47.222  1.00 41.25           C  
ANISOU 3427  CG  TYR A 411     5357   5674   4639   -288    -44   -369       C  
ATOM   3428  CD1 TYR A 411       7.425  -1.817 -48.523  1.00 40.18           C  
ANISOU 3428  CD1 TYR A 411     5170   5642   4453   -277    -33   -381       C  
ATOM   3429  CD2 TYR A 411       7.818  -1.186 -46.250  1.00 37.16           C  
ANISOU 3429  CD2 TYR A 411     4849   5134   4134   -240    -57   -316       C  
ATOM   3430  CE1 TYR A 411       7.142  -0.493 -48.842  1.00 37.34           C  
ANISOU 3430  CE1 TYR A 411     4775   5354   4058   -212    -33   -334       C  
ATOM   3431  CE2 TYR A 411       7.533   0.135 -46.563  1.00 35.06           C  
ANISOU 3431  CE2 TYR A 411     4550   4931   3837   -181    -52   -276       C  
ATOM   3432  CZ  TYR A 411       7.206   0.478 -47.848  1.00 35.36           C  
ANISOU 3432  CZ  TYR A 411     4543   5065   3828   -163    -39   -282       C  
ATOM   3433  OH  TYR A 411       6.937   1.794 -48.148  1.00 36.15           O  
ANISOU 3433  OH  TYR A 411     4616   5220   3896    -96    -27   -233       O  
ATOM   3434  N   GLU A 412      11.153  -2.322 -46.893  1.00 40.16           N  
ANISOU 3434  N   GLU A 412     5301   5301   4655   -215    -55   -354       N  
ATOM   3435  CA  GLU A 412      12.059  -1.439 -46.193  1.00 37.69           C  
ANISOU 3435  CA  GLU A 412     5003   4936   4380   -163    -68   -315       C  
ATOM   3436  C   GLU A 412      11.308  -0.219 -45.702  1.00 36.18           C  
ANISOU 3436  C   GLU A 412     4795   4797   4155   -137    -71   -275       C  
ATOM   3437  O   GLU A 412      10.885   0.642 -46.482  1.00 40.41           O  
ANISOU 3437  O   GLU A 412     5298   5403   4652   -110    -56   -262       O  
ATOM   3438  CB  GLU A 412      13.221  -1.023 -47.095  1.00 38.29           C  
ANISOU 3438  CB  GLU A 412     5070   4995   4482   -127    -59   -321       C  
ATOM   3439  CG  GLU A 412      14.340  -2.035 -47.143  1.00 39.38           C  
ANISOU 3439  CG  GLU A 412     5234   5054   4675   -134    -60   -347       C  
ATOM   3440  CD  GLU A 412      15.446  -1.630 -48.098  1.00 40.38           C  
ANISOU 3440  CD  GLU A 412     5346   5171   4824   -102    -49   -359       C  
ATOM   3441  OE1 GLU A 412      16.393  -0.913 -47.683  1.00 38.89           O  
ANISOU 3441  OE1 GLU A 412     5160   4949   4666    -65    -56   -338       O  
ATOM   3442  OE2 GLU A 412      15.368  -2.043 -49.263  1.00 40.63           O  
ANISOU 3442  OE2 GLU A 412     5363   5234   4840   -118    -30   -392       O  
ATOM   3443  N   ILE A 413      11.190  -0.133 -44.396  1.00 34.58           N  
ANISOU 3443  N   ILE A 413     4615   4557   3964   -140    -85   -252       N  
ATOM   3444  CA  ILE A 413      10.264   0.780 -43.745  1.00 33.44           C  
ANISOU 3444  CA  ILE A 413     4460   4458   3787   -128    -84   -220       C  
ATOM   3445  C   ILE A 413      10.655   2.245 -44.003  1.00 32.41           C  
ANISOU 3445  C   ILE A 413     4318   4340   3657    -72    -66   -191       C  
ATOM   3446  O   ILE A 413       9.811   3.123 -43.990  1.00 32.30           O  
ANISOU 3446  O   ILE A 413     4286   4380   3606    -49    -51   -165       O  
ATOM   3447  CB  ILE A 413      10.144   0.436 -42.228  1.00 32.17           C  
ANISOU 3447  CB  ILE A 413     4332   4248   3642   -150   -102   -207       C  
ATOM   3448  CG1 ILE A 413       8.997   1.202 -41.545  1.00 33.19           C  
ANISOU 3448  CG1 ILE A 413     4449   4428   3732   -147    -97   -181       C  
ATOM   3449  CG2 ILE A 413      11.489   0.593 -41.511  1.00 30.71           C  
ANISOU 3449  CG2 ILE A 413     4173   3985   3507   -128   -116   -196       C  
ATOM   3450  CD1 ILE A 413       7.647   0.544 -41.651  1.00 32.31           C  
ANISOU 3450  CD1 ILE A 413     4319   4381   3575   -190    -94   -196       C  
ATOM   3451  N   ARG A 414      11.929   2.478 -44.309  1.00 31.75           N  
ANISOU 3451  N   ARG A 414     4244   4205   3612    -50    -63   -196       N  
ATOM   3452  CA  ARG A 414      12.414   3.819 -44.629  1.00 29.93           C  
ANISOU 3452  CA  ARG A 414     4009   3976   3386     -5    -37   -175       C  
ATOM   3453  C   ARG A 414      11.676   4.416 -45.810  1.00 31.03           C  
ANISOU 3453  C   ARG A 414     4119   4193   3479     23    -10   -161       C  
ATOM   3454  O   ARG A 414      11.721   5.629 -46.002  1.00 30.83           O  
ANISOU 3454  O   ARG A 414     4093   4174   3445     66     21   -132       O  
ATOM   3455  CB  ARG A 414      13.912   3.805 -44.909  1.00 29.40           C  
ANISOU 3455  CB  ARG A 414     3952   3851   3367      4    -36   -193       C  
ATOM   3456  CG  ARG A 414      14.286   3.175 -46.241  1.00 27.71           C  
ANISOU 3456  CG  ARG A 414     3723   3652   3154      2    -32   -220       C  
ATOM   3457  CD  ARG A 414      15.774   3.194 -46.469  1.00 26.93           C  
ANISOU 3457  CD  ARG A 414     3630   3498   3103     13    -29   -238       C  
ATOM   3458  NE  ARG A 414      16.141   2.172 -47.431  1.00 25.64           N  
ANISOU 3458  NE  ARG A 414     3458   3333   2948      0    -33   -271       N  
ATOM   3459  CZ  ARG A 414      16.070   2.320 -48.751  1.00 26.02           C  
ANISOU 3459  CZ  ARG A 414     3487   3424   2974      8    -11   -282       C  
ATOM   3460  NH1 ARG A 414      15.643   3.466 -49.303  1.00 25.18           N  
ANISOU 3460  NH1 ARG A 414     3368   3366   2833     39     15   -255       N  
ATOM   3461  NH2 ARG A 414      16.383   1.305 -49.520  1.00 25.76           N  
ANISOU 3461  NH2 ARG A 414     3450   3387   2951    -12    -12   -319       N  
ATOM   3462  N   HIS A 415      11.007   3.554 -46.596  1.00 33.08           N  
ANISOU 3462  N   HIS A 415     4353   4511   3704      0    -18   -182       N  
ATOM   3463  CA  HIS A 415      10.216   3.964 -47.765  1.00 34.46           C  
ANISOU 3463  CA  HIS A 415     4488   4782   3821     24      1   -171       C  
ATOM   3464  C   HIS A 415       8.917   4.609 -47.383  1.00 36.17           C  
ANISOU 3464  C   HIS A 415     4684   5069   3988     45     10   -136       C  
ATOM   3465  O   HIS A 415       8.291   5.266 -48.222  1.00 39.15           O  
ANISOU 3465  O   HIS A 415     5028   5530   4314     87     31   -109       O  
ATOM   3466  CB  HIS A 415       9.904   2.765 -48.685  1.00 37.27           C  
ANISOU 3466  CB  HIS A 415     4819   5189   4150    -20     -9   -216       C  
ATOM   3467  CG  HIS A 415      11.065   2.316 -49.528  1.00 38.91           C  
ANISOU 3467  CG  HIS A 415     5036   5356   4393    -26     -6   -247       C  
ATOM   3468  ND1 HIS A 415      11.720   3.143 -50.362  1.00 37.95           N  
ANISOU 3468  ND1 HIS A 415     4908   5238   4272     18     16   -231       N  
ATOM   3469  CD2 HIS A 415      11.678   1.076 -49.648  1.00 38.92           C  
ANISOU 3469  CD2 HIS A 415     5053   5305   4428    -71    -17   -295       C  
ATOM   3470  CE1 HIS A 415      12.714   2.477 -50.952  1.00 38.83           C  
ANISOU 3470  CE1 HIS A 415     5028   5306   4417      0     15   -269       C  
ATOM   3471  NE2 HIS A 415      12.686   1.211 -50.516  1.00 37.79           N  
ANISOU 3471  NE2 HIS A 415     4910   5141   4307    -52     -4   -307       N  
ATOM   3472  N   LYS A 416       8.453   4.375 -46.151  1.00 35.45           N  
ANISOU 3472  N   LYS A 416     4608   4952   3905     18     -5   -133       N  
ATOM   3473  CA  LYS A 416       7.228   5.011 -45.647  1.00 35.64           C  
ANISOU 3473  CA  LYS A 416     4614   5038   3887     39      4   -100       C  
ATOM   3474  C   LYS A 416       7.406   6.520 -45.418  1.00 34.75           C  
ANISOU 3474  C   LYS A 416     4516   4903   3781    105     42    -52       C  
ATOM   3475  O   LYS A 416       6.429   7.279 -45.427  1.00 35.80           O  
ANISOU 3475  O   LYS A 416     4628   5100   3873    147     65    -15       O  
ATOM   3476  CB  LYS A 416       6.745   4.332 -44.343  1.00 39.04           C  
ANISOU 3476  CB  LYS A 416     5063   5442   4328    -11    -19   -114       C  
ATOM   3477  CG  LYS A 416       5.342   3.688 -44.408  1.00 42.74           C  
ANISOU 3477  CG  LYS A 416     5492   6006   4739    -48    -28   -128       C  
ATOM   3478  CD  LYS A 416       4.963   3.244 -45.822  1.00 43.48           C  
ANISOU 3478  CD  LYS A 416     5539   6195   4786    -56    -25   -151       C  
ATOM   3479  CE  LYS A 416       3.588   2.616 -45.888  1.00 47.11           C  
ANISOU 3479  CE  LYS A 416     5953   6762   5184   -100    -31   -174       C  
ATOM   3480  NZ  LYS A 416       3.630   1.124 -45.948  1.00 47.43           N  
ANISOU 3480  NZ  LYS A 416     6004   6783   5234   -188    -45   -236       N  
ATOM   3481  N   PHE A 417       8.653   6.948 -45.274  1.00 30.52           N  
ANISOU 3481  N   PHE A 417     4017   4281   3298    115     53    -54       N  
ATOM   3482  CA  PHE A 417       8.956   8.265 -44.769  1.00 30.94           C  
ANISOU 3482  CA  PHE A 417     4097   4287   3369    157     93    -21       C  
ATOM   3483  C   PHE A 417       9.523   9.219 -45.817  1.00 32.68           C  
ANISOU 3483  C   PHE A 417     4322   4503   3589    212    139      0       C  
ATOM   3484  O   PHE A 417      10.136   8.800 -46.789  1.00 36.28           O  
ANISOU 3484  O   PHE A 417     4768   4966   4050    208    132    -18       O  
ATOM   3485  CB  PHE A 417       9.881   8.128 -43.553  1.00 29.88           C  
ANISOU 3485  CB  PHE A 417     4002   4061   3290    119     77    -44       C  
ATOM   3486  CG  PHE A 417       9.362   7.155 -42.522  1.00 29.06           C  
ANISOU 3486  CG  PHE A 417     3898   3956   3183     69     35    -61       C  
ATOM   3487  CD1 PHE A 417       8.124   7.360 -41.924  1.00 29.29           C  
ANISOU 3487  CD1 PHE A 417     3918   4032   3178     71     40    -41       C  
ATOM   3488  CD2 PHE A 417      10.070   6.022 -42.196  1.00 29.46           C  
ANISOU 3488  CD2 PHE A 417     3961   3964   3265     23     -3    -94       C  
ATOM   3489  CE1 PHE A 417       7.621   6.474 -40.992  1.00 29.14           C  
ANISOU 3489  CE1 PHE A 417     3902   4012   3155     21      6    -56       C  
ATOM   3490  CE2 PHE A 417       9.572   5.114 -41.267  1.00 29.83           C  
ANISOU 3490  CE2 PHE A 417     4016   4008   3309    -19    -35   -104       C  
ATOM   3491  CZ  PHE A 417       8.340   5.338 -40.674  1.00 29.28           C  
ANISOU 3491  CZ  PHE A 417     3938   3982   3204    -24    -29    -86       C  
ATOM   3492  N   LYS A 418       9.275  10.508 -45.627  1.00 34.28           N  
ANISOU 3492  N   LYS A 418     4542   4694   3786    263    192     42       N  
ATOM   3493  CA  LYS A 418       9.823  11.548 -46.481  1.00 34.71           C  
ANISOU 3493  CA  LYS A 418     4613   4730   3844    317    250     69       C  
ATOM   3494  C   LYS A 418      10.662  12.507 -45.629  1.00 34.92           C  
ANISOU 3494  C   LYS A 418     4691   4656   3921    312    294     65       C  
ATOM   3495  O   LYS A 418      10.126  13.398 -44.970  1.00 35.66           O  
ANISOU 3495  O   LYS A 418     4805   4733   4009    339    337     94       O  
ATOM   3496  CB  LYS A 418       8.693  12.297 -47.204  1.00 35.68           C  
ANISOU 3496  CB  LYS A 418     4713   4937   3907    393    290    128       C  
ATOM   3497  CG  LYS A 418       9.170  13.492 -48.021  1.00 37.79           C  
ANISOU 3497  CG  LYS A 418     5006   5176   4174    459    362    169       C  
ATOM   3498  CD  LYS A 418       8.022  14.217 -48.731  1.00 38.67           C  
ANISOU 3498  CD  LYS A 418     5092   5377   4221    548    403    239       C  
ATOM   3499  CE  LYS A 418       8.582  15.130 -49.815  1.00 41.04           C  
ANISOU 3499  CE  LYS A 418     5417   5660   4516    611    469    278       C  
ATOM   3500  NZ  LYS A 418       7.672  16.235 -50.227  1.00 44.31           N  
ANISOU 3500  NZ  LYS A 418     5831   6121   4881    715    536    361       N  
ATOM   3501  N   LEU A 419      11.981  12.315 -45.647  1.00 34.42           N  
ANISOU 3501  N   LEU A 419     4644   4530   3902    276    287     26       N  
ATOM   3502  CA  LEU A 419      12.877  13.095 -44.811  1.00 33.03           C  
ANISOU 3502  CA  LEU A 419     4508   4269   3770    254    323      8       C  
ATOM   3503  C   LEU A 419      13.424  14.317 -45.528  1.00 34.42           C  
ANISOU 3503  C   LEU A 419     4715   4406   3956    294    404     28       C  
ATOM   3504  O   LEU A 419      13.953  15.236 -44.892  1.00 34.19           O  
ANISOU 3504  O   LEU A 419     4724   4311   3955    282    458     18       O  
ATOM   3505  CB  LEU A 419      14.043  12.226 -44.353  1.00 35.51           C  
ANISOU 3505  CB  LEU A 419     4819   4546   4126    192    272    -45       C  
ATOM   3506  CG  LEU A 419      13.696  10.888 -43.696  1.00 38.46           C  
ANISOU 3506  CG  LEU A 419     5170   4944   4496    152    195    -65       C  
ATOM   3507  CD1 LEU A 419      14.967  10.149 -43.302  1.00 36.38           C  
ANISOU 3507  CD1 LEU A 419     4906   4641   4274    107    155   -110       C  
ATOM   3508  CD2 LEU A 419      12.782  11.106 -42.483  1.00 39.51           C  
ANISOU 3508  CD2 LEU A 419     5314   5083   4615    142    193    -51       C  
ATOM   3509  N   TRP A 420      13.324  14.308 -46.856  1.00 34.72           N  
ANISOU 3509  N   TRP A 420     4737   4486   3967    337    417     53       N  
ATOM   3510  CA  TRP A 420      13.952  15.320 -47.692  1.00 35.99           C  
ANISOU 3510  CA  TRP A 420     4928   4609   4135    373    493     71       C  
ATOM   3511  C   TRP A 420      12.928  16.092 -48.448  1.00 35.52           C  
ANISOU 3511  C   TRP A 420     4870   4597   4026    458    546    142       C  
ATOM   3512  O   TRP A 420      12.106  15.512 -49.159  1.00 36.06           O  
ANISOU 3512  O   TRP A 420     4896   4758   4046    488    510    167       O  
ATOM   3513  CB  TRP A 420      14.917  14.657 -48.679  1.00 35.69           C  
ANISOU 3513  CB  TRP A 420     4872   4578   4109    353    466     39       C  
ATOM   3514  CG  TRP A 420      15.901  13.760 -47.997  1.00 34.66           C  
ANISOU 3514  CG  TRP A 420     4731   4413   4023    280    407    -24       C  
ATOM   3515  CD1 TRP A 420      15.773  12.402 -47.739  1.00 33.54           C  
ANISOU 3515  CD1 TRP A 420     4555   4305   3881    244    325    -53       C  
ATOM   3516  CD2 TRP A 420      17.194  14.136 -47.445  1.00 34.20           C  
ANISOU 3516  CD2 TRP A 420     4695   4284   4015    236    429    -68       C  
ATOM   3517  NE1 TRP A 420      16.879  11.929 -47.082  1.00 32.18           N  
ANISOU 3517  NE1 TRP A 420     4384   4087   3754    193    295   -102       N  
ATOM   3518  CE2 TRP A 420      17.773  12.923 -46.891  1.00 33.78           C  
ANISOU 3518  CE2 TRP A 420     4614   4233   3986    184    351   -115       C  
ATOM   3519  CE3 TRP A 420      17.915  15.312 -47.383  1.00 36.47           C  
ANISOU 3519  CE3 TRP A 420     5021   4508   4325    233    507    -75       C  
ATOM   3520  CZ2 TRP A 420      19.007  12.917 -46.274  1.00 35.57           C  
ANISOU 3520  CZ2 TRP A 420     4844   4417   4254    138    345   -163       C  
ATOM   3521  CZ3 TRP A 420      19.176  15.291 -46.764  1.00 37.39           C  
ANISOU 3521  CZ3 TRP A 420     5140   4581   4485    173    503   -133       C  
ATOM   3522  CH2 TRP A 420      19.697  14.124 -46.219  1.00 36.58           C  
ANISOU 3522  CH2 TRP A 420     5002   4496   4400    130    420   -175       C  
ATOM   3523  N   ASN A 421      12.965  17.410 -48.315  1.00 35.42           N  
ANISOU 3523  N   ASN A 421     4907   4526   4023    497    639    175       N  
ATOM   3524  CA  ASN A 421      12.058  18.247 -49.074  1.00 38.01           C  
ANISOU 3524  CA  ASN A 421     5243   4893   4304    593    702    254       C  
ATOM   3525  C   ASN A 421      12.835  19.249 -49.892  1.00 37.81           C  
ANISOU 3525  C   ASN A 421     5265   4807   4292    628    793    276       C  
ATOM   3526  O   ASN A 421      13.332  20.250 -49.360  1.00 37.91           O  
ANISOU 3526  O   ASN A 421     5337   4722   4342    619    875    270       O  
ATOM   3527  CB  ASN A 421      11.023  18.948 -48.167  1.00 40.03           C  
ANISOU 3527  CB  ASN A 421     5517   5142   4550    631    742    292       C  
ATOM   3528  CG  ASN A 421      10.051  19.831 -48.956  1.00 43.43           C  
ANISOU 3528  CG  ASN A 421     5952   5620   4928    745    812    383       C  
ATOM   3529  OD1 ASN A 421      10.152  19.956 -50.185  1.00 44.13           O  
ANISOU 3529  OD1 ASN A 421     6032   5749   4985    797    831    420       O  
ATOM   3530  ND2 ASN A 421       9.104  20.450 -48.250  1.00 44.61           N  
ANISOU 3530  ND2 ASN A 421     6114   5768   5066    790    852    422       N  
ATOM   3531  N   PHE A 422      12.922  18.982 -51.196  1.00 36.59           N  
ANISOU 3531  N   PHE A 422     5087   4712   4104    663    784    299       N  
ATOM   3532  CA  PHE A 422      13.722  19.801 -52.093  1.00 36.37           C  
ANISOU 3532  CA  PHE A 422     5102   4632   4084    691    865    318       C  
ATOM   3533  C   PHE A 422      13.338  21.282 -52.074  1.00 36.90           C  
ANISOU 3533  C   PHE A 422     5232   4640   4145    769    987    387       C  
ATOM   3534  O   PHE A 422      14.156  22.125 -52.411  1.00 36.34           O  
ANISOU 3534  O   PHE A 422     5219   4485   4102    772   1075    389       O  
ATOM   3535  CB  PHE A 422      13.689  19.257 -53.524  1.00 36.16           C  
ANISOU 3535  CB  PHE A 422     5034   4695   4008    724    834    340       C  
ATOM   3536  CG  PHE A 422      14.843  19.729 -54.373  1.00 35.48           C  
ANISOU 3536  CG  PHE A 422     4985   4552   3944    719    893    330       C  
ATOM   3537  CD1 PHE A 422      16.121  19.202 -54.184  1.00 32.44           C  
ANISOU 3537  CD1 PHE A 422     4600   4111   3612    630    863    248       C  
ATOM   3538  CD2 PHE A 422      14.657  20.726 -55.346  1.00 36.32           C  
ANISOU 3538  CD2 PHE A 422     5126   4659   4014    806    984    407       C  
ATOM   3539  CE1 PHE A 422      17.194  19.631 -54.960  1.00 33.27           C  
ANISOU 3539  CE1 PHE A 422     4736   4168   3737    620    919    235       C  
ATOM   3540  CE2 PHE A 422      15.736  21.171 -56.123  1.00 36.63           C  
ANISOU 3540  CE2 PHE A 422     5204   4641   4073    797   1045    397       C  
ATOM   3541  CZ  PHE A 422      17.012  20.616 -55.927  1.00 34.20           C  
ANISOU 3541  CZ  PHE A 422     4891   4281   3820    699   1011    307       C  
ATOM   3542  N   ASN A 423      12.105  21.579 -51.667  1.00 38.67           N  
ANISOU 3542  N   ASN A 423     5448   4906   4337    831    998    442       N  
ATOM   3543  CA  ASN A 423      11.612  22.969 -51.529  1.00 42.26           C  
ANISOU 3543  CA  ASN A 423     5966   5302   4788    914   1119    513       C  
ATOM   3544  C   ASN A 423      11.950  23.643 -50.187  1.00 40.96           C  
ANISOU 3544  C   ASN A 423     5860   5017   4684    861   1177    471       C  
ATOM   3545  O   ASN A 423      11.764  24.858 -50.037  1.00 39.83           O  
ANISOU 3545  O   ASN A 423     5784   4797   4551    915   1295    517       O  
ATOM   3546  CB  ASN A 423      10.093  23.021 -51.723  1.00 46.69           C  
ANISOU 3546  CB  ASN A 423     6485   5970   5281   1015   1109    595       C  
ATOM   3547  CG  ASN A 423       9.643  22.351 -53.004  1.00 55.74           C  
ANISOU 3547  CG  ASN A 423     7563   7256   6356   1065   1050    633       C  
ATOM   3548  OD1 ASN A 423      10.034  22.754 -54.111  1.00 60.88           O  
ANISOU 3548  OD1 ASN A 423     8233   7912   6986   1113   1097    672       O  
ATOM   3549  ND2 ASN A 423       8.812  21.315 -52.865  1.00 58.60           N  
ANISOU 3549  ND2 ASN A 423     7847   7738   6679   1048    948    618       N  
ATOM   3550  N   ASN A 424      12.395  22.851 -49.204  1.00 37.39           N  
ANISOU 3550  N   ASN A 424     5384   4553   4268    757   1098    388       N  
ATOM   3551  CA  ASN A 424      12.709  23.371 -47.875  1.00 34.26           C  
ANISOU 3551  CA  ASN A 424     5033   4063   3922    695   1140    340       C  
ATOM   3552  C   ASN A 424      13.947  22.667 -47.357  1.00 32.80           C  
ANISOU 3552  C   ASN A 424     4834   3847   3781    578   1078    242       C  
ATOM   3553  O   ASN A 424      13.854  21.721 -46.577  1.00 31.96           O  
ANISOU 3553  O   ASN A 424     4683   3779   3679    520    983    198       O  
ATOM   3554  CB  ASN A 424      11.505  23.192 -46.925  1.00 34.18           C  
ANISOU 3554  CB  ASN A 424     4998   4095   3891    714   1107    358       C  
ATOM   3555  CG  ASN A 424      11.565  24.113 -45.698  1.00 34.16           C  
ANISOU 3555  CG  ASN A 424     5057   3993   3929    682   1189    333       C  
ATOM   3556  OD1 ASN A 424      12.461  24.949 -45.571  1.00 34.74           O  
ANISOU 3556  OD1 ASN A 424     5192   3963   4041    647   1279    303       O  
ATOM   3557  ND2 ASN A 424      10.603  23.964 -44.801  1.00 33.21           N  
ANISOU 3557  ND2 ASN A 424     4918   3904   3795    689   1162    342       N  
ATOM   3558  N   GLN A 425      15.108  23.121 -47.827  1.00 33.41           N  
ANISOU 3558  N   GLN A 425     4946   3858   3888    546   1135    212       N  
ATOM   3559  CA  GLN A 425      16.381  22.402 -47.661  1.00 33.95           C  
ANISOU 3559  CA  GLN A 425     4989   3916   3991    449   1074    127       C  
ATOM   3560  C   GLN A 425      17.122  22.829 -46.394  1.00 33.73           C  
ANISOU 3560  C   GLN A 425     4991   3814   4008    359   1106     53       C  
ATOM   3561  O   GLN A 425      17.104  24.004 -46.021  1.00 33.05           O  
ANISOU 3561  O   GLN A 425     4969   3649   3938    362   1218     59       O  
ATOM   3562  CB  GLN A 425      17.296  22.570 -48.903  1.00 33.16           C  
ANISOU 3562  CB  GLN A 425     4902   3801   3896    456   1111    126       C  
ATOM   3563  CG  GLN A 425      16.577  22.474 -50.246  1.00 33.32           C  
ANISOU 3563  CG  GLN A 425     4906   3889   3865    553   1110    206       C  
ATOM   3564  CD  GLN A 425      17.475  22.096 -51.436  1.00 33.73           C  
ANISOU 3564  CD  GLN A 425     4941   3958   3914    543   1097    190       C  
ATOM   3565  OE1 GLN A 425      18.707  22.073 -51.347  1.00 32.72           O  
ANISOU 3565  OE1 GLN A 425     4822   3780   3828    470   1106    123       O  
ATOM   3566  NE2 GLN A 425      16.840  21.811 -52.567  1.00 33.12           N  
ANISOU 3566  NE2 GLN A 425     4837   3961   3785    617   1077    251       N  
ATOM   3567  N   ILE A 426      17.785  21.867 -45.753  1.00 32.19           N  
ANISOU 3567  N   ILE A 426     4751   3648   3832    279   1012    -14       N  
ATOM   3568  CA  ILE A 426      18.417  22.072 -44.456  1.00 31.09           C  
ANISOU 3568  CA  ILE A 426     4621   3468   3723    190   1019    -86       C  
ATOM   3569  C   ILE A 426      19.909  21.859 -44.631  1.00 32.14           C  
ANISOU 3569  C   ILE A 426     4738   3586   3885    118   1008   -157       C  
ATOM   3570  O   ILE A 426      20.324  20.842 -45.188  1.00 31.81           O  
ANISOU 3570  O   ILE A 426     4647   3598   3841    115    924   -167       O  
ATOM   3571  CB  ILE A 426      17.850  21.067 -43.426  1.00 30.81           C  
ANISOU 3571  CB  ILE A 426     4538   3491   3676    165    911    -99       C  
ATOM   3572  CG1 ILE A 426      16.332  21.240 -43.309  1.00 30.29           C  
ANISOU 3572  CG1 ILE A 426     4481   3449   3578    238    919    -29       C  
ATOM   3573  CG2 ILE A 426      18.584  21.161 -42.076  1.00 31.04           C  
ANISOU 3573  CG2 ILE A 426     4568   3496   3728     71    905   -174       C  
ATOM   3574  CD1 ILE A 426      15.630  20.258 -42.388  1.00 32.11           C  
ANISOU 3574  CD1 ILE A 426     4668   3739   3792    219    820    -35       C  
ATOM   3575  N   SER A 427      20.734  22.818 -44.209  1.00 33.79           N  
ANISOU 3575  N   SER A 427     4988   3728   4121     57   1099   -209       N  
ATOM   3576  CA  SER A 427      22.170  22.687 -44.498  1.00 35.85           C  
ANISOU 3576  CA  SER A 427     5230   3985   4407     -8   1098   -277       C  
ATOM   3577  C   SER A 427      22.755  21.506 -43.730  1.00 34.83           C  
ANISOU 3577  C   SER A 427     5029   3922   4281    -67    975   -333       C  
ATOM   3578  O   SER A 427      22.164  21.036 -42.756  1.00 33.38           O  
ANISOU 3578  O   SER A 427     4826   3770   4086    -76    914   -331       O  
ATOM   3579  CB  SER A 427      22.957  23.980 -44.228  1.00 37.15           C  
ANISOU 3579  CB  SER A 427     5451   4067   4596    -71   1229   -330       C  
ATOM   3580  OG  SER A 427      23.392  24.070 -42.885  1.00 39.84           O  
ANISOU 3580  OG  SER A 427     5779   4411   4946   -160   1220   -404       O  
ATOM   3581  N   ASP A 428      23.918  21.050 -44.157  1.00 34.91           N  
ANISOU 3581  N   ASP A 428     5003   3953   4307   -105    944   -380       N  
ATOM   3582  CA  ASP A 428      24.502  19.851 -43.599  1.00 38.54           C  
ANISOU 3582  CA  ASP A 428     5393   4479   4770   -143    829   -421       C  
ATOM   3583  C   ASP A 428      24.980  19.991 -42.154  1.00 40.10           C  
ANISOU 3583  C   ASP A 428     5574   4690   4971   -222    818   -484       C  
ATOM   3584  O   ASP A 428      25.387  18.996 -41.536  1.00 43.61           O  
ANISOU 3584  O   ASP A 428     5961   5194   5412   -246    721   -510       O  
ATOM   3585  CB  ASP A 428      25.619  19.308 -44.508  1.00 38.94           C  
ANISOU 3585  CB  ASP A 428     5405   4552   4836   -153    802   -451       C  
ATOM   3586  CG  ASP A 428      26.768  20.285 -44.692  1.00 39.82           C  
ANISOU 3586  CG  ASP A 428     5536   4624   4969   -214    896   -512       C  
ATOM   3587  OD1 ASP A 428      26.766  21.373 -44.077  1.00 42.29           O  
ANISOU 3587  OD1 ASP A 428     5893   4889   5285   -257    986   -537       O  
ATOM   3588  OD2 ASP A 428      27.704  19.948 -45.440  1.00 39.15           O  
ANISOU 3588  OD2 ASP A 428     5421   4556   4896   -225    885   -539       O  
ATOM   3589  N   ASP A 429      24.933  21.209 -41.613  1.00 40.13           N  
ANISOU 3589  N   ASP A 429     5627   4639   4978   -262    920   -509       N  
ATOM   3590  CA  ASP A 429      25.365  21.423 -40.226  1.00 42.11           C  
ANISOU 3590  CA  ASP A 429     5862   4910   5225   -345    917   -576       C  
ATOM   3591  C   ASP A 429      24.221  21.745 -39.260  1.00 41.15           C  
ANISOU 3591  C   ASP A 429     5774   4773   5087   -336    930   -549       C  
ATOM   3592  O   ASP A 429      24.450  22.237 -38.152  1.00 43.95           O  
ANISOU 3592  O   ASP A 429     6133   5129   5436   -407    960   -603       O  
ATOM   3593  CB  ASP A 429      26.511  22.449 -40.129  1.00 46.21           C  
ANISOU 3593  CB  ASP A 429     6398   5397   5760   -432   1018   -657       C  
ATOM   3594  CG  ASP A 429      26.069  23.882 -40.436  1.00 51.81           C  
ANISOU 3594  CG  ASP A 429     7197   6005   6479   -428   1170   -645       C  
ATOM   3595  OD1 ASP A 429      24.879  24.125 -40.738  1.00 50.36           O  
ANISOU 3595  OD1 ASP A 429     7061   5782   6290   -350   1197   -568       O  
ATOM   3596  OD2 ASP A 429      26.941  24.780 -40.374  1.00 57.08           O  
ANISOU 3596  OD2 ASP A 429     7889   6636   7161   -504   1268   -714       O  
ATOM   3597  N   ASN A 430      22.994  21.472 -39.694  1.00 38.07           N  
ANISOU 3597  N   ASN A 430     5403   4376   4686   -251    910   -468       N  
ATOM   3598  CA  ASN A 430      21.836  21.571 -38.832  1.00 36.90           C  
ANISOU 3598  CA  ASN A 430     5274   4226   4520   -233    905   -436       C  
ATOM   3599  C   ASN A 430      21.086  20.251 -38.749  1.00 34.27           C  
ANISOU 3599  C   ASN A 430     4895   3957   4167   -186    781   -389       C  
ATOM   3600  O   ASN A 430      19.907  20.181 -39.095  1.00 35.09           O  
ANISOU 3600  O   ASN A 430     5016   4059   4256   -117    780   -323       O  
ATOM   3601  CB  ASN A 430      20.898  22.699 -39.288  1.00 39.62           C  
ANISOU 3601  CB  ASN A 430     5690   4496   4865   -176   1020   -384       C  
ATOM   3602  CG  ASN A 430      20.058  23.268 -38.133  1.00 43.69           C  
ANISOU 3602  CG  ASN A 430     6238   4990   5370   -191   1060   -384       C  
ATOM   3603  OD1 ASN A 430      19.821  22.589 -37.114  1.00 42.50           O  
ANISOU 3603  OD1 ASN A 430     6052   4892   5204   -222    979   -400       O  
ATOM   3604  ND2 ASN A 430      19.605  24.513 -38.287  1.00 43.08           N  
ANISOU 3604  ND2 ASN A 430     6232   4833   5301   -167   1191   -364       N  
ATOM   3605  N   PRO A 431      21.763  19.188 -38.278  1.00 32.07           N  
ANISOU 3605  N   PRO A 431     4559   3739   3886   -222    681   -422       N  
ATOM   3606  CA  PRO A 431      21.078  17.916 -38.127  1.00 31.11           C  
ANISOU 3606  CA  PRO A 431     4402   3669   3748   -185    573   -381       C  
ATOM   3607  C   PRO A 431      19.915  17.961 -37.137  1.00 31.21           C  
ANISOU 3607  C   PRO A 431     4431   3687   3738   -179    564   -355       C  
ATOM   3608  O   PRO A 431      18.901  17.288 -37.350  1.00 33.17           O  
ANISOU 3608  O   PRO A 431     4673   3958   3972   -129    516   -302       O  
ATOM   3609  CB  PRO A 431      22.191  16.968 -37.644  1.00 31.77           C  
ANISOU 3609  CB  PRO A 431     4429   3806   3836   -230    489   -426       C  
ATOM   3610  CG  PRO A 431      23.241  17.847 -37.091  1.00 31.96           C  
ANISOU 3610  CG  PRO A 431     4453   3820   3867   -303    548   -497       C  
ATOM   3611  CD  PRO A 431      23.187  19.094 -37.916  1.00 31.65           C  
ANISOU 3611  CD  PRO A 431     4468   3711   3843   -294    666   -495       C  
ATOM   3612  N   ALA A 432      20.028  18.783 -36.094  1.00 30.46           N  
ANISOU 3612  N   ALA A 432     4358   3574   3641   -234    617   -394       N  
ATOM   3613  CA  ALA A 432      18.987  18.855 -35.073  1.00 29.38           C  
ANISOU 3613  CA  ALA A 432     4236   3443   3482   -236    612   -377       C  
ATOM   3614  C   ALA A 432      17.643  19.304 -35.684  1.00 28.93           C  
ANISOU 3614  C   ALA A 432     4216   3355   3419   -160    662   -309       C  
ATOM   3615  O   ALA A 432      16.597  18.698 -35.428  1.00 27.15           O  
ANISOU 3615  O   ALA A 432     3980   3161   3172   -126    610   -267       O  
ATOM   3616  CB  ALA A 432      19.422  19.768 -33.926  1.00 29.64           C  
ANISOU 3616  CB  ALA A 432     4289   3460   3513   -315    674   -439       C  
ATOM   3617  N   ARG A 433      17.689  20.335 -36.521  1.00 28.90           N  
ANISOU 3617  N   ARG A 433     4255   3295   3431   -130    762   -296       N  
ATOM   3618  CA  ARG A 433      16.518  20.759 -37.271  1.00 30.33           C  
ANISOU 3618  CA  ARG A 433     4466   3456   3602    -44    810   -224       C  
ATOM   3619  C   ARG A 433      15.942  19.616 -38.132  1.00 30.32           C  
ANISOU 3619  C   ARG A 433     4421   3515   3582     16    719   -172       C  
ATOM   3620  O   ARG A 433      14.750  19.372 -38.115  1.00 32.24           O  
ANISOU 3620  O   ARG A 433     4658   3788   3801     64    699   -123       O  
ATOM   3621  CB  ARG A 433      16.861  21.974 -38.149  1.00 31.80           C  
ANISOU 3621  CB  ARG A 433     4703   3570   3806    -18    932   -216       C  
