CNRS Nantes University UFIP UFIP
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***  papaína  ***

elNémo ID: 21040915052255616

Job options:

ID        	=	 21040915052255616
JOBID     	=	 papaína
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 3
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER papaína

HEADER    HYDROLASE                               02-JUL-14   4QRV              
TITLE     CRYSTAL STRUCTURE OF I86F MUTANT OF PAPAIN                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PAPAIN;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 27-345;                                       
COMPND   5 SYNONYM: PAPAYA PROTEINASE I, PPI;                                   
COMPND   6 EC: 3.4.22.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;                                  
SOURCE   3 ORGANISM_COMMON: MAMON;                                              
SOURCE   4 ORGANISM_TAXID: 3649;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET30 EK/LIC                              
KEYWDS    PROTEASE, ZYMOGEN, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DUTTA,D.CHOUDHURY,S.ROY                                             
REVDAT   2   22-NOV-17 4QRV    1       REMARK                                   
REVDAT   1   12-AUG-15 4QRV    0                                                
JRNL        AUTH   S.DUTTA,D.CHOUDHURY,S.ROY,S.BISWAS                           
JRNL        TITL   PRO-PEPTIDE REGULATES THE SUBSTRATE SPECIFICITY AND ZYMOGEN  
JRNL        TITL 2 ACTIVATION PROCESS OF PAPAIN: A STRUCTURAL AND MECHANISTIC   
JRNL        TITL 3 INSIGHT                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 50402                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2564                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.1400 -  5.1797    0.99     2769   136  0.1992 0.2263        
REMARK   3     2  5.1797 -  4.1130    1.00     2703   140  0.1677 0.2280        
REMARK   3     3  4.1130 -  3.5936    1.00     2680   140  0.1740 0.2348        
REMARK   3     4  3.5936 -  3.2653    1.00     2689   150  0.1888 0.2169        
REMARK   3     5  3.2653 -  3.0313    1.00     2710   127  0.1951 0.2240        
REMARK   3     6  3.0313 -  2.8527    1.00     2630   147  0.2137 0.2979        
REMARK   3     7  2.8527 -  2.7099    1.00     2699   154  0.2088 0.2445        
REMARK   3     8  2.7099 -  2.5919    1.00     2641   163  0.2116 0.2708        
REMARK   3     9  2.5919 -  2.4922    1.00     2695   121  0.2083 0.2461        
REMARK   3    10  2.4922 -  2.4062    1.00     2675   147  0.2164 0.2954        
REMARK   3    11  2.4062 -  2.3310    1.00     2669   157  0.2106 0.2862        
REMARK   3    12  2.3310 -  2.2643    1.00     2651   118  0.2143 0.2876        
REMARK   3    13  2.2643 -  2.2047    1.00     2666   148  0.2104 0.2666        
REMARK   3    14  2.2047 -  2.1510    1.00     2624   173  0.2090 0.2599        
REMARK   3    15  2.1510 -  2.1021    1.00     2678   135  0.2210 0.2462        
REMARK   3    16  2.1021 -  2.0573    1.00     2643   152  0.2360 0.2796        
REMARK   3    17  2.0573 -  2.0162    1.00     2646   143  0.2450 0.3138        
REMARK   3    18  2.0162 -  1.9781    0.88     2370   113  0.2455 0.2959        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4940                                  
REMARK   3   ANGLE     :  1.008           6681                                  
REMARK   3   CHIRALITY :  0.046            687                                  
REMARK   3   PLANARITY :  0.005            866                                  
REMARK   3   DIHEDRAL  : 13.247           1789                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 4 THROUGH 80 )                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0440  -9.8665  77.8332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3235 T22:   0.1915                                     
REMARK   3      T33:   0.2066 T12:  -0.0182                                     
REMARK   3      T13:   0.0600 T23:   0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5333 L22:   1.3826                                     
REMARK   3      L33:   7.5892 L12:  -0.9572                                     
REMARK   3      L13:   0.5135 L23:  -0.2434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0187 S12:  -0.3528 S13:  -0.1771                       
REMARK   3      S21:   0.2992 S22:   0.0134 S23:   0.0807                       
REMARK   3      S31:   0.5460 S32:   0.2215 S33:  -0.0337                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 81 THROUGH 117 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2704  -3.6461  52.4421              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2291 T22:   0.2792                                     
REMARK   3      T33:   0.3708 T12:  -0.0399                                     
REMARK   3      T13:   0.1172 T23:  -0.1105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8175 L22:   7.4169                                     
REMARK   3      L33:   4.9696 L12:  -1.7840                                     
REMARK   3      L13:  -0.9441 L23:   2.7151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3189 S12:  -0.1909 S13:   0.4780                       
REMARK   3      S21:  -0.1012 S22:  -0.2217 S23:   0.2548                       
REMARK   3      S31:   0.0362 S32:  -0.1319 S33:   0.0268                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 118 THROUGH 319 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3589   2.6601  55.9018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1472 T22:   0.1437                                     
REMARK   3      T33:   0.1436 T12:   0.0207                                     
REMARK   3      T13:   0.0221 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0765 L22:   2.2376                                     
REMARK   3      L33:   1.1363 L12:   0.6521                                     
REMARK   3      L13:  -0.0951 L23:  -0.2341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0462 S12:   0.1756 S13:   0.0658                       
REMARK   3      S21:  -0.1493 S22:   0.0081 S23:  -0.1018                       
REMARK   3      S31:   0.0462 S32:   0.0635 S33:   0.0365                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 3 THROUGH 109 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7578  -6.6151 -14.4710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3608 T22:   0.2939                                     
REMARK   3      T33:   0.2162 T12:   0.0445                                     
REMARK   3      T13:  -0.0249 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6323 L22:   1.8920                                     
REMARK   3      L33:   6.8610 L12:   1.0257                                     
REMARK   3      L13:  -4.0833 L23:  -0.9090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0391 S12:  -0.2508 S13:   0.2065                       
REMARK   3      S21:   0.0182 S22:   0.1386 S23:   0.1423                       
REMARK   3      S31:   0.0500 S32:   0.4362 S33:  -0.1181                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 110 THROUGH 319 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2351 -16.5514   7.5531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2520 T22:   0.2294                                     
REMARK   3      T33:   0.1666 T12:  -0.0484                                     
REMARK   3      T13:   0.0316 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9091 L22:   4.0308                                     
REMARK   3      L33:   2.5605 L12:   0.2251                                     
REMARK   3      L13:  -0.2952 L23:  -1.6718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0959 S12:  -0.2995 S13:  -0.0655                       
REMARK   3      S21:   0.3418 S22:  -0.0959 S23:   0.1182                       
REMARK   3      S31:  -0.1368 S32:   0.0812 S33:  -0.0014                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086434.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50450                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.978                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61100                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, PH 7.5, HANGING DROP,       
REMARK 280  TEMPERATURE 298K                                                    
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       37.13350            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -43                                                      
REMARK 465     HIS A   -42                                                      
REMARK 465     HIS A   -41                                                      
REMARK 465     HIS A   -40                                                      
REMARK 465     HIS A   -39                                                      
REMARK 465     HIS A   -38                                                      
REMARK 465     HIS A   -37                                                      
REMARK 465     SER A   -36                                                      
REMARK 465     SER A   -35                                                      
REMARK 465     GLY A   -34                                                      
REMARK 465     LEU A   -33                                                      
REMARK 465     VAL A   -32                                                      
REMARK 465     PRO A   -31                                                      
REMARK 465     ARG A   -30                                                      
REMARK 465     GLY A   -29                                                      
REMARK 465     SER A   -28                                                      
REMARK 465     GLY A   -27                                                      
REMARK 465     MET A   -26                                                      
REMARK 465     LYS A   -25                                                      
REMARK 465     GLU A   -24                                                      
REMARK 465     THR A   -23                                                      
REMARK 465     ALA A   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     ALA A   -20                                                      
REMARK 465     LYS A   -19                                                      
REMARK 465     PHE A   -18                                                      
REMARK 465     GLU A   -17                                                      
REMARK 465     ARG A   -16                                                      
REMARK 465     GLN A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     PRO A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     THR A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     LYS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PHE A    86                                                      
REMARK 465     ALA A    87                                                      
REMARK 465     GLY A    88                                                      
REMARK 465     ASN A    89                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     SER A    96                                                      
REMARK 465     TYR A    97                                                      
REMARK 465     GLU A    98                                                      
REMARK 465     GLU A    99                                                      
REMARK 465     VAL A   100                                                      
REMARK 465     LEU A   101                                                      
REMARK 465     ASN A   102                                                      
REMARK 465     ASP A   103                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     ASP A   105                                                      
REMARK 465     MET B   -43                                                      
REMARK 465     HIS B   -42                                                      
REMARK 465     HIS B   -41                                                      
REMARK 465     HIS B   -40                                                      
REMARK 465     HIS B   -39                                                      
REMARK 465     HIS B   -38                                                      
REMARK 465     HIS B   -37                                                      
REMARK 465     SER B   -36                                                      
REMARK 465     SER B   -35                                                      
REMARK 465     GLY B   -34                                                      
REMARK 465     LEU B   -33                                                      
REMARK 465     VAL B   -32                                                      
REMARK 465     PRO B   -31                                                      
REMARK 465     ARG B   -30                                                      
REMARK 465     GLY B   -29                                                      
REMARK 465     SER B   -28                                                      
REMARK 465     GLY B   -27                                                      
REMARK 465     MET B   -26                                                      
REMARK 465     LYS B   -25                                                      
REMARK 465     GLU B   -24                                                      
REMARK 465     THR B   -23                                                      
REMARK 465     ALA B   -22                                                      
REMARK 465     ALA B   -21                                                      
REMARK 465     ALA B   -20                                                      
REMARK 465     LYS B   -19                                                      
REMARK 465     PHE B   -18                                                      
REMARK 465     GLU B   -17                                                      
REMARK 465     ARG B   -16                                                      
REMARK 465     GLN B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     PRO B   -10                                                      
REMARK 465     ASP B    -9                                                      
REMARK 465     LEU B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     THR B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     LYS B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     PHE B     2                                                      
REMARK 465     PHE B    86                                                      
REMARK 465     ALA B    87                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     ASN B    89                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     SER B    96                                                      
REMARK 465     TYR B    97                                                      
REMARK 465     GLU B    98                                                      
REMARK 465     GLU B    99                                                      
REMARK 465     VAL B   100                                                      
REMARK 465     LEU B   101                                                      
REMARK 465     ASN B   102                                                      
REMARK 465     ASP B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     ASP B   105                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  90    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  94    CG   CD   OE1  OE2                                  
REMARK 470     TYR B  90    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   523     O    HOH A   640              2.09            
REMARK 500   O    HOH A   573     O    HOH A   650              2.11            
REMARK 500   O    HOH A   563     O    HOH A   575              2.15            
REMARK 500   O    HOH B   515     O    HOH B   549              2.15            
REMARK 500   O    HOH A   709     O    HOH A   715              2.16            
REMARK 500   O    HOH A   554     O    HOH A   643              2.16            
REMARK 500   O    HOH B   591     O    HOH B   592              2.16            
REMARK 500   NZ   LYS B   124     OE2  GLU B   154              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  82      -35.91     91.66                                   
REMARK 500    THR A  83       49.66   -143.01                                   
REMARK 500    SER A 312       99.70   -161.92                                   
REMARK 500    ASN B  30       14.20     51.56                                   
REMARK 500    LYS B  34      -70.70    -72.56                                   
REMARK 500    THR B  83       27.86   -154.55                                   
REMARK 500    ASP B 265       -0.32   -148.75                                   
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 TYR A   90     THR A   91                  148.24                    
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 CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QRG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4QRX   RELATED DB: PDB                                   
DBREF  4QRV A    1   319  UNP    P00784   PAPA1_CARPA     27    345             
DBREF  4QRV B    1   319  UNP    P00784   PAPA1_CARPA     27    345             
SEQADV 4QRV MET A  -43  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -42  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -41  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -40  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -39  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -38  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -37  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER A  -36  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER A  -35  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY A  -34  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LEU A  -33  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV VAL A  -32  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PRO A  -31  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ARG A  -30  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY A  -29  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER A  -28  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY A  -27  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV MET A  -26  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LYS A  -25  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLU A  -24  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV THR A  -23  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ALA A  -22  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ALA A  -21  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ALA A  -20  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LYS A  -19  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PHE A  -18  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLU A  -17  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ARG A  -16  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLN A  -15  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS A  -14  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV MET A  -13  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP A  -12  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER A  -11  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PRO A  -10  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP A   -9  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LEU A   -8  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY A   -7  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV THR A   -6  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP A   -5  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP A   -4  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP A   -3  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP A   -2  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LYS A   -1  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV MET A    0  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PHE A   86  UNP  P00784    ILE   112 ENGINEERED MUTATION            
SEQADV 4QRV ALA A  132  UNP  P00784    CYS   158 ENGINEERED MUTATION            
SEQADV 4QRV SER A  139  UNP  P00784    VAL   165 ENGINEERED MUTATION            
SEQADV 4QRV SER A  143  UNP  P00784    GLY   169 ENGINEERED MUTATION            
SEQADV 4QRV ARG A  281  UNP  P00784    LYS   307 ENGINEERED MUTATION            
SEQADV 4QRV MET B  -43  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -42  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -41  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -40  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -39  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -38  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -37  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER B  -36  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER B  -35  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY B  -34  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LEU B  -33  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV VAL B  -32  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PRO B  -31  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ARG B  -30  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY B  -29  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER B  -28  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY B  -27  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV MET B  -26  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LYS B  -25  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLU B  -24  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV THR B  -23  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ALA B  -22  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ALA B  -21  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ALA B  -20  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LYS B  -19  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PHE B  -18  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLU B  -17  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ARG B  -16  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLN B  -15  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV HIS B  -14  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV MET B  -13  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP B  -12  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV SER B  -11  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PRO B  -10  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP B   -9  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LEU B   -8  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV GLY B   -7  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV THR B   -6  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP B   -5  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP B   -4  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP B   -3  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV ASP B   -2  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV LYS B   -1  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV MET B    0  UNP  P00784              EXPRESSION TAG                 
SEQADV 4QRV PHE B   86  UNP  P00784    ILE   112 ENGINEERED MUTATION            
SEQADV 4QRV ALA B  132  UNP  P00784    CYS   158 ENGINEERED MUTATION            
SEQADV 4QRV SER B  139  UNP  P00784    VAL   165 ENGINEERED MUTATION            
SEQADV 4QRV SER B  143  UNP  P00784    GLY   169 ENGINEERED MUTATION            
SEQADV 4QRV ARG B  281  UNP  P00784    LYS   307 ENGINEERED MUTATION            
SEQRES   1 A  363  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  363  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 A  363  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 A  363  ASP ASP ASP LYS MET ASP PHE SER ILE VAL GLY TYR SER          
SEQRES   5 A  363  GLN ASN ASP LEU THR SER THR GLU ARG LEU ILE GLN LEU          
SEQRES   6 A  363  PHE GLU SER TRP MET LEU LYS HIS ASN LYS ILE TYR LYS          
SEQRES   7 A  363  ASN ILE ASP GLU LYS ILE TYR ARG PHE GLU ILE PHE LYS          
SEQRES   8 A  363  ASP ASN LEU LYS TYR ILE ASP GLU THR ASN LYS LYS ASN          
SEQRES   9 A  363  ASN SER TYR TRP LEU GLY LEU ASN VAL PHE ALA ASP MET          
SEQRES  10 A  363  SER ASN ASP GLU PHE LYS GLU LYS TYR THR GLY SER PHE          
SEQRES  11 A  363  ALA GLY ASN TYR THR THR THR GLU LEU SER TYR GLU GLU          
SEQRES  12 A  363  VAL LEU ASN ASP GLY ASP VAL ASN ILE PRO GLU TYR VAL          
SEQRES  13 A  363  ASP TRP ARG GLN LYS GLY ALA VAL THR PRO VAL LYS ASN          
SEQRES  14 A  363  GLN GLY SER CYS GLY SER ALA TRP ALA PHE SER ALA VAL          
SEQRES  15 A  363  SER THR ILE GLU SER ILE ILE LYS ILE ARG THR GLY ASN          
SEQRES  16 A  363  LEU ASN GLU TYR SER GLU GLN GLU LEU LEU ASP CYS ASP          
SEQRES  17 A  363  ARG ARG SER TYR GLY CYS ASN GLY GLY TYR PRO TRP SER          
SEQRES  18 A  363  ALA LEU GLN LEU VAL ALA GLN TYR GLY ILE HIS TYR ARG          
SEQRES  19 A  363  ASN THR TYR PRO TYR GLU GLY VAL GLN ARG TYR CYS ARG          
SEQRES  20 A  363  SER ARG GLU LYS GLY PRO TYR ALA ALA LYS THR ASP GLY          
SEQRES  21 A  363  VAL ARG GLN VAL GLN PRO TYR ASN GLU GLY ALA LEU LEU          
SEQRES  22 A  363  TYR SER ILE ALA ASN GLN PRO VAL SER VAL VAL LEU GLU          
SEQRES  23 A  363  ALA ALA GLY LYS ASP PHE GLN LEU TYR ARG GLY GLY ILE          
SEQRES  24 A  363  PHE VAL GLY PRO CYS GLY ASN LYS VAL ASP HIS ALA VAL          
SEQRES  25 A  363  ALA ALA VAL GLY TYR GLY PRO ASN TYR ILE LEU ILE ARG          
SEQRES  26 A  363  ASN SER TRP GLY THR GLY TRP GLY GLU ASN GLY TYR ILE          
SEQRES  27 A  363  ARG ILE LYS ARG GLY THR GLY ASN SER TYR GLY VAL CYS          
SEQRES  28 A  363  GLY LEU TYR THR SER SER PHE TYR PRO VAL LYS ASN              
SEQRES   1 B  363  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 B  363  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 B  363  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 B  363  ASP ASP ASP LYS MET ASP PHE SER ILE VAL GLY TYR SER          
SEQRES   5 B  363  GLN ASN ASP LEU THR SER THR GLU ARG LEU ILE GLN LEU          
SEQRES   6 B  363  PHE GLU SER TRP MET LEU LYS HIS ASN LYS ILE TYR LYS          
SEQRES   7 B  363  ASN ILE ASP GLU LYS ILE TYR ARG PHE GLU ILE PHE LYS          
SEQRES   8 B  363  ASP ASN LEU LYS TYR ILE ASP GLU THR ASN LYS LYS ASN          
SEQRES   9 B  363  ASN SER TYR TRP LEU GLY LEU ASN VAL PHE ALA ASP MET          
SEQRES  10 B  363  SER ASN ASP GLU PHE LYS GLU LYS TYR THR GLY SER PHE          
SEQRES  11 B  363  ALA GLY ASN TYR THR THR THR GLU LEU SER TYR GLU GLU          
SEQRES  12 B  363  VAL LEU ASN ASP GLY ASP VAL ASN ILE PRO GLU TYR VAL          
SEQRES  13 B  363  ASP TRP ARG GLN LYS GLY ALA VAL THR PRO VAL LYS ASN          
SEQRES  14 B  363  GLN GLY SER CYS GLY SER ALA TRP ALA PHE SER ALA VAL          
SEQRES  15 B  363  SER THR ILE GLU SER ILE ILE LYS ILE ARG THR GLY ASN          
SEQRES  16 B  363  LEU ASN GLU TYR SER GLU GLN GLU LEU LEU ASP CYS ASP          
SEQRES  17 B  363  ARG ARG SER TYR GLY CYS ASN GLY GLY TYR PRO TRP SER          
SEQRES  18 B  363  ALA LEU GLN LEU VAL ALA GLN TYR GLY ILE HIS TYR ARG          
SEQRES  19 B  363  ASN THR TYR PRO TYR GLU GLY VAL GLN ARG TYR CYS ARG          
SEQRES  20 B  363  SER ARG GLU LYS GLY PRO TYR ALA ALA LYS THR ASP GLY          
SEQRES  21 B  363  VAL ARG GLN VAL GLN PRO TYR ASN GLU GLY ALA LEU LEU          
SEQRES  22 B  363  TYR SER ILE ALA ASN GLN PRO VAL SER VAL VAL LEU GLU          
SEQRES  23 B  363  ALA ALA GLY LYS ASP PHE GLN LEU TYR ARG GLY GLY ILE          
SEQRES  24 B  363  PHE VAL GLY PRO CYS GLY ASN LYS VAL ASP HIS ALA VAL          
SEQRES  25 B  363  ALA ALA VAL GLY TYR GLY PRO ASN TYR ILE LEU ILE ARG          
SEQRES  26 B  363  ASN SER TRP GLY THR GLY TRP GLY GLU ASN GLY TYR ILE          
SEQRES  27 B  363  ARG ILE LYS ARG GLY THR GLY ASN SER TYR GLY VAL CYS          
SEQRES  28 B  363  GLY LEU TYR THR SER SER PHE TYR PRO VAL LYS ASN              
HET     CL  A 401       1                                                       
HET     NA  A 402       1                                                       
HET     CL  B 401       1                                                       
HET     NA  B 402       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4   NA    2(NA 1+)                                                     
FORMUL   7  HOH   *369(H2 O)                                                    
HELIX    1   1 SER A    8  THR A   13  5                                   6    
HELIX    2   2 SER A   14  HIS A   29  1                                  16    
HELIX    3   3 ASN A   35  ASN A   57  1                                  23    
HELIX    4   4 SER A   74  LYS A   81  1                                   8    
HELIX    5   5 ARG A  115  GLY A  118  5                                   4    
HELIX    6   6 SER A  131  GLY A  150  1                                  20    
HELIX    7   7 SER A  156  ASP A  164  1                                   9    
HELIX    8   8 TYR A  168  GLY A  172  5                                   5    
HELIX    9   9 TYR A  174  TYR A  185  1                                  12    
HELIX   10  10 ARG A  203  GLY A  208  5                                   6    
HELIX   11  11 ASN A  224  GLN A  235  1                                  12    
HELIX   12  12 GLY A  245  LEU A  250  1                                   6    
HELIX   13  13 GLY A  305  LEU A  309  5                                   5    
HELIX   14  14 SER B    8  THR B   13  5                                   6    
HELIX   15  15 SER B   14  HIS B   29  1                                  16    
HELIX   16  16 ASN B   35  ASN B   57  1                                  23    
HELIX   17  17 SER B   74  GLU B   80  1                                   7    
HELIX   18  18 SER B  131  GLY B  150  1                                  20    
HELIX   19  19 SER B  156  ASP B  164  1                                   9    
HELIX   20  20 TYR B  168  GLY B  172  5                                   5    
HELIX   21  21 TYR B  174  TYR B  185  1                                  12    
HELIX   22  22 ARG B  203  LYS B  207  5                                   5    
HELIX   23  23 ASN B  224  GLN B  235  1                                  12    
HELIX   24  24 GLY B  245  LEU B  250  1                                   6    
HELIX   25  25 GLY B  305  LEU B  309  5                                   5    
SHEET    1   A 6 TYR A  63  LEU A  65  0                                        
SHEET    2   A 6 TYR A 251  PHE A 256 -1  O  GLY A 253   N  TRP A  64           
SHEET    3   A 6 TYR A 293  LYS A 297  1  O  ARG A 295   N  PHE A 256           
SHEET    4   A 6 TYR A 277  ARG A 281 -1  N  ILE A 280   O  ILE A 294           
SHEET    5   A 6 HIS A 266  GLY A 274 -1  N  ALA A 269   O  ARG A 281           
SHEET    6   A 6 VAL A 112  ASP A 113 -1  N  VAL A 112   O  TYR A 273           
SHEET    1   B 6 TYR A  63  LEU A  65  0                                        
SHEET    2   B 6 TYR A 251  PHE A 256 -1  O  GLY A 253   N  TRP A  64           
SHEET    3   B 6 TYR A 293  LYS A 297  1  O  ARG A 295   N  PHE A 256           
SHEET    4   B 6 TYR A 277  ARG A 281 -1  N  ILE A 280   O  ILE A 294           
SHEET    5   B 6 HIS A 266  GLY A 274 -1  N  ALA A 269   O  ARG A 281           
SHEET    6   B 6 VAL A 237  LEU A 241 -1  N  VAL A 237   O  ALA A 270           
SHEET    1   C 2 GLY A 216  GLN A 219  0                                        
SHEET    2   C 2 PHE A 314  VAL A 317 -1  O  TYR A 315   N  ARG A 218           
SHEET    1   D 6 TYR B  63  LEU B  65  0                                        
SHEET    2   D 6 TYR B 251  PHE B 256 -1  O  GLY B 253   N  TRP B  64           
SHEET    3   D 6 TYR B 293  LYS B 297  1  O  ARG B 295   N  PHE B 256           
SHEET    4   D 6 TYR B 277  ARG B 281 -1  N  ILE B 280   O  ILE B 294           
SHEET    5   D 6 HIS B 266  GLY B 274 -1  N  ALA B 269   O  ARG B 281           
SHEET    6   D 6 VAL B 112  ASP B 113 -1  N  VAL B 112   O  TYR B 273           
SHEET    1   E 6 TYR B  63  LEU B  65  0                                        
SHEET    2   E 6 TYR B 251  PHE B 256 -1  O  GLY B 253   N  TRP B  64           
SHEET    3   E 6 TYR B 293  LYS B 297  1  O  ARG B 295   N  PHE B 256           
SHEET    4   E 6 TYR B 277  ARG B 281 -1  N  ILE B 280   O  ILE B 294           
SHEET    5   E 6 HIS B 266  GLY B 274 -1  N  ALA B 269   O  ARG B 281           
SHEET    6   E 6 VAL B 237  LEU B 241 -1  N  VAL B 237   O  ALA B 270           
SHEET    1   F 2 GLY B 216  GLN B 219  0                                        
SHEET    2   F 2 PHE B 314  VAL B 317 -1  O  TYR B 315   N  ARG B 218           
SSBOND   1 CYS A  129    CYS A  170                          1555   1555  2.06  
SSBOND   2 CYS A  163    CYS A  202                          1555   1555  2.06  
SSBOND   3 CYS A  260    CYS A  307                          1555   1555  2.08  
SSBOND   4 CYS B  129    CYS B  170                          1555   1555  2.03  
SSBOND   5 CYS B  163    CYS B  202                          1555   1555  2.04  
SSBOND   6 CYS B  260    CYS B  307                          1555   1555  2.06  
LINK         O   CYS A 260                NA    NA A 402     1555   1555  2.62  
CISPEP   1 GLY A  258    PRO A  259          0         8.30                     
CISPEP   2 GLY B  258    PRO B  259          0         5.27                     
SITE     1 AC1  5 ASN A 262  ASN A 302  GLY A 305  CYS A 307                    
SITE     2 AC1  5  NA A 402                                                     
SITE     1 AC2  5 CYS A 260  VAL A 306  CYS A 307   CL A 401                    
SITE     2 AC2  5 HOH A 679                                                     
SITE     1 AC3  2 LYS B  31  ASP B  72                                          
SITE     1 AC4  1 GLU B  38                                                     
CRYST1   42.670   74.267  116.326  90.00  92.85  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      0.023436  0.000000  0.001168        0.00000                         
SCALE2      0.000000  0.013465  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008607        0.00000                         
ATOM      1  N   ILE A   4      -5.437 -20.062  67.021  1.00 68.83           N  
ANISOU    1  N   ILE A   4    11333   6687   8134   1119      3   -653       N  
ATOM      2  CA  ILE A   4      -5.250 -19.835  68.449  1.00 60.42           C  
ANISOU    2  CA  ILE A   4    10275   5591   7092   1081     65   -474       C  
ATOM      3  C   ILE A   4      -5.618 -18.394  68.798  1.00 49.09           C  
ANISOU    3  C   ILE A   4     8538   4360   5755    882    159   -418       C  
ATOM      4  O   ILE A   4      -5.307 -17.455  68.058  1.00 44.09           O  
ANISOU    4  O   ILE A   4     7574   4067   5111    934    179   -457       O  
ATOM      5  CB  ILE A   4      -3.793 -20.149  68.898  1.00 58.64           C  
ANISOU    5  CB  ILE A   4    10084   5507   6690   1532     52   -404       C  
ATOM      6  CG1 ILE A   4      -3.640 -20.004  70.419  1.00 61.00           C  
ANISOU    6  CG1 ILE A   4    10416   5771   6991   1502    105   -222       C  
ATOM      7  CG2 ILE A   4      -2.794 -19.275  68.154  1.00 60.01           C  
ANISOU    7  CG2 ILE A   4     9937   6105   6758   1829     72   -458       C  
ATOM      8  CD1 ILE A   4      -2.320 -20.525  70.969  1.00 58.08           C  
ANISOU    8  CD1 ILE A   4    10114   5535   6421   1936     76   -149       C  
ATOM      9  N   VAL A   5      -6.300 -18.237  69.926  1.00 43.41           N  
ANISOU    9  N   VAL A   5     7826   3543   5123    602    212   -287       N  