ATOM   3622  CG  ARG A 433      15.691  22.434 -38.990  1.00 33.13           C  
ANISOU 3622  CG  ARG A 433     4899   3727   3959     84    984   -132       C  
ATOM   3623  CD  ARG A 433      16.013  23.579 -39.933  1.00 35.74           C  
ANISOU 3623  CD  ARG A 433     5286   3987   4306    122   1106   -112       C  
ATOM   3624  NE  ARG A 433      14.958  23.689 -40.948  1.00 37.32           N  
ANISOU 3624  NE  ARG A 433     5491   4208   4481    234   1125    -21       N  
ATOM   3625  CZ  ARG A 433      15.093  24.303 -42.124  1.00 37.80           C  
ANISOU 3625  CZ  ARG A 433     5583   4237   4542    294   1198     21       C  
ATOM   3626  NH1 ARG A 433      16.232  24.898 -42.456  1.00 37.49           N  
ANISOU 3626  NH1 ARG A 433     5579   4133   4531    250   1268    -20       N  
ATOM   3627  NH2 ARG A 433      14.077  24.323 -42.968  1.00 39.66           N  
ANISOU 3627  NH2 ARG A 433     5812   4512   4744    398   1204    106       N  
ATOM   3628  N   PHE A 434      16.796  18.934 -38.886  1.00 29.68           N  
ANISOU 3628  N   PHE A 434     4309   3453   3511      9    670   -187       N  
ATOM   3629  CA  PHE A 434      16.380  17.766 -39.667  1.00 30.08           C  
ANISOU 3629  CA  PHE A 434     4320   3562   3547     51    585   -152       C  
ATOM   3630  C   PHE A 434      15.694  16.758 -38.761  1.00 29.19           C  
ANISOU 3630  C   PHE A 434     4178   3497   3415     35    499   -148       C  
ATOM   3631  O   PHE A 434      14.575  16.305 -39.053  1.00 27.53           O  
ANISOU 3631  O   PHE A 434     3954   3325   3179     79    471   -103       O  
ATOM   3632  CB  PHE A 434      17.604  17.132 -40.370  1.00 29.61           C  
ANISOU 3632  CB  PHE A 434     4232   3511   3507     29    545   -185       C  
ATOM   3633  CG  PHE A 434      17.291  15.912 -41.215  1.00 29.08           C  
ANISOU 3633  CG  PHE A 434     4126   3495   3426     63    467   -159       C  
ATOM   3634  CD1 PHE A 434      16.884  16.045 -42.530  1.00 29.67           C  
ANISOU 3634  CD1 PHE A 434     4202   3582   3487    122    492   -118       C  
ATOM   3635  CD2 PHE A 434      17.532  14.624 -40.730  1.00 30.50           C  
ANISOU 3635  CD2 PHE A 434     4268   3710   3608     33    373   -180       C  
ATOM   3636  CE1 PHE A 434      16.664  14.927 -43.330  1.00 30.08           C  
ANISOU 3636  CE1 PHE A 434     4218   3685   3525    143    425   -105       C  
ATOM   3637  CE2 PHE A 434      17.325  13.499 -41.533  1.00 28.96           C  
ANISOU 3637  CE2 PHE A 434     4044   3554   3405     56    312   -165       C  
ATOM   3638  CZ  PHE A 434      16.875  13.650 -42.826  1.00 27.69           C  
ANISOU 3638  CZ  PHE A 434     3883   3409   3228    106    338   -131       C  
ATOM   3639  N   LEU A 435      16.343  16.430 -37.642  1.00 30.11           N  
ANISOU 3639  N   LEU A 435     4283   3616   3541    -29    461   -195       N  
ATOM   3640  CA  LEU A 435      15.724  15.531 -36.674  1.00 30.90           C  
ANISOU 3640  CA  LEU A 435     4362   3754   3621    -47    387   -189       C  
ATOM   3641  C   LEU A 435      14.350  16.027 -36.227  1.00 31.00           C  
ANISOU 3641  C   LEU A 435     4396   3770   3611    -20    421   -153       C  
ATOM   3642  O   LEU A 435      13.364  15.294 -36.330  1.00 32.31           O  
ANISOU 3642  O   LEU A 435     4543   3976   3754      6    375   -119       O  
ATOM   3643  CB  LEU A 435      16.613  15.315 -35.467  1.00 32.59           C  
ANISOU 3643  CB  LEU A 435     4566   3975   3841   -116    354   -240       C  
ATOM   3644  CG  LEU A 435      16.647  13.877 -34.940  1.00 34.29           C  
ANISOU 3644  CG  LEU A 435     4747   4235   4046   -131    252   -238       C  
ATOM   3645  CD1 LEU A 435      17.003  13.898 -33.468  1.00 32.65           C  
ANISOU 3645  CD1 LEU A 435     4535   4042   3826   -188    233   -270       C  
ATOM   3646  CD2 LEU A 435      15.346  13.134 -35.165  1.00 32.56           C  
ANISOU 3646  CD2 LEU A 435     4524   4041   3806    -93    215   -190       C  
ATOM   3647  N   GLN A 436      14.284  17.274 -35.759  1.00 30.41           N  
ANISOU 3647  N   GLN A 436     4361   3652   3542    -29    508   -164       N  
ATOM   3648  CA  GLN A 436      13.037  17.831 -35.266  1.00 31.54           C  
ANISOU 3648  CA  GLN A 436     4525   3792   3665     -1    551   -132       C  
ATOM   3649  C   GLN A 436      11.978  17.894 -36.339  1.00 32.32           C  
ANISOU 3649  C   GLN A 436     4619   3914   3746     82    568    -68       C  
ATOM   3650  O   GLN A 436      10.811  17.580 -36.080  1.00 34.85           O  
ANISOU 3650  O   GLN A 436     4925   4275   4039    109    545    -35       O  
ATOM   3651  CB  GLN A 436      13.237  19.224 -34.678  1.00 32.87           C  
ANISOU 3651  CB  GLN A 436     4742   3898   3847    -24    657   -157       C  
ATOM   3652  CG  GLN A 436      14.079  19.254 -33.428  1.00 34.66           C  
ANISOU 3652  CG  GLN A 436     4968   4119   4079   -114    645   -224       C  
ATOM   3653  CD  GLN A 436      14.729  20.601 -33.214  1.00 39.08           C  
ANISOU 3653  CD  GLN A 436     5574   4613   4659   -151    757   -268       C  
ATOM   3654  OE1 GLN A 436      14.590  21.508 -34.038  1.00 43.15           O  
ANISOU 3654  OE1 GLN A 436     6129   5075   5190   -105    848   -244       O  
ATOM   3655  NE2 GLN A 436      15.459  20.737 -32.114  1.00 38.61           N  
ANISOU 3655  NE2 GLN A 436     5512   4558   4599   -237    755   -334       N  
ATOM   3656  N   LYS A 437      12.357  18.304 -37.543  1.00 31.05           N  
ANISOU 3656  N   LYS A 437     4468   3735   3595    124    609    -49       N  
ATOM   3657  CA  LYS A 437      11.386  18.350 -38.631  1.00 33.09           C  
ANISOU 3657  CA  LYS A 437     4714   4030   3826    209    623     13       C  
ATOM   3658  C   LYS A 437      10.819  16.937 -38.880  1.00 30.84           C  
ANISOU 3658  C   LYS A 437     4375   3826   3515    210    519     25       C  
ATOM   3659  O   LYS A 437       9.630  16.767 -39.091  1.00 33.33           O  
ANISOU 3659  O   LYS A 437     4670   4197   3797    255    509     66       O  
ATOM   3660  CB  LYS A 437      12.004  18.961 -39.907  1.00 34.89           C  
ANISOU 3660  CB  LYS A 437     4961   4229   4067    250    682     30       C  
ATOM   3661  CG  LYS A 437      11.000  19.276 -40.998  1.00 37.45           C  
ANISOU 3661  CG  LYS A 437     5278   4594   4357    347    715    103       C  
ATOM   3662  CD  LYS A 437      11.717  19.767 -42.240  1.00 43.09           C  
ANISOU 3662  CD  LYS A 437     6010   5281   5079    382    766    118       C  
ATOM   3663  CE  LYS A 437      10.971  19.380 -43.511  1.00 48.45           C  
ANISOU 3663  CE  LYS A 437     6651   6041   5714    459    742    177       C  
ATOM   3664  NZ  LYS A 437       9.918  20.369 -43.885  1.00 54.71           N  
ANISOU 3664  NZ  LYS A 437     7463   6846   6476    556    823    252       N  
ATOM   3665  N   ALA A 438      11.661  15.924 -38.782  1.00 29.05           N  
ANISOU 3665  N   ALA A 438     4126   3606   3303    157    445    -14       N  
ATOM   3666  CA  ALA A 438      11.204  14.550 -38.982  1.00 28.30           C  
ANISOU 3666  CA  ALA A 438     3989   3573   3188    149    357    -11       C  
ATOM   3667  C   ALA A 438      10.226  14.095 -37.887  1.00 29.86           C  
ANISOU 3667  C   ALA A 438     4178   3801   3365    127    322     -7       C  
ATOM   3668  O   ALA A 438       9.338  13.296 -38.145  1.00 29.89           O  
ANISOU 3668  O   ALA A 438     4151   3864   3339    138    278     10       O  
ATOM   3669  CB  ALA A 438      12.392  13.611 -39.071  1.00 26.74           C  
ANISOU 3669  CB  ALA A 438     3777   3365   3016    103    297    -52       C  
ATOM   3670  N   MET A 439      10.380  14.610 -36.671  1.00 30.81           N  
ANISOU 3670  N   MET A 439     4323   3885   3496     91    344    -27       N  
ATOM   3671  CA  MET A 439       9.479  14.214 -35.570  1.00 33.32           C  
ANISOU 3671  CA  MET A 439     4636   4230   3793     67    314    -25       C  
ATOM   3672  C   MET A 439       8.175  15.044 -35.460  1.00 35.06           C  
ANISOU 3672  C   MET A 439     4863   4469   3987    116    372     13       C  
ATOM   3673  O   MET A 439       7.327  14.751 -34.626  1.00 35.64           O  
ANISOU 3673  O   MET A 439     4929   4570   4040     99    352     17       O  
ATOM   3674  CB  MET A 439      10.232  14.167 -34.243  1.00 30.31           C  
ANISOU 3674  CB  MET A 439     4271   3816   3426      0    297    -67       C  
ATOM   3675  CG  MET A 439      11.272  13.060 -34.191  1.00 31.04           C  
ANISOU 3675  CG  MET A 439     4346   3912   3534    -39    224    -95       C  
ATOM   3676  SD  MET A 439      10.517  11.410 -34.249  1.00 32.77           S  
ANISOU 3676  SD  MET A 439     4536   4183   3731    -45    138    -78       S  
ATOM   3677  CE  MET A 439      10.712  10.895 -35.967  1.00 29.80           C  
ANISOU 3677  CE  MET A 439     4136   3824   3361     -5    126    -67       C  
ATOM   3678  N   ASP A 440       8.035  16.056 -36.314  1.00 36.17           N  
ANISOU 3678  N   ASP A 440     5018   4595   4128    178    445     44       N  
ATOM   3679  CA  ASP A 440       6.788  16.816 -36.479  1.00 41.00           C  
ANISOU 3679  CA  ASP A 440     5630   5234   4713    247    503     94       C  
ATOM   3680  C   ASP A 440       5.585  15.908 -36.793  1.00 43.75           C  
ANISOU 3680  C   ASP A 440     5925   5677   5017    269    445    121       C  
ATOM   3681  O   ASP A 440       5.695  14.943 -37.552  1.00 39.61           O  
ANISOU 3681  O   ASP A 440     5368   5200   4482    261    385    116       O  
ATOM   3682  CB  ASP A 440       6.932  17.861 -37.611  1.00 41.39           C  
ANISOU 3682  CB  ASP A 440     5699   5258   4766    323    584    133       C  
ATOM   3683  CG  ASP A 440       7.615  19.163 -37.158  1.00 43.12           C  
ANISOU 3683  CG  ASP A 440     5981   5381   5021    316    682    117       C  
ATOM   3684  OD1 ASP A 440       7.722  19.412 -35.945  1.00 44.92           O  
ANISOU 3684  OD1 ASP A 440     6233   5572   5263    262    696     81       O  
ATOM   3685  OD2 ASP A 440       8.003  19.973 -38.035  1.00 46.45           O  
ANISOU 3685  OD2 ASP A 440     6429   5764   5453    364    753    140       O  
ATOM   3686  N   PHE A 441       4.432  16.293 -36.255  1.00 48.33           N  
ANISOU 3686  N   PHE A 441     6500   6290   5573    297    473    146       N  
ATOM   3687  CA  PHE A 441       3.201  15.499 -36.249  1.00 56.35           C  
ANISOU 3687  CA  PHE A 441     7465   7400   6544    303    424    162       C  
ATOM   3688  C   PHE A 441       2.559  15.132 -37.615  1.00 60.40           C  
ANISOU 3688  C   PHE A 441     7925   8008   7016    360    406    197       C  
ATOM   3689  O   PHE A 441       2.123  13.990 -37.794  1.00 62.11           O  
ANISOU 3689  O   PHE A 441     8099   8294   7206    325    338    181       O  
ATOM   3690  CB  PHE A 441       2.179  16.199 -35.327  1.00 62.78           C  
ANISOU 3690  CB  PHE A 441     8287   8222   7343    325    472    180       C  
ATOM   3691  CG  PHE A 441       0.811  15.563 -35.301  1.00 68.58           C  
ANISOU 3691  CG  PHE A 441     8966   9062   8030    336    436    198       C  
ATOM   3692  CD1 PHE A 441       0.564  14.429 -34.525  1.00 68.60           C  
ANISOU 3692  CD1 PHE A 441     8951   9090   8022    258    366    162       C  
ATOM   3693  CD2 PHE A 441      -0.255  16.142 -35.998  1.00 71.74           C  
ANISOU 3693  CD2 PHE A 441     9331   9537   8390    427    478    252       C  
ATOM   3694  CE1 PHE A 441      -0.706  13.869 -34.472  1.00 69.77           C  
ANISOU 3694  CE1 PHE A 441     9049   9335   8125    259    340    172       C  
ATOM   3695  CE2 PHE A 441      -1.526  15.582 -35.949  1.00 72.53           C  
ANISOU 3695  CE2 PHE A 441     9371   9745   8440    433    446    263       C  
ATOM   3696  CZ  PHE A 441      -1.751  14.445 -35.184  1.00 71.53           C  
ANISOU 3696  CZ  PHE A 441     9229   9641   8307    344    378    219       C  
ATOM   3697  N   PRO A 442       2.480  16.088 -38.571  1.00 61.53           N  
ANISOU 3697  N   PRO A 442     8071   8157   7149    446    469    244       N  
ATOM   3698  CA  PRO A 442       1.600  15.877 -39.742  1.00 64.39           C  
ANISOU 3698  CA  PRO A 442     8374   8634   7456    511    458    286       C  
ATOM   3699  C   PRO A 442       1.694  14.501 -40.429  1.00 63.67           C  
ANISOU 3699  C   PRO A 442     8236   8612   7344    461    374    254       C  
ATOM   3700  O   PRO A 442       0.669  13.957 -40.843  1.00 67.56           O  
ANISOU 3700  O   PRO A 442     8667   9218   7782    473    344    265       O  
ATOM   3701  CB  PRO A 442       2.023  16.996 -40.699  1.00 62.09           C  
ANISOU 3701  CB  PRO A 442     8109   8310   7170    597    534    334       C  
ATOM   3702  CG  PRO A 442       2.433  18.095 -39.783  1.00 62.67           C  
ANISOU 3702  CG  PRO A 442     8252   8271   7289    600    612    333       C  
ATOM   3703  CD  PRO A 442       3.136  17.409 -38.632  1.00 63.73           C  
ANISOU 3703  CD  PRO A 442     8408   8344   7462    489    560    263       C  
ATOM   3704  N   PHE A 443       2.899  13.947 -40.534  1.00 61.41           N  
ANISOU 3704  N   PHE A 443     7975   8261   7097    404    341    213       N  
ATOM   3705  CA  PHE A 443       3.105  12.670 -41.230  1.00 64.53           C  
ANISOU 3705  CA  PHE A 443     8333   8705   7478    357    272    180       C  
ATOM   3706  C   PHE A 443       2.355  11.497 -40.566  1.00 63.49           C  
ANISOU 3706  C   PHE A 443     8172   8624   7326    290    213    147       C  
ATOM   3707  O   PHE A 443       1.916  10.563 -41.251  1.00 65.71           O  
ANISOU 3707  O   PHE A 443     8408   8987   7572    267    173    131       O  
ATOM   3708  CB  PHE A 443       4.614  12.348 -41.348  1.00 62.25           C  
ANISOU 3708  CB  PHE A 443     8082   8325   7242    312    254    142       C  
ATOM   3709  CG  PHE A 443       5.164  11.616 -40.158  1.00 58.55           C  
ANISOU 3709  CG  PHE A 443     7639   7794   6811    231    211     96       C  
ATOM   3710  CD1 PHE A 443       5.501  12.310 -38.992  1.00 55.82           C  
ANISOU 3710  CD1 PHE A 443     7335   7375   6496    217    240     91       C  
ATOM   3711  CD2 PHE A 443       5.278  10.221 -40.171  1.00 57.11           C  
ANISOU 3711  CD2 PHE A 443     7439   7630   6629    170    146     59       C  
ATOM   3712  CE1 PHE A 443       5.980  11.637 -37.877  1.00 53.77           C  
ANISOU 3712  CE1 PHE A 443     7096   7072   6262    147    198     54       C  
ATOM   3713  CE2 PHE A 443       5.752   9.539 -39.055  1.00 55.03           C  
ANISOU 3713  CE2 PHE A 443     7202   7312   6395    106    110     27       C  
ATOM   3714  CZ  PHE A 443       6.105  10.248 -37.910  1.00 56.08           C  
ANISOU 3714  CZ  PHE A 443     7371   7383   6553     96    132     27       C  
ATOM   3715  N   ILE A 444       2.225  11.549 -39.238  1.00 62.11           N  
ANISOU 3715  N   ILE A 444     8024   8402   7171    253    212    134       N  
ATOM   3716  CA  ILE A 444       1.636  10.439 -38.452  1.00 65.40           C  
ANISOU 3716  CA  ILE A 444     8425   8848   7574    181    161    102       C  
ATOM   3717  C   ILE A 444       0.167  10.739 -38.071  1.00 67.78           C  
ANISOU 3717  C   ILE A 444     8690   9234   7828    206    179    126       C  
ATOM   3718  O   ILE A 444      -0.445   9.995 -37.290  1.00 68.42           O  
ANISOU 3718  O   ILE A 444     8762   9339   7896    150    149    103       O  
ATOM   3719  CB  ILE A 444       2.518  10.094 -37.192  1.00 59.14           C  
ANISOU 3719  CB  ILE A 444     7684   7954   6829    115    139     70       C  
ATOM   3720  CG1 ILE A 444       2.033   8.832 -36.445  1.00 59.38           C  
ANISOU 3720  CG1 ILE A 444     7708   8005   6848     41     88     40       C  
ATOM   3721  CG2 ILE A 444       2.585  11.268 -36.232  1.00 58.64           C  
ANISOU 3721  CG2 ILE A 444     7658   7836   6786    136    189     85       C  
ATOM   3722  CD1 ILE A 444       2.596   7.517 -36.955  1.00 52.08           C  
ANISOU 3722  CD1 ILE A 444     6780   7072   5933     -7     40      7       C  
ATOM   3723  N   CYS A 445      -0.398  11.800 -38.663  1.00 69.28           N  
ANISOU 3723  N   CYS A 445     8858   9471   7990    295    231    175       N  
ATOM   3724  CA  CYS A 445      -1.722  12.324 -38.267  1.00 73.05           C  
ANISOU 3724  CA  CYS A 445     9302  10024   8427    338    261    206       C  
ATOM   3725  C   CYS A 445      -2.880  11.316 -38.398  1.00 73.25           C  
ANISOU 3725  C   CYS A 445     9260  10175   8396    300    217    187       C  
ATOM   3726  O   CYS A 445      -3.795  11.307 -37.560  1.00 71.58           O  
ANISOU 3726  O   CYS A 445     9032   9999   8164    286    221    186       O  
ATOM   3727  CB  CYS A 445      -2.052  13.668 -38.977  1.00 78.33           C  
ANISOU 3727  CB  CYS A 445     9963  10721   9077    455    332    271       C  
ATOM   3728  SG  CYS A 445      -2.486  13.611 -40.750  1.00 81.55           S  
ANISOU 3728  SG  CYS A 445    10300  11262   9421    528    327    308       S  
ATOM   3729  N   ASN A 446      -2.819  10.457 -39.424  1.00 70.77           N  
ANISOU 3729  N   ASN A 446     8906   9925   8055    276    178    166       N  
ATOM   3730  CA  ASN A 446      -3.862   9.436 -39.662  1.00 69.49           C  
ANISOU 3730  CA  ASN A 446     8678   9887   7836    226    141    136       C  
ATOM   3731  C   ASN A 446      -3.713   8.162 -38.807  1.00 67.64           C  
ANISOU 3731  C   ASN A 446     8469   9605   7624    112     97     76       C  
ATOM   3732  O   ASN A 446      -4.381   7.148 -39.046  1.00 68.24           O  
ANISOU 3732  O   ASN A 446     8502   9764   7661     51     68     39       O  
ATOM   3733  CB  ASN A 446      -3.982   9.103 -41.161  1.00 69.78           C  
ANISOU 3733  CB  ASN A 446     8656  10030   7825    248    127    135       C  
ATOM   3734  CG  ASN A 446      -5.030   9.961 -41.871  1.00 71.60           C  
ANISOU 3734  CG  ASN A 446     8817  10399   7987    347    159    190       C  
ATOM   3735  OD1 ASN A 446      -6.176  10.076 -41.413  1.00 69.53           O  
ANISOU 3735  OD1 ASN A 446     8509  10225   7683    358    167    200       O  
ATOM   3736  ND2 ASN A 446      -4.645  10.555 -43.004  1.00 67.91           N  
ANISOU 3736  ND2 ASN A 446     8338   9958   7504    423    180    229       N  
ATOM   3737  N   SER A 447      -2.830   8.234 -37.815  1.00 64.82           N  
ANISOU 3737  N   SER A 447     8183   9117   7327     83     95     69       N  
ATOM   3738  CA  SER A 447      -2.703   7.212 -36.790  1.00 61.21           C  
ANISOU 3738  CA  SER A 447     7759   8605   6892     -9     63     28       C  
ATOM   3739  C   SER A 447      -3.175   7.839 -35.478  1.00 61.78           C  
ANISOU 3739  C   SER A 447     7853   8649   6969     -5     86     44       C  
ATOM   3740  O   SER A 447      -3.269   7.166 -34.451  1.00 63.35           O  
ANISOU 3740  O   SER A 447     8079   8813   7178    -73     66     19       O  
ATOM   3741  CB  SER A 447      -1.236   6.795 -36.669  1.00 62.30           C  
ANISOU 3741  CB  SER A 447     7958   8624   7090    -40     41      9       C  
ATOM   3742  OG  SER A 447      -1.086   5.391 -36.635  1.00 63.63           O  
ANISOU 3742  OG  SER A 447     8134   8779   7262   -119      4    -32       O  
ATOM   3743  N   PHE A 448      -3.477   9.136 -35.536  1.00 58.57           N  
ANISOU 3743  N   PHE A 448     7439   8259   6556     77    133     86       N  
ATOM   3744  CA  PHE A 448      -3.822   9.928 -34.355  1.00 57.17           C  
ANISOU 3744  CA  PHE A 448     7288   8045   6389     91    167    102       C  
ATOM   3745  C   PHE A 448      -5.205  10.567 -34.467  1.00 52.49           C  
ANISOU 3745  C   PHE A 448     6637   7560   5744    151    203    134       C  
ATOM   3746  O   PHE A 448      -5.362  11.774 -34.264  1.00 53.24           O  
ANISOU 3746  O   PHE A 448     6744   7636   5846    224    259    172       O  
ATOM   3747  CB  PHE A 448      -2.773  11.023 -34.138  1.00 61.23           C  
ANISOU 3747  CB  PHE A 448     7859   8451   6952    134    207    122       C  
ATOM   3748  CG  PHE A 448      -1.770  10.703 -33.075  1.00 58.51           C  
ANISOU 3748  CG  PHE A 448     7575   8000   6653     66    186     91       C  
ATOM   3749  CD1 PHE A 448      -0.929   9.601 -33.197  1.00 60.10           C  
ANISOU 3749  CD1 PHE A 448     7793   8165   6875      6    133     60       C  
ATOM   3750  CD2 PHE A 448      -1.650  11.519 -31.955  1.00 58.69           C  
ANISOU 3750  CD2 PHE A 448     7639   7963   6697     65    223     94       C  
ATOM   3751  CE1 PHE A 448      -0.006   9.302 -32.201  1.00 57.17           C  
ANISOU 3751  CE1 PHE A 448     7472   7709   6540    -46    112     38       C  
ATOM   3752  CE2 PHE A 448      -0.719  11.237 -30.967  1.00 57.43           C  
ANISOU 3752  CE2 PHE A 448     7528   7721   6570      3    202     65       C  
ATOM   3753  CZ  PHE A 448       0.102  10.126 -31.091  1.00 57.83           C  
ANISOU 3753  CZ  PHE A 448     7589   7745   6636    -48    144     40       C  
ATOM   3754  N   THR A 449      -6.205   9.753 -34.783  1.00 48.45           N  
ANISOU 3754  N   THR A 449     6062   7164   5181    119    176    116       N  
ATOM   3755  CA  THR A 449      -7.550  10.249 -35.021  1.00 47.78           C  
ANISOU 3755  CA  THR A 449     5906   7209   5038    178    203    144       C  
ATOM   3756  C   THR A 449      -8.504   9.809 -33.909  1.00 47.64           C  
ANISOU 3756  C   THR A 449     5874   7226   4999    117    198    119       C  
ATOM   3757  O   THR A 449      -8.097   9.137 -32.946  1.00 46.38           O  
ANISOU 3757  O   THR A 449     5766   6985   4871     31    174     83       O  
ATOM   3758  CB  THR A 449      -8.092   9.732 -36.361  1.00 47.64           C  
ANISOU 3758  CB  THR A 449     5808   7329   4961    191    181    140       C  
ATOM   3759  OG1 THR A 449      -8.357   8.329 -36.252  1.00 47.07           O  
ANISOU 3759  OG1 THR A 449     5717   7294   4870     80    134     80       O  
ATOM   3760  CG2 THR A 449      -7.081   9.958 -37.468  1.00 46.76           C  
ANISOU 3760  CG2 THR A 449     5715   7182   4870    233    179    157       C  
ATOM   3761  N   LYS A 450      -9.777  10.177 -34.063  1.00 47.82           N  
ANISOU 3761  N   LYS A 450     5824   7377   4966    164    221    139       N  
ATOM   3762  CA  LYS A 450     -10.832   9.773 -33.136  1.00 46.59           C  
ANISOU 3762  CA  LYS A 450     5641   7279   4780    110    219    114       C  
ATOM   3763  C   LYS A 450     -11.009   8.261 -33.165  1.00 43.52           C  
ANISOU 3763  C   LYS A 450     5236   6928   4372     -8    168     52       C  
ATOM   3764  O   LYS A 450     -11.461   7.667 -32.195  1.00 42.60           O  
ANISOU 3764  O   LYS A 450     5131   6804   4251    -86    160     20       O  
ATOM   3765  CB  LYS A 450     -12.175  10.436 -33.488  1.00 51.60           C  
ANISOU 3765  CB  LYS A 450     6186   8066   5352    193    252    149       C  
ATOM   3766  CG  LYS A 450     -12.095  11.712 -34.314  1.00 56.48           C  
ANISOU 3766  CG  LYS A 450     6788   8705   5964    333    299    218       C  
ATOM   3767  CD  LYS A 450     -13.478  12.289 -34.604  1.00 58.73           C  
ANISOU 3767  CD  LYS A 450     6978   9152   6181    420    331    257       C  
ATOM   3768  CE  LYS A 450     -13.965  11.934 -36.001  1.00 60.66           C  
ANISOU 3768  CE  LYS A 450     7127   9564   6355    453    305    265       C  
ATOM   3769  NZ  LYS A 450     -13.194  12.626 -37.078  1.00 65.30           N  
ANISOU 3769  NZ  LYS A 450     7734  10123   6955    548    323    317       N  
ATOM   3770  N   PHE A 451     -10.678   7.646 -34.292  1.00 42.31           N  
ANISOU 3770  N   PHE A 451     5056   6814   4203    -23    140     35       N  
ATOM   3771  CA  PHE A 451     -10.789   6.199 -34.416  1.00 42.79           C  
ANISOU 3771  CA  PHE A 451     5108   6900   4248   -138    102    -27       C  
ATOM   3772  C   PHE A 451      -9.832   5.495 -33.469  1.00 41.85           C  
ANISOU 3772  C   PHE A 451     5085   6625   4191   -218     83    -53       C  
ATOM   3773  O   PHE A 451     -10.178   4.488 -32.873  1.00 41.30           O  
ANISOU 3773  O   PHE A 451     5026   6551   4113   -314     71    -95       O  
ATOM   3774  CB  PHE A 451     -10.511   5.757 -35.843  1.00 44.29           C  
ANISOU 3774  CB  PHE A 451     5258   7154   4414   -135     82    -41       C  
ATOM   3775  CG  PHE A 451     -11.745   5.592 -36.681  1.00 48.24           C  
ANISOU 3775  CG  PHE A 451     5648   7852   4829   -129     83    -55       C  
ATOM   3776  CD1 PHE A 451     -12.721   4.660 -36.334  1.00 49.16           C  
ANISOU 3776  CD1 PHE A 451     5721   8055   4901   -227     76   -111       C  
ATOM   3777  CD2 PHE A 451     -11.915   6.337 -37.845  1.00 49.89           C  
ANISOU 3777  CD2 PHE A 451     5793   8166   4997    -30     92    -14       C  
ATOM   3778  CE1 PHE A 451     -13.853   4.492 -37.116  1.00 51.55           C  
ANISOU 3778  CE1 PHE A 451     5912   8556   5119   -229     76   -131       C  
ATOM   3779  CE2 PHE A 451     -13.043   6.166 -38.637  1.00 49.86           C  
ANISOU 3779  CE2 PHE A 451     5677   8362   4905    -23     89    -27       C  
ATOM   3780  CZ  PHE A 451     -14.007   5.242 -38.276  1.00 50.68           C  
ANISOU 3780  CZ  PHE A 451     5732   8560   4964   -126     79    -89       C  
ATOM   3781  N   GLU A 452      -8.625   6.033 -33.335  1.00 40.72           N  
ANISOU 3781  N   GLU A 452     5007   6356   4105   -178     85    -26       N  
ATOM   3782  CA  GLU A 452      -7.642   5.429 -32.469  1.00 40.49           C  
ANISOU 3782  CA  GLU A 452     5063   6190   4131   -241     65    -44       C  
ATOM   3783  C   GLU A 452      -7.869   5.773 -31.001  1.00 38.75           C  
ANISOU 3783  C   GLU A 452     4881   5918   3923   -259     80    -37       C  
ATOM   3784  O   GLU A 452      -7.702   4.917 -30.142  1.00 36.18           O  
ANISOU 3784  O   GLU A 452     4600   5536   3611   -337     62    -61       O  
ATOM   3785  CB  GLU A 452      -6.225   5.801 -32.901  1.00 42.01           C  
ANISOU 3785  CB  GLU A 452     5304   6281   4376   -200     58    -26       C  
ATOM   3786  CG  GLU A 452      -5.744   5.047 -34.142  1.00 46.69           C  
ANISOU 3786  CG  GLU A 452     5879   6892   4966   -216     34    -49       C  
ATOM   3787  CD  GLU A 452      -6.204   5.681 -35.456  1.00 47.72           C  
ANISOU 3787  CD  GLU A 452     5941   7134   5056   -142     49    -27       C  
ATOM   3788  OE1 GLU A 452      -6.063   5.023 -36.509  1.00 50.99           O  
ANISOU 3788  OE1 GLU A 452     6327   7593   5453   -162     32    -51       O  
ATOM   3789  OE2 GLU A 452      -6.689   6.838 -35.448  1.00 46.75           O  
ANISOU 3789  OE2 GLU A 452     5792   7054   4916    -61     81     14       O  
ATOM   3790  N   PHE A 453      -8.280   7.012 -30.722  1.00 38.01           N  
ANISOU 3790  N   PHE A 453     4772   5845   3823   -185    117     -1       N  
ATOM   3791  CA  PHE A 453      -8.226   7.542 -29.351  1.00 37.04           C  
ANISOU 3791  CA  PHE A 453     4697   5652   3722   -194    138      6       C  
ATOM   3792  C   PHE A 453      -9.561   7.646 -28.604  1.00 37.11           C  
ANISOU 3792  C   PHE A 453     4670   5740   3690   -209    160      2       C  
ATOM   3793  O   PHE A 453      -9.574   7.932 -27.406  1.00 38.24           O  
ANISOU 3793  O   PHE A 453     4853   5830   3847   -231    176      1       O  
ATOM   3794  CB  PHE A 453      -7.497   8.891 -29.321  1.00 37.38           C  
ANISOU 3794  CB  PHE A 453     4775   5625   3802   -112    175     42       C  
ATOM   3795  CG  PHE A 453      -6.028   8.777 -29.558  1.00 39.03           C  
ANISOU 3795  CG  PHE A 453     5037   5730   4059   -119    153     38       C  
ATOM   3796  CD1 PHE A 453      -5.192   8.279 -28.572  1.00 39.54           C  
ANISOU 3796  CD1 PHE A 453     5163   5703   4156   -183    129     19       C  
ATOM   3797  CD2 PHE A 453      -5.477   9.141 -30.772  1.00 40.44           C  
ANISOU 3797  CD2 PHE A 453     5202   5912   4249    -60    158     56       C  
ATOM   3798  CE1 PHE A 453      -3.838   8.145 -28.793  1.00 39.99           C  
ANISOU 3798  CE1 PHE A 453     5262   5678   4255   -187    108     15       C  
ATOM   3799  CE2 PHE A 453      -4.123   9.015 -30.991  1.00 40.44           C  
ANISOU 3799  CE2 PHE A 453     5248   5822   4293    -69    139     49       C  
ATOM   3800  CZ  PHE A 453      -3.304   8.512 -30.004  1.00 40.59           C  
ANISOU 3800  CZ  PHE A 453     5323   5755   4344   -132    114     28       C  
ATOM   3801  N   ASN A 454     -10.675   7.413 -29.292  1.00 35.95           N  
ANISOU 3801  N   ASN A 454     4442   5726   3489   -201    163     -4       N  
ATOM   3802  CA  ASN A 454     -11.970   7.493 -28.641  1.00 36.16           C  
ANISOU 3802  CA  ASN A 454     4424   5840   3473   -216    185    -11       C  
ATOM   3803  C   ASN A 454     -12.132   6.410 -27.576  1.00 36.27           C  
ANISOU 3803  C   ASN A 454     4475   5817   3486   -332    165    -52       C  
ATOM   3804  O   ASN A 454     -11.570   5.318 -27.698  1.00 34.86           O  
ANISOU 3804  O   ASN A 454     4331   5592   3321   -404    132    -81       O  
ATOM   3805  CB  ASN A 454     -13.110   7.401 -29.671  1.00 37.58           C  
ANISOU 3805  CB  ASN A 454     4499   6189   3588   -187    188    -14       C  
ATOM   3806  CG  ASN A 454     -13.436   5.967 -30.059  1.00 36.59           C  
ANISOU 3806  CG  ASN A 454     4346   6124   3432   -292    153    -69       C  
ATOM   3807  OD1 ASN A 454     -14.254   5.321 -29.414  1.00 37.53           O  
ANISOU 3807  OD1 ASN A 454     4448   6289   3521   -369    155   -104       O  
ATOM   3808  ND2 ASN A 454     -12.756   5.450 -31.080  1.00 35.49           N  
ANISOU 3808  ND2 ASN A 454     4209   5975   3301   -301    127    -81       N  
ATOM   3809  N   THR A 455     -12.894   6.716 -26.528  1.00 37.05           N  
ANISOU 3809  N   THR A 455     4572   5934   3569   -346    191    -53       N  
ATOM   3810  CA  THR A 455     -13.373   5.678 -25.617  1.00 39.01           C  
ANISOU 3810  CA  THR A 455     4838   6182   3800   -454    180    -92       C  
ATOM   3811  C   THR A 455     -14.907   5.628 -25.580  1.00 41.02           C  
ANISOU 3811  C   THR A 455     5010   6582   3994   -468    202   -110       C  
ATOM   3812  O   THR A 455     -15.513   5.444 -24.522  1.00 43.02           O  
ANISOU 3812  O   THR A 455     5273   6838   4232   -521    217   -126       O  
ATOM   3813  CB  THR A 455     -12.781   5.800 -24.201  1.00 37.55           C  
ANISOU 3813  CB  THR A 455     4738   5879   3649   -488    184    -87       C  
ATOM   3814  OG1 THR A 455     -12.808   7.165 -23.793  1.00 39.19           O  
ANISOU 3814  OG1 THR A 455     4948   6071   3869   -409    222    -55       O  
ATOM   3815  CG2 THR A 455     -11.339   5.298 -24.176  1.00 37.47           C  
ANISOU 3815  CG2 THR A 455     4805   5745   3687   -512    149    -84       C  
ATOM   3816  N   VAL A 456     -15.514   5.788 -26.755  1.00 41.79           N  
ANISOU 3816  N   VAL A 456     5019   6804   4052   -420    204   -108       N  
ATOM   3817  CA  VAL A 456     -16.954   5.613 -26.933  1.00 41.85           C  
ANISOU 3817  CA  VAL A 456     4931   6977   3993   -437    219   -131       C  
ATOM   3818  C   VAL A 456     -17.214   4.140 -27.273  1.00 40.98           C  
ANISOU 3818  C   VAL A 456     4805   6910   3854   -558    194   -193       C  
ATOM   3819  O   VAL A 456     -17.759   3.396 -26.457  1.00 38.00           O  
ANISOU 3819  O   VAL A 456     4440   6535   3460   -655    201   -231       O  
ATOM   3820  CB  VAL A 456     -17.494   6.540 -28.055  1.00 44.60           C  
ANISOU 3820  CB  VAL A 456     5185   7456   4304   -319    234    -95       C  
ATOM   3821  CG1 VAL A 456     -19.000   6.379 -28.216  1.00 44.44           C  
ANISOU 3821  CG1 VAL A 456     5052   7624   4207   -332    248   -119       C  
ATOM   3822  CG2 VAL A 456     -17.135   7.996 -27.763  1.00 44.65           C  
ANISOU 3822  CG2 VAL A 456     5221   7396   4346   -198    271    -32       C  
ATOM   3823  N   PHE A 457     -16.779   3.713 -28.461  1.00 39.79           N  
ANISOU 3823  N   PHE A 457     4634   6784   3699   -557    170   -204       N  
ATOM   3824  CA  PHE A 457     -16.787   2.291 -28.794  1.00 40.75           C  
ANISOU 3824  CA  PHE A 457     4762   6913   3806   -676    154   -266       C  
ATOM   3825  C   PHE A 457     -15.498   1.535 -28.411  1.00 41.28           C  
ANISOU 3825  C   PHE A 457     4945   6800   3937   -731    135   -271       C  
ATOM   3826  O   PHE A 457     -15.556   0.360 -28.061  1.00 43.04           O  
ANISOU 3826  O   PHE A 457     5206   6987   4160   -840    136   -315       O  
ATOM   3827  CB  PHE A 457     -17.171   2.047 -30.266  1.00 40.09           C  
ANISOU 3827  CB  PHE A 457     4587   6973   3672   -668    144   -291       C  
ATOM   3828  CG  PHE A 457     -16.371   2.845 -31.258  1.00 40.26           C  
ANISOU 3828  CG  PHE A 457     4603   6980   3714   -557    130   -242       C  
ATOM   3829  CD1 PHE A 457     -15.190   2.335 -31.793  1.00 39.26           C  
ANISOU 3829  CD1 PHE A 457     4538   6746   3632   -575    107   -249       C  
ATOM   3830  CD2 PHE A 457     -16.822   4.089 -31.698  1.00 40.77           C  
ANISOU 3830  CD2 PHE A 457     4597   7140   3751   -432    144   -190       C  
ATOM   3831  CE1 PHE A 457     -14.463   3.060 -32.725  1.00 38.96           C  
ANISOU 3831  CE1 PHE A 457     4494   6696   3610   -477     98   -207       C  
ATOM   3832  CE2 PHE A 457     -16.101   4.816 -32.634  1.00 40.42           C  
ANISOU 3832  CE2 PHE A 457     4553   7081   3724   -331    138   -143       C  
ATOM   3833  CZ  PHE A 457     -14.918   4.302 -33.148  1.00 39.13           C  
ANISOU 3833  CZ  PHE A 457     4451   6811   3604   -357    114   -154       C  
ATOM   3834  N   ASN A 458     -14.348   2.204 -28.483  1.00 40.15           N  
ANISOU 3834  N   ASN A 458     4856   6550   3848   -653    121   -224       N  
ATOM   3835  CA  ASN A 458     -13.064   1.591 -28.103  1.00 39.47           C  
ANISOU 3835  CA  ASN A 458     4873   6303   3822   -689    102   -222       C  
ATOM   3836  C   ASN A 458     -12.854   1.528 -26.599  1.00 38.70           C  
ANISOU 3836  C   ASN A 458     4850   6103   3749   -725    108   -210       C  
ATOM   3837  O   ASN A 458     -13.085   2.511 -25.892  1.00 41.01           O  
ANISOU 3837  O   ASN A 458     5140   6397   4042   -674    123   -181       O  
ATOM   3838  CB  ASN A 458     -11.898   2.378 -28.707  1.00 36.93           C  
ANISOU 3838  CB  ASN A 458     4575   5912   3544   -596     87   -180       C  
ATOM   3839  CG  ASN A 458     -11.517   1.902 -30.093  1.00 37.59           C  
ANISOU 3839  CG  ASN A 458     4631   6028   3624   -594     70   -198       C  
ATOM   3840  OD1 ASN A 458     -12.043   0.904 -30.594  1.00 38.85           O  
ANISOU 3840  OD1 ASN A 458     4759   6252   3750   -670     69   -247       O  
ATOM   3841  ND2 ASN A 458     -10.596   2.613 -30.724  1.00 34.60           N  
ANISOU 3841  ND2 ASN A 458     4264   5605   3277   -512     61   -164       N  
ATOM   3842  N   ASP A 459     -12.363   0.401 -26.107  1.00 38.78           N  
ANISOU 3842  N   ASP A 459     4931   6022   3780   -807     99   -230       N  
ATOM   3843  CA  ASP A 459     -11.842   0.351 -24.727  1.00 39.20           C  
ANISOU 3843  CA  ASP A 459     5068   5965   3862   -828     97   -208       C  
ATOM   3844  C   ASP A 459     -10.545   1.143 -24.581  1.00 37.80           C  
ANISOU 3844  C   ASP A 459     4937   5690   3734   -752     78   -164       C  
ATOM   3845  O   ASP A 459      -9.874   1.484 -25.566  1.00 36.87           O  
ANISOU 3845  O   ASP A 459     4805   5565   3638   -695     64   -154       O  
ATOM   3846  CB  ASP A 459     -11.591  -1.088 -24.277  1.00 40.75           C  
ANISOU 3846  CB  ASP A 459     5332   6085   4066   -925     96   -231       C  
ATOM   3847  CG  ASP A 459     -12.868  -1.879 -24.128  1.00 44.95           C  
ANISOU 3847  CG  ASP A 459     5832   6697   4549  -1018    125   -278       C  
ATOM   3848  OD1 ASP A 459     -13.686  -1.537 -23.235  1.00 46.33           O  
ANISOU 3848  OD1 ASP A 459     5993   6913   4696  -1036    144   -278       O  
ATOM   3849  OD2 ASP A 459     -13.045  -2.849 -24.896  1.00 46.14           O  
ANISOU 3849  OD2 ASP A 459     5972   6868   4688  -1079    134   -319       O  
ATOM   3850  N   GLN A 460     -10.181   1.404 -23.341  1.00 36.90           N  
ANISOU 3850  N   GLN A 460     4878   5505   3634   -757     78   -143       N  
ATOM   3851  CA  GLN A 460      -8.943   2.090 -23.037  1.00 36.29           C  
ANISOU 3851  CA  GLN A 460     4847   5340   3599   -702     63   -111       C  
ATOM   3852  C   GLN A 460      -7.729   1.242 -23.427  1.00 34.51           C  
ANISOU 3852  C   GLN A 460     4672   5029   3410   -713     32   -108       C  
ATOM   3853  O   GLN A 460      -6.744   1.764 -23.955  1.00 33.51           O  
ANISOU 3853  O   GLN A 460     4551   4863   3316   -656     17    -91       O  
ATOM   3854  CB  GLN A 460      -8.924   2.444 -21.553  1.00 37.43           C  
ANISOU 3854  CB  GLN A 460     5036   5445   3740   -720     72    -97       C  
ATOM   3855  CG  GLN A 460      -7.702   3.174 -21.076  1.00 36.31           C  
ANISOU 3855  CG  GLN A 460     4936   5224   3632   -677     59    -72       C  
ATOM   3856  CD  GLN A 460      -7.867   3.634 -19.647  1.00 36.64           C  
ANISOU 3856  CD  GLN A 460     5008   5251   3659   -698     74    -66       C  
ATOM   3857  OE1 GLN A 460      -8.892   4.212 -19.292  1.00 37.20           O  
ANISOU 3857  OE1 GLN A 460     5048   5381   3705   -697    107    -74       O  
ATOM   3858  NE2 GLN A 460      -6.858   3.394 -18.825  1.00 34.79           N  
ANISOU 3858  NE2 GLN A 460     4833   4946   3439   -716     52    -53       N  
ATOM   3859  N   ARG A 461      -7.812  -0.068 -23.221  1.00 34.72           N  
ANISOU 3859  N   ARG A 461     4734   5026   3431   -786     28   -124       N  
ATOM   3860  CA  ARG A 461      -6.711  -0.951 -23.630  1.00 35.47           C  
ANISOU 3860  CA  ARG A 461     4877   5039   3561   -793      6   -120       C  
ATOM   3861  C   ARG A 461      -6.466  -0.887 -25.142  1.00 34.64           C  
ANISOU 3861  C   ARG A 461     4727   4964   3468   -757      0   -135       C  
ATOM   3862  O   ARG A 461      -5.337  -0.983 -25.609  1.00 35.92           O  
ANISOU 3862  O   ARG A 461     4915   5065   3668   -724    -19   -123       O  
ATOM   3863  CB  ARG A 461      -6.943  -2.386 -23.149  1.00 37.59           C  
ANISOU 3863  CB  ARG A 461     5197   5265   3819   -877     17   -133       C  
ATOM   3864  CG  ARG A 461      -8.173  -3.077 -23.722  1.00 40.75           C  
ANISOU 3864  CG  ARG A 461     5557   5741   4184   -945     46   -180       C  
ATOM   3865  CD  ARG A 461      -8.531  -4.287 -22.876  1.00 42.52           C  
ANISOU 3865  CD  ARG A 461     5843   5918   4395  -1033     70   -190       C  
ATOM   3866  NE  ARG A 461      -9.073  -5.384 -23.674  1.00 47.18           N  
ANISOU 3866  NE  ARG A 461     6426   6527   4972  -1105     99   -239       N  
ATOM   3867  CZ  ARG A 461     -10.332  -5.801 -23.615  1.00 49.47           C  
ANISOU 3867  CZ  ARG A 461     6685   6891   5219  -1183    134   -282       C  
ATOM   3868  NH1 ARG A 461     -11.197  -5.214 -22.788  1.00 53.35           N  
ANISOU 3868  NH1 ARG A 461     7148   7443   5676  -1193    143   -279       N  
ATOM   3869  NH2 ARG A 461     -10.721  -6.815 -24.365  1.00 49.59           N  
ANISOU 3869  NH2 ARG A 461     6696   6920   5224  -1257    164   -334       N  
ATOM   3870  N   THR A 462      -7.537  -0.668 -25.890  1.00 33.86           N  
ANISOU 3870  N   THR A 462     4558   4970   3334   -761     17   -161       N  
ATOM   3871  CA  THR A 462      -7.455  -0.462 -27.321  1.00 33.11           C  
ANISOU 3871  CA  THR A 462     4410   4928   3239   -723     13   -173       C  
ATOM   3872  C   THR A 462      -6.769   0.863 -27.687  1.00 31.23           C  
ANISOU 3872  C   THR A 462     4156   4682   3025   -625      5   -138       C  
ATOM   3873  O   THR A 462      -5.900   0.904 -28.559  1.00 29.99           O  
ANISOU 3873  O   THR A 462     4002   4496   2896   -589     -8   -134       O  
ATOM   3874  CB  THR A 462      -8.855  -0.573 -27.941  1.00 33.68           C  
ANISOU 3874  CB  THR A 462     4404   5135   3257   -754     34   -209       C  
ATOM   3875  OG1 THR A 462      -9.325  -1.915 -27.745  1.00 34.93           O  
ANISOU 3875  OG1 THR A 462     4585   5286   3398   -856     48   -250       O  
ATOM   3876  CG2 THR A 462      -8.838  -0.253 -29.441  1.00 33.04           C  
ANISOU 3876  CG2 THR A 462     4259   5129   3164   -707     29   -218       C  
ATOM   3877  N   VAL A 463      -7.137   1.929 -26.996  1.00 29.87           N  
ANISOU 3877  N   VAL A 463     3973   4532   2845   -586     19   -116       N  
ATOM   3878  CA  VAL A 463      -6.501   3.224 -27.212  1.00 29.84           C  
ANISOU 3878  CA  VAL A 463     3965   4507   2865   -500     25    -85       C  
ATOM   3879  C   VAL A 463      -4.976   3.110 -27.009  1.00 29.52           C  
ANISOU 3879  C   VAL A 463     3986   4354   2874   -490      1    -72       C  
ATOM   3880  O   VAL A 463      -4.187   3.530 -27.863  1.00 28.59           O  
ANISOU 3880  O   VAL A 463     3863   4217   2782   -440     -4    -63       O  
ATOM   3881  CB  VAL A 463      -7.102   4.289 -26.272  1.00 30.00           C  
ANISOU 3881  CB  VAL A 463     3979   4548   2872   -473     54    -67       C  
ATOM   3882  CG1 VAL A 463      -6.266   5.555 -26.300  1.00 31.20           C  
ANISOU 3882  CG1 VAL A 463     4147   4650   3056   -398     68    -40       C  
ATOM   3883  CG2 VAL A 463      -8.544   4.592 -26.676  1.00 30.83           C  
ANISOU 3883  CG2 VAL A 463     4007   4777   2927   -458     79    -74       C  
ATOM   3884  N   PHE A 464      -4.578   2.490 -25.897  1.00 29.52           N  
ANISOU 3884  N   PHE A 464     4043   4289   2884   -539    -12    -71       N  
ATOM   3885  CA  PHE A 464      -3.176   2.232 -25.608  1.00 29.47           C  
ANISOU 3885  CA  PHE A 464     4090   4190   2917   -534    -38    -59       C  
ATOM   3886  C   PHE A 464      -2.459   1.434 -26.726  1.00 30.11           C  
ANISOU 3886  C   PHE A 464     4173   4244   3022   -531    -57    -68       C  
ATOM   3887  O   PHE A 464      -1.356   1.787 -27.128  1.00 28.91           O  
ANISOU 3887  O   PHE A 464     4032   4048   2904   -489    -70    -59       O  
ATOM   3888  CB  PHE A 464      -3.038   1.529 -24.252  1.00 29.35           C  
ANISOU 3888  CB  PHE A 464     4129   4126   2896   -587    -50    -51       C  
ATOM   3889  CG  PHE A 464      -3.313   2.418 -23.072  1.00 30.67           C  
ANISOU 3889  CG  PHE A 464     4304   4301   3047   -585    -35    -41       C  
ATOM   3890  CD1 PHE A 464      -3.228   3.817 -23.183  1.00 30.71           C  
ANISOU 3890  CD1 PHE A 464     4285   4323   3059   -531    -14    -36       C  
ATOM   3891  CD2 PHE A 464      -3.647   1.864 -21.828  1.00 31.38           C  
ANISOU 3891  CD2 PHE A 464     4430   4378   3114   -640    -36    -36       C  
ATOM   3892  CE1 PHE A 464      -3.462   4.633 -22.079  1.00 30.76           C  
ANISOU 3892  CE1 PHE A 464     4302   4331   3052   -534      6    -32       C  
ATOM   3893  CE2 PHE A 464      -3.899   2.680 -20.732  1.00 31.46           C  
ANISOU 3893  CE2 PHE A 464     4447   4399   3107   -642    -21    -31       C  
ATOM   3894  CZ  PHE A 464      -3.794   4.060 -20.851  1.00 31.65           C  
ANISOU 3894  CZ  PHE A 464     4447   4438   3141   -591      0    -31       C  
ATOM   3895  N   ALA A 465      -3.093   0.373 -27.231  1.00 30.02           N  
ANISOU 3895  N   ALA A 465     4152   4260   2994   -579    -54    -93       N  
ATOM   3896  CA  ALA A 465      -2.509  -0.399 -28.351  1.00 30.28           C  
ANISOU 3896  CA  ALA A 465     4185   4270   3046   -582    -64   -109       C  
ATOM   3897  C   ALA A 465      -2.366   0.455 -29.615  1.00 30.12           C  
ANISOU 3897  C   ALA A 465     4113   4299   3030   -521    -61   -110       C  
ATOM   3898  O   ALA A 465      -1.318   0.477 -30.263  1.00 28.76           O  
ANISOU 3898  O   ALA A 465     3952   4083   2891   -488    -74   -106       O  
ATOM   3899  CB  ALA A 465      -3.353  -1.634 -28.643  1.00 29.68           C  
ANISOU 3899  CB  ALA A 465     4107   4222   2946   -656    -49   -145       C  
ATOM   3900  N   ASN A 466      -3.446   1.129 -29.986  1.00 31.30           N  
ANISOU 3900  N   ASN A 466     4204   4545   3141   -503    -42   -114       N  
ATOM   3901  CA  ASN A 466      -3.369   2.088 -31.066  1.00 31.14           C  
ANISOU 3901  CA  ASN A 466     4137   4575   3119   -433    -34   -103       C  
ATOM   3902  C   ASN A 466      -2.195   3.043 -30.852  1.00 29.66           C  
ANISOU 3902  C   ASN A 466     3981   4314   2973   -373    -37    -74       C  
ATOM   3903  O   ASN A 466      -1.395   3.242 -31.750  1.00 30.56           O  
ANISOU 3903  O   ASN A 466     4092   4409   3110   -336    -42    -71       O  
ATOM   3904  CB  ASN A 466      -4.696   2.844 -31.234  1.00 31.59           C  
ANISOU 3904  CB  ASN A 466     4130   4745   3127   -407     -9    -97       C  
ATOM   3905  CG  ASN A 466      -5.780   1.988 -31.869  1.00 32.93           C  
ANISOU 3905  CG  ASN A 466     4248   5016   3249   -461     -6   -134       C  
ATOM   3906  OD1 ASN A 466      -5.492   1.116 -32.686  1.00 35.44           O  
ANISOU 3906  OD1 ASN A 466     4563   5333   3568   -495    -17   -163       O  
ATOM   3907  ND2 ASN A 466      -7.041   2.234 -31.495  1.00 32.28           N  
ANISOU 3907  ND2 ASN A 466     4119   5024   3120   -471     11   -138       N  
ATOM   3908  N   PHE A 467      -2.066   3.596 -29.647  1.00 28.07           N  
ANISOU 3908  N   PHE A 467     3811   4073   2781   -372    -31    -57       N  
ATOM   3909  CA  PHE A 467      -1.018   4.579 -29.392  1.00 26.58           C  
ANISOU 3909  CA  PHE A 467     3649   3824   2627   -325    -26    -38       C  
ATOM   3910  C   PHE A 467       0.380   3.975 -29.509  1.00 26.76           C  
ANISOU 3910  C   PHE A 467     3708   3769   2689   -333    -56    -43       C  
ATOM   3911  O   PHE A 467       1.296   4.574 -30.100  1.00 26.63           O  
ANISOU 3911  O   PHE A 467     3692   3724   2700   -290    -53    -38       O  
ATOM   3912  CB  PHE A 467      -1.199   5.205 -28.016  1.00 26.38           C  
ANISOU 3912  CB  PHE A 467     3647   3778   2596   -335    -11    -29       C  
ATOM   3913  CG  PHE A 467      -0.192   6.271 -27.703  1.00 26.82           C  
ANISOU 3913  CG  PHE A 467     3727   3779   2681   -298      2    -19       C  
ATOM   3914  CD1 PHE A 467      -0.091   7.406 -28.500  1.00 26.34           C  
ANISOU 3914  CD1 PHE A 467     3647   3729   2630   -235     38     -8       C  
ATOM   3915  CD2 PHE A 467       0.643   6.154 -26.591  1.00 26.94           C  
ANISOU 3915  CD2 PHE A 467     3785   3738   2712   -330    -14    -22       C  
ATOM   3916  CE1 PHE A 467       0.842   8.392 -28.213  1.00 27.01           C  
ANISOU 3916  CE1 PHE A 467     3758   3758   2743   -211     60     -6       C  
ATOM   3917  CE2 PHE A 467       1.554   7.143 -26.286  1.00 25.92           C  
ANISOU 3917  CE2 PHE A 467     3673   3568   2605   -307      2    -23       C  
ATOM   3918  CZ  PHE A 467       1.653   8.261 -27.097  1.00 26.77           C  
ANISOU 3918  CZ  PHE A 467     3765   3678   2726   -252     42    -18       C  
ATOM   3919  N   TYR A 468       0.542   2.785 -28.944  1.00 25.58           N  
ANISOU 3919  N   TYR A 468     3590   3585   2541   -386    -80    -51       N  
ATOM   3920  CA  TYR A 468       1.822   2.117 -28.939  1.00 25.53           C  
ANISOU 3920  CA  TYR A 468     3620   3509   2571   -390   -107    -50       C  
ATOM   3921  C   TYR A 468       2.254   1.853 -30.386  1.00 26.07           C  
ANISOU 3921  C   TYR A 468     3667   3580   2656   -366   -110    -63       C  
ATOM   3922  O   TYR A 468       3.404   2.109 -30.761  1.00 26.59           O  
ANISOU 3922  O   TYR A 468     3741   3606   2756   -334   -120    -60       O  
ATOM   3923  CB  TYR A 468       1.706   0.820 -28.128  1.00 24.91           C  
ANISOU 3923  CB  TYR A 468     3580   3395   2485   -446   -123    -50       C  
ATOM   3924  CG  TYR A 468       2.954  -0.030 -28.065  1.00 24.25           C  
ANISOU 3924  CG  TYR A 468     3536   3241   2436   -443   -148    -43       C  
ATOM   3925  CD1 TYR A 468       4.075   0.373 -27.310  1.00 23.16           C  
ANISOU 3925  CD1 TYR A 468     3418   3064   2315   -419   -167    -24       C  
ATOM   3926  CD2 TYR A 468       2.997  -1.270 -28.719  1.00 23.99           C  
ANISOU 3926  CD2 TYR A 468     3518   3183   2414   -467   -148    -56       C  
ATOM   3927  CE1 TYR A 468       5.190  -0.437 -27.212  1.00 23.43           C  
ANISOU 3927  CE1 TYR A 468     3482   3044   2375   -410   -191    -12       C  
ATOM   3928  CE2 TYR A 468       4.099  -2.096 -28.632  1.00 22.96           C  
ANISOU 3928  CE2 TYR A 468     3425   2984   2314   -458   -165    -44       C  
ATOM   3929  CZ  TYR A 468       5.200  -1.694 -27.906  1.00 24.19           C  
ANISOU 3929  CZ  TYR A 468     3595   3108   2486   -424   -188    -19       C  
ATOM   3930  OH  TYR A 468       6.311  -2.534 -27.866  1.00 23.07           O  
ANISOU 3930  OH  TYR A 468     3484   2908   2373   -406   -205     -4       O  
ATOM   3931  N   ASP A 469       1.308   1.413 -31.209  1.00 26.43           N  
ANISOU 3931  N   ASP A 469     3681   3685   2677   -384    -99    -81       N  
ATOM   3932  CA  ASP A 469       1.566   1.153 -32.612  1.00 26.86           C  
ANISOU 3932  CA  ASP A 469     3710   3758   2738   -369    -98    -98       C  
ATOM   3933  C   ASP A 469       2.010   2.417 -33.361  1.00 27.57           C  
ANISOU 3933  C   ASP A 469     3772   3866   2837   -300    -86    -83       C  
ATOM   3934  O   ASP A 469       2.952   2.378 -34.176  1.00 26.94           O  
ANISOU 3934  O   ASP A 469     3694   3756   2784   -276    -93    -87       O  
ATOM   3935  CB  ASP A 469       0.316   0.574 -33.281  1.00 27.77           C  
ANISOU 3935  CB  ASP A 469     3784   3956   2810   -407    -85   -124       C  
ATOM   3936  CG  ASP A 469       0.089  -0.884 -32.939  1.00 28.33           C  
ANISOU 3936  CG  ASP A 469     3888   3995   2880   -481    -88   -150       C  
ATOM   3937  OD1 ASP A 469       0.989  -1.513 -32.371  1.00 28.17           O  
ANISOU 3937  OD1 ASP A 469     3922   3886   2895   -491   -100   -142       O  
ATOM   3938  OD2 ASP A 469      -0.986  -1.409 -33.271  1.00 29.83           O  
ANISOU 3938  OD2 ASP A 469     4048   4252   3031   -529    -73   -179       O  
ATOM   3939  N   ALA A 470       1.329   3.532 -33.111  1.00 28.23           N  
ANISOU 3939  N   ALA A 470     3833   3994   2899   -267    -63    -64       N  
ATOM   3940  CA  ALA A 470       1.683   4.791 -33.799  1.00 27.36           C  
ANISOU 3940  CA  ALA A 470     3704   3893   2796   -199    -39    -45       C  
ATOM   3941  C   ALA A 470       3.088   5.184 -33.394  1.00 27.42           C  
ANISOU 3941  C   ALA A 470     3752   3815   2850   -185    -45    -41       C  
ATOM   3942  O   ALA A 470       3.854   5.689 -34.202  1.00 30.82           O  
ANISOU 3942  O   ALA A 470     4179   4229   3301   -146    -35    -38       O  
ATOM   3943  CB  ALA A 470       0.684   5.897 -33.465  1.00 26.30           C  
ANISOU 3943  CB  ALA A 470     3547   3812   2633   -163     -4    -22       C  
ATOM   3944  N   MET A 471       3.451   4.897 -32.146  1.00 26.31           N  
ANISOU 3944  N   MET A 471     3647   3626   2721   -220    -61    -42       N  
ATOM   3945  CA  MET A 471       4.758   5.311 -31.640  1.00 25.90           C  
ANISOU 3945  CA  MET A 471     3625   3510   2705   -211    -68    -42       C  
ATOM   3946  C   MET A 471       5.900   4.413 -32.164  1.00 25.68           C  
ANISOU 3946  C   MET A 471     3607   3439   2708   -217    -99    -53       C  
ATOM   3947  O   MET A 471       7.015   4.888 -32.362  1.00 24.10           O  
ANISOU 3947  O   MET A 471     3413   3205   2536   -194    -97    -57       O  
ATOM   3948  CB  MET A 471       4.767   5.442 -30.101  1.00 25.52           C  
ANISOU 3948  CB  MET A 471     3605   3440   2651   -242    -73    -38       C  
ATOM   3949  CG  MET A 471       3.893   6.574 -29.537  1.00 25.65           C  
ANISOU 3949  CG  MET A 471     3615   3484   2645   -230    -33    -30       C  
ATOM   3950  SD  MET A 471       4.105   8.197 -30.341  1.00 26.99           S  
ANISOU 3950  SD  MET A 471     3772   3652   2828   -165     23    -22       S  
ATOM   3951  CE  MET A 471       5.835   8.543 -29.974  1.00 24.90           C  
ANISOU 3951  CE  MET A 471     3536   3320   2602   -175     16    -40       C  
ATOM   3952  N   ILE A 472       5.597   3.136 -32.430  1.00 25.95           N  
ANISOU 3952  N   ILE A 472     3645   3478   2737   -247   -119    -63       N  
ATOM   3953  CA  ILE A 472       6.505   2.246 -33.143  1.00 26.17           C  
ANISOU 3953  CA  ILE A 472     3680   3469   2793   -247   -138    -75       C  
ATOM   3954  C   ILE A 472       6.794   2.829 -34.551  1.00 27.69           C  
ANISOU 3954  C   ILE A 472     3843   3683   2994   -208   -121    -82       C  
ATOM   3955  O   ILE A 472       7.955   2.930 -34.979  1.00 26.48           O  
ANISOU 3955  O   ILE A 472     3694   3494   2873   -185   -127    -87       O  
ATOM   3956  CB  ILE A 472       5.888   0.823 -33.290  1.00 28.69           C  
ANISOU 3956  CB  ILE A 472     4009   3789   3100   -292   -147    -88       C  
ATOM   3957  CG1 ILE A 472       5.825   0.084 -31.937  1.00 27.11           C  
ANISOU 3957  CG1 ILE A 472     3849   3552   2897   -328   -162    -76       C  
ATOM   3958  CG2 ILE A 472       6.598   0.009 -34.390  1.00 27.65           C  
ANISOU 3958  CG2 ILE A 472     3877   3631   2994   -288   -151   -108       C  
ATOM   3959  CD1 ILE A 472       7.155  -0.472 -31.459  1.00 27.29           C  
ANISOU 3959  CD1 ILE A 472     3905   3509   2955   -316   -185    -64       C  
ATOM   3960  N   CYS A 473       5.752   3.252 -35.264  1.00 28.65           N  
ANISOU 3960  N   CYS A 473     3930   3870   3082   -195    -99    -81       N  
ATOM   3961  CA  CYS A 473       5.995   3.938 -36.542  1.00 30.34           C  
ANISOU 3961  CA  CYS A 473     4118   4111   3298   -150    -79    -80       C  
ATOM   3962  C   CYS A 473       6.911   5.146 -36.398  1.00 29.11           C  
ANISOU 3962  C   CYS A 473     3973   3916   3168   -110    -60    -67       C  
ATOM   3963  O   CYS A 473       7.875   5.272 -37.142  1.00 28.74           O  
ANISOU 3963  O   CYS A 473     3927   3845   3147    -89    -58    -74       O  
ATOM   3964  CB  CYS A 473       4.710   4.340 -37.223  1.00 32.04           C  
ANISOU 3964  CB  CYS A 473     4291   4416   3466   -133    -57    -72       C  
ATOM   3965  SG  CYS A 473       3.743   2.931 -37.727  1.00 40.70           S  
ANISOU 3965  SG  CYS A 473     5363   5573   4527   -189    -73   -103       S  
ATOM   3966  N   VAL A 474       6.578   6.051 -35.472  1.00 28.63           N  
ANISOU 3966  N   VAL A 474     3924   3853   3100   -102    -40    -51       N  
ATOM   3967  CA  VAL A 474       7.434   7.248 -35.172  1.00 26.70           C  
ANISOU 3967  CA  VAL A 474     3697   3567   2881    -76    -11    -46       C  
ATOM   3968  C   VAL A 474       8.884   6.861 -34.842  1.00 26.02           C  
ANISOU 3968  C   VAL A 474     3630   3422   2832    -96    -37    -65       C  
ATOM   3969  O   VAL A 474       9.833   7.557 -35.236  1.00 26.01           O  
ANISOU 3969  O   VAL A 474     3632   3394   2854    -76    -17    -73       O  
ATOM   3970  CB  VAL A 474       6.844   8.062 -33.982  1.00 26.96           C  
ANISOU 3970  CB  VAL A 474     3744   3599   2900    -82     14    -36       C  
ATOM   3971  CG1 VAL A 474       7.814   9.128 -33.481  1.00 24.72           C  
ANISOU 3971  CG1 VAL A 474     3485   3265   2642    -77     45    -44       C  
ATOM   3972  CG2 VAL A 474       5.493   8.680 -34.378  1.00 26.45           C  
ANISOU 3972  CG2 VAL A 474     3656   3593   2799    -47     50    -12       C  
ATOM   3973  N   ALA A 475       9.055   5.758 -34.114  1.00 25.19           N  
ANISOU 3973  N   ALA A 475     3537   3302   2730   -133    -79    -72       N  
ATOM   3974  CA  ALA A 475      10.387   5.313 -33.695  1.00 24.70           C  
ANISOU 3974  CA  ALA A 475     3488   3198   2697   -144   -108    -84       C  
ATOM   3975  C   ALA A 475      11.206   4.828 -34.910  1.00 26.28           C  
ANISOU 3975  C   ALA A 475     3676   3384   2924   -124   -116    -96       C  
ATOM   3976  O   ALA A 475      12.424   5.068 -34.999  1.00 27.95           O  
ANISOU 3976  O   ALA A 475     3887   3570   3163   -114   -119   -108       O  
ATOM   3977  CB  ALA A 475      10.269   4.215 -32.649  1.00 24.84           C  
ANISOU 3977  CB  ALA A 475     3524   3204   2707   -177   -145    -78       C  
ATOM   3978  N   TYR A 476      10.519   4.184 -35.852  1.00 25.46           N  
ANISOU 3978  N   TYR A 476     3560   3303   2808   -123   -116    -98       N  
ATOM   3979  CA  TYR A 476      11.117   3.738 -37.078  1.00 26.16           C  
ANISOU 3979  CA  TYR A 476     3638   3386   2916   -108   -117   -112       C  
ATOM   3980  C   TYR A 476      11.497   4.939 -37.941  1.00 26.32           C  
ANISOU 3980  C   TYR A 476     3643   3416   2942    -71    -82   -112       C  
ATOM   3981  O   TYR A 476      12.584   4.958 -38.529  1.00 26.72           O  
ANISOU 3981  O   TYR A 476     3689   3440   3020    -58    -82   -125       O  
ATOM   3982  CB  TYR A 476      10.170   2.820 -37.841  1.00 26.57           C  
ANISOU 3982  CB  TYR A 476     3677   3471   2944   -125   -120   -120       C  
ATOM   3983  CG  TYR A 476      10.276   1.359 -37.521  1.00 27.15           C  
ANISOU 3983  CG  TYR A 476     3772   3513   3030   -160   -145   -132       C  
ATOM   3984  CD1 TYR A 476      11.491   0.682 -37.639  1.00 28.52           C  
ANISOU 3984  CD1 TYR A 476     3959   3633   3241   -152   -160   -141       C  
ATOM   3985  CD2 TYR A 476       9.136   0.622 -37.174  1.00 28.48           C  
ANISOU 3985  CD2 TYR A 476     3946   3703   3169   -198   -146   -134       C  
ATOM   3986  CE1 TYR A 476      11.580  -0.680 -37.373  1.00 30.01           C  
ANISOU 3986  CE1 TYR A 476     4174   3784   3443   -176   -173   -146       C  
ATOM   3987  CE2 TYR A 476       9.204  -0.743 -36.909  1.00 29.37           C  
ANISOU 3987  CE2 TYR A 476     4088   3776   3295   -232   -157   -144       C  
ATOM   3988  CZ  TYR A 476      10.428  -1.386 -36.997  1.00 30.11           C  
ANISOU 3988  CZ  TYR A 476     4201   3809   3428   -217   -169   -147       C  
ATOM   3989  OH  TYR A 476      10.506  -2.723 -36.737  1.00 30.38           O  
ANISOU 3989  OH  TYR A 476     4270   3796   3476   -242   -170   -151       O  
ATOM   3990  N   LYS A 477      10.629   5.949 -37.998  1.00 25.54           N  
ANISOU 3990  N   LYS A 477     3536   3349   2816    -52    -49    -94       N  
ATOM   3991  CA  LYS A 477      11.015   7.209 -38.647  1.00 26.74           C  
ANISOU 3991  CA  LYS A 477     3686   3498   2974    -13     -4    -87       C  
ATOM   3992  C   LYS A 477      12.257   7.782 -37.967  1.00 27.30           C  
ANISOU 3992  C   LYS A 477     3775   3517   3079    -22      2   -102       C  
ATOM   3993  O   LYS A 477      13.152   8.265 -38.637  1.00 27.62           O  
ANISOU 3993  O   LYS A 477     3814   3537   3140     -6     24   -112       O  
ATOM   3994  CB  LYS A 477       9.879   8.231 -38.640  1.00 26.40           C  
ANISOU 3994  CB  LYS A 477     3639   3492   2899     16     37    -58       C  
ATOM   3995  CG  LYS A 477       9.929   9.181 -39.835  1.00 28.20           C  
ANISOU 3995  CG  LYS A 477     3859   3735   3121     68     86    -41       C  
ATOM   3996  CD  LYS A 477       9.298  10.563 -39.588  1.00 29.85           C  
ANISOU 3996  CD  LYS A 477     4079   3946   3314    108    147     -9       C  
ATOM   3997  CE  LYS A 477       8.687  11.073 -40.887  1.00 30.83           C  
ANISOU 3997  CE  LYS A 477     4182   4123   3407    170    182     23       C  
ATOM   3998  NZ  LYS A 477       8.717  12.538 -41.159  1.00 28.88           N  
ANISOU 3998  NZ  LYS A 477     3958   3852   3162    226    259     55       N  
ATOM   3999  N   PHE A 478      12.322   7.689 -36.630  1.00 27.16           N  
ANISOU 3999  N   PHE A 478     3772   3485   3062    -53    -15   -105       N  
ATOM   4000  CA  PHE A 478      13.452   8.249 -35.887  1.00 27.00           C  
ANISOU 4000  CA  PHE A 478     3761   3432   3064    -69     -9   -125       C  
ATOM   4001  C   PHE A 478      14.708   7.526 -36.323  1.00 28.03           C  
ANISOU 4001  C   PHE A 478     3880   3547   3224    -71    -40   -145       C  
ATOM   4002  O   PHE A 478      15.762   8.127 -36.545  1.00 26.23           O  
ANISOU 4002  O   PHE A 478     3647   3302   3017    -69    -20   -165       O  
ATOM   4003  CB  PHE A 478      13.246   8.066 -34.382  1.00 25.82           C  
ANISOU 4003  CB  PHE A 478     3624   3285   2901   -104    -32   -125       C  
ATOM   4004  CG  PHE A 478      14.474   8.364 -33.545  1.00 25.39           C  
ANISOU 4004  CG  PHE A 478     3569   3216   2861   -129    -40   -150       C  
ATOM   4005  CD1 PHE A 478      15.358   7.354 -33.202  1.00 26.30           C  
ANISOU 4005  CD1 PHE A 478     3673   3331   2986   -138    -91   -156       C  
ATOM   4006  CD2 PHE A 478      14.700   9.638 -33.042  1.00 25.88           C  
ANISOU 4006  CD2 PHE A 478     3641   3269   2921   -143      8   -167       C  
ATOM   4007  CE1 PHE A 478      16.478   7.603 -32.406  1.00 27.36           C  
ANISOU 4007  CE1 PHE A 478     3797   3472   3125   -160   -103   -179       C  
ATOM   4008  CE2 PHE A 478      15.810   9.901 -32.244  1.00 27.15           C  
ANISOU 4008  CE2 PHE A 478     3795   3432   3088   -176      1   -198       C  
ATOM   4009  CZ  PHE A 478      16.710   8.888 -31.934  1.00 26.65           C  
ANISOU 4009  CZ  PHE A 478     3711   3384   3030   -183    -57   -204       C  
ATOM   4010  N   ASP A 479      14.578   6.208 -36.431  1.00 29.48           N  
ANISOU 4010  N   ASP A 479     4060   3733   3408    -75    -84   -140       N  