ATOM     10  CA  VAL A   5      -6.830 -16.942  70.342  1.00 39.47           C  
ANISOU   10  CA  VAL A   5     6966   3312   4720    353    288   -217       C  
ATOM     11  C   VAL A   5      -6.284 -16.518  71.704  1.00 36.91           C  
ANISOU   11  C   VAL A   5     6559   3106   4359    407    337    -66       C  
ATOM     12  O   VAL A   5      -6.586 -15.428  72.198  1.00 29.93           O  
ANISOU   12  O   VAL A   5     5416   2425   3530    248    393    -19       O  
ATOM     13  CB  VAL A   5      -8.357 -16.975  70.402  1.00 39.55           C  
ANISOU   13  CB  VAL A   5     6987   3196   4842    -53    313   -224       C  
ATOM     14  CG1 VAL A   5      -8.921 -17.118  69.003  1.00 43.85           C  
ANISOU   14  CG1 VAL A   5     7517   3735   5410   -129    255   -390       C  
ATOM     15  CG2 VAL A   5      -8.818 -18.122  71.299  1.00 40.83           C  
ANISOU   15  CG2 VAL A   5     7463   3050   4999   -203    307   -130       C  
ATOM     16  N   GLY A   6      -5.493 -17.394  72.313  1.00 41.33           N  
ANISOU   16  N   GLY A   6     7361   3534   4807    656    308     -1       N  
ATOM     17  CA  GLY A   6      -4.775 -17.054  73.524  1.00 41.74           C  
ANISOU   17  CA  GLY A   6     7323   3759   4779    775    333    127       C  
ATOM     18  C   GLY A   6      -5.319 -17.699  74.782  1.00 44.75           C  
ANISOU   18  C   GLY A   6     7951   3907   5144    649    367    272       C  
ATOM     19  O   GLY A   6      -4.762 -17.512  75.860  1.00 52.78           O  
ANISOU   19  O   GLY A   6     8919   5067   6066    762    382    381       O  
ATOM     20  N   TYR A   7      -6.396 -18.465  74.650  1.00 46.98           N  
ANISOU   20  N   TYR A   7     8492   3856   5502    397    375    280       N  
ATOM     21  CA  TYR A   7      -7.045 -19.057  75.814  1.00 41.91           C  
ANISOU   21  CA  TYR A   7     7989   3091   4845    197    413    432       C  
ATOM     22  C   TYR A   7      -7.929 -20.262  75.481  1.00 54.48           C  
ANISOU   22  C   TYR A   7     9777   4432   6490    -33    369    408       C  
ATOM     23  O   TYR A   7      -8.416 -20.400  74.357  1.00 53.98           O  
ANISOU   23  O   TYR A   7     9691   4315   6504   -152    323    267       O  
ATOM     24  CB  TYR A   7      -7.890 -18.001  76.516  1.00 38.27           C  
ANISOU   24  CB  TYR A   7     7287   2816   4439    -93    514    500       C  
ATOM     25  CG  TYR A   7      -9.091 -17.582  75.706  1.00 43.93           C  
ANISOU   25  CG  TYR A   7     7815   3589   5289   -415    533    392       C  
ATOM     26  CD1 TYR A   7      -8.974 -16.633  74.687  1.00 41.40           C  
ANISOU   26  CD1 TYR A   7     7237   3461   5032   -366    516    246       C  
ATOM     27  CD2 TYR A   7     -10.343 -18.139  75.947  1.00 47.31           C  
ANISOU   27  CD2 TYR A   7     8236   3978   5760   -739    548    434       C  
ATOM     28  CE1 TYR A   7     -10.068 -16.252  73.945  1.00 41.00           C  
ANISOU   28  CE1 TYR A   7     7027   3477   5073   -617    530    160       C  
ATOM     29  CE2 TYR A   7     -11.444 -17.762  75.205  1.00 45.19           C  
ANISOU   29  CE2 TYR A   7     7768   3823   5580   -997    555    342       C  
ATOM     30  CZ  TYR A   7     -11.299 -16.820  74.210  1.00 43.21           C  
ANISOU   30  CZ  TYR A   7     7341   3696   5380   -932    551    206       C  
ATOM     31  OH  TYR A   7     -12.389 -16.445  73.479  1.00 42.06           O  
ANISOU   31  OH  TYR A   7     6996   3688   5296  -1159    555    121       O  
ATOM     32  N   SER A   8      -8.135 -21.125  76.475  1.00 62.05           N  
ANISOU   32  N   SER A   8    10935   5243   7398    -98    381    555       N  
ATOM     33  CA  SER A   8      -9.114 -22.207  76.383  1.00 63.92           C  
ANISOU   33  CA  SER A   8    11355   5243   7691   -391    354    575       C  
ATOM     34  C   SER A   8     -10.380 -21.787  77.111  1.00 67.06           C  
ANISOU   34  C   SER A   8    11544   5787   8150   -790    442    683       C  
ATOM     35  O   SER A   8     -10.341 -20.908  77.977  1.00 59.32           O  
ANISOU   35  O   SER A   8    10369   5038   7131   -778    523    775       O  
ATOM     36  CB  SER A   8      -8.569 -23.506  76.976  1.00 65.42           C  
ANISOU   36  CB  SER A   8    11922   5154   7779   -215    314    682       C  
ATOM     37  OG  SER A   8      -7.456 -23.969  76.235  1.00 69.80           O  
ANISOU   37  OG  SER A   8    12661   5609   8249    183    231    567       O  
ATOM     38  N   GLN A   9     -11.503 -22.404  76.766  1.00 69.17           N  
ANISOU   38  N   GLN A   9    11840   5950   8490  -1133    425    669       N  
ATOM     39  CA  GLN A   9     -12.771 -22.018  77.369  1.00 73.68           C  
ANISOU   39  CA  GLN A   9    12168   6731   9097  -1498    510    767       C  
ATOM     40  C   GLN A   9     -12.830 -22.430  78.836  1.00 71.16           C  
ANISOU   40  C   GLN A   9    11945   6396   8698  -1540    581   1002       C  
ATOM     41  O   GLN A   9     -13.637 -21.906  79.610  1.00 67.14           O  
ANISOU   41  O   GLN A   9    11196   6143   8170  -1742    675   1112       O  
ATOM     42  CB  GLN A   9     -13.942 -22.616  76.594  1.00 79.81           C  
ANISOU   42  CB  GLN A   9    12937   7437   9949  -1856    467    694       C  
ATOM     43  CG  GLN A   9     -14.483 -21.675  75.532  1.00 80.20           C  
ANISOU   43  CG  GLN A   9    12677   7733  10062  -1943    456    520       C  
ATOM     44  CD  GLN A   9     -15.969 -21.427  75.685  1.00 83.95           C  
ANISOU   44  CD  GLN A   9    12872   8470  10556  -2329    511    560       C  
ATOM     45  OE1 GLN A   9     -16.726 -22.331  76.050  1.00 93.34           O  
ANISOU   45  OE1 GLN A   9    14163   9564  11739  -2614    512    656       O  
ATOM     46  NE2 GLN A   9     -16.395 -20.197  75.417  1.00 75.18           N  
ANISOU   46  NE2 GLN A   9    11407   7706   9454  -2332    560    492       N  
ATOM     47  N   ASN A  10     -11.958 -23.356  79.219  1.00 67.77           N  
ANISOU   47  N   ASN A  10    11860   5691   8199  -1317    537   1081       N  
ATOM     48  CA  ASN A  10     -11.839 -23.738  80.616  1.00 71.60           C  
ANISOU   48  CA  ASN A  10    12457   6161   8586  -1294    600   1319       C  
ATOM     49  C   ASN A  10     -11.277 -22.583  81.446  1.00 65.15           C  
ANISOU   49  C   ASN A  10    11412   5666   7676  -1082    670   1374       C  
ATOM     50  O   ASN A  10     -11.584 -22.456  82.631  1.00 59.22           O  
ANISOU   50  O   ASN A  10    10586   5073   6842  -1157    753   1560       O  
ATOM     51  CB  ASN A  10     -10.971 -24.992  80.758  1.00 76.12           C  
ANISOU   51  CB  ASN A  10    13470   6364   9087  -1051    528   1381       C  
ATOM     52  CG  ASN A  10     -11.609 -26.219  80.115  1.00 84.49           C  
ANISOU   52  CG  ASN A  10    14814   7069  10219  -1300    464   1349       C  
ATOM     53  OD1 ASN A  10     -10.966 -26.939  79.351  1.00 90.08           O  
ANISOU   53  OD1 ASN A  10    15814   7498  10913  -1091    367   1228       O  
ATOM     54  ND2 ASN A  10     -12.881 -26.462  80.426  1.00 81.61           N  
ANISOU   54  ND2 ASN A  10    14361   6734   9913  -1745    518   1455       N  
ATOM     55  N   ASP A  11     -10.484 -21.723  80.808  1.00 53.52           N  
ANISOU   55  N   ASP A  11     9823   4306   6206   -832    639   1213       N  
ATOM     56  CA  ASP A  11      -9.941 -20.535  81.468  1.00 51.81           C  
ANISOU   56  CA  ASP A  11     9395   4389   5899   -654    697   1235       C  
ATOM     57  C   ASP A  11     -11.035 -19.563  81.916  1.00 52.49           C  
ANISOU   57  C   ASP A  11     9155   4787   6003   -931    801   1259       C  
ATOM     58  O   ASP A  11     -10.811 -18.735  82.795  1.00 49.27           O  
ANISOU   58  O   ASP A  11     8607   4631   5482   -837    868   1316       O  
ATOM     59  CB  ASP A  11      -8.962 -19.804  80.543  1.00 46.74           C  
ANISOU   59  CB  ASP A  11     8687   3798   5272   -381    646   1060       C  
ATOM     60  CG  ASP A  11      -7.695 -20.598  80.290  1.00 48.95           C  
ANISOU   60  CG  ASP A  11     9233   3896   5471      3    555   1046       C  
ATOM     61  OD1 ASP A  11      -7.268 -21.335  81.203  1.00 44.44           O  
ANISOU   61  OD1 ASP A  11     8856   3248   4781    156    548   1192       O  
ATOM     62  OD2 ASP A  11      -7.126 -20.479  79.180  1.00 54.99           O  
ANISOU   62  OD2 ASP A  11     9996   4625   6272    177    492    890       O  
ATOM     63  N   LEU A  12     -12.214 -19.680  81.311  1.00 51.36           N  
ANISOU   63  N   LEU A  12     8888   4655   5972  -1247    812   1205       N  
ATOM     64  CA  LEU A  12     -13.303 -18.734  81.528  1.00 49.33           C  
ANISOU   64  CA  LEU A  12     8288   4735   5721  -1463    905   1194       C  
ATOM     65  C   LEU A  12     -14.246 -19.163  82.657  1.00 54.04           C  
ANISOU   65  C   LEU A  12     8824   5467   6239  -1683    995   1400       C  
ATOM     66  O   LEU A  12     -15.253 -18.504  82.935  1.00 50.69           O  
ANISOU   66  O   LEU A  12     8107   5365   5789  -1843   1084   1408       O  
ATOM     67  CB  LEU A  12     -14.094 -18.555  80.227  1.00 51.90           C  
ANISOU   67  CB  LEU A  12     8461   5079   6178  -1651    866   1026       C  
ATOM     68  CG  LEU A  12     -13.627 -17.515  79.192  1.00 57.96           C  
ANISOU   68  CG  LEU A  12     9093   5920   7008  -1496    835    828       C  
ATOM     69  CD1 LEU A  12     -12.126 -17.548  78.947  1.00 58.50           C  
ANISOU   69  CD1 LEU A  12     9370   5800   7058  -1169    773    782       C  
ATOM     70  CD2 LEU A  12     -14.370 -17.727  77.885  1.00 60.71           C  
ANISOU   70  CD2 LEU A  12     9368   6234   7464  -1676    773    690       C  
ATOM     71  N   THR A  13     -13.923 -20.267  83.316  1.00 55.39           N  
ANISOU   71  N   THR A  13     9271   5415   6359  -1666    981   1573       N  
ATOM     72  CA  THR A  13     -14.890 -20.877  84.215  1.00 61.62           C  
ANISOU   72  CA  THR A  13    10033   6285   7096  -1922   1068   1786       C  
ATOM     73  C   THR A  13     -14.779 -20.398  85.663  1.00 63.26           C  
ANISOU   73  C   THR A  13    10132   6784   7119  -1804   1176   1965       C  
ATOM     74  O   THR A  13     -15.591 -20.786  86.505  1.00 64.10           O  
ANISOU   74  O   THR A  13    10177   7025   7154  -1990   1277   2160       O  
ATOM     75  CB  THR A  13     -14.772 -22.408  84.176  1.00 65.99           C  
ANISOU   75  CB  THR A  13    10962   6423   7687  -2017   1006   1904       C  
ATOM     76  OG1 THR A  13     -13.466 -22.804  84.611  1.00 67.89           O  
ANISOU   76  OG1 THR A  13    11492   6459   7844  -1675    951   1969       O  
ATOM     77  CG2 THR A  13     -15.007 -22.906  82.757  1.00 63.39           C  
ANISOU   77  CG2 THR A  13    10739   5839   7506  -2154    900   1710       C  
ATOM     78  N   SER A  14     -13.797 -19.547  85.954  1.00 44.80           N  
ANISOU   78  N   SER A  14     7766   4570   4685  -1498   1162   1894       N  
ATOM     79  CA  SER A  14     -13.641 -19.034  87.313  1.00 53.27           C  
ANISOU   79  CA  SER A  14     8739   5957   5545  -1363   1250   2029       C  
ATOM     80  C   SER A  14     -12.708 -17.841  87.331  1.00 48.89           C  
ANISOU   80  C   SER A  14     8102   5570   4901  -1079   1224   1857       C  
ATOM     81  O   SER A  14     -11.973 -17.607  86.379  1.00 39.26           O  
ANISOU   81  O   SER A  14     6959   4173   3785   -951   1141   1689       O  
ATOM     82  CB  SER A  14     -13.123 -20.124  88.265  1.00 48.66           C  
ANISOU   82  CB  SER A  14     8429   5214   4845  -1275   1235   2279       C  
ATOM     83  OG  SER A  14     -11.721 -20.296  88.161  1.00 47.70           O  
ANISOU   83  OG  SER A  14     8543   4901   4681   -947   1125   2225       O  
ATOM     84  N   THR A  15     -12.731 -17.088  88.423  1.00 41.62           N  
ANISOU   84  N   THR A  15     7030   5008   3776   -974   1301   1895       N  
ATOM     85  CA  THR A  15     -11.909 -15.895  88.497  1.00 50.37           C  
ANISOU   85  CA  THR A  15     8064   6288   4786   -726   1282   1704       C  
ATOM     86  C   THR A  15     -10.449 -16.310  88.637  1.00 44.90           C  
ANISOU   86  C   THR A  15     7605   5428   4026   -435   1174   1727       C  
ATOM     87  O   THR A  15      -9.561 -15.671  88.082  1.00 38.28           O  
ANISOU   87  O   THR A  15     6764   4574   3208   -245   1113   1562       O  
ATOM     88  CB  THR A  15     -12.359 -14.981  89.651  1.00 47.29           C  
ANISOU   88  CB  THR A  15     7460   6341   4166   -671   1380   1690       C  
ATOM     89  OG1 THR A  15     -13.686 -14.517  89.379  1.00 45.04           O  
ANISOU   89  OG1 THR A  15     6924   6247   3940   -863   1481   1642       O  
ATOM     90  CG2 THR A  15     -11.445 -13.779  89.781  1.00 45.32           C  
ANISOU   90  CG2 THR A  15     7158   6239   3823   -399   1336   1461       C  
ATOM     91  N   GLU A  16     -10.210 -17.415  89.337  1.00 47.10           N  
ANISOU   91  N   GLU A  16     8075   5598   4223   -391   1148   1943       N  
ATOM     92  CA  GLU A  16      -8.846 -17.899  89.547  1.00 52.01           C  
ANISOU   92  CA  GLU A  16     8899   6109   4754    -62   1041   1976       C  
ATOM     93  C   GLU A  16      -8.162 -18.306  88.233  1.00 49.88           C  
ANISOU   93  C   GLU A  16     8785   5506   4661     48    945   1865       C  
ATOM     94  O   GLU A  16      -6.996 -17.984  88.016  1.00 50.95           O  
ANISOU   94  O   GLU A  16     8923   5703   4731    351    863   1769       O  
ATOM     95  CB  GLU A  16      -8.841 -19.073  90.522  1.00 61.43           C  
ANISOU   95  CB  GLU A  16    10289   7223   5830    -43   1039   2241       C  
ATOM     96  CG  GLU A  16      -7.461 -19.627  90.804  1.00 75.20           C  
ANISOU   96  CG  GLU A  16    12224   8891   7458    341    929   2278       C  
ATOM     97  CD  GLU A  16      -6.630 -18.708  91.682  1.00 85.91           C  
ANISOU   97  CD  GLU A  16    13394  10665   8583    611    895   2193       C  
ATOM     98  OE1 GLU A  16      -7.209 -17.855  92.395  1.00 87.63           O  
ANISOU   98  OE1 GLU A  16    13403  11203   8688    494    966   2154       O  
ATOM     99  OE2 GLU A  16      -5.385 -18.843  91.664  1.00 87.82           O  
ANISOU   99  OE2 GLU A  16    13678  10946   8745    951    787   2146       O  
ATOM    100  N   ARG A  17      -8.881 -19.011  87.365  1.00 46.13           N  
ANISOU  100  N   ARG A  17     8412   4727   4387   -189    946   1868       N  
ATOM    101  CA  ARG A  17      -8.326 -19.395  86.074  1.00 44.51           C  
ANISOU  101  CA  ARG A  17     8350   4231   4332    -86    855   1732       C  
ATOM    102  C   ARG A  17      -8.073 -18.159  85.194  1.00 42.07           C  
ANISOU  102  C   ARG A  17     7831   4064   4090    -47    849   1517       C  
ATOM    103  O   ARG A  17      -7.013 -18.049  84.579  1.00 46.45           O  
ANISOU  103  O   ARG A  17     8433   4583   4634    223    770   1426       O  
ATOM    104  CB  ARG A  17      -9.248 -20.384  85.360  1.00 42.83           C  
ANISOU  104  CB  ARG A  17     8274   3701   4299   -377    847   1749       C  
ATOM    105  CG  ARG A  17      -9.293 -21.765  86.015  1.00 47.31           C  
ANISOU  105  CG  ARG A  17     9133   4029   4815   -388    833   1960       C  
ATOM    106  CD  ARG A  17     -10.388 -22.632  85.420  1.00 53.65           C  
ANISOU  106  CD  ARG A  17    10035   4570   5780   -750    837   1980       C  
ATOM    107  NE  ARG A  17     -10.340 -24.012  85.900  1.00 66.93           N  
ANISOU  107  NE  ARG A  17    12060   5947   7425   -756    814   2171       N  
ATOM    108  CZ  ARG A  17     -11.126 -24.498  86.856  1.00 73.70           C  
ANISOU  108  CZ  ARG A  17    12934   6837   8233   -996    895   2416       C  
ATOM    109  NH1 ARG A  17     -12.025 -23.714  87.439  1.00 75.16           N  
ANISOU  109  NH1 ARG A  17    12786   7387   8385  -1222   1008   2488       N  
ATOM    110  NH2 ARG A  17     -11.017 -25.766  87.229  1.00 79.34           N  
ANISOU  110  NH2 ARG A  17    13999   7229   8918   -994    871   2596       N  
ATOM    111  N   LEU A  18      -9.040 -17.244  85.141  1.00 35.39           N  
ANISOU  111  N   LEU A  18     6747   3403   3298   -298    936   1446       N  
ATOM    112  CA  LEU A  18      -8.880 -15.993  84.399  1.00 32.16           C  
ANISOU  112  CA  LEU A  18     6078   3161   2980   -271    915   1218       C  
ATOM    113  C   LEU A  18      -7.605 -15.251  84.807  1.00 34.58           C  
ANISOU  113  C   LEU A  18     6245   3710   3182     28    829   1116       C  
ATOM    114  O   LEU A  18      -6.842 -14.763  83.956  1.00 29.64           O  
ANISOU  114  O   LEU A  18     5505   3114   2644    145    742    955       O  
ATOM    115  CB  LEU A  18     -10.097 -15.100  84.605  1.00 31.33           C  
ANISOU  115  CB  LEU A  18     5714   3287   2903   -508   1013   1157       C  
ATOM    116  CG  LEU A  18     -11.384 -15.471  83.865  1.00 46.60           C  
ANISOU  116  CG  LEU A  18     7632   5106   4968   -833   1075   1175       C  
ATOM    117  CD1 LEU A  18     -12.527 -14.502  84.211  1.00 40.79           C  
ANISOU  117  CD1 LEU A  18     6594   4704   4198   -979   1177   1120       C  
ATOM    118  CD2 LEU A  18     -11.127 -15.477  82.371  1.00 42.18           C  
ANISOU  118  CD2 LEU A  18     7081   4349   4597   -824    987   1015       C  
ATOM    119  N   ILE A  19      -7.371 -15.207  86.116  1.00 36.34           N  
ANISOU  119  N   ILE A  19     6476   4134   3198    132    851   1219       N  
ATOM    120  CA  ILE A  19      -6.199 -14.561  86.690  1.00 39.31           C  
ANISOU  120  CA  ILE A  19     6715   4791   3432    380    759   1129       C  
ATOM    121  C   ILE A  19      -4.924 -15.270  86.268  1.00 40.75           C  
ANISOU  121  C   ILE A  19     7017   4896   3571    664    651   1161       C  
ATOM    122  O   ILE A  19      -3.935 -14.622  85.916  1.00 32.10           O  
ANISOU  122  O   ILE A  19     5726   3999   2470    797    553   1010       O  
ATOM    123  CB  ILE A  19      -6.276 -14.525  88.220  1.00 36.07           C  
ANISOU  123  CB  ILE A  19     6313   4625   2769    445    802   1246       C  
ATOM    124  CG1 ILE A  19      -7.342 -13.525  88.673  1.00 38.27           C  
ANISOU  124  CG1 ILE A  19     6402   5096   3044    250    891   1146       C  
ATOM    125  CG2 ILE A  19      -4.937 -14.146  88.818  1.00 34.88           C  
ANISOU  125  CG2 ILE A  19     6060   4760   2434    716    680   1175       C  
ATOM    126  CD1 ILE A  19      -7.733 -13.692  90.149  1.00 36.06           C  
ANISOU  126  CD1 ILE A  19     6158   5049   2497    283    974   1301       C  
ATOM    127  N   GLN A  20      -4.955 -16.601  86.288  1.00 40.94           N  
ANISOU  127  N   GLN A  20     7369   4635   3550    756    669   1363       N  
ATOM    128  CA  GLN A  20      -3.783 -17.380  85.906  1.00 36.78           C  
ANISOU  128  CA  GLN A  20     7000   4026   2948   1107    571   1400       C  
ATOM    129  C   GLN A  20      -3.514 -17.202  84.425  1.00 34.90           C  
ANISOU  129  C   GLN A  20     6677   3683   2901   1108    517   1219       C  
ATOM    130  O   GLN A  20      -2.364 -17.117  84.005  1.00 44.87           O  
ANISOU  130  O   GLN A  20     7829   5121   4100   1383    425   1138       O  
ATOM    131  CB  GLN A  20      -3.966 -18.864  86.250  1.00 45.49           C  
ANISOU  131  CB  GLN A  20     8459   4800   4027   1174    582   1592       C  
ATOM    132  CG  GLN A  20      -3.875 -19.170  87.746  1.00 52.44           C  
ANISOU  132  CG  GLN A  20     9362   5850   4713   1254    599   1756       C  
ATOM    133  CD  GLN A  20      -2.639 -18.563  88.398  1.00 59.25           C  
ANISOU  133  CD  GLN A  20    10008   7151   5352   1582    513   1703       C  
ATOM    134  OE1 GLN A  20      -1.559 -18.541  87.807  1.00 55.87           O  
ANISOU  134  OE1 GLN A  20     9503   6836   4889   1862    418   1606       O  
ATOM    135  NE2 GLN A  20      -2.795 -18.067  89.626  1.00 58.19           N  
ANISOU  135  NE2 GLN A  20     9738   7314   5057   1537    539   1750       N  
ATOM    136  N   LEU A  21      -4.587 -17.147  83.645  1.00 33.56           N  
ANISOU  136  N   LEU A  21     6534   3279   2938    801    578   1162       N  
ATOM    137  CA  LEU A  21      -4.495 -16.828  82.224  1.00 34.04           C  
ANISOU  137  CA  LEU A  21     6481   3280   3174    765    537    981       C  
ATOM    138  C   LEU A  21      -3.844 -15.465  82.000  1.00 36.26           C  
ANISOU  138  C   LEU A  21     6374   3931   3471    781    491    808       C  
ATOM    139  O   LEU A  21      -2.947 -15.332  81.166  1.00 34.60           O  
ANISOU  139  O   LEU A  21     6054   3826   3268    950    422    715       O  
ATOM    140  CB  LEU A  21      -5.876 -16.851  81.572  1.00 38.12           C  
ANISOU  140  CB  LEU A  21     7037   3567   3880    406    609    948       C  
ATOM    141  CG  LEU A  21      -5.888 -16.284  80.155  1.00 38.71           C  
ANISOU  141  CG  LEU A  21     6936   3653   4118    351    573    754       C  
ATOM    142  CD1 LEU A  21      -5.107 -17.186  79.203  1.00 40.43           C  
ANISOU  142  CD1 LEU A  21     7356   3683   4325    609    494    718       C  
ATOM    143  CD2 LEU A  21      -7.309 -16.068  79.662  1.00 37.81           C  
ANISOU  143  CD2 LEU A  21     6772   3437   4158     -3    639    712       C  
ATOM    144  N   PHE A  22      -4.305 -14.457  82.743  1.00 34.84           N  
ANISOU  144  N   PHE A  22     6005   3949   3285    600    531    767       N  
ATOM    145  CA  PHE A  22      -3.734 -13.110  82.659  1.00 32.33           C  
ANISOU  145  CA  PHE A  22     5382   3925   2976    566    479    605       C  
ATOM    146  C   PHE A  22      -2.239 -13.139  83.000  1.00 28.04           C  
ANISOU  146  C   PHE A  22     4733   3666   2254    828    375    604       C  
ATOM    147  O   PHE A  22      -1.423 -12.582  82.271  1.00 31.13           O  
ANISOU  147  O   PHE A  22     4924   4233   2671    857    310    500       O  
ATOM    148  CB  PHE A  22      -4.498 -12.149  83.592  1.00 26.26           C  
ANISOU  148  CB  PHE A  22     4512   3282   2185    381    531    557       C  
ATOM    149  CG  PHE A  22      -3.881 -10.781  83.706  1.00 30.13           C  
ANISOU  149  CG  PHE A  22     4771   4019   2659    333    460    387       C  
ATOM    150  CD1 PHE A  22      -3.703  -9.990  82.586  1.00 28.54           C  
ANISOU  150  CD1 PHE A  22     4436   3797   2611    231    428    265       C  
ATOM    151  CD2 PHE A  22      -3.494 -10.284  84.941  1.00 32.88           C  
ANISOU  151  CD2 PHE A  22     5058   4609   2826    371    420    353       C  
ATOM    152  CE1 PHE A  22      -3.152  -8.719  82.694  1.00 31.24           C  
ANISOU  152  CE1 PHE A  22     4615   4313   2942    132    359    124       C  
ATOM    153  CE2 PHE A  22      -2.942  -9.024  85.058  1.00 34.82           C  
ANISOU  153  CE2 PHE A  22     5133   5039   3056    277    338    179       C  
ATOM    154  CZ  PHE A  22      -2.772  -8.238  83.933  1.00 33.41           C  
ANISOU  154  CZ  PHE A  22     4852   4795   3048    140    308     71       C  
ATOM    155  N   GLU A  23      -1.899 -13.811  84.098  1.00 30.20           N  
ANISOU  155  N   GLU A  23     5130   4018   2325   1017    363    736       N  
ATOM    156  CA  GLU A  23      -0.515 -14.020  84.514  1.00 39.67           C  
ANISOU  156  CA  GLU A  23     6231   5533   3307   1320    261    761       C  
ATOM    157  C   GLU A  23       0.321 -14.626  83.394  1.00 44.30           C  
ANISOU  157  C   GLU A  23     6820   6110   3903   1564    209    753       C  
ATOM    158  O   GLU A  23       1.408 -14.155  83.086  1.00 46.99           O  
ANISOU  158  O   GLU A  23     6888   6804   4160   1669    128    671       O  
ATOM    159  CB  GLU A  23      -0.457 -14.940  85.734  1.00 41.65           C  
ANISOU  159  CB  GLU A  23     6703   5786   3336   1540    271    954       C  
ATOM    160  CG  GLU A  23      -0.999 -14.346  87.020  1.00 48.10           C  
ANISOU  160  CG  GLU A  23     7470   6757   4048   1385    307    964       C  
ATOM    161  CD  GLU A  23      -0.027 -13.396  87.679  1.00 49.79           C  
ANISOU  161  CD  GLU A  23     7387   7442   4089   1428    196    829       C  
ATOM    162  OE1 GLU A  23       1.164 -13.406  87.302  1.00 50.63           O  
ANISOU  162  OE1 GLU A  23     7324   7803   4111   1613     92    785       O  
ATOM    163  OE2 GLU A  23      -0.451 -12.644  88.582  1.00 42.72           O  
ANISOU  163  OE2 GLU A  23     6420   6687   3123   1275    209    759       O  
ATOM    164  N   SER A  24      -0.201 -15.694  82.807  1.00 46.60           N  
ANISOU  164  N   SER A  24     7422   6010   4274   1647    255    835       N  
ATOM    165  CA  SER A  24       0.435 -16.370  81.687  1.00 43.46           C  
ANISOU  165  CA  SER A  24     7093   5544   3877   1911    213    807       C  
ATOM    166  C   SER A  24       0.668 -15.408  80.504  1.00 36.70           C  
ANISOU  166  C   SER A  24     5924   4863   3159   1752    198    637       C  
ATOM    167  O   SER A  24       1.760 -15.353  79.928  1.00 33.12           O  
ANISOU  167  O   SER A  24     5273   4711   2602   1979    138    589       O  
ATOM    168  CB  SER A  24      -0.428 -17.565  81.269  1.00 43.09           C  
ANISOU  168  CB  SER A  24     7486   4962   3925   1919    262    889       C  
ATOM    169  OG  SER A  24       0.204 -18.340  80.266  1.00 47.45           O  
ANISOU  169  OG  SER A  24     8175   5415   4438   2242    211    847       O  
ATOM    170  N   TRP A  25      -0.362 -14.640  80.165  1.00 30.20           N  
ANISOU  170  N   TRP A  25     5046   3885   2544   1377    259    561       N  
ATOM    171  CA  TRP A  25      -0.293 -13.659  79.085  1.00 27.28           C  
ANISOU  171  CA  TRP A  25     4421   3635   2308   1198    256    430       C  
ATOM    172  C   TRP A  25       0.756 -12.568  79.338  1.00 31.89           C  
ANISOU  172  C   TRP A  25     4651   4669   2797   1153    192    371       C  
ATOM    173  O   TRP A  25       1.450 -12.150  78.421  1.00 31.41           O  
ANISOU  173  O   TRP A  25     4374   4823   2737   1163    164    317       O  
ATOM    174  CB  TRP A  25      -1.671 -13.024  78.887  1.00 25.46           C  
ANISOU  174  CB  TRP A  25     4223   3167   2285    844    330    381       C  
ATOM    175  CG  TRP A  25      -1.709 -11.941  77.858  1.00 28.25           C  
ANISOU  175  CG  TRP A  25     4355   3611   2769    663    332    272       C  
ATOM    176  CD1 TRP A  25      -1.987 -12.086  76.534  1.00 25.70           C  
ANISOU  176  CD1 TRP A  25     4043   3171   2551    652    347    226       C  
ATOM    177  CD2 TRP A  25      -1.482 -10.541  78.072  1.00 29.74           C  
ANISOU  177  CD2 TRP A  25     4316   4003   2981    461    313    203       C  
ATOM    178  NE1 TRP A  25      -1.944 -10.866  75.904  1.00 25.84           N  
ANISOU  178  NE1 TRP A  25     3844   3322   2653    471    349    161       N  
ATOM    179  CE2 TRP A  25      -1.639  -9.900  76.825  1.00 27.54           C  
ANISOU  179  CE2 TRP A  25     3932   3703   2829    340    327    147       C  
ATOM    180  CE3 TRP A  25      -1.178  -9.766  79.199  1.00 31.68           C  
ANISOU  180  CE3 TRP A  25     4467   4427   3143    367    278    177       C  
ATOM    181  CZ2 TRP A  25      -1.479  -8.522  76.666  1.00 23.14           C  
ANISOU  181  CZ2 TRP A  25     3208   3259   2326    123    311     91       C  
ATOM    182  CZ3 TRP A  25      -1.018  -8.397  79.044  1.00 26.31           C  
ANISOU  182  CZ3 TRP A  25     3628   3850   2521    139    251     86       C  
ATOM    183  CH2 TRP A  25      -1.175  -7.787  77.789  1.00 30.32           C  
ANISOU  183  CH2 TRP A  25     4064   4290   3165     15    270     56       C  
ATOM    184  N   MET A  26       0.857 -12.097  80.578  1.00 33.00           N  
ANISOU  184  N   MET A  26     4731   4966   2841   1076    167    380       N  
ATOM    185  CA  MET A  26       1.882 -11.119  80.942  1.00 32.93           C  
ANISOU  185  CA  MET A  26     4408   5386   2718    994     83    310       C  
ATOM    186  C   MET A  26       3.271 -11.671  80.654  1.00 39.31           C  
ANISOU  186  C   MET A  26     5036   6576   3323   1311     10    351       C  
ATOM    187  O   MET A  26       4.130 -10.972  80.116  1.00 41.45           O  
ANISOU  187  O   MET A  26     5001   7193   3557   1216    -39    296       O  
ATOM    188  CB  MET A  26       1.787 -10.738  82.418  1.00 34.91           C  
ANISOU  188  CB  MET A  26     4665   5750   2848    922     53    301       C  
ATOM    189  CG  MET A  26       0.539  -9.969  82.804  1.00 38.18           C  
ANISOU  189  CG  MET A  26     5192   5906   3411    634    118    233       C  
ATOM    190  SD  MET A  26       0.595  -9.532  84.547  1.00 35.78           S  
ANISOU  190  SD  MET A  26     4878   5816   2902    609     70    197       S  
ATOM    191  CE  MET A  26       2.125  -8.610  84.614  1.00 37.32           C  
ANISOU  191  CE  MET A  26     4734   6490   2956    516    -86     74       C  
ATOM    192  N   LEU A  27       3.482 -12.932  81.016  1.00 35.91           N  
ANISOU  192  N   LEU A  27     4804   6094   2746   1693      5    458       N  
ATOM    193  CA  LEU A  27       4.774 -13.576  80.796  1.00 46.38           C  
ANISOU  193  CA  LEU A  27     5984   7801   3837   2100    -64    502       C  
ATOM    194  C   LEU A  27       5.076 -13.732  79.314  1.00 47.38           C  
ANISOU  194  C   LEU A  27     6026   7951   4023   2198    -43    459       C  
ATOM    195  O   LEU A  27       6.170 -13.410  78.862  1.00 51.57           O  
ANISOU  195  O   LEU A  27     6210   8971   4413   2290    -92    434       O  
ATOM    196  CB  LEU A  27       4.818 -14.940  81.479  1.00 54.67           C  
ANISOU  196  CB  LEU A  27     7360   8695   4718   2534    -70    639       C  
ATOM    197  CG  LEU A  27       5.178 -14.927  82.960  1.00 59.68           C  
ANISOU  197  CG  LEU A  27     7954   9586   5133   2627   -127    711       C  
ATOM    198  CD1 LEU A  27       5.389 -16.346  83.453  1.00 68.19           C  
ANISOU  198  CD1 LEU A  27     9334  10469   6105   3055   -107    832       C  
ATOM    199  CD2 LEU A  27       6.424 -14.085  83.189  1.00 61.46           C  
ANISOU  199  CD2 LEU A  27     7687  10463   5200   2583   -224    621       C  
ATOM    200  N   LYS A  28       4.095 -14.225  78.568  1.00 47.32           N  
ANISOU  200  N   LYS A  28     6318   7455   4205   2165     28    449       N  
ATOM    201  CA  LYS A  28       4.220 -14.378  77.127  1.00 46.86           C  
ANISOU  201  CA  LYS A  28     6218   7382   4204   2249     51    391       C  
ATOM    202  C   LYS A  28       4.650 -13.076  76.463  1.00 49.14           C  
ANISOU  202  C   LYS A  28     6100   8026   4547   1941     50    328       C  
ATOM    203  O   LYS A  28       5.433 -13.094  75.517  1.00 55.79           O  
ANISOU  203  O   LYS A  28     6725   9183   5289   2099     43    313       O  
ATOM    204  CB  LYS A  28       2.897 -14.865  76.531  1.00 46.18           C  
ANISOU  204  CB  LYS A  28     6494   6715   4338   2125    117    364       C  
ATOM    205  CG  LYS A  28       2.878 -14.921  75.011  1.00 61.64           C  
ANISOU  205  CG  LYS A  28     8413   8648   6360   2169    137    280       C  
ATOM    206  CD  LYS A  28       1.514 -15.339  74.472  1.00 68.69           C  
ANISOU  206  CD  LYS A  28     9633   9006   7460   1992    184    235       C  
ATOM    207  CE  LYS A  28       1.495 -15.360  72.943  1.00 70.48           C  
ANISOU  207  CE  LYS A  28     9809   9246   7723   2044    194    136       C  
ATOM    208  NZ  LYS A  28       0.197 -15.860  72.400  1.00 67.46           N  
ANISOU  208  NZ  LYS A  28     9737   8383   7511   1879    217     73       N  
ATOM    209  N   HIS A  29       4.161 -11.946  76.972  1.00 40.45           N  
ANISOU  209  N   HIS A  29     4909   6878   3581   1512     58    298       N  
ATOM    210  CA  HIS A  29       4.401 -10.660  76.309  1.00 36.57           C  
ANISOU  210  CA  HIS A  29     4128   6595   3173   1163     60    254       C  
ATOM    211  C   HIS A  29       5.331  -9.732  77.078  1.00 43.25           C  
ANISOU  211  C   HIS A  29     4661   7882   3892    958    -19    243       C  
ATOM    212  O   HIS A  29       5.418  -8.545  76.764  1.00 38.58           O  
ANISOU  212  O   HIS A  29     3898   7374   3385    579    -26    210       O  
ATOM    213  CB  HIS A  29       3.071  -9.957  76.042  1.00 34.13           C  
ANISOU  213  CB  HIS A  29     3994   5848   3127    820    124    209       C  
ATOM    214  CG  HIS A  29       2.227 -10.665  75.033  1.00 33.82           C  
ANISOU  214  CG  HIS A  29     4174   5467   3208    934    187    201       C  
ATOM    215  ND1 HIS A  29       1.102 -11.383  75.375  1.00 41.35           N  
ANISOU  215  ND1 HIS A  29     5449   6001   4260    963    226    201       N  
ATOM    216  CD2 HIS A  29       2.372 -10.811  73.697  1.00 33.35           C  
ANISOU  216  CD2 HIS A  29     4052   5460   3161   1019    212    188       C  
ATOM    217  CE1 HIS A  29       0.573 -11.915  74.289  1.00 37.08           C  
ANISOU  217  CE1 HIS A  29     5039   5251   3800   1032    259    172       C  
ATOM    218  NE2 HIS A  29       1.322 -11.580  73.256  1.00 42.62           N  
ANISOU  218  NE2 HIS A  29     5519   6229   4446   1089    250    156       N  
ATOM    219  N   ASN A  30       6.033 -10.289  78.063  1.00 47.38           N  
ANISOU  219  N   ASN A  30     5126   8681   4196   1207    -86    272       N  
ATOM    220  CA  ASN A  30       7.011  -9.552  78.868  1.00 58.08           C  
ANISOU  220  CA  ASN A  30     6160  10531   5379   1042   -186    247       C  
ATOM    221  C   ASN A  30       6.481  -8.232  79.398  1.00 51.00           C  
ANISOU  221  C   ASN A  30     5282   9462   4632    537   -208    157       C  
ATOM    222  O   ASN A  30       7.142  -7.197  79.319  1.00 47.36           O  
ANISOU  222  O   ASN A  30     4555   9299   4140    197   -270    113       O  
ATOM    223  CB  ASN A  30       8.281  -9.318  78.062  1.00 62.45           C  
ANISOU  223  CB  ASN A  30     6287  11672   5767   1062   -221    275       C  
ATOM    224  CG  ASN A  30       9.051 -10.589  77.848  1.00 62.82           C  
ANISOU  224  CG  ASN A  30     6269  12032   5569   1649   -230    343       C  
ATOM    225  OD1 ASN A  30       9.313 -10.990  76.715  1.00 63.22           O  
ANISOU  225  OD1 ASN A  30     6251  12180   5590   1858   -180    368       O  
ATOM    226  ND2 ASN A  30       9.395 -11.254  78.942  1.00 62.55           N  
ANISOU  226  ND2 ASN A  30     6294  12093   5379   1937   -270    360       N  
ATOM    227  N   LYS A  31       5.272  -8.291  79.934  1.00 48.47           N  
ANISOU  227  N   LYS A  31     5296   8660   4461    493   -157    130       N  
ATOM    228  CA  LYS A  31       4.627  -7.125  80.499  1.00 49.47           C  
ANISOU  228  CA  LYS A  31     5508   8576   4711    109   -171     26       C  
ATOM    229  C   LYS A  31       4.980  -7.006  81.981  1.00 48.56           C  
ANISOU  229  C   LYS A  31     5360   8685   4406    113   -264    -30       C  
ATOM    230  O   LYS A  31       4.721  -7.916  82.761  1.00 58.85           O  
ANISOU  230  O   LYS A  31     6815   9943   5604    404   -248     29       O  
ATOM    231  CB  LYS A  31       3.106  -7.204  80.282  1.00 40.87           C  
ANISOU  231  CB  LYS A  31     4747   6934   3848     81    -61     21       C  
ATOM    232  CG  LYS A  31       2.658  -6.647  78.931  1.00 43.60           C  
ANISOU  232  CG  LYS A  31     5099   7069   4397    -97      1     19       C  
ATOM    233  CD  LYS A  31       2.741  -5.121  78.928  1.00 50.96           C  
ANISOU  233  CD  LYS A  31     5969   7990   5404   -496    -45    -68       C  
ATOM    234  CE  LYS A  31       3.012  -4.544  77.549  1.00 48.86           C  