ATOM   4011  CA  ASP A 479      15.688   5.368 -36.758  1.00 29.27           C  
ANISOU 4011  CA  ASP A 479     4024   3689   3409    -72   -113   -155       C  
ATOM   4012  C   ASP A 479      16.197   5.710 -38.177  1.00 28.87           C  
ANISOU 4012  C   ASP A 479     3958   3634   3375    -47    -86   -168       C  
ATOM   4013  O   ASP A 479      17.409   5.813 -38.405  1.00 25.81           O  
ANISOU 4013  O   ASP A 479     3560   3232   3014    -43    -87   -188       O  
ATOM   4014  CB  ASP A 479      15.261   3.915 -36.643  1.00 29.31           C  
ANISOU 4014  CB  ASP A 479     4036   3688   3410    -81   -150   -145       C  
ATOM   4015  CG  ASP A 479      16.285   2.986 -37.186  1.00 29.87           C  
ANISOU 4015  CG  ASP A 479     4100   3735   3511    -68   -170   -157       C  
ATOM   4016  OD1 ASP A 479      17.405   2.944 -36.631  1.00 28.48           O  
ANISOU 4016  OD1 ASP A 479     3917   3549   3353    -62   -188   -162       O  
ATOM   4017  OD2 ASP A 479      15.957   2.292 -38.174  1.00 32.09           O  
ANISOU 4017  OD2 ASP A 479     4381   4014   3796    -64   -166   -163       O  
ATOM   4018  N   ALA A 480      15.254   5.958 -39.093  1.00 28.07           N  
ANISOU 4018  N   ALA A 480     3855   3554   3254    -32    -61   -157       N  
ATOM   4019  CA  ALA A 480      15.583   6.296 -40.474  1.00 28.79           C  
ANISOU 4019  CA  ALA A 480     3935   3651   3353     -7    -33   -164       C  
ATOM   4020  C   ALA A 480      16.245   7.682 -40.592  1.00 29.44           C  
ANISOU 4020  C   ALA A 480     4021   3716   3446      5     14   -169       C  
ATOM   4021  O   ALA A 480      17.203   7.863 -41.365  1.00 30.33           O  
ANISOU 4021  O   ALA A 480     4127   3816   3581     14     29   -187       O  
ATOM   4022  CB  ALA A 480      14.334   6.202 -41.363  1.00 29.78           C  
ANISOU 4022  CB  ALA A 480     4051   3821   3443      7    -20   -147       C  
ATOM   4023  N   ALA A 481      15.733   8.651 -39.842  1.00 27.45           N  
ANISOU 4023  N   ALA A 481     3785   3463   3180      2     44   -156       N  
ATOM   4024  CA  ALA A 481      16.462   9.913 -39.593  1.00 29.54           C  
ANISOU 4024  CA  ALA A 481     4063   3700   3459     -1     94   -170       C  
ATOM   4025  C   ALA A 481      17.891   9.687 -39.068  1.00 31.53           C  
ANISOU 4025  C   ALA A 481     4304   3934   3739    -31     71   -208       C  
ATOM   4026  O   ALA A 481      18.851  10.329 -39.545  1.00 32.48           O  
ANISOU 4026  O   ALA A 481     4421   4038   3879    -33    106   -231       O  
ATOM   4027  CB  ALA A 481      15.682  10.804 -38.631  1.00 27.95           C  
ANISOU 4027  CB  ALA A 481     3883   3496   3240     -8    128   -157       C  
ATOM   4028  N   MET A 482      18.052   8.782 -38.103  1.00 31.30           N  
ANISOU 4028  N   MET A 482     4267   3915   3711    -53     16   -212       N  
ATOM   4029  CA  MET A 482      19.397   8.525 -37.578  1.00 32.86           C  
ANISOU 4029  CA  MET A 482     4444   4111   3927    -73     -9   -242       C  
ATOM   4030  C   MET A 482      20.307   8.079 -38.702  1.00 33.36           C  
ANISOU 4030  C   MET A 482     4489   4168   4017    -55    -14   -257       C  
ATOM   4031  O   MET A 482      21.504   8.377 -38.684  1.00 37.32           O  
ANISOU 4031  O   MET A 482     4971   4670   4536    -66     -7   -288       O  
ATOM   4032  CB  MET A 482      19.411   7.454 -36.473  1.00 32.01           C  
ANISOU 4032  CB  MET A 482     4331   4019   3811    -86    -71   -233       C  
ATOM   4033  CG  MET A 482      18.875   7.870 -35.117  1.00 32.08           C  
ANISOU 4033  CG  MET A 482     4352   4040   3794   -114    -72   -227       C  
ATOM   4034  SD  MET A 482      19.348   9.539 -34.620  1.00 34.28           S  
ANISOU 4034  SD  MET A 482     4636   4319   4070   -148     -9   -262       S  
ATOM   4035  CE  MET A 482      17.916  10.408 -35.272  1.00 34.34           C  
ANISOU 4035  CE  MET A 482     4677   4302   4067   -125     52   -235       C  
ATOM   4036  N   MET A 483      19.765   7.320 -39.653  1.00 33.05           N  
ANISOU 4036  N   MET A 483     4450   4128   3977    -30    -26   -241       N  
ATOM   4037  CA  MET A 483      20.614   6.740 -40.692  1.00 35.04           C  
ANISOU 4037  CA  MET A 483     4685   4374   4254    -14    -34   -258       C  
ATOM   4038  C   MET A 483      21.022   7.853 -41.637  1.00 33.38           C  
ANISOU 4038  C   MET A 483     4475   4156   4051     -7     23   -271       C  
ATOM   4039  O   MET A 483      22.174   7.972 -42.002  1.00 31.55           O  
ANISOU 4039  O   MET A 483     4226   3919   3842    -10     31   -300       O  
ATOM   4040  CB  MET A 483      19.913   5.598 -41.444  1.00 36.77           C  
ANISOU 4040  CB  MET A 483     4905   4595   4468      0    -56   -244       C  
ATOM   4041  CG  MET A 483      19.710   4.324 -40.632  1.00 41.63           C  
ANISOU 4041  CG  MET A 483     5526   5205   5084     -6   -106   -233       C  
ATOM   4042  SD  MET A 483      21.202   3.707 -39.798  1.00 45.21           S  
ANISOU 4042  SD  MET A 483     5961   5649   5566     -3   -143   -246       S  
ATOM   4043  CE  MET A 483      20.955   4.354 -38.143  1.00 44.56           C  
ANISOU 4043  CE  MET A 483     5885   5585   5459    -27   -155   -234       C  
ATOM   4044  N   ALA A 484      20.060   8.694 -41.979  1.00 33.96           N  
ANISOU 4044  N   ALA A 484     4569   4232   4102      4     65   -249       N  
ATOM   4045  CA  ALA A 484      20.322   9.856 -42.797  1.00 35.00           C  
ANISOU 4045  CA  ALA A 484     4711   4349   4235     16    131   -252       C  
ATOM   4046  C   ALA A 484      21.293  10.785 -42.102  1.00 34.59           C  
ANISOU 4046  C   ALA A 484     4663   4277   4201    -14    165   -284       C  
ATOM   4047  O   ALA A 484      22.153  11.360 -42.755  1.00 37.83           O  
ANISOU 4047  O   ALA A 484     5071   4672   4628    -18    206   -307       O  
ATOM   4048  CB  ALA A 484      19.017  10.588 -43.149  1.00 33.30           C  
ANISOU 4048  CB  ALA A 484     4518   4144   3989     45    173   -212       C  
ATOM   4049  N   LEU A 485      21.161  10.958 -40.784  1.00 35.64           N  
ANISOU 4049  N   LEU A 485     4801   4414   4327    -42    152   -290       N  
ATOM   4050  CA  LEU A 485      22.052  11.916 -40.085  1.00 36.26           C  
ANISOU 4050  CA  LEU A 485     4880   4480   4415    -84    191   -329       C  
ATOM   4051  C   LEU A 485      23.515  11.463 -40.180  1.00 35.61           C  
ANISOU 4051  C   LEU A 485     4760   4414   4355   -103    164   -371       C  
ATOM   4052  O   LEU A 485      24.415  12.290 -40.291  1.00 34.21           O  
ANISOU 4052  O   LEU A 485     4579   4229   4191   -131    212   -410       O  
ATOM   4053  CB  LEU A 485      21.646  12.165 -38.623  1.00 33.64           C  
ANISOU 4053  CB  LEU A 485     4557   4158   4065   -116    182   -332       C  
ATOM   4054  CG  LEU A 485      20.369  12.950 -38.255  1.00 35.29           C  
ANISOU 4054  CG  LEU A 485     4804   4350   4254   -108    226   -303       C  
ATOM   4055  CD1 LEU A 485      20.228  12.996 -36.746  1.00 34.62           C  
ANISOU 4055  CD1 LEU A 485     4719   4281   4152   -148    206   -317       C  
ATOM   4056  CD2 LEU A 485      20.329  14.370 -38.819  1.00 36.74           C  
ANISOU 4056  CD2 LEU A 485     5023   4493   4443   -102    325   -306       C  
ATOM   4057  N   ARG A 486      23.727  10.144 -40.163  1.00 35.58           N  
ANISOU 4057  N   ARG A 486     4729   4432   4358    -86     93   -363       N  
ATOM   4058  CA  ARG A 486      25.064   9.567 -40.250  1.00 38.42           C  
ANISOU 4058  CA  ARG A 486     5048   4812   4739    -91     62   -396       C  
ATOM   4059  C   ARG A 486      25.679   9.600 -41.666  1.00 37.86           C  
ANISOU 4059  C   ARG A 486     4968   4726   4690    -73     91   -410       C  
ATOM   4060  O   ARG A 486      26.870   9.891 -41.820  1.00 37.99           O  
ANISOU 4060  O   ARG A 486     4957   4754   4723    -91    107   -451       O  
ATOM   4061  CB  ARG A 486      25.049   8.139 -39.694  1.00 43.02           C  
ANISOU 4061  CB  ARG A 486     5610   5413   5320    -71    -13   -376       C  
ATOM   4062  CG  ARG A 486      26.134   7.208 -40.214  1.00 45.54           C  
ANISOU 4062  CG  ARG A 486     5893   5743   5664    -48    -45   -390       C  
ATOM   4063  CD  ARG A 486      27.546   7.690 -39.895  1.00 52.89           C  
ANISOU 4063  CD  ARG A 486     6781   6709   6603    -73    -38   -436       C  
ATOM   4064  NE  ARG A 486      27.937   7.436 -38.516  1.00 56.46           N  
ANISOU 4064  NE  ARG A 486     7205   7207   7037    -87    -81   -439       N  
ATOM   4065  CZ  ARG A 486      29.196   7.405 -38.091  1.00 61.65           C  
ANISOU 4065  CZ  ARG A 486     7810   7917   7695    -97    -98   -472       C  
ATOM   4066  NH1 ARG A 486      30.193   7.606 -38.948  1.00 62.65           N  
ANISOU 4066  NH1 ARG A 486     7907   8052   7845    -98    -74   -509       N  
ATOM   4067  NH2 ARG A 486      29.461   7.178 -36.806  1.00 65.39           N  
ANISOU 4067  NH2 ARG A 486     8257   8445   8142   -108   -139   -470       N  
ATOM   4068  N   THR A 487      24.864   9.317 -42.684  1.00 38.03           N  
ANISOU 4068  N   THR A 487     5010   4730   4707    -39     99   -380       N  
ATOM   4069  CA  THR A 487      25.352   9.096 -44.058  1.00 36.12           C  
ANISOU 4069  CA  THR A 487     4759   4481   4482    -19    116   -390       C  
ATOM   4070  C   THR A 487      25.376  10.336 -44.929  1.00 36.50           C  
ANISOU 4070  C   THR A 487     4830   4510   4527    -20    193   -393       C  
ATOM   4071  O   THR A 487      26.057  10.353 -45.953  1.00 38.00           O  
ANISOU 4071  O   THR A 487     5010   4696   4732    -13    215   -411       O  
ATOM   4072  CB  THR A 487      24.513   8.059 -44.809  1.00 35.98           C  
ANISOU 4072  CB  THR A 487     4748   4466   4457     12     85   -361       C  
ATOM   4073  OG1 THR A 487      23.157   8.504 -44.865  1.00 34.91           O  
ANISOU 4073  OG1 THR A 487     4642   4332   4291     23    105   -324       O  
ATOM   4074  CG2 THR A 487      24.591   6.692 -44.132  1.00 36.63           C  
ANISOU 4074  CG2 THR A 487     4813   4555   4547     17     18   -357       C  
ATOM   4075  N   SER A 488      24.604  11.351 -44.555  1.00 34.84           N  
ANISOU 4075  N   SER A 488     4654   4284   4298    -25    239   -374       N  
ATOM   4076  CA  SER A 488      24.520  12.581 -45.337  1.00 34.12           C  
ANISOU 4076  CA  SER A 488     4595   4165   4202    -17    323   -367       C  
ATOM   4077  C   SER A 488      24.931  13.863 -44.556  1.00 36.07           C  
ANISOU 4077  C   SER A 488     4864   4384   4455    -59    389   -394       C  
ATOM   4078  O   SER A 488      25.612  14.734 -45.101  1.00 39.31           O  
ANISOU 4078  O   SER A 488     5290   4769   4877    -75    459   -418       O  
ATOM   4079  CB  SER A 488      23.114  12.726 -45.901  1.00 31.88           C  
ANISOU 4079  CB  SER A 488     4338   3884   3888     27    339   -310       C  
ATOM   4080  OG  SER A 488      22.943  13.996 -46.489  1.00 32.49           O  
ANISOU 4080  OG  SER A 488     4453   3932   3958     44    427   -292       O  
ATOM   4081  N   PHE A 489      24.490  13.993 -43.308  1.00 33.14           N  
ANISOU 4081  N   PHE A 489     4500   4018   4074    -81    374   -394       N  
ATOM   4082  CA  PHE A 489      24.859  15.152 -42.499  1.00 35.70           C  
ANISOU 4082  CA  PHE A 489     4844   4318   4400   -131    438   -429       C  
ATOM   4083  C   PHE A 489      26.223  14.872 -41.926  1.00 37.60           C  
ANISOU 4083  C   PHE A 489     5039   4591   4655   -183    408   -491       C  
ATOM   4084  O   PHE A 489      26.865  15.743 -41.333  1.00 36.80           O  
ANISOU 4084  O   PHE A 489     4940   4484   4556   -239    459   -539       O  
ATOM   4085  CB  PHE A 489      23.865  15.364 -41.360  1.00 32.08           C  
ANISOU 4085  CB  PHE A 489     4407   3860   3922   -137    432   -408       C  
ATOM   4086  CG  PHE A 489      22.546  15.922 -41.802  1.00 30.65           C  
ANISOU 4086  CG  PHE A 489     4271   3651   3724    -88    479   -351       C  
ATOM   4087  CD1 PHE A 489      21.589  15.098 -42.389  1.00 28.80           C  
ANISOU 4087  CD1 PHE A 489     4028   3442   3473    -34    429   -300       C  
ATOM   4088  CD2 PHE A 489      22.239  17.262 -41.586  1.00 29.97           C  
ANISOU 4088  CD2 PHE A 489     4233   3517   3635    -96    575   -350       C  
ATOM   4089  CE1 PHE A 489      20.370  15.597 -42.771  1.00 26.86           C  
ANISOU 4089  CE1 PHE A 489     3813   3188   3205     14    469   -247       C  
ATOM   4090  CE2 PHE A 489      21.018  17.769 -41.980  1.00 29.36           C  
ANISOU 4090  CE2 PHE A 489     4192   3420   3540    -39    620   -290       C  
ATOM   4091  CZ  PHE A 489      20.088  16.937 -42.581  1.00 28.05           C  
ANISOU 4091  CZ  PHE A 489     4009   3293   3353     17    563   -238       C  
ATOM   4092  N   LEU A 490      26.645  13.626 -42.105  1.00 40.68           N  
ANISOU 4092  N   LEU A 490     5384   5018   5052   -163    328   -490       N  
ATOM   4093  CA  LEU A 490      27.895  13.119 -41.557  1.00 43.50           C  
ANISOU 4093  CA  LEU A 490     5686   5421   5419   -196    284   -538       C  
ATOM   4094  C   LEU A 490      28.068  13.457 -40.077  1.00 43.35           C  
ANISOU 4094  C   LEU A 490     5653   5433   5382   -246    274   -567       C  
ATOM   4095  O   LEU A 490      29.097  13.997 -39.683  1.00 47.88           O  
ANISOU 4095  O   LEU A 490     6199   6033   5956   -300    300   -625       O  
ATOM   4096  CB  LEU A 490      29.103  13.608 -42.386  1.00 42.83           C  
ANISOU 4096  CB  LEU A 490     5583   5333   5355   -219    333   -586       C  
ATOM   4097  CG  LEU A 490      29.104  13.412 -43.917  1.00 45.41           C  
ANISOU 4097  CG  LEU A 490     5921   5633   5697   -177    354   -566       C  
ATOM   4098  CD1 LEU A 490      30.458  13.834 -44.505  1.00 42.96           C  
ANISOU 4098  CD1 LEU A 490     5586   5330   5407   -210    397   -622       C  
ATOM   4099  CD2 LEU A 490      28.747  11.976 -44.323  1.00 43.34           C  
ANISOU 4099  CD2 LEU A 490     5639   5388   5438   -124    274   -529       C  
ATOM   4100  N   VAL A 491      27.080  13.106 -39.256  1.00 44.49           N  
ANISOU 4100  N   VAL A 491     5814   5582   5507   -234    236   -531       N  
ATOM   4101  CA  VAL A 491      27.189  13.292 -37.783  1.00 47.43           C  
ANISOU 4101  CA  VAL A 491     6171   5993   5856   -280    218   -555       C  
ATOM   4102  C   VAL A 491      28.028  12.177 -37.132  1.00 48.90           C  
ANISOU 4102  C   VAL A 491     6295   6248   6036   -277    131   -565       C  
ATOM   4103  O   VAL A 491      27.908  11.005 -37.498  1.00 52.37           O  
ANISOU 4103  O   VAL A 491     6722   6691   6484   -225     71   -527       O  
ATOM   4104  CB  VAL A 491      25.790  13.345 -37.104  1.00 46.99           C  
ANISOU 4104  CB  VAL A 491     6156   5917   5779   -268    212   -511       C  
ATOM   4105  CG1 VAL A 491      25.900  13.389 -35.578  1.00 44.77           C  
ANISOU 4105  CG1 VAL A 491     5857   5683   5470   -315    185   -534       C  
ATOM   4106  CG2 VAL A 491      24.995  14.530 -37.613  1.00 44.26           C  
ANISOU 4106  CG2 VAL A 491     5868   5510   5437   -266    304   -499       C  
ATOM   4107  N   ASN A 492      28.879  12.543 -36.180  1.00 52.78           N  
ANISOU 4107  N   ASN A 492     6748   6797   6509   -331    129   -615       N  
ATOM   4108  CA  ASN A 492      29.592  11.546 -35.365  1.00 61.09           C  
ANISOU 4108  CA  ASN A 492     7739   7928   7544   -321     46   -616       C  
ATOM   4109  C   ASN A 492      29.267  11.601 -33.865  1.00 63.24           C  
ANISOU 4109  C   ASN A 492     8004   8249   7775   -354     18   -616       C  
ATOM   4110  O   ASN A 492      29.314  10.568 -33.184  1.00 64.47           O  
ANISOU 4110  O   ASN A 492     8132   8451   7913   -322    -56   -583       O  
ATOM   4111  CB  ASN A 492      31.110  11.590 -35.603  1.00 63.96           C  
ANISOU 4111  CB  ASN A 492     8036   8351   7914   -343     46   -671       C  
ATOM   4112  CG  ASN A 492      31.582  12.935 -36.121  1.00 72.08           C  
ANISOU 4112  CG  ASN A 492     9077   9355   8953   -405    140   -734       C  
ATOM   4113  OD1 ASN A 492      31.240  13.988 -35.568  1.00 76.76           O  
ANISOU 4113  OD1 ASN A 492     9702   9933   9530   -463    200   -764       O  
ATOM   4114  ND2 ASN A 492      32.370  12.909 -37.194  1.00 71.42           N  
ANISOU 4114  ND2 ASN A 492     8974   9264   8897   -394    161   -755       N  
ATOM   4115  N   ASP A 493      28.938  12.796 -33.357  1.00 60.60           N  
ANISOU 4115  N   ASP A 493     7698   7901   7425   -416     83   -652       N  
ATOM   4116  CA  ASP A 493      28.444  12.937 -31.979  1.00 60.17           C  
ANISOU 4116  CA  ASP A 493     7648   7883   7330   -451     66   -652       C  
ATOM   4117  C   ASP A 493      26.924  13.102 -31.928  1.00 55.98           C  
ANISOU 4117  C   ASP A 493     7186   7282   6801   -430     87   -603       C  
ATOM   4118  O   ASP A 493      26.379  14.168 -32.251  1.00 53.40           O  
ANISOU 4118  O   ASP A 493     6909   6895   6486   -452    169   -616       O  
ATOM   4119  CB  ASP A 493      29.139  14.083 -31.227  1.00 62.10           C  
ANISOU 4119  CB  ASP A 493     7870   8175   7548   -544    122   -734       C  
ATOM   4120  CG  ASP A 493      28.862  14.051 -29.709  1.00 65.43           C  
ANISOU 4120  CG  ASP A 493     8277   8661   7919   -582     89   -740       C  
ATOM   4121  OD1 ASP A 493      27.704  13.790 -29.301  1.00 62.89           O  
ANISOU 4121  OD1 ASP A 493     8000   8304   7590   -556     73   -689       O  
ATOM   4122  OD2 ASP A 493      29.805  14.300 -28.922  1.00 70.35           O  
ANISOU 4122  OD2 ASP A 493     8843   9379   8506   -641     81   -799       O  
ATOM   4123  N   PHE A 494      26.253  12.047 -31.485  1.00 51.18           N  
ANISOU 4123  N   PHE A 494     6582   6684   6180   -386     17   -546       N  
ATOM   4124  CA  PHE A 494      24.804  12.014 -31.485  1.00 51.94           C  
ANISOU 4124  CA  PHE A 494     6733   6724   6275   -361     27   -497       C  
ATOM   4125  C   PHE A 494      24.190  12.505 -30.165  1.00 50.88           C  
ANISOU 4125  C   PHE A 494     6615   6611   6104   -406     38   -506       C  
ATOM   4126  O   PHE A 494      23.069  12.140 -29.833  1.00 53.11           O  
ANISOU 4126  O   PHE A 494     6929   6873   6377   -384     20   -461       O  
ATOM   4127  CB  PHE A 494      24.306  10.604 -31.839  1.00 53.06           C  
ANISOU 4127  CB  PHE A 494     6877   6856   6426   -294    -42   -434       C  
ATOM   4128  CG  PHE A 494      24.575  10.201 -33.272  1.00 53.62           C  
ANISOU 4128  CG  PHE A 494     6946   6891   6534   -249    -38   -422       C  
ATOM   4129  CD1 PHE A 494      23.640  10.462 -34.271  1.00 52.47           C  
ANISOU 4129  CD1 PHE A 494     6842   6687   6407   -223      0   -397       C  
ATOM   4130  CD2 PHE A 494      25.766   9.567 -33.622  1.00 54.28           C  
ANISOU 4130  CD2 PHE A 494     6983   7007   6633   -232    -73   -437       C  
ATOM   4131  CE1 PHE A 494      23.883  10.096 -35.587  1.00 55.46           C  
ANISOU 4131  CE1 PHE A 494     7218   7040   6814   -185      4   -389       C  
ATOM   4132  CE2 PHE A 494      26.017   9.206 -34.935  1.00 56.46           C  
ANISOU 4132  CE2 PHE A 494     7259   7250   6943   -195    -66   -430       C  
ATOM   4133  CZ  PHE A 494      25.073   9.468 -35.920  1.00 56.76           C  
ANISOU 4133  CZ  PHE A 494     7341   7230   6995   -174    -27   -407       C  
ATOM   4134  N   GLY A 495      24.914  13.361 -29.446  1.00 46.40           N  
ANISOU 4134  N   GLY A 495     6026   6085   5516   -475     72   -569       N  
ATOM   4135  CA  GLY A 495      24.497  13.817 -28.122  1.00 45.46           C  
ANISOU 4135  CA  GLY A 495     5916   5999   5357   -528     82   -588       C  
ATOM   4136  C   GLY A 495      23.200  14.616 -28.087  1.00 43.64           C  
ANISOU 4136  C   GLY A 495     5751   5696   5132   -532    150   -574       C  
ATOM   4137  O   GLY A 495      22.272  14.276 -27.329  1.00 42.38           O  
ANISOU 4137  O   GLY A 495     5610   5542   4949   -525    123   -540       O  
ATOM   4138  N   PHE A 496      23.154  15.685 -28.891  1.00 41.09           N  
ANISOU 4138  N   PHE A 496     5463   5308   4838   -542    242   -598       N  
ATOM   4139  CA  PHE A 496      21.960  16.516 -29.091  1.00 37.89           C  
ANISOU 4139  CA  PHE A 496     5122   4827   4444   -529    318   -577       C  
ATOM   4140  C   PHE A 496      20.679  15.704 -29.304  1.00 35.62           C  
ANISOU 4140  C   PHE A 496     4856   4520   4157   -460    271   -500       C  
ATOM   4141  O   PHE A 496      19.588  16.208 -29.080  1.00 34.24           O  
ANISOU 4141  O   PHE A 496     4721   4309   3977   -451    315   -479       O  
ATOM   4142  CB  PHE A 496      22.168  17.494 -30.275  1.00 38.49           C  
ANISOU 4142  CB  PHE A 496     5233   4833   4558   -520    413   -592       C  
ATOM   4143  CG  PHE A 496      22.053  16.845 -31.643  1.00 38.17           C  
ANISOU 4143  CG  PHE A 496     5190   4765   4545   -444    384   -540       C  
ATOM   4144  CD1 PHE A 496      20.821  16.746 -32.280  1.00 38.49           C  
ANISOU 4144  CD1 PHE A 496     5267   4763   4594   -378    394   -476       C  
ATOM   4145  CD2 PHE A 496      23.178  16.325 -32.282  1.00 38.00           C  
ANISOU 4145  CD2 PHE A 496     5127   4772   4539   -440    347   -558       C  
ATOM   4146  CE1 PHE A 496      20.708  16.124 -33.518  1.00 40.92           C  
ANISOU 4146  CE1 PHE A 496     5569   5058   4921   -315    366   -434       C  
ATOM   4147  CE2 PHE A 496      23.076  15.726 -33.529  1.00 40.17           C  
ANISOU 4147  CE2 PHE A 496     5401   5023   4838   -376    324   -516       C  
ATOM   4148  CZ  PHE A 496      21.837  15.620 -34.148  1.00 40.83           C  
ANISOU 4148  CZ  PHE A 496     5520   5067   4925   -316    333   -455       C  
ATOM   4149  N   ILE A 497      20.820  14.451 -29.736  1.00 35.16           N  
ANISOU 4149  N   ILE A 497     4768   4486   4104   -414    188   -461       N  
ATOM   4150  CA  ILE A 497      19.673  13.571 -29.966  1.00 35.20           C  
ANISOU 4150  CA  ILE A 497     4789   4479   4107   -358    143   -396       C  
ATOM   4151  C   ILE A 497      18.813  13.370 -28.710  1.00 34.34           C  
ANISOU 4151  C   ILE A 497     4691   4393   3964   -378    119   -380       C  
ATOM   4152  O   ILE A 497      17.562  13.398 -28.788  1.00 33.36           O  
ANISOU 4152  O   ILE A 497     4597   4243   3836   -352    134   -343       O  
ATOM   4153  CB  ILE A 497      20.107  12.213 -30.572  1.00 37.08           C  
ANISOU 4153  CB  ILE A 497     4995   4735   4356   -315     64   -366       C  
ATOM   4154  CG1 ILE A 497      20.053  12.282 -32.087  1.00 37.32           C  
ANISOU 4154  CG1 ILE A 497     5035   4723   4419   -271     92   -351       C  
ATOM   4155  CG2 ILE A 497      19.226  11.055 -30.105  1.00 37.07           C  
ANISOU 4155  CG2 ILE A 497     4998   4748   4337   -290      0   -317       C  
ATOM   4156  CD1 ILE A 497      21.365  12.678 -32.711  1.00 40.25           C  
ANISOU 4156  CD1 ILE A 497     5384   5096   4813   -285    116   -393       C  
ATOM   4157  N   TRP A 498      19.467  13.204 -27.558  1.00 32.25           N  
ANISOU 4157  N   TRP A 498     4399   4185   3669   -426     85   -410       N  
ATOM   4158  CA  TRP A 498      18.737  12.892 -26.314  1.00 31.12           C  
ANISOU 4158  CA  TRP A 498     4263   4071   3487   -446     56   -394       C  
ATOM   4159  C   TRP A 498      17.581  13.815 -26.033  1.00 30.65           C  
ANISOU 4159  C   TRP A 498     4248   3973   3424   -458    124   -393       C  
ATOM   4160  O   TRP A 498      16.453  13.367 -25.803  1.00 28.48           O  
ANISOU 4160  O   TRP A 498     3992   3691   3137   -434    106   -351       O  
ATOM   4161  CB  TRP A 498      19.660  12.856 -25.098  1.00 31.09           C  
ANISOU 4161  CB  TRP A 498     4223   4143   3445   -502     24   -434       C  
ATOM   4162  CG  TRP A 498      18.878  12.508 -23.871  1.00 30.42           C  
ANISOU 4162  CG  TRP A 498     4149   4089   3319   -520     -5   -412       C  
ATOM   4163  CD1 TRP A 498      18.694  13.278 -22.735  1.00 31.28           C  
ANISOU 4163  CD1 TRP A 498     4265   4226   3392   -582     29   -451       C  
ATOM   4164  CD2 TRP A 498      18.038  11.318 -23.670  1.00 30.65           C  
ANISOU 4164  CD2 TRP A 498     4190   4117   3337   -478    -66   -348       C  
ATOM   4165  NE1 TRP A 498      17.845  12.648 -21.848  1.00 30.23           N  
ANISOU 4165  NE1 TRP A 498     4145   4114   3226   -579    -10   -413       N  
ATOM   4166  CE2 TRP A 498      17.419  11.466 -22.359  1.00 31.24           C  
ANISOU 4166  CE2 TRP A 498     4277   4224   3368   -518    -67   -350       C  
ATOM   4167  CE3 TRP A 498      17.767  10.178 -24.417  1.00 29.16           C  
ANISOU 4167  CE3 TRP A 498     4004   3904   3170   -419   -113   -295       C  
ATOM   4168  CZ2 TRP A 498      16.574  10.493 -21.827  1.00 30.27           C  
ANISOU 4168  CZ2 TRP A 498     4169   4108   3224   -498   -114   -298       C  
ATOM   4169  CZ3 TRP A 498      16.917   9.219 -23.882  1.00 30.04           C  
ANISOU 4169  CZ3 TRP A 498     4132   4020   3261   -403   -156   -247       C  
ATOM   4170  CH2 TRP A 498      16.340   9.370 -22.610  1.00 29.89           C  
ANISOU 4170  CH2 TRP A 498     4125   4031   3199   -441   -157   -247       C  
ATOM   4171  N   LEU A 499      17.851  15.121 -26.045  1.00 31.19           N  
ANISOU 4171  N   LEU A 499     4335   4015   3501   -496    211   -442       N  
ATOM   4172  CA  LEU A 499      16.810  16.087 -25.721  1.00 31.30           C  
ANISOU 4172  CA  LEU A 499     4393   3987   3512   -505    288   -444       C  
ATOM   4173  C   LEU A 499      15.763  16.225 -26.817  1.00 29.24           C  
ANISOU 4173  C   LEU A 499     4162   3669   3277   -434    322   -391       C  
ATOM   4174  O   LEU A 499      14.609  16.507 -26.523  1.00 29.48           O  
ANISOU 4174  O   LEU A 499     4219   3682   3297   -418    352   -367       O  
ATOM   4175  CB  LEU A 499      17.402  17.455 -25.320  1.00 33.31           C  
ANISOU 4175  CB  LEU A 499     4664   4222   3766   -572    382   -515       C  
ATOM   4176  CG  LEU A 499      18.163  17.456 -23.978  1.00 35.43           C  
ANISOU 4176  CG  LEU A 499     4903   4565   3993   -655    357   -573       C  
ATOM   4177  CD1 LEU A 499      19.151  18.611 -23.915  1.00 36.76           C  
ANISOU 4177  CD1 LEU A 499     5072   4725   4167   -727    441   -656       C  
ATOM   4178  CD2 LEU A 499      17.221  17.458 -22.759  1.00 35.01           C  
ANISOU 4178  CD2 LEU A 499     4865   4531   3902   -680    353   -567       C  
ATOM   4179  N   VAL A 500      16.144  15.995 -28.072  1.00 27.93           N  
ANISOU 4179  N   VAL A 500     3988   3483   3140   -390    316   -373       N  
ATOM   4180  CA  VAL A 500      15.156  15.999 -29.154  1.00 28.39           C  
ANISOU 4180  CA  VAL A 500     4065   3507   3213   -318    338   -320       C  
ATOM   4181  C   VAL A 500      14.224  14.780 -28.985  1.00 28.60           C  
ANISOU 4181  C   VAL A 500     4077   3568   3220   -289    259   -272       C  
ATOM   4182  O   VAL A 500      12.999  14.919 -29.048  1.00 27.52           O  
ANISOU 4182  O   VAL A 500     3956   3425   3073   -258    280   -237       O  
ATOM   4183  CB  VAL A 500      15.815  15.966 -30.565  1.00 30.71           C  
ANISOU 4183  CB  VAL A 500     4351   3779   3537   -281    346   -313       C  
ATOM   4184  CG1 VAL A 500      14.751  15.999 -31.666  1.00 28.14           C  
ANISOU 4184  CG1 VAL A 500     4039   3433   3217   -207    369   -257       C  
ATOM   4185  CG2 VAL A 500      16.821  17.110 -30.737  1.00 29.47           C  
ANISOU 4185  CG2 VAL A 500     4209   3586   3399   -317    427   -365       C  
ATOM   4186  N   LEU A 501      14.816  13.598 -28.760  1.00 27.75           N  
ANISOU 4186  N   LEU A 501     3939   3498   3107   -300    174   -270       N  
ATOM   4187  CA  LEU A 501      14.054  12.386 -28.458  1.00 27.98           C  
ANISOU 4187  CA  LEU A 501     3959   3554   3116   -286    104   -231       C  
ATOM   4188  C   LEU A 501      13.093  12.612 -27.260  1.00 27.99           C  
ANISOU 4188  C   LEU A 501     3977   3569   3086   -313    115   -227       C  
ATOM   4189  O   LEU A 501      11.882  12.361 -27.377  1.00 26.96           O  
ANISOU 4189  O   LEU A 501     3856   3441   2946   -287    115   -193       O  
ATOM   4190  CB  LEU A 501      14.996  11.176 -28.187  1.00 28.31           C  
ANISOU 4190  CB  LEU A 501     3973   3627   3156   -296     23   -232       C  
ATOM   4191  CG  LEU A 501      14.313   9.816 -27.901  1.00 28.68           C  
ANISOU 4191  CG  LEU A 501     4018   3690   3186   -282    -41   -192       C  
ATOM   4192  CD1 LEU A 501      13.269   9.492 -28.965  1.00 28.24           C  
ANISOU 4192  CD1 LEU A 501     3970   3617   3140   -241    -32   -160       C  
ATOM   4193  CD2 LEU A 501      15.304   8.661 -27.754  1.00 28.16           C  
ANISOU 4193  CD2 LEU A 501     3931   3644   3123   -279   -108   -187       C  
ATOM   4194  N   SER A 502      13.635  13.104 -26.138  1.00 29.07           N  
ANISOU 4194  N   SER A 502     4116   3723   3206   -367    127   -265       N  
ATOM   4195  CA  SER A 502      12.829  13.470 -24.935  1.00 30.06           C  
ANISOU 4195  CA  SER A 502     4259   3861   3301   -401    147   -271       C  
ATOM   4196  C   SER A 502      11.660  14.436 -25.195  1.00 30.15           C  
ANISOU 4196  C   SER A 502     4300   3836   3317   -376    226   -259       C  
ATOM   4197  O   SER A 502      10.541  14.172 -24.750  1.00 31.80           O  
ANISOU 4197  O   SER A 502     4517   4058   3506   -369    219   -232       O  
ATOM   4198  CB  SER A 502      13.720  14.026 -23.810  1.00 32.04           C  
ANISOU 4198  CB  SER A 502     4504   4139   3530   -469    160   -325       C  
ATOM   4199  OG  SER A 502      14.716  13.082 -23.437  1.00 36.28           O  
ANISOU 4199  OG  SER A 502     5007   4725   4052   -484     82   -328       O  
ATOM   4200  N   SER A 503      11.922  15.566 -25.857  1.00 28.45           N  
ANISOU 4200  N   SER A 503     4103   3578   3128   -363    306   -277       N  
ATOM   4201  CA  SER A 503      10.848  16.468 -26.301  1.00 29.34           C  
ANISOU 4201  CA  SER A 503     4244   3653   3249   -319    386   -254       C  
ATOM   4202  C   SER A 503       9.770  15.756 -27.117  1.00 28.80           C  
ANISOU 4202  C   SER A 503     4162   3602   3177   -254    352   -195       C  
ATOM   4203  O   SER A 503       8.561  15.946 -26.876  1.00 29.45           O  
ANISOU 4203  O   SER A 503     4252   3694   3243   -231    376   -169       O  
ATOM   4204  CB  SER A 503      11.417  17.570 -27.168  1.00 32.58           C  
ANISOU 4204  CB  SER A 503     4677   4010   3692   -300    471   -270       C  
ATOM   4205  OG  SER A 503      12.327  18.319 -26.418  1.00 45.07           O  
ANISOU 4205  OG  SER A 503     6273   5577   5275   -369    515   -332       O  