ANISOU  234  CE  LYS A  31     5584   7745   5237   -668    -19    -20       C  
ATOM    235  NZ  LYS A  31       1.890  -4.788  76.616  1.00 45.13           N  
ANISOU  235  NZ  LYS A  31     5295   6912   4940   -580     85     13       N  
ATOM    236  N   ILE A  32       5.621  -5.902  82.351  1.00 42.80           N  
ANISOU  236  N   ILE A  32     4439   8211   3613   -218   -369   -137       N  
ATOM    237  CA  ILE A  32       5.821  -5.577  83.754  1.00 46.58           C  
ANISOU  237  CA  ILE A  32     4911   8868   3920   -279   -471   -238       C  
ATOM    238  C   ILE A  32       5.166  -4.225  84.027  1.00 52.03           C  
ANISOU  238  C   ILE A  32     5764   9253   4754   -684   -495   -404       C  
ATOM    239  O   ILE A  32       5.357  -3.259  83.282  1.00 56.43           O  
ANISOU  239  O   ILE A  32     6265   9741   5436  -1026   -517   -451       O  
ATOM    240  CB  ILE A  32       7.323  -5.560  84.162  1.00 64.80           C  
ANISOU  240  CB  ILE A  32     6833  11843   5944   -282   -616   -251       C  
ATOM    241  CG1 ILE A  32       8.112  -4.500  83.387  1.00 74.35           C  
ANISOU  241  CG1 ILE A  32     7768  13286   7195   -720   -682   -302       C  
ATOM    242  CG2 ILE A  32       7.945  -6.943  83.982  1.00 60.23           C  
ANISOU  242  CG2 ILE A  32     6130  11570   5184    225   -595    -91       C  
ATOM    243  CD1 ILE A  32       8.446  -3.259  84.204  1.00 78.92           C  
ANISOU  243  CD1 ILE A  32     8294  13982   7709  -1181   -829   -487       C  
ATOM    244  N   TYR A  33       4.371  -4.174  85.090  1.00 42.06           N  
ANISOU  244  N   TYR A  33     4726   7797   3455   -619   -486   -483       N  
ATOM    245  CA  TYR A  33       3.552  -3.008  85.378  1.00 39.41           C  
ANISOU  245  CA  TYR A  33     4615   7117   3242   -887   -491   -650       C  
ATOM    246  C   TYR A  33       4.180  -2.103  86.436  1.00 47.55           C  
ANISOU  246  C   TYR A  33     5592   8383   4092  -1130   -658   -851       C  
ATOM    247  O   TYR A  33       5.080  -2.521  87.161  1.00 55.10           O  
ANISOU  247  O   TYR A  33     6337   9795   4803  -1040   -759   -853       O  
ATOM    248  CB  TYR A  33       2.161  -3.463  85.813  1.00 35.05           C  
ANISOU  248  CB  TYR A  33     4340   6224   2753   -659   -361   -623       C  
ATOM    249  CG  TYR A  33       1.386  -4.120  84.699  1.00 30.71           C  
ANISOU  249  CG  TYR A  33     3877   5382   2411   -526   -214   -471       C  
ATOM    250  CD1 TYR A  33       1.326  -3.538  83.442  1.00 30.80           C  
ANISOU  250  CD1 TYR A  33     3872   5210   2620   -710   -188   -465       C  
ATOM    251  CD2 TYR A  33       0.716  -5.323  84.900  1.00 37.92           C  
ANISOU  251  CD2 TYR A  33     4901   6202   3307   -238   -108   -331       C  
ATOM    252  CE1 TYR A  33       0.616  -4.130  82.409  1.00 30.70           C  
ANISOU  252  CE1 TYR A  33     3928   4964   2774   -588    -68   -348       C  
ATOM    253  CE2 TYR A  33       0.002  -5.921  83.877  1.00 34.05           C  
ANISOU  253  CE2 TYR A  33     4496   5445   2995   -159      7   -219       C  
ATOM    254  CZ  TYR A  33      -0.035  -5.320  82.628  1.00 27.22           C  
ANISOU  254  CZ  TYR A  33     3589   4439   2316   -323     21   -241       C  
ATOM    255  OH  TYR A  33      -0.732  -5.895  81.604  1.00 26.42           O  
ANISOU  255  OH  TYR A  33     3560   4109   2368   -245    120   -152       O  
ATOM    256  N   LYS A  34       3.699  -0.863  86.516  1.00 51.62           N  
ANISOU  256  N   LYS A  34     6316   8585   4712  -1421   -696  -1031       N  
ATOM    257  CA  LYS A  34       4.283   0.137  87.410  1.00 51.04           C  
ANISOU  257  CA  LYS A  34     6247   8661   4484  -1718   -875  -1264       C  
ATOM    258  C   LYS A  34       4.160  -0.288  88.865  1.00 59.03           C  
ANISOU  258  C   LYS A  34     7289   9902   5237  -1475   -922  -1354       C  
ATOM    259  O   LYS A  34       5.153  -0.352  89.589  1.00 65.56           O  
ANISOU  259  O   LYS A  34     7899  11185   5827  -1529  -1066  -1419       O  
ATOM    260  CB  LYS A  34       3.620   1.505  87.213  1.00 48.46           C  
ANISOU  260  CB  LYS A  34     6248   7841   4324  -2007   -897  -1444       C  
ATOM    261  CG  LYS A  34       4.265   2.607  88.042  1.00 58.36           C  
ANISOU  261  CG  LYS A  34     7562   9135   5479  -2312  -1078  -1670       C  
ATOM    262  CD  LYS A  34       3.230   3.451  88.777  1.00 60.29           C  
ANISOU  262  CD  LYS A  34     8211   8949   5748  -2235  -1084  -1886       C  
ATOM    263  CE  LYS A  34       3.891   4.390  89.784  1.00 60.90           C  
ANISOU  263  CE  LYS A  34     8344   9062   5732  -2409  -1262  -2089       C  
ATOM    264  NZ  LYS A  34       2.878   5.127  90.598  1.00 64.14           N  
ANISOU  264  NZ  LYS A  34     9138   9113   6119  -2242  -1280  -2318       N  
ATOM    265  N   ASN A  35       2.932  -0.577  89.286  1.00 57.57           N  
ANISOU  265  N   ASN A  35     7351   9438   5085  -1204   -794  -1344       N  
ATOM    266  CA  ASN A  35       2.672  -1.060  90.638  1.00 56.82           C  
ANISOU  266  CA  ASN A  35     7299   9555   4734   -940   -801  -1386       C  
ATOM    267  C   ASN A  35       1.552  -2.100  90.652  1.00 54.53           C  
ANISOU  267  C   ASN A  35     7131   9093   4497   -581   -599  -1181       C  
ATOM    268  O   ASN A  35       1.068  -2.521  89.602  1.00 51.51           O  
ANISOU  268  O   ASN A  35     6775   8457   4341   -536   -471  -1020       O  
ATOM    269  CB  ASN A  35       2.337   0.109  91.576  1.00 52.59           C  
ANISOU  269  CB  ASN A  35     6983   8912   4088  -1090   -906  -1695       C  
ATOM    270  CG  ASN A  35       1.255   1.020  91.023  1.00 52.01           C  
ANISOU  270  CG  ASN A  35     7217   8298   4246  -1176   -825  -1800       C  
ATOM    271  OD1 ASN A  35       0.279   0.564  90.435  1.00 42.51           O  
ANISOU  271  OD1 ASN A  35     6095   6846   3210   -982   -647  -1641       O  
ATOM    272  ND2 ASN A  35       1.422   2.322  91.225  1.00 61.73           N  
ANISOU  272  ND2 ASN A  35     8633   9332   5487  -1449   -963  -2060       N  
ATOM    273  N   ILE A  36       1.138  -2.517  91.841  1.00 53.45           N  
ANISOU  273  N   ILE A  36     7063   9111   4133   -350   -573  -1182       N  
ATOM    274  CA  ILE A  36       0.110  -3.541  91.940  1.00 52.19           C  
ANISOU  274  CA  ILE A  36     7009   8826   3995    -67   -383   -962       C  
ATOM    275  C   ILE A  36      -1.278  -3.004  91.540  1.00 43.12           C  
ANISOU  275  C   ILE A  36     6063   7278   3042    -99   -247  -1016       C  
ATOM    276  O   ILE A  36      -2.071  -3.714  90.916  1.00 38.79           O  
ANISOU  276  O   ILE A  36     5556   6533   2648     -3    -92   -824       O  
ATOM    277  CB  ILE A  36       0.053  -4.144  93.363  1.00 64.24           C  
ANISOU  277  CB  ILE A  36     8548  10669   5191    182   -380   -912       C  
ATOM    278  CG1 ILE A  36      -0.980  -5.264  93.412  1.00 70.19           C  
ANISOU  278  CG1 ILE A  36     9417  11283   5970    410   -177   -640       C  
ATOM    279  CG2 ILE A  36      -0.253  -3.081  94.411  1.00 66.56           C  
ANISOU  279  CG2 ILE A  36     8949  11040   5301    124   -458  -1200       C  
ATOM    280  CD1 ILE A  36      -0.922  -6.156  92.203  1.00 72.65           C  
ANISOU  280  CD1 ILE A  36     9706  11383   6513    434    -97   -413       C  
ATOM    281  N   ASP A  37      -1.565  -1.754  91.879  1.00 39.02           N  
ANISOU  281  N   ASP A  37     5677   6645   2504   -226   -315  -1285       N  
ATOM    282  CA  ASP A  37      -2.837  -1.155  91.506  1.00 39.94           C  
ANISOU  282  CA  ASP A  37     5979   6423   2772   -199   -199  -1352       C  
ATOM    283  C   ASP A  37      -2.982  -1.150  89.980  1.00 40.83           C  
ANISOU  283  C   ASP A  37     6074   6237   3203   -323   -139  -1236       C  
ATOM    284  O   ASP A  37      -4.092  -1.257  89.440  1.00 38.56           O  
ANISOU  284  O   ASP A  37     5857   5738   3055   -232      3  -1158       O  
ATOM    285  CB  ASP A  37      -2.946   0.254  92.104  1.00 40.66           C  
ANISOU  285  CB  ASP A  37     6265   6415   2769   -285   -314  -1688       C  
ATOM    286  CG  ASP A  37      -3.049   0.222  93.615  1.00 48.34           C  
ANISOU  286  CG  ASP A  37     7271   7693   3401   -106   -348  -1815       C  
ATOM    287  OD1 ASP A  37      -3.407  -0.858  94.128  1.00 54.86           O  
ANISOU  287  OD1 ASP A  37     8000   8749   4095    110   -227  -1601       O  
ATOM    288  OD2 ASP A  37      -2.772   1.245  94.287  1.00 50.36           O  
ANISOU  288  OD2 ASP A  37     7670   7944   3522   -186   -494  -2108       O  
ATOM    289  N   GLU A  38      -1.846  -1.078  89.290  1.00 43.33           N  
ANISOU  289  N   GLU A  38     6262   6596   3605   -522   -246  -1213       N  
ATOM    290  CA  GLU A  38      -1.830  -1.149  87.837  1.00 33.15           C  
ANISOU  290  CA  GLU A  38     4926   5092   2578   -627   -194  -1087       C  
ATOM    291  C   GLU A  38      -2.174  -2.549  87.351  1.00 32.38           C  
ANISOU  291  C   GLU A  38     4738   5023   2541   -432    -59   -828       C  
ATOM    292  O   GLU A  38      -2.956  -2.719  86.410  1.00 31.37           O  
ANISOU  292  O   GLU A  38     4655   4660   2605   -412     49   -738       O  
ATOM    293  CB  GLU A  38      -0.463  -0.727  87.291  1.00 50.70           C  
ANISOU  293  CB  GLU A  38     6997   7438   4828   -895   -338  -1118       C  
ATOM    294  CG  GLU A  38      -0.336  -0.774  85.773  1.00 48.53           C  
ANISOU  294  CG  GLU A  38     6652   7000   4787  -1002   -286   -980       C  
ATOM    295  CD  GLU A  38      -1.149   0.294  85.055  1.00 57.12           C  
ANISOU  295  CD  GLU A  38     7956   7680   6067  -1122   -248  -1058       C  
ATOM    296  OE1 GLU A  38      -1.667   1.229  85.712  1.00 57.00           O  
ANISOU  296  OE1 GLU A  38     8163   7488   6006  -1147   -286  -1250       O  
ATOM    297  OE2 GLU A  38      -1.259   0.196  83.814  1.00 61.68           O  
ANISOU  297  OE2 GLU A  38     8494   8121   6823  -1159   -183   -928       O  
ATOM    298  N   LYS A  39      -1.581  -3.550  87.990  1.00 35.63           N  
ANISOU  298  N   LYS A  39     5045   5715   2779   -286    -77   -712       N  
ATOM    299  CA  LYS A  39      -1.816  -4.928  87.606  1.00 34.35           C  
ANISOU  299  CA  LYS A  39     4864   5535   2654   -100     31   -470       C  
ATOM    300  C   LYS A  39      -3.290  -5.305  87.726  1.00 36.99           C  
ANISOU  300  C   LYS A  39     5342   5669   3044    -12    191   -390       C  
ATOM    301  O   LYS A  39      -3.836  -5.963  86.844  1.00 38.37           O  
ANISOU  301  O   LYS A  39     5542   5658   3379      4    286   -255       O  
ATOM    302  CB  LYS A  39      -0.961  -5.860  88.455  1.00 33.60           C  
ANISOU  302  CB  LYS A  39     4690   5761   2317     87    -24   -361       C  
ATOM    303  CG  LYS A  39      -1.073  -7.310  88.066  1.00 31.30           C  
ANISOU  303  CG  LYS A  39     4447   5397   2049    294     66   -112       C  
ATOM    304  CD  LYS A  39       0.207  -8.044  88.404  1.00 41.60           C  
ANISOU  304  CD  LYS A  39     5634   7022   3149    491    -31    -20       C  
ATOM    305  CE  LYS A  39       0.040  -9.539  88.262  1.00 42.07           C  
ANISOU  305  CE  LYS A  39     5841   6960   3186    753     53    228       C  
ATOM    306  NZ  LYS A  39       1.338 -10.260  88.430  1.00 50.66           N  
ANISOU  306  NZ  LYS A  39     6822   8358   4067   1023    -46    320       N  
ATOM    307  N   ILE A  40      -3.927  -4.867  88.809  1.00 30.50           N  
ANISOU  307  N   ILE A  40     4595   4922   2070     35    216   -485       N  
ATOM    308  CA  ILE A  40      -5.351  -5.093  89.017  1.00 30.08           C  
ANISOU  308  CA  ILE A  40     4626   4776   2028    105    372   -419       C  
ATOM    309  C   ILE A  40      -6.189  -4.385  87.949  1.00 28.50           C  
ANISOU  309  C   ILE A  40     4454   4318   2057     15    426   -493       C  
ATOM    310  O   ILE A  40      -7.054  -4.988  87.341  1.00 29.78           O  
ANISOU  310  O   ILE A  40     4611   4371   2334     19    542   -358       O  
ATOM    311  CB  ILE A  40      -5.791  -4.628  90.433  1.00 32.27           C  
ANISOU  311  CB  ILE A  40     4953   5259   2047    208    383   -533       C  
ATOM    312  CG1 ILE A  40      -4.968  -5.357  91.494  1.00 39.95           C  
ANISOU  312  CG1 ILE A  40     5894   6522   2765    321    327   -439       C  
ATOM    313  CG2 ILE A  40      -7.296  -4.865  90.640  1.00 32.26           C  
ANISOU  313  CG2 ILE A  40     4983   5250   2026    283    561   -447       C  
ATOM    314  CD1 ILE A  40      -5.103  -4.787  92.902  1.00 36.62           C  
ANISOU  314  CD1 ILE A  40     5507   6360   2048    423    296   -593       C  
ATOM    315  N   TYR A  41      -5.912  -3.112  87.704  1.00 29.11           N  
ANISOU  315  N   TYR A  41     4575   4294   2190    -76    333   -702       N  
ATOM    316  CA  TYR A  41      -6.578  -2.380  86.632  1.00 27.69           C  
ANISOU  316  CA  TYR A  41     4446   3860   2215   -132    369   -758       C  
ATOM    317  C   TYR A  41      -6.403  -3.104  85.288  1.00 27.96           C  
ANISOU  317  C   TYR A  41     4393   3778   2451   -203    401   -589       C  
ATOM    318  O   TYR A  41      -7.362  -3.273  84.533  1.00 24.47           O  
ANISOU  318  O   TYR A  41     3947   3217   2133   -179    497   -524       O  
ATOM    319  CB  TYR A  41      -6.043  -0.942  86.553  1.00 30.45           C  
ANISOU  319  CB  TYR A  41     4911   4069   2589   -252    238   -983       C  
ATOM    320  CG  TYR A  41      -6.538  -0.162  85.350  1.00 40.16           C  
ANISOU  320  CG  TYR A  41     6223   5011   4024   -304    259  -1007       C  
ATOM    321  CD1 TYR A  41      -7.785   0.449  85.355  1.00 46.29           C  
ANISOU  321  CD1 TYR A  41     7116   5671   4800   -142    338  -1085       C  
ATOM    322  CD2 TYR A  41      -5.762  -0.049  84.200  1.00 41.89           C  
ANISOU  322  CD2 TYR A  41     6390   5117   4410   -485    205   -938       C  
ATOM    323  CE1 TYR A  41      -8.246   1.157  84.250  1.00 50.22           C  
ANISOU  323  CE1 TYR A  41     7699   5920   5462   -144    353  -1090       C  
ATOM    324  CE2 TYR A  41      -6.214   0.657  83.090  1.00 47.19           C  
ANISOU  324  CE2 TYR A  41     7147   5536   5248   -518    227   -933       C  
ATOM    325  CZ  TYR A  41      -7.456   1.258  83.119  1.00 51.98           C  
ANISOU  325  CZ  TYR A  41     7892   6005   5855   -340    297  -1008       C  
ATOM    326  OH  TYR A  41      -7.910   1.955  82.018  1.00 54.30           O  
ANISOU  326  OH  TYR A  41     8280   6063   6290   -330    315   -988       O  
ATOM    327  N   ARG A  42      -5.182  -3.548  85.002  1.00 25.41           N  
ANISOU  327  N   ARG A  42     3986   3533   2136   -270    318   -528       N  
ATOM    328  CA  ARG A  42      -4.882  -4.220  83.743  1.00 25.85           C  
ANISOU  328  CA  ARG A  42     3966   3510   2346   -299    337   -395       C  
ATOM    329  C   ARG A  42      -5.635  -5.544  83.605  1.00 23.01           C  
ANISOU  329  C   ARG A  42     3623   3114   2004   -193    449   -224       C  
ATOM    330  O   ARG A  42      -6.087  -5.896  82.512  1.00 23.94           O  
ANISOU  330  O   ARG A  42     3733   3090   2271   -216    499   -160       O  
ATOM    331  CB  ARG A  42      -3.374  -4.461  83.605  1.00 24.47           C  
ANISOU  331  CB  ARG A  42     3670   3513   2115   -337    226   -369       C  
ATOM    332  CG  ARG A  42      -2.579  -3.184  83.334  1.00 34.02           C  
ANISOU  332  CG  ARG A  42     4838   4736   3354   -546    114   -506       C  
ATOM    333  CD  ARG A  42      -3.005  -2.490  82.042  1.00 31.54           C  
ANISOU  333  CD  ARG A  42     4565   4178   3242   -660    148   -508       C  
ATOM    334  NE  ARG A  42      -2.447  -1.136  81.958  1.00 28.30           N  
ANISOU  334  NE  ARG A  42     4200   3702   2851   -894     48   -634       N  
ATOM    335  CZ  ARG A  42      -2.859  -0.200  81.108  1.00 27.35           C  
ANISOU  335  CZ  ARG A  42     4193   3326   2872  -1003     61   -657       C  
ATOM    336  NH1 ARG A  42      -3.843  -0.452  80.245  1.00 25.48           N  
ANISOU  336  NH1 ARG A  42     3993   2928   2760   -877    168   -575       N  
ATOM    337  NH2 ARG A  42      -2.289   0.997  81.130  1.00 32.27           N  
ANISOU  337  NH2 ARG A  42     4909   3852   3500  -1248    -41   -760       N  
ATOM    338  N   PHE A  43      -5.760  -6.275  84.710  1.00 24.84           N  
ANISOU  338  N   PHE A  43     3894   3472   2072    -96    482   -146       N  
ATOM    339  CA  PHE A  43      -6.531  -7.508  84.700  1.00 27.09           C  
ANISOU  339  CA  PHE A  43     4242   3691   2362    -53    588     31       C  
ATOM    340  C   PHE A  43      -7.997  -7.227  84.356  1.00 23.46           C  
ANISOU  340  C   PHE A  43     3779   3143   1994   -124    698     17       C  
ATOM    341  O   PHE A  43      -8.625  -7.991  83.630  1.00 24.89           O  
ANISOU  341  O   PHE A  43     3973   3206   2277   -182    760    120       O  
ATOM    342  CB  PHE A  43      -6.427  -8.248  86.048  1.00 25.86           C  
ANISOU  342  CB  PHE A  43     4149   3694   1984     51    612    145       C  
ATOM    343  CG  PHE A  43      -7.404  -9.386  86.172  1.00 26.43           C  
ANISOU  343  CG  PHE A  43     4318   3675   2048     27    735    341       C  
ATOM    344  CD1 PHE A  43      -7.227 -10.552  85.443  1.00 26.30           C  
ANISOU  344  CD1 PHE A  43     4407   3466   2119     29    740    485       C  
ATOM    345  CD2 PHE A  43      -8.542  -9.254  86.960  1.00 27.46           C  
ANISOU  345  CD2 PHE A  43     4439   3914   2078    -14    846    374       C  
ATOM    346  CE1 PHE A  43      -8.150 -11.591  85.523  1.00 27.33           C  
ANISOU  346  CE1 PHE A  43     4665   3468   2252    -64    842    664       C  
ATOM    347  CE2 PHE A  43      -9.457 -10.299  87.057  1.00 42.28           C  
ANISOU  347  CE2 PHE A  43     6388   5734   3943   -109    962    576       C  
ATOM    348  CZ  PHE A  43      -9.254 -11.465  86.335  1.00 28.44           C  
ANISOU  348  CZ  PHE A  43     4771   3741   2296   -161    954    722       C  
ATOM    349  N   GLU A  44      -8.542  -6.128  84.875  1.00 27.23           N  
ANISOU  349  N   GLU A  44     4239   3695   2414   -107    712   -123       N  
ATOM    350  CA  GLU A  44      -9.936  -5.790  84.606  1.00 25.82           C  
ANISOU  350  CA  GLU A  44     4021   3512   2278   -113    814   -143       C  
ATOM    351  C   GLU A  44     -10.192  -5.516  83.125  1.00 22.39           C  
ANISOU  351  C   GLU A  44     3548   2906   2051   -174    804   -166       C  
ATOM    352  O   GLU A  44     -11.210  -5.926  82.582  1.00 23.22           O  
ANISOU  352  O   GLU A  44     3593   3015   2215   -215    885    -99       O  
ATOM    353  CB  GLU A  44     -10.360  -4.571  85.424  1.00 27.21           C  
ANISOU  353  CB  GLU A  44     4218   3796   2327     -4    816   -318       C  
ATOM    354  CG  GLU A  44     -10.730  -4.896  86.833  1.00 29.67           C  
ANISOU  354  CG  GLU A  44     4527   4349   2399     79    883   -279       C  
ATOM    355  CD  GLU A  44     -12.140  -5.379  86.899  1.00 41.08           C  
ANISOU  355  CD  GLU A  44     5871   5939   3797     76   1036   -161       C  
ATOM    356  OE1 GLU A  44     -13.076  -4.543  86.893  1.00 59.79           O  
ANISOU  356  OE1 GLU A  44     8186   8407   6125    186   1089   -275       O  
ATOM    357  OE2 GLU A  44     -12.320  -6.596  86.923  1.00 30.55           O  
ANISOU  357  OE2 GLU A  44     4518   4627   2462    -38   1101     48       O  
ATOM    358  N   ILE A  45      -9.267  -4.791  82.502  1.00 21.65           N  
ANISOU  358  N   ILE A  45     3478   2700   2047   -195    703   -257       N  
ATOM    359  CA  ILE A  45      -9.340  -4.462  81.102  1.00 22.11           C  
ANISOU  359  CA  ILE A  45     3508   2616   2276   -240    687   -265       C  
ATOM    360  C   ILE A  45      -9.195  -5.731  80.302  1.00 23.22           C  
ANISOU  360  C   ILE A  45     3613   2714   2495   -290    702   -133       C  
ATOM    361  O   ILE A  45      -9.924  -5.969  79.344  1.00 22.98           O  
ANISOU  361  O   ILE A  45     3541   2629   2560   -320    741   -104       O  
ATOM    362  CB  ILE A  45      -8.220  -3.472  80.682  1.00 25.96           C  
ANISOU  362  CB  ILE A  45     4031   3016   2817   -297    577   -354       C  
ATOM    363  CG1 ILE A  45      -8.390  -2.125  81.374  1.00 28.85           C  
ANISOU  363  CG1 ILE A  45     4508   3339   3117   -266    542   -514       C  
ATOM    364  CG2 ILE A  45      -8.164  -3.336  79.173  1.00 24.70           C  
ANISOU  364  CG2 ILE A  45     3832   2742   2811   -344    570   -312       C  
ATOM    365  CD1 ILE A  45      -9.672  -1.427  81.016  1.00 45.42           C  
ANISOU  365  CD1 ILE A  45     6650   5360   5246   -150    609   -565       C  
ATOM    366  N   PHE A  46      -8.220  -6.526  80.709  1.00 22.81           N  
ANISOU  366  N   PHE A  46     3591   2695   2381   -274    660    -67       N  
ATOM    367  CA  PHE A  46      -7.917  -7.808  80.086  1.00 19.50           C  
ANISOU  367  CA  PHE A  46     3204   2203   2002   -267    658     45       C  
ATOM    368  C   PHE A  46      -9.137  -8.714  80.110  1.00 27.63           C  
ANISOU  368  C   PHE A  46     4280   3176   3042   -335    749    135       C  
ATOM    369  O   PHE A  46      -9.493  -9.327  79.113  1.00 25.00           O  
ANISOU  369  O   PHE A  46     3962   2731   2804   -390    755    161       O  
ATOM    370  CB  PHE A  46      -6.762  -8.466  80.835  1.00 30.93           C  
ANISOU  370  CB  PHE A  46     4699   3731   3323   -169    603    106       C  
ATOM    371  CG  PHE A  46      -6.410  -9.840  80.353  1.00 27.87           C  
ANISOU  371  CG  PHE A  46     4411   3238   2939    -91    595    217       C  
ATOM    372  CD1 PHE A  46      -5.587 -10.015  79.252  1.00 25.00           C  
ANISOU  372  CD1 PHE A  46     4011   2857   2632    -20    537    196       C  
ATOM    373  CD2 PHE A  46      -6.860 -10.955  81.032  1.00 30.58           C  
ANISOU  373  CD2 PHE A  46     4910   3500   3207    -76    646    348       C  
ATOM    374  CE1 PHE A  46      -5.229 -11.279  78.840  1.00 21.19           C  
ANISOU  374  CE1 PHE A  46     3661   2264   2126    110    521    271       C  
ATOM    375  CE2 PHE A  46      -6.516 -12.218  80.603  1.00 34.37           C  
ANISOU  375  CE2 PHE A  46     5558   3816   3684     15    627    441       C  
ATOM    376  CZ  PHE A  46      -5.696 -12.370  79.510  1.00 22.55           C  
ANISOU  376  CZ  PHE A  46     4038   2291   2238    131    559    386       C  
ATOM    377  N   LYS A  47      -9.754  -8.805  81.282  1.00 21.15           N  
ANISOU  377  N   LYS A  47     3474   2457   2103   -348    815    181       N  
ATOM    378  CA  LYS A  47     -10.970  -9.578  81.437  1.00 22.18           C  
ANISOU  378  CA  LYS A  47     3615   2596   2218   -471    912    286       C  
ATOM    379  C   LYS A  47     -12.063  -9.086  80.485  1.00 27.29           C  
ANISOU  379  C   LYS A  47     4130   3273   2968   -551    948    217       C  
ATOM    380  O   LYS A  47     -12.748  -9.885  79.849  1.00 30.10           O  
ANISOU  380  O   LYS A  47     4483   3572   3383   -696    975    277       O  
ATOM    381  CB  LYS A  47     -11.443  -9.526  82.899  1.00 23.81           C  
ANISOU  381  CB  LYS A  47     3812   2992   2243   -457    989    347       C  
ATOM    382  CG  LYS A  47     -12.804 -10.123  83.130  1.00 36.79           C  
ANISOU  382  CG  LYS A  47     5403   4735   3841   -623   1108    465       C  
ATOM    383  CD  LYS A  47     -12.967 -10.536  84.583  1.00 42.94           C  
ANISOU  383  CD  LYS A  47     6226   5678   4413   -619   1185    603       C  
ATOM    384  CE  LYS A  47     -12.966  -9.340  85.522  1.00 47.71           C  
ANISOU  384  CE  LYS A  47     6733   6528   4867   -439   1197    471       C  
ATOM    385  NZ  LYS A  47     -14.321  -8.722  85.687  1.00 51.62           N  
ANISOU  385  NZ  LYS A  47     7040   7286   5288   -447   1304    426       N  
ATOM    386  N   ASP A  48     -12.201  -7.776  80.348  1.00 28.36           N  
ANISOU  386  N   ASP A  48     4173   3488   3116   -455    936     87       N  
ATOM    387  CA  ASP A  48     -13.264  -7.235  79.522  1.00 25.12           C  
ANISOU  387  CA  ASP A  48     3633   3145   2765   -465    970     32       C  
ATOM    388  C   ASP A  48     -12.990  -7.437  78.034  1.00 29.07           C  
ANISOU  388  C   ASP A  48     4131   3503   3412   -506    908     14       C  
ATOM    389  O   ASP A  48     -13.900  -7.764  77.261  1.00 26.29           O  
ANISOU  389  O   ASP A  48     3686   3202   3100   -590    932     23       O  
ATOM    390  CB  ASP A  48     -13.487  -5.768  79.847  1.00 36.39           C  
ANISOU  390  CB  ASP A  48     5029   4655   4142   -298    972    -95       C  
ATOM    391  CG  ASP A  48     -14.441  -5.584  81.013  1.00 68.38           C  
ANISOU  391  CG  ASP A  48     9007   8952   8022   -234   1067    -95       C  
ATOM    392  OD1 ASP A  48     -14.903  -6.606  81.580  1.00 72.99           O  
ANISOU  392  OD1 ASP A  48     9546   9658   8529   -362   1140     33       O  
ATOM    393  OD2 ASP A  48     -14.732  -4.425  81.372  1.00 84.64           O  
ANISOU  393  OD2 ASP A  48    11071  11080  10007    -51   1072   -217       O  
ATOM    394  N   ASN A  49     -11.740  -7.274  77.625  1.00 21.45           N  
ANISOU  394  N   ASN A  49     3245   2404   2503   -451    827    -12       N  
ATOM    395  CA  ASN A  49     -11.398  -7.535  76.246  1.00 17.65           C  
ANISOU  395  CA  ASN A  49     2756   1827   2124   -465    776    -21       C  
ATOM    396  C   ASN A  49     -11.548  -9.021  75.913  1.00 21.42           C  
ANISOU  396  C   ASN A  49     3307   2216   2616   -565    775     43       C  
ATOM    397  O   ASN A  49     -11.938  -9.367  74.807  1.00 23.44           O  
ANISOU  397  O   ASN A  49     3535   2439   2931   -615    754     17       O  
ATOM    398  CB  ASN A  49      -9.976  -7.073  75.933  1.00 22.35           C  
ANISOU  398  CB  ASN A  49     3384   2367   2741   -392    701    -45       C  
ATOM    399  CG  ASN A  49      -9.884  -5.586  75.732  1.00 27.51           C  
ANISOU  399  CG  ASN A  49     4005   3028   3418   -354    682   -111       C  
ATOM    400  OD1 ASN A  49     -10.856  -4.944  75.368  1.00 23.50           O  
ANISOU  400  OD1 ASN A  49     3458   2539   2932   -324    716   -142       O  
ATOM    401  ND2 ASN A  49      -8.708  -5.030  75.961  1.00 23.32           N  
ANISOU  401  ND2 ASN A  49     3500   2488   2871   -358    623   -128       N  
ATOM    402  N   LEU A  50     -11.240  -9.895  76.868  1.00 28.77           N  
ANISOU  402  N   LEU A  50     4360   3093   3477   -589    788    126       N  
ATOM    403  CA  LEU A  50     -11.410 -11.333  76.655  1.00 20.38           C  
ANISOU  403  CA  LEU A  50     3450   1872   2420   -693    783    198       C  
ATOM    404  C   LEU A  50     -12.870 -11.689  76.394  1.00 23.04           C  
ANISOU  404  C   LEU A  50     3715   2262   2777   -916    836    212       C  
ATOM    405  O   LEU A  50     -13.188 -12.501  75.501  1.00 26.26           O  
ANISOU  405  O   LEU A  50     4194   2547   3237  -1038    798    191       O  
ATOM    406  CB  LEU A  50     -10.893 -12.104  77.866  1.00 34.95           C  
ANISOU  406  CB  LEU A  50     5466   3649   4164   -661    797    317       C  
ATOM    407  CG  LEU A  50     -11.119 -13.616  77.889  1.00 33.51           C  
ANISOU  407  CG  LEU A  50     5526   3238   3969   -778    798    425       C  
ATOM    408  CD1 LEU A  50     -10.481 -14.274  76.684  1.00 32.74           C  
ANISOU  408  CD1 LEU A  50     5570   2936   3935   -687    709    354       C  
ATOM    409  CD2 LEU A  50     -10.544 -14.203  79.156  1.00 36.33           C  
ANISOU  409  CD2 LEU A  50     6057   3547   4198   -692    815    568       C  
ATOM    410  N   LYS A  51     -13.754 -11.091  77.183  1.00 22.03           N  
ANISOU  410  N   LYS A  51     3438   2348   2584   -968    917    237       N  
ATOM    411  CA  LYS A  51     -15.178 -11.308  77.007  1.00 30.73           C  
ANISOU  411  CA  LYS A  51     4391   3616   3669  -1178    976    257       C  
ATOM    412  C   LYS A  51     -15.571 -10.879  75.610  1.00 32.34           C  
ANISOU  412  C   LYS A  51     4461   3874   3954  -1164    924    141       C  
ATOM    413  O   LYS A  51     -16.317 -11.586  74.920  1.00 32.74           O  
ANISOU  413  O   LYS A  51     4475   3939   4025  -1371    906    132       O  
ATOM    414  CB  LYS A  51     -15.997 -10.545  78.043  1.00 28.74           C  
ANISOU  414  CB  LYS A  51     3955   3666   3296  -1147   1076    284       C  
ATOM    415  CG  LYS A  51     -17.505 -10.711  77.879  1.00 39.14           C  
ANISOU  415  CG  LYS A  51     5044   5270   4559  -1350   1145    312       C  
ATOM    416  CD  LYS A  51     -18.287 -10.139  79.065  1.00 48.91           C  
ANISOU  416  CD  LYS A  51     6100   6856   5627  -1292   1263    360       C  
ATOM    417  CE  LYS A  51     -18.081  -8.639  79.197  1.00 53.96           C  
ANISOU  417  CE  LYS A  51     6672   7596   6234   -941   1257    224       C  
ATOM    418  NZ  LYS A  51     -18.854  -8.077  80.337  1.00 65.14           N  
ANISOU  418  NZ  LYS A  51     7931   9363   7455   -827   1367    239       N  
ATOM    419  N   TYR A  52     -15.059  -9.725  75.189  1.00 25.41           N  
ANISOU  419  N   TYR A  52     3522   3025   3108   -936    893     56       N  
ATOM    420  CA  TYR A  52     -15.351  -9.215  73.863  1.00 24.18           C  
ANISOU  420  CA  TYR A  52     3252   2929   3006   -878    847    -30       C  
ATOM    421  C   TYR A  52     -14.791 -10.153  72.788  1.00 30.02           C  
ANISOU  421  C   TYR A  52     4118   3478   3812   -941    764    -62       C  
ATOM    422  O   TYR A  52     -15.447 -10.412  71.773  1.00 28.02           O  
ANISOU  422  O   TYR A  52     3781   3295   3571  -1027    728   -119       O  
ATOM    423  CB  TYR A  52     -14.775  -7.798  73.677  1.00 26.51           C  
ANISOU  423  CB  TYR A  52     3524   3231   3319   -639    831    -80       C  
ATOM    424  CG  TYR A  52     -15.072  -7.202  72.312  1.00 31.80           C  
ANISOU  424  CG  TYR A  52     4094   3966   4023   -553    791   -133       C  
ATOM    425  CD1 TYR A  52     -16.324  -6.658  72.024  1.00 30.64           C  
ANISOU  425  CD1 TYR A  52     3761   4059   3820   -505    823   -156       C  
ATOM    426  CD2 TYR A  52     -14.112  -7.201  71.300  1.00 28.38           C  
ANISOU  426  CD2 TYR A  52     3732   3403   3646   -497    725   -149       C  
ATOM    427  CE1 TYR A  52     -16.605  -6.118  70.772  1.00 31.55           C  
ANISOU  427  CE1 TYR A  52     3789   4256   3941   -395    782   -189       C  
ATOM    428  CE2 TYR A  52     -14.389  -6.675  70.038  1.00 24.57           C  
ANISOU  428  CE2 TYR A  52     3162   3004   3170   -411    693   -176       C  
ATOM    429  CZ  TYR A  52     -15.636  -6.128  69.781  1.00 30.94           C  
ANISOU  429  CZ  TYR A  52     3808   4022   3926   -357    718   -193       C  
ATOM    430  OH  TYR A  52     -15.924  -5.598  68.530  1.00 27.97           O  
ANISOU  430  OH  TYR A  52     3348   3750   3530   -240    682   -205       O  
ATOM    431  N   ILE A  53     -13.570 -10.633  73.000  1.00 23.35           N  
ANISOU  431  N   ILE A  53     3465   2424   2983   -866    728    -38       N  
ATOM    432  CA  ILE A  53     -12.919 -11.526  72.047  1.00 26.21           C  
ANISOU  432  CA  ILE A  53     3975   2610   3375   -848    650    -83       C  
ATOM    433  C   ILE A  53     -13.701 -12.824  71.910  1.00 30.69           C  
ANISOU  433  C   ILE A  53     4664   3058   3940  -1090    631    -84       C  
ATOM    434  O   ILE A  53     -13.979 -13.292  70.808  1.00 29.00           O  
ANISOU  434  O   ILE A  53     4471   2806   3742  -1153    566   -178       O  
ATOM    435  CB  ILE A  53     -11.483 -11.844  72.486  1.00 27.96           C  
ANISOU  435  CB  ILE A  53     4364   2686   3573   -679    622    -45       C  
ATOM    436  CG1 ILE A  53     -10.579 -10.631  72.258  1.00 23.19           C  
ANISOU  436  CG1 ILE A  53     3636   2203   2974   -500    611    -63       C  
ATOM    437  CG2 ILE A  53     -10.941 -13.027  71.726  1.00 20.45           C  
ANISOU  437  CG2 ILE A  53     3616   1540   2614   -629    550    -88       C  
ATOM    438  CD1 ILE A  53      -9.325 -10.664  73.088  1.00 23.19           C  
ANISOU  438  CD1 ILE A  53     3708   2185   2920   -374    597    -13       C  
ATOM    439  N   ASP A  54     -14.069 -13.386  73.051  1.00 25.82           N  
ANISOU  439  N   ASP A  54     4136   2387   3289  -1246    686     22       N  
ATOM    440  CA  ASP A  54     -14.820 -14.630  73.083  1.00 30.48           C  
ANISOU  440  CA  ASP A  54     4877   2831   3871  -1548    675     56       C  
ATOM    441  C   ASP A  54     -16.171 -14.514  72.378  1.00 33.67           C  
ANISOU  441  C   ASP A  54     5051   3465   4278  -1794    671    -12       C  
ATOM    442  O   ASP A  54     -16.545 -15.389  71.596  1.00 37.44           O  
ANISOU  442  O   ASP A  54     5616   3839   4769  -1947    580    -85       O  
ATOM    443  CB  ASP A  54     -14.995 -15.074  74.537  1.00 27.33           C  
ANISOU  443  CB  ASP A  54     4549   2423   3412  -1625    735    220       C  
ATOM    444  CG  ASP A  54     -15.435 -16.508  74.657  1.00 48.23           C  
ANISOU  444  CG  ASP A  54     7384   4886   6056  -1816    674    278       C  
ATOM    445  OD1 ASP A  54     -14.592 -17.398  74.434  1.00 49.56           O  
ANISOU  445  OD1 ASP A  54     7844   4751   6234  -1698    598    267       O  
ATOM    446  OD2 ASP A  54     -16.615 -16.741  75.000  1.00 50.91           O  
ANISOU  446  OD2 ASP A  54     7580   5395   6370  -2071    706    338       O  
ATOM    447  N   GLU A  55     -16.894 -13.426  72.632  1.00 35.48           N  
ANISOU  447  N   GLU A  55     4963   4046   4471  -1753    741     -2       N  
ATOM    448  CA  GLU A  55     -18.212 -13.251  72.024  1.00 37.81           C  
ANISOU  448  CA  GLU A  55     4982   4652   4731  -1941    739    -57       C  
ATOM    449  C   GLU A  55     -18.133 -12.919  70.523  1.00 33.74           C  
ANISOU  449  C   GLU A  55     4390   4185   4245  -1813    643   -208       C  
ATOM    450  O   GLU A  55     -18.985 -13.328  69.739  1.00 35.04           O  
ANISOU  450  O   GLU A  55     4440   4490   4382  -2024    586   -286       O  
ATOM    451  CB  GLU A  55     -18.997 -12.169  72.775  1.00 34.85           C  
ANISOU  451  CB  GLU A  55     4303   4667   4273  -1849    845     -3       C  
ATOM    452  CG  GLU A  55     -19.389 -12.573  74.190  1.00 52.89           C  
ANISOU  452  CG  GLU A  55     6595   7017   6483  -2000    938    145       C  
ATOM    453  CD  GLU A  55     -19.972 -11.420  74.991  1.00 66.73           C  
ANISOU  453  CD  GLU A  55     8081   9151   8123  -1831   1055    174       C  
ATOM    454  OE1 GLU A  55     -19.907 -10.264  74.512  1.00 71.84           O  
ANISOU  454  OE1 GLU A  55     8609   9914   8774  -1527   1039     79       O  
ATOM    455  OE2 GLU A  55     -20.490 -11.672  76.100  1.00 65.12           O  
ANISOU  455  OE2 GLU A  55     7826   9086   7833  -1891   1112    285       O  
ATOM    456  N   THR A  56     -17.105 -12.190  70.119  1.00 28.01           N  
ANISOU  456  N   THR A  56     3717   3368   3556  -1491    622   -242       N  
ATOM    457  CA  THR A  56     -16.965 -11.813  68.720  1.00 27.83           C  
ANISOU  457  CA  THR A  56     3621   3416   3537  -1347    545   -352       C  
ATOM    458  C   THR A  56     -16.519 -13.015  67.868  1.00 34.11           C  
ANISOU  458  C   THR A  56     4649   3965   4347  -1440    441   -453       C  
ATOM    459  O   THR A  56     -16.999 -13.203  66.751  1.00 42.65           O  
ANISOU  459  O   THR A  56     5653   5159   5393  -1497    363   -570       O  
ATOM    460  CB  THR A  56     -15.979 -10.637  68.556  1.00 30.38           C  
ANISOU  460  CB  THR A  56     3934   3728   3882  -1014    563   -328       C  
ATOM    461  OG1 THR A  56     -16.469  -9.495  69.275  1.00 31.25           O  
ANISOU  461  OG1 THR A  56     3881   4025   3967   -913    642   -268       O  
ATOM    462  CG2 THR A  56     -15.815 -10.264  67.087  1.00 33.99           C  
ANISOU  462  CG2 THR A  56     4320   4275   4319   -870    496   -406       C  
ATOM    463  N   ASN A  57     -15.627 -13.842  68.405  1.00 27.80           N  
ANISOU  463  N   ASN A  57     4146   2840   3576  -1430    432   -419       N  
ATOM    464  CA  ASN A  57     -15.140 -15.015  67.687  1.00 31.71           C  
ANISOU  464  CA  ASN A  57     4929   3055   4065  -1454    331   -526       C  
ATOM    465  C   ASN A  57     -16.170 -16.134  67.551  1.00 40.24           C  
ANISOU  465  C   ASN A  57     6123   4031   5135  -1850    271   -588       C  
ATOM    466  O   ASN A  57     -15.930 -17.121  66.853  1.00 41.58           O  
ANISOU  466  O   ASN A  57     6551   3958   5290  -1877    165   -708       O  
ATOM    467  CB  ASN A  57     -13.906 -15.589  68.367  1.00 28.84           C  
ANISOU  467  CB  ASN A  57     4867   2383   3707  -1278    337   -459       C  
ATOM    468  CG  ASN A  57     -12.669 -14.763  68.124  1.00 29.42           C  
ANISOU  468  CG  ASN A  57     4864   2547   3766   -911    351   -448       C  
ATOM    469  OD1 ASN A  57     -12.672 -13.820  67.325  1.00 29.50           O  
ANISOU  469  OD1 ASN A  57     4649   2791   3769   -796    352   -487       O  
ATOM    470  ND2 ASN A  57     -11.592 -15.120  68.807  1.00 27.80           N  
ANISOU  470  ND2 ASN A  57     4844   2178   3541   -734    361   -379       N  
ATOM    471  N   LYS A  58     -17.298 -15.995  68.237  1.00 35.94           N  
ANISOU  471  N   LYS A  58     5379   3694   4583  -2136    334   -500       N  
ATOM    472  CA  LYS A  58     -18.375 -16.978  68.129  1.00 44.30           C  
ANISOU  472  CA  LYS A  58     6435   4780   5617  -2443    266   -508       C  
ATOM    473  C   LYS A  58     -19.004 -16.881  66.758  1.00 43.66           C  
ANISOU  473  C   LYS A  58     6189   4908   5492  -2544    168   -697       C  
ATOM    474  O   LYS A  58     -19.444 -17.878  66.179  1.00 57.09           O  
ANISOU  474  O   LYS A  58     8013   6501   7177  -2726     58   -786       O  
ATOM    475  CB  LYS A  58     -19.454 -16.750  69.198  1.00 46.44           C  
ANISOU  475  CB  LYS A  58     6456   5338   5852  -2644    362   -352       C  
ATOM    476  CG  LYS A  58     -19.153 -17.311  70.570  1.00 49.61           C  
ANISOU  476  CG  LYS A  58     7050   5536   6264  -2652    426   -170       C  
ATOM    477  CD  LYS A  58     -20.244 -16.891  71.542  1.00 53.68           C  
ANISOU  477  CD  LYS A  58     7267   6417   6713  -2809    528    -38       C  
ATOM    478  CE  LYS A  58     -20.063 -17.526  72.905  1.00 59.98           C  
ANISOU  478  CE  LYS A  58     8242   7046   7501  -2854    589    144       C  
ATOM    479  NZ  LYS A  58     -21.066 -16.993  73.867  1.00 62.24           N  
ANISOU  479  NZ  LYS A  58     8217   7733   7699  -2953    699    263       N  
ATOM    480  N   LYS A  59     -19.059 -15.654  66.260  1.00 36.46           N  
ANISOU  480  N   LYS A  59     4982   4320   4551  -2383    204   -748       N  
ATOM    481  CA  LYS A  59     -19.714 -15.352  64.996  1.00 39.70           C  
ANISOU  481  CA  LYS A  59     5152   5048   4885  -2386    115   -898       C  
ATOM    482  C   LYS A  59     -18.922 -15.886  63.802  1.00 44.54           C  
ANISOU  482  C   LYS A  59     6013   5432   5477  -2230    -10  -1078       C  
ATOM    483  O   LYS A  59     -17.728 -16.182  63.903  1.00 46.54           O  
ANISOU  483  O   LYS A  59     6565   5346   5772  -2001     -7  -1070       O  
ATOM    484  CB  LYS A  59     -19.909 -13.840  64.867  1.00 41.88           C  
ANISOU  484  CB  LYS A  59     5071   5721   5122  -2062    191   -829       C  
ATOM    485  CG  LYS A  59     -20.725 -13.237  66.013  1.00 60.02           C  
ANISOU  485  CG  LYS A  59     7115   8289   7401  -2138    313   -681       C  
ATOM    486  CD  LYS A  59     -20.349 -11.780  66.279  1.00 64.40           C  
ANISOU  486  CD  LYS A  59     7536   8975   7956  -1719    404   -588       C  
ATOM    487  CE  LYS A  59     -21.265 -11.159  67.333  1.00 64.33           C  
ANISOU  487  CE  LYS A  59     7273   9282   7888  -1739    516   -480       C  
ATOM    488  NZ  LYS A  59     -21.441 -12.031  68.535  1.00 64.60           N  
ANISOU  488  NZ  LYS A  59     7411   9192   7942  -2058    577   -391       N  
ATOM    489  N   ASN A  60     -19.592 -15.982  62.665  1.00 46.31           N  
ANISOU  489  N   ASN A  60     6088   5898   5610  -2326   -120  -1244       N  
ATOM    490  CA  ASN A  60     -18.973 -16.501  61.462  1.00 36.81           C  
ANISOU  490  CA  ASN A  60     5098   4540   4347  -2177   -246  -1443       C  
ATOM    491  C   ASN A  60     -18.400 -15.377  60.600  1.00 34.27           C  
ANISOU  491  C   ASN A  60     4579   4480   3961  -1725   -221  -1429       C  
ATOM    492  O   ASN A  60     -18.957 -15.042  59.571  1.00 42.38           O  
ANISOU  492  O   ASN A  60     5386   5842   4874  -1686   -293  -1532       O  
ATOM    493  CB  ASN A  60     -19.995 -17.325  60.676  1.00 40.77           C  
ANISOU  493  CB  ASN A  60     5572   5150   4770  -2512   -396  -1624       C  
ATOM    494  CG  ASN A  60     -19.387 -18.030  59.478  1.00 47.34           C  
ANISOU  494  CG  ASN A  60     6677   5783   5528  -2351   -542  -1850       C  
ATOM    495  OD1 ASN A  60     -18.172 -18.223  59.400  1.00 40.93           O  
ANISOU  495  OD1 ASN A  60     6164   4667   4721  -2064   -533  -1889       O  
ATOM    496  ND2 ASN A  60     -20.236 -18.435  58.547  1.00 45.43           N  
ANISOU  496  ND2 ASN A  60     6327   5738   5198  -2510   -678  -2000       N  
ATOM    497  N   ASN A  61     -17.280 -14.803  61.030  1.00 34.94           N  
ANISOU  497  N   ASN A  61     4745   4426   4105  -1403   -123  -1291       N  
ATOM    498  CA  ASN A  61     -16.564 -13.774  60.260  1.00 41.07           C  
ANISOU  498  CA  ASN A  61     5385   5396   4824  -1013    -90  -1243       C  
ATOM    499  C   ASN A  61     -15.305 -14.337  59.616  1.00 38.85           C  
ANISOU  499  C   ASN A  61     5362   4909   4490   -769   -136  -1336       C  
ATOM    500  O   ASN A  61     -14.834 -15.379  60.027  1.00 30.45           O  
ANISOU  500  O   ASN A  61     4610   3502   3459   -829   -170  -1402       O  
ATOM    501  CB  ASN A  61     -16.179 -12.591  61.148  1.00 46.60           C  
ANISOU  501  CB  ASN A  61     5961   6140   5605   -846     49  -1021       C  
ATOM    502  CG  ASN A  61     -17.354 -11.692  61.458  1.00 54.87           C  
ANISOU  502  CG  ASN A  61     6705   7498   6644   -917     98   -938       C  
ATOM    503  OD1 ASN A  61     -17.784 -10.906  60.609  1.00 60.60           O  
ANISOU  503  OD1 ASN A  61     7219   8528   7279   -764     82   -935       O  
ATOM    504  ND2 ASN A  61     -17.877 -11.793  62.678  1.00 47.08           N  
ANISOU  504  ND2 ASN A  61     5697   6464   5727  -1114    163   -861       N  
ATOM    505  N   SER A  62     -14.745 -13.649  58.628  1.00 28.60           N  
ANISOU  505  N   SER A  62     3942   3833   3090   -471   -131  -1326       N  
ATOM    506  CA  SER A  62     -13.589 -14.194  57.933  1.00 29.16           C  
ANISOU  506  CA  SER A  62     4210   3804   3065   -212   -170  -1423       C  
ATOM    507  C   SER A  62     -12.287 -13.986  58.700  1.00 27.32           C  
ANISOU  507  C   SER A  62     4073   3415   2893    -13    -73  -1270       C  
ATOM    508  O   SER A  62     -11.232 -14.362  58.229  1.00 27.86           O  
ANISOU  508  O   SER A  62     4261   3462   2863    245    -87  -1322       O  
ATOM    509  CB  SER A  62     -13.464 -13.589  56.529  1.00 42.83           C  
ANISOU  509  CB  SER A  62     5756   5892   4626     24   -196  -1458       C  
ATOM    510  OG  SER A  62     -13.270 -12.190  56.586  1.00 38.33           O  
ANISOU  510  OG  SER A  62     4943   5543   4075    157    -84  -1223       O  
ATOM    511  N   TYR A  63     -12.355 -13.371  59.874  1.00 25.46           N  
ANISOU  511  N   TYR A  63     3763   3118   2792   -115     21  -1090       N  
ATOM    512  CA  TYR A  63     -11.149 -13.185  60.673  1.00 29.24           C  
ANISOU  512  CA  TYR A  63     4314   3482   3315     40     97   -957       C  
ATOM    513  C   TYR A  63     -11.514 -13.411  62.121  1.00 24.51           C  
ANISOU  513  C   TYR A  63     3807   2658   2847   -170    138   -878       C  
ATOM    514  O   TYR A  63     -12.699 -13.523  62.440  1.00 24.12           O  
ANISOU  514  O   TYR A  63     3715   2599   2850   -429    127   -899       O  
ATOM    515  CB  TYR A  63     -10.538 -11.784  60.474  1.00 22.87           C  
ANISOU  515  CB  TYR A  63     3273   2924   2494    193    183   -782       C  
ATOM    516  CG  TYR A  63     -11.364 -10.654  61.057  1.00 22.33           C  
ANISOU  516  CG  TYR A  63     3033   2930   2522     52    246   -651       C  
ATOM    517  CD1 TYR A  63     -12.448 -10.127  60.351  1.00 22.76           C  
ANISOU  517  CD1 TYR A  63     2926   3184   2537     11    225   -670       C  
ATOM    518  CD2 TYR A  63     -11.062 -10.110  62.309  1.00 19.52           C  
ANISOU  518  CD2 TYR A  63     2682   2465   2268     -3    318   -521       C  
ATOM    519  CE1 TYR A  63     -13.223  -9.090  60.885  1.00 20.66           C  
ANISOU  519  CE1 TYR A  63     2521   2997   2331    -46    281   -559       C  
ATOM    520  CE2 TYR A  63     -11.819  -9.070  62.842  1.00 18.73           C  
ANISOU  520  CE2 TYR A  63     2461   2422   2232    -80    370   -428       C  
ATOM    521  CZ  TYR A  63     -12.896  -8.567  62.125  1.00 28.75           C  
ANISOU  521  CZ  TYR A  63     3585   3879   3459    -83    354   -445       C  
ATOM    522  OH  TYR A  63     -13.647  -7.534  62.648  1.00 27.28           O  
ANISOU  522  OH  TYR A  63     3297   3759   3308    -88    405   -359       O  
ATOM    523  N   TRP A  64     -10.512 -13.489  62.988  1.00 22.76           N  
ANISOU  523  N   TRP A  64     3687   2308   2653    -57    184   -784       N  
ATOM    524  CA  TRP A  64     -10.765 -13.632  64.420  1.00 22.33           C  
ANISOU  524  CA  TRP A  64     3713   2076   2696   -223    231   -687       C  
ATOM    525  C   TRP A  64      -9.877 -12.720  65.255  1.00 23.06           C  
ANISOU  525  C   TRP A  64     3698   2249   2815   -108    310   -533       C  
ATOM    526  O   TRP A  64      -8.839 -12.232  64.787  1.00 22.11           O  
ANISOU  526  O   TRP A  64     3490   2277   2636     94    320   -499       O  
ATOM    527  CB  TRP A  64     -10.561 -15.086  64.862  1.00 24.36           C  
ANISOU  527  CB  TRP A  64     4314   2000   2940   -250    177   -751       C  
ATOM    528  CG  TRP A  64      -9.195 -15.651  64.514  1.00 25.14           C  
ANISOU  528  CG  TRP A  64     4581   2035   2936     91    142   -795       C  
ATOM    529  CD1 TRP A  64      -8.105 -15.744  65.343  1.00 32.73           C  
ANISOU  529  CD1 TRP A  64     5612   2955   3869    290    176   -694       C  
ATOM    530  CD2 TRP A  64      -8.789 -16.209  63.257  1.00 26.75           C  
ANISOU  530  CD2 TRP A  64     4884   2263   3017    305     65   -960       C  
ATOM    531  NE1 TRP A  64      -7.049 -16.332  64.673  1.00 26.29           N  
ANISOU  531  NE1 TRP A  64     4915   2158   2916    631    128   -777       N  
ATOM    532  CE2 TRP A  64      -7.443 -16.620  63.392  1.00 27.45           C  
ANISOU  532  CE2 TRP A  64     5092   2336   3002    654     64   -945       C  
ATOM    533  CE3 TRP A  64      -9.432 -16.405  62.031  1.00 27.96           C  
ANISOU  533  CE3 TRP A  64     5024   2486   3113    255     -9  -1129       C  
ATOM    534  CZ2 TRP A  64      -6.734 -17.212  62.348  1.00 29.36           C  
ANISOU  534  CZ2 TRP A  64     5444   2630   3079    978      3  -1093       C  
ATOM    535  CZ3 TRP A  64      -8.723 -16.987  60.992  1.00 29.74           C  
ANISOU  535  CZ3 TRP A  64     5378   2741   3181    556    -76  -1285       C  
ATOM    536  CH2 TRP A  64      -7.389 -17.391  61.160  1.00 30.96           C  
ANISOU  536  CH2 TRP A  64     5658   2876   3229    925    -66  -1267       C  
ATOM    537  N   LEU A  65     -10.316 -12.495  66.492  1.00 19.92           N  
ANISOU  537  N   LEU A  65     3297   1781   2490   -260    362   -445       N  
ATOM    538  CA  LEU A  65      -9.597 -11.697  67.487  1.00 18.59           C  
ANISOU  538  CA  LEU A  65     3060   1664   2342   -198    420   -325       C  
ATOM    539  C   LEU A  65      -8.853 -12.604  68.454  1.00 22.97           C  
ANISOU  539  C   LEU A  65     3815   2046   2866   -132    412   -287       C  
ATOM    540  O   LEU A  65      -9.049 -13.820  68.459  1.00 21.95           O  
ANISOU  540  O   LEU A  65     3916   1705   2718   -156    372   -335       O  
ATOM    541  CB  LEU A  65     -10.557 -10.812  68.279  1.00 17.82           C  
ANISOU  541  CB  LEU A  65     2836   1630   2304   -355    481   -266       C  
ATOM    542  CG  LEU A  65     -11.508  -9.924  67.475  1.00 25.49           C  
ANISOU  542  CG  LEU A  65     3624   2772   3288   -390    491   -289       C  
ATOM    543  CD1 LEU A  65     -12.354  -9.077  68.400  1.00 18.28           C  
ANISOU  543  CD1 LEU A  65     2613   1931   2403   -464    554   -237       C  
ATOM    544  CD2 LEU A  65     -10.739  -9.045  66.495  1.00 20.69           C  
ANISOU  544  CD2 LEU A  65     2923   2287   2652   -230    482   -265       C  
ATOM    545  N   GLY A  66      -8.045 -12.013  69.317  1.00 21.01           N  
ANISOU  545  N   GLY A  66     3504   1876   2603    -58    443   -200       N  
ATOM    546  CA  GLY A  66      -7.208 -12.814  70.184  1.00 24.22           C  
ANISOU  546  CA  GLY A  66     4075   2183   2945     67    428   -153       C  
ATOM    547  C   GLY A  66      -6.572 -11.974  71.258  1.00 21.76           C  
ANISOU  547  C   GLY A  66     3643   2010   2614     81    458    -68       C  
ATOM    548  O   GLY A  66      -6.558 -10.746  71.165  1.00 20.69           O  
ANISOU  548  O   GLY A  66     3321   2026   2514     12    480    -60       O  
ATOM    549  N   LEU A  67      -6.071 -12.641  72.291  1.00 24.07           N  
ANISOU  549  N   LEU A  67     4073   2235   2839    167    451     -8       N  
ATOM    550  CA  LEU A  67      -5.371 -11.974  73.370  1.00 21.62           C  
ANISOU  550  CA  LEU A  67     3658   2084   2474    194    458     54       C  
ATOM    551  C   LEU A  67      -3.997 -11.610  72.881  1.00 21.39           C  
ANISOU  551  C   LEU A  67     3468   2298   2360    367    416     47       C  
ATOM    552  O   LEU A  67      -2.999 -12.226  73.281  1.00 21.09           O  
ANISOU  552  O   LEU A  67     3466   2351   2196    581    379     81       O  
ATOM    553  CB  LEU A  67      -5.274 -12.870  74.600  1.00 24.33           C  
ANISOU  553  CB  LEU A  67     4193   2313   2737    258    460    136       C  
ATOM    554  CG  LEU A  67      -6.612 -13.294  75.188  1.00 22.53           C  
ANISOU  554  CG  LEU A  67     4108   1888   2566     47    516    179       C  
ATOM    555  CD1 LEU A  67      -6.410 -14.320  76.335  1.00 23.01           C  
ANISOU  555  CD1 LEU A  67     4405   1816   2522    125    520    301       C  
ATOM    556  CD2 LEU A  67      -7.327 -12.051  75.662  1.00 22.96           C  
ANISOU  556  CD2 LEU A  67     3969   2083   2671   -130    569    163       C  
ATOM    557  N   ASN A  68      -3.935 -10.624  71.992  1.00 19.65           N  
ANISOU  557  N   ASN A  68     3063   2214   2189    285    423     18       N  
ATOM    558  CA  ASN A  68      -2.643 -10.253  71.426  1.00 19.22           C  
ANISOU  558  CA  ASN A  68     2820   2444   2039    400    394     34       C  
ATOM    559  C   ASN A  68      -1.987  -9.238  72.352  1.00 22.57           C  
ANISOU  559  C   ASN A  68     3091   3050   2433    274    380     74       C  
ATOM    560  O   ASN A  68      -2.403  -9.087  73.506  1.00 21.58           O  
ANISOU  560  O   ASN A  68     3046   2826   2328    187    384     75       O  
ATOM    561  CB  ASN A  68      -2.786  -9.706  70.004  1.00 19.24           C  
ANISOU  561  CB  ASN A  68     2706   2526   2079    359    410     15       C  
ATOM    562  CG  ASN A  68      -3.594  -8.419  69.949  1.00 17.50           C  
ANISOU  562  CG  ASN A  68     2429   2240   1981    115    444     28       C  
ATOM    563  OD1 ASN A  68      -3.742  -7.729  70.940  1.00 17.46           O  
ANISOU  563  OD1 ASN A  68     2428   2192   2013    -19    448     42       O  
ATOM    564  ND2 ASN A  68      -4.111  -8.095  68.775  1.00 17.42           N  
ANISOU  564  ND2 ASN A  68     2382   2227   2010     92    462     19       N  
ATOM    565  N   VAL A  69      -0.985  -8.531  71.841  1.00 26.32           N  
ANISOU  565  N   VAL A  69     3347   3806   2845    242    361    103       N  
ATOM    566  CA  VAL A  69      -0.161  -7.657  72.676  1.00 21.22           C  
ANISOU  566  CA  VAL A  69     2549   3370   2142     94    323    127       C  
ATOM    567  C   VAL A  69      -0.961  -6.509  73.306  1.00 23.03           C  
ANISOU  567  C   VAL A  69     2856   3400   2493   -173    332     95       C  
ATOM    568  O   VAL A  69      -0.532  -5.945  74.306  1.00 23.59           O  
ANISOU  568  O   VAL A  69     2891   3554   2517   -291    288     75       O  
ATOM    569  CB  VAL A  69       1.025  -7.095  71.854  1.00 22.07           C  
ANISOU  569  CB  VAL A  69     2386   3844   2155     43    306    183       C  
ATOM    570  CG1 VAL A  69       0.524  -6.166  70.742  1.00 21.36           C  
ANISOU  570  CG1 VAL A  69     2279   3660   2176   -146    350    215       C  
ATOM    571  CG2 VAL A  69       2.045  -6.414  72.740  1.00 23.65           C  
ANISOU  571  CG2 VAL A  69     2404   4324   2256   -121    244    199       C  
ATOM    572  N   PHE A  70      -2.136  -6.192  72.755  1.00 23.85           N  
ANISOU  572  N   PHE A  70     3074   3258   2729   -237    382     77       N  
ATOM    573  CA  PHE A  70      -2.943  -5.059  73.255  1.00 24.87           C  
ANISOU  573  CA  PHE A  70     3294   3204   2951   -418    394     39       C  
ATOM    574  C   PHE A  70      -4.142  -5.484  74.110  1.00 20.03           C  
ANISOU  574  C   PHE A  70     2833   2403   2374   -367    431     -9       C  
ATOM    575  O   PHE A  70      -5.037  -4.679  74.384  1.00 23.12           O  
ANISOU  575  O   PHE A  70     3301   2657   2825   -439    456    -50       O  
ATOM    576  CB  PHE A  70      -3.430  -4.204  72.079  1.00 20.35           C  
ANISOU  576  CB  PHE A  70     2721   2543   2467   -501    424     69       C  
ATOM    577  CG  PHE A  70      -2.311  -3.600  71.280  1.00 21.05           C  
ANISOU  577  CG  PHE A  70     2660   2827   2511   -611    401    148       C  
ATOM    578  CD1 PHE A  70      -1.306  -2.881  71.912  1.00 26.47           C  
ANISOU  578  CD1 PHE A  70     3270   3645   3141   -802    345    157       C  
ATOM    579  CD2 PHE A  70      -2.238  -3.783  69.908  1.00 20.69           C  
ANISOU  579  CD2 PHE A  70     2532   2875   2456   -543    433    214       C  
ATOM    580  CE1 PHE A  70      -0.254  -2.349  71.187  1.00 28.84           C  
ANISOU  580  CE1 PHE A  70     3400   4177   3383   -959    330    253       C  
ATOM    581  CE2 PHE A  70      -1.205  -3.243  69.178  1.00 20.27           C  
ANISOU  581  CE2 PHE A  70     2314   3053   2333   -658    428    314       C  
ATOM    582  CZ  PHE A  70      -0.209  -2.529  69.812  1.00 26.81           C  
ANISOU  582  CZ  PHE A  70     3050   4023   3112   -882    381    344       C  
ATOM    583  N   ALA A  71      -4.148  -6.746  74.538  1.00 17.40           N  
ANISOU  583  N   ALA A  71     2552   2074   1984   -231    438      8       N  
ATOM    584  CA  ALA A  71      -5.289  -7.296  75.279  1.00 18.66           C  
ANISOU  584  CA  ALA A  71     2842   2085   2162   -221    486      1       C  
ATOM    585  C   ALA A  71      -5.504  -6.591  76.621  1.00 20.13           C  
ANISOU  585  C   ALA A  71     3059   2287   2301   -286    488    -36       C  
ATOM    586  O   ALA A  71      -6.616  -6.571  77.117  1.00 19.92           O  
ANISOU  586  O   ALA A  71     3095   2184   2289   -307    544    -50       O  
ATOM    587  CB  ALA A  71      -5.105  -8.816  75.480  1.00 21.98           C  
ANISOU  587  CB  ALA A  71     3367   2468   2518    -82    485     53       C  
ATOM    588  N   ASP A  72      -4.451  -5.980  77.179  1.00 26.78           N  
ANISOU  588  N   ASP A  72     3839   3266   3068   -323    423    -63       N  
ATOM    589  CA  ASP A  72      -4.563  -5.266  78.463  1.00 28.95           C  
ANISOU  589  CA  ASP A  72     4160   3567   3273   -379    404   -133       C  
ATOM    590  C   ASP A  72      -4.807  -3.774  78.317  1.00 21.54           C  
ANISOU  590  C   ASP A  72     3257   2532   2396   -512    383   -226       C  
ATOM    591  O   ASP A  72      -4.685  -3.037  79.292  1.00 26.04           O  
ANISOU  591  O   ASP A  72     3885   3115   2894   -566    340   -320       O  
ATOM    592  CB  ASP A  72      -3.307  -5.468  79.327  1.00 23.35           C  
ANISOU  592  CB  ASP A  72     3381   3079   2413   -355    322   -134       C  
ATOM    593  CG  ASP A  72      -2.081  -4.763  78.761  1.00 24.16           C  
ANISOU  593  CG  ASP A  72     3335   3340   2506   -480    240   -152       C  
ATOM    594  OD1 ASP A  72      -2.120  -4.333  77.590  1.00 30.07           O  
ANISOU  594  OD1 ASP A  72     4047   4017   3362   -559    257   -129       O  
ATOM    595  OD2 ASP A  72      -1.065  -4.661  79.482  1.00 31.35           O  
ANISOU  595  OD2 ASP A  72     4146   4486   3280   -509    157   -177       O  
ATOM    596  N   MET A  73      -5.144  -3.327  77.114  1.00 19.39           N  
ANISOU  596  N   MET A  73     2980   2149   2239   -550    407   -204       N  
ATOM    597  CA  MET A  73      -5.455  -1.908  76.890  1.00 21.42           C  
ANISOU  597  CA  MET A  73     3334   2251   2552   -644    390   -267       C  
ATOM    598  C   MET A  73      -6.917  -1.691  76.503  1.00 18.79           C  
ANISOU  598  C   MET A  73     3074   1781   2283   -529    468   -278       C  
ATOM    599  O   MET A  73      -7.447  -2.440  75.711  1.00 22.54           O  
ANISOU  599  O   MET A  73     3479   2282   2805   -462    518   -213       O  
ATOM    600  CB  MET A  73      -4.545  -1.334  75.803  1.00 20.80           C  
ANISOU  600  CB  MET A  73     3194   2185   2525   -789    347   -205       C  
ATOM    601  CG  MET A  73      -3.184  -0.907  76.340  1.00 31.43           C  
ANISOU  601  CG  MET A  73     4475   3675   3790   -978    252   -230       C  
ATOM    602  SD  MET A  73      -2.185  -0.063  75.114  1.00 56.98           S  
ANISOU  602  SD  MET A  73     7628   6954   7067  -1225    215   -130       S  
ATOM    603  CE  MET A  73      -0.617   0.015  75.986  1.00 53.24           C  
ANISOU  603  CE  MET A  73     6984   6794   6450  -1440    100   -166       C  
ATOM    604  N   SER A  74      -7.571  -0.688  77.083  1.00 22.87           N  
ANISOU  604  N   SER A  74     3733   2179   2779   -489    469   -375       N  
ATOM    605  CA  SER A  74      -8.927  -0.355  76.661  1.00 26.12           C  
ANISOU  605  CA  SER A  74     4186   2520   3220   -337    537   -384       C  
ATOM    606  C   SER A  74      -8.814   0.241  75.274  1.00 27.33           C  
ANISOU  606  C   SER A  74     4359   2558   3466   -367    524   -312       C  
ATOM    607  O   SER A  74      -7.748   0.737  74.918  1.00 23.95           O  
ANISOU  607  O   SER A  74     3967   2066   3067   -528    462   -279       O  
ATOM    608  CB  SER A  74      -9.604   0.622  77.622  1.00 23.15           C  
ANISOU  608  CB  SER A  74     3973   2060   2763   -215    539   -516       C  
ATOM    609  OG  SER A  74      -9.064   1.932  77.509  1.00 27.30           O  
ANISOU  609  OG  SER A  74     4707   2354   3312   -287    460   -581       O  
ATOM    610  N   ASN A  75      -9.878   0.170  74.475  1.00 23.56           N  
ANISOU  610  N   ASN A  75     3837   2099   3016   -228    580   -274       N  
ATOM    611  CA  ASN A  75      -9.815   0.797  73.156  1.00 28.38           C  
ANISOU  611  CA  ASN A  75     4480   2616   3688   -225    569   -192       C  
ATOM    612  C   ASN A  75      -9.660   2.303  73.278  1.00 28.67           C  
ANISOU  612  C   ASN A  75     4770   2397   3726   -226    525   -222       C  
ATOM    613  O   ASN A  75      -9.006   2.936  72.452  1.00 30.09           O  
ANISOU  613  O   ASN A  75     5028   2454   3950   -344    492   -130       O  
ATOM    614  CB  ASN A  75     -11.042   0.462  72.315  1.00 30.04           C  
ANISOU  614  CB  ASN A  75     4581   2936   3896    -55    625   -157       C  
ATOM    615  CG  ASN A  75     -10.913   0.958  70.889  1.00 26.10           C  
ANISOU  615  CG  ASN A  75     4094   2389   3433    -37    613    -52       C  
ATOM    616  OD1 ASN A  75     -11.678   1.815  70.445  1.00 28.85           O  
ANISOU  616  OD1 ASN A  75     4536   2666   3760    134    623    -34       O  
ATOM    617  ND2 ASN A  75      -9.905   0.444  70.168  1.00 18.62           N  
ANISOU  617  ND2 ASN A  75     3057   1503   2516   -183    592     26       N  
ATOM    618  N   ASP A  76     -10.242   2.888  74.320  1.00 33.85           N  
ANISOU  618  N   ASP A  76     5579   2965   4319    -99    523   -349       N  
ATOM    619  CA  ASP A  76     -10.111   4.326  74.524  1.00 32.61           C  
ANISOU  619  CA  ASP A  76     5740   2497   4152    -84    465   -410       C  
ATOM    620  C   ASP A  76      -8.635   4.663  74.682  1.00 28.23           C  
ANISOU  620  C   ASP A  76     5265   1827   3634   -425    377   -399       C  
ATOM    621  O   ASP A  76      -8.129   5.628  74.119  1.00 34.25           O  
ANISOU  621  O   ASP A  76     6227   2347   4440   -569    327   -338       O  
ATOM    622  CB  ASP A  76     -10.906   4.788  75.757  1.00 40.89           C  
ANISOU  622  CB  ASP A  76     6940   3505   5091    139    472   -587       C  
ATOM    623  CG  ASP A  76     -12.406   4.896  75.490  1.00 48.78           C  
ANISOU  623  CG  ASP A  76     7901   4610   6024    506    551   -594       C  
ATOM    624  OD1 ASP A  76     -12.874   4.492  74.403  1.00 44.72           O  
ANISOU  624  OD1 ASP A  76     7216   4225   5550    566    595   -469       O  
ATOM    625  OD2 ASP A  76     -13.124   5.376  76.388  1.00 56.34           O  
ANISOU  625  OD2 ASP A  76     8977   5568   6862    749    566   -734       O  
ATOM    626  N   GLU A  77      -7.930   3.823  75.419  1.00 25.00           N  
ANISOU  626  N   GLU A  77     4682   1623   3194   -565    358   -438       N  
ATOM    627  CA  GLU A  77      -6.524   4.064  75.682  1.00 26.03           C  
ANISOU  627  CA  GLU A  77     4817   1750   3322   -883    267   -440       C  
ATOM    628  C   GLU A  77      -5.689   3.824  74.412  1.00 27.38           C  
ANISOU  628  C   GLU A  77     4824   2024   3557  -1066    273   -255       C  
ATOM    629  O   GLU A  77      -4.879   4.650  74.008  1.00 35.54           O  
ANISOU  629  O   GLU A  77     5953   2937   4612  -1323    216   -193       O  
ATOM    630  CB  GLU A  77      -6.089   3.173  76.830  1.00 31.01           C  
ANISOU  630  CB  GLU A  77     5287   2627   3866   -905    248   -524       C  
ATOM    631  CG  GLU A  77      -4.625   3.133  77.097  1.00 48.37           C  
ANISOU  631  CG  GLU A  77     7383   4966   6029  -1197    157   -518       C  
ATOM    632  CD  GLU A  77      -4.293   2.169  78.219  1.00 57.61           C  
ANISOU  632  CD  GLU A  77     8396   6407   7087  -1141    142   -582       C  
ATOM    633  OE1 GLU A  77      -5.191   1.388  78.621  1.00 51.88           O  
ANISOU  633  OE1 GLU A  77     7630   5751   6332   -903    222   -589       O  
ATOM    634  OE2 GLU A  77      -3.141   2.211  78.705  1.00 62.56           O  
ANISOU  634  OE2 GLU A  77     8936   7194   7639  -1345     50   -613       O  
ATOM    635  N   PHE A  78      -5.924   2.684  73.784  1.00 30.93           N  
ANISOU  635  N   PHE A  78     5032   2700   4018   -936    342   -169       N  
ATOM    636  CA  PHE A  78      -5.296   2.336  72.521  1.00 25.27           C  
ANISOU  636  CA  PHE A  78     4146   2126   3329  -1022    362    -10       C  
ATOM    637  C   PHE A  78      -5.497   3.416  71.465  1.00 24.12           C  
ANISOU  637  C   PHE A  78     4163   1773   3230  -1065    371    103       C  
ATOM    638  O   PHE A  78      -4.558   3.812  70.757  1.00 26.07           O  
ANISOU  638  O   PHE A  78     4370   2060   3476  -1292    352    234       O  
ATOM    639  CB  PHE A  78      -5.875   1.007  72.041  1.00 28.54           C  
ANISOU  639  CB  PHE A  78     4368   2735   3742   -813    430     15       C  
ATOM    640  CG  PHE A  78      -5.355   0.561  70.712  1.00 24.04           C  
ANISOU  640  CG  PHE A  78     3634   2331   3171   -830    452    147       C  
ATOM    641  CD1 PHE A  78      -4.124  -0.072  70.620  1.00 27.05           C  
ANISOU  641  CD1 PHE A  78     3828   2956   3494   -927    428    190       C  
ATOM    642  CD2 PHE A  78      -6.105   0.745  69.565  1.00 22.94           C  
ANISOU  642  CD2 PHE A  78     3510   2150   3057   -711    495    220       C  
ATOM    643  CE1 PHE A  78      -3.637  -0.479  69.398  1.00 24.35           C  
ANISOU  643  CE1 PHE A  78     3328   2807   3117   -902    454    298       C  
ATOM    644  CE2 PHE A  78      -5.629   0.330  68.340  1.00 30.32           C  
ANISOU  644  CE2 PHE A  78     4294   3267   3961   -707    515    329       C  
ATOM    645  CZ  PHE A  78      -4.389  -0.285  68.258  1.00 24.53           C  
ANISOU  645  CZ  PHE A  78     3383   2772   3167   -798    499    364       C  
ATOM    646  N   LYS A  79      -6.731   3.899  71.371  1.00 31.04           N  
ANISOU  646  N   LYS A  79     5214   2454   4124   -836    403     70       N  
ATOM    647  CA  LYS A  79      -7.133   4.842  70.327  1.00 33.30           C  
ANISOU  647  CA  LYS A  79     5677   2542   4434   -780    419    194       C  
ATOM    648  C   LYS A  79      -6.842   6.310  70.673  1.00 43.75           C  
ANISOU  648  C   LYS A  79     7321   3533   5769   -909    342    182       C  
ATOM    649  O   LYS A  79      -6.976   7.185  69.821  1.00 49.11           O  
ANISOU  649  O   LYS A  79     8136   4061   6462   -881    335    309       O  
ATOM    650  CB  LYS A  79      -8.624   4.623  70.034  1.00 47.59           C  
ANISOU  650  CB  LYS A  79     7476   4381   6226   -415    478    163       C  
ATOM    651  CG  LYS A  79      -9.337   5.617  69.160  1.00 57.48           C  
ANISOU  651  CG  LYS A  79     8936   5437   7467   -232    492    265       C  
ATOM    652  CD  LYS A  79     -10.370   6.380  69.964  1.00 63.46           C  
ANISOU  652  CD  LYS A  79     9945   5985   8183     39    485    132       C  
ATOM    653  CE  LYS A  79     -11.389   5.447  70.586  1.00 57.53           C  
ANISOU  653  CE  LYS A  79     8963   5515   7382    266    534     -1       C  
ATOM    654  NZ  LYS A  79     -12.466   6.213  71.283  1.00 63.97           N  
ANISOU  654  NZ  LYS A  79     9980   6211   8115    593    541   -122       N  
ATOM    655  N   GLU A  80      -6.409   6.596  71.898  1.00 45.99           N  
ANISOU  655  N   GLU A  80     7671   3767   6036  -1025    267     28       N  
ATOM    656  CA  GLU A  80      -6.279   8.002  72.308  1.00 50.50           C  
ANISOU  656  CA  GLU A  80     8516   4062   6612  -1084    180    -25       C  
ATOM    657  C   GLU A  80      -5.201   8.712  71.492  1.00 56.28           C  
ANISOU  657  C   GLU A  80     9243   4758   7381  -1393    141    144       C  
ATOM    658  O   GLU A  80      -5.342   9.889  71.161  1.00 65.20           O  
ANISOU  658  O   GLU A  80    10624   5617   8533  -1395    109    196       O  
ATOM    659  CB  GLU A  80      -6.004   8.122  73.817  1.00 55.71           C  
ANISOU  659  CB  GLU A  80     9246   4700   7224  -1151    106   -238       C  
ATOM    660  CG  GLU A  80      -4.566   7.900  74.250  1.00 69.07           C  
ANISOU  660  CG  GLU A  80    10774   6571   8900  -1524     35   -246       C  
ATOM    661  CD  GLU A  80      -4.410   7.852  75.763  1.00 72.38           C  
ANISOU  661  CD  GLU A  80    11246   7012   9242  -1549    -35   -467       C  
ATOM    662  OE1 GLU A  80      -5.297   7.291  76.439  1.00 67.00           O  
ANISOU  662  OE1 GLU A  80    10582   6364   8512  -1286     11   -589       O  
ATOM    663  OE2 GLU A  80      -3.398   8.379  76.273  1.00 79.52           O  
ANISOU  663  OE2 GLU A  80    12168   7925  10122  -1834   -134   -518       O  
ATOM    664  N   LYS A  81      -4.146   7.993  71.133  1.00 79.13           N  
ANISOU  664  N   LYS A  81    10307   9806   9954   -481   2888  -3510       N  
ATOM    665  CA  LYS A  81      -3.182   8.540  70.191  1.00 85.64           C  
ANISOU  665  CA  LYS A  81    10946  10555  11037   -524   2637  -3531       C  
ATOM    666  C   LYS A  81      -3.532   8.010  68.814  1.00 86.34           C  
ANISOU  666  C   LYS A  81    10751  10641  11412   -597   2637  -3311       C  
ATOM    667  O   LYS A  81      -2.869   8.342  67.831  1.00 87.96           O  
ANISOU  667  O   LYS A  81    10794  10775  11851   -633   2481  -3275       O  
ATOM    668  CB  LYS A  81      -1.758   8.166  70.564  1.00 89.46           C  
ANISOU  668  CB  LYS A  81    11618  11099  11273   -522   2354  -3623       C  
ATOM    669  CG  LYS A  81      -1.601   7.706  72.001  1.00 95.34           C  
ANISOU  669  CG  LYS A  81    12779  11931  11516   -404   2337  -3735       C  
ATOM    670  CD  LYS A  81      -0.521   6.653  72.098  1.00 93.08           C  
ANISOU  670  CD  LYS A  81    12673  11748  10944   -372   2066  -3704       C  
ATOM    671  CE  LYS A  81      -0.733   5.759  73.290  1.00 93.08           C  
ANISOU  671  CE  LYS A  81    13127  11836  10403   -226   2123  -3689       C  
ATOM    672  NZ  LYS A  81       0.195   4.606  73.200  1.00 93.69           N  
ANISOU  672  NZ  LYS A  81    13375  12001  10221   -167   1861  -3613       N  
ATOM    673  N   TYR A  82      -4.580   7.178  68.798  1.00 86.27           N  
ANISOU  673  N   TYR A  82    10705  10700  11375   -619   2824  -3179       N  
ATOM    674  CA  TYR A  82      -5.201   6.554  67.619  1.00 83.60           C  
ANISOU  674  CA  TYR A  82    10117  10367  11279   -669   2829  -2996       C  
ATOM    675  C   TYR A  82      -4.630   5.194  67.272  1.00 86.93           C  
ANISOU  675  C   TYR A  82    10615  10879  11537   -751   2731  -2845       C  
ATOM    676  O   TYR A  82      -5.356   4.320  66.800  1.00 96.47           O  
ANISOU  676  O   TYR A  82    11724  12116  12813   -809   2809  -2716       O  
ATOM    677  CB  TYR A  82      -5.090   7.433  66.380  1.00 71.28           C  
ANISOU  677  CB  TYR A  82     8323   8686  10073   -619   2691  -2972       C  
ATOM    678  CG  TYR A  82      -6.065   8.574  66.260  1.00 63.40           C  
ANISOU  678  CG  TYR A  82     7185   7582   9324   -501   2793  -3054       C  
ATOM    679  CD1 TYR A  82      -7.093   8.530  65.332  1.00 66.56           C  
ANISOU  679  CD1 TYR A  82     7351   7964   9974   -423   2799  -2973       C  
ATOM    680  CD2 TYR A  82      -5.949   9.701  67.059  1.00 66.55           C  
ANISOU  680  CD2 TYR A  82     7692   7896   9700   -439   2857  -3232       C  
ATOM    681  CE1 TYR A  82      -7.978   9.579  65.197  1.00 76.16           C  
ANISOU  681  CE1 TYR A  82     8440   9090  11409   -263   2865  -3061       C  
ATOM    682  CE2 TYR A  82      -6.826  10.754  66.935  1.00 77.99           C  
ANISOU  682  CE2 TYR A  82     9029   9234  11368   -301   2949  -3311       C  
ATOM    683  CZ  TYR A  82      -7.842  10.688  66.005  1.00 84.41           C  