ATOM   4206  N   THR A 504      10.210  14.963 -28.097  1.00 27.73           N  
ANISOU 4206  N   THR A 504     4003   3477   3054   -227    301   -178       N  
ATOM   4207  CA  THR A 504       9.314  14.172 -28.942  1.00 27.63           C  
ANISOU 4207  CA  THR A 504     3972   3491   3034   -177    264   -132       C  
ATOM   4208  C   THR A 504       8.397  13.265 -28.144  1.00 27.18           C  
ANISOU 4208  C   THR A 504     3904   3474   2946   -196    212   -116       C  
ATOM   4209  O   THR A 504       7.193  13.285 -28.350  1.00 29.24           O  
ANISOU 4209  O   THR A 504     4160   3757   3191   -165    227    -88       O  
ATOM   4210  CB  THR A 504      10.106  13.331 -29.956  1.00 28.41           C  
ANISOU 4210  CB  THR A 504     4048   3594   3150   -162    213   -129       C  
ATOM   4211  OG1 THR A 504      11.002  14.187 -30.667  1.00 28.78           O  
ANISOU 4211  OG1 THR A 504     4105   3604   3223   -149    264   -146       O  
ATOM   4212  CG2 THR A 504       9.167  12.646 -30.952  1.00 28.18           C  
ANISOU 4212  CG2 THR A 504     3999   3596   3110   -115    189    -90       C  
ATOM   4213  N   VAL A 505       8.951  12.468 -27.231  1.00 27.16           N  
ANISOU 4213  N   VAL A 505     3899   3486   2935   -245    153   -133       N  
ATOM   4214  CA  VAL A 505       8.098  11.596 -26.380  1.00 26.60           C  
ANISOU 4214  CA  VAL A 505     3825   3448   2833   -269    109   -117       C  
ATOM   4215  C   VAL A 505       7.113  12.444 -25.564  1.00 25.74           C  
ANISOU 4215  C   VAL A 505     3731   3343   2703   -278    163   -119       C  
ATOM   4216  O   VAL A 505       5.927  12.126 -25.465  1.00 25.07           O  
ANISOU 4216  O   VAL A 505     3641   3285   2599   -267    159    -96       O  
ATOM   4217  CB  VAL A 505       8.931  10.719 -25.429  1.00 26.74           C  
ANISOU 4217  CB  VAL A 505     3841   3478   2839   -315     46   -130       C  
ATOM   4218  CG1 VAL A 505       8.038  10.041 -24.373  1.00 26.31           C  
ANISOU 4218  CG1 VAL A 505     3794   3451   2750   -344     17   -115       C  
ATOM   4219  CG2 VAL A 505       9.746   9.697 -26.210  1.00 25.56           C  
ANISOU 4219  CG2 VAL A 505     3676   3325   2709   -298     -7   -121       C  
ATOM   4220  N   ARG A 506       7.603  13.550 -25.021  1.00 26.20           N  
ANISOU 4220  N   ARG A 506     3810   3376   2769   -300    218   -151       N  
ATOM   4221  CA  ARG A 506       6.731  14.493 -24.337  1.00 26.72           C  
ANISOU 4221  CA  ARG A 506     3895   3435   2821   -305    284   -156       C  
ATOM   4222  C   ARG A 506       5.591  14.979 -25.261  1.00 25.53           C  
ANISOU 4222  C   ARG A 506     3741   3283   2675   -235    334   -119       C  
ATOM   4223  O   ARG A 506       4.439  14.878 -24.910  1.00 24.59           O  
ANISOU 4223  O   ARG A 506     3616   3192   2533   -225    340   -100       O  
ATOM   4224  CB  ARG A 506       7.559  15.646 -23.736  1.00 28.71           C  
ANISOU 4224  CB  ARG A 506     4171   3652   3082   -345    348   -204       C  
ATOM   4225  CG  ARG A 506       6.733  16.692 -22.978  1.00 30.61           C  
ANISOU 4225  CG  ARG A 506     4439   3877   3312   -354    429   -217       C  
ATOM   4226  CD  ARG A 506       6.578  17.907 -23.906  1.00 33.81           C  
ANISOU 4226  CD  ARG A 506     4868   4228   3748   -298    528   -208       C  
ATOM   4227  NE  ARG A 506       5.212  18.392 -23.914  1.00 34.05           N  
ANISOU 4227  NE  ARG A 506     4907   4258   3770   -248    582   -175       N  
ATOM   4228  CZ  ARG A 506       4.679  19.148 -24.858  1.00 35.24           C  
ANISOU 4228  CZ  ARG A 506     5068   4382   3938   -172    651   -141       C  
ATOM   4229  NH1 ARG A 506       5.391  19.517 -25.936  1.00 32.52           N  
ANISOU 4229  NH1 ARG A 506     4731   4003   3622   -137    678   -133       N  
ATOM   4230  NH2 ARG A 506       3.414  19.526 -24.718  1.00 35.95           N  
ANISOU 4230  NH2 ARG A 506     5159   4485   4015   -126    696   -110       N  
ATOM   4231  N   ALA A 507       5.932  15.409 -26.473  1.00 25.37           N  
ANISOU 4231  N   ALA A 507     3719   3240   2680   -185    365   -106       N  
ATOM   4232  CA  ALA A 507       4.963  15.991 -27.409  1.00 25.91           C  
ANISOU 4232  CA  ALA A 507     3782   3312   2747   -109    418    -66       C  
ATOM   4233  C   ALA A 507       3.917  15.014 -27.893  1.00 26.59           C  
ANISOU 4233  C   ALA A 507     3830   3463   2808    -81    365    -30       C  
ATOM   4234  O   ALA A 507       2.737  15.382 -28.017  1.00 28.62           O  
ANISOU 4234  O   ALA A 507     4076   3751   3046    -36    400     -1       O  
ATOM   4235  CB  ALA A 507       5.676  16.624 -28.602  1.00 25.36           C  
ANISOU 4235  CB  ALA A 507     3722   3206   2707    -64    461    -58       C  
ATOM   4236  N   TYR A 508       4.330  13.782 -28.203  1.00 26.08           N  
ANISOU 4236  N   TYR A 508     3745   3421   2742   -105    285    -33       N  
ATOM   4237  CA  TYR A 508       3.381  12.785 -28.701  1.00 26.54           C  
ANISOU 4237  CA  TYR A 508     3768   3540   2775    -91    238     -9       C  
ATOM   4238  C   TYR A 508       2.459  12.289 -27.594  1.00 28.10           C  
ANISOU 4238  C   TYR A 508     3962   3770   2942   -131    218    -12       C  
ATOM   4239  O   TYR A 508       1.246  12.154 -27.798  1.00 28.05           O  
ANISOU 4239  O   TYR A 508     3929   3817   2909   -108    224      8       O  
ATOM   4240  CB  TYR A 508       4.107  11.639 -29.401  1.00 26.91           C  
ANISOU 4240  CB  TYR A 508     3800   3590   2832   -106    172    -15       C  
ATOM   4241  CG  TYR A 508       4.404  11.962 -30.855  1.00 28.45           C  
ANISOU 4241  CG  TYR A 508     3981   3787   3041    -50    192      0       C  
ATOM   4242  CD1 TYR A 508       3.420  11.829 -31.821  1.00 28.76           C  
ANISOU 4242  CD1 TYR A 508     3986   3885   3056     -4    197     27       C  
ATOM   4243  CD2 TYR A 508       5.645  12.446 -31.248  1.00 28.95           C  
ANISOU 4243  CD2 TYR A 508     4062   3799   3137    -45    209    -14       C  
ATOM   4244  CE1 TYR A 508       3.671  12.119 -33.139  1.00 29.77           C  
ANISOU 4244  CE1 TYR A 508     4098   4021   3188     47    215     43       C  
ATOM   4245  CE2 TYR A 508       5.909  12.751 -32.579  1.00 30.44           C  
ANISOU 4245  CE2 TYR A 508     4240   3988   3336      5    230      0       C  
ATOM   4246  CZ  TYR A 508       4.910  12.593 -33.522  1.00 30.42           C  
ANISOU 4246  CZ  TYR A 508     4205   4045   3306     53    233     32       C  
ATOM   4247  OH  TYR A 508       5.125  12.913 -34.859  1.00 29.76           O  
ANISOU 4247  OH  TYR A 508     4109   3971   3225    106    255     51       O  
ATOM   4248  N   ALA A 509       3.029  12.080 -26.404  1.00 28.14           N  
ANISOU 4248  N   ALA A 509     3992   3749   2949   -190    197    -37       N  
ATOM   4249  CA  ALA A 509       2.240  11.776 -25.209  1.00 29.78           C  
ANISOU 4249  CA  ALA A 509     4205   3981   3128   -232    187    -41       C  
ATOM   4250  C   ALA A 509       1.192  12.857 -24.912  1.00 29.84           C  
ANISOU 4250  C   ALA A 509     4213   4002   3123   -202    258    -32       C  
ATOM   4251  O   ALA A 509       0.071  12.554 -24.478  1.00 28.39           O  
ANISOU 4251  O   ALA A 509     4013   3861   2909   -210    256    -23       O  
ATOM   4252  CB  ALA A 509       3.156  11.574 -24.002  1.00 29.22           C  
ANISOU 4252  CB  ALA A 509     4160   3884   3056   -294    161    -67       C  
ATOM   4253  N   SER A 510       1.563  14.112 -25.149  1.00 29.96           N  
ANISOU 4253  N   SER A 510     4247   3976   3160   -167    327    -36       N  
ATOM   4254  CA  SER A 510       0.659  15.215 -24.904  1.00 32.88           C  
ANISOU 4254  CA  SER A 510     4624   4344   3523   -129    407    -25       C  
ATOM   4255  C   SER A 510      -0.466  15.273 -25.940  1.00 34.23           C  
ANISOU 4255  C   SER A 510     4756   4570   3678    -52    424     18       C  
ATOM   4256  O   SER A 510      -1.621  15.453 -25.588  1.00 36.23           O  
ANISOU 4256  O   SER A 510     4992   4865   3906    -34    449     32       O  
ATOM   4257  CB  SER A 510       1.418  16.534 -24.878  1.00 33.14           C  
ANISOU 4257  CB  SER A 510     4696   4308   3586   -116    488    -42       C  
ATOM   4258  OG  SER A 510       0.508  17.600 -24.979  1.00 34.34           O  
ANISOU 4258  OG  SER A 510     4856   4454   3737    -56    575    -19       O  
ATOM   4259  N   ARG A 511      -0.132  15.102 -27.213  1.00 36.55           N  
ANISOU 4259  N   ARG A 511     5032   4873   3982     -9    410     37       N  
ATOM   4260  CA  ARG A 511      -1.170  15.046 -28.250  1.00 37.41           C  
ANISOU 4260  CA  ARG A 511     5094   5054   4066     61    416     78       C  
ATOM   4261  C   ARG A 511      -2.130  13.894 -28.000  1.00 35.41           C  
ANISOU 4261  C   ARG A 511     4799   4880   3775     24    356     75       C  
ATOM   4262  O   ARG A 511      -3.333  14.052 -28.164  1.00 35.16           O  
ANISOU 4262  O   ARG A 511     4729   4917   3711     64    377     98       O  
ATOM   4263  CB  ARG A 511      -0.569  14.976 -29.666  1.00 39.99           C  
ANISOU 4263  CB  ARG A 511     5407   5381   4404    106    406     96       C  
ATOM   4264  CG  ARG A 511       0.002  16.311 -30.143  1.00 48.00           C  
ANISOU 4264  CG  ARG A 511     6457   6333   5449    165    488    112       C  
ATOM   4265  CD  ARG A 511       0.485  16.267 -31.594  1.00 51.53           C  
ANISOU 4265  CD  ARG A 511     6888   6789   5901    215    482    135       C  
ATOM   4266  NE  ARG A 511       1.638  17.153 -31.844  1.00 55.52           N  
ANISOU 4266  NE  ARG A 511     7441   7206   6446    225    537    126       N  
ATOM   4267  CZ  ARG A 511       2.896  16.729 -32.028  1.00 53.99           C  
ANISOU 4267  CZ  ARG A 511     7262   6971   6280    178    499     94       C  
ATOM   4268  NH1 ARG A 511       3.183  15.439 -31.983  1.00 49.04           N  
ANISOU 4268  NH1 ARG A 511     6610   6374   5647    124    410     71       N  
ATOM   4269  NH2 ARG A 511       3.874  17.602 -32.258  1.00 53.79           N  
ANISOU 4269  NH2 ARG A 511     7277   6871   6288    185    557     83       N  
ATOM   4270  N   ALA A 512      -1.598  12.742 -27.592  1.00 32.77           N  
ANISOU 4270  N   ALA A 512     4472   4535   3442    -49    287     48       N  
ATOM   4271  CA  ALA A 512      -2.441  11.618 -27.240  1.00 32.64           C  
ANISOU 4271  CA  ALA A 512     4429   4579   3394    -96    238     40       C  
ATOM   4272  C   ALA A 512      -3.406  11.973 -26.095  1.00 33.32           C  
ANISOU 4272  C   ALA A 512     4517   4687   3457   -113    269     38       C  
ATOM   4273  O   ALA A 512      -4.619  11.746 -26.214  1.00 33.09           O  
ANISOU 4273  O   ALA A 512     4445   4734   3392   -102    272     48       O  
ATOM   4274  CB  ALA A 512      -1.602  10.400 -26.885  1.00 30.50           C  
ANISOU 4274  CB  ALA A 512     4180   4275   3134   -168    171     16       C  
ATOM   4275  N   PHE A 513      -2.869  12.532 -25.000  1.00 32.93           N  
ANISOU 4275  N   PHE A 513     4513   4575   3424   -144    293     20       N  
ATOM   4276  CA  PHE A 513      -3.680  12.921 -23.832  1.00 33.67           C  
ANISOU 4276  CA  PHE A 513     4613   4680   3497   -165    326     13       C  
ATOM   4277  C   PHE A 513      -4.883  13.777 -24.244  1.00 34.93           C  
ANISOU 4277  C   PHE A 513     4739   4892   3640    -90    389     40       C  
ATOM   4278  O   PHE A 513      -6.014  13.506 -23.831  1.00 35.18           O  
ANISOU 4278  O   PHE A 513     4740   4986   3638   -100    390     43       O  
ATOM   4279  CB  PHE A 513      -2.819  13.658 -22.774  1.00 34.17           C  
ANISOU 4279  CB  PHE A 513     4729   4670   3581   -200    358    -12       C  
ATOM   4280  CG  PHE A 513      -3.533  13.908 -21.458  1.00 33.53           C  
ANISOU 4280  CG  PHE A 513     4661   4599   3476   -239    385    -27       C  
ATOM   4281  CD1 PHE A 513      -4.325  15.046 -21.278  1.00 34.00           C  
ANISOU 4281  CD1 PHE A 513     4721   4662   3535   -192    467    -19       C  
ATOM   4282  CD2 PHE A 513      -3.408  13.006 -20.392  1.00 34.05           C  
ANISOU 4282  CD2 PHE A 513     4741   4671   3522   -319    334    -47       C  
ATOM   4283  CE1 PHE A 513      -4.981  15.279 -20.062  1.00 34.16           C  
ANISOU 4283  CE1 PHE A 513     4752   4691   3534   -229    496    -37       C  
ATOM   4284  CE2 PHE A 513      -4.060  13.233 -19.175  1.00 34.12           C  
ANISOU 4284  CE2 PHE A 513     4763   4694   3507   -357    360    -62       C  
ATOM   4285  CZ  PHE A 513      -4.848  14.369 -19.010  1.00 33.78           C  
ANISOU 4285  CZ  PHE A 513     4717   4654   3463   -315    440    -60       C  
ATOM   4286  N   LYS A 514      -4.630  14.794 -25.069  1.00 36.98           N  
ANISOU 4286  N   LYS A 514     5002   5127   3920    -13    444     64       N  
ATOM   4287  CA  LYS A 514      -5.670  15.711 -25.540  1.00 38.83           C  
ANISOU 4287  CA  LYS A 514     5207   5407   4140     77    512    101       C  
ATOM   4288  C   LYS A 514      -6.712  15.019 -26.392  1.00 37.69           C  
ANISOU 4288  C   LYS A 514     4989   5376   3953    109    476    125       C  
ATOM   4289  O   LYS A 514      -7.900  15.230 -26.211  1.00 37.60           O  
ANISOU 4289  O   LYS A 514     4938   5435   3910    140    503    140       O  
ATOM   4290  CB  LYS A 514      -5.054  16.868 -26.326  1.00 43.97           C  
ANISOU 4290  CB  LYS A 514     5884   5998   4821    155    579    126       C  
ATOM   4291  CG  LYS A 514      -4.521  17.981 -25.443  1.00 51.97           C  
ANISOU 4291  CG  LYS A 514     6961   6915   5867    144    657    106       C  
ATOM   4292  CD  LYS A 514      -3.979  19.148 -26.262  1.00 58.77           C  
ANISOU 4292  CD  LYS A 514     7855   7714   6760    221    737    132       C  
ATOM   4293  CE  LYS A 514      -3.472  20.266 -25.352  1.00 61.54           C  
ANISOU 4293  CE  LYS A 514     8273   7965   7142    199    826    102       C  
ATOM   4294  NZ  LYS A 514      -2.627  19.739 -24.239  1.00 63.64           N  
ANISOU 4294  NZ  LYS A 514     8567   8196   7415     82    777     40       N  
ATOM   4295  N   LYS A 515      -6.263  14.193 -27.328  1.00 37.37           N  
ANISOU 4295  N   LYS A 515     4928   5358   3910     98    418    124       N  
ATOM   4296  CA  LYS A 515      -7.175  13.453 -28.182  1.00 38.69           C  
ANISOU 4296  CA  LYS A 515     5024   5642   4035    113    382    135       C  
ATOM   4297  C   LYS A 515      -8.072  12.532 -27.351  1.00 38.40           C  
ANISOU 4297  C   LYS A 515     4961   5663   3963     38    348    108       C  
ATOM   4298  O   LYS A 515      -9.267  12.439 -27.599  1.00 40.21           O  
ANISOU 4298  O   LYS A 515     5129   5999   4149     63    355    118       O  
ATOM   4299  CB  LYS A 515      -6.397  12.668 -29.241  1.00 40.87           C  
ANISOU 4299  CB  LYS A 515     5292   5917   4318     98    329    128       C  
ATOM   4300  CG  LYS A 515      -6.439  13.275 -30.638  1.00 44.42           C  
ANISOU 4300  CG  LYS A 515     5708   6411   4758    194    355    168       C  
ATOM   4301  CD  LYS A 515      -5.526  14.486 -30.780  1.00 48.33           C  
ANISOU 4301  CD  LYS A 515     6257   6808   5297    252    415    191       C  
ATOM   4302  CE  LYS A 515      -5.243  14.808 -32.248  1.00 50.97           C  
ANISOU 4302  CE  LYS A 515     6570   7170   5626    329    427    226       C  
ATOM   4303  NZ  LYS A 515      -6.404  15.439 -32.949  1.00 53.49           N  
ANISOU 4303  NZ  LYS A 515     6830   7594   5899    432    469    279       N  
ATOM   4304  N   ILE A 516      -7.492  11.892 -26.337  1.00 36.88           N  
ANISOU 4304  N   ILE A 516     4817   5405   3788    -49    314     74       N  
ATOM   4305  CA  ILE A 516      -8.224  11.000 -25.451  1.00 36.27           C  
ANISOU 4305  CA  ILE A 516     4730   5367   3683   -127    286     48       C  
ATOM   4306  C   ILE A 516      -9.288  11.759 -24.643  1.00 38.48           C  
ANISOU 4306  C   ILE A 516     4995   5684   3941   -105    340     55       C  
ATOM   4307  O   ILE A 516     -10.409  11.261 -24.459  1.00 37.66           O  
ANISOU 4307  O   ILE A 516     4844   5667   3796   -129    333     47       O  
ATOM   4308  CB  ILE A 516      -7.265  10.196 -24.525  1.00 34.97           C  
ANISOU 4308  CB  ILE A 516     4627   5118   3540   -217    242     20       C  
ATOM   4309  CG1 ILE A 516      -6.597   9.060 -25.313  1.00 33.86           C  
ANISOU 4309  CG1 ILE A 516     4486   4969   3408   -249    184      9       C  
ATOM   4310  CG2 ILE A 516      -8.003   9.634 -23.312  1.00 34.17           C  
ANISOU 4310  CG2 ILE A 516     4532   5038   3411   -288    235      0       C  
ATOM   4311  CD1 ILE A 516      -5.444   8.382 -24.594  1.00 32.26           C  
ANISOU 4311  CD1 ILE A 516     4344   4680   3233   -312    145     -6       C  
ATOM   4312  N   VAL A 517      -8.943  12.972 -24.198  1.00 38.32           N  
ANISOU 4312  N   VAL A 517     5013   5598   3948    -60    399     68       N  
ATOM   4313  CA  VAL A 517      -9.875  13.831 -23.473  1.00 39.34           C  
ANISOU 4313  CA  VAL A 517     5133   5750   4063    -28    462     76       C  
ATOM   4314  C   VAL A 517     -11.025  14.277 -24.381  1.00 42.51           C  
ANISOU 4314  C   VAL A 517     5461   6258   4431     65    496    113       C  
ATOM   4315  O   VAL A 517     -12.195  14.134 -24.032  1.00 44.53           O  
ANISOU 4315  O   VAL A 517     5669   6599   4649     63    506    111       O  
ATOM   4316  CB  VAL A 517      -9.148  15.055 -22.847  1.00 39.57           C  
ANISOU 4316  CB  VAL A 517     5228   5674   4132     -5    528     75       C  
ATOM   4317  CG1 VAL A 517     -10.138  16.149 -22.445  1.00 40.00           C  
ANISOU 4317  CG1 VAL A 517     5270   5750   4177     58    613     93       C  
ATOM   4318  CG2 VAL A 517      -8.317  14.622 -21.637  1.00 36.98           C  
ANISOU 4318  CG2 VAL A 517     4958   5274   3818   -106    498     34       C  
ATOM   4319  N   THR A 518     -10.682  14.791 -25.555  1.00 45.01           N  
ANISOU 4319  N   THR A 518     5765   6578   4759    148    513    147       N  
ATOM   4320  CA  THR A 518     -11.666  15.281 -26.522  1.00 48.00           C  
ANISOU 4320  CA  THR A 518     6071   7064   5102    252    545    192       C  
ATOM   4321  C   THR A 518     -12.696  14.223 -26.936  1.00 48.70           C  
ANISOU 4321  C   THR A 518     6073   7296   5131    221    491    180       C  
ATOM   4322  O   THR A 518     -13.878  14.531 -27.090  1.00 50.88           O  
ANISOU 4322  O   THR A 518     6282   7684   5366    278    520    202       O  
ATOM   4323  CB  THR A 518     -10.969  15.822 -27.783  1.00 47.29           C  
ANISOU 4323  CB  THR A 518     5986   6951   5029    335    561    231       C  
ATOM   4324  OG1 THR A 518     -10.141  16.926 -27.421  1.00 47.92           O  
ANISOU 4324  OG1 THR A 518     6143   6904   5160    368    627    241       O  
ATOM   4325  CG2 THR A 518     -11.985  16.291 -28.815  1.00 48.93           C  
ANISOU 4325  CG2 THR A 518     6114   7284   5191    450    591    284       C  
ATOM   4326  N   TYR A 519     -12.237  12.990 -27.127  1.00 45.66           N  
ANISOU 4326  N   TYR A 519     5691   6911   4744    130    419    143       N  
ATOM   4327  CA  TYR A 519     -13.094  11.928 -27.633  1.00 44.25           C  
ANISOU 4327  CA  TYR A 519     5436   6862   4512     88    373    122       C  
ATOM   4328  C   TYR A 519     -13.403  10.895 -26.567  1.00 43.27           C  
ANISOU 4328  C   TYR A 519     5327   6733   4378    -31    340     73       C  
ATOM   4329  O   TYR A 519     -13.683   9.735 -26.866  1.00 43.09           O  
ANISOU 4329  O   TYR A 519     5273   6769   4327   -105    295     39       O  
ATOM   4330  CB  TYR A 519     -12.465  11.294 -28.867  1.00 44.67           C  
ANISOU 4330  CB  TYR A 519     5475   6933   4565     83    327    118       C  
ATOM   4331  CG  TYR A 519     -12.244  12.306 -29.953  1.00 46.32           C  
ANISOU 4331  CG  TYR A 519     5666   7158   4776    204    362    171       C  
ATOM   4332  CD1 TYR A 519     -13.319  13.024 -30.474  1.00 48.71           C  
ANISOU 4332  CD1 TYR A 519     5893   7582   5032    304    402    214       C  
ATOM   4333  CD2 TYR A 519     -10.962  12.584 -30.438  1.00 45.42           C  
ANISOU 4333  CD2 TYR A 519     5609   6938   4708    224    360    183       C  
ATOM   4334  CE1 TYR A 519     -13.135  13.977 -31.461  1.00 51.27           C  
ANISOU 4334  CE1 TYR A 519     6204   7919   5354    424    441    271       C  
ATOM   4335  CE2 TYR A 519     -10.768  13.535 -31.431  1.00 47.55           C  
ANISOU 4335  CE2 TYR A 519     5868   7219   4979    335    400    234       C  
ATOM   4336  CZ  TYR A 519     -11.861  14.231 -31.935  1.00 49.66           C  
ANISOU 4336  CZ  TYR A 519     6065   7604   5199    437    441    281       C  
ATOM   4337  OH  TYR A 519     -11.708  15.180 -32.917  1.00 53.62           O  
ANISOU 4337  OH  TYR A 519     6558   8118   5697    556    486    341       O  
ATOM   4338  N   LYS A 520     -13.358  11.345 -25.317  1.00 42.72           N  
ANISOU 4338  N   LYS A 520     5309   6591   4330    -52    370     67       N  
ATOM   4339  CA  LYS A 520     -13.698  10.528 -24.165  1.00 43.06           C  
ANISOU 4339  CA  LYS A 520     5372   6625   4361   -157    350     28       C  
ATOM   4340  C   LYS A 520     -15.147  10.051 -24.234  1.00 43.06           C  
ANISOU 4340  C   LYS A 520     5288   6769   4301   -177    351     13       C  
ATOM   4341  O   LYS A 520     -16.052  10.823 -24.538  1.00 43.44           O  
ANISOU 4341  O   LYS A 520     5273   6909   4322    -96    391     38       O  
ATOM   4342  CB  LYS A 520     -13.473  11.338 -22.889  1.00 42.60           C  
ANISOU 4342  CB  LYS A 520     5374   6479   4329   -158    392     30       C  
ATOM   4343  CG  LYS A 520     -13.718  10.570 -21.599  1.00 43.79           C  
ANISOU 4343  CG  LYS A 520     5557   6613   4469   -264    374     -5       C  
ATOM   4344  CD  LYS A 520     -13.358  11.403 -20.379  1.00 42.74           C  
ANISOU 4344  CD  LYS A 520     5486   6394   4360   -268    416     -6       C  
ATOM   4345  CE  LYS A 520     -11.849  11.555 -20.252  1.00 43.67           C  
ANISOU 4345  CE  LYS A 520     5677   6391   4524   -280    399     -7       C  
ATOM   4346  NZ  LYS A 520     -11.492  12.449 -19.115  1.00 45.50           N  
ANISOU 4346  NZ  LYS A 520     5963   6548   4774   -287    445    -16       N  
ATOM   4347  N   GLY A 521     -15.354   8.771 -23.964  1.00 42.90           N  
ANISOU 4347  N   GLY A 521     5267   6769   4261   -285    310    -28       N  
ATOM   4348  CA  GLY A 521     -16.701   8.229 -23.848  1.00 44.96           C  
ANISOU 4348  CA  GLY A 521     5456   7161   4465   -329    314    -55       C  
ATOM   4349  C   GLY A 521     -16.864   7.327 -22.643  1.00 44.91           C  
ANISOU 4349  C   GLY A 521     5495   7113   4454   -447    303    -94       C  
ATOM   4350  O   GLY A 521     -15.945   7.179 -21.835  1.00 44.97           O  
ANISOU 4350  O   GLY A 521     5589   6995   4500   -487    291    -94       O  
ATOM   4351  N   GLY A 522     -18.021   6.681 -22.552  1.00 45.80           N  
ANISOU 4351  N   GLY A 522     5547   7339   4516   -506    306   -127       N  
ATOM   4352  CA  GLY A 522     -18.380   5.877 -21.389  1.00 43.68           C  
ANISOU 4352  CA  GLY A 522     5315   7046   4235   -616    307   -162       C  
ATOM   4353  C   GLY A 522     -17.402   4.783 -20.999  1.00 43.95           C  
ANISOU 4353  C   GLY A 522     5439   6959   4298   -707    271   -179       C  
ATOM   4354  O   GLY A 522     -17.471   4.278 -19.892  1.00 44.15           O  
ANISOU 4354  O   GLY A 522     5516   6936   4321   -784    275   -194       O  
ATOM   4355  N   LYS A 523     -16.491   4.407 -21.901  1.00 45.38           N  
ANISOU 4355  N   LYS A 523     5640   7095   4505   -696    239   -174       N  
ATOM   4356  CA  LYS A 523     -15.540   3.310 -21.619  1.00 43.15           C  
ANISOU 4356  CA  LYS A 523     5441   6701   4251   -773    208   -186       C  
ATOM   4357  C   LYS A 523     -14.229   3.802 -20.998  1.00 43.91           C  
ANISOU 4357  C   LYS A 523     5622   6662   4399   -739    195   -152       C  
ATOM   4358  O   LYS A 523     -13.343   2.997 -20.656  1.00 44.73           O  
ANISOU 4358  O   LYS A 523     5796   6670   4526   -789    169   -153       O  
ATOM   4359  CB  LYS A 523     -15.279   2.474 -22.878  1.00 42.35           C  
ANISOU 4359  CB  LYS A 523     5317   6623   4148   -794    183   -207       C  
ATOM   4360  CG  LYS A 523     -16.522   1.748 -23.375  1.00 42.32           C  
ANISOU 4360  CG  LYS A 523     5238   6753   4089   -859    196   -254       C  
ATOM   4361  CD  LYS A 523     -16.248   0.834 -24.544  1.00 41.19           C  
ANISOU 4361  CD  LYS A 523     5079   6629   3942   -896    177   -285       C  
ATOM   4362  CE  LYS A 523     -17.534   0.115 -24.921  1.00 43.78           C  
ANISOU 4362  CE  LYS A 523     5328   7097   4206   -976    196   -342       C  
ATOM   4363  NZ  LYS A 523     -17.420  -0.682 -26.164  1.00 42.40           N  
ANISOU 4363  NZ  LYS A 523     5123   6967   4018  -1015    185   -381       N  
ATOM   4364  N   TYR A 524     -14.113   5.118 -20.840  1.00 41.22           N  
ANISOU 4364  N   TYR A 524     5273   6315   4073   -655    217   -124       N  
ATOM   4365  CA  TYR A 524     -12.926   5.708 -20.242  1.00 41.66           C  
ANISOU 4365  CA  TYR A 524     5399   6257   4171   -628    213   -101       C  
ATOM   4366  C   TYR A 524     -12.773   5.201 -18.829  1.00 42.42           C  
ANISOU 4366  C   TYR A 524     5559   6293   4263   -705    208   -109       C  
ATOM   4367  O   TYR A 524     -13.763   5.081 -18.105  1.00 43.81           O  
ANISOU 4367  O   TYR A 524     5720   6520   4406   -747    231   -124       O  
ATOM   4368  CB  TYR A 524     -13.042   7.231 -20.221  1.00 41.61           C  
ANISOU 4368  CB  TYR A 524     5373   6260   4176   -535    255    -77       C  
ATOM   4369  CG  TYR A 524     -11.868   7.912 -19.569  1.00 40.66           C  
ANISOU 4369  CG  TYR A 524     5322   6031   4096   -517    259    -63       C  
ATOM   4370  CD1 TYR A 524     -10.646   8.031 -20.242  1.00 39.67           C  
ANISOU 4370  CD1 TYR A 524     5224   5838   4009   -484    236    -51       C  
ATOM   4371  CD2 TYR A 524     -11.968   8.430 -18.286  1.00 40.48           C  
ANISOU 4371  CD2 TYR A 524     5334   5976   4069   -539    288    -68       C  
ATOM   4372  CE1 TYR A 524      -9.560   8.646 -19.649  1.00 39.93           C  
ANISOU 4372  CE1 TYR A 524     5314   5782   4074   -475    241    -45       C  
ATOM   4373  CE2 TYR A 524     -10.884   9.049 -17.677  1.00 40.97           C  
ANISOU 4373  CE2 TYR A 524     5455   5950   4162   -533    293    -64       C  
ATOM   4374  CZ  TYR A 524      -9.683   9.157 -18.366  1.00 40.85           C  
ANISOU 4374  CZ  TYR A 524     5462   5875   4183   -502    270    -54       C  
ATOM   4375  OH  TYR A 524      -8.602   9.761 -17.772  1.00 41.13           O  
ANISOU 4375  OH  TYR A 524     5549   5834   4245   -502    277    -56       O  
ATOM   4376  N   ARG A 525     -11.543   4.898 -18.424  1.00 43.03           N  
ANISOU 4376  N   ARG A 525     5706   6271   4370   -722    179    -98       N  
ATOM   4377  CA  ARG A 525     -11.299   4.521 -17.025  1.00 43.00           C  
ANISOU 4377  CA  ARG A 525     5765   6215   4358   -784    175    -98       C  
ATOM   4378  C   ARG A 525     -10.464   5.596 -16.345  1.00 41.70           C  
ANISOU 4378  C   ARG A 525     5634   5994   4214   -746    184    -85       C  
ATOM   4379  O   ARG A 525     -10.928   6.280 -15.439  1.00 44.04           O  
ANISOU 4379  O   ARG A 525     5934   6304   4494   -752    218    -90       O  
ATOM   4380  CB  ARG A 525     -10.612   3.150 -16.897  1.00 43.80           C  
ANISOU 4380  CB  ARG A 525     5920   6255   4464   -845    136    -95       C  
ATOM   4381  CG  ARG A 525     -11.010   2.097 -17.921  1.00 48.69           C  
ANISOU 4381  CG  ARG A 525     6515   6907   5078   -874    127   -112       C  
ATOM   4382  CD  ARG A 525     -12.224   1.290 -17.511  1.00 52.70           C  
ANISOU 4382  CD  ARG A 525     7009   7468   5543   -954    149   -138       C  
ATOM   4383  NE  ARG A 525     -11.885   0.151 -16.654  1.00 59.67           N  
ANISOU 4383  NE  ARG A 525     7967   8281   6421  -1027    140   -132       N  
ATOM   4384  CZ  ARG A 525     -12.029  -1.135 -16.991  1.00 57.50           C  
ANISOU 4384  CZ  ARG A 525     7714   7989   6141  -1089    142   -148       C  
ATOM   4385  NH1 ARG A 525     -12.496  -1.478 -18.185  1.00 53.88           N  
ANISOU 4385  NH1 ARG A 525     7204   7586   5680  -1097    148   -178       N  
ATOM   4386  NH2 ARG A 525     -11.703  -2.083 -16.119  1.00 56.18           N  
ANISOU 4386  NH2 ARG A 525     7623   7751   5969  -1145    142   -133       N  
ATOM   4387  N   LYS A 526      -9.228   5.736 -16.803  1.00 40.95           N  
ANISOU 4387  N   LYS A 526     5564   5839   4154   -713    159    -72       N  
ATOM   4388  CA  LYS A 526      -8.295   6.713 -16.296  1.00 38.63           C  
ANISOU 4388  CA  LYS A 526     5301   5493   3882   -684    168    -66       C  
ATOM   4389  C   LYS A 526      -7.006   6.597 -17.091  1.00 36.88           C  
ANISOU 4389  C   LYS A 526     5095   5219   3698   -652    134    -56       C  
ATOM   4390  O   LYS A 526      -6.343   5.552 -17.063  1.00 34.85           O  
ANISOU 4390  O   LYS A 526     4867   4927   3444   -684     91    -48       O  
ATOM   4391  CB  LYS A 526      -8.001   6.476 -14.806  1.00 41.19           C  
ANISOU 4391  CB  LYS A 526     5677   5789   4185   -744    160    -69       C  
ATOM   4392  CG  LYS A 526      -6.926   7.401 -14.243  1.00 41.65           C  
ANISOU 4392  CG  LYS A 526     5764   5801   4259   -729    167    -72       C  
ATOM   4393  CD  LYS A 526      -6.590   7.078 -12.792  1.00 43.36           C  
ANISOU 4393  CD  LYS A 526     6025   6004   4443   -791    153    -74       C  
ATOM   4394  CE  LYS A 526      -5.457   7.960 -12.284  1.00 43.23           C  
ANISOU 4394  CE  LYS A 526     6031   5955   4437   -783    158    -85       C  
ATOM   4395  NZ  LYS A 526      -4.976   7.501 -10.951  1.00 46.45           N  
ANISOU 4395  NZ  LYS A 526     6478   6362   4808   -842    132    -83       N  
ATOM   4396  N   VAL A 527      -6.651   7.684 -17.776  1.00 35.50           N  
ANISOU 4396  N   VAL A 527     4902   5036   3551   -586    160    -54       N  
ATOM   4397  CA  VAL A 527      -5.416   7.771 -18.535  1.00 32.58           C  
ANISOU 4397  CA  VAL A 527     4543   4616   3216   -552    136    -47       C  
ATOM   4398  C   VAL A 527      -4.564   8.921 -17.989  1.00 31.78           C  
ANISOU 4398  C   VAL A 527     4469   4472   3135   -535    164    -55       C  
ATOM   4399  O   VAL A 527      -4.993  10.067 -18.009  1.00 33.55           O  
ANISOU 4399  O   VAL A 527     4681   4703   3363   -498    220    -59       O  
ATOM   4400  CB  VAL A 527      -5.692   8.027 -20.035  1.00 32.60           C  