ANISOU  683  CZ  TYR A  82     9607  10041  12426   -202   2953  -3221       C  
ATOM    684  OH  TYR A  82      -8.728  11.735  65.878  1.00 93.02           O  
ANISOU  684  OH  TYR A  82    10587  11030  13725    -13   3021  -3313       O  
ATOM    685  N   THR A  83      -3.329   5.014  67.466  1.00 80.56           N  
ANISOU  685  N   THR A  83     9968  10108  10533   -747   2542  -2881       N  
ATOM    686  CA  THR A  83      -2.635   4.043  66.639  1.00 74.77           C  
ANISOU  686  CA  THR A  83     9204   9425   9781   -792   2385  -2743       C  
ATOM    687  C   THR A  83      -1.525   3.188  67.250  1.00 69.18           C  
ANISOU  687  C   THR A  83     8771   8810   8704   -764   2230  -2762       C  
ATOM    688  O   THR A  83      -0.441   3.073  66.673  1.00 42.51           O  
ANISOU  688  O   THR A  83     5330   5451   5371   -760   2008  -2773       O  
ATOM    689  CB  THR A  83      -2.048   4.779  65.455  1.00 78.61           C  
ANISOU  689  CB  THR A  83     9459   9824  10587   -790   2228  -2737       C  
ATOM    690  OG1 THR A  83      -1.450   5.992  65.923  1.00 90.89           O  
ANISOU  690  OG1 THR A  83    11032  11304  12199   -764   2173  -2925       O  
ATOM    691  CG2 THR A  83      -3.147   5.148  64.513  1.00 78.79           C  
ANISOU  691  CG2 THR A  83     9261   9762  10915   -765   2307  -2643       C  
ATOM    692  N   GLY A  84      -1.804   2.571  68.393  1.00 69.49           N  
ANISOU  692  N   GLY A  84     9130   8898   8375   -726   2344  -2765       N  
ATOM    693  CA  GLY A  84      -1.002   1.455  68.860  1.00 64.81           C  
ANISOU  693  CA  GLY A  84     8859   8378   7387   -659   2201  -2720       C  
ATOM    694  C   GLY A  84       0.240   1.729  69.676  1.00 75.54           C  
ANISOU  694  C   GLY A  84    10458   9784   8460   -507   1900  -2917       C  
ATOM    695  O   GLY A  84       0.418   2.807  70.243  1.00 88.97           O  
ANISOU  695  O   GLY A  84    12159  11455  10191   -460   1844  -3119       O  
ATOM    696  N   SER A  85       1.094   0.712  69.741  1.00 72.05           N  
ANISOU  696  N   SER A  85    10232   9405   7739   -416   1678  -2875       N  
ATOM    697  CA  SER A  85       2.354   0.798  70.461  1.00 76.18           C  
ANISOU  697  CA  SER A  85    10978   9980   7986   -235   1300  -3082       C  
ATOM    698  C   SER A  85       3.323  -0.280  69.983  1.00 78.56           C  
ANISOU  698  C   SER A  85    11338  10345   8165   -160   1025  -3016       C  
ATOM    699  O   SER A  85       3.015  -1.064  69.078  1.00 74.12           O  
ANISOU  699  O   SER A  85    10659   9781   7724   -255   1150  -2808       O  
ATOM    700  CB  SER A  85       2.145   0.675  71.978  1.00 76.42           C  
ANISOU  700  CB  SER A  85    11504  10029   7505    -37   1309  -3169       C  
ATOM    701  OG  SER A  85       2.529  -0.616  72.433  1.00 76.90           O  
ANISOU  701  OG  SER A  85    11930  10171   7117    140   1167  -3080       O  
ATOM    702  N   TYR A  90      -3.609   8.850  64.174  1.00 63.50           N  
ANISOU  702  N   TYR A  90     7157   7422   9547   -571   2390  -2894       N  
ATOM    703  CA  TYR A  90      -2.798  10.045  64.289  1.00 53.78           C  
ANISOU  703  CA  TYR A  90     5979   6032   8424   -580   2367  -3024       C  
ATOM    704  C   TYR A  90      -1.344   9.675  64.480  1.00 45.66           C  
ANISOU  704  C   TYR A  90     5003   5058   7287   -708   2233  -3084       C  
ATOM    705  O   TYR A  90      -0.569  10.463  64.997  1.00 51.63           O  
ANISOU  705  O   TYR A  90     5808   5738   8071   -754   2196  -3262       O  
ATOM    706  CB  TYR A  90      -3.277  10.925  65.431  1.00 71.90           C  
ANISOU  706  CB  TYR A  90     8365   8288  10667   -527   2481  -3218       C  
ATOM    707  N   THR A  91      -0.975   8.454  64.089  1.00 53.21           N  
ANISOU  707  N   THR A  91     5940   6150   8126   -753   2144  -2960       N  
ATOM    708  CA  THR A  91       0.368   8.271  63.593  1.00 42.12           C  
ANISOU  708  CA  THR A  91     4490   4739   6774   -836   2015  -2969       C  
ATOM    709  C   THR A  91       0.353   9.043  62.272  1.00 52.59           C  
ANISOU  709  C   THR A  91     5726   5846   8412   -818   2082  -2850       C  
ATOM    710  O   THR A  91       1.351   9.631  61.853  1.00 42.15           O  
ANISOU  710  O   THR A  91     4360   4395   7259   -896   2084  -2898       O  
ATOM    711  CB  THR A  91       0.792   6.788  63.398  1.00 39.91           C  
ANISOU  711  CB  THR A  91     4229   4639   6297   -857   1903  -2862       C  
ATOM    712  OG1 THR A  91      -0.330   5.979  63.058  1.00 49.86           O  
ANISOU  712  OG1 THR A  91     5496   5957   7492   -810   1975  -2684       O  
ATOM    713  CG2 THR A  91       1.392   6.233  64.625  1.00 41.20           C  
ANISOU  713  CG2 THR A  91     4544   4960   6150   -855   1784  -3011       C  
ATOM    714  N   THR A  92      -0.814   9.096  61.643  1.00 47.05           N  
ANISOU  714  N   THR A  92     5009   5086   7781   -697   2148  -2704       N  
ATOM    715  CA  THR A  92      -0.943   9.823  60.388  1.00 49.94           C  
ANISOU  715  CA  THR A  92     5374   5228   8374   -603   2197  -2573       C  
ATOM    716  C   THR A  92      -1.976  10.954  60.389  1.00 60.21           C  
ANISOU  716  C   THR A  92     6706   6367   9804   -439   2286  -2602       C  
ATOM    717  O   THR A  92      -3.104  10.821  60.875  1.00 60.80           O  
ANISOU  717  O   THR A  92     6729   6545   9828   -341   2301  -2639       O  
ATOM    718  CB  THR A  92      -1.226   8.831  59.260  1.00 41.96           C  
ANISOU  718  CB  THR A  92     4333   4277   7332   -526   2125  -2361       C  
ATOM    719  OG1 THR A  92       0.011   8.560  58.604  1.00 39.33           O  
ANISOU  719  OG1 THR A  92     4018   3894   7031   -624   2111  -2301       O  
ATOM    720  CG2 THR A  92      -2.247   9.361  58.250  1.00 46.60           C  
ANISOU  720  CG2 THR A  92     4933   4722   8050   -294   2141  -2238       C  
ATOM    721  N   THR A  93      -1.562  12.086  59.839  1.00 72.77           N  
ANISOU  721  N   THR A  93     8389   7689  11573   -407   2364  -2591       N  
ATOM    722  CA  THR A  93      -2.377  13.285  59.884  1.00 73.85           C  
ANISOU  722  CA  THR A  93     8604   7632  11825   -230   2442  -2637       C  
ATOM    723  C   THR A  93      -2.869  13.700  58.485  1.00 71.55           C  
ANISOU  723  C   THR A  93     8421   7126  11638     18   2441  -2439       C  
ATOM    724  O   THR A  93      -2.542  13.061  57.483  1.00 59.97           O  
ANISOU  724  O   THR A  93     6981   5660  10146     37   2395  -2265       O  
ATOM    725  CB  THR A  93      -1.592  14.417  60.560  1.00 77.46           C  
ANISOU  725  CB  THR A  93     9149   7906  12375   -363   2538  -2814       C  
ATOM    726  OG1 THR A  93      -0.363  14.629  59.857  1.00 82.89           O  
ANISOU  726  OG1 THR A  93     9885   8432  13179   -515   2596  -2752       O  
ATOM    727  CG2 THR A  93      -1.263  14.029  61.991  1.00 70.14           C  
ANISOU  727  CG2 THR A  93     8154   7204  11292   -520   2490  -3034       C  
ATOM    728  N   GLU A  94      -3.681  14.750  58.423  1.00 87.06           N  
ANISOU  728  N   GLU A  94    10480   8907  13693    247   2476  -2471       N  
ATOM    729  CA  GLU A  94      -4.277  15.171  57.158  1.00 85.61           C  
ANISOU  729  CA  GLU A  94    10448   8520  13561    571   2426  -2302       C  
ATOM    730  C   GLU A  94      -3.791  16.558  56.745  1.00 77.83           C  
ANISOU  730  C   GLU A  94     9768   7125  12679    629   2556  -2260       C  
ATOM    731  O   GLU A  94      -2.828  17.079  57.305  1.00 66.97           O  
ANISOU  731  O   GLU A  94     8440   5637  11370    359   2697  -2354       O  
ATOM    732  CB  GLU A  94      -5.800  15.146  57.257  1.00 88.67           C  
ANISOU  732  CB  GLU A  94    10690   9039  13962    879   2315  -2368       C  
ATOM    733  N   VAL A 106       0.334  -4.026  32.954  1.00105.94           N  
ANISOU  733  N   VAL A 106    18055  11694  10502   3520   -162    286       N  
ATOM    734  CA  VAL A 106      -1.065  -4.158  33.342  1.00104.82           C  
ANISOU  734  CA  VAL A 106    17575  11699  10553   3627   -786     55       C  
ATOM    735  C   VAL A 106      -1.338  -5.564  33.885  1.00100.08           C  
ANISOU  735  C   VAL A 106    16530  11325  10172   3385  -1074   -188       C  
ATOM    736  O   VAL A 106      -2.223  -5.756  34.722  1.00 99.53           O  
ANISOU  736  O   VAL A 106    15908  11429  10481   3202  -1359   -411       O  
ATOM    737  CB  VAL A 106      -2.009  -3.837  32.152  1.00 86.84           C  
ANISOU  737  CB  VAL A 106    15643   9409   7943   4010  -1202    -88       C  
ATOM    738  CG1 VAL A 106      -1.770  -4.793  30.991  1.00 85.44           C  
ANISOU  738  CG1 VAL A 106    15849   9205   7407   4162  -1297   -194       C  
ATOM    739  CG2 VAL A 106      -3.470  -3.859  32.591  1.00 89.68           C  
ANISOU  739  CG2 VAL A 106    15558   9933   8581   4110  -1825   -369       C  
ATOM    740  N   ASN A 107      -0.555  -6.537  33.424  1.00 93.32           N  
ANISOU  740  N   ASN A 107    15893  10468   9097   3332   -932   -165       N  
ATOM    741  CA  ASN A 107      -0.672  -7.912  33.901  1.00 83.97           C  
ANISOU  741  CA  ASN A 107    14337   9464   8103   3053  -1120   -387       C  
ATOM    742  C   ASN A 107       0.223  -8.172  35.107  1.00 73.27           C  
ANISOU  742  C   ASN A 107    12559   8183   7095   2612   -685   -325       C  
ATOM    743  O   ASN A 107       1.450  -8.208  34.989  1.00 71.78           O  
ANISOU  743  O   ASN A 107    12549   7921   6804   2557   -241   -157       O  
ATOM    744  CB  ASN A 107      -0.327  -8.901  32.788  1.00 86.54           C  
ANISOU  744  CB  ASN A 107    15136   9738   8006   3259  -1234   -427       C  
ATOM    745  CG  ASN A 107      -0.909  -8.501  31.454  1.00 96.22           C  
ANISOU  745  CG  ASN A 107    16782  10827   8951   3661  -1484   -482       C  
ATOM    746  OD1 ASN A 107      -1.972  -7.885  31.388  1.00101.54           O  
ANISOU  746  OD1 ASN A 107    17368  11534   9680   3832  -1855   -607       O  
ATOM    747  ND2 ASN A 107      -0.215  -8.853  30.377  1.00 97.54           N  
ANISOU  747  ND2 ASN A 107    17366  10831   8862   3808  -1267   -416       N  
ATOM    748  N   ILE A 108      -0.398  -8.363  36.266  1.00 61.42           N  
ANISOU  748  N   ILE A 108    10504   6829   6003   2315   -815   -481       N  
ATOM    749  CA  ILE A 108       0.338  -8.583  37.503  1.00 47.61           C  
ANISOU  749  CA  ILE A 108     8381   5157   4554   1937   -475   -443       C  
ATOM    750  C   ILE A 108       0.067  -9.996  38.034  1.00 43.22           C  
ANISOU  750  C   ILE A 108     7583   4707   4133   1700   -661   -631       C  
ATOM    751  O   ILE A 108      -0.950 -10.594  37.687  1.00 44.31           O  
ANISOU  751  O   ILE A 108     7687   4877   4273   1745  -1059   -833       O  
ATOM    752  CB  ILE A 108      -0.035  -7.495  38.559  1.00 53.11           C  
ANISOU  752  CB  ILE A 108     8705   5892   5582   1782   -364   -432       C  
ATOM    753  CG1 ILE A 108      -1.531  -7.511  38.887  1.00 43.50           C  
ANISOU  753  CG1 ILE A 108     7173   4776   4578   1771   -772   -658       C  
ATOM    754  CG2 ILE A 108       0.364  -6.117  38.058  1.00 57.49           C  
ANISOU  754  CG2 ILE A 108     9551   6281   6013   1992   -115   -231       C  
ATOM    755  CD1 ILE A 108      -1.978  -6.346  39.788  1.00 36.18           C  
ANISOU  755  CD1 ILE A 108     5935   3869   3942   1691   -665   -659       C  
ATOM    756  N   PRO A 109       0.981 -10.541  38.863  1.00 37.27           N  
ANISOU  756  N   PRO A 109     6676   3989   3496   1457   -382   -580       N  
ATOM    757  CA  PRO A 109       0.823 -11.888  39.431  1.00 39.60           C  
ANISOU  757  CA  PRO A 109     6826   4328   3892   1240   -502   -718       C  
ATOM    758  C   PRO A 109      -0.444 -12.046  40.265  1.00 40.19           C  
ANISOU  758  C   PRO A 109     6531   4475   4265   1012   -716   -903       C  
ATOM    759  O   PRO A 109      -0.983 -11.055  40.770  1.00 34.49           O  
ANISOU  759  O   PRO A 109     5566   3807   3730    974   -693   -908       O  
ATOM    760  CB  PRO A 109       2.056 -12.044  40.333  1.00 40.50           C  
ANISOU  760  CB  PRO A 109     6830   4469   4091   1081   -152   -605       C  
ATOM    761  CG  PRO A 109       3.022 -11.045  39.858  1.00 39.99           C  
ANISOU  761  CG  PRO A 109     6906   4362   3925   1236    148   -438       C  
ATOM    762  CD  PRO A 109       2.211  -9.895  39.350  1.00 39.68           C  
ANISOU  762  CD  PRO A 109     6933   4280   3863   1382     50   -409       C  
ATOM    763  N   GLU A 110      -0.905 -13.283  40.420  1.00 33.09           N  
ANISOU  763  N   GLU A 110     5592   3554   3425    851   -881  -1064       N  
ATOM    764  CA  GLU A 110      -2.080 -13.534  41.234  1.00 39.50           C  
ANISOU  764  CA  GLU A 110     6043   4410   4555    583   -999  -1256       C  
ATOM    765  C   GLU A 110      -1.745 -13.248  42.688  1.00 31.17           C  
ANISOU  765  C   GLU A 110     4753   3405   3685    334   -682  -1159       C  
ATOM    766  O   GLU A 110      -2.549 -12.687  43.429  1.00 35.51           O  
ANISOU  766  O   GLU A 110     4987   4022   4483    188   -653  -1241       O  
ATOM    767  CB  GLU A 110      -2.573 -14.973  41.071  1.00 35.35           C  
ANISOU  767  CB  GLU A 110     5569   3796   4067    424  -1183  -1452       C  
ATOM    768  CG  GLU A 110      -3.935 -15.200  41.725  1.00 45.35           C  
ANISOU  768  CG  GLU A 110     6436   5088   5707    133  -1288  -1702       C  
ATOM    769  CD  GLU A 110      -4.464 -16.605  41.525  1.00 46.37           C  
ANISOU  769  CD  GLU A 110     6611   5086   5923    -70  -1442  -1927       C  
ATOM    770  OE1 GLU A 110      -3.647 -17.533  41.373  1.00 47.29           O  
ANISOU  770  OE1 GLU A 110     7063   5072   5832    -65  -1362  -1837       O  
ATOM    771  OE2 GLU A 110      -5.697 -16.783  41.521  1.00 56.02           O  
ANISOU  771  OE2 GLU A 110     7516   6321   7447   -236  -1636  -2217       O  
ATOM    772  N   TYR A 111      -0.535 -13.625  43.076  1.00 29.40           N  
ANISOU  772  N   TYR A 111     4691   3151   3327    319   -456  -1003       N  
ATOM    773  CA  TYR A 111      -0.039 -13.418  44.432  1.00 29.73           C  
ANISOU  773  CA  TYR A 111     4582   3240   3475    140   -199   -919       C  
ATOM    774  C   TYR A 111       1.260 -12.629  44.435  1.00 36.65           C  
ANISOU  774  C   TYR A 111     5516   4158   4252    291      3   -756       C  
ATOM    775  O   TYR A 111       2.112 -12.861  43.583  1.00 32.48           O  
ANISOU  775  O   TYR A 111     5213   3589   3540    478     28   -684       O  
ATOM    776  CB  TYR A 111       0.202 -14.757  45.122  1.00 36.96           C  
ANISOU  776  CB  TYR A 111     5618   4069   4356    -28   -145   -931       C  
ATOM    777  CG  TYR A 111      -1.051 -15.519  45.471  1.00 38.70           C  
ANISOU  777  CG  TYR A 111     5738   4215   4752   -286   -224  -1100       C  
ATOM    778  CD1 TYR A 111      -1.608 -16.432  44.580  1.00 38.80           C  
ANISOU  778  CD1 TYR A 111     5870   4119   4752   -293   -440  -1245       C  
ATOM    779  CD2 TYR A 111      -1.669 -15.331  46.699  1.00 38.07           C  
ANISOU  779  CD2 TYR A 111     5446   4158   4861   -538    -53  -1138       C  
ATOM    780  CE1 TYR A 111      -2.761 -17.131  44.903  1.00 35.92           C  
ANISOU  780  CE1 TYR A 111     5366   3667   4617   -578   -481  -1442       C  
ATOM    781  CE2 TYR A 111      -2.813 -16.022  47.034  1.00 42.17           C  
ANISOU  781  CE2 TYR A 111     5849   4589   5584   -815    -44  -1308       C  
ATOM    782  CZ  TYR A 111      -3.354 -16.923  46.136  1.00 41.35           C  
ANISOU  782  CZ  TYR A 111     5818   4372   5521   -852   -254  -1467       C  
ATOM    783  OH  TYR A 111      -4.497 -17.600  46.482  1.00 46.04           O  
ANISOU  783  OH  TYR A 111     6247   4861   6384  -1174   -211  -1675       O  
ATOM    784  N   VAL A 112       1.412 -11.714  45.395  1.00 31.00           N  
ANISOU  784  N   VAL A 112     4588   3516   3675    197    166   -724       N  
ATOM    785  CA  VAL A 112       2.688 -11.023  45.613  1.00 30.41           C  
ANISOU  785  CA  VAL A 112     4499   3476   3578    272    372   -625       C  
ATOM    786  C   VAL A 112       3.002 -11.019  47.113  1.00 26.50           C  
ANISOU  786  C   VAL A 112     3843   3050   3175    104    476   -652       C  
ATOM    787  O   VAL A 112       2.111 -10.826  47.933  1.00 30.50           O  
ANISOU  787  O   VAL A 112     4211   3582   3793    -56    473   -717       O  
ATOM    788  CB  VAL A 112       2.670  -9.568  45.056  1.00 26.84           C  
ANISOU  788  CB  VAL A 112     4003   3010   3186    381    466   -572       C  
ATOM    789  CG1 VAL A 112       3.939  -8.806  45.463  1.00 24.16           C  
ANISOU  789  CG1 VAL A 112     3576   2688   2914    373    722   -520       C  
ATOM    790  CG2 VAL A 112       2.557  -9.587  43.535  1.00 29.74           C  
ANISOU  790  CG2 VAL A 112     4642   3290   3369    613    377   -519       C  
ATOM    791  N   ASP A 113       4.259 -11.285  47.460  1.00 24.97           N  
ANISOU  791  N   ASP A 113     3679   2886   2922    162    557   -623       N  
ATOM    792  CA  ASP A 113       4.725 -11.241  48.842  1.00 22.25           C  
ANISOU  792  CA  ASP A 113     3228   2614   2612     74    602   -666       C  
ATOM    793  C   ASP A 113       6.220 -10.934  48.871  1.00 26.06           C  
ANISOU  793  C   ASP A 113     3624   3158   3121    196    683   -683       C  
ATOM    794  O   ASP A 113       7.057 -11.831  48.748  1.00 25.20           O  
ANISOU  794  O   ASP A 113     3615   3049   2911    325    635   -682       O  
ATOM    795  CB  ASP A 113       4.440 -12.568  49.564  1.00 22.73           C  
ANISOU  795  CB  ASP A 113     3473   2625   2540     11    513   -671       C  
ATOM    796  CG  ASP A 113       4.733 -12.494  51.061  1.00 22.96           C  
ANISOU  796  CG  ASP A 113     3478   2711   2533    -51    542   -709       C  
ATOM    797  OD1 ASP A 113       5.404 -11.537  51.509  1.00 25.67           O  
ANISOU  797  OD1 ASP A 113     3636   3155   2961    -21    587   -764       O  
ATOM    798  OD2 ASP A 113       4.291 -13.391  51.795  1.00 25.54           O  
ANISOU  798  OD2 ASP A 113     4003   2964   2737   -129    528   -695       O  
ATOM    799  N   TRP A 114       6.552  -9.667  49.048  1.00 22.44           N  
ANISOU  799  N   TRP A 114     2958   2741   2829    153    812   -723       N  
ATOM    800  CA  TRP A 114       7.942  -9.249  49.027  1.00 25.57           C  
ANISOU  800  CA  TRP A 114     3192   3188   3335    222    923   -789       C  
ATOM    801  C   TRP A 114       8.814  -9.842  50.142  1.00 24.01           C  
ANISOU  801  C   TRP A 114     2916   3099   3110    275    791   -907       C  
ATOM    802  O   TRP A 114      10.045  -9.859  50.009  1.00 25.97           O  
ANISOU  802  O   TRP A 114     3009   3405   3454    381    828   -998       O  
ATOM    803  CB  TRP A 114       7.997  -7.715  49.043  1.00 25.92           C  
ANISOU  803  CB  TRP A 114     3045   3208   3596    119   1107   -829       C  
ATOM    804  CG  TRP A 114       7.669  -7.183  47.704  1.00 24.88           C  
ANISOU  804  CG  TRP A 114     3048   2946   3460    173   1260   -705       C  
ATOM    805  CD1 TRP A 114       6.499  -6.613  47.304  1.00 25.24           C  
ANISOU  805  CD1 TRP A 114     3199   2907   3483    163   1241   -630       C  
ATOM    806  CD2 TRP A 114       8.499  -7.243  46.551  1.00 27.94           C  
ANISOU  806  CD2 TRP A 114     3526   3263   3825    289   1445   -644       C  
ATOM    807  NE1 TRP A 114       6.573  -6.278  45.980  1.00 24.64           N  
ANISOU  807  NE1 TRP A 114     3319   2705   3340    290   1373   -515       N  
ATOM    808  CE2 TRP A 114       7.785  -6.665  45.490  1.00 32.25           C  
ANISOU  808  CE2 TRP A 114     4298   3667   4288    354   1531   -511       C  
ATOM    809  CE3 TRP A 114       9.784  -7.741  46.307  1.00 26.40           C  
ANISOU  809  CE3 TRP A 114     3248   3111   3669    368   1555   -702       C  
ATOM    810  CZ2 TRP A 114       8.319  -6.538  44.211  1.00 27.30           C  
ANISOU  810  CZ2 TRP A 114     3882   2919   3571    484   1757   -410       C  
ATOM    811  CZ3 TRP A 114      10.308  -7.619  45.039  1.00 30.28           C  
ANISOU  811  CZ3 TRP A 114     3885   3497   4123    469   1814   -619       C  
ATOM    812  CH2 TRP A 114       9.576  -7.027  44.010  1.00 28.41           C  
ANISOU  812  CH2 TRP A 114     3939   3100   3756    522   1926   -462       C  
ATOM    813  N   ARG A 115       8.200 -10.352  51.215  1.00 23.74           N  
ANISOU  813  N   ARG A 115     2998   3083   2938    224    645   -916       N  
ATOM    814  CA  ARG A 115       8.956 -11.102  52.234  1.00 32.30           C  
ANISOU  814  CA  ARG A 115     4137   4238   3896    348    470  -1000       C  
ATOM    815  C   ARG A 115       9.654 -12.327  51.635  1.00 30.42           C  
ANISOU  815  C   ARG A 115     4052   3966   3539    560    383   -961       C  
ATOM    816  O   ARG A 115      10.743 -12.727  52.060  1.00 27.46           O  
ANISOU  816  O   ARG A 115     3614   3670   3150    751    251  -1069       O  
ATOM    817  CB  ARG A 115       8.045 -11.565  53.371  1.00 26.35           C  
ANISOU  817  CB  ARG A 115     3618   3450   2944    264    392   -967       C  
ATOM    818  CG  ARG A 115       7.356 -10.432  54.089  1.00 27.01           C  
ANISOU  818  CG  ARG A 115     3569   3571   3124     83    485  -1030       C  
ATOM    819  CD  ARG A 115       6.383 -10.958  55.142  1.00 25.98           C  
ANISOU  819  CD  ARG A 115     3699   3385   2786    -13    491   -989       C  
ATOM    820  NE  ARG A 115       5.286 -11.722  54.555  1.00 24.59           N  
ANISOU  820  NE  ARG A 115     3689   3080   2574   -124    571   -864       N  
ATOM    821  CZ  ARG A 115       4.297 -12.265  55.266  1.00 25.44           C  
ANISOU  821  CZ  ARG A 115     4008   3098   2561   -266    662   -826       C  
ATOM    822  NH1 ARG A 115       4.277 -12.127  56.587  1.00 26.76           N  
ANISOU  822  NH1 ARG A 115     4310   3286   2569   -283    699   -870       N  
ATOM    823  NH2 ARG A 115       3.338 -12.952  54.659  1.00 27.59           N  
ANISOU  823  NH2 ARG A 115     4364   3248   2871   -394    730   -762       N  
ATOM    824  N   GLN A 116       9.015 -12.924  50.645  1.00 25.08           N  
ANISOU  824  N   GLN A 116     3572   3172   2783    548    432   -834       N  
ATOM    825  CA  GLN A 116       9.555 -14.136  50.045  1.00 39.04           C  
ANISOU  825  CA  GLN A 116     5538   4876   4421    749    359   -801       C  
ATOM    826  C   GLN A 116      10.776 -13.826  49.173  1.00 40.73           C  
ANISOU  826  C   GLN A 116     5535   5158   4783    906    474   -872       C  
ATOM    827  O   GLN A 116      11.593 -14.702  48.908  1.00 34.79           O  
ANISOU  827  O   GLN A 116     4850   4400   3968   1127    414   -907       O  
ATOM    828  CB  GLN A 116       8.469 -14.848  49.239  1.00 37.72           C  
ANISOU  828  CB  GLN A 116     5647   4551   4133    674    363   -687       C  
ATOM    829  CG  GLN A 116       7.309 -15.329  50.119  1.00 45.45           C  
ANISOU  829  CG  GLN A 116     6820   5437   5010    493    305   -646       C  
ATOM    830  CD  GLN A 116       6.283 -16.159  49.362  1.00 51.09           C  
ANISOU  830  CD  GLN A 116     7763   5987   5661    398    286   -596       C  
ATOM    831  OE1 GLN A 116       6.167 -16.068  48.139  1.00 47.89           O  
ANISOU  831  OE1 GLN A 116     7350   5561   5284    446    291   -593       O  
ATOM    832  NE2 GLN A 116       5.533 -16.978  50.094  1.00 57.21           N  
ANISOU  832  NE2 GLN A 116     8763   6628   6345    260    272   -573       N  
ATOM    833  N   LYS A 117      10.906 -12.571  48.749  1.00 36.83           N  
ANISOU  833  N   LYS A 117     4790   4708   4495    792    672   -900       N  
ATOM    834  CA  LYS A 117      12.026 -12.165  47.908  1.00 33.68           C  
ANISOU  834  CA  LYS A 117     4184   4343   4271    885    884   -969       C  
ATOM    835  C   LYS A 117      13.159 -11.545  48.727  1.00 35.97           C  
ANISOU  835  C   LYS A 117     4071   4779   4818    892    884  -1184       C  
ATOM    836  O   LYS A 117      14.065 -10.942  48.178  1.00 34.64           O  
ANISOU  836  O   LYS A 117     3634   4637   4890    888   1123  -1284       O  
ATOM    837  CB  LYS A 117      11.552 -11.174  46.843  1.00 35.36           C  
ANISOU  837  CB  LYS A 117     4428   4460   4546    766   1152   -864       C  
ATOM    838  CG  LYS A 117      10.363 -11.649  45.999  1.00 34.01           C  
ANISOU  838  CG  LYS A 117     4622   4163   4137    777   1090   -701       C  
ATOM    839  CD  LYS A 117      10.730 -12.821  45.095  1.00 48.29           C  
ANISOU  839  CD  LYS A 117     6673   5913   5764    982   1074   -672       C  
ATOM    840  CE  LYS A 117      10.513 -12.496  43.607  1.00 55.76           C  
ANISOU  840  CE  LYS A 117     7844   6745   6596   1052   1268   -570       C  
ATOM    841  NZ  LYS A 117       9.093 -12.204  43.235  1.00 48.80           N  
ANISOU  841  NZ  LYS A 117     7168   5782   5591    974   1135   -480       N  
ATOM    842  N   GLY A 118      13.086 -11.655  50.046  1.00 31.79           N  
ANISOU  842  N   GLY A 118     4109   3406   4562    693   1345   -667       N  
ATOM    843  CA  GLY A 118      14.125 -11.120  50.904  1.00 26.61           C  
ANISOU  843  CA  GLY A 118     3300   2758   4053    760   1312   -542       C  
ATOM    844  C   GLY A 118      14.188  -9.602  50.908  1.00 30.22           C  
ANISOU  844  C   GLY A 118     3726   3359   4399    705   1263   -453       C  
ATOM    845  O   GLY A 118      15.246  -9.024  51.157  1.00 28.92           O  
ANISOU  845  O   GLY A 118     3436   3223   4331    744   1286   -385       O  
ATOM    846  N   ALA A 119      13.057  -8.948  50.647  1.00 25.38           N  
ANISOU  846  N   ALA A 119     3217   2829   3597    613   1185   -445       N  
ATOM    847  CA  ALA A 119      13.043  -7.497  50.486  1.00 24.77           C  
ANISOU  847  CA  ALA A 119     3124   2876   3412    556   1145   -367       C  
ATOM    848  C   ALA A 119      12.435  -6.774  51.684  1.00 24.22           C  
ANISOU  848  C   ALA A 119     3034   2825   3345    534    975   -252       C  
ATOM    849  O   ALA A 119      12.322  -5.546  51.693  1.00 20.29           O  
ANISOU  849  O   ALA A 119     2523   2409   2776    488    926   -185       O  
ATOM    850  CB  ALA A 119      12.295  -7.121  49.212  1.00 38.08           C  
ANISOU  850  CB  ALA A 119     4933   4649   4886    468   1186   -431       C  
ATOM    851  N   VAL A 120      12.058  -7.544  52.701  1.00 23.67           N  
ANISOU  851  N   VAL A 120     2962   2671   3358    566    892   -231       N  
ATOM    852  CA  VAL A 120      11.418  -6.977  53.888  1.00 25.94           C  
ANISOU  852  CA  VAL A 120     3244   2976   3635    541    746   -137       C  
ATOM    853  C   VAL A 120      12.193  -7.328  55.164  1.00 24.51           C  
ANISOU  853  C   VAL A 120     2970   2734   3609    602    685    -58       C  
ATOM    854  O   VAL A 120      12.458  -8.499  55.433  1.00 22.78           O  
ANISOU  854  O   VAL A 120     2737   2418   3499    658    704    -73       O  
ATOM    855  CB  VAL A 120       9.959  -7.467  54.007  1.00 22.70           C  
ANISOU  855  CB  VAL A 120     2938   2543   3143    493    684   -167       C  
ATOM    856  CG1 VAL A 120       9.281  -6.845  55.217  1.00 19.93           C  
ANISOU  856  CG1 VAL A 120     2581   2215   2776    465    559    -80       C  
ATOM    857  CG2 VAL A 120       9.188  -7.119  52.743  1.00 19.97           C  
ANISOU  857  CG2 VAL A 120     2680   2264   2644    426    719   -234       C  
ATOM    858  N   THR A 121      12.563  -6.321  55.946  1.00 18.68           N  
ANISOU  858  N   THR A 121     2168   2048   2882    589    606     29       N  
ATOM    859  CA  THR A 121      13.268  -6.569  57.206  1.00 19.07           C  
ANISOU  859  CA  THR A 121     2134   2057   3053    631    522    114       C  
ATOM    860  C   THR A 121      12.350  -7.165  58.284  1.00 21.87           C  
ANISOU  860  C   THR A 121     2555   2369   3385    616    422    152       C  
ATOM    861  O   THR A 121      11.135  -7.221  58.101  1.00 24.00           O  
ANISOU  861  O   THR A 121     2921   2648   3551    569    417    113       O  
ATOM    862  CB  THR A 121      13.898  -5.285  57.745  1.00 20.08           C  
ANISOU  862  CB  THR A 121     2186   2257   3185    602    458    183       C  
ATOM    863  OG1 THR A 121      12.867  -4.324  57.991  1.00 24.06           O  
ANISOU  863  OG1 THR A 121     2766   2819   3557    530    397    188       O  
ATOM    864  CG2 THR A 121      14.901  -4.726  56.729  1.00 20.08           C  
ANISOU  864  CG2 THR A 121     2107   2296   3226    612    563    161       C  
ATOM    865  N   PRO A 122      12.932  -7.616  59.411  1.00 21.24           N  
ANISOU  865  N   PRO A 122     2419   2247   3404    651    340    236       N  
ATOM    866  CA  PRO A 122      12.046  -8.110  60.470  1.00 20.85           C  
ANISOU  866  CA  PRO A 122     2441   2169   3311    624    251    285       C  
ATOM    867  C   PRO A 122      11.088  -7.052  60.991  1.00 16.47           C  
ANISOU  867  C   PRO A 122     1949   1699   2611    543    192    292       C  
ATOM    868  O   PRO A 122      11.396  -5.868  61.011  1.00 17.88           O  
ANISOU  868  O   PRO A 122     2093   1949   2751    515    174    297       O  
ATOM    869  CB  PRO A 122      13.024  -8.550  61.567  1.00 24.15           C  
ANISOU  869  CB  PRO A 122     2779   2550   3847    668    160    394       C  
ATOM    870  CG  PRO A 122      14.251  -9.015  60.795  1.00 26.77           C  
ANISOU  870  CG  PRO A 122     3002   2828   4341    752    241    374       C  
ATOM    871  CD  PRO A 122      14.338  -8.045  59.616  1.00 27.32           C  
ANISOU  871  CD  PRO A 122     3064   2972   4345    726    341    287       C  
ATOM    872  N   VAL A 123       9.919  -7.505  61.417  1.00 20.49           N  
ANISOU  872  N   VAL A 123     2543   2188   3054    507    171    289       N  
ATOM    873  CA  VAL A 123       8.898  -6.630  61.976  1.00 22.79           C  
ANISOU  873  CA  VAL A 123     2889   2546   3225    437    131    290       C  
ATOM    874  C   VAL A 123       9.406  -5.793  63.147  1.00 19.01           C  
ANISOU  874  C   VAL A 123     2383   2122   2720    413     45    354       C  
ATOM    875  O   VAL A 123      10.088  -6.294  64.040  1.00 22.55           O  
ANISOU  875  O   VAL A 123     2805   2549   3214    430    -23    430       O  
ATOM    876  CB  VAL A 123       7.678  -7.475  62.406  1.00 26.44           C  
ANISOU  876  CB  VAL A 123     3430   2968   3649    405    127    292       C  
ATOM    877  CG1 VAL A 123       6.707  -6.653  63.219  1.00 16.49           C  
ANISOU  877  CG1 VAL A 123     2211   1771   2283    340     94    301       C  
ATOM    878  CG2 VAL A 123       7.012  -8.022  61.163  1.00 21.77           C  
ANISOU  878  CG2 VAL A 123     2873   2340   3060    405    202    208       C  
ATOM    879  N   LYS A 124       9.090  -4.499  63.102  1.00 18.02           N  
ANISOU  879  N   LYS A 124     2262   2062   2522    370     44    322       N  
ATOM    880  CA  LYS A 124       9.530  -3.522  64.097  1.00 14.93           C  
ANISOU  880  CA  LYS A 124     1853   1723   2097    333    -30    354       C  
ATOM    881  C   LYS A 124       8.385  -3.095  65.014  1.00 19.55           C  
ANISOU  881  C   LYS A 124     2517   2339   2574    272    -48    340       C  
ATOM    882  O   LYS A 124       7.217  -3.382  64.728  1.00 19.27           O  
ANISOU  882  O   LYS A 124     2530   2290   2502    260      2    306       O  
ATOM    883  CB  LYS A 124      10.095  -2.300  63.374  1.00 16.50           C  
ANISOU  883  CB  LYS A 124     1997   1957   2315    327     -7    322       C  
ATOM    884  CG  LYS A 124      11.190  -2.680  62.371  1.00 19.48           C  
ANISOU  884  CG  LYS A 124     2294   2312   2795    382     41    327       C  
ATOM    885  CD  LYS A 124      11.715  -1.474  61.645  1.00 21.01           C  
ANISOU  885  CD  LYS A 124     2437   2542   3003    365     73    307       C  
ATOM    886  CE  LYS A 124      12.815  -1.865  60.633  1.00 31.82           C  
ANISOU  886  CE  LYS A 124     3723   3898   4471    415    144    309       C  
ATOM    887  NZ  LYS A 124      13.674  -0.703  60.255  1.00 24.39           N  
ANISOU  887  NZ  LYS A 124     2706   2993   3567    390    157    320       N  
ATOM    888  N   ASN A 125       8.721  -2.402  66.096  1.00 16.32           N  
ANISOU  888  N   ASN A 125     2115   1971   2115    230   -115    360       N  
ATOM    889  CA  ASN A 125       7.720  -1.912  67.043  1.00 17.93           C  
ANISOU  889  CA  ASN A 125     2393   2208   2211    169   -115    333       C  
ATOM    890  C   ASN A 125       7.899  -0.416  67.295  1.00 19.33           C  
ANISOU  890  C   ASN A 125     2563   2422   2359    128   -129    282       C  
ATOM    891  O   ASN A 125       8.936   0.014  67.816  1.00 21.56           O  
ANISOU  891  O   ASN A 125     2816   2728   2647    107   -203    304       O  
ATOM    892  CB  ASN A 125       7.809  -2.679  68.372  1.00 17.82           C  
ANISOU  892  CB  ASN A 125     2430   2207   2132    138   -182    403       C  
ATOM    893  CG  ASN A 125       6.557  -2.519  69.211  1.00 24.19           C  
ANISOU  893  CG  ASN A 125     3324   3043   2825     78   -142    373       C  
ATOM    894  OD1 ASN A 125       5.845  -1.523  69.083  1.00 24.39           O  
ANISOU  894  OD1 ASN A 125     3361   3085   2820     55    -86    293       O  
ATOM    895  ND2 ASN A 125       6.258  -3.514  70.039  1.00 25.81           N  
ANISOU  895  ND2 ASN A 125     3586   3246   2977     55   -161    440       N  
ATOM    896  N   GLN A 126       6.895   0.375  66.926  1.00 17.27           N  
ANISOU  896  N   GLN A 126     2322   2159   2079    115    -63    215       N  
ATOM    897  CA  GLN A 126       6.949   1.822  67.099  1.00 18.55           C  
ANISOU  897  CA  GLN A 126     2481   2333   2236     81    -63    159       C  
ATOM    898  C   GLN A 126       6.782   2.244  68.565  1.00 20.22           C  
ANISOU  898  C   GLN A 126     2758   2576   2347     15    -94    128       C  
ATOM    899  O   GLN A 126       7.075   3.382  68.914  1.00 18.30           O  
ANISOU  899  O   GLN A 126     2518   2337   2099    -23   -111     76       O  
ATOM    900  CB  GLN A 126       5.878   2.503  66.252  1.00 19.95           C  
ANISOU  900  CB  GLN A 126     2652   2484   2442     95     13    108       C  
ATOM    901  CG  GLN A 126       4.474   2.261  66.770  1.00 13.49           C  
ANISOU  901  CG  GLN A 126     1884   1668   1574     79     67     75       C  
ATOM    902  CD  GLN A 126       3.449   2.797  65.811  1.00 20.01           C  
ANISOU  902  CD  GLN A 126     2682   2467   2455    103    125     44       C  
ATOM    903  OE1 GLN A 126       3.130   2.166  64.804  1.00 16.87           O  
ANISOU  903  OE1 GLN A 126     2262   2060   2088    133    137     70       O  
ATOM    904  NE2 GLN A 126       2.976   4.012  66.083  1.00 19.30           N  
ANISOU  904  NE2 GLN A 126     2591   2359   2384     88    153    -11       N  
ATOM    905  N   GLY A 127       6.324   1.332  69.414  1.00 23.32           N  
ANISOU  905  N   GLY A 127     3210   2991   2659     -5    -98    157       N  
ATOM    906  CA  GLY A 127       6.162   1.632  70.834  1.00 24.60           C  
ANISOU  906  CA  GLY A 127     3452   3198   2696    -78   -120    130       C  
ATOM    907  C   GLY A 127       5.111   2.703  71.081  1.00 25.76           C  
ANISOU  907  C   GLY A 127     3635   3340   2813   -107    -29     22       C  