ANISOU 4400  CB  VAL A 527     4501   4650   3236   -489    147    -38       C  
ATOM   4401  CG1 VAL A 527      -4.377   8.244 -20.796  1.00 33.17           C  
ANISOU 4401  CG1 VAL A 527     4586   4668   3346   -453    130    -33       C  
ATOM   4402  CG2 VAL A 527      -6.468   6.864 -20.645  1.00 33.35           C  
ANISOU 4402  CG2 VAL A 527     4565   4796   3309   -515    121    -40       C  
ATOM   4403  N   THR A 528      -3.353   8.625 -17.540  1.00 28.35           N  
ANISOU 4403  N   THR A 528     4068   3992   2709   -562    129    -58       N  
ATOM   4404  CA  THR A 528      -2.451   9.669 -17.150  1.00 29.73           C  
ANISOU 4404  CA  THR A 528     4263   4133   2900   -554    154    -74       C  
ATOM   4405  C   THR A 528      -1.455   9.984 -18.250  1.00 29.61           C  
ANISOU 4405  C   THR A 528     4241   4083   2923   -508    149    -72       C  
ATOM   4406  O   THR A 528      -1.183   9.158 -19.102  1.00 29.85           O  
ANISOU 4406  O   THR A 528     4261   4112   2967   -494    109    -58       O  
ATOM   4407  CB  THR A 528      -1.643   9.284 -15.931  1.00 29.55           C  
ANISOU 4407  CB  THR A 528     4273   4098   2856   -611    122    -83       C  
ATOM   4408  OG1 THR A 528      -0.749   8.248 -16.311  1.00 29.11           O  
ANISOU 4408  OG1 THR A 528     4224   4024   2810   -613     61    -66       O  
ATOM   4409  CG2 THR A 528      -2.566   8.829 -14.767  1.00 29.48           C  
ANISOU 4409  CG2 THR A 528     4276   4121   2803   -663    122    -82       C  
ATOM   4410  N   PHE A 529      -0.920  11.199 -18.210  1.00 29.37           N  
ANISOU 4410  N   PHE A 529     4220   4025   2912   -489    197    -90       N  
ATOM   4411  CA  PHE A 529       0.207  11.592 -19.036  1.00 29.87           C  
ANISOU 4411  CA  PHE A 529     4285   4051   3011   -458    197    -95       C  
ATOM   4412  C   PHE A 529       1.390  10.638 -18.832  1.00 31.00           C  
ANISOU 4412  C   PHE A 529     4438   4183   3155   -491    128    -96       C  
ATOM   4413  O   PHE A 529       2.056  10.238 -19.798  1.00 30.48           O  
ANISOU 4413  O   PHE A 529     4363   4103   3115   -464     99    -87       O  
ATOM   4414  CB  PHE A 529       0.634  13.024 -18.701  1.00 27.42           C  
ANISOU 4414  CB  PHE A 529     3995   3708   2716   -455    268   -124       C  
ATOM   4415  CG  PHE A 529       1.757  13.539 -19.565  1.00 26.65           C  
ANISOU 4415  CG  PHE A 529     3900   3570   2654   -427    280   -133       C  
ATOM   4416  CD1 PHE A 529       1.508  13.988 -20.861  1.00 25.43           C  
ANISOU 4416  CD1 PHE A 529     3732   3402   2526   -358    314   -112       C  
ATOM   4417  CD2 PHE A 529       3.075  13.554 -19.093  1.00 26.25           C  
ANISOU 4417  CD2 PHE A 529     3862   3502   2607   -470    258   -163       C  
ATOM   4418  CE1 PHE A 529       2.539  14.469 -21.657  1.00 24.74           C  
ANISOU 4418  CE1 PHE A 529     3651   3276   2472   -335    330   -121       C  
ATOM   4419  CE2 PHE A 529       4.113  14.030 -19.897  1.00 26.19           C  
ANISOU 4419  CE2 PHE A 529     3855   3462   2633   -449    273   -175       C  
ATOM   4420  CZ  PHE A 529       3.840  14.485 -21.179  1.00 24.86           C  
ANISOU 4420  CZ  PHE A 529     3680   3271   2494   -382    310   -154       C  
ATOM   4421  N   GLN A 530       1.643  10.294 -17.574  1.00 32.44           N  
ANISOU 4421  N   GLN A 530     4639   4378   3307   -546    104   -105       N  
ATOM   4422  CA  GLN A 530       2.710   9.363 -17.210  1.00 35.48           C  
ANISOU 4422  CA  GLN A 530     5033   4764   3685   -571     39    -99       C  
ATOM   4423  C   GLN A 530       2.558   8.014 -17.935  1.00 34.05           C  
ANISOU 4423  C   GLN A 530     4846   4579   3511   -554    -11    -66       C  
ATOM   4424  O   GLN A 530       3.529   7.497 -18.519  1.00 31.60           O  
ANISOU 4424  O   GLN A 530     4533   4251   3222   -536    -47    -58       O  
ATOM   4425  CB  GLN A 530       2.752   9.152 -15.686  1.00 37.60           C  
ANISOU 4425  CB  GLN A 530     5319   5059   3907   -628     24   -105       C  
ATOM   4426  CG  GLN A 530       3.191  10.376 -14.875  1.00 43.60           C  
ANISOU 4426  CG  GLN A 530     6085   5824   4654   -660     68   -148       C  
ATOM   4427  CD  GLN A 530       2.212  11.572 -14.937  1.00 45.84           C  
ANISOU 4427  CD  GLN A 530     6371   6096   4948   -649    150   -169       C  
ATOM   4428  OE1 GLN A 530       0.982  11.412 -14.829  1.00 42.75           O  
ANISOU 4428  OE1 GLN A 530     5978   5718   4544   -644    167   -153       O  
ATOM   4429  NE2 GLN A 530       2.767  12.779 -15.097  1.00 45.90           N  
ANISOU 4429  NE2 GLN A 530     6383   6078   4976   -646    207   -205       N  
ATOM   4430  N   CYS A 531       1.346   7.461 -17.919  1.00 32.16           N  
ANISOU 4430  N   CYS A 531     4605   4358   3254   -563     -7    -51       N  
ATOM   4431  CA  CYS A 531       1.106   6.174 -18.567  1.00 32.16           C  
ANISOU 4431  CA  CYS A 531     4604   4355   3259   -559    -44    -28       C  
ATOM   4432  C   CYS A 531       1.431   6.221 -20.084  1.00 30.93           C  
ANISOU 4432  C   CYS A 531     4425   4184   3142   -510    -44    -28       C  
ATOM   4433  O   CYS A 531       2.137   5.343 -20.617  1.00 29.33           O  
ANISOU 4433  O   CYS A 531     4227   3958   2956   -502    -81    -18       O  
ATOM   4434  CB  CYS A 531      -0.327   5.699 -18.327  1.00 33.86           C  
ANISOU 4434  CB  CYS A 531     4816   4600   3446   -585    -29    -23       C  
ATOM   4435  SG  CYS A 531      -0.683   4.070 -19.063  1.00 40.50           S  
ANISOU 4435  SG  CYS A 531     5662   5436   4291   -598    -62     -6       S  
ATOM   4436  N   LEU A 532       0.936   7.265 -20.755  1.00 29.20           N  
ANISOU 4436  N   LEU A 532     4181   3976   2934   -474      0    -38       N  
ATOM   4437  CA  LEU A 532       1.193   7.477 -22.153  1.00 27.22           C  
ANISOU 4437  CA  LEU A 532     3909   3720   2714   -425      7    -36       C  
ATOM   4438  C   LEU A 532       2.675   7.642 -22.442  1.00 27.68           C  
ANISOU 4438  C   LEU A 532     3976   3739   2802   -411    -10    -43       C  
ATOM   4439  O   LEU A 532       3.210   7.082 -23.423  1.00 27.50           O  
ANISOU 4439  O   LEU A 532     3944   3702   2801   -390    -35    -37       O  
ATOM   4440  CB  LEU A 532       0.420   8.692 -22.650  1.00 29.22           C  
ANISOU 4440  CB  LEU A 532     4140   3993   2968   -382     66    -37       C  
ATOM   4441  CG  LEU A 532      -1.102   8.538 -22.780  1.00 28.86           C  
ANISOU 4441  CG  LEU A 532     4067   4004   2894   -378     85    -28       C  
ATOM   4442  CD1 LEU A 532      -1.764   9.894 -22.940  1.00 28.65           C  
ANISOU 4442  CD1 LEU A 532     4024   3994   2866   -329    151    -24       C  
ATOM   4443  CD2 LEU A 532      -1.462   7.610 -23.940  1.00 29.19           C  
ANISOU 4443  CD2 LEU A 532     4079   4077   2934   -368     58    -21       C  
ATOM   4444  N   LYS A 533       3.363   8.391 -21.591  1.00 27.09           N  
ANISOU 4444  N   LYS A 533     3917   3650   2726   -428      3    -59       N  
ATOM   4445  CA  LYS A 533       4.771   8.619 -21.805  1.00 26.35           C  
ANISOU 4445  CA  LYS A 533     3824   3530   2655   -421    -10    -72       C  
ATOM   4446  C   LYS A 533       5.536   7.311 -21.779  1.00 25.68           C  
ANISOU 4446  C   LYS A 533     3744   3439   2572   -431    -74    -57       C  
ATOM   4447  O   LYS A 533       6.445   7.106 -22.583  1.00 24.29           O  
ANISOU 4447  O   LYS A 533     3560   3245   2425   -406    -92    -58       O  
ATOM   4448  CB  LYS A 533       5.303   9.553 -20.760  1.00 28.64           C  
ANISOU 4448  CB  LYS A 533     4127   3820   2934   -452     15    -99       C  
ATOM   4449  CG  LYS A 533       6.564  10.284 -21.159  1.00 31.37           C  
ANISOU 4449  CG  LYS A 533     4468   4143   3306   -443     31   -125       C  
ATOM   4450  CD  LYS A 533       6.556  11.682 -20.573  1.00 30.89           C  
ANISOU 4450  CD  LYS A 533     4419   4074   3241   -464     99   -160       C  
ATOM   4451  CE  LYS A 533       6.655  11.639 -19.053  1.00 33.01           C  
ANISOU 4451  CE  LYS A 533     4697   4373   3469   -524     86   -179       C  
ATOM   4452  NZ  LYS A 533       8.068  11.758 -18.598  1.00 34.41           N  
ANISOU 4452  NZ  LYS A 533     4867   4565   3640   -558     65   -210       N  
ATOM   4453  N   SER A 534       5.149   6.419 -20.871  1.00 25.92           N  
ANISOU 4453  N   SER A 534     3792   3483   2574   -463   -103    -41       N  
ATOM   4454  CA  SER A 534       5.783   5.089 -20.754  1.00 27.18           C  
ANISOU 4454  CA  SER A 534     3963   3629   2732   -467   -156    -18       C  
ATOM   4455  C   SER A 534       5.550   4.193 -21.959  1.00 27.58           C  
ANISOU 4455  C   SER A 534     4010   3660   2807   -444   -167     -6       C  
ATOM   4456  O   SER A 534       6.446   3.483 -22.379  1.00 29.26           O  
ANISOU 4456  O   SER A 534     4226   3850   3040   -426   -197      3       O  
ATOM   4457  CB  SER A 534       5.286   4.350 -19.510  1.00 26.81           C  
ANISOU 4457  CB  SER A 534     3943   3597   2645   -506   -174      2       C  
ATOM   4458  OG  SER A 534       5.731   4.996 -18.361  1.00 28.85           O  
ANISOU 4458  OG  SER A 534     4205   3881   2877   -530   -173     -9       O  
ATOM   4459  N   ILE A 535       4.318   4.167 -22.455  1.00 28.28           N  
ANISOU 4459  N   ILE A 535     4090   3763   2889   -447   -142     -7       N  
ATOM   4460  CA  ILE A 535       3.977   3.416 -23.670  1.00 27.70           C  
ANISOU 4460  CA  ILE A 535     4006   3685   2834   -433   -146     -6       C  
ATOM   4461  C   ILE A 535       4.859   3.886 -24.852  1.00 28.26           C  
ANISOU 4461  C   ILE A 535     4056   3740   2940   -389   -144    -16       C  
ATOM   4462  O   ILE A 535       5.447   3.056 -25.591  1.00 27.65           O  
ANISOU 4462  O   ILE A 535     3981   3639   2885   -377   -165    -14       O  
ATOM   4463  CB  ILE A 535       2.456   3.546 -23.951  1.00 27.42           C  
ANISOU 4463  CB  ILE A 535     3952   3691   2776   -445   -116    -12       C  
ATOM   4464  CG1 ILE A 535       1.676   2.800 -22.852  1.00 27.37           C  
ANISOU 4464  CG1 ILE A 535     3970   3693   2736   -496   -120     -4       C  
ATOM   4465  CG2 ILE A 535       2.084   3.054 -25.343  1.00 27.69           C  
ANISOU 4465  CG2 ILE A 535     3961   3737   2820   -430   -113    -20       C  
ATOM   4466  CD1 ILE A 535       0.169   2.831 -23.006  1.00 27.78           C  
ANISOU 4466  CD1 ILE A 535     3999   3794   2760   -516    -92    -13       C  
ATOM   4467  N   ALA A 536       5.031   5.208 -24.953  1.00 26.10           N  
ANISOU 4467  N   ALA A 536     3767   3474   2673   -367   -113    -28       N  
ATOM   4468  CA  ALA A 536       5.876   5.819 -25.979  1.00 26.11           C  
ANISOU 4468  CA  ALA A 536     3753   3460   2706   -328   -102    -38       C  
ATOM   4469  C   ALA A 536       7.348   5.390 -25.846  1.00 26.13           C  
ANISOU 4469  C   ALA A 536     3763   3433   2729   -327   -138    -41       C  
ATOM   4470  O   ALA A 536       7.963   4.987 -26.827  1.00 24.23           O  
ANISOU 4470  O   ALA A 536     3514   3177   2516   -303   -150    -43       O  
ATOM   4471  CB  ALA A 536       5.758   7.352 -25.934  1.00 24.70           C  
ANISOU 4471  CB  ALA A 536     3568   3287   2529   -310    -51    -49       C  
ATOM   4472  N   TRP A 537       7.907   5.486 -24.635  1.00 25.90           N  
ANISOU 4472  N   TRP A 537     3747   3406   2686   -351   -153    -42       N  
ATOM   4473  CA  TRP A 537       9.289   5.044 -24.411  1.00 26.90           C  
ANISOU 4473  CA  TRP A 537     3872   3522   2824   -346   -190    -42       C  
ATOM   4474  C   TRP A 537       9.445   3.587 -24.782  1.00 28.79           C  
ANISOU 4474  C   TRP A 537     4123   3741   3074   -335   -226    -18       C  
ATOM   4475  O   TRP A 537      10.497   3.163 -25.320  1.00 28.21           O  
ANISOU 4475  O   TRP A 537     4041   3650   3025   -310   -247    -17       O  
ATOM   4476  CB  TRP A 537       9.725   5.276 -22.962  1.00 25.60           C  
ANISOU 4476  CB  TRP A 537     3714   3381   2628   -377   -204    -44       C  
ATOM   4477  CG  TRP A 537      10.125   6.707 -22.687  1.00 24.64           C  
ANISOU 4477  CG  TRP A 537     3582   3274   2506   -391   -167    -80       C  
ATOM   4478  CD1 TRP A 537       9.568   7.587 -21.745  1.00 24.16           C  
ANISOU 4478  CD1 TRP A 537     3529   3232   2417   -424   -133    -96       C  
ATOM   4479  CD2 TRP A 537      11.186   7.461 -23.342  1.00 23.32           C  
ANISOU 4479  CD2 TRP A 537     3395   3099   2366   -376   -150   -108       C  
ATOM   4480  NE1 TRP A 537      10.194   8.823 -21.800  1.00 24.36           N  
ANISOU 4480  NE1 TRP A 537     3545   3256   2453   -433    -92   -135       N  
ATOM   4481  CE2 TRP A 537      11.170   8.814 -22.740  1.00 24.08           C  
ANISOU 4481  CE2 TRP A 537     3493   3205   2450   -407    -99   -144       C  
ATOM   4482  CE3 TRP A 537      12.094   7.183 -24.359  1.00 22.88           C  
ANISOU 4482  CE3 TRP A 537     3323   3027   2344   -345   -164   -111       C  
ATOM   4483  CZ2 TRP A 537      12.053   9.805 -23.139  1.00 23.50           C  
ANISOU 4483  CZ2 TRP A 537     3408   3123   2397   -410    -63   -181       C  
ATOM   4484  CZ3 TRP A 537      12.968   8.191 -24.770  1.00 22.46           C  
ANISOU 4484  CZ3 TRP A 537     3254   2970   2310   -346   -132   -146       C  
ATOM   4485  CH2 TRP A 537      12.952   9.478 -24.166  1.00 23.83           C  
ANISOU 4485  CH2 TRP A 537     3432   3150   2471   -379    -81   -181       C  
ATOM   4486  N   ARG A 538       8.400   2.809 -24.520  1.00 28.59           N  
ANISOU 4486  N   ARG A 538     4118   3714   3030   -355   -227     -1       N  
ATOM   4487  CA  ARG A 538       8.471   1.380 -24.782  1.00 31.71           C  
ANISOU 4487  CA  ARG A 538     4534   4080   3434   -352   -249     18       C  
ATOM   4488  C   ARG A 538       8.500   1.150 -26.274  1.00 30.17           C  
ANISOU 4488  C   ARG A 538     4323   3867   3270   -330   -239      4       C  
ATOM   4489  O   ARG A 538       9.108   0.209 -26.740  1.00 30.72           O  
ANISOU 4489  O   ARG A 538     4403   3905   3362   -315   -254     11       O  
ATOM   4490  CB  ARG A 538       7.311   0.614 -24.115  1.00 31.86           C  
ANISOU 4490  CB  ARG A 538     4582   4100   3424   -390   -244     34       C  
ATOM   4491  CG  ARG A 538       7.524   0.407 -22.622  1.00 34.97           C  
ANISOU 4491  CG  ARG A 538     5000   4502   3786   -408   -263     59       C  
ATOM   4492  CD  ARG A 538       6.610  -0.673 -22.114  1.00 38.89           C  
ANISOU 4492  CD  ARG A 538     5533   4981   4259   -441   -258     80       C  
ATOM   4493  NE  ARG A 538       6.673  -0.904 -20.664  1.00 42.46           N  
ANISOU 4493  NE  ARG A 538     6012   5445   4674   -459   -272    108       N  
ATOM   4494  CZ  ARG A 538       7.100  -2.039 -20.102  1.00 42.74           C  
ANISOU 4494  CZ  ARG A 538     6085   5451   4701   -451   -290    148       C  
ATOM   4495  NH1 ARG A 538       7.578  -3.024 -20.860  1.00 43.43           N  
ANISOU 4495  NH1 ARG A 538     6190   5489   4821   -425   -292    161       N  
ATOM   4496  NH2 ARG A 538       7.065  -2.188 -18.786  1.00 39.27           N  
ANISOU 4496  NH2 ARG A 538     5669   5031   4221   -467   -301    177       N  
ATOM   4497  N   ALA A 539       7.835   2.030 -27.018  1.00 29.92           N  
ANISOU 4497  N   ALA A 539     4267   3861   3239   -325   -209    -14       N  
ATOM   4498  CA  ALA A 539       7.704   1.856 -28.459  1.00 27.53           C  
ANISOU 4498  CA  ALA A 539     3946   3557   2956   -306   -197    -28       C  
ATOM   4499  C   ALA A 539       9.045   2.154 -29.101  1.00 28.15           C  
ANISOU 4499  C   ALA A 539     4012   3614   3068   -271   -206    -36       C  
ATOM   4500  O   ALA A 539       9.442   1.480 -30.056  1.00 30.53           O  
ANISOU 4500  O   ALA A 539     4310   3895   3392   -257   -212    -42       O  
ATOM   4501  CB  ALA A 539       6.618   2.751 -29.011  1.00 24.71           C  
ANISOU 4501  CB  ALA A 539     3562   3242   2581   -301   -164    -38       C  
ATOM   4502  N   PHE A 540       9.751   3.145 -28.553  1.00 27.22           N  
ANISOU 4502  N   PHE A 540     3887   3501   2952   -263   -203    -41       N  
ATOM   4503  CA  PHE A 540      11.070   3.502 -29.013  1.00 27.94           C  
ANISOU 4503  CA  PHE A 540     3963   3579   3072   -237   -209    -53       C  
ATOM   4504  C   PHE A 540      12.061   2.400 -28.682  1.00 30.29           C  
ANISOU 4504  C   PHE A 540     4270   3855   3382   -229   -248    -41       C  
ATOM   4505  O   PHE A 540      12.855   2.008 -29.530  1.00 32.30           O  
ANISOU 4505  O   PHE A 540     4514   4090   3665   -204   -256    -47       O  
ATOM   4506  CB  PHE A 540      11.512   4.855 -28.431  1.00 26.43           C  
ANISOU 4506  CB  PHE A 540     3763   3403   2876   -242   -188    -70       C  
ATOM   4507  CG  PHE A 540      11.117   6.036 -29.283  1.00 26.53           C  
ANISOU 4507  CG  PHE A 540     3764   3419   2895   -225   -139    -83       C  
ATOM   4508  CD1 PHE A 540      11.909   6.437 -30.353  1.00 26.48           C  
ANISOU 4508  CD1 PHE A 540     3743   3399   2918   -199   -123    -98       C  
ATOM   4509  CD2 PHE A 540       9.930   6.715 -29.054  1.00 27.36           C  
ANISOU 4509  CD2 PHE A 540     3874   3542   2979   -231   -104    -78       C  
ATOM   4510  CE1 PHE A 540      11.530   7.511 -31.169  1.00 27.32           C  
ANISOU 4510  CE1 PHE A 540     3844   3506   3029   -176    -73   -102       C  
ATOM   4511  CE2 PHE A 540       9.542   7.793 -29.865  1.00 27.61           C  
ANISOU 4511  CE2 PHE A 540     3898   3576   3016   -202    -53    -81       C  
ATOM   4512  CZ  PHE A 540      10.344   8.188 -30.923  1.00 27.06           C  
ANISOU 4512  CZ  PHE A 540     3817   3489   2972   -174    -37    -91       C  
ATOM   4513  N   LEU A 541      11.998   1.885 -27.453  1.00 32.01           N  
ANISOU 4513  N   LEU A 541     4508   4078   3576   -247   -271    -19       N  
ATOM   4514  CA  LEU A 541      12.832   0.763 -27.053  1.00 31.26           C  
ANISOU 4514  CA  LEU A 541     4425   3964   3487   -230   -305      4       C  
ATOM   4515  C   LEU A 541      12.683  -0.459 -27.948  1.00 32.77           C  
ANISOU 4515  C   LEU A 541     4635   4111   3703   -216   -303     12       C  
ATOM   4516  O   LEU A 541      13.653  -1.153 -28.221  1.00 35.86           O  
ANISOU 4516  O   LEU A 541     5028   4479   4119   -185   -318     22       O  
ATOM   4517  CB  LEU A 541      12.525   0.361 -25.627  1.00 33.32           C  
ANISOU 4517  CB  LEU A 541     4710   4237   3711   -250   -322     33       C  
ATOM   4518  CG  LEU A 541      13.077   1.257 -24.532  1.00 32.98           C  
ANISOU 4518  CG  LEU A 541     4649   4241   3640   -262   -334     27       C  
ATOM   4519  CD1 LEU A 541      12.669   0.648 -23.227  1.00 34.14           C  
ANISOU 4519  CD1 LEU A 541     4823   4399   3747   -281   -352     61       C  
ATOM   4520  CD2 LEU A 541      14.603   1.393 -24.626  1.00 33.90           C  
ANISOU 4520  CD2 LEU A 541     4733   4375   3770   -232   -357     19       C  
ATOM   4521  N   ALA A 542      11.471  -0.754 -28.382  1.00 31.36           N  
ANISOU 4521  N   ALA A 542     4471   3926   3518   -242   -280      6       N  
ATOM   4522  CA  ALA A 542      11.270  -1.971 -29.125  1.00 30.42           C  
ANISOU 4522  CA  ALA A 542     4373   3767   3416   -243   -272      7       C  
ATOM   4523  C   ALA A 542      11.932  -1.867 -30.523  1.00 29.49           C  
ANISOU 4523  C   ALA A 542     4231   3639   3334   -215   -264    -17       C  
ATOM   4524  O   ALA A 542      12.257  -2.870 -31.142  1.00 27.01           O  
ANISOU 4524  O   ALA A 542     3932   3285   3043   -206   -260    -19       O  
ATOM   4525  CB  ALA A 542       9.784  -2.295 -29.224  1.00 29.04           C  
ANISOU 4525  CB  ALA A 542     4213   3601   3219   -287   -248     -1       C  
ATOM   4526  N   VAL A 543      12.147  -0.641 -30.988  1.00 29.63           N  
ANISOU 4526  N   VAL A 543     4213   3689   3354   -204   -258    -37       N  
ATOM   4527  CA  VAL A 543      12.728  -0.411 -32.307  1.00 29.92           C  
ANISOU 4527  CA  VAL A 543     4226   3722   3419   -179   -247    -60       C  
ATOM   4528  C   VAL A 543      14.226  -0.247 -32.182  1.00 30.52           C  
ANISOU 4528  C   VAL A 543     4288   3787   3519   -146   -266    -59       C  
ATOM   4529  O   VAL A 543      14.979  -0.821 -32.942  1.00 31.58           O  
ANISOU 4529  O   VAL A 543     4418   3897   3683   -123   -268    -66       O  
ATOM   4530  CB  VAL A 543      12.150   0.861 -32.961  1.00 31.22           C  
ANISOU 4530  CB  VAL A 543     4364   3926   3572   -179   -221    -77       C  
ATOM   4531  CG1 VAL A 543      13.021   1.312 -34.118  1.00 31.43           C  
ANISOU 4531  CG1 VAL A 543     4367   3949   3626   -150   -211    -96       C  
ATOM   4532  CG2 VAL A 543      10.726   0.629 -33.424  1.00 30.37           C  
ANISOU 4532  CG2 VAL A 543     4255   3843   3438   -204   -202    -82       C  
ATOM   4533  N   LEU A 544      14.653   0.549 -31.212  1.00 30.52           N  
ANISOU 4533  N   LEU A 544     4278   3812   3505   -148   -278    -54       N  
ATOM   4534  CA  LEU A 544      16.057   0.805 -31.016  1.00 30.22           C  
ANISOU 4534  CA  LEU A 544     4216   3782   3482   -123   -296    -59       C  
ATOM   4535  C   LEU A 544      16.817  -0.491 -30.749  1.00 33.83           C  
ANISOU 4535  C   LEU A 544     4685   4214   3953    -95   -323    -33       C  
ATOM   4536  O   LEU A 544      18.005  -0.614 -31.126  1.00 33.06           O  
ANISOU 4536  O   LEU A 544     4564   4117   3880    -62   -334    -40       O  
ATOM   4537  CB  LEU A 544      16.265   1.791 -29.864  1.00 28.10           C  
ANISOU 4537  CB  LEU A 544     3936   3554   3187   -142   -301    -62       C  
ATOM   4538  CG  LEU A 544      15.767   3.236 -30.058  1.00 27.75           C  
ANISOU 4538  CG  LEU A 544     3882   3527   3134   -164   -263    -88       C  
ATOM   4539  CD1 LEU A 544      15.826   4.006 -28.734  1.00 25.05           C  
ANISOU 4539  CD1 LEU A 544     3536   3219   2760   -193   -264    -93       C  
ATOM   4540  CD2 LEU A 544      16.554   3.950 -31.154  1.00 24.82           C  
ANISOU 4540  CD2 LEU A 544     3487   3152   2792   -147   -240   -117       C  
ATOM   4541  N   LYS A 545      16.144  -1.450 -30.097  1.00 34.65           N  
ANISOU 4541  N   LYS A 545     4826   4297   4042   -104   -330     -3       N  
ATOM   4542  CA  LYS A 545      16.773  -2.737 -29.725  1.00 37.26           C  
ANISOU 4542  CA  LYS A 545     5178   4594   4382    -70   -347     31       C  
ATOM   4543  C   LYS A 545      17.201  -3.518 -30.955  1.00 37.72           C  
ANISOU 4543  C   LYS A 545     5242   4607   4484    -44   -332     19       C  
ATOM   4544  O   LYS A 545      18.072  -4.392 -30.875  1.00 37.03           O  
ANISOU 4544  O   LYS A 545     5161   4493   4415      0   -341     43       O  
ATOM   4545  CB  LYS A 545      15.815  -3.601 -28.901  1.00 37.60           C  
ANISOU 4545  CB  LYS A 545     5270   4612   4402    -91   -344     64       C  
ATOM   4546  CG  LYS A 545      15.986  -3.476 -27.400  1.00 40.98           C  
ANISOU 4546  CG  LYS A 545     5702   5076   4792    -90   -371     99       C  
ATOM   4547  CD  LYS A 545      14.734  -3.989 -26.720  1.00 43.47           C  
ANISOU 4547  CD  LYS A 545     6063   5372   5080   -127   -357    120       C  
ATOM   4548  CE  LYS A 545      15.075  -4.765 -25.477  1.00 47.91           C  
ANISOU 4548  CE  LYS A 545     6654   5933   5617   -104   -377    175       C  
ATOM   4549  NZ  LYS A 545      13.934  -5.627 -25.063  1.00 53.43           N  
ANISOU 4549  NZ  LYS A 545     7412   6589   6301   -137   -352    197       N  
ATOM   4550  N   ARG A 546      16.553  -3.222 -32.084  1.00 35.92           N  
ANISOU 4550  N   ARG A 546     5009   4372   4266    -68   -305    -15       N  
ATOM   4551  CA  ARG A 546      16.886  -3.857 -33.359  1.00 34.88           C  
ANISOU 4551  CA  ARG A 546     4878   4203   4170    -52   -286    -35       C  
ATOM   4552  C   ARG A 546      18.295  -3.520 -33.835  1.00 34.32           C  
ANISOU 4552  C   ARG A 546     4770   4142   4128    -10   -297    -47       C  
ATOM   4553  O   ARG A 546      18.801  -4.169 -34.749  1.00 33.55           O  
ANISOU 4553  O   ARG A 546     4674   4011   4062     11   -284    -60       O  
ATOM   4554  CB  ARG A 546      15.861  -3.512 -34.429  1.00 31.27           C  
ANISOU 4554  CB  ARG A 546     4416   3756   3707    -88   -257    -70       C  
ATOM   4555  CG  ARG A 546      14.531  -4.181 -34.208  1.00 32.06           C  
ANISOU 4555  CG  ARG A 546     4552   3845   3785   -132   -240    -67       C  
ATOM   4556  CD  ARG A 546      13.671  -4.102 -35.463  1.00 32.42           C  
ANISOU 4556  CD  ARG A 546     4584   3908   3824   -162   -212   -104       C  
ATOM   4557  NE  ARG A 546      14.216  -4.898 -36.556  1.00 28.87           N  
ANISOU 4557  NE  ARG A 546     4138   3422   3405   -152   -194   -128       N  
ATOM   4558  CZ  ARG A 546      13.593  -5.093 -37.713  1.00 29.81           C  
ANISOU 4558  CZ  ARG A 546     4248   3558   3519   -181   -168   -164       C  
ATOM   4559  NH1 ARG A 546      12.385  -4.560 -37.930  1.00 28.35           N  
ANISOU 4559  NH1 ARG A 546     4045   3430   3295   -216   -159   -178       N  
ATOM   4560  NH2 ARG A 546      14.161  -5.850 -38.643  1.00 28.45           N  
ANISOU 4560  NH2 ARG A 546     4084   3350   3377   -174   -149   -188       N  
ATOM   4561  N   ARG A 547      18.908  -2.499 -33.229  1.00 33.19           N  
ANISOU 4561  N   ARG A 547     4592   4047   3971     -4   -317    -49       N  
ATOM   4562  CA  ARG A 547      20.335  -2.185 -33.456  1.00 35.59           C  
ANISOU 4562  CA  ARG A 547     4854   4371   4294     31   -331    -60       C  
ATOM   4563  C   ARG A 547      21.032  -1.991 -32.125  1.00 36.62           C  
ANISOU 4563  C   ARG A 547     4965   4547   4401     45   -364    -37       C  
ATOM   4564  O   ARG A 547      21.486  -0.869 -31.807  1.00 34.64           O  
ANISOU 4564  O   ARG A 547     4678   4348   4135     29   -370    -60       O  
ATOM   4565  CB  ARG A 547      20.512  -0.902 -34.282  1.00 36.16           C  
ANISOU 4565  CB  ARG A 547     4893   4471   4372     14   -311   -102       C  
ATOM   4566  CG  ARG A 547      19.816  -0.874 -35.638  1.00 37.61           C  
ANISOU 4566  CG  ARG A 547     5087   4631   4570      1   -279   -126       C  
ATOM   4567  CD  ARG A 547      20.297   0.333 -36.457  1.00 38.52           C  
ANISOU 4567  CD  ARG A 547     5170   4770   4693     -1   -258   -159       C  
ATOM   4568  NE  ARG A 547      19.287   0.817 -37.399  1.00 38.18           N  
ANISOU 4568  NE  ARG A 547     5136   4729   4642    -19   -226   -172       N  
ATOM   4569  CZ  ARG A 547      19.135   0.361 -38.643  1.00 40.34           C  
ANISOU 4569  CZ  ARG A 547     5410   4988   4929    -14   -209   -187       C  
ATOM   4570  NH1 ARG A 547      19.933  -0.598 -39.109  1.00 41.10           N  
ANISOU 4570  NH1 ARG A 547     5504   5054   5054      7   -215   -195       N  
ATOM   4571  NH2 ARG A 547      18.185   0.865 -39.430  1.00 38.19           N  
ANISOU 4571  NH2 ARG A 547     5138   4734   4637    -28   -183   -195       N  
ATOM   4572  N   THR A 548      21.102  -3.065 -31.335  1.00 38.52           N  
ANISOU 4572  N   THR A 548     5232   4770   4634     73   -382      7       N  
ATOM   4573  CA  THR A 548      21.593  -2.982 -29.946  1.00 43.09           C  
ANISOU 4573  CA  THR A 548     5794   5402   5176     87   -417     39       C  
ATOM   4574  C   THR A 548      23.015  -2.429 -29.873  1.00 44.82           C  
ANISOU 4574  C   THR A 548     5950   5684   5395    113   -439     21       C  
ATOM   4575  O   THR A 548      23.342  -1.703 -28.945  1.00 50.95           O  
ANISOU 4575  O   THR A 548     6693   6529   6134     96   -460     16       O  
ATOM   4576  CB  THR A 548      21.528  -4.346 -29.189  1.00 44.04           C  
ANISOU 4576  CB  THR A 548     5955   5489   5288    126   -427    100       C  
ATOM   4577  OG1 THR A 548      21.752  -5.422 -30.109  1.00 48.29           O  
ANISOU 4577  OG1 THR A 548     6520   5958   5870    164   -405    108       O  
ATOM   4578  CG2 THR A 548      20.173  -4.558 -28.523  1.00 41.51           C  
ANISOU 4578  CG2 THR A 548     5686   5144   4939     84   -417    120       C  
ATOM   4579  N   GLU A 549      23.848  -2.762 -30.853  1.00 45.14           N  
ANISOU 4579  N   GLU A 549     5969   5706   5474    150   -431      7       N  
ATOM   4580  CA  GLU A 549      25.238  -2.250 -30.909  1.00 48.69           C  
ANISOU 4580  CA  GLU A 549     6352   6219   5926    173   -448    -16       C  
ATOM   4581  C   GLU A 549      25.307  -0.732 -31.122  1.00 45.19           C  
ANISOU 4581  C   GLU A 549     5875   5820   5473    116   -433    -74       C  
ATOM   4582  O   GLU A 549      26.048  -0.039 -30.447  1.00 49.65           O  
ANISOU 4582  O   GLU A 549     6392   6461   6011    103   -450    -92       O  
ATOM   4583  CB  GLU A 549      26.059  -2.986 -31.994  1.00 52.06           C  
ANISOU 4583  CB  GLU A 549     6767   6610   6400    225   -437    -20       C  
ATOM   4584  CG  GLU A 549      25.640  -2.703 -33.447  1.00 58.62           C  
ANISOU 4584  CG  GLU A 549     7615   7388   7270    198   -398    -64       C  
ATOM   4585  CD  GLU A 549      24.207  -3.148 -33.786  1.00 58.17           C  
ANISOU 4585  CD  GLU A 549     7621   7263   7216    168   -373    -54       C  
ATOM   4586  OE1 GLU A 549      23.748  -4.175 -33.242  1.00 62.66           O  
ANISOU 4586  OE1 GLU A 549     8233   7795   7780    186   -376    -12       O  
ATOM   4587  OE2 GLU A 549      23.546  -2.484 -34.617  1.00 53.80           O  
ANISOU 4587  OE2 GLU A 549     7075   6696   6668    128   -346    -89       O  
ATOM   4588  N   ILE A 550      24.530  -0.226 -32.061  1.00 41.11           N  
ANISOU 4588  N   ILE A 550     5384   5258   4977     82   -397   -102       N  
ATOM   4589  CA  ILE A 550      24.469   1.212 -32.303  1.00 39.63           C  
ANISOU 4589  CA  ILE A 550     5177   5096   4782     33   -370   -150       C  
ATOM   4590  C   ILE A 550      23.773   1.956 -31.147  1.00 39.48           C  
ANISOU 4590  C   ILE A 550     5170   5110   4721    -12   -372   -148       C  
ATOM   4591  O   ILE A 550      24.249   2.976 -30.682  1.00 38.79           O  
ANISOU 4591  O   ILE A 550     5052   5073   4614    -45   -365   -182       O  
ATOM   4592  CB  ILE A 550      23.786   1.507 -33.665  1.00 37.85           C  
ANISOU 4592  CB  ILE A 550     4977   4817   4585     20   -329   -171       C  
ATOM   4593  CG1 ILE A 550      24.813   1.343 -34.809  1.00 38.76           C  
ANISOU 4593  CG1 ILE A 550     5064   4923   4738     48   -319   -196       C  
ATOM   4594  CG2 ILE A 550      23.211   2.901 -33.688  1.00 37.18           C  
ANISOU 4594  CG2 ILE A 550     4897   4743   4485    -26   -294   -200       C  