ATOM    908  O   GLY A 127       4.292   2.974  70.217  1.00 24.17           O  
ANISOU  908  O   GLY A 127     3397   3099   2688    -66     47    -11       O  
ATOM    909  N   SER A 128       5.154   3.357  72.238  1.00 26.85           N  
ANISOU  909  N   SER A 128     3843   3513   2845   -178    -40    -38       N  
ATOM    910  CA  SER A 128       4.171   4.398  72.534  1.00 35.69           C  
ANISOU  910  CA  SER A 128     4995   4614   3951   -201     63   -157       C  
ATOM    911  C   SER A 128       4.638   5.749  71.976  1.00 33.30           C  
ANISOU  911  C   SER A 128     4645   4260   3750   -193     53   -222       C  
ATOM    912  O   SER A 128       4.993   6.674  72.715  1.00 43.33           O  
ANISOU  912  O   SER A 128     5959   5532   4974   -253     35   -303       O  
ATOM    913  CB  SER A 128       3.919   4.482  74.040  1.00 35.93           C  
ANISOU  913  CB  SER A 128     5136   4704   3810   -289     80   -211       C  
ATOM    914  OG  SER A 128       5.147   4.601  74.730  1.00 42.85           O  
ANISOU  914  OG  SER A 128     6049   5626   4607   -349    -47   -189       O  
ATOM    915  N   CYS A 129       4.650   5.823  70.655  1.00 27.24           N  
ANISOU  915  N   CYS A 129     3792   3444   3114   -125     62   -184       N  
ATOM    916  CA  CYS A 129       5.113   6.982  69.909  1.00 20.05           C  
ANISOU  916  CA  CYS A 129     2826   2477   2315   -112     52   -212       C  
ATOM    917  C   CYS A 129       4.316   6.930  68.631  1.00 24.37           C  
ANISOU  917  C   CYS A 129     3312   2981   2965    -41    111   -181       C  
ATOM    918  O   CYS A 129       4.243   5.884  68.001  1.00 24.03           O  
ANISOU  918  O   CYS A 129     3246   2960   2926     -3    104   -110       O  
ATOM    919  CB  CYS A 129       6.631   6.923  69.634  1.00 16.62           C  
ANISOU  919  CB  CYS A 129     2346   2059   1911   -123    -54   -149       C  
ATOM    920  SG  CYS A 129       7.277   8.281  68.592  1.00 24.97           S  
ANISOU  920  SG  CYS A 129     3327   3045   3114   -115    -60   -159       S  
ATOM    921  N   GLY A 130       3.682   8.031  68.253  1.00 22.86           N  
ANISOU  921  N   GLY A 130     3099   2728   2860    -26    166   -235       N  
ATOM    922  CA  GLY A 130       2.895   8.025  67.033  1.00 19.40           C  
ANISOU  922  CA  GLY A 130     2602   2255   2515     35    203   -193       C  
ATOM    923  C   GLY A 130       3.766   8.246  65.804  1.00 14.87           C  
ANISOU  923  C   GLY A 130     1973   1666   2010     57    154   -120       C  
ATOM    924  O   GLY A 130       3.583   9.201  65.060  1.00 18.74           O  
ANISOU  924  O   GLY A 130     2427   2100   2594     75    166   -112       O  
ATOM    925  N   SER A 131       4.693   7.319  65.576  1.00 18.19           N  
ANISOU  925  N   SER A 131     2386   2135   2389     58    105    -61       N  
ATOM    926  CA  SER A 131       5.714   7.478  64.550  1.00 25.51           C  
ANISOU  926  CA  SER A 131     3263   3059   3370     69     73      0       C  
ATOM    927  C   SER A 131       5.537   6.572  63.329  1.00 21.65           C  
ANISOU  927  C   SER A 131     2749   2592   2884    114     88     62       C  
ATOM    928  O   SER A 131       6.456   6.419  62.534  1.00 19.82           O  
ANISOU  928  O   SER A 131     2482   2373   2675    123     77    109       O  
ATOM    929  CB  SER A 131       7.075   7.202  65.183  1.00 22.24           C  
ANISOU  929  CB  SER A 131     2842   2678   2930     37      9     14       C  
ATOM    930  OG  SER A 131       7.070   5.906  65.754  1.00 21.29           O  
ANISOU  930  OG  SER A 131     2749   2604   2736     45    -10     35       O  
ATOM    931  N   ALA A 132       4.360   5.974  63.165  1.00 16.25           N  
ANISOU  931  N   ALA A 132     2083   1913   2178    136    120     56       N  
ATOM    932  CA  ALA A 132       4.189   4.977  62.114  1.00 14.35           C  
ANISOU  932  CA  ALA A 132     1834   1695   1923    164    127     97       C  
ATOM    933  C   ALA A 132       4.418   5.522  60.711  1.00 13.16           C  
ANISOU  933  C   ALA A 132     1652   1539   1808    176    131    141       C  
ATOM    934  O   ALA A 132       4.759   4.760  59.806  1.00 15.75           O  
ANISOU  934  O   ALA A 132     1979   1894   2112    189    139    168       O  
ATOM    935  CB  ALA A 132       2.815   4.360  62.196  1.00 11.18           C  
ANISOU  935  CB  ALA A 132     1450   1296   1503    172    152     80       C  
ATOM    936  N   TRP A 133       4.213   6.829  60.532  1.00 11.29           N  
ANISOU  936  N   TRP A 133     1397   1264   1629    167    130    146       N  
ATOM    937  CA  TRP A 133       4.517   7.489  59.264  1.00 15.03           C  
ANISOU  937  CA  TRP A 133     1846   1731   2132    167    129    206       C  
ATOM    938  C   TRP A 133       5.973   7.240  58.880  1.00 22.61           C  
ANISOU  938  C   TRP A 133     2790   2720   3082    157    135    234       C  
ATOM    939  O   TRP A 133       6.291   7.020  57.705  1.00 17.57           O  
ANISOU  939  O   TRP A 133     2146   2111   2419    159    155    279       O  
ATOM    940  CB  TRP A 133       4.238   9.002  59.347  1.00 18.46           C  
ANISOU  940  CB  TRP A 133     2262   2098   2654    158    123    214       C  
ATOM    941  CG  TRP A 133       4.930   9.725  60.490  1.00 18.42           C  
ANISOU  941  CG  TRP A 133     2257   2054   2688    129    118    161       C  
ATOM    942  CD1 TRP A 133       4.492   9.832  61.787  1.00 18.83           C  
ANISOU  942  CD1 TRP A 133     2333   2085   2735    120    126     81       C  
ATOM    943  CD2 TRP A 133       6.179  10.433  60.432  1.00 17.37           C  
ANISOU  943  CD2 TRP A 133     2101   1903   2597     95    105    181       C  
ATOM    944  NE1 TRP A 133       5.393  10.560  62.530  1.00 20.07           N  
ANISOU  944  NE1 TRP A 133     2495   2214   2918     79    108     43       N  
ATOM    945  CE2 TRP A 133       6.433  10.942  61.723  1.00 16.62           C  
ANISOU  945  CE2 TRP A 133     2020   1774   2519     62     90    106       C  
ATOM    946  CE3 TRP A 133       7.106  10.679  59.414  1.00 16.10           C  
ANISOU  946  CE3 TRP A 133     1908   1754   2456     80    109    254       C  
ATOM    947  CZ2 TRP A 133       7.567  11.685  62.019  1.00 14.52           C  
ANISOU  947  CZ2 TRP A 133     1734   1482   2302     14     64    101       C  
ATOM    948  CZ3 TRP A 133       8.248  11.414  59.720  1.00 15.28           C  
ANISOU  948  CZ3 TRP A 133     1773   1623   2411     35     95    256       C  
ATOM    949  CH2 TRP A 133       8.466  11.900  61.010  1.00 16.07           C  
ANISOU  949  CH2 TRP A 133     1883   1686   2537      2     65    180       C  
ATOM    950  N   ALA A 134       6.844   7.243  59.884  1.00 15.85           N  
ANISOU  950  N   ALA A 134     1921   1861   2239    141    118    206       N  
ATOM    951  CA  ALA A 134       8.278   7.036  59.634  1.00 17.02           C  
ANISOU  951  CA  ALA A 134     2028   2033   2406    133    121    235       C  
ATOM    952  C   ALA A 134       8.575   5.557  59.390  1.00 17.65           C  
ANISOU  952  C   ALA A 134     2110   2153   2444    166    139    236       C  
ATOM    953  O   ALA A 134       9.348   5.224  58.502  1.00 16.73           O  
ANISOU  953  O   ALA A 134     1962   2058   2335    177    178    264       O  
ATOM    954  CB  ALA A 134       9.106   7.566  60.795  1.00 17.47           C  
ANISOU  954  CB  ALA A 134     2062   2074   2500     98     76    211       C  
ATOM    955  N   PHE A 135       7.959   4.673  60.177  1.00 17.19           N  
ANISOU  955  N   PHE A 135     2088   2098   2346    181    122    205       N  
ATOM    956  CA  PHE A 135       8.127   3.231  59.962  1.00 16.01           C  
ANISOU  956  CA  PHE A 135     1945   1964   2173    214    139    206       C  
ATOM    957  C   PHE A 135       7.649   2.832  58.586  1.00 13.86           C  
ANISOU  957  C   PHE A 135     1692   1704   1870    229    189    207       C  
ATOM    958  O   PHE A 135       8.302   2.074  57.894  1.00 18.92           O  
ANISOU  958  O   PHE A 135     2321   2355   2512    250    230    208       O  
ATOM    959  CB  PHE A 135       7.393   2.434  61.057  1.00 14.70           C  
ANISOU  959  CB  PHE A 135     1824   1791   1971    216    112    183       C  
ATOM    960  CG  PHE A 135       8.164   2.377  62.319  1.00 15.89           C  
ANISOU  960  CG  PHE A 135     1962   1945   2129    202     58    193       C  
ATOM    961  CD1 PHE A 135       8.171   3.466  63.181  1.00 15.07           C  
ANISOU  961  CD1 PHE A 135     1866   1842   2019    160     23    172       C  
ATOM    962  CD2 PHE A 135       8.949   1.264  62.622  1.00 16.23           C  
ANISOU  962  CD2 PHE A 135     1985   1988   2192    228     36    224       C  
ATOM    963  CE1 PHE A 135       8.934   3.448  64.331  1.00 15.96           C  
ANISOU  963  CE1 PHE A 135     1975   1969   2120    132    -42    180       C  
ATOM    964  CE2 PHE A 135       9.707   1.239  63.771  1.00 16.85           C  
ANISOU  964  CE2 PHE A 135     2049   2078   2275    209    -35    250       C  
ATOM    965  CZ  PHE A 135       9.707   2.325  64.624  1.00 19.65           C  
ANISOU  965  CZ  PHE A 135     2418   2447   2599    156    -79    228       C  
ATOM    966  N   SER A 136       6.485   3.334  58.203  1.00 14.01           N  
ANISOU  966  N   SER A 136     1741   1720   1861    215    184    204       N  
ATOM    967  CA  SER A 136       5.932   3.058  56.888  1.00 17.85           C  
ANISOU  967  CA  SER A 136     2253   2228   2300    213    209    210       C  
ATOM    968  C   SER A 136       6.894   3.483  55.772  1.00 21.93           C  
ANISOU  968  C   SER A 136     2752   2771   2809    205    251    244       C  
ATOM    969  O   SER A 136       7.192   2.715  54.854  1.00 21.21           O  
ANISOU  969  O   SER A 136     2681   2706   2673    210    299    230       O  
ATOM    970  CB  SER A 136       4.602   3.788  56.719  1.00 16.18           C  
ANISOU  970  CB  SER A 136     2055   2009   2084    198    177    222       C  
ATOM    971  OG  SER A 136       4.173   3.716  55.373  1.00 21.62           O  
ANISOU  971  OG  SER A 136     2767   2729   2719    184    179    246       O  
ATOM    972  N   ALA A 137       7.390   4.710  55.864  1.00 19.08           N  
ANISOU  972  N   ALA A 137     2356   2399   2495    186    243    284       N  
ATOM    973  CA  ALA A 137       8.328   5.203  54.864  1.00 20.05           C  
ANISOU  973  CA  ALA A 137     2455   2546   2616    167    291    328       C  
ATOM    974  C   ALA A 137       9.619   4.382  54.837  1.00 17.83           C  
ANISOU  974  C   ALA A 137     2133   2282   2359    188    348    308       C  
ATOM    975  O   ALA A 137      10.091   3.987  53.761  1.00 20.04           O  
ANISOU  975  O   ALA A 137     2419   2597   2597    187    422    310       O  
ATOM    976  CB  ALA A 137       8.640   6.678  55.119  1.00 20.81           C  
ANISOU  976  CB  ALA A 137     2516   2610   2781    137    267    376       C  
ATOM    977  N   VAL A 138      10.194   4.129  56.011  1.00 15.17           N  
ANISOU  977  N   VAL A 138     1753   1921   2089    206    315    291       N  
ATOM    978  CA  VAL A 138      11.472   3.411  56.054  1.00 19.78           C  
ANISOU  978  CA  VAL A 138     2273   2512   2730    233    357    287       C  
ATOM    979  C   VAL A 138      11.321   2.000  55.469  1.00 22.19           C  
ANISOU  979  C   VAL A 138     2612   2822   2998    273    414    243       C  
ATOM    980  O   VAL A 138      12.199   1.512  54.755  1.00 19.54           O  
ANISOU  980  O   VAL A 138     2240   2499   2686    294    498    233       O  
ATOM    981  CB  VAL A 138      12.029   3.325  57.489  1.00 22.37           C  
ANISOU  981  CB  VAL A 138     2552   2817   3131    240    283    290       C  
ATOM    982  CG1 VAL A 138      13.148   2.276  57.585  1.00 20.12           C  
ANISOU  982  CG1 VAL A 138     2197   2529   2918    285    311    292       C  
ATOM    983  CG2 VAL A 138      12.530   4.685  57.943  1.00 18.02           C  
ANISOU  983  CG2 VAL A 138     1957   2259   2632    191    241    319       C  
ATOM    984  N   SER A 139      10.199   1.349  55.751  1.00 18.59           N  
ANISOU  984  N   SER A 139     2223   2350   2490    281    379    210       N  
ATOM    985  CA  SER A 139      10.015  -0.017  55.271  1.00 20.03           C  
ANISOU  985  CA  SER A 139     2442   2519   2648    312    427    160       C  
ATOM    986  C   SER A 139      10.085  -0.036  53.750  1.00 16.55           C  
ANISOU  986  C   SER A 139     2036   2117   2135    295    514    137       C  
ATOM    987  O   SER A 139      10.756  -0.884  53.164  1.00 22.17           O  
ANISOU  987  O   SER A 139     2739   2823   2860    323    599     94       O  
ATOM    988  CB  SER A 139       8.689  -0.608  55.763  1.00 18.55           C  
ANISOU  988  CB  SER A 139     2322   2310   2418    306    373    134       C  
ATOM    989  OG  SER A 139       8.673  -2.013  55.560  1.00 23.54           O  
ANISOU  989  OG  SER A 139     2980   2905   3057    336    410     86       O  
ATOM    990  N   THR A 140       9.434   0.923  53.108  1.00 14.84           N  
ANISOU  990  N   THR A 140     1856   1939   1842    248    495    168       N  
ATOM    991  CA  THR A 140       9.438   0.949  51.645  1.00 20.99           C  
ANISOU  991  CA  THR A 140     2684   2769   2521    217    566    159       C  
ATOM    992  C   THR A 140      10.821   1.314  51.073  1.00 18.50           C  
ANISOU  992  C   THR A 140     2313   2482   2236    216    667    180       C  
ATOM    993  O   THR A 140      11.174   0.894  49.975  1.00 19.58           O  
ANISOU  993  O   THR A 140     2482   2656   2301    204    767    145       O  
ATOM    994  CB  THR A 140       8.370   1.917  51.095  1.00 19.90           C  
ANISOU  994  CB  THR A 140     2597   2665   2298    165    503    212       C  
ATOM    995  OG1 THR A 140       8.711   3.278  51.401  1.00 21.40           O  
ANISOU  995  OG1 THR A 140     2737   2850   2546    149    475    291       O  
ATOM    996  CG2 THR A 140       7.013   1.586  51.701  1.00 20.30           C  
ANISOU  996  CG2 THR A 140     2680   2689   2344    167    412    192       C  
ATOM    997  N   ILE A 141      11.599   2.081  51.818  1.00 18.01           N  
ANISOU  997  N   ILE A 141     2163   2402   2278    222    645    233       N  
ATOM    998  CA  ILE A 141      12.945   2.430  51.363  1.00 18.81           C  
ANISOU  998  CA  ILE A 141     2188   2526   2434    217    740    259       C  
ATOM    999  C   ILE A 141      13.855   1.211  51.489  1.00 21.98           C  
ANISOU  999  C   ILE A 141     2531   2904   2916    278    819    199       C  
ATOM   1000  O   ILE A 141      14.567   0.859  50.548  1.00 24.23           O  
ANISOU 1000  O   ILE A 141     2802   3217   3188    283    950    169       O  
ATOM   1001  CB  ILE A 141      13.520   3.609  52.160  1.00 17.87           C  
ANISOU 1001  CB  ILE A 141     1985   2388   2417    195    682    330       C  
ATOM   1002  CG1 ILE A 141      12.740   4.889  51.851  1.00 22.22           C  
ANISOU 1002  CG1 ILE A 141     2587   2947   2911    138    628    393       C  
ATOM   1003  CG2 ILE A 141      15.010   3.818  51.831  1.00 18.30           C  
ANISOU 1003  CG2 ILE A 141     1932   2460   2561    191    778    355       C  
ATOM   1004  CD1 ILE A 141      12.763   5.884  52.993  1.00 26.17           C  
ANISOU 1004  CD1 ILE A 141     3040   3398   3507    122    532    427       C  
ATOM   1005  N   GLU A 142      13.823   0.555  52.648  1.00 20.61           N  
ANISOU 1005  N   GLU A 142     2326   2676   2829    326    745    183       N  
ATOM   1006  CA  GLU A 142      14.568  -0.695  52.830  1.00 24.82           C  
ANISOU 1006  CA  GLU A 142     2804   3166   3459    395    803    136       C  
ATOM   1007  C   GLU A 142      14.313  -1.652  51.673  1.00 22.65           C  
ANISOU 1007  C   GLU A 142     2606   2895   3105    407    920     49       C  
ATOM   1008  O   GLU A 142      15.230  -2.236  51.136  1.00 21.59           O  
ANISOU 1008  O   GLU A 142     2419   2750   3032    444   1043      7       O  
ATOM   1009  CB  GLU A 142      14.190  -1.359  54.157  1.00 24.41           C  
ANISOU 1009  CB  GLU A 142     2751   3056   3469    432    690    142       C  
ATOM   1010  CG  GLU A 142      14.725  -0.625  55.389  1.00 20.62           C  
ANISOU 1010  CG  GLU A 142     2186   2571   3075    423    583    213       C  
ATOM   1011  CD  GLU A 142      14.170  -1.166  56.687  1.00 21.86           C  
ANISOU 1011  CD  GLU A 142     2372   2689   3246    439    468    225       C  
ATOM   1012  OE1 GLU A 142      13.132  -1.879  56.652  1.00 16.98           O  
ANISOU 1012  OE1 GLU A 142     1845   2047   2559    445    461    187       O  
ATOM   1013  OE2 GLU A 142      14.763  -0.864  57.749  1.00 23.29           O  
ANISOU 1013  OE2 GLU A 142     2486   2866   3499    437    381    276       O  
ATOM   1014  N   SER A 143      13.048  -1.783  51.287  1.00 21.80           N  
ANISOU 1014  N   SER A 143     2619   2801   2864    370    881     17       N  
ATOM   1015  CA  SER A 143      12.623  -2.700  50.231  1.00 20.59           C  
ANISOU 1015  CA  SER A 143     2560   2651   2611    363    967    -79       C  
ATOM   1016  C   SER A 143      13.109  -2.309  48.839  1.00 20.61           C  
ANISOU 1016  C   SER A 143     2591   2729   2512    321   1099   -100       C  
ATOM   1017  O   SER A 143      13.697  -3.122  48.122  1.00 24.74           O  
ANISOU 1017  O   SER A 143     3122   3244   3036    344   1237   -186       O  
ATOM   1018  CB  SER A 143      11.094  -2.793  50.232  1.00 20.45           C  
ANISOU 1018  CB  SER A 143     2651   2639   2481    318    865    -92       C  
ATOM   1019  OG  SER A 143      10.634  -3.432  51.415  1.00 27.31           O  
ANISOU 1019  OG  SER A 143     3506   3436   3434    355    777    -91       O  
ATOM   1020  N   ILE A 144      12.909  -1.049  48.461  1.00 18.86           N  
ANISOU 1020  N   ILE A 144     2384   2575   2206    257   1066    -18       N  
ATOM   1021  CA  ILE A 144      13.306  -0.627  47.112  1.00 20.14           C  
ANISOU 1021  CA  ILE A 144     2588   2819   2246    202   1188    -19       C  
ATOM   1022  C   ILE A 144      14.831  -0.656  46.935  1.00 24.53           C  
ANISOU 1022  C   ILE A 144     3031   3376   2913    236   1339    -25       C  
ATOM   1023  O   ILE A 144      15.328  -0.872  45.824  1.00 27.98           O  
ANISOU 1023  O   ILE A 144     3501   3864   3267    212   1496    -76       O  
ATOM   1024  CB  ILE A 144      12.757   0.768  46.770  1.00 25.89           C  
ANISOU 1024  CB  ILE A 144     3353   3607   2876    127   1109     93       C  
ATOM   1025  CG1 ILE A 144      12.748   0.970  45.259  1.00 28.83           C  
ANISOU 1025  CG1 ILE A 144     3822   4073   3060     53   1209     89       C  
ATOM   1026  CG2 ILE A 144      13.524   1.879  47.492  1.00 21.05           C  
ANISOU 1026  CG2 ILE A 144     2622   2977   2398    130   1080    195       C  
ATOM   1027  CD1 ILE A 144      12.092  -0.166  44.499  1.00 31.65           C  
ANISOU 1027  CD1 ILE A 144     4301   4449   3275     37   1243    -31       C  
ATOM   1028  N   ILE A 145      15.583  -0.467  48.013  1.00 20.82           N  
ANISOU 1028  N   ILE A 145     2427   2856   2629    287   1298     24       N  
ATOM   1029  CA  ILE A 145      17.038  -0.571  47.888  1.00 25.09           C  
ANISOU 1029  CA  ILE A 145     2835   3393   3305    323   1434     20       C  
ATOM   1030  C   ILE A 145      17.473  -2.024  47.704  1.00 31.20           C  
ANISOU 1030  C   ILE A 145     3592   4112   4152    401   1551    -97       C  
ATOM   1031  O   ILE A 145      18.454  -2.310  46.994  1.00 30.94           O  
ANISOU 1031  O   ILE A 145     3500   4094   4163    419   1722   -144       O  
ATOM   1032  CB  ILE A 145      17.750   0.076  49.087  1.00 23.81           C  
ANISOU 1032  CB  ILE A 145     2525   3196   3325    344   1338    111       C  
ATOM   1033  CG1 ILE A 145      17.569   1.590  48.967  1.00 26.09           C  
ANISOU 1033  CG1 ILE A 145     2825   3535   3553    259   1279    213       C  
ATOM   1034  CG2 ILE A 145      19.274  -0.263  49.104  1.00 22.94           C  
ANISOU 1034  CG2 ILE A 145     2246   3069   3399    398   1463    105       C  
ATOM   1035  CD1 ILE A 145      17.930   2.335  50.174  1.00 37.45           C  
ANISOU 1035  CD1 ILE A 145     4161   4938   5129    257   1152    288       C  
ATOM   1036  N   LYS A 146      16.737  -2.946  48.314  1.00 28.97           N  
ANISOU 1036  N   LYS A 146     3361   3758   3888    444   1462   -147       N  
ATOM   1037  CA  LYS A 146      16.992  -4.366  48.091  1.00 28.63           C  
ANISOU 1037  CA  LYS A 146     3323   3641   3914    515   1567   -264       C  
ATOM   1038  C   LYS A 146      16.659  -4.694  46.663  1.00 31.30           C  
ANISOU 1038  C   LYS A 146     3794   4032   4066    462   1697   -372       C  
ATOM   1039  O   LYS A 146      17.470  -5.295  45.942  1.00 33.94           O  
ANISOU 1039  O   LYS A 146     4104   4362   4428    478   1806   -448       O  
ATOM   1040  CB  LYS A 146      16.167  -5.242  49.036  1.00 34.37           C  
ANISOU 1040  CB  LYS A 146     4092   4277   4690    556   1433   -282       C  
ATOM   1041  CG  LYS A 146      16.150  -6.728  48.667  1.00 36.70           C  
ANISOU 1041  CG  LYS A 146     4432   4481   5031    612   1533   -413       C  
ATOM   1042  CD  LYS A 146      17.527  -7.339  48.756  1.00 46.03           C  
ANISOU 1042  CD  LYS A 146     5478   5607   6404    685   1598   -423       C  
ATOM   1043  CE  LYS A 146      17.468  -8.861  48.647  1.00 57.30           C  
ANISOU 1043  CE  LYS A 146     6946   6923   7901    735   1624   -525       C  
ATOM   1044  NZ  LYS A 146      17.147  -9.319  47.269  1.00 62.88           N  
ANISOU 1044  NZ  LYS A 146     7781   7662   8448    683   1738   -661       N  
ATOM   1045  N   ILE A 147      15.469  -4.279  46.248  1.00 28.04           N  
ANISOU 1045  N   ILE A 147     3523   3678   3455    382   1620   -366       N  
ATOM   1046  CA  ILE A 147      14.985  -4.593  44.910  1.00 31.18           C  
ANISOU 1046  CA  ILE A 147     4069   4137   3643    314   1711   -465       C  
ATOM   1047  C   ILE A 147      15.951  -4.086  43.841  1.00 32.04           C  
ANISOU 1047  C   ILE A 147     4150   4335   3688    272   1832   -457       C  
ATOM   1048  O   ILE A 147      16.268  -4.797  42.886  1.00 34.96           O  
ANISOU 1048  O   ILE A 147     4569   4721   3994    263   1928   -562       O  
ATOM   1049  CB  ILE A 147      13.573  -4.014  44.686  1.00 33.47           C  
ANISOU 1049  CB  ILE A 147     4489   4489   3741    225   1561   -417       C  
ATOM   1050  CG1 ILE A 147      12.540  -4.862  45.439  1.00 29.41           C  
ANISOU 1050  CG1 ILE A 147     4017   3889   3267    249   1428   -460       C  
ATOM   1051  CG2 ILE A 147      13.223  -3.995  43.202  1.00 37.26           C  
ANISOU 1051  CG2 ILE A 147     5116   5067   3974    131   1648   -483       C  
ATOM   1052  CD1 ILE A 147      11.165  -4.197  45.564  1.00 25.83           C  
ANISOU 1052  CD1 ILE A 147     3638   3482   2695    180   1248   -385       C  
ATOM   1053  N   ARG A 148      16.459  -2.877  44.029  1.00 33.85           N  
ANISOU 1053  N   ARG A 148     4297   4616   3948    248   1831   -332       N  
ATOM   1054  CA  ARG A 148      17.352  -2.287  43.046  1.00 35.85           C  
ANISOU 1054  CA  ARG A 148     4522   4958   4141    198   1943   -307       C  
ATOM   1055  C   ARG A 148      18.810  -2.744  43.159  1.00 39.24           C  
ANISOU 1055  C   ARG A 148     4797   5346   4767    269   2051   -341       C  
ATOM   1056  O   ARG A 148      19.470  -2.892  42.140  1.00 42.59           O  
ANISOU 1056  O   ARG A 148     5229   5825   5128    246   2178   -391       O  
ATOM   1057  CB  ARG A 148      17.285  -0.771  43.140  1.00 35.81           C  
ANISOU 1057  CB  ARG A 148     4497   5017   4094    131   1895   -150       C  
ATOM   1058  CG  ARG A 148      15.973  -0.202  42.645  1.00 45.33           C  
ANISOU 1058  CG  ARG A 148     5864   6285   5075     44   1807   -101       C  
ATOM   1059  CD  ARG A 148      15.810  -0.370  41.135  1.00 52.09           C  
ANISOU 1059  CD  ARG A 148     6847   7244   5700    -34   1870   -153       C  
ATOM   1060  NE  ARG A 148      14.541   0.208  40.708  1.00 53.41           N  
ANISOU 1060  NE  ARG A 148     7157   7471   5664   -119   1751    -85       N  
ATOM   1061  CZ  ARG A 148      13.405  -0.472  40.610  1.00 58.39           C  
ANISOU 1061  CZ  ARG A 148     7906   8092   6186   -134   1662   -158       C  
ATOM   1062  NH1 ARG A 148      13.380  -1.770  40.882  1.00 66.14           N  
ANISOU 1062  NH1 ARG A 148     8890   9001   7240    -71   1691   -306       N  
ATOM   1063  NH2 ARG A 148      12.294   0.141  40.225  1.00 51.20           N  
ANISOU 1063  NH2 ARG A 148     7106   7241   5108   -214   1534    -77       N  
ATOM   1064  N   THR A 149      19.307  -2.984  44.372  1.00 38.40           N  
ANISOU 1064  N   THR A 149     4552   5147   4893    353   1995   -309       N  
ATOM   1065  CA  THR A 149      20.741  -3.255  44.572  1.00 38.73           C  
ANISOU 1065  CA  THR A 149     4425   5152   5138    415   2071   -311       C  
ATOM   1066  C   THR A 149      21.090  -4.657  45.083  1.00 41.74           C  
ANISOU 1066  C   THR A 149     4752   5416   5690    520   2073   -397       C  
ATOM   1067  O   THR A 149      22.252  -5.054  45.050  1.00 40.25           O  
ANISOU 1067  O   THR A 149     4442   5196   5657    572   2150   -413       O  
ATOM   1068  CB  THR A 149      21.369  -2.243  45.562  1.00 39.14           C  
ANISOU 1068  CB  THR A 149     4321   5199   5353    419   1993   -174       C  
ATOM   1069  OG1 THR A 149      20.934  -2.543  46.898  1.00 32.69           O  
ANISOU 1069  OG1 THR A 149     3464   4296   4661    480   1849   -140       O  
ATOM   1070  CG2 THR A 149      20.984  -0.810  45.196  1.00 32.34           C  
ANISOU 1070  CG2 THR A 149     3509   4429   4352    316   1975    -72       C  
ATOM   1071  N   GLY A 150      20.105  -5.408  45.561  1.00 40.01           N  
ANISOU 1071  N   GLY A 150     4621   5128   5453    549   1987   -442       N  
ATOM   1072  CA  GLY A 150      20.366  -6.762  46.026  1.00 29.85           C  
ANISOU 1072  CA  GLY A 150     3295   3719   4325    640   1982   -512       C  
ATOM   1073  C   GLY A 150      20.655  -6.878  47.514  1.00 36.52           C  
ANISOU 1073  C   GLY A 150     4011   4479   5385    713   1849   -417       C  
ATOM   1074  O   GLY A 150      20.750  -7.981  48.050  1.00 37.21           O  
ANISOU 1074  O   GLY A 150     4073   4459   5605    786   1815   -448       O  
ATOM   1075  N   ASN A 151      20.773  -5.740  48.194  1.00 35.69           N  
ANISOU 1075  N   ASN A 151     3829   4421   5310    687   1765   -296       N  
ATOM   1076  CA  ASN A 151      21.106  -5.737  49.613  1.00 30.61           C  
ANISOU 1076  CA  ASN A 151     3061   3716   4852    743   1624   -197       C  
ATOM   1077  C   ASN A 151      19.971  -5.242  50.493  1.00 28.81           C  
ANISOU 1077  C   ASN A 151     2895   3490   4561    722   1484   -134       C  
ATOM   1078  O   ASN A 151      19.441  -4.163  50.255  1.00 30.54           O  
ANISOU 1078  O   ASN A 151     3164   3788   4653    654   1480    -95       O  
ATOM   1079  CB  ASN A 151      22.334  -4.873  49.861  1.00 37.16           C  
ANISOU 1079  CB  ASN A 151     3725   4588   5806    733   1622   -107       C  
ATOM   1080  CG  ASN A 151      23.533  -5.371  49.122  1.00 49.10           C  
ANISOU 1080  CG  ASN A 151     5153   6091   7410    764   1760   -160       C  
ATOM   1081  OD1 ASN A 151      24.017  -6.471  49.382  1.00 53.87           O  
ANISOU 1081  OD1 ASN A 151     5705   6608   8155    842   1764   -194       O  
ATOM   1082  ND2 ASN A 151      24.022  -4.573  48.183  1.00 60.15           N  
ANISOU 1082  ND2 ASN A 151     6540   7580   8734    702   1876   -162       N  
ATOM   1083  N   LEU A 152      19.624  -6.027  51.514  1.00 25.50           N  
ANISOU 1083  N   LEU A 152     2471   2983   4234    779   1371   -115       N  
ATOM   1084  CA  LEU A 152      18.597  -5.651  52.495  1.00 28.29           C  
ANISOU 1084  CA  LEU A 152     2885   3335   4527    755   1210    -50       C  
ATOM   1085  C   LEU A 152      19.254  -5.021  53.710  1.00 31.47           C  
ANISOU 1085  C   LEU A 152     3158   3747   5054    760   1069     72       C  
ATOM   1086  O   LEU A 152      20.011  -5.691  54.421  1.00 31.13           O  
ANISOU 1086  O   LEU A 152     2998   3636   5193    833   1030    113       O  
ATOM   1087  CB  LEU A 152      17.784  -6.873  52.927  1.00 26.35           C  
ANISOU 1087  CB  LEU A 152     2728   2995   4288    795   1157    -94       C  
ATOM   1088  CG  LEU A 152      16.641  -6.558  53.889  1.00 22.97           C  
ANISOU 1088  CG  LEU A 152     2390   2579   3760    744    976    -34       C  
ATOM   1089  CD1 LEU A 152      15.562  -5.768  53.151  1.00 27.67           C  
ANISOU 1089  CD1 LEU A 152     3116   3258   4140    652    979    -69       C  
ATOM   1090  CD2 LEU A 152      16.062  -7.832  54.532  1.00 26.74           C  
ANISOU 1090  CD2 LEU A 152     2918   2949   4291    788    919    -48       C  
ATOM   1091  N   ASN A 153      18.999  -3.732  53.917  1.00 27.83           N  
ANISOU 1091  N   ASN A 153     2714   3363   4497    678    989    130       N  
ATOM   1092  CA  ASN A 153      19.575  -2.972  55.025  1.00 23.91           C  
ANISOU 1092  CA  ASN A 153     2111   2883   4089    659    850    231       C  
ATOM   1093  C   ASN A 153      18.470  -2.459  55.950  1.00 22.66           C  
ANISOU 1093  C   ASN A 153     2062   2739   3808    602    687    264       C  
ATOM   1094  O   ASN A 153      17.320  -2.363  55.542  1.00 23.99           O  
ANISOU 1094  O   ASN A 153     2367   2922   3824    566    696    220       O  
ATOM   1095  CB  ASN A 153      20.384  -1.773  54.519  1.00 26.74           C  
ANISOU 1095  CB  ASN A 153     2380   3310   4471    604    909    267       C  
ATOM   1096  CG  ASN A 153      21.510  -2.165  53.567  1.00 30.20           C  
ANISOU 1096  CG  ASN A 153     2699   3747   5029    651   1096    234       C  
ATOM   1097  OD1 ASN A 153      21.580  -1.685  52.438  1.00 37.15           O  
ANISOU 1097  OD1 ASN A 153     3609   4681   5824    609   1237    201       O  
ATOM   1098  ND2 ASN A 153      22.385  -3.030  54.022  1.00 24.28           N  
ANISOU 1098  ND2 ASN A 153     1841   2939   4446    721   1075    243       N  
ATOM   1099  N   GLU A 154      18.821  -2.104  57.179  1.00 25.60           N  
ANISOU 1099  N   GLU A 154     2370   3111   4246    588    542    338       N  
ATOM   1100  CA  GLU A 154      17.862  -1.458  58.064  1.00 25.30           C  
ANISOU 1100  CA  GLU A 154     2430   3094   4090    526    408    359       C  
ATOM   1101  C   GLU A 154      18.207   0.012  58.162  1.00 26.56           C  
ANISOU 1101  C   GLU A 154     2549   3305   4239    450    371    391       C  
ATOM   1102  O   GLU A 154      19.357   0.368  58.454  1.00 18.94           O  
ANISOU 1102  O   GLU A 154     1449   2349   3396    444    343    438       O  
ATOM   1103  CB  GLU A 154      17.875  -2.100  59.446  1.00 32.02           C  
ANISOU 1103  CB  GLU A 154     3270   3910   4985    548    267    410       C  
ATOM   1104  CG  GLU A 154      17.577  -3.585  59.450  1.00 42.43           C  
ANISOU 1104  CG  GLU A 154     4623   5157   6341    623    294    394       C  
ATOM   1105  CD  GLU A 154      16.400  -3.902  60.333  1.00 44.66           C  
ANISOU 1105  CD  GLU A 154     5030   5426   6511    596    199    402       C  
ATOM   1106  OE1 GLU A 154      15.749  -2.943  60.787  1.00 58.86           O  
ANISOU 1106  OE1 GLU A 154     6894   7275   8196    525    137    402       O  
ATOM   1107  OE2 GLU A 154      16.121  -5.087  60.580  1.00 40.53           O  
ANISOU 1107  OE2 GLU A 154     4540   4838   6022    643    194    409       O  
ATOM   1108  N   TYR A 155      17.228   0.869  57.901  1.00 18.53           N  
ANISOU 1108  N   TYR A 155     1638   2312   3090    391    368    368       N  
ATOM   1109  CA  TYR A 155      17.468   2.307  57.958  1.00 20.81           C  
ANISOU 1109  CA  TYR A 155     1901   2630   3378    317    337    397       C  
ATOM   1110  C   TYR A 155      16.740   2.947  59.134  1.00 24.98           C  
ANISOU 1110  C   TYR A 155     2497   3151   3843    267    204    398       C  
ATOM   1111  O   TYR A 155      15.951   2.291  59.809  1.00 22.69           O  
ANISOU 1111  O   TYR A 155     2283   2847   3492    287    150    379       O  
ATOM   1112  CB  TYR A 155      17.060   2.977  56.645  1.00 16.70           C  
ANISOU 1112  CB  TYR A 155     1432   2133   2779    284    446    383       C  
ATOM   1113  CG  TYR A 155      17.894   2.485  55.483  1.00 20.23           C  
ANISOU 1113  CG  TYR A 155     1814   2598   3274    317    595    375       C  
ATOM   1114  CD1 TYR A 155      19.262   2.758  55.420  1.00 23.37           C  
ANISOU 1114  CD1 TYR A 155     2063   3007   3811    313    635    414       C  
ATOM   1115  CD2 TYR A 155      17.331   1.728  54.471  1.00 21.90           C  
ANISOU 1115  CD2 TYR A 155     2109   2817   3396    346    699    321       C  
ATOM   1116  CE1 TYR A 155      20.039   2.296  54.364  1.00 22.36           C  
ANISOU 1116  CE1 TYR A 155     1868   2897   3733    344    795    398       C  
ATOM   1117  CE2 TYR A 155      18.106   1.253  53.406  1.00 18.90           C  
ANISOU 1117  CE2 TYR A 155     1679   2456   3048    373    855    296       C  
ATOM   1118  CZ  TYR A 155      19.456   1.550  53.366  1.00 24.90           C  
ANISOU 1118  CZ  TYR A 155     2287   3226   3950    375    910    334       C  
ATOM   1119  OH  TYR A 155      20.210   1.090  52.325  1.00 23.52           O  
ANISOU 1119  OH  TYR A 155     2057   3069   3810    402   1085    302       O  
ATOM   1120  N   SER A 156      17.004   4.234  59.362  1.00 18.34           N  
ANISOU 1120  N   SER A 156     1630   2317   3020    198    163    414       N  
ATOM   1121  CA  SER A 156      16.625   4.877  60.615  1.00 18.35           C  
ANISOU 1121  CA  SER A 156     1675   2310   2986    146     40    403       C  
ATOM   1122  C   SER A 156      15.251   5.551  60.644  1.00 19.45           C  
ANISOU 1122  C   SER A 156     1939   2433   3020    118     41    362       C  
ATOM   1123  O   SER A 156      15.085   6.639  60.082  1.00 18.63           O  
ANISOU 1123  O   SER A 156     1843   2313   2920     78     74    364       O  
ATOM   1124  CB  SER A 156      17.667   5.936  60.981  1.00 20.36           C  
ANISOU 1124  CB  SER A 156     1835   2566   3334     78    -16    430       C  
ATOM   1125  OG  SER A 156      17.346   6.546  62.214  1.00 18.13           O  
ANISOU 1125  OG  SER A 156     1606   2275   3008     19   -132    401       O  
ATOM   1126  N   GLU A 157      14.296   4.955  61.360  1.00 16.33           N  
ANISOU 1126  N   GLU A 157     1629   2033   2543    137      2    331       N  
ATOM   1127  CA  GLU A 157      13.020   5.660  61.617  1.00 13.79           C  
ANISOU 1127  CA  GLU A 157     1404   1691   2143    109     -4    288       C  
ATOM   1128  C   GLU A 157      13.260   6.886  62.502  1.00 19.87           C  
ANISOU 1128  C   GLU A 157     2173   2444   2935     39    -72    265       C  
ATOM   1129  O   GLU A 157      12.657   7.945  62.314  1.00 21.41           O  
ANISOU 1129  O   GLU A 157     2404   2603   3130      9    -52    240       O  
ATOM   1130  CB  GLU A 157      11.996   4.733  62.289  1.00 14.54           C  
ANISOU 1130  CB  GLU A 157     1580   1790   2155    135    -22    261       C  
ATOM   1131  CG  GLU A 157      11.528   3.596  61.394  1.00 16.49           C  
ANISOU 1131  CG  GLU A 157     1847   2039   2379    193     45    266       C  
ATOM   1132  CD  GLU A 157      12.403   2.355  61.518  1.00 18.88           C  