ATOM   4595  CD1 ILE A 550      24.264   0.753 -36.098  1.00 34.85           C  
ANISOU 4595  CD1 ILE A 550     4598   4371   4272     61   -296   -196       C  
ATOM   4596  N   TYR A 551      22.670   1.404 -30.657  1.00 38.51           N  
ANISOU 4596  N   TYR A 551     5091   4958   4582    -16   -378   -112       N  
ATOM   4597  CA  TYR A 551      21.795   2.137 -29.757  1.00 36.18           C  
ANISOU 4597  CA  TYR A 551     4813   4682   4251    -61   -370   -114       C  
ATOM   4598  C   TYR A 551      21.938   1.748 -28.260  1.00 36.99           C  
ANISOU 4598  C   TYR A 551     4911   4832   4310    -61   -409    -83       C  
ATOM   4599  O   TYR A 551      21.202   2.254 -27.402  1.00 36.07           O  
ANISOU 4599  O   TYR A 551     4810   4734   4160   -100   -404    -82       O  
ATOM   4600  CB  TYR A 551      20.362   1.949 -30.217  1.00 33.41           C  
ANISOU 4600  CB  TYR A 551     4509   4279   3905    -74   -347   -100       C  
ATOM   4601  CG  TYR A 551      19.992   2.664 -31.502  1.00 30.82           C  
ANISOU 4601  CG  TYR A 551     4183   3924   3602    -83   -305   -130       C  
ATOM   4602  CD1 TYR A 551      20.291   4.021 -31.695  1.00 30.86           C  
ANISOU 4602  CD1 TYR A 551     4168   3948   3606   -106   -272   -167       C  
ATOM   4603  CD2 TYR A 551      19.253   2.019 -32.470  1.00 28.79           C  
ANISOU 4603  CD2 TYR A 551     3949   3625   3362    -71   -292   -121       C  
ATOM   4604  CE1 TYR A 551      19.912   4.679 -32.859  1.00 29.21           C  
ANISOU 4604  CE1 TYR A 551     3966   3714   3416   -106   -229   -185       C  
ATOM   4605  CE2 TYR A 551      18.861   2.664 -33.611  1.00 29.21           C  
ANISOU 4605  CE2 TYR A 551     4001   3666   3429    -75   -256   -142       C  
ATOM   4606  CZ  TYR A 551      19.188   3.996 -33.802  1.00 30.16           C  
ANISOU 4606  CZ  TYR A 551     4106   3804   3550    -87   -225   -170       C  
ATOM   4607  OH  TYR A 551      18.759   4.624 -34.951  1.00 31.29           O  
ANISOU 4607  OH  TYR A 551     4251   3935   3702    -83   -185   -182       O  
ATOM   4608  N   LYS A 552      22.885   0.855 -27.981  1.00 37.82           N  
ANISOU 4608  N   LYS A 552     4994   4961   4414    -14   -444    -55       N  
ATOM   4609  CA  LYS A 552      23.264   0.436 -26.633  1.00 41.02           C  
ANISOU 4609  CA  LYS A 552     5384   5426   4774      0   -484    -20       C  
ATOM   4610  C   LYS A 552      23.154   1.525 -25.568  1.00 37.78           C  
ANISOU 4610  C   LYS A 552     4954   5085   4315    -58   -485    -47       C  
ATOM   4611  O   LYS A 552      22.405   1.383 -24.592  1.00 37.54           O  
ANISOU 4611  O   LYS A 552     4951   5064   4247    -76   -494    -21       O  
ATOM   4612  CB  LYS A 552      24.706  -0.095 -26.658  1.00 46.40           C  
ANISOU 4612  CB  LYS A 552     6014   6155   5459     56   -514     -8       C  
ATOM   4613  CG  LYS A 552      25.230  -0.591 -25.315  1.00 53.36           C  
ANISOU 4613  CG  LYS A 552     6871   7114   6287     85   -559     35       C  
ATOM   4614  CD  LYS A 552      25.221  -2.109 -25.229  1.00 57.65           C  
ANISOU 4614  CD  LYS A 552     7450   7611   6841    161   -574    109       C  
ATOM   4615  CE  LYS A 552      25.826  -2.588 -23.913  1.00 63.10           C  
ANISOU 4615  CE  LYS A 552     8112   8387   7473    202   -618    162       C  
ATOM   4616  NZ  LYS A 552      24.992  -2.201 -22.734  1.00 62.62           N  
ANISOU 4616  NZ  LYS A 552     8074   8360   7357    151   -626    172       N  
ATOM   4617  N   GLY A 553      23.921   2.593 -25.744  1.00 35.52           N  
ANISOU 4617  N   GLY A 553     4620   4847   4027    -89   -470   -104       N  
ATOM   4618  CA  GLY A 553      23.978   3.673 -24.764  1.00 34.65           C  
ANISOU 4618  CA  GLY A 553     4487   4806   3871   -151   -463   -143       C  
ATOM   4619  C   GLY A 553      22.632   4.359 -24.600  1.00 34.16           C  
ANISOU 4619  C   GLY A 553     4475   4698   3804   -200   -424   -154       C  
ATOM   4620  O   GLY A 553      22.271   4.772 -23.502  1.00 35.20           O  
ANISOU 4620  O   GLY A 553     4609   4871   3891   -241   -426   -159       O  
ATOM   4621  N   LEU A 554      21.895   4.480 -25.703  1.00 32.39           N  
ANISOU 4621  N   LEU A 554     4287   4394   3624   -195   -388   -157       N  
ATOM   4622  CA  LEU A 554      20.624   5.187 -25.708  1.00 31.40           C  
ANISOU 4622  CA  LEU A 554     4203   4229   3497   -232   -346   -166       C  
ATOM   4623  C   LEU A 554      19.558   4.380 -24.952  1.00 31.96           C  
ANISOU 4623  C   LEU A 554     4313   4286   3544   -227   -367   -117       C  
ATOM   4624  O   LEU A 554      18.895   4.899 -24.069  1.00 30.96           O  
ANISOU 4624  O   LEU A 554     4201   4178   3384   -267   -355   -122       O  
ATOM   4625  CB  LEU A 554      20.196   5.460 -27.140  1.00 29.77           C  
ANISOU 4625  CB  LEU A 554     4016   3957   3338   -217   -306   -177       C  
ATOM   4626  CG  LEU A 554      18.943   6.291 -27.415  1.00 30.38           C  
ANISOU 4626  CG  LEU A 554     4128   3997   3418   -241   -255   -185       C  
ATOM   4627  CD1 LEU A 554      18.954   7.588 -26.608  1.00 29.92           C  
ANISOU 4627  CD1 LEU A 554     4065   3967   3333   -293   -218   -225       C  
ATOM   4628  CD2 LEU A 554      18.851   6.581 -28.915  1.00 28.46           C  
ANISOU 4628  CD2 LEU A 554     3889   3708   3215   -218   -219   -196       C  
ATOM   4629  N   ILE A 555      19.447   3.095 -25.293  1.00 33.19           N  
ANISOU 4629  N   ILE A 555     4487   4407   3716   -182   -394    -71       N  
ATOM   4630  CA  ILE A 555      18.622   2.139 -24.570  1.00 34.35           C  
ANISOU 4630  CA  ILE A 555     4673   4539   3840   -175   -414    -22       C  
ATOM   4631  C   ILE A 555      18.900   2.146 -23.067  1.00 35.77           C  
ANISOU 4631  C   ILE A 555     4840   4786   3964   -191   -444     -6       C  
ATOM   4632  O   ILE A 555      17.967   2.193 -22.271  1.00 39.71           O  
ANISOU 4632  O   ILE A 555     5367   5287   4431   -221   -439      7       O  
ATOM   4633  CB  ILE A 555      18.813   0.705 -25.122  1.00 33.96           C  
ANISOU 4633  CB  ILE A 555     4642   4443   3818   -122   -433     20       C  
ATOM   4634  CG1 ILE A 555      18.422   0.642 -26.602  1.00 32.00           C  
ANISOU 4634  CG1 ILE A 555     4406   4133   3617   -113   -403      1       C  
ATOM   4635  CG2 ILE A 555      18.016  -0.303 -24.306  1.00 31.56           C  
ANISOU 4635  CG2 ILE A 555     4384   4118   3488   -119   -446     72       C  
ATOM   4636  CD1 ILE A 555      18.917  -0.612 -27.301  1.00 32.11           C  
ANISOU 4636  CD1 ILE A 555     4431   4104   3665    -63   -413     26       C  
ATOM   4637  N   ASP A 556      20.175   2.105 -22.680  1.00 37.03           N  
ANISOU 4637  N   ASP A 556     4953   5010   4106   -172   -475     -8       N  
ATOM   4638  CA  ASP A 556      20.548   2.149 -21.266  1.00 36.95           C  
ANISOU 4638  CA  ASP A 556     4920   5084   4033   -186   -507      4       C  
ATOM   4639  C   ASP A 556      20.129   3.444 -20.613  1.00 36.85           C  
ANISOU 4639  C   ASP A 556     4901   5109   3988   -260   -478    -47       C  
ATOM   4640  O   ASP A 556      19.617   3.434 -19.491  1.00 38.91           O  
ANISOU 4640  O   ASP A 556     5176   5405   4201   -287   -488    -31       O  
ATOM   4641  CB  ASP A 556      22.050   1.929 -21.081  1.00 40.43           C  
ANISOU 4641  CB  ASP A 556     5299   5603   4458   -150   -544      5       C  
ATOM   4642  CG  ASP A 556      22.470   0.504 -21.407  1.00 46.16           C  
ANISOU 4642  CG  ASP A 556     6036   6298   5204    -68   -573     69       C  
ATOM   4643  OD1 ASP A 556      21.591  -0.400 -21.396  1.00 48.05           O  
ANISOU 4643  OD1 ASP A 556     6335   6468   5454    -47   -568    119       O  
ATOM   4644  OD2 ASP A 556      23.670   0.284 -21.697  1.00 49.27           O  
ANISOU 4644  OD2 ASP A 556     6380   6734   5605    -24   -595     68       O  
ATOM   4645  N   ARG A 557      20.352   4.568 -21.292  1.00 34.11           N  
ANISOU 4645  N   ARG A 557     4536   4754   3668   -292   -438   -108       N  
ATOM   4646  CA  ARG A 557      19.859   5.841 -20.772  1.00 34.99           C  
ANISOU 4646  CA  ARG A 557     4653   4882   3758   -361   -395   -159       C  
ATOM   4647  C   ARG A 557      18.335   5.798 -20.558  1.00 33.51           C  
ANISOU 4647  C   ARG A 557     4521   4641   3569   -376   -371   -135       C  
ATOM   4648  O   ARG A 557      17.841   6.296 -19.564  1.00 34.70           O  
ANISOU 4648  O   ARG A 557     4681   4823   3680   -421   -359   -148       O  
ATOM   4649  CB  ARG A 557      20.257   7.029 -21.680  1.00 34.99           C  
ANISOU 4649  CB  ARG A 557     4638   4861   3795   -388   -341   -223       C  
ATOM   4650  CG  ARG A 557      19.835   8.392 -21.142  1.00 36.64           C  
ANISOU 4650  CG  ARG A 557     4856   5079   3984   -458   -283   -278       C  
ATOM   4651  CD  ARG A 557      20.441   9.563 -21.929  1.00 38.33           C  
ANISOU 4651  CD  ARG A 557     5056   5276   4230   -487   -224   -342       C  
ATOM   4652  NE  ARG A 557      21.886   9.670 -21.735  1.00 41.41           N  
ANISOU 4652  NE  ARG A 557     5386   5744   4602   -504   -245   -381       N  
ATOM   4653  CZ  ARG A 557      22.650  10.694 -22.134  1.00 43.90           C  
ANISOU 4653  CZ  ARG A 557     5679   6068   4931   -547   -195   -449       C  
ATOM   4654  NH1 ARG A 557      22.126  11.750 -22.762  1.00 41.11           N  
ANISOU 4654  NH1 ARG A 557     5365   5642   4612   -571   -115   -481       N  
ATOM   4655  NH2 ARG A 557      23.958  10.655 -21.901  1.00 43.36           N  
ANISOU 4655  NH2 ARG A 557     5547   6086   4840   -563   -222   -483       N  
ATOM   4656  N   ILE A 558      17.597   5.183 -21.472  1.00 31.05           N  
ANISOU 4656  N   ILE A 558     4243   4255   3297   -340   -365   -104       N  
ATOM   4657  CA  ILE A 558      16.157   5.199 -21.340  1.00 30.46           C  
ANISOU 4657  CA  ILE A 558     4212   4140   3219   -357   -340    -88       C  
ATOM   4658  C   ILE A 558      15.743   4.392 -20.112  1.00 31.55           C  
ANISOU 4658  C   ILE A 558     4370   4307   3310   -363   -374    -45       C  
ATOM   4659  O   ILE A 558      14.927   4.833 -19.312  1.00 29.91           O  
ANISOU 4659  O   ILE A 558     4179   4112   3071   -403   -355    -52       O  
ATOM   4660  CB  ILE A 558      15.443   4.714 -22.620  1.00 28.70           C  
ANISOU 4660  CB  ILE A 558     4013   3847   3042   -323   -324    -70       C  
ATOM   4661  CG1 ILE A 558      15.778   5.640 -23.797  1.00 27.00           C  
ANISOU 4661  CG1 ILE A 558     3782   3608   2867   -318   -284   -110       C  
ATOM   4662  CG2 ILE A 558      13.933   4.654 -22.397  1.00 28.21           C  
ANISOU 4662  CG2 ILE A 558     3988   3761   2968   -342   -302    -54       C  
ATOM   4663  CD1 ILE A 558      15.297   5.139 -25.149  1.00 25.41           C  
ANISOU 4663  CD1 ILE A 558     3594   3354   2706   -282   -274    -95       C  
ATOM   4664  N   LYS A 559      16.361   3.230 -19.948  1.00 33.47           N  
ANISOU 4664  N   LYS A 559     4609   4560   3547   -322   -420      0       N  
ATOM   4665  CA  LYS A 559      16.037   2.346 -18.835  1.00 34.57           C  
ANISOU 4665  CA  LYS A 559     4772   4720   3641   -318   -450     50       C  
ATOM   4666  C   LYS A 559      16.459   2.923 -17.492  1.00 34.31           C  
ANISOU 4666  C   LYS A 559     4713   4777   3545   -355   -466     35       C  
ATOM   4667  O   LYS A 559      15.797   2.679 -16.481  1.00 32.55           O  
ANISOU 4667  O   LYS A 559     4515   4574   3279   -377   -471     61       O  
ATOM   4668  CB  LYS A 559      16.673   0.976 -19.030  1.00 35.88           C  
ANISOU 4668  CB  LYS A 559     4945   4870   3818   -254   -486    106       C  
ATOM   4669  CG  LYS A 559      16.116   0.223 -20.213  1.00 36.14           C  
ANISOU 4669  CG  LYS A 559     5013   4812   3905   -227   -467    121       C  
ATOM   4670  CD  LYS A 559      16.581  -1.213 -20.226  1.00 38.54           C  
ANISOU 4670  CD  LYS A 559     5339   5088   4216   -168   -492    181       C  
ATOM   4671  CE  LYS A 559      15.777  -1.993 -21.260  1.00 41.04           C  
ANISOU 4671  CE  LYS A 559     5700   5313   4579   -160   -462    189       C  
ATOM   4672  NZ  LYS A 559      16.338  -3.350 -21.466  1.00 45.82           N  
ANISOU 4672  NZ  LYS A 559     6329   5875   5203   -101   -473    240       N  
ATOM   4673  N   SER A 560      17.541   3.696 -17.467  1.00 33.60           N  
ANISOU 4673  N   SER A 560     4571   4748   3446   -368   -470     -8       N  
ATOM   4674  CA  SER A 560      17.965   4.262 -16.186  1.00 35.65           C  
ANISOU 4674  CA  SER A 560     4799   5106   3639   -413   -483    -31       C  
ATOM   4675  C   SER A 560      17.300   5.573 -15.836  1.00 35.00           C  
ANISOU 4675  C   SER A 560     4725   5026   3545   -487   -430    -93       C  
ATOM   4676  O   SER A 560      17.175   5.898 -14.648  1.00 35.77           O  
ANISOU 4676  O   SER A 560     4817   5189   3584   -532   -433   -105       O  
ATOM   4677  CB  SER A 560      19.494   4.354 -16.040  1.00 36.21           C  
ANISOU 4677  CB  SER A 560     4803   5267   3687   -399   -517    -50       C  
ATOM   4678  OG  SER A 560      20.085   5.003 -17.129  1.00 39.38           O  
ANISOU 4678  OG  SER A 560     5179   5643   4139   -400   -490   -100       O  
ATOM   4679  N   ARG A 561      16.857   6.317 -16.852  1.00 33.50           N  
ANISOU 4679  N   ARG A 561     4550   4766   3410   -496   -379   -129       N  
ATOM   4680  CA  ARG A 561      16.395   7.694 -16.646  1.00 34.11           C  
ANISOU 4680  CA  ARG A 561     4635   4840   3485   -559   -316   -192       C  
ATOM   4681  C   ARG A 561      14.891   7.846 -16.747  1.00 33.58           C  
ANISOU 4681  C   ARG A 561     4617   4708   3433   -565   -277   -178       C  
ATOM   4682  O   ARG A 561      14.329   8.755 -16.144  1.00 32.55           O  
ANISOU 4682  O   ARG A 561     4498   4584   3282   -615   -232   -214       O  
ATOM   4683  CB  ARG A 561      17.070   8.663 -17.623  1.00 35.75           C  
ANISOU 4683  CB  ARG A 561     4822   5026   3736   -567   -272   -248       C  
ATOM   4684  CG  ARG A 561      18.494   9.069 -17.251  1.00 37.80           C  
ANISOU 4684  CG  ARG A 561     5025   5370   3968   -597   -287   -296       C  
ATOM   4685  CD  ARG A 561      18.965  10.262 -18.084  1.00 38.52           C  
ANISOU 4685  CD  ARG A 561     5107   5431   4099   -626   -222   -363       C  
ATOM   4686  NE  ARG A 561      20.427  10.405 -18.066  1.00 41.81           N  
ANISOU 4686  NE  ARG A 561     5462   5923   4499   -642   -242   -404       N  
ATOM   4687  CZ  ARG A 561      21.107  11.413 -18.627  1.00 43.37           C  
ANISOU 4687  CZ  ARG A 561     5642   6114   4720   -679   -187   -471       C  
ATOM   4688  NH1 ARG A 561      20.474  12.408 -19.272  1.00 41.74           N  
ANISOU 4688  NH1 ARG A 561     5480   5822   4557   -698   -105   -501       N  
ATOM   4689  NH2 ARG A 561      22.428  11.429 -18.538  1.00 42.14           N  
ANISOU 4689  NH2 ARG A 561     5425   6041   4545   -695   -212   -508       N  
ATOM   4690  N   GLU A 562      14.242   6.984 -17.528  1.00 32.45           N  
ANISOU 4690  N   GLU A 562     4500   4504   3324   -518   -289   -130       N  
ATOM   4691  CA  GLU A 562      12.796   7.083 -17.722  1.00 32.31           C  
ANISOU 4691  CA  GLU A 562     4520   4436   3318   -522   -254   -118       C  
ATOM   4692  C   GLU A 562      12.045   5.986 -17.012  1.00 32.93           C  
ANISOU 4692  C   GLU A 562     4626   4518   3367   -519   -286    -67       C  
ATOM   4693  O   GLU A 562      12.554   4.898 -16.791  1.00 31.90           O  
ANISOU 4693  O   GLU A 562     4495   4400   3223   -491   -335    -25       O  
ATOM   4694  CB  GLU A 562      12.396   7.051 -19.212  1.00 32.09           C  
ANISOU 4694  CB  GLU A 562     4500   4342   3348   -481   -230   -113       C  
ATOM   4695  CG  GLU A 562      13.084   8.084 -20.102  1.00 33.27           C  
ANISOU 4695  CG  GLU A 562     4629   4476   3534   -476   -191   -157       C  
ATOM   4696  CD  GLU A 562      13.064   9.475 -19.507  1.00 31.53           C  
ANISOU 4696  CD  GLU A 562     4409   4271   3297   -525   -134   -209       C  
ATOM   4697  OE1 GLU A 562      11.983   9.945 -19.079  1.00 31.77           O  
ANISOU 4697  OE1 GLU A 562     4463   4290   3315   -545    -96   -211       O  
ATOM   4698  OE2 GLU A 562      14.132  10.081 -19.462  1.00 31.73           O  
ANISOU 4698  OE2 GLU A 562     4410   4321   3323   -547   -124   -250       O  
ATOM   4699  N   LYS A 563      10.801   6.308 -16.696  1.00 33.62           N  
ANISOU 4699  N   LYS A 563     4738   4590   3443   -544   -252    -69       N  
ATOM   4700  CA  LYS A 563       9.849   5.408 -16.128  1.00 33.96           C  
ANISOU 4700  CA  LYS A 563     4812   4628   3461   -550   -267    -28       C  
ATOM   4701  C   LYS A 563       9.216   4.575 -17.251  1.00 33.70           C  
ANISOU 4701  C   LYS A 563     4796   4539   3469   -514   -268      0       C  
ATOM   4702  O   LYS A 563       8.557   5.122 -18.133  1.00 34.02           O  
ANISOU 4702  O   LYS A 563     4833   4551   3540   -507   -230    -19       O  
ATOM   4703  CB  LYS A 563       8.794   6.267 -15.402  1.00 34.23           C  
ANISOU 4703  CB  LYS A 563     4859   4675   3470   -596   -221    -53       C  
ATOM   4704  CG  LYS A 563       7.553   5.543 -14.926  1.00 35.57           C  
ANISOU 4704  CG  LYS A 563     5059   4836   3617   -610   -221    -21       C  
ATOM   4705  CD  LYS A 563       7.873   4.569 -13.810  1.00 35.47           C  
ANISOU 4705  CD  LYS A 563     5063   4858   3556   -621   -267     18       C  
ATOM   4706  CE  LYS A 563       7.477   5.150 -12.463  1.00 37.65           C  
ANISOU 4706  CE  LYS A 563     5345   5183   3777   -675   -251      0       C  
ATOM   4707  NZ  LYS A 563       7.515   4.121 -11.376  1.00 35.76           N  
ANISOU 4707  NZ  LYS A 563     5128   4975   3483   -684   -290     49       N  
ATOM   4708  N   LEU A 564       9.402   3.256 -17.202  1.00 35.96           N  
ANISOU 4708  N   LEU A 564     5099   4810   3751   -492   -306     45       N  
ATOM   4709  CA  LEU A 564       8.885   2.329 -18.247  1.00 36.60           C  
ANISOU 4709  CA  LEU A 564     5198   4838   3868   -467   -304     66       C  
ATOM   4710  C   LEU A 564       7.716   1.435 -17.780  1.00 36.85           C  
ANISOU 4710  C   LEU A 564     5268   4853   3877   -491   -297     95       C  
ATOM   4711  O   LEU A 564       7.065   0.757 -18.593  1.00 36.74           O  
ANISOU 4711  O   LEU A 564     5268   4802   3887   -486   -285    101       O  
ATOM   4712  CB  LEU A 564      10.018   1.445 -18.783  1.00 38.08           C  
ANISOU 4712  CB  LEU A 564     5382   5005   4080   -421   -338     90       C  
ATOM   4713  CG  LEU A 564      11.235   2.139 -19.416  1.00 39.43           C  
ANISOU 4713  CG  LEU A 564     5514   5189   4279   -395   -345     62       C  
ATOM   4714  CD1 LEU A 564      12.335   1.121 -19.641  1.00 39.53           C  
ANISOU 4714  CD1 LEU A 564     5523   5190   4304   -349   -383     94       C  
ATOM   4715  CD2 LEU A 564      10.857   2.813 -20.728  1.00 38.03           C  
ANISOU 4715  CD2 LEU A 564     5322   4982   4144   -388   -310     28       C  
ATOM   4716  N   THR A 565       7.466   1.422 -16.476  1.00 37.30           N  
ANISOU 4716  N   THR A 565     5341   4942   3886   -522   -303    109       N  
ATOM   4717  CA  THR A 565       6.371   0.640 -15.901  1.00 37.08           C  
ANISOU 4717  CA  THR A 565     5351   4903   3832   -552   -292    135       C  
ATOM   4718  C   THR A 565       5.129   1.529 -15.805  1.00 38.08           C  
ANISOU 4718  C   THR A 565     5469   5049   3949   -590   -251    100       C  
ATOM   4719  O   THR A 565       5.240   2.718 -15.533  1.00 39.47           O  
ANISOU 4719  O   THR A 565     5622   5256   4119   -600   -236     68       O  
ATOM   4720  CB  THR A 565       6.743   0.102 -14.509  1.00 36.00           C  
ANISOU 4720  CB  THR A 565     5239   4794   3643   -562   -319    174       C  
ATOM   4721  OG1 THR A 565       7.136   1.190 -13.666  1.00 34.08           O  
ANISOU 4721  OG1 THR A 565     4969   4612   3366   -583   -322    148       O  
ATOM   4722  CG2 THR A 565       7.900  -0.903 -14.608  1.00 35.83           C  
ANISOU 4722  CG2 THR A 565     5228   4755   3629   -512   -355    220       C  
ATOM   4723  N   MET A 566       3.959   0.967 -16.077  1.00 38.52           N  
ANISOU 4723  N   MET A 566     5542   5086   4006   -611   -229    104       N  
ATOM   4724  CA  MET A 566       2.715   1.718 -15.951  1.00 39.54           C  
ANISOU 4724  CA  MET A 566     5659   5242   4122   -641   -191     76       C  
ATOM   4725  C   MET A 566       1.644   0.895 -15.265  1.00 40.37           C  
ANISOU 4725  C   MET A 566     5796   5348   4194   -685   -179     94       C  
ATOM   4726  O   MET A 566       1.682  -0.323 -15.287  1.00 41.02           O  
ANISOU 4726  O   MET A 566     5912   5398   4276   -690   -190    123       O  
ATOM   4727  CB  MET A 566       2.207   2.204 -17.316  1.00 40.55           C  
ANISOU 4727  CB  MET A 566     5754   5365   4287   -619   -165     49       C  
ATOM   4728  CG  MET A 566       1.981   1.117 -18.350  1.00 43.09           C  
ANISOU 4728  CG  MET A 566     6082   5656   4632   -611   -170     58       C  
ATOM   4729  SD  MET A 566       3.483   0.737 -19.276  1.00 51.11           S  
ANISOU 4729  SD  MET A 566     7095   6633   5692   -560   -202     67       S  
ATOM   4730  CE  MET A 566       2.831  -0.010 -20.761  1.00 39.78           C  
ANISOU 4730  CE  MET A 566     5650   5179   4285   -557   -186     54       C  
ATOM   4731  N   LYS A 567       0.696   1.584 -14.646  1.00 40.35           N  
ANISOU 4731  N   LYS A 567     5785   5381   4164   -718   -149     74       N  
ATOM   4732  CA  LYS A 567      -0.452   0.954 -14.032  1.00 40.47           C  
ANISOU 4732  CA  LYS A 567     5824   5405   4147   -765   -130     82       C  
ATOM   4733  C   LYS A 567      -1.588   0.819 -15.065  1.00 39.00           C  
ANISOU 4733  C   LYS A 567     5613   5225   3978   -772   -101     59       C  
ATOM   4734  O   LYS A 567      -1.919   1.783 -15.763  1.00 36.11           O  
ANISOU 4734  O   LYS A 567     5204   4884   3629   -748    -81     33       O  
ATOM   4735  CB  LYS A 567      -0.907   1.803 -12.841  1.00 40.23           C  
ANISOU 4735  CB  LYS A 567     5791   5416   4076   -797   -111     69       C  
ATOM   4736  CG  LYS A 567      -2.025   1.194 -12.017  1.00 40.45           C  
ANISOU 4736  CG  LYS A 567     5846   5458   4064   -851    -91     77       C  
ATOM   4737  CD  LYS A 567      -2.470   2.167 -10.939  1.00 40.74           C  
ANISOU 4737  CD  LYS A 567     5875   5538   4064   -880    -68     57       C  
ATOM   4738  CE  LYS A 567      -3.454   1.519  -9.961  1.00 43.37           C  
ANISOU 4738  CE  LYS A 567     6238   5886   4351   -937    -51     69       C  
ATOM   4739  NZ  LYS A 567      -3.367   2.182  -8.618  1.00 43.97           N  
ANISOU 4739  NZ  LYS A 567     6325   6000   4383   -966    -44     63       N  
ATOM   4740  N   PHE A 568      -2.171  -0.376 -15.154  1.00 37.56           N  
ANISOU 4740  N   PHE A 568     5458   5025   3788   -805    -95     70       N  
ATOM   4741  CA  PHE A 568      -3.305  -0.628 -16.057  1.00 37.34           C  
ANISOU 4741  CA  PHE A 568     5403   5018   3766   -825    -66     43       C  
ATOM   4742  C   PHE A 568      -4.614  -0.693 -15.281  1.00 37.91           C  
ANISOU 4742  C   PHE A 568     5476   5129   3797   -882    -34     31       C  
ATOM   4743  O   PHE A 568      -4.628  -1.069 -14.113  1.00 41.84           O  
ANISOU 4743  O   PHE A 568     6015   5616   4264   -915    -35     52       O  
ATOM   4744  CB  PHE A 568      -3.116  -1.939 -16.829  1.00 37.11           C  
ANISOU 4744  CB  PHE A 568     5398   4942   3757   -835    -70     50       C  
ATOM   4745  CG  PHE A 568      -2.026  -1.895 -17.863  1.00 38.56           C  
ANISOU 4745  CG  PHE A 568     5571   5096   3985   -781    -94     53       C  
ATOM   4746  CD1 PHE A 568      -2.160  -1.109 -19.016  1.00 37.94           C  
ANISOU 4746  CD1 PHE A 568     5437   5050   3928   -747    -89     25       C  
ATOM   4747  CD2 PHE A 568      -0.875  -2.672 -17.715  1.00 38.78           C  
ANISOU 4747  CD2 PHE A 568     5641   5064   4029   -759   -120     86       C  
ATOM   4748  CE1 PHE A 568      -1.153  -1.085 -19.980  1.00 38.34           C  
ANISOU 4748  CE1 PHE A 568     5477   5071   4017   -700   -109     26       C  
ATOM   4749  CE2 PHE A 568       0.132  -2.653 -18.686  1.00 39.18           C  
ANISOU 4749  CE2 PHE A 568     5679   5088   4120   -710   -140     86       C  
ATOM   4750  CZ  PHE A 568      -0.005  -1.856 -19.809  1.00 37.40           C  
ANISOU 4750  CZ  PHE A 568     5400   4893   3917   -684   -135     54       C  
ATOM   4751  N   HIS A 569      -5.718  -0.353 -15.930  1.00 37.96           N  
ANISOU 4751  N   HIS A 569     5434   5188   3799   -891     -6      0       N  
ATOM   4752  CA  HIS A 569      -7.009  -0.288 -15.242  1.00 37.38           C  
ANISOU 4752  CA  HIS A 569     5349   5164   3686   -942     26    -16       C  
ATOM   4753  C   HIS A 569      -8.036  -1.223 -15.781  1.00 37.85           C  
ANISOU 4753  C   HIS A 569     5398   5248   3732   -994     49    -39       C  
ATOM   4754  O   HIS A 569      -9.192  -1.209 -15.355  1.00 38.30           O  
ANISOU 4754  O   HIS A 569     5436   5358   3757  -1039     79    -59       O  
ATOM   4755  CB  HIS A 569      -7.530   1.131 -15.247  1.00 36.38           C  
ANISOU 4755  CB  HIS A 569     5170   5096   3555   -908     47    -34       C  
ATOM   4756  CG  HIS A 569      -6.716   2.058 -14.416  1.00 37.01           C  
ANISOU 4756  CG  HIS A 569     5268   5155   3637   -881     38    -22       C  
ATOM   4757  ND1 HIS A 569      -5.760   2.839 -14.937  1.00 37.63           N  
ANISOU 4757  ND1 HIS A 569     5335   5214   3748   -825     25    -19       N  
ATOM   4758  CD2 HIS A 569      -6.717   2.296 -13.051  1.00 38.02           C  
ANISOU 4758  CD2 HIS A 569     5426   5284   3733   -913     44    -15       C  
ATOM   4759  CE1 HIS A 569      -5.184   3.559 -13.961  1.00 36.80           C  
ANISOU 4759  CE1 HIS A 569     5249   5099   3633   -824     25    -17       C  
ATOM   4760  NE2 HIS A 569      -5.770   3.228 -12.807  1.00 39.22           N  
ANISOU 4760  NE2 HIS A 569     5580   5422   3899   -877     35    -14       N  
ATOM   4761  N   ASP A 570      -7.627  -2.066 -16.712  1.00 38.56           N  
ANISOU 4761  N   ASP A 570     5498   5304   3847   -993     40    -42       N  
ATOM   4762  CA  ASP A 570      -8.512  -3.090 -17.233  1.00 41.94           C  
ANISOU 4762  CA  ASP A 570     5922   5750   4262  -1056     67    -71       C  
ATOM   4763  C   ASP A 570      -7.817  -4.446 -17.113  1.00 41.55           C  
ANISOU 4763  C   ASP A 570     5950   5609   4228  -1085     66    -50       C  
ATOM   4764  O   ASP A 570      -6.706  -4.625 -17.595  1.00 42.72           O  
ANISOU 4764  O   ASP A 570     6117   5701   4411  -1039     40    -30       O  
ATOM   4765  CB  ASP A 570      -8.885  -2.765 -18.690  1.00 42.21           C  
ANISOU 4765  CB  ASP A 570     5884   5845   4307  -1031     70   -106       C  
ATOM   4766  CG  ASP A 570      -9.820  -3.798 -19.309  1.00 45.17           C  
ANISOU 4766  CG  ASP A 570     6244   6254   4663  -1105    101   -148       C  
ATOM   4767  OD1 ASP A 570      -9.884  -4.937 -18.807  1.00 44.44           O  
ANISOU 4767  OD1 ASP A 570     6213   6106   4564  -1171    121   -148       O  
ATOM   4768  OD2 ASP A 570     -10.483  -3.471 -20.324  1.00 47.86           O  
ANISOU 4768  OD2 ASP A 570     6511   6680   4993  -1098    109   -182       O  
ATOM   4769  N   GLY A 571      -8.462  -5.392 -16.446  1.00 42.44           N  
ANISOU 4769  N   GLY A 571     6106   5702   4313  -1159     98    -53       N  
ATOM   4770  CA  GLY A 571      -7.871  -6.728 -16.252  1.00 44.18           C  
ANISOU 4770  CA  GLY A 571     6411   5827   4548  -1184    110    -27       C  
ATOM   4771  C   GLY A 571      -7.838  -7.570 -17.522  1.00 42.98           C  
ANISOU 4771  C   GLY A 571     6257   5649   4422  -1204    129    -60       C  
ATOM   4772  O   GLY A 571      -7.303  -8.676 -17.537  1.00 44.26           O  
ANISOU 4772  O   GLY A 571     6489   5724   4603  -1219    146    -41       O  
ATOM   4773  N   GLU A 572      -8.406  -7.030 -18.589  1.00 44.68           N  
ANISOU 4773  N   GLU A 572     6392   5944   4637  -1202    129   -107       N  
ATOM   4774  CA  GLU A 572      -8.538  -7.730 -19.859  1.00 44.98           C  
ANISOU 4774  CA  GLU A 572     6415   5984   4691  -1231    149   -150       C  
ATOM   4775  C   GLU A 572      -7.392  -7.328 -20.776  1.00 42.56           C  
ANISOU 4775  C   GLU A 572     6091   5652   4427  -1149    110   -135       C  
ATOM   4776  O   GLU A 572      -7.211  -7.899 -21.864  1.00 41.08           O  
ANISOU 4776  O   GLU A 572     5896   5451   4259  -1160    121   -165       O  
ATOM   4777  CB  GLU A 572      -9.858  -7.332 -20.503  1.00 49.04           C  
ANISOU 4777  CB  GLU A 572     6840   6621   5169  -1273    168   -210       C  
ATOM   4778  CG  GLU A 572     -10.543  -8.435 -21.276  1.00 55.51           C  
ANISOU 4778  CG  GLU A 572     7657   7456   5977  -1362    215   -270       C  
ATOM   4779  CD  GLU A 572     -11.526  -9.198 -20.433  1.00 57.45           C  
ANISOU 4779  CD  GLU A 572     7938   7702   6187  -1462    266   -292       C  
ATOM   4780  OE1 GLU A 572     -11.764  -8.777 -19.290  1.00 58.35           O  
ANISOU 4780  OE1 GLU A 572     8068   7819   6283  -1458    262   -261       O  
ATOM   4781  OE2 GLU A 572     -12.059 -10.222 -20.918  1.00 65.96           O  
ANISOU 4781  OE2 GLU A 572     9029   8777   7254  -1551    316   -344       O  
ATOM   4782  N   VAL A 573      -6.634  -6.325 -20.342  1.00 40.05           N  
ANISOU 4782  N   VAL A 573     5764   5331   4122  -1073     68    -95       N  
ATOM   4783  CA  VAL A 573      -5.489  -5.835 -21.093  1.00 38.95           C  
ANISOU 4783  CA  VAL A 573     5609   5168   4021   -995     32    -79       C  
ATOM   4784  C   VAL A 573      -4.548  -6.982 -21.396  1.00 39.16           C  
ANISOU 4784  C   VAL A 573     5699   5096   4082   -994     35    -63       C  
ATOM   4785  O   VAL A 573      -4.361  -7.893 -20.561  1.00 37.34           O  
ANISOU 4785  O   VAL A 573     5543   4795   3849  -1021     53    -35       O  
ATOM   4786  CB  VAL A 573      -4.733  -4.727 -20.308  1.00 38.66           C  
ANISOU 4786  CB  VAL A 573     5570   5128   3990   -929     -4    -38       C  
ATOM   4787  CG1 VAL A 573      -3.874  -5.314 -19.191  1.00 36.74           C  
ANISOU 4787  CG1 VAL A 573     5402   4806   3750   -924    -16     10       C  
ATOM   4788  CG2 VAL A 573      -3.909  -3.849 -21.251  1.00 37.65           C  
ANISOU 4788  CG2 VAL A 573     5399   5012   3894   -855    -33    -39       C  
ATOM   4789  N   ASP A 574      -3.982  -6.961 -22.599  1.00 39.75           N  