ANISOU 1132  CD  GLU A 157     2099   2345   2729    237     37    296       C  
ATOM   1133  OE1 GLU A 157      13.284   2.321  62.400  1.00 24.05           O  
ANISOU 1133  OE1 GLU A 157     2702   3006   3428    225    -37    326       O  
ATOM   1134  OE2 GLU A 157      12.202   1.412  60.730  1.00 26.70           O  
ANISOU 1134  OE2 GLU A 157     3100   3325   3718    283    101    289       O  
ATOM   1135  N   GLN A 158      14.146   6.728  63.477  1.00 14.92           N  
ANISOU 1135  N   GLN A 158     1504   1836   2331     10   -158    273       N  
ATOM   1136  CA  GLN A 158      14.419   7.779  64.435  1.00 18.35           C  
ANISOU 1136  CA  GLN A 158     1946   2256   2769    -69   -236    236       C  
ATOM   1137  C   GLN A 158      14.852   9.053  63.706  1.00 23.03           C  
ANISOU 1137  C   GLN A 158     2490   2809   3453   -112   -202    242       C  
ATOM   1138  O   GLN A 158      14.441  10.167  64.066  1.00 21.23           O  
ANISOU 1138  O   GLN A 158     2308   2533   3225   -165   -214    190       O  
ATOM   1139  CB  GLN A 158      15.498   7.338  65.417  1.00 17.29           C  
ANISOU 1139  CB  GLN A 158     1756   2161   2654    -99   -350    265       C  
ATOM   1140  CG  GLN A 158      15.781   8.350  66.519  1.00 24.19           C  
ANISOU 1140  CG  GLN A 158     2654   3030   3507   -197   -447    213       C  
ATOM   1141  CD  GLN A 158      14.600   8.517  67.454  1.00 27.53           C  
ANISOU 1141  CD  GLN A 158     3214   3448   3797   -222   -452    132       C  
ATOM   1142  OE1 GLN A 158      13.938   7.536  67.805  1.00 21.05           O  
ANISOU 1142  OE1 GLN A 158     2453   2656   2888   -181   -443    141       O  
ATOM   1143  NE2 GLN A 158      14.342   9.759  67.881  1.00 24.86           N  
ANISOU 1143  NE2 GLN A 158     2926   3069   3453   -293   -458     50       N  
ATOM   1144  N   GLU A 159      15.658   8.876  62.661  1.00 20.07           N  
ANISOU 1144  N   GLU A 159     2023   2446   3157    -89   -148    304       N  
ATOM   1145  CA  GLU A 159      16.166  10.022  61.893  1.00 21.56           C  
ANISOU 1145  CA  GLU A 159     2158   2600   3434   -137   -107    331       C  
ATOM   1146  C   GLU A 159      15.021  10.815  61.263  1.00 22.08           C  
ANISOU 1146  C   GLU A 159     2306   2614   3468   -134    -46    317       C  
ATOM   1147  O   GLU A 159      15.017  12.038  61.301  1.00 20.93           O  
ANISOU 1147  O   GLU A 159     2166   2408   3379   -191    -56    307       O  
ATOM   1148  CB  GLU A 159      17.126   9.572  60.805  1.00 18.08           C  
ANISOU 1148  CB  GLU A 159     1612   2191   3065   -109    -32    400       C  
ATOM   1149  CG  GLU A 159      17.747  10.746  59.999  1.00 19.04           C  
ANISOU 1149  CG  GLU A 159     1672   2283   3280   -170     19    445       C  
ATOM   1150  CD  GLU A 159      18.961  10.293  59.195  1.00 25.07           C  
ANISOU 1150  CD  GLU A 159     2307   3089   4131   -157     92    507       C  
ATOM   1151  OE1 GLU A 159      18.904   9.210  58.585  1.00 29.68           O  
ANISOU 1151  OE1 GLU A 159     2888   3712   4676    -84    166    515       O  
ATOM   1152  OE2 GLU A 159      19.979  10.999  59.203  1.00 26.75           O  
ANISOU 1152  OE2 GLU A 159     2416   3291   4456   -222     79    541       O  
ATOM   1153  N   LEU A 160      14.043  10.118  60.699  1.00 17.12           N  
ANISOU 1153  N   LEU A 160     1740   2003   2763    -70      9    318       N  
ATOM   1154  CA  LEU A 160      12.929  10.805  60.064  1.00 20.26           C  
ANISOU 1154  CA  LEU A 160     2201   2357   3139    -63     52    320       C  
ATOM   1155  C   LEU A 160      12.025  11.450  61.114  1.00 21.16           C  
ANISOU 1155  C   LEU A 160     2383   2417   3241    -82      7    246       C  
ATOM   1156  O   LEU A 160      11.547  12.556  60.927  1.00 19.08           O  
ANISOU 1156  O   LEU A 160     2139   2082   3027   -104     19    243       O  
ATOM   1157  CB  LEU A 160      12.130   9.844  59.180  1.00 18.16           C  
ANISOU 1157  CB  LEU A 160     1977   2131   2794      1    109    339       C  
ATOM   1158  CG  LEU A 160      12.980   9.222  58.066  1.00 26.40           C  
ANISOU 1158  CG  LEU A 160     2967   3226   3840     18    177    394       C  
ATOM   1159  CD1 LEU A 160      12.184   8.205  57.293  1.00 24.59           C  
ANISOU 1159  CD1 LEU A 160     2792   3033   3519     70    225    390       C  
ATOM   1160  CD2 LEU A 160      13.505  10.302  57.142  1.00 32.96           C  
ANISOU 1160  CD2 LEU A 160     3760   4037   4726    -29    221    460       C  
ATOM   1161  N   LEU A 161      11.797  10.729  62.202  1.00 21.11           N  
ANISOU 1161  N   LEU A 161     2412   2441   3169    -73    -36    190       N  
ATOM   1162  CA  LEU A 161      11.138  11.254  63.395  1.00 19.25           C  
ANISOU 1162  CA  LEU A 161     2240   2168   2904   -104    -70    103       C  
ATOM   1163  C   LEU A 161      11.705  12.588  63.883  1.00 21.08           C  
ANISOU 1163  C   LEU A 161     2460   2335   3214   -180   -106     63       C  
ATOM   1164  O   LEU A 161      10.963  13.548  64.111  1.00 20.32           O  
ANISOU 1164  O   LEU A 161     2409   2162   3150   -195    -85      7       O  
ATOM   1165  CB  LEU A 161      11.241  10.212  64.519  1.00 18.68           C  
ANISOU 1165  CB  LEU A 161     2198   2158   2740   -104   -122     72       C  
ATOM   1166  CG  LEU A 161      10.449  10.510  65.796  1.00 21.88           C  
ANISOU 1166  CG  LEU A 161     2690   2550   3074   -137   -138    -23       C  
ATOM   1167  CD1 LEU A 161       8.971  10.435  65.462  1.00 33.72           C  
ANISOU 1167  CD1 LEU A 161     4237   4024   4553    -85    -60    -45       C  
ATOM   1168  CD2 LEU A 161      10.791   9.495  66.884  1.00 25.58           C  
ANISOU 1168  CD2 LEU A 161     3187   3090   3442   -153   -204    -27       C  
ATOM   1169  N   ASP A 162      13.025  12.627  64.078  1.00 18.03           N  
ANISOU 1169  N   ASP A 162     2007   1973   2869   -230   -163     88       N  
ATOM   1170  CA  ASP A 162      13.723  13.830  64.533  1.00 19.20           C  
ANISOU 1170  CA  ASP A 162     2134   2063   3100   -319   -210     51       C  
ATOM   1171  C   ASP A 162      13.800  14.952  63.492  1.00 25.01           C  
ANISOU 1171  C   ASP A 162     2834   2713   3955   -336   -157     99       C  
ATOM   1172  O   ASP A 162      13.778  16.141  63.835  1.00 19.83           O  
ANISOU 1172  O   ASP A 162     2198   1965   3373   -396   -170     48       O  
ATOM   1173  CB  ASP A 162      15.179  13.508  64.928  1.00 20.23           C  
ANISOU 1173  CB  ASP A 162     2176   2249   3261   -371   -295     83       C  
ATOM   1174  CG  ASP A 162      15.291  12.617  66.146  1.00 25.17           C  
ANISOU 1174  CG  ASP A 162     2837   2948   3780   -379   -382     46       C  
ATOM   1175  OD1 ASP A 162      14.272  12.473  66.853  1.00 22.92           O  
ANISOU 1175  OD1 ASP A 162     2655   2661   3390   -368   -372    -25       O  
ATOM   1176  OD2 ASP A 162      16.419  12.112  66.395  1.00 19.89           O  
ANISOU 1176  OD2 ASP A 162     2083   2335   3139   -401   -459     95       O  
ATOM   1177  N   CYS A 163      13.970  14.569  62.229  1.00 19.00           N  
ANISOU 1177  N   CYS A 163     2024   1983   3213   -291    -96    200       N  
ATOM   1178  CA  CYS A 163      14.410  15.535  61.214  1.00 19.94           C  
ANISOU 1178  CA  CYS A 163     2093   2044   3440   -326    -54    276       C  
ATOM   1179  C   CYS A 163      13.337  16.029  60.230  1.00 19.47           C  
ANISOU 1179  C   CYS A 163     2081   1928   3389   -284     10    327       C  
ATOM   1180  O   CYS A 163      13.525  17.073  59.607  1.00 22.88           O  
ANISOU 1180  O   CYS A 163     2493   2283   3916   -324     32    385       O  
ATOM   1181  CB  CYS A 163      15.570  14.944  60.415  1.00 24.67           C  
ANISOU 1181  CB  CYS A 163     2593   2717   4062   -328    -24    365       C  
ATOM   1182  SG  CYS A 163      16.996  14.513  61.445  1.00 26.14           S  
ANISOU 1182  SG  CYS A 163     2685   2959   4290   -382   -116    337       S  
ATOM   1183  N   ASP A 164      12.248  15.283  60.057  1.00 17.59           N  
ANISOU 1183  N   ASP A 164     1897   1726   3059   -209     34    317       N  
ATOM   1184  CA  ASP A 164      11.197  15.703  59.123  1.00 20.42           C  
ANISOU 1184  CA  ASP A 164     2291   2040   3427   -170     74    375       C  
ATOM   1185  C   ASP A 164      10.412  16.892  59.680  1.00 22.63           C  
ANISOU 1185  C   ASP A 164     2607   2193   3799   -181     60    322       C  
ATOM   1186  O   ASP A 164       9.524  16.714  60.520  1.00 26.09           O  
ANISOU 1186  O   ASP A 164     3091   2616   4207   -149     54    230       O  
ATOM   1187  CB  ASP A 164      10.246  14.538  58.829  1.00 15.64           C  
ANISOU 1187  CB  ASP A 164     1724   1511   2708    -96     92    372       C  
ATOM   1188  CG  ASP A 164       9.145  14.901  57.814  1.00 23.69           C  
ANISOU 1188  CG  ASP A 164     2770   2498   3732    -60    113    444       C  
ATOM   1189  OD1 ASP A 164       9.139  16.034  57.261  1.00 22.83           O  
ANISOU 1189  OD1 ASP A 164     2651   2309   3714    -86    115    513       O  
ATOM   1190  OD2 ASP A 164       8.281  14.039  57.578  1.00 23.49           O  
ANISOU 1190  OD2 ASP A 164     2774   2527   3625    -10    118    438       O  
ATOM   1191  N   ARG A 165      10.712  18.097  59.200  1.00 21.11           N  
ANISOU 1191  N   ARG A 165     2393   1902   3726   -225     65    381       N  
ATOM   1192  CA  ARG A 165      10.104  19.287  59.774  1.00 18.99           C  
ANISOU 1192  CA  ARG A 165     2153   1488   3576   -237     57    320       C  
ATOM   1193  C   ARG A 165       8.614  19.471  59.416  1.00 19.35           C  
ANISOU 1193  C   ARG A 165     2228   1479   3645   -159     78    340       C  
ATOM   1194  O   ARG A 165       7.945  20.297  60.015  1.00 21.71           O  
ANISOU 1194  O   ARG A 165     2547   1657   4044   -149     85    268       O  
ATOM   1195  CB  ARG A 165      10.887  20.530  59.362  1.00 20.26           C  
ANISOU 1195  CB  ARG A 165     2279   1540   3879   -311     55    385       C  
ATOM   1196  CG  ARG A 165      12.223  20.660  60.086  1.00 30.01           C  
ANISOU 1196  CG  ARG A 165     3476   2787   5138   -402     20    326       C  
ATOM   1197  CD  ARG A 165      12.909  21.978  59.741  1.00 42.23           C  
ANISOU 1197  CD  ARG A 165     4989   4207   6849   -486     19    382       C  
ATOM   1198  NE  ARG A 165      14.355  21.865  59.899  1.00 57.53           N  
ANISOU 1198  NE  ARG A 165     6856   6200   8803   -573     -8    391       N  
ATOM   1199  CZ  ARG A 165      15.232  22.749  59.436  1.00 70.29           C  
ANISOU 1199  CZ  ARG A 165     8416   7744  10547   -660     -2    467       C  
ATOM   1200  NH1 ARG A 165      14.811  23.822  58.780  1.00 78.39           N  
ANISOU 1200  NH1 ARG A 165     9459   8632  11691   -670     27    547       N  
ATOM   1201  NH2 ARG A 165      16.531  22.558  59.630  1.00 69.89           N  
ANISOU 1201  NH2 ARG A 165     8282   7754  10517   -737    -28    471       N  
ATOM   1202  N   ARG A 166       8.109  18.722  58.439  1.00 20.42           N  
ANISOU 1202  N   ARG A 166     2362   1699   3697   -107     88    434       N  
ATOM   1203  CA  ARG A 166       6.691  18.816  58.087  1.00 24.28           C  
ANISOU 1203  CA  ARG A 166     2863   2149   4212    -37     89    462       C  
ATOM   1204  C   ARG A 166       5.847  17.912  58.966  1.00 24.13           C  
ANISOU 1204  C   ARG A 166     2868   2187   4114     12     99    348       C  
ATOM   1205  O   ARG A 166       4.626  18.048  59.026  1.00 25.80           O  
ANISOU 1205  O   ARG A 166     3078   2353   4372     67    107    335       O  
ATOM   1206  CB  ARG A 166       6.465  18.473  56.614  1.00 27.70           C  
ANISOU 1206  CB  ARG A 166     3290   2650   4584    -18     81    616       C  
ATOM   1207  CG  ARG A 166       7.092  19.495  55.690  1.00 32.82           C  
ANISOU 1207  CG  ARG A 166     3922   3233   5317    -68     79    751       C  
ATOM   1208  CD  ARG A 166       7.051  19.119  54.212  1.00 35.40           C  
ANISOU 1208  CD  ARG A 166     4258   3650   5543    -70     75    905       C  
ATOM   1209  NE  ARG A 166       7.497  20.259  53.414  1.00 30.58           N  
ANISOU 1209  NE  ARG A 166     3637   2956   5025   -121     74   1046       N  
ATOM   1210  CZ  ARG A 166       8.722  20.421  52.925  1.00 33.05           C  
ANISOU 1210  CZ  ARG A 166     3937   3302   5319   -193    112   1109       C  
ATOM   1211  NH1 ARG A 166       9.654  19.493  53.117  1.00 31.76           N  
ANISOU 1211  NH1 ARG A 166     3759   3255   5053   -215    153   1043       N  
ATOM   1212  NH2 ARG A 166       9.011  21.527  52.229  1.00 30.25           N  
ANISOU 1212  NH2 ARG A 166     3575   2857   5059   -243    111   1249       N  
ATOM   1213  N   SER A 167       6.499  16.974  59.642  1.00 18.79           N  
ANISOU 1213  N   SER A 167     2207   1608   3326    -10     98    275       N  
ATOM   1214  CA  SER A 167       5.778  16.049  60.501  1.00 22.73           C  
ANISOU 1214  CA  SER A 167     2735   2165   3737     25    110    180       C  
ATOM   1215  C   SER A 167       5.879  16.517  61.948  1.00 16.42           C  
ANISOU 1215  C   SER A 167     1967   1311   2961     -9    118     40       C  
ATOM   1216  O   SER A 167       6.510  17.534  62.233  1.00 19.41           O  
ANISOU 1216  O   SER A 167     2344   1604   3428    -60    109     12       O  
ATOM   1217  CB  SER A 167       6.314  14.623  60.327  1.00 20.32           C  
ANISOU 1217  CB  SER A 167     2433   1997   3292     27    101    199       C  
ATOM   1218  OG  SER A 167       5.991  14.123  59.038  1.00 17.94           O  
ANISOU 1218  OG  SER A 167     2119   1746   2950     58    104    301       O  
ATOM   1219  N   TYR A 168       5.271  15.770  62.859  1.00 16.33           N  
ANISOU 1219  N   TYR A 168     1990   1351   2863      9    138    -49       N  
ATOM   1220  CA  TYR A 168       5.149  16.206  64.251  1.00 24.34           C  
ANISOU 1220  CA  TYR A 168     3052   2322   3874    -26    159   -192       C  
ATOM   1221  C   TYR A 168       5.719  15.205  65.245  1.00 25.19           C  
ANISOU 1221  C   TYR A 168     3203   2540   3829    -66    132   -249       C  
ATOM   1222  O   TYR A 168       5.191  15.059  66.344  1.00 23.27           O  
ANISOU 1222  O   TYR A 168     3013   2307   3521    -79    163   -355       O  
ATOM   1223  CB  TYR A 168       3.677  16.452  64.589  1.00 26.49           C  
ANISOU 1223  CB  TYR A 168     3331   2536   4198     29    229   -256       C  
ATOM   1224  CG  TYR A 168       3.026  17.469  63.708  1.00 26.42           C  
ANISOU 1224  CG  TYR A 168     3272   2406   4361     76    245   -194       C  
ATOM   1225  CD1 TYR A 168       3.087  18.821  64.026  1.00 34.39           C  
ANISOU 1225  CD1 TYR A 168     4284   3268   5515     58    268   -255       C  
ATOM   1226  CD2 TYR A 168       2.349  17.091  62.552  1.00 31.55           C  
ANISOU 1226  CD2 TYR A 168     3872   3082   5032    135    230    -70       C  
ATOM   1227  CE1 TYR A 168       2.490  19.770  63.221  1.00 39.09           C  
ANISOU 1227  CE1 TYR A 168     4829   3737   6288    106    276   -181       C  
ATOM   1228  CE2 TYR A 168       1.745  18.037  61.738  1.00 34.51           C  
ANISOU 1228  CE2 TYR A 168     4199   3348   5567    176    227      9       C  
ATOM   1229  CZ  TYR A 168       1.818  19.374  62.083  1.00 40.53           C  
ANISOU 1229  CZ  TYR A 168     4959   3955   6486    166    250    -40       C  
ATOM   1230  OH  TYR A 168       1.232  20.332  61.286  1.00 39.52           O  
ANISOU 1230  OH  TYR A 168     4779   3703   6535    212    240     53       O  
ATOM   1231  N   GLY A 169       6.790  14.515  64.860  1.00 21.19           N  
ANISOU 1231  N   GLY A 169     2670   2113   3267    -86     77   -174       N  
ATOM   1232  CA  GLY A 169       7.431  13.568  65.749  1.00 29.47           C  
ANISOU 1232  CA  GLY A 169     3748   3258   4192   -121     32   -203       C  
ATOM   1233  C   GLY A 169       6.500  12.448  66.197  1.00 27.83           C  
ANISOU 1233  C   GLY A 169     3580   3117   3877    -82     63   -221       C  
ATOM   1234  O   GLY A 169       5.889  11.761  65.372  1.00 20.20           O  
ANISOU 1234  O   GLY A 169     2590   2177   2909    -23     90   -156       O  
ATOM   1235  N   CYS A 170       6.415  12.254  67.512  1.00 23.79           N  
ANISOU 1235  N   CYS A 170     3133   2636   3268   -125     58   -308       N  
ATOM   1236  CA  CYS A 170       5.571  11.212  68.081  1.00 20.44           C  
ANISOU 1236  CA  CYS A 170     2753   2276   2737   -104     93   -323       C  
ATOM   1237  C   CYS A 170       4.106  11.568  68.049  1.00 19.59           C  
ANISOU 1237  C   CYS A 170     2652   2116   2675    -62    191   -376       C  
ATOM   1238  O   CYS A 170       3.275  10.753  68.403  1.00 21.58           O  
ANISOU 1238  O   CYS A 170     2927   2413   2860    -44    235   -383       O  
ATOM   1239  CB  CYS A 170       5.990  10.926  69.516  1.00 21.51           C  
ANISOU 1239  CB  CYS A 170     2965   2470   2738   -176     55   -388       C  
ATOM   1240  SG  CYS A 170       7.585  10.064  69.575  1.00 27.07           S  
ANISOU 1240  SG  CYS A 170     3639   3255   3391   -207    -76   -292       S  
ATOM   1241  N   ASN A 171       3.791  12.786  67.628  1.00 23.46           N  
ANISOU 1241  N   ASN A 171     3113   2505   3296    -46    225   -406       N  
ATOM   1242  CA  ASN A 171       2.393  13.208  67.492  1.00 29.38           C  
ANISOU 1242  CA  ASN A 171     3842   3189   4130      6    314   -444       C  
ATOM   1243  C   ASN A 171       1.870  13.022  66.085  1.00 27.00           C  
ANISOU 1243  C   ASN A 171     3465   2874   3918     74    305   -329       C  
ATOM   1244  O   ASN A 171       0.844  13.578  65.731  1.00 32.60           O  
ANISOU 1244  O   ASN A 171     4133   3515   4740    122    353   -332       O  
ATOM   1245  CB  ASN A 171       2.220  14.677  67.900  1.00 27.64           C  
ANISOU 1245  CB  ASN A 171     3631   2846   4023     -8    361   -547       C  
ATOM   1246  CG  ASN A 171       2.370  14.877  69.386  1.00 36.19           C  
ANISOU 1246  CG  ASN A 171     4805   3943   5003    -79    395   -694       C  
ATOM   1247  OD1 ASN A 171       2.002  14.010  70.173  1.00 37.31           O  
ANISOU 1247  OD1 ASN A 171     4997   4173   5007    -96    425   -727       O  
ATOM   1248  ND2 ASN A 171       2.922  16.013  69.781  1.00 37.82           N  
ANISOU 1248  ND2 ASN A 171     5040   4063   5266   -129    388   -781       N  
ATOM   1249  N   GLY A 172       2.599  12.270  65.272  1.00 21.68           N  
ANISOU 1249  N   GLY A 172     2773   2265   3198     77    242   -228       N  
ATOM   1250  CA  GLY A 172       2.134  11.959  63.940  1.00 22.66           C  
ANISOU 1250  CA  GLY A 172     2845   2398   3368    126    229   -125       C  
ATOM   1251  C   GLY A 172       2.844  12.688  62.818  1.00 20.72           C  
ANISOU 1251  C   GLY A 172     2563   2112   3197    126    188    -39       C  
ATOM   1252  O   GLY A 172       3.602  13.622  63.048  1.00 19.33           O  
ANISOU 1252  O   GLY A 172     2391   1878   3076     90    176    -60       O  
ATOM   1253  N   GLY A 173       2.584  12.272  61.583  1.00 19.56           N  
ANISOU 1253  N   GLY A 173     2386   1996   3049    155    168     59       N  
ATOM   1254  CA  GLY A 173       3.281  12.871  60.462  1.00 19.15           C  
ANISOU 1254  CA  GLY A 173     2310   1924   3042    146    138    153       C  
ATOM   1255  C   GLY A 173       2.847  12.317  59.137  1.00 22.78           C  
ANISOU 1255  C   GLY A 173     2755   2435   3467    170    117    251       C  
ATOM   1256  O   GLY A 173       1.749  11.753  59.020  1.00 18.16           O  
ANISOU 1256  O   GLY A 173     2162   1872   2866    201    118    249       O  
ATOM   1257  N   TYR A 174       3.724  12.469  58.149  1.00 17.33           N  
ANISOU 1257  N   TYR A 174     2060   1766   2759    148    102    334       N  
ATOM   1258  CA  TYR A 174       3.383  12.241  56.754  1.00 17.97           C  
ANISOU 1258  CA  TYR A 174     2139   1889   2801    156     81    434       C  
ATOM   1259  C   TYR A 174       4.378  11.331  56.065  1.00 18.63           C  
ANISOU 1259  C   TYR A 174     2242   2064   2773    134     96    460       C  
ATOM   1260  O   TYR A 174       5.562  11.695  55.934  1.00 19.40           O  
ANISOU 1260  O   TYR A 174     2329   2160   2882    102    115    483       O  
ATOM   1261  CB  TYR A 174       3.321  13.568  55.998  1.00 16.77           C  
ANISOU 1261  CB  TYR A 174     1965   1661   2745    147     59    533       C  
ATOM   1262  CG  TYR A 174       2.370  14.611  56.570  1.00 15.76           C  
ANISOU 1262  CG  TYR A 174     1807   1416   2765    179     51    513       C  
ATOM   1263  CD1 TYR A 174       0.995  14.460  56.468  1.00 20.15           C  
ANISOU 1263  CD1 TYR A 174     2336   1962   3358    224     30    521       C  
ATOM   1264  CD2 TYR A 174       2.864  15.762  57.182  1.00 25.64           C  
ANISOU 1264  CD2 TYR A 174     3049   2559   4133    161     68    483       C  
ATOM   1265  CE1 TYR A 174       0.126  15.424  56.975  1.00 23.38           C  
ANISOU 1265  CE1 TYR A 174     2702   2254   3927    262     38    500       C  
ATOM   1266  CE2 TYR A 174       2.007  16.734  57.681  1.00 27.54           C  
ANISOU 1266  CE2 TYR A 174     3262   2676   4525    195     76    453       C  
ATOM   1267  CZ  TYR A 174       0.639  16.555  57.582  1.00 28.56           C  
ANISOU 1267  CZ  TYR A 174     3358   2796   4698    251     66    461       C  
ATOM   1268  OH  TYR A 174      -0.194  17.525  58.082  1.00 30.03           O  
ANISOU 1268  OH  TYR A 174     3503   2850   5057    294     88    426       O  
ATOM   1269  N   PRO A 175       3.918  10.141  55.624  1.00 21.45           N  
ANISOU 1269  N   PRO A 175     2622   2495   3033    147     95    451       N  
ATOM   1270  CA  PRO A 175       4.799   9.258  54.855  1.00 21.90           C  
ANISOU 1270  CA  PRO A 175     2701   2629   2993    132    125    465       C  
ATOM   1271  C   PRO A 175       5.390   9.966  53.638  1.00 24.12           C  
ANISOU 1271  C   PRO A 175     2983   2924   3257     99    137    562       C  
ATOM   1272  O   PRO A 175       6.569   9.756  53.369  1.00 18.62           O  
ANISOU 1272  O   PRO A 175     2280   2261   2535     79    186    567       O  
ATOM   1273  CB  PRO A 175       3.866   8.110  54.436  1.00 21.67           C  
ANISOU 1273  CB  PRO A 175     2702   2652   2880    145    111    443       C  
ATOM   1274  CG  PRO A 175       2.863   8.048  55.514  1.00 15.86           C  
ANISOU 1274  CG  PRO A 175     1951   1875   2198    170     90    388       C  
ATOM   1275  CD  PRO A 175       2.645   9.476  55.965  1.00 16.72           C  
ANISOU 1275  CD  PRO A 175     2027   1905   2421    174     77    409       C  
ATOM   1276  N   TRP A 176       4.618  10.805  52.943  1.00 16.34           N  
ANISOU 1276  N   TRP A 176     2000   1911   2295     92     95    646       N  
ATOM   1277  CA  TRP A 176       5.139  11.430  51.721  1.00 18.83           C  
ANISOU 1277  CA  TRP A 176     2331   2249   2574     50    105    758       C  
ATOM   1278  C   TRP A 176       6.273  12.420  52.011  1.00 19.06           C  
ANISOU 1278  C   TRP A 176     2325   2221   2695     22    140    787       C  
ATOM   1279  O   TRP A 176       7.222  12.550  51.224  1.00 18.91           O  
ANISOU 1279  O   TRP A 176     2311   2243   2632    -20    189    847       O  
ATOM   1280  CB  TRP A 176       4.018  12.114  50.926  1.00 32.49           C  
ANISOU 1280  CB  TRP A 176     4070   3959   4314     48     31    863       C  
ATOM   1281  CG  TRP A 176       3.145  13.045  51.708  1.00 33.69           C  
ANISOU 1281  CG  TRP A 176     4176   4000   4625     85    -17    867       C  
ATOM   1282  CD1 TRP A 176       1.925  12.759  52.261  1.00 33.50           C  
ANISOU 1282  CD1 TRP A 176     4128   3954   4648    128    -57    817       C  
ATOM   1283  CD2 TRP A 176       3.415  14.414  52.017  1.00 28.92           C  
ANISOU 1283  CD2 TRP A 176     3539   3283   4166     81    -20    916       C  
ATOM   1284  NE1 TRP A 176       1.424  13.867  52.898  1.00 33.66           N  
ANISOU 1284  NE1 TRP A 176     4101   3856   4834    159    -73    825       N  
ATOM   1285  CE2 TRP A 176       2.319  14.897  52.764  1.00 29.37           C  
ANISOU 1285  CE2 TRP A 176     3556   3249   4355    131    -54    882       C  
ATOM   1286  CE3 TRP A 176       4.476  15.283  51.734  1.00 30.20           C  
ANISOU 1286  CE3 TRP A 176     3698   3405   4370     37     11    982       C  
ATOM   1287  CZ2 TRP A 176       2.260  16.207  53.239  1.00 32.55           C  
ANISOU 1287  CZ2 TRP A 176     3924   3513   4930    142    -57    901       C  
ATOM   1288  CZ3 TRP A 176       4.418  16.576  52.213  1.00 33.18           C  
ANISOU 1288  CZ3 TRP A 176     4042   3645   4918     41     -3   1008       C  
ATOM   1289  CH2 TRP A 176       3.316  17.028  52.953  1.00 31.64           C  
ANISOU 1289  CH2 TRP A 176     3816   3353   4853     96    -36    963       C  
ATOM   1290  N   SER A 177       6.178  13.105  53.148  1.00 21.43           N  
ANISOU 1290  N   SER A 177     2592   2429   3123     37    121    739       N  
ATOM   1291  CA  SER A 177       7.227  14.017  53.586  1.00 19.35           C  
ANISOU 1291  CA  SER A 177     2293   2101   2957      1    143    746       C  
ATOM   1292  C   SER A 177       8.492  13.260  53.945  1.00 17.66           C  
ANISOU 1292  C   SER A 177     2057   1949   2705    -16    191    688       C  
ATOM   1293  O   SER A 177       9.598  13.667  53.564  1.00 18.61           O  
ANISOU 1293  O   SER A 177     2146   2074   2853    -61    229    737       O  
ATOM   1294  CB  SER A 177       6.772  14.827  54.802  1.00 20.75           C  
ANISOU 1294  CB  SER A 177     2452   2167   3266     16    113    679       C  
ATOM   1295  OG  SER A 177       7.675  15.888  55.014  1.00 39.83           O  
ANISOU 1295  OG  SER A 177     4841   4507   5786    -32    122    701       O  
ATOM   1296  N   ALA A 178       8.328  12.184  54.721  1.00 20.83           N  
ANISOU 1296  N   ALA A 178     2465   2390   3060     19    187    591       N  
ATOM   1297  CA  ALA A 178       9.468  11.338  55.100  1.00 18.55           C  
ANISOU 1297  CA  ALA A 178     2146   2154   2749     16    219    544       C  
ATOM   1298  C   ALA A 178      10.168  10.792  53.860  1.00 25.40           C  
ANISOU 1298  C   ALA A 178     3009   3098   3543      4    288    596       C  
ATOM   1299  O   ALA A 178      11.394  10.815  53.775  1.00 23.71           O  
ANISOU 1299  O   ALA A 178     2742   2902   3366    -20    333    610       O  
ATOM   1300  CB  ALA A 178       9.022  10.186  56.010  1.00 15.48           C  
ANISOU 1300  CB  ALA A 178     1777   1792   2314     58    199    454       C  
ATOM   1301  N   LEU A 179       9.388  10.287  52.905  1.00 23.84           N  
ANISOU 1301  N   LEU A 179     2867   2948   3243     17    299    620       N  
ATOM   1302  CA  LEU A 179       9.968   9.767  51.667  1.00 23.07           C  
ANISOU 1302  CA  LEU A 179     2786   2928   3052     -1    376    656       C  
ATOM   1303  C   LEU A 179      10.697  10.849  50.866  1.00 22.85           C  
ANISOU 1303  C   LEU A 179     2738   2896   3048    -59    418    760       C  
ATOM   1304  O   LEU A 179      11.756  10.601  50.279  1.00 23.84           O  
ANISOU 1304  O   LEU A 179     2835   3072   3151    -83    509    775       O  
ATOM   1305  CB  LEU A 179       8.883   9.131  50.810  1.00 20.41           C  
ANISOU 1305  CB  LEU A 179     2526   2642   2588      7    360    658       C  
ATOM   1306  CG  LEU A 179       8.354   7.786  51.323  1.00 20.38           C  
ANISOU 1306  CG  LEU A 179     2545   2656   2544     53    348    556       C  
ATOM   1307  CD1 LEU A 179       7.117   7.391  50.546  1.00 20.20           C  
ANISOU 1307  CD1 LEU A 179     2590   2669   2416     46    306    565       C  
ATOM   1308  CD2 LEU A 179       9.438   6.691  51.228  1.00 20.92           C  
ANISOU 1308  CD2 LEU A 179     2594   2764   2590     70    436    495       C  
ATOM   1309  N   GLN A 180      10.122  12.046  50.838  1.00 21.53           N  
ANISOU 1309  N   GLN A 180     2580   2663   2939    -81    360    835       N  
ATOM   1310  CA  GLN A 180      10.736  13.169  50.133  1.00 24.07           C  
ANISOU 1310  CA  GLN A 180     2885   2962   3300   -143    391    950       C  
ATOM   1311  C   GLN A 180      12.081  13.529  50.756  1.00 20.50           C  
ANISOU 1311  C   GLN A 180     2348   2479   2964   -173    434    931       C  
ATOM   1312  O   GLN A 180      13.039  13.844  50.050  1.00 22.51           O  
ANISOU 1312  O   GLN A 180     2571   2761   3219   -225    511   1000       O  
ATOM   1313  CB  GLN A 180       9.802  14.391  50.132  1.00 25.15           C  
ANISOU 1313  CB  GLN A 180     3041   3004   3513   -151    309   1033       C  
ATOM   1314  CG  GLN A 180      10.450  15.648  49.575  1.00 33.93           C  
ANISOU 1314  CG  GLN A 180     4132   4062   4697   -218    333   1160       C  
ATOM   1315  CD  GLN A 180      10.997  15.438  48.174  1.00 51.76           C  
ANISOU 1315  CD  GLN A 180     6424   6422   6818   -271    414   1258       C  
ATOM   1316  OE1 GLN A 180      10.391  14.745  47.355  1.00 53.16           O  
ANISOU 1316  OE1 GLN A 180     6670   6688   6839   -262    413   1271       O  
ATOM   1317  NE2 GLN A 180      12.154  16.034  47.895  1.00 62.14           N  
ANISOU 1317  NE2 GLN A 180     7693   7728   8187   -334    488   1321       N  
ATOM   1318  N   LEU A 181      12.161  13.461  52.077  1.00 20.48           N  
ANISOU 1318  N   LEU A 181     2306   2424   3052   -147    384    840       N  
ATOM   1319  CA  LEU A 181      13.407  13.800  52.769  1.00 24.80           C  
ANISOU 1319  CA  LEU A 181     2766   2943   3713   -183    397    818       C  
ATOM   1320  C   LEU A 181      14.560  12.869  52.357  1.00 22.18           C  
ANISOU 1320  C   LEU A 181     2376   2701   3350   -182    487    807       C  
ATOM   1321  O   LEU A 181      15.716  13.298  52.157  1.00 25.54           O  
ANISOU 1321  O   LEU A 181     2721   3128   3854   -233    540    851       O  
ATOM   1322  CB  LEU A 181      13.178  13.729  54.278  1.00 27.25           C  
ANISOU 1322  CB  LEU A 181     3065   3201   4087   -159    315    714       C  
ATOM   1323  CG  LEU A 181      14.136  14.442  55.229  1.00 36.28           C  
ANISOU 1323  CG  LEU A 181     4138   4287   5360   -212    279    686       C  
ATOM   1324  CD1 LEU A 181      13.989  15.962  55.107  1.00 37.13           C  
ANISOU 1324  CD1 LEU A 181     4252   4286   5571   -269    259    743       C  
ATOM   1325  CD2 LEU A 181      13.886  13.978  56.665  1.00 31.76           C  
ANISOU 1325  CD2 LEU A 181     3576   3704   4788   -185    204    573       C  
ATOM   1326  N   VAL A 182      14.237  11.589  52.222  1.00 18.80           N  
ANISOU 1326  N   VAL A 182     1982   2339   2824   -124    510    746       N  
ATOM   1327  CA  VAL A 182      15.223  10.580  51.858  1.00 22.85           C  
ANISOU 1327  CA  VAL A 182     2440   2923   3321   -105    604    719       C  
ATOM   1328  C   VAL A 182      15.638  10.726  50.390  1.00 23.77           C  
ANISOU 1328  C   VAL A 182     2570   3099   3361   -146    725    792       C  
ATOM   1329  O   VAL A 182      16.763  10.411  50.030  1.00 21.76           O  
ANISOU 1329  O   VAL A 182     2239   2887   3143   -156    828    795       O  
ATOM   1330  CB  VAL A 182      14.665   9.183  52.142  1.00 22.44           C  
ANISOU 1330  CB  VAL A 182     2431   2901   3195    -32    593    629       C  
ATOM   1331  CG1 VAL A 182      15.647   8.082  51.703  1.00 21.04           C  
ANISOU 1331  CG1 VAL A 182     2197   2779   3017     -1    701    594       C  
ATOM   1332  CG2 VAL A 182      14.354   9.070  53.631  1.00 18.61           C  
ANISOU 1332  CG2 VAL A 182     1932   2365   2774     -4    482    570       C  
ATOM   1333  N   ALA A 183      14.723  11.203  49.550  1.00 24.76           N  
ANISOU 1333  N   ALA A 183     2792   3234   3383   -171    713    856       N  
ATOM   1334  CA  ALA A 183      15.029  11.484  48.151  1.00 27.96           C  
ANISOU 1334  CA  ALA A 183     3231   3702   3689   -228    817    944       C  
ATOM   1335  C   ALA A 183      15.920  12.697  48.002  1.00 26.39           C  
ANISOU 1335  C   ALA A 183     2962   3467   3598   -302    853   1046       C  
ATOM   1336  O   ALA A 183      16.807  12.733  47.145  1.00 28.57           O  
ANISOU 1336  O   ALA A 183     3208   3802   3846   -350    982   1096       O  
ATOM   1337  CB  ALA A 183      13.759  11.697  47.361  1.00 23.87           C  
ANISOU 1337  CB  ALA A 183     2834   3203   3032   -241    764   1001       C  
ATOM   1338  N   GLN A 184      15.673  13.712  48.819  1.00 23.09           N  
ANISOU 1338  N   GLN A 184     2521   2948   3307   -319    749   1075       N  
ATOM   1339  CA  GLN A 184      16.390  14.974  48.652  1.00 24.89           C  
ANISOU 1339  CA  GLN A 184     2693   3119   3646   -401    771   1180       C  
ATOM   1340  C   GLN A 184      17.720  14.979  49.380  1.00 29.92           C  
ANISOU 1340  C   GLN A 184     3193   3740   4434   -423    803   1138       C  
ATOM   1341  O   GLN A 184      18.681  15.609  48.940  1.00 30.99           O  
ANISOU 1341  O   GLN A 184     3257   3875   4641   -496    880   1217       O  
ATOM   1342  CB  GLN A 184      15.539  16.138  49.153  1.00 28.21           C  
ANISOU 1342  CB  GLN A 184     3150   3417   4152   -414    650   1225       C  
ATOM   1343  CG  GLN A 184      16.124  17.480  48.827  1.00 36.79           C  
ANISOU 1343  CG  GLN A 184     4200   4428   5351   -505    670   1348       C  
ATOM   1344  CD  GLN A 184      16.242  17.708  47.326  1.00 38.63           C  
ANISOU 1344  CD  GLN A 184     4483   4730   5464   -562    764   1492       C  
ATOM   1345  OE1 GLN A 184      15.493  17.130  46.532  1.00 42.83           O  
ANISOU 1345  OE1 GLN A 184     5109   5343   5823   -535    772   1512       O  
ATOM   1346  NE2 GLN A 184      17.191  18.542  46.934  1.00 42.53           N  
ANISOU 1346  NE2 GLN A 184     4925   5199   6033   -645    825   1576       N  
ATOM   1347  N   TYR A 185      17.759  14.296  50.517  1.00 23.08           N  
ANISOU 1347  N   TYR A 185     2286   2863   3620   -364    735   1023       N  
ATOM   1348  CA  TYR A 185      18.932  14.325  51.374  1.00 30.18           C  
ANISOU 1348  CA  TYR A 185     3052   3743   4671   -386    724    986       C  
ATOM   1349  C   TYR A 185      19.529  12.927  51.490  1.00 33.94           C  
ANISOU 1349  C   TYR A 185     3466   4300   5130   -319    780    911       C  
ATOM   1350  O   TYR A 185      20.639  12.672  51.021  1.00 35.54           O  
ANISOU 1350  O   TYR A 185     3566   4551   5388   -337    890    934       O  
ATOM   1351  CB  TYR A 185      18.567  14.891  52.755  1.00 24.08           C  
ANISOU 1351  CB  TYR A 185     2281   2877   3992   -390    576    927       C  
ATOM   1352  CG  TYR A 185      18.042  16.315  52.679  1.00 28.67           C  
ANISOU 1352  CG  TYR A 185     2912   3353   4628   -451    529    992       C  
ATOM   1353  CD1 TYR A 185      18.918  17.389  52.562  1.00 36.45           C  
ANISOU 1353  CD1 TYR A 185     3823   4280   5746   -546    548   1063       C  
ATOM   1354  CD2 TYR A 185      16.676  16.586  52.703  1.00 31.53           C  
ANISOU 1354  CD2 TYR A 185     3387   3666   4928   -414    470    986       C  
ATOM   1355  CE1 TYR A 185      18.449  18.699  52.478  1.00 33.88           C  
ANISOU 1355  CE1 TYR A 185     3544   3838   5491   -600    508   1127       C  
ATOM   1356  CE2 TYR A 185      16.196  17.900  52.621  1.00 33.57           C  
ANISOU 1356  CE2 TYR A 185     3681   3810   5264   -459    430   1051       C  