ANISOU 4789  N   ASP A 574     5748   5166   4188   -959     24    -80       N  
ATOM   4790  CA  ASP A 574      -2.831  -7.803 -22.896  1.00 39.75           C  
ANISOU 4790  CA  ASP A 574     5803   5071   4228   -933     21    -58       C  
ATOM   4791  C   ASP A 574      -1.593  -7.005 -22.594  1.00 37.26           C  
ANISOU 4791  C   ASP A 574     5484   4737   3936   -848    -26    -14       C  
ATOM   4792  O   ASP A 574      -1.194  -6.140 -23.374  1.00 35.26           O  
ANISOU 4792  O   ASP A 574     5178   4519   3698   -800    -50    -25       O  
ATOM   4793  CB  ASP A 574      -2.808  -8.259 -24.347  1.00 40.91           C  
ANISOU 4793  CB  ASP A 574     5926   5221   4396   -945     37   -103       C  
ATOM   4794  CG  ASP A 574      -1.662  -9.220 -24.628  1.00 43.44           C  
ANISOU 4794  CG  ASP A 574     6308   5436   4760   -919     43    -82       C  
ATOM   4795  OD1 ASP A 574      -0.784  -9.367 -23.758  1.00 43.31           O  
ANISOU 4795  OD1 ASP A 574     6341   5356   4757   -875     25    -26       O  
ATOM   4796  OD2 ASP A 574      -1.647  -9.844 -25.706  1.00 48.29           O  
ANISOU 4796  OD2 ASP A 574     6920   6035   5392   -943     68   -121       O  
ATOM   4797  N   ALA A 575      -1.003  -7.276 -21.437  1.00 37.40           N  
ANISOU 4797  N   ALA A 575     5555   4703   3949   -831    -38     35       N  
ATOM   4798  CA  ALA A 575       0.150  -6.499 -20.966  1.00 36.17           C  
ANISOU 4798  CA  ALA A 575     5393   4545   3805   -760    -84     73       C  
ATOM   4799  C   ALA A 575       1.383  -6.842 -21.795  1.00 34.03           C  
ANISOU 4799  C   ALA A 575     5128   4223   3579   -706   -100     83       C  
ATOM   4800  O   ALA A 575       2.306  -6.036 -21.898  1.00 31.51           O  
ANISOU 4800  O   ALA A 575     4778   3918   3275   -649   -136     95       O  
ATOM   4801  CB  ALA A 575       0.405  -6.767 -19.494  1.00 34.69           C  
ANISOU 4801  CB  ALA A 575     5256   4333   3591   -761    -92    124       C  
ATOM   4802  N   SER A 576       1.378  -8.036 -22.393  1.00 32.16           N  
ANISOU 4802  N   SER A 576     4929   3926   3362   -728    -69     75       N  
ATOM   4803  CA  SER A 576       2.509  -8.493 -23.167  1.00 32.96           C  
ANISOU 4803  CA  SER A 576     5042   3972   3506   -678    -77     84       C  
ATOM   4804  C   SER A 576       2.684  -7.662 -24.425  1.00 33.08           C  
ANISOU 4804  C   SER A 576     4990   4035   3543   -654    -93     43       C  
ATOM   4805  O   SER A 576       3.805  -7.477 -24.914  1.00 34.59           O  
ANISOU 4805  O   SER A 576     5170   4206   3766   -596   -117     54       O  
ATOM   4806  CB  SER A 576       2.410  -9.984 -23.500  1.00 33.97           C  
ANISOU 4806  CB  SER A 576     5236   4017   3654   -712    -27     80       C  
ATOM   4807  OG  SER A 576       1.268 -10.275 -24.305  1.00 35.54           O  
ANISOU 4807  OG  SER A 576     5417   4243   3843   -787     13     18       O  
ATOM   4808  N   TYR A 577       1.594  -7.121 -24.937  1.00 32.78           N  
ANISOU 4808  N   TYR A 577     4905   4067   3483   -694    -80      0       N  
ATOM   4809  CA  TYR A 577       1.685  -6.338 -26.160  1.00 32.63           C  
ANISOU 4809  CA  TYR A 577     4823   4098   3477   -667    -91    -33       C  
ATOM   4810  C   TYR A 577       2.767  -5.262 -26.046  1.00 32.19           C  
ANISOU 4810  C   TYR A 577     4740   4050   3439   -596   -131     -8       C  
ATOM   4811  O   TYR A 577       3.460  -4.974 -27.014  1.00 32.53           O  
ANISOU 4811  O   TYR A 577     4757   4091   3509   -557   -141    -20       O  
ATOM   4812  CB  TYR A 577       0.334  -5.725 -26.523  1.00 31.97           C  
ANISOU 4812  CB  TYR A 577     4684   4106   3357   -706    -75    -71       C  
ATOM   4813  CG  TYR A 577       0.259  -5.251 -27.944  1.00 32.63           C  
ANISOU 4813  CG  TYR A 577     4708   4242   3447   -688    -75   -106       C  
ATOM   4814  CD1 TYR A 577       0.262  -6.164 -29.007  1.00 32.81           C  
ANISOU 4814  CD1 TYR A 577     4735   4248   3483   -717    -53   -141       C  
ATOM   4815  CD2 TYR A 577       0.189  -3.884 -28.244  1.00 32.05           C  
ANISOU 4815  CD2 TYR A 577     4578   4234   3366   -641    -91   -103       C  
ATOM   4816  CE1 TYR A 577       0.184  -5.728 -30.320  1.00 33.06           C  
ANISOU 4816  CE1 TYR A 577     4709   4339   3513   -700    -54   -172       C  
ATOM   4817  CE2 TYR A 577       0.104  -3.446 -29.554  1.00 31.13           C  
ANISOU 4817  CE2 TYR A 577     4408   4170   3250   -618    -88   -128       C  
ATOM   4818  CZ  TYR A 577       0.110  -4.369 -30.586  1.00 32.33           C  
ANISOU 4818  CZ  TYR A 577     4560   4314   3409   -648    -73   -162       C  
ATOM   4819  OH  TYR A 577       0.038  -3.939 -31.898  1.00 33.90           O  
ANISOU 4819  OH  TYR A 577     4704   4573   3602   -626    -72   -186       O  
ATOM   4820  N   PHE A 578       2.957  -4.726 -24.846  1.00 31.23           N  
ANISOU 4820  N   PHE A 578     4630   3935   3301   -583   -150     23       N  
ATOM   4821  CA  PHE A 578       3.816  -3.556 -24.666  1.00 32.79           C  
ANISOU 4821  CA  PHE A 578     4797   4154   3507   -530   -180     35       C  
ATOM   4822  C   PHE A 578       5.299  -3.877 -24.420  1.00 34.47           C  
ANISOU 4822  C   PHE A 578     5032   4319   3746   -483   -208     66       C  
ATOM   4823  O   PHE A 578       6.136  -2.965 -24.266  1.00 34.39           O  
ANISOU 4823  O   PHE A 578     4995   4328   3742   -445   -231     70       O  
ATOM   4824  CB  PHE A 578       3.215  -2.631 -23.592  1.00 32.65           C  
ANISOU 4824  CB  PHE A 578     4767   4183   3453   -545   -181     41       C  
ATOM   4825  CG  PHE A 578       1.781  -2.248 -23.878  1.00 32.13           C  
ANISOU 4825  CG  PHE A 578     4671   4174   3361   -581   -152     12       C  
ATOM   4826  CD1 PHE A 578       1.480  -1.216 -24.788  1.00 32.40           C  
ANISOU 4826  CD1 PHE A 578     4651   4258   3399   -555   -143    -10       C  
ATOM   4827  CD2 PHE A 578       0.734  -2.975 -23.331  1.00 30.72           C  
ANISOU 4827  CD2 PHE A 578     4516   4001   3154   -639   -131      9       C  
ATOM   4828  CE1 PHE A 578       0.151  -0.895 -25.094  1.00 32.57           C  
ANISOU 4828  CE1 PHE A 578     4637   4344   3393   -579   -118    -32       C  
ATOM   4829  CE2 PHE A 578      -0.591  -2.672 -23.652  1.00 31.51           C  
ANISOU 4829  CE2 PHE A 578     4578   4165   3227   -672   -105    -20       C  
ATOM   4830  CZ  PHE A 578      -0.883  -1.622 -24.522  1.00 30.85           C  
ANISOU 4830  CZ  PHE A 578     4435   4140   3145   -639   -101    -39       C  
ATOM   4831  N   CYS A 579       5.613  -5.171 -24.460  1.00 37.24           N  
ANISOU 4831  N   CYS A 579     5428   4608   4111   -485   -200     83       N  
ATOM   4832  CA  CYS A 579       6.933  -5.720 -24.128  1.00 40.88           C  
ANISOU 4832  CA  CYS A 579     5916   5023   4593   -435   -222    122       C  
ATOM   4833  C   CYS A 579       7.821  -5.796 -25.352  1.00 41.30           C  
ANISOU 4833  C   CYS A 579     5947   5054   4689   -395   -226    105       C  
ATOM   4834  O   CYS A 579       9.045  -5.832 -25.238  1.00 41.84           O  
ANISOU 4834  O   CYS A 579     6013   5107   4775   -343   -251    129       O  
ATOM   4835  CB  CYS A 579       6.782  -7.165 -23.637  1.00 44.81           C  
ANISOU 4835  CB  CYS A 579     6482   5454   5088   -450   -198    155       C  
ATOM   4836  SG  CYS A 579       6.291  -7.388 -21.932  1.00 53.93           S  
ANISOU 4836  SG  CYS A 579     7680   6616   6194   -476   -199    200       S  
ATOM   4837  N   LYS A 580       7.195  -5.897 -26.517  1.00 38.90           N  
ANISOU 4837  N   LYS A 580     5628   4753   4398   -421   -200     63       N  
ATOM   4838  CA  LYS A 580       7.882  -6.350 -27.711  1.00 38.86           C  
ANISOU 4838  CA  LYS A 580     5618   4714   4433   -395   -193     45       C  
ATOM   4839  C   LYS A 580       7.352  -5.655 -28.956  1.00 36.27           C  
ANISOU 4839  C   LYS A 580     5239   4435   4106   -409   -183     -2       C  
ATOM   4840  O   LYS A 580       6.259  -5.093 -28.951  1.00 34.47           O  
ANISOU 4840  O   LYS A 580     4986   4261   3847   -444   -173    -21       O  
ATOM   4841  CB  LYS A 580       7.690  -7.869 -27.861  1.00 40.50           C  
ANISOU 4841  CB  LYS A 580     5884   4849   4654   -420   -156     49       C  
ATOM   4842  CG  LYS A 580       6.217  -8.293 -27.890  1.00 41.55           C  
ANISOU 4842  CG  LYS A 580     6032   4994   4759   -497   -118     19       C  
ATOM   4843  CD  LYS A 580       6.019  -9.793 -27.673  1.00 43.51           C  
ANISOU 4843  CD  LYS A 580     6354   5160   5017   -530    -73     28       C  
ATOM   4844  CE  LYS A 580       4.536 -10.152 -27.484  1.00 44.63           C  
ANISOU 4844  CE  LYS A 580     6510   5323   5124   -617    -34     -2       C  
ATOM   4845  NZ  LYS A 580       3.686  -9.878 -28.686  1.00 44.95           N  
ANISOU 4845  NZ  LYS A 580     6498   5426   5153   -665    -16    -69       N  
ATOM   4846  N   LEU A 581       8.136  -5.700 -30.019  1.00 34.35           N  
ANISOU 4846  N   LEU A 581     4978   4176   3895   -378   -184    -18       N  
ATOM   4847  CA  LEU A 581       7.629  -5.414 -31.336  1.00 36.64           C  
ANISOU 4847  CA  LEU A 581     5230   4504   4185   -394   -167    -62       C  
ATOM   4848  C   LEU A 581       6.433  -6.309 -31.586  1.00 36.80           C  
ANISOU 4848  C   LEU A 581     5269   4526   4185   -460   -131    -90       C  
ATOM   4849  O   LEU A 581       6.545  -7.513 -31.437  1.00 39.71           O  
ANISOU 4849  O   LEU A 581     5688   4829   4568   -481   -108    -88       O  
ATOM   4850  CB  LEU A 581       8.714  -5.713 -32.385  1.00 36.89           C  
ANISOU 4850  CB  LEU A 581     5256   4501   4257   -357   -167    -75       C  
ATOM   4851  CG  LEU A 581       9.362  -4.578 -33.180  1.00 39.02           C  
ANISOU 4851  CG  LEU A 581     5476   4809   4539   -315   -183    -86       C  
ATOM   4852  CD1 LEU A 581       9.100  -3.193 -32.603  1.00 38.34           C  
ANISOU 4852  CD1 LEU A 581     5359   4778   4429   -303   -198    -74       C  
ATOM   4853  CD2 LEU A 581      10.856  -4.810 -33.377  1.00 39.84           C  
ANISOU 4853  CD2 LEU A 581     5585   4867   4685   -264   -198    -75       C  
ATOM   4854  N   PRO A 582       5.284  -5.726 -31.972  1.00 36.42           N  
ANISOU 4854  N   PRO A 582     5180   4556   4102   -493   -121   -118       N  
ATOM   4855  CA  PRO A 582       4.193  -6.531 -32.505  1.00 36.94           C  
ANISOU 4855  CA  PRO A 582     5246   4643   4144   -562    -85   -159       C  
ATOM   4856  C   PRO A 582       4.629  -7.185 -33.804  1.00 39.01           C  
ANISOU 4856  C   PRO A 582     5506   4885   4431   -567    -66   -196       C  
ATOM   4857  O   PRO A 582       5.369  -6.576 -34.592  1.00 38.62           O  
ANISOU 4857  O   PRO A 582     5424   4848   4399   -518    -83   -197       O  
ATOM   4858  CB  PRO A 582       3.102  -5.495 -32.804  1.00 35.95           C  
ANISOU 4858  CB  PRO A 582     5056   4625   3975   -572    -87   -176       C  
ATOM   4859  CG  PRO A 582       3.491  -4.281 -32.037  1.00 35.29           C  
ANISOU 4859  CG  PRO A 582     4960   4553   3893   -518   -116   -137       C  
ATOM   4860  CD  PRO A 582       4.977  -4.294 -32.030  1.00 35.45           C  
ANISOU 4860  CD  PRO A 582     5004   4507   3958   -466   -137   -114       C  
ATOM   4861  N   GLU A 583       4.156  -8.396 -34.051  1.00 42.10           N  
ANISOU 4861  N   GLU A 583     5930   5244   4820   -630    -26   -229       N  
ATOM   4862  CA  GLU A 583       4.614  -9.149 -35.216  1.00 45.68           C  
ANISOU 4862  CA  GLU A 583     6392   5666   5298   -641      0   -268       C  
ATOM   4863  C   GLU A 583       4.405  -8.426 -36.588  1.00 41.97           C  
ANISOU 4863  C   GLU A 583     5847   5289   4807   -635     -7   -307       C  
ATOM   4864  O   GLU A 583       5.241  -8.535 -37.478  1.00 40.38           O  
ANISOU 4864  O   GLU A 583     5641   5064   4634   -607     -6   -320       O  
ATOM   4865  CB  GLU A 583       4.074 -10.591 -35.198  1.00 50.78           C  
ANISOU 4865  CB  GLU A 583     7092   6255   5944   -721     57   -304       C  
ATOM   4866  CG  GLU A 583       4.224 -11.328 -33.848  1.00 58.76           C  
ANISOU 4866  CG  GLU A 583     8181   7172   6970   -724     71   -259       C  
ATOM   4867  CD  GLU A 583       5.553 -11.069 -33.101  1.00 65.67           C  
ANISOU 4867  CD  GLU A 583     9084   7983   7884   -632     33   -190       C  
ATOM   4868  OE1 GLU A 583       6.484 -11.899 -33.233  1.00 64.63           O  
ANISOU 4868  OE1 GLU A 583     9000   7761   7794   -602     53   -176       O  
ATOM   4869  OE2 GLU A 583       5.656 -10.066 -32.341  1.00 65.10           O  
ANISOU 4869  OE2 GLU A 583     8984   7952   7796   -591    -11   -151       O  
ATOM   4870  N   LYS A 584       3.350  -7.632 -36.722  1.00 39.59           N  
ANISOU 4870  N   LYS A 584     5489   5096   4457   -652    -15   -318       N  
ATOM   4871  CA  LYS A 584       3.184  -6.833 -37.949  1.00 39.69           C  
ANISOU 4871  CA  LYS A 584     5430   5203   4444   -630    -24   -340       C  
ATOM   4872  C   LYS A 584       4.337  -5.845 -38.196  1.00 39.66           C  
ANISOU 4872  C   LYS A 584     5413   5181   4472   -543    -56   -303       C  
ATOM   4873  O   LYS A 584       4.586  -5.467 -39.331  1.00 44.33           O  
ANISOU 4873  O   LYS A 584     5966   5816   5059   -520    -56   -321       O  
ATOM   4874  CB  LYS A 584       1.836  -6.115 -37.970  1.00 37.38           C  
ANISOU 4874  CB  LYS A 584     5076   5035   4089   -650    -26   -349       C  
ATOM   4875  CG  LYS A 584       1.671  -5.067 -36.889  1.00 38.74           C  
ANISOU 4875  CG  LYS A 584     5244   5218   4256   -605    -51   -297       C  
ATOM   4876  CD  LYS A 584       0.207  -4.727 -36.687  1.00 40.04           C  
ANISOU 4876  CD  LYS A 584     5361   5490   4362   -640    -42   -309       C  
ATOM   4877  CE  LYS A 584       0.059  -3.559 -35.735  1.00 41.01           C  
ANISOU 4877  CE  LYS A 584     5476   5627   4480   -588    -60   -260       C  
ATOM   4878  NZ  LYS A 584      -1.161  -3.721 -34.904  1.00 41.33           N  
ANISOU 4878  NZ  LYS A 584     5508   5713   4480   -639    -48   -267       N  
ATOM   4879  N   PHE A 585       5.040  -5.444 -37.133  1.00 38.72           N  
ANISOU 4879  N   PHE A 585     5326   5002   4383   -498    -79   -255       N  
ATOM   4880  CA  PHE A 585       6.189  -4.537 -37.256  1.00 37.14           C  
ANISOU 4880  CA  PHE A 585     5116   4781   4213   -425   -104   -226       C  
ATOM   4881  C   PHE A 585       7.547  -5.245 -37.085  1.00 37.97           C  
ANISOU 4881  C   PHE A 585     5266   4787   4372   -399   -110   -215       C  
ATOM   4882  O   PHE A 585       8.601  -4.624 -37.239  1.00 35.79           O  
ANISOU 4882  O   PHE A 585     4981   4494   4124   -345   -128   -198       O  
ATOM   4883  CB  PHE A 585       6.090  -3.407 -36.210  1.00 35.30           C  
ANISOU 4883  CB  PHE A 585     4875   4566   3970   -392   -125   -185       C  
ATOM   4884  CG  PHE A 585       4.953  -2.425 -36.449  1.00 33.24           C  
ANISOU 4884  CG  PHE A 585     4564   4402   3662   -391   -118   -187       C  
ATOM   4885  CD1 PHE A 585       4.923  -1.633 -37.584  1.00 31.01           C  
ANISOU 4885  CD1 PHE A 585     4234   4181   3366   -356   -112   -193       C  
ATOM   4886  CD2 PHE A 585       3.957  -2.253 -35.494  1.00 30.81           C  
ANISOU 4886  CD2 PHE A 585     4256   4125   3323   -417   -115   -176       C  
ATOM   4887  CE1 PHE A 585       3.904  -0.711 -37.782  1.00 31.55           C  
ANISOU 4887  CE1 PHE A 585     4257   4340   3390   -341   -103   -185       C  
ATOM   4888  CE2 PHE A 585       2.942  -1.336 -35.691  1.00 31.27           C  
ANISOU 4888  CE2 PHE A 585     4266   4274   3339   -406   -106   -172       C  
ATOM   4889  CZ  PHE A 585       2.915  -0.559 -36.834  1.00 29.92           C  
ANISOU 4889  CZ  PHE A 585     4048   4163   3154   -364    -99   -174       C  
ATOM   4890  N   ARG A 586       7.517  -6.529 -36.730  1.00 40.66           N  
ANISOU 4890  N   ARG A 586     5657   5063   4727   -437    -90   -222       N  
ATOM   4891  CA  ARG A 586       8.711  -7.214 -36.236  1.00 42.51           C  
ANISOU 4891  CA  ARG A 586     5939   5202   5007   -402    -95   -196       C  
ATOM   4892  C   ARG A 586       9.725  -7.543 -37.334  1.00 43.87           C  
ANISOU 4892  C   ARG A 586     6107   5342   5217   -374    -86   -217       C  
ATOM   4893  O   ARG A 586      10.920  -7.640 -37.051  1.00 47.80           O  
ANISOU 4893  O   ARG A 586     6621   5786   5752   -321   -101   -189       O  
ATOM   4894  CB  ARG A 586       8.337  -8.480 -35.445  1.00 44.83           C  
ANISOU 4894  CB  ARG A 586     6297   5430   5304   -444    -67   -188       C  
ATOM   4895  CG  ARG A 586       9.493  -9.125 -34.689  1.00 49.22           C  
ANISOU 4895  CG  ARG A 586     6905   5896   5901   -394    -73   -143       C  
ATOM   4896  CD  ARG A 586       9.023 -10.025 -33.546  1.00 55.53           C  
ANISOU 4896  CD  ARG A 586     7767   6641   6691   -423    -52   -115       C  
ATOM   4897  NE  ARG A 586       8.829 -11.425 -33.941  1.00 62.99           N  
ANISOU 4897  NE  ARG A 586     8767   7509   7654   -464      5   -139       N  
ATOM   4898  CZ  ARG A 586       9.718 -12.410 -33.750  1.00 68.59           C  
ANISOU 4898  CZ  ARG A 586     9534   8122   8404   -426     28   -111       C  
ATOM   4899  NH1 ARG A 586      10.898 -12.160 -33.183  1.00 69.87           N  
ANISOU 4899  NH1 ARG A 586     9695   8263   8587   -343     -8    -57       N  
ATOM   4900  NH2 ARG A 586       9.430 -13.656 -34.134  1.00 63.06           N  
ANISOU 4900  NH2 ARG A 586     8891   7348   7720   -472     94   -140       N  
ATOM   4901  N   PHE A 587       9.265  -7.694 -38.573  1.00 41.78           N  
ANISOU 4901  N   PHE A 587     5816   5117   4939   -407    -63   -266       N  
ATOM   4902  CA  PHE A 587      10.152  -8.153 -39.650  1.00 46.54           C  
ANISOU 4902  CA  PHE A 587     6419   5685   5576   -390    -47   -293       C  
ATOM   4903  C   PHE A 587      10.227  -7.200 -40.838  1.00 47.70           C  
ANISOU 4903  C   PHE A 587     6507   5909   5708   -372    -56   -315       C  
ATOM   4904  O   PHE A 587      10.490  -7.635 -41.959  1.00 48.51           O  
ANISOU 4904  O   PHE A 587     6601   6010   5818   -384    -34   -355       O  
ATOM   4905  CB  PHE A 587       9.738  -9.551 -40.161  1.00 49.39           C  
ANISOU 4905  CB  PHE A 587     6820   6003   5943   -453      4   -339       C  
ATOM   4906  CG  PHE A 587       9.527 -10.575 -39.071  1.00 51.66           C  
ANISOU 4906  CG  PHE A 587     7175   6209   6242   -478     28   -318       C  
ATOM   4907  CD1 PHE A 587      10.608 -11.080 -38.339  1.00 52.47           C  
ANISOU 4907  CD1 PHE A 587     7326   6218   6390   -421     24   -272       C  
ATOM   4908  CD2 PHE A 587       8.246 -11.063 -38.799  1.00 52.62           C  
ANISOU 4908  CD2 PHE A 587     7311   6352   6327   -556     57   -344       C  
ATOM   4909  CE1 PHE A 587      10.411 -12.039 -37.351  1.00 53.51           C  
ANISOU 4909  CE1 PHE A 587     7525   6274   6530   -437     51   -245       C  
ATOM   4910  CE2 PHE A 587       8.044 -12.024 -37.810  1.00 53.59           C  
ANISOU 4910  CE2 PHE A 587     7504   6395   6461   -581     87   -324       C  
ATOM   4911  CZ  PHE A 587       9.125 -12.515 -37.092  1.00 54.31           C  
ANISOU 4911  CZ  PHE A 587     7648   6387   6597   -519     85   -271       C  
ATOM   4912  N   VAL A 588       9.986  -5.907 -40.611  1.00 46.43           N  
ANISOU 4912  N   VAL A 588     6306   5812   5521   -343    -83   -290       N  
ATOM   4913  CA  VAL A 588      10.240  -4.909 -41.656  1.00 40.52           C  
ANISOU 4913  CA  VAL A 588     5509   5124   4763   -311    -89   -298       C  
ATOM   4914  C   VAL A 588      11.739  -4.817 -41.835  1.00 38.08           C  
ANISOU 4914  C   VAL A 588     5208   4756   4504   -259    -99   -288       C  
ATOM   4915  O   VAL A 588      12.485  -4.987 -40.871  1.00 36.71           O  
ANISOU 4915  O   VAL A 588     5062   4522   4361   -233   -115   -258       O  
ATOM   4916  CB  VAL A 588       9.646  -3.506 -41.320  1.00 39.88           C  
ANISOU 4916  CB  VAL A 588     5391   5113   4646   -286   -105   -268       C  
ATOM   4917  CG1 VAL A 588       8.167  -3.603 -41.007  1.00 39.96           C  
ANISOU 4917  CG1 VAL A 588     5389   5186   4606   -332    -97   -275       C  
ATOM   4918  CG2 VAL A 588      10.382  -2.843 -40.179  1.00 35.39           C  
ANISOU 4918  CG2 VAL A 588     4840   4502   4103   -245   -128   -227       C  
ATOM   4919  N   LYS A 589      12.192  -4.601 -43.065  1.00 38.60           N  
ANISOU 4919  N   LYS A 589     5247   4843   4573   -245    -88   -312       N  
ATOM   4920  CA  LYS A 589      13.632  -4.470 -43.317  1.00 38.98           C  
ANISOU 4920  CA  LYS A 589     5298   4844   4669   -197    -95   -307       C  
ATOM   4921  C   LYS A 589      14.124  -3.090 -42.881  1.00 37.99           C  
ANISOU 4921  C   LYS A 589     5151   4739   4545   -152   -116   -274       C  
ATOM   4922  O   LYS A 589      13.510  -2.069 -43.210  1.00 35.55           O  
ANISOU 4922  O   LYS A 589     4812   4492   4201   -147   -112   -268       O  
ATOM   4923  CB  LYS A 589      13.957  -4.701 -44.799  1.00 43.08           C  
ANISOU 4923  CB  LYS A 589     5797   5380   5191   -202    -73   -348       C  
ATOM   4924  CG  LYS A 589      14.453  -6.103 -45.138  1.00 47.34           C  
ANISOU 4924  CG  LYS A 589     6370   5850   5766   -221    -49   -380       C  
ATOM   4925  CD  LYS A 589      15.447  -6.076 -46.302  1.00 49.20           C  
ANISOU 4925  CD  LYS A 589     6588   6078   6027   -197    -35   -406       C  
ATOM   4926  CE  LYS A 589      14.845  -6.671 -47.573  1.00 54.64           C  
ANISOU 4926  CE  LYS A 589     7265   6805   6688   -248     -1   -462       C  
ATOM   4927  NZ  LYS A 589      15.395  -6.075 -48.833  1.00 54.27           N  
ANISOU 4927  NZ  LYS A 589     7182   6802   6636   -227      4   -482       N  
ATOM   4928  N   ILE A 590      15.229  -3.058 -42.141  1.00 36.19           N  
ANISOU 4928  N   ILE A 590     4936   4461   4354   -119   -134   -254       N  
ATOM   4929  CA  ILE A 590      15.850  -1.787 -41.771  1.00 35.09           C  
ANISOU 4929  CA  ILE A 590     4775   4338   4218    -85   -147   -234       C  
ATOM   4930  C   ILE A 590      17.283  -1.665 -42.302  1.00 35.46           C  
ANISOU 4930  C   ILE A 590     4808   4360   4303    -51   -146   -246       C  
ATOM   4931  O   ILE A 590      17.999  -0.730 -41.975  1.00 35.31           O  
ANISOU 4931  O   ILE A 590     4774   4349   4293    -29   -153   -238       O  
ATOM   4932  CB  ILE A 590      15.811  -1.557 -40.239  1.00 35.09           C  
ANISOU 4932  CB  ILE A 590     4791   4327   4214    -84   -170   -202       C  
ATOM   4933  CG1 ILE A 590      16.754  -2.540 -39.507  1.00 35.34           C  
ANISOU 4933  CG1 ILE A 590     4845   4303   4279    -67   -188   -190       C  
ATOM   4934  CG2 ILE A 590      14.383  -1.694 -39.735  1.00 34.12           C  
ANISOU 4934  CG2 ILE A 590     4680   4228   4052   -120   -167   -193       C  
ATOM   4935  CD1 ILE A 590      16.812  -2.356 -38.005  1.00 35.00           C  
ANISOU 4935  CD1 ILE A 590     4814   4258   4226    -63   -213   -157       C  
ATOM   4936  N   ASN A 591      17.716  -2.634 -43.087  1.00 37.03           N  
ANISOU 4936  N   ASN A 591     5013   4529   4525    -51   -135   -270       N  
ATOM   4937  CA  ASN A 591      19.072  -2.596 -43.597  1.00 39.74           C  
ANISOU 4937  CA  ASN A 591     5341   4852   4907    -17   -133   -284       C  
ATOM   4938  C   ASN A 591      19.069  -2.309 -45.087  1.00 40.12           C  
ANISOU 4938  C   ASN A 591     5367   4927   4947    -22   -107   -315       C  
ATOM   4939  O   ASN A 591      18.419  -3.012 -45.865  1.00 38.76           O  
ANISOU 4939  O   ASN A 591     5202   4762   4762    -49    -89   -339       O  
ATOM   4940  CB  ASN A 591      19.824  -3.896 -43.294  1.00 42.30           C  
ANISOU 4940  CB  ASN A 591     5688   5115   5270      0   -137   -283       C  
ATOM   4941  CG  ASN A 591      20.168  -4.047 -41.821  1.00 44.05           C  
ANISOU 4941  CG  ASN A 591     5922   5316   5497     19   -166   -244       C  
ATOM   4942  OD1 ASN A 591      20.471  -3.063 -41.126  1.00 46.98           O  
ANISOU 4942  OD1 ASN A 591     6273   5719   5858     29   -186   -229       O  
ATOM   4943  ND2 ASN A 591      20.138  -5.284 -41.337  1.00 42.06           N  
ANISOU 4943  ND2 ASN A 591     5706   5013   5260     24   -163   -230       N  
ATOM   4944  N   ARG A 592      19.784  -1.259 -45.463  1.00 37.02           N  
ANISOU 4944  N   ARG A 592     4950   4554   4561      0   -102   -317       N  
ATOM   4945  CA  ARG A 592      19.831  -0.807 -46.834  1.00 40.06           C  
ANISOU 4945  CA  ARG A 592     5315   4970   4935      1    -75   -339       C  
ATOM   4946  C   ARG A 592      20.975  -1.472 -47.591  1.00 40.44           C  
ANISOU 4946  C   ARG A 592     5356   4985   5021     15    -65   -369       C  
ATOM   4947  O   ARG A 592      22.141  -1.268 -47.253  1.00 45.03           O  
ANISOU 4947  O   ARG A 592     5927   5545   5637     41    -74   -369       O  
ATOM   4948  CB  ARG A 592      20.041   0.711 -46.830  1.00 37.64           C  
ANISOU 4948  CB  ARG A 592     4992   4693   4616     18    -64   -324       C  
ATOM   4949  CG  ARG A 592      19.576   1.395 -48.082  1.00 34.00           C  
ANISOU 4949  CG  ARG A 592     4517   4278   4123     22    -34   -329       C  
ATOM   4950  CD  ARG A 592      19.732   2.902 -47.997  1.00 31.45           C  
ANISOU 4950  CD  ARG A 592     4189   3970   3789     41    -11   -308       C  
ATOM   4951  NE  ARG A 592      19.363   3.521 -49.272  1.00 29.01           N  
ANISOU 4951  NE  ARG A 592     3869   3705   3448     54     21   -306       N  
ATOM   4952  CZ  ARG A 592      19.001   4.791 -49.402  1.00 29.49           C  
ANISOU 4952  CZ  ARG A 592     3932   3788   3484     76     52   -278       C  
ATOM   4953  NH1 ARG A 592      18.907   5.561 -48.325  1.00 30.41           N  
ANISOU 4953  NH1 ARG A 592     4062   3886   3604     78     56   -257       N  
ATOM   4954  NH2 ARG A 592      18.693   5.283 -50.596  1.00 28.83           N  
ANISOU 4954  NH2 ARG A 592     3837   3747   3367     95     84   -269       N  
ATOM   4955  N   LYS A 593      20.665  -2.241 -48.621  1.00 42.07           N  
ANISOU 4955  N   LYS A 593     5566   5196   5223     -2    -46   -399       N  
ATOM   4956  CA  LYS A 593      21.728  -2.707 -49.536  1.00 49.33           C  
ANISOU 4956  CA  LYS A 593     6475   6091   6175     10    -28   -432       C  
ATOM   4957  C   LYS A 593      21.314  -2.828 -51.012  1.00 48.97           C  
ANISOU 4957  C   LYS A 593     6418   6084   6102    -12      1   -467       C  
ATOM   4958  O   LYS A 593      20.180  -3.200 -51.316  1.00 46.76           O  
ANISOU 4958  O   LYS A 593     6144   5837   5784    -48      8   -477       O  
ATOM   4959  CB  LYS A 593      22.356  -4.017 -49.047  1.00 54.48           C  
ANISOU 4959  CB  LYS A 593     7150   6675   6873     21    -32   -438       C  
ATOM   4960  CG  LYS A 593      23.845  -4.138 -49.389  1.00 60.39           C  
ANISOU 4960  CG  LYS A 593     7881   7396   7668     59    -26   -454       C  
ATOM   4961  CD  LYS A 593      24.486  -5.365 -48.745  1.00 64.18           C  
ANISOU 4961  CD  LYS A 593     8382   7810   8191     86    -29   -447       C  
ATOM   4962  CE  LYS A 593      24.093  -6.650 -49.461  1.00 66.97           C  
ANISOU 4962  CE  LYS A 593     8768   8122   8556     62      6   -479       C  
ATOM   4963  NZ  LYS A 593      24.750  -6.773 -50.796  1.00 70.58           N  
ANISOU 4963  NZ  LYS A 593     9207   8581   9029     63     37   -524       N  
ATOM   4964  N   ALA A 594      22.258  -2.530 -51.913  1.00 51.13           N  
ANISOU 4964  N   ALA A 594     6674   6360   6394      4     18   -488       N  
ATOM   4965  CA  ALA A 594      22.032  -2.601 -53.376  1.00 50.97           C  
ANISOU 4965  CA  ALA A 594     6639   6382   6346    -14     48   -522       C  
ATOM   4966  C   ALA A 594      21.771  -4.014 -53.871  1.00 52.06           C  
ANISOU 4966  C   ALA A 594     6793   6497   6490    -49     66   -565       C  
ATOM   4967  O   ALA A 594      22.487  -4.951 -53.507  1.00 50.73           O  
ANISOU 4967  O   ALA A 594     6644   6258   6371    -39     69   -578       O  
ATOM   4968  CB  ALA A 594      23.199  -1.992 -54.130  1.00 50.40           C  
ANISOU 4968  CB  ALA A 594     6546   6308   6293     11     65   -535       C  
ATOM   4969  N   SER A 595      20.748  -4.150 -54.717  1.00 53.29           N  
ANISOU 4969  N   SER A 595     6939   6715   6592    -89     82   -588       N  
ATOM   4970  CA  SER A 595      20.281  -5.458 -55.198  1.00 57.62           C  
ANISOU 4970  CA  SER A 595     7503   7252   7135   -139    106   -638       C  
ATOM   4971  C   SER A 595      20.184  -5.514 -56.737  1.00 56.20           C  
ANISOU 4971  C   SER A 595     7299   7135   6918   -167    137   -685       C  
ATOM   4972  O   SER A 595      19.662  -6.481 -57.299  1.00 57.40           O  
ANISOU 4972  O   SER A 595     7458   7299   7052   -221    163   -736       O  
ATOM   4973  CB  SER A 595      18.919  -5.795 -54.559  1.00 58.61           C  
ANISOU 4973  CB  SER A 595     7641   7404   7223   -180     97   -631       C  
ATOM   4974  OG  SER A 595      18.438  -7.065 -54.977  1.00 60.21           O  
ANISOU 4974  OG  SER A 595     7862   7593   7419   -239    129   -685       O  
ATOM   4975  N   ILE A 596      20.672  -4.467 -57.402  1.00 52.59           N  
ANISOU 4975  N   ILE A 596     6815   6721   6446   -135    137   -670       N  
ATOM   4976  CA  ILE A 596      20.788  -4.451 -58.866  1.00 52.39           C  
ANISOU 4976  CA  ILE A 596     6765   6753   6386   -152    166   -710       C  
ATOM   4977  C   ILE A 596      22.123  -3.832 -59.355  1.00 52.94           C  
ANISOU 4977  C   ILE A 596     6825   6797   6492   -109    177   -706       C  
ATOM   4978  O   ILE A 596      22.612  -4.137 -60.458  1.00 51.16           O  
ANISOU 4978  O   ILE A 596     6590   6585   6264   -123    206   -749       O  
ATOM   4979  CB  ILE A 596      19.555  -3.789 -59.571  1.00 50.28           C  
ANISOU 4979  CB  ILE A 596     6464   6611   6027   -171    165   -699       C  
ATOM   4980  CG1 ILE A 596      19.526  -2.256 -59.413  1.00 48.36           C  
ANISOU 4980  CG1 ILE A 596     6205   6408   5760   -115    151   -634       C  
ATOM   4981  CG2 ILE A 596      18.245  -4.429 -59.129  1.00 51.79           C  
ANISOU 4981  CG2 ILE A 596     6657   6840   6181   -220    157   -711       C  
ATOM   4982  CD1 ILE A 596      19.222  -1.767 -58.020  1.00 47.53           C  
ANISOU 4982  CD1 ILE A 596     6116   6266   5674    -91    123   -582       C  
TER    4983      ILE A 596                                                      
MASTER      371    0    2   55   32    0    5    610423    2   50   92          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.