ATOM   1357  CZ  TYR A 185      17.089  18.948  52.512  1.00 37.92           C  
ANISOU 1357  CZ  TYR A 185     4168   4294   5948   -551    449   1120       C  
ATOM   1358  OH  TYR A 185      16.621  20.250  52.431  1.00 33.15           O  
ANISOU 1358  OH  TYR A 185     3599   3555   5439   -594    411   1187       O  
ATOM   1359  N   GLY A 186      18.766  12.018  52.085  1.00 26.56           N  
ANISOU 1359  N   GLY A 186     2591   3372   4128   -241    714    825       N  
ATOM   1360  CA  GLY A 186      19.215  10.658  52.293  1.00 20.71           C  
ANISOU 1360  CA  GLY A 186     1800   2683   3386   -170    751    755       C  
ATOM   1361  C   GLY A 186      18.804  10.166  53.660  1.00 19.63           C  
ANISOU 1361  C   GLY A 186     1673   2512   3274   -122    617    680       C  
ATOM   1362  O   GLY A 186      17.965  10.785  54.334  1.00 24.08           O  
ANISOU 1362  O   GLY A 186     2305   3022   3821   -138    513    666       O  
ATOM   1363  N   ILE A 187      19.349   9.021  54.059  1.00 20.28           N  
ANISOU 1363  N   ILE A 187     1690   2622   3395    -61    625    634       N  
ATOM   1364  CA  ILE A 187      18.994   8.415  55.350  1.00 22.29           C  
ANISOU 1364  CA  ILE A 187     1959   2853   3657    -18    500    577       C  
ATOM   1365  C   ILE A 187      20.165   7.590  55.852  1.00 23.53           C  
ANISOU 1365  C   ILE A 187     1979   3027   3934     19    494    572       C  
ATOM   1366  O   ILE A 187      20.949   7.050  55.060  1.00 23.48           O  
ANISOU 1366  O   ILE A 187     1891   3052   3978     48    616    584       O  
ATOM   1367  CB  ILE A 187      17.713   7.519  55.269  1.00 18.51           C  
ANISOU 1367  CB  ILE A 187     1611   2380   3042     44    493    524       C  
ATOM   1368  CG1 ILE A 187      17.190   7.220  56.673  1.00 16.89           C  
ANISOU 1368  CG1 ILE A 187     1439   2145   2833     64    360    481       C  
ATOM   1369  CG2 ILE A 187      17.992   6.205  54.497  1.00 18.03           C  
ANISOU 1369  CG2 ILE A 187     1538   2357   2956    111    605    496       C  
ATOM   1370  CD1 ILE A 187      15.772   6.583  56.730  1.00 20.87           C  
ANISOU 1370  CD1 ILE A 187     2072   2645   3214    105    343    435       C  
ATOM   1371  N   HIS A 188      20.306   7.516  57.168  1.00 22.74           N  
ANISOU 1371  N   HIS A 188     1851   2907   3885     16    354    557       N  
ATOM   1372  CA  HIS A 188      21.373   6.709  57.761  1.00 27.64           C  
ANISOU 1372  CA  HIS A 188     2336   3539   4628     54    316    570       C  
ATOM   1373  C   HIS A 188      20.867   5.324  58.172  1.00 27.53           C  
ANISOU 1373  C   HIS A 188     2374   3522   4564    144    290    536       C  
ATOM   1374  O   HIS A 188      19.653   5.086  58.257  1.00 18.53           O  
ANISOU 1374  O   HIS A 188     1376   2371   3292    161    274    496       O  
ATOM   1375  CB  HIS A 188      21.975   7.425  58.964  1.00 22.60           C  
ANISOU 1375  CB  HIS A 188     1626   2889   4074    -16    161    588       C  
ATOM   1376  CG  HIS A 188      22.770   8.640  58.602  1.00 31.42           C  
ANISOU 1376  CG  HIS A 188     2650   3999   5291   -107    186    628       C  
ATOM   1377  ND1 HIS A 188      22.214   9.900  58.534  1.00 32.81           N  
ANISOU 1377  ND1 HIS A 188     2909   4136   5420   -186    170    623       N  
ATOM   1378  CD2 HIS A 188      24.077   8.785  58.281  1.00 29.39           C  
ANISOU 1378  CD2 HIS A 188     2217   3759   5191   -132    230    679       C  
ATOM   1379  CE1 HIS A 188      23.146  10.768  58.180  1.00 32.48           C  
ANISOU 1379  CE1 HIS A 188     2756   4087   5499   -262    201    671       C  
ATOM   1380  NE2 HIS A 188      24.286  10.117  58.026  1.00 27.43           N  
ANISOU 1380  NE2 HIS A 188     1955   3486   4982   -234    239    705       N  
ATOM   1381  N   TYR A 189      21.806   4.410  58.411  1.00 20.61           N  
ANISOU 1381  N   TYR A 189     1373   2647   3810    201    287    557       N  
ATOM   1382  CA  TYR A 189      21.477   3.074  58.909  1.00 20.35           C  
ANISOU 1382  CA  TYR A 189     1372   2594   3764    285    248    542       C  
ATOM   1383  C   TYR A 189      20.861   3.092  60.296  1.00 28.31           C  
ANISOU 1383  C   TYR A 189     2461   3595   4700    258     75    544       C  
ATOM   1384  O   TYR A 189      21.130   3.999  61.096  1.00 22.67           O  
ANISOU 1384  O   TYR A 189     1725   2892   3996    181    -40    562       O  
ATOM   1385  CB  TYR A 189      22.728   2.187  58.963  1.00 21.80           C  
ANISOU 1385  CB  TYR A 189     1383   2768   4133    353    266    581       C  
ATOM   1386  CG  TYR A 189      23.311   1.790  57.629  1.00 29.19           C  
ANISOU 1386  CG  TYR A 189     2242   3707   5144    404    468    561       C  
ATOM   1387  CD1 TYR A 189      22.528   1.182  56.658  1.00 27.23           C  
ANISOU 1387  CD1 TYR A 189     2113   3449   4783    446    604    494       C  
ATOM   1388  CD2 TYR A 189      24.663   2.005  57.349  1.00 24.26           C  
ANISOU 1388  CD2 TYR A 189     1421   3095   4700    403    524    603       C  
ATOM   1389  CE1 TYR A 189      23.071   0.809  55.446  1.00 24.02           C  
ANISOU 1389  CE1 TYR A 189     1651   3050   4424    484    799    461       C  
ATOM   1390  CE2 TYR A 189      25.209   1.634  56.141  1.00 31.91           C  
ANISOU 1390  CE2 TYR A 189     2350   4068   5706    440    719    567       C  
ATOM   1391  CZ  TYR A 189      24.406   1.035  55.194  1.00 28.78           C  
ANISOU 1391  CZ  TYR A 189     2076   3667   5191    483    864    496       C  
ATOM   1392  OH  TYR A 189      24.939   0.670  53.980  1.00 34.44           O  
ANISOU 1392  OH  TYR A 189     2791   4394   5901    502   1047    441       O  
ATOM   1393  N   ARG A 190      20.051   2.075  60.590  1.00 23.00           N  
ANISOU 1393  N   ARG A 190     1884   2901   3953    314     60    523       N  
ATOM   1394  CA  ARG A 190      19.439   1.944  61.916  1.00 21.60           C  
ANISOU 1394  CA  ARG A 190     1791   2723   3694    289    -87    530       C  
ATOM   1395  C   ARG A 190      20.479   1.956  63.026  1.00 23.82           C  
ANISOU 1395  C   ARG A 190     1962   3019   4071    265   -238    595       C  
ATOM   1396  O   ARG A 190      20.326   2.658  64.017  1.00 25.82           O  
ANISOU 1396  O   ARG A 190     2259   3295   4257    187   -362    594       O  
ATOM   1397  CB  ARG A 190      18.622   0.660  62.020  1.00 35.42           C  
ANISOU 1397  CB  ARG A 190     3631   4442   5385    357    -70    517       C  
ATOM   1398  CG  ARG A 190      18.549   0.136  63.456  1.00 53.39           C  
ANISOU 1398  CG  ARG A 190     5933   6717   7636    349   -224    565       C  
ATOM   1399  CD  ARG A 190      17.949  -1.252  63.563  1.00 55.93           C  
ANISOU 1399  CD  ARG A 190     6318   6994   7939    418   -207    574       C  
ATOM   1400  NE  ARG A 190      16.496  -1.207  63.686  1.00 63.40           N  
ANISOU 1400  NE  ARG A 190     7422   7941   8726    389   -186    522       N  
ATOM   1401  CZ  ARG A 190      15.728  -2.283  63.824  1.00 59.99           C  
ANISOU 1401  CZ  ARG A 190     7068   7470   8255    426   -171    522       C  
ATOM   1402  NH1 ARG A 190      16.279  -3.492  63.859  1.00 48.52           N  
ANISOU 1402  NH1 ARG A 190     5559   5964   6912    497   -176    572       N  
ATOM   1403  NH2 ARG A 190      14.414  -2.148  63.931  1.00 52.26           N  
ANISOU 1403  NH2 ARG A 190     6215   6498   7145    391   -150    475       N  
ATOM   1404  N   ASN A 191      21.538   1.176  62.851  1.00 23.64           N  
ANISOU 1404  N   ASN A 191     1793   2983   4208    329   -229    649       N  
ATOM   1405  CA  ASN A 191      22.579   1.059  63.852  1.00 30.98           C  
ANISOU 1405  CA  ASN A 191     2595   3927   5249    315   -386    729       C  
ATOM   1406  C   ASN A 191      23.302   2.380  64.099  1.00 31.96           C  
ANISOU 1406  C   ASN A 191     2637   4089   5415    212   -457    737       C  
ATOM   1407  O   ASN A 191      23.786   2.634  65.200  1.00 37.59           O  
ANISOU 1407  O   ASN A 191     3311   4831   6142    151   -632    781       O  
ATOM   1408  CB  ASN A 191      23.582  -0.017  63.436  1.00 35.74           C  
ANISOU 1408  CB  ASN A 191     3032   4493   6052    419   -338    786       C  
ATOM   1409  CG  ASN A 191      24.585  -0.318  64.519  1.00 55.39           C  
ANISOU 1409  CG  ASN A 191     5389   6993   8664    415   -523    888       C  
ATOM   1410  OD1 ASN A 191      24.295  -1.063  65.457  1.00 65.04           O  
ANISOU 1410  OD1 ASN A 191     6678   8203   9832    431   -645    936       O  
ATOM   1411  ND2 ASN A 191      25.778   0.259  64.401  1.00 61.74           N  
ANISOU 1411  ND2 ASN A 191     6057   7817   9582    373   -533    905       N  
ATOM   1412  N   THR A 192      23.368   3.214  63.064  1.00 27.78           N  
ANISOU 1412  N   THR A 192     2089   3561   4905    184   -324    696       N  
ATOM   1413  CA  THR A 192      23.964   4.546  63.173  1.00 26.77           C  
ANISOU 1413  CA  THR A 192     1894   3454   4823     78   -370    698       C  
ATOM   1414  C   THR A 192      23.088   5.518  63.992  1.00 27.14           C  
ANISOU 1414  C   THR A 192     2097   3504   4710    -20   -469    643       C  
ATOM   1415  O   THR A 192      23.596   6.379  64.713  1.00 23.50           O  
ANISOU 1415  O   THR A 192     1598   3057   4276   -117   -590    645       O  
ATOM   1416  CB  THR A 192      24.201   5.138  61.775  1.00 24.05           C  
ANISOU 1416  CB  THR A 192     1501   3103   4534     74   -186    682       C  
ATOM   1417  OG1 THR A 192      25.148   4.324  61.061  1.00 31.56           O  
ANISOU 1417  OG1 THR A 192     2292   4054   5647    155    -81    721       O  
ATOM   1418  CG2 THR A 192      24.724   6.564  61.870  1.00 27.64           C  
ANISOU 1418  CG2 THR A 192     1900   3563   5040    -45   -229    688       C  
ATOM   1419  N   TYR A 193      21.773   5.363  63.879  1.00 24.09           N  
ANISOU 1419  N   TYR A 193     1883   3103   4169      5   -412    588       N  
ATOM   1420  CA  TYR A 193      20.817   6.317  64.419  1.00 22.95           C  
ANISOU 1420  CA  TYR A 193     1884   2949   3888    -71   -454    521       C  
ATOM   1421  C   TYR A 193      19.632   5.470  64.931  1.00 23.61           C  
ANISOU 1421  C   TYR A 193     2112   3032   3825    -24   -464    494       C  
ATOM   1422  O   TYR A 193      18.571   5.384  64.286  1.00 24.16           O  
ANISOU 1422  O   TYR A 193     2282   3082   3816     13   -357    454       O  
ATOM   1423  CB  TYR A 193      20.391   7.284  63.313  1.00 24.73           C  
ANISOU 1423  CB  TYR A 193     2142   3143   4110    -92   -322    489       C  
ATOM   1424  CG  TYR A 193      19.807   8.636  63.688  1.00 24.21           C  
ANISOU 1424  CG  TYR A 193     2168   3045   3988   -182   -355    430       C  
ATOM   1425  CD1 TYR A 193      19.966   9.735  62.809  1.00 22.12           C  
ANISOU 1425  CD1 TYR A 193     1874   2744   3787   -227   -275    435       C  
ATOM   1426  CD2 TYR A 193      19.151   8.848  64.911  1.00 21.02           C  
ANISOU 1426  CD2 TYR A 193     1873   2639   3474   -227   -457    371       C  
ATOM   1427  CE1 TYR A 193      19.440  11.003  63.110  1.00 23.55           C  
ANISOU 1427  CE1 TYR A 193     2133   2871   3944   -304   -299    383       C  
ATOM   1428  CE2 TYR A 193      18.649  10.123  65.232  1.00 25.47           C  
ANISOU 1428  CE2 TYR A 193     2515   3157   4006   -305   -470    302       C  
ATOM   1429  CZ  TYR A 193      18.792  11.180  64.326  1.00 27.34           C  
ANISOU 1429  CZ  TYR A 193     2717   3341   4328   -338   -394    309       C  
ATOM   1430  OH  TYR A 193      18.246  12.400  64.665  1.00 23.68           O  
ANISOU 1430  OH  TYR A 193     2333   2812   3853   -407   -405    240       O  
ATOM   1431  N   PRO A 194      19.826   4.773  66.056  1.00 22.31           N  
ANISOU 1431  N   PRO A 194     1954   2893   3629    -25   -593    528       N  
ATOM   1432  CA  PRO A 194      18.835   3.789  66.510  1.00 19.45           C  
ANISOU 1432  CA  PRO A 194     1711   2530   3148     22   -595    524       C  
ATOM   1433  C   PRO A 194      17.563   4.424  67.033  1.00 21.46           C  
ANISOU 1433  C   PRO A 194     2128   2784   3242    -32   -587    443       C  
ATOM   1434  O   PRO A 194      17.524   5.609  67.324  1.00 25.29           O  
ANISOU 1434  O   PRO A 194     2640   3268   3701   -112   -612    389       O  
ATOM   1435  CB  PRO A 194      19.565   3.045  67.626  1.00 20.55           C  
ANISOU 1435  CB  PRO A 194     1801   2699   3307     16   -753    604       C  
ATOM   1436  CG  PRO A 194      20.585   4.029  68.126  1.00 27.62           C  
ANISOU 1436  CG  PRO A 194     2607   3625   4263    -76   -870    612       C  
ATOM   1437  CD  PRO A 194      20.986   4.873  66.957  1.00 24.59           C  
ANISOU 1437  CD  PRO A 194     2136   3215   3992    -80   -753    583       C  
ATOM   1438  N   TYR A 195      16.528   3.615  67.157  1.00 22.89           N  
ANISOU 1438  N   TYR A 195     2411   2959   3328     12   -545    434       N  
ATOM   1439  CA  TYR A 195      15.206   4.105  67.537  1.00 22.97           C  
ANISOU 1439  CA  TYR A 195     2561   2965   3202    -24   -508    356       C  
ATOM   1440  C   TYR A 195      15.076   4.304  69.044  1.00 23.09           C  
ANISOU 1440  C   TYR A 195     2658   3020   3097   -104   -622    338       C  
ATOM   1441  O   TYR A 195      15.439   3.425  69.832  1.00 21.31           O  
ANISOU 1441  O   TYR A 195     2434   2827   2838   -104   -717    406       O  
ATOM   1442  CB  TYR A 195      14.137   3.137  67.044  1.00 18.02           C  
ANISOU 1442  CB  TYR A 195     1999   2317   2530     45   -415    355       C  
ATOM   1443  CG  TYR A 195      12.722   3.645  67.234  1.00 20.38           C  
ANISOU 1443  CG  TYR A 195     2414   2608   2722     20   -355    278       C  
ATOM   1444  CD1 TYR A 195      12.285   4.809  66.599  1.00 19.07           C  
ANISOU 1444  CD1 TYR A 195     2256   2414   2576      2   -289    219       C  
ATOM   1445  CD2 TYR A 195      11.812   2.942  68.021  1.00 20.27           C  
ANISOU 1445  CD2 TYR A 195     2494   2607   2601     16   -358    274       C  
ATOM   1446  CE1 TYR A 195      10.990   5.269  66.768  1.00 17.44           C  
ANISOU 1446  CE1 TYR A 195     2135   2190   2300    -11   -233    153       C  
ATOM   1447  CE2 TYR A 195      10.498   3.398  68.187  1.00 15.71           C  
ANISOU 1447  CE2 TYR A 195     2004   2021   1945     -4   -290    202       C  
ATOM   1448  CZ  TYR A 195      10.095   4.549  67.557  1.00 18.89           C  
ANISOU 1448  CZ  TYR A 195     2400   2392   2384    -12   -229    140       C  
ATOM   1449  OH  TYR A 195       8.792   4.987  67.726  1.00 21.37           O  
ANISOU 1449  OH  TYR A 195     2783   2690   2648    -22   -160     74       O  
ATOM   1450  N   GLU A 196      14.556   5.466  69.433  1.00 27.68           N  
ANISOU 1450  N   GLU A 196     3311   3594   3611   -175   -610    246       N  
ATOM   1451  CA  GLU A 196      14.373   5.809  70.836  1.00 27.93           C  
ANISOU 1451  CA  GLU A 196     3439   3665   3507   -265   -698    199       C  
ATOM   1452  C   GLU A 196      12.894   5.936  71.253  1.00 26.84           C  
ANISOU 1452  C   GLU A 196     3438   3520   3240   -274   -607    116       C  
ATOM   1453  O   GLU A 196      12.581   5.921  72.441  1.00 27.89           O  
ANISOU 1453  O   GLU A 196     3669   3696   3231   -340   -654     82       O  
ATOM   1454  CB  GLU A 196      15.115   7.110  71.144  1.00 24.32           C  
ANISOU 1454  CB  GLU A 196     2953   3202   3085   -357   -766    142       C  
ATOM   1455  CG  GLU A 196      16.621   7.052  70.843  1.00 22.77           C  
ANISOU 1455  CG  GLU A 196     2605   3019   3028   -363   -862    225       C  
ATOM   1456  CD  GLU A 196      17.313   8.375  71.096  1.00 26.61           C  
ANISOU 1456  CD  GLU A 196     3059   3490   3562   -466   -927    165       C  
ATOM   1457  OE1 GLU A 196      17.985   8.883  70.176  1.00 34.17           O  
ANISOU 1457  OE1 GLU A 196     3901   4410   4672   -456   -892    188       O  
ATOM   1458  OE2 GLU A 196      17.193   8.907  72.221  1.00 28.24           O  
ANISOU 1458  OE2 GLU A 196     3358   3722   3650   -565  -1008     91       O  
ATOM   1459  N   GLY A 197      11.989   6.065  70.285  1.00 25.80           N  
ANISOU 1459  N   GLY A 197     3309   3339   3155   -212   -478     86       N  
ATOM   1460  CA  GLY A 197      10.560   6.170  70.579  1.00 22.46           C  
ANISOU 1460  CA  GLY A 197     2986   2904   2643   -212   -384     14       C  
ATOM   1461  C   GLY A 197      10.174   7.494  71.225  1.00 26.37           C  
ANISOU 1461  C   GLY A 197     3547   3377   3096   -284   -363   -107       C  
ATOM   1462  O   GLY A 197       9.125   7.616  71.852  1.00 21.89           O  
ANISOU 1462  O   GLY A 197     3068   2811   2438   -302   -296   -180       O  
ATOM   1463  N   VAL A 198      11.055   8.479  71.092  1.00 22.28           N  
ANISOU 1463  N   VAL A 198     2980   2831   2654   -328   -415   -132       N  
ATOM   1464  CA  VAL A 198      10.840   9.834  71.596  1.00 25.17           C  
ANISOU 1464  CA  VAL A 198     3399   3151   3013   -399   -397   -255       C  
ATOM   1465  C   VAL A 198      11.523  10.770  70.614  1.00 27.44           C  
ANISOU 1465  C   VAL A 198     3592   3369   3463   -396   -397   -242       C  
ATOM   1466  O   VAL A 198      12.627  10.476  70.169  1.00 29.38           O  
ANISOU 1466  O   VAL A 198     3745   3638   3780   -393   -467   -157       O  
ATOM   1467  CB  VAL A 198      11.456  10.075  73.006  1.00 28.76           C  
ANISOU 1467  CB  VAL A 198     3924   3660   3342   -513   -509   -311       C  
ATOM   1468  CG1 VAL A 198      11.167  11.497  73.481  1.00 29.99           C  
ANISOU 1468  CG1 VAL A 198     4145   3752   3500   -587   -472   -464       C  
ATOM   1469  CG2 VAL A 198      10.977   9.051  74.022  1.00 33.94           C  
ANISOU 1469  CG2 VAL A 198     4674   4401   3819   -530   -527   -293       C  
ATOM   1470  N   GLN A 199      10.910  11.901  70.290  1.00 26.73           N  
ANISOU 1470  N   GLN A 199     3521   3192   3444   -399   -319   -321       N  
ATOM   1471  CA  GLN A 199      11.550  12.807  69.352  1.00 22.76           C  
ANISOU 1471  CA  GLN A 199     2935   2618   3096   -404   -318   -292       C  
ATOM   1472  C   GLN A 199      12.648  13.616  70.032  1.00 29.45           C  
ANISOU 1472  C   GLN A 199     3770   3452   3965   -513   -418   -341       C  
ATOM   1473  O   GLN A 199      12.448  14.218  71.083  1.00 28.34           O  
ANISOU 1473  O   GLN A 199     3716   3296   3754   -589   -439   -459       O  
ATOM   1474  CB  GLN A 199      10.539  13.749  68.707  1.00 27.65           C  
ANISOU 1474  CB  GLN A 199     3568   3132   3805   -366   -211   -336       C  
ATOM   1475  CG  GLN A 199      11.188  14.693  67.717  1.00 31.35           C  
ANISOU 1475  CG  GLN A 199     3959   3523   4430   -378   -210   -287       C  
ATOM   1476  CD  GLN A 199      10.256  15.793  67.259  1.00 30.96           C  
ANISOU 1476  CD  GLN A 199     3929   3352   4483   -353   -125   -329       C  
ATOM   1477  OE1 GLN A 199       9.849  16.634  68.046  1.00 44.81           O  
ANISOU 1477  OE1 GLN A 199     5745   5033   6248   -395   -106   -449       O  
ATOM   1478  NE2 GLN A 199       9.938  15.805  65.975  1.00 29.40           N  
ANISOU 1478  NE2 GLN A 199     3679   3127   4364   -288    -77   -230       N  
ATOM   1479  N   ARG A 200      13.818  13.622  69.421  1.00 22.35           N  
ANISOU 1479  N   ARG A 200     2762   2564   3167   -527   -477   -253       N  
ATOM   1480  CA  ARG A 200      14.909  14.453  69.904  1.00 21.39           C  
ANISOU 1480  CA  ARG A 200     2605   2423   3101   -637   -576   -288       C  
ATOM   1481  C   ARG A 200      15.323  15.399  68.780  1.00 25.74           C  
ANISOU 1481  C   ARG A 200     3069   2882   3829   -640   -528   -246       C  
ATOM   1482  O   ARG A 200      14.659  15.459  67.747  1.00 33.67           O  
ANISOU 1482  O   ARG A 200     4063   3842   4889   -561   -423   -200       O  
ATOM   1483  CB  ARG A 200      16.062  13.567  70.372  1.00 29.32           C  
ANISOU 1483  CB  ARG A 200     3540   3531   4071   -667   -709   -211       C  
ATOM   1484  CG  ARG A 200      15.603  12.452  71.315  1.00 32.19           C  
ANISOU 1484  CG  ARG A 200     3986   3985   4258   -649   -751   -211       C  
ATOM   1485  CD  ARG A 200      16.251  12.558  72.688  1.00 42.72           C  
ANISOU 1485  CD  ARG A 200     5368   5381   5484   -767   -904   -259       C  
ATOM   1486  NE  ARG A 200      15.954  11.398  73.530  1.00 50.82           N  
ANISOU 1486  NE  ARG A 200     6463   6502   6343   -753   -956   -222       N  
ATOM   1487  CZ  ARG A 200      15.169  11.419  74.608  1.00 51.52           C  
ANISOU 1487  CZ  ARG A 200     6703   6623   6249   -805   -949   -316       C  
ATOM   1488  NH1 ARG A 200      14.591  12.546  75.001  1.00 52.93           N  
ANISOU 1488  NH1 ARG A 200     6977   6740   6394   -868   -887   -470       N  
ATOM   1489  NH2 ARG A 200      14.967  10.308  75.302  1.00 48.38           N  
ANISOU 1489  NH2 ARG A 200     6363   6314   5706   -795   -998   -254       N  
ATOM   1490  N   TYR A 201      16.409  16.142  68.957  1.00 29.05           N  
ANISOU 1490  N   TYR A 201     3426   3275   4339   -738   -609   -254       N  
ATOM   1491  CA  TYR A 201      16.803  17.059  67.892  1.00 35.35           C  
ANISOU 1491  CA  TYR A 201     4143   3981   5307   -751   -556   -203       C  
ATOM   1492  C   TYR A 201      17.418  16.271  66.732  1.00 28.57           C  
ANISOU 1492  C   TYR A 201     3161   3183   4511   -681   -519    -53       C  
ATOM   1493  O   TYR A 201      17.884  15.147  66.909  1.00 26.75           O  
ANISOU 1493  O   TYR A 201     2884   3054   4228   -647   -565      1       O  
ATOM   1494  CB  TYR A 201      17.756  18.143  68.412  1.00 39.41           C  
ANISOU 1494  CB  TYR A 201     4624   4437   5915   -888   -646   -260       C  
ATOM   1495  CG  TYR A 201      19.139  17.672  68.802  1.00 52.05           C  
ANISOU 1495  CG  TYR A 201     6113   6129   7534   -956   -780   -204       C  
ATOM   1496  CD1 TYR A 201      20.247  17.990  68.022  1.00 58.24           C  
ANISOU 1496  CD1 TYR A 201     6747   6898   8482   -993   -788   -109       C  
ATOM   1497  CD2 TYR A 201      19.344  16.927  69.957  1.00 58.51           C  
ANISOU 1497  CD2 TYR A 201     6970   7049   8213   -987   -899   -239       C  
ATOM   1498  CE1 TYR A 201      21.518  17.574  68.376  1.00 61.63           C  
ANISOU 1498  CE1 TYR A 201     7051   7409   8957  -1051   -911    -54       C  
ATOM   1499  CE2 TYR A 201      20.616  16.503  70.321  1.00 62.79           C  
ANISOU 1499  CE2 TYR A 201     7396   7672   8790  -1046  -1040   -175       C  
ATOM   1500  CZ  TYR A 201      21.697  16.829  69.527  1.00 66.13           C  
ANISOU 1500  CZ  TYR A 201     7654   8075   9397  -1074  -1045    -85       C  
ATOM   1501  OH  TYR A 201      22.962  16.408  69.883  1.00 69.78           O  
ANISOU 1501  OH  TYR A 201     7977   8616   9919  -1128  -1185    -15       O  
ATOM   1502  N   CYS A 202      17.372  16.851  65.540  1.00 28.41           N  
ANISOU 1502  N   CYS A 202     3097   3097   4601   -659   -427     13       N  
ATOM   1503  CA  CYS A 202      17.897  16.206  64.340  1.00 29.82           C  
ANISOU 1503  CA  CYS A 202     3173   3329   4827   -600   -364    142       C  
ATOM   1504  C   CYS A 202      19.411  16.056  64.422  1.00 30.58           C  
ANISOU 1504  C   CYS A 202     3129   3476   5015   -662   -433    196       C  
ATOM   1505  O   CYS A 202      20.124  17.051  64.510  1.00 28.08           O  
ANISOU 1505  O   CYS A 202     2757   3101   4811   -761   -471    190       O  
ATOM   1506  CB  CYS A 202      17.522  17.021  63.104  1.00 32.75           C  
ANISOU 1506  CB  CYS A 202     3544   3619   5281   -586   -258    204       C  
ATOM   1507  SG  CYS A 202      18.044  16.284  61.550  1.00 32.47           S  
ANISOU 1507  SG  CYS A 202     3412   3656   5269   -523   -155    347       S  
ATOM   1508  N   ARG A 203      19.901  14.823  64.371  1.00 26.77           N  
ANISOU 1508  N   ARG A 203     2578   3092   4503   -603   -448    252       N  
ATOM   1509  CA  ARG A 203      21.328  14.572  64.579  1.00 26.39           C  
ANISOU 1509  CA  ARG A 203     2377   3095   4555   -651   -526    305       C  
ATOM   1510  C   ARG A 203      21.969  14.021  63.317  1.00 29.68           C  
ANISOU 1510  C   ARG A 203     2669   3549   5060   -590   -415    412       C  
ATOM   1511  O   ARG A 203      23.064  13.479  63.362  1.00 30.44           O  
ANISOU 1511  O   ARG A 203     2623   3700   5245   -591   -452    466       O  
ATOM   1512  CB  ARG A 203      21.536  13.611  65.765  1.00 29.41           C  
ANISOU 1512  CB  ARG A 203     2765   3556   4853   -642   -659    284       C  
ATOM   1513  CG  ARG A 203      21.235  14.259  67.125  1.00 30.12           C  
ANISOU 1513  CG  ARG A 203     2963   3625   4857   -740   -784    174       C  
ATOM   1514  CD  ARG A 203      20.907  13.247  68.201  1.00 27.13           C  
ANISOU 1514  CD  ARG A 203     2657   3324   4327   -713   -878    153       C  
ATOM   1515  NE  ARG A 203      19.560  12.705  68.060  1.00 29.95           N  
ANISOU 1515  NE  ARG A 203     3146   3678   4557   -621   -780    123       N  
ATOM   1516  CZ  ARG A 203      19.106  11.656  68.736  1.00 29.01           C  
ANISOU 1516  CZ  ARG A 203     3094   3621   4309   -575   -820    127       C  
ATOM   1517  NH1 ARG A 203      19.899  11.023  69.598  1.00 23.18           N  
ANISOU 1517  NH1 ARG A 203     2307   2953   3546   -608   -963    169       N  
ATOM   1518  NH2 ARG A 203      17.857  11.239  68.551  1.00 27.12           N  
ANISOU 1518  NH2 ARG A 203     2964   3371   3971   -501   -722     99       N  
ATOM   1519  N   SER A 204      21.290  14.198  62.185  1.00 27.67           N  
ANISOU 1519  N   SER A 204     2465   3264   4783   -540   -276    441       N  
ATOM   1520  CA  SER A 204      21.820  13.766  60.888  1.00 29.76           C  
ANISOU 1520  CA  SER A 204     2636   3566   5106   -493   -147    530       C  
ATOM   1521  C   SER A 204      23.258  14.201  60.628  1.00 24.10           C  
ANISOU 1521  C   SER A 204     1745   2857   4557   -568   -144    593       C  
ATOM   1522  O   SER A 204      24.081  13.412  60.201  1.00 29.76           O  
ANISOU 1522  O   SER A 204     2336   3634   5339   -525    -93    645       O  
ATOM   1523  CB  SER A 204      20.917  14.276  59.762  1.00 25.99           C  
ANISOU 1523  CB  SER A 204     2251   3047   4577   -471    -24    557       C  
ATOM   1524  OG  SER A 204      19.687  13.610  59.839  1.00 33.48           O  
ANISOU 1524  OG  SER A 204     3326   4008   5385   -388    -13    513       O  
ATOM   1525  N   ARG A 205      23.580  15.450  60.916  1.00 27.94           N  
ANISOU 1525  N   ARG A 205     2212   3273   5129   -681   -196    583       N  
ATOM   1526  CA  ARG A 205      24.876  15.948  60.508  1.00 29.65           C  
ANISOU 1526  CA  ARG A 205     2260   3490   5517   -761   -173    652       C  
ATOM   1527  C   ARG A 205      26.000  15.353  61.371  1.00 33.46           C  
ANISOU 1527  C   ARG A 205     2589   4034   6090   -783   -297    655       C  
ATOM   1528  O   ARG A 205      27.123  15.220  60.909  1.00 33.90           O  
ANISOU 1528  O   ARG A 205     2466   4124   6290   -801   -253    726       O  
ATOM   1529  CB  ARG A 205      24.919  17.482  60.542  1.00 32.79           C  
ANISOU 1529  CB  ARG A 205     2679   3781   6000   -887   -195    645       C  
ATOM   1530  CG  ARG A 205      26.156  18.020  59.770  1.00 47.99           C  
ANISOU 1530  CG  ARG A 205     4429   5702   8103   -969   -122    743       C  
ATOM   1531  CD  ARG A 205      26.657  19.384  60.244  1.00 54.38           C  
ANISOU 1531  CD  ARG A 205     5242   6421   8997  -1095   -202    710       C  
ATOM   1532  NE  ARG A 205      28.120  19.430  60.269  1.00 61.57           N  
ANISOU 1532  NE  ARG A 205     6000   7382  10011  -1138   -221    742       N  
ATOM   1533  CZ  ARG A 205      28.847  20.514  60.535  1.00 70.80           C  
ANISOU 1533  CZ  ARG A 205     7135   8494  11272  -1250   -274    729       C  
ATOM   1534  NH1 ARG A 205      28.261  21.676  60.802  1.00 74.55           N  
ANISOU 1534  NH1 ARG A 205     7724   8851  11752  -1328   -309    678       N  
ATOM   1535  NH2 ARG A 205      30.171  20.436  60.528  1.00 72.65           N  
ANISOU 1535  NH2 ARG A 205     7217   8782  11604  -1282   -286    764       N  
ATOM   1536  N   GLU A 206      25.675  14.967  62.601  1.00 38.89           N  
ANISOU 1536  N   GLU A 206     3344   4740   6692   -778   -449    585       N  
ATOM   1537  CA  GLU A 206      26.614  14.291  63.504  1.00 43.28           C  
ANISOU 1537  CA  GLU A 206     3773   5361   7309   -790   -595    600       C  
ATOM   1538  C   GLU A 206      27.048  12.892  63.047  1.00 38.53           C  
ANISOU 1538  C   GLU A 206     3063   4834   6743   -665   -531    669       C  
ATOM   1539  O   GLU A 206      28.083  12.384  63.465  1.00 35.35           O  
ANISOU 1539  O   GLU A 206     2510   4476   6445   -663   -616    714       O  
ATOM   1540  CB  GLU A 206      25.994  14.154  64.897  1.00 46.43           C  
ANISOU 1540  CB  GLU A 206     4308   5770   7564   -813   -761    514       C  
ATOM   1541  CG  GLU A 206      25.584  15.458  65.537  1.00 56.34           C  
ANISOU 1541  CG  GLU A 206     5677   6948   8783   -936   -832    419       C  
ATOM   1542  CD  GLU A 206      24.988  15.255  66.912  1.00 59.20           C  
ANISOU 1542  CD  GLU A 206     6179   7333   8982   -961   -977    325       C  
ATOM   1543  OE1 GLU A 206      24.861  14.088  67.343  1.00 59.01           O  
ANISOU 1543  OE1 GLU A 206     6166   7385   8869   -883  -1025    352       O  
ATOM   1544  OE2 GLU A 206      24.648  16.263  67.563  1.00 64.37           O  
ANISOU 1544  OE2 GLU A 206     6936   7925   9597  -1063  -1036    225       O  
ATOM   1545  N   LYS A 207      26.245  12.256  62.212  1.00 33.41           N  
ANISOU 1545  N   LYS A 207     2505   4191   5999   -556   -383    671       N  
ATOM   1546  CA  LYS A 207      26.459  10.848  61.907  1.00 31.16           C  
ANISOU 1546  CA  LYS A 207     2154   3958   5726   -431   -326    708       C  
ATOM   1547  C   LYS A 207      27.140  10.629  60.550  1.00 31.39           C  
ANISOU 1547  C   LYS A 207     2052   4003   5871   -389   -134    768       C  
ATOM   1548  O   LYS A 207      27.159   9.524  60.013  1.00 35.23           O  
ANISOU 1548  O   LYS A 207     2511   4517   6358   -278    -33    780       O  
ATOM   1549  CB  LYS A 207      25.117  10.122  61.992  1.00 32.37           C  
ANISOU 1549  CB  LYS A 207     2498   4110   5691   -342   -301    657       C  
ATOM   1550  CG  LYS A 207      24.724   9.914  63.453  1.00 29.59           C  
ANISOU 1550  CG  LYS A 207     2232   3768   5244   -366   -488    615       C  
ATOM   1551  CD  LYS A 207      23.284   9.603  63.640  1.00 42.64           C  
ANISOU 1551  CD  LYS A 207     4085   5407   6710   -317   -465    554       C  
ATOM   1552  CE  LYS A 207      22.878   9.800  65.095  1.00 30.14           C  
ANISOU 1552  CE  LYS A 207     2603   3830   5020   -379   -633    500       C  
ATOM   1553  NZ  LYS A 207      23.724   9.033  66.030  1.00 27.55           N  
ANISOU 1553  NZ  LYS A 207     2181   3554   4734   -380   -786    551       N  
ATOM   1554  N   GLY A 208      27.701  11.701  60.009  1.00 33.66           N  
ANISOU 1554  N   GLY A 208     2273   4268   6247   -481    -75    796       N  
ATOM   1555  CA  GLY A 208      28.485  11.614  58.794  1.00 35.01           C  
ANISOU 1555  CA  GLY A 208     2367   4458   6476   -450    107    835       C  
ATOM   1556  C   GLY A 208      27.622  11.390  57.575  1.00 32.76           C  
ANISOU 1556  C   GLY A 208     2181   4180   6086   -396    296    839       C  
ATOM   1557  O   GLY A 208      26.403  11.616  57.613  1.00 29.81           O  
ANISOU 1557  O   GLY A 208     1968   3780   5577   -395    281    809       O  
ATOM   1558  N   PRO A 209      28.251  10.957  56.477  1.00 28.90           N  
ANISOU 1558  N   PRO A 209     1642   3725   5614   -348    469    857       N  
ATOM   1559  CA  PRO A 209      27.608  10.693  55.187  1.00 28.33           C  
ANISOU 1559  CA  PRO A 209     1666   3675   5422   -304    660    857       C  
ATOM   1560  C   PRO A 209      26.384   9.782  55.310  1.00 30.47           C  
ANISOU 1560  C   PRO A 209     2049   3953   5576   -217    659    817       C  
ATOM   1561  O   PRO A 209      26.390   8.875  56.141  1.00 31.38           O  
ANISOU 1561  O   PRO A 209     2141   4068   5712   -147    560    784       O  
ATOM   1562  CB  PRO A 209      28.713  10.020  54.393  1.00 29.90           C  
ANISOU 1562  CB  PRO A 209     1765   3915   5681   -252    801    854       C  
ATOM   1563  CG  PRO A 209      29.968  10.652  54.937  1.00 40.26           C  
ANISOU 1563  CG  PRO A 209     2928   5216   7153   -322    716    887       C  
ATOM   1564  CD  PRO A 209      29.719  10.822  56.404  1.00 30.86           C  
ANISOU 1564  CD  PRO A 209     1732   3994   6001   -350    488    877       C  
ATOM   1565  N   TYR A 210      25.357  10.031  54.497  1.00 25.69           N  
ANISOU 1565  N   TYR A 210     1613   3346   4800   -218    740    807       N  
ATOM   1566  CA  TYR A 210      24.173   9.179  54.474  1.00 24.22           C  
ANISOU 1566  CA  TYR A 210     1589   3164   4449   -134    730    745       C  
ATOM   1567  C   TYR A 210      24.528   7.758  54.021  1.00 24.62           C  
ANISOU 1567  C   TYR A 210     1588   3250   4516    -30    843    709       C  
ATOM   1568  O   TYR A 210      25.536   7.551  53.353  1.00 26.68           O  
ANISOU 1568  O   TYR A 210     1719   3540   4878    -23    980    730       O  
ATOM   1569  CB  TYR A 210      23.104   9.780  53.554  1.00 26.89           C  
ANISOU 1569  CB  TYR A 210     2095   3501   4622   -165    795    757       C  
ATOM   1570  CG  TYR A 210      22.444  11.029  54.106  1.00 34.55           C  
ANISOU 1570  CG  TYR A 210     3145   4410   5572   -240    672    775       C  
ATOM   1571  CD1 TYR A 210      21.599  10.959  55.207  1.00 37.29           C  
ANISOU 1571  CD1 TYR A 210     3578   4719   5872   -219    523    718       C  
ATOM   1572  CD2 TYR A 210      22.664  12.280  53.526  1.00 40.52           C  
ANISOU 1572  CD2 TYR A 210     3892   5140   6363   -334    715    849       C  
ATOM   1573  CE1 TYR A 210      20.983  12.096  55.720  1.00 38.49           C  
ANISOU 1573  CE1 TYR A 210     3803   4805   6017   -281    429    718       C  
ATOM   1574  CE2 TYR A 210      22.063  13.425  54.032  1.00 38.39           C  
ANISOU 1574  CE2 TYR A 210     3693   4792   6099   -397    609    859       C  
ATOM   1575  CZ  TYR A 210      21.218  13.326  55.131  1.00 40.91           C  
ANISOU 1575  CZ  TYR A 210     4095   5072   6376   -366    470    785       C  
ATOM   1576  OH  TYR A 210      20.599  14.448  55.643  1.00 37.63           O  
ANISOU 1576  OH  TYR A 210     3751   4571   5976   -422    382    777       O  
ATOM   1577  N   ALA A 211      23.704   6.785  54.385  1.00 23.51           N  
ANISOU 1577  N   ALA A 211     1550   3099   4284     50    793    650       N  
ATOM   1578  CA  ALA A 211      23.928   5.398  53.990  1.00 28.25           C  
ANISOU 1578  CA  ALA A 211     2119   3710   4904    152    896    605       C  
ATOM   1579  C   ALA A 211      23.275   5.105  52.640  1.00 25.75           C  
ANISOU 1579  C   ALA A 211     1931   3425   4428    164   1062    565       C  
ATOM   1580  O   ALA A 211      23.743   4.274  51.861  1.00 24.79           O  
ANISOU 1580  O   ALA A 211     1767   3322   4329    219   1221    526       O  
ATOM   1581  CB  ALA A 211      23.389   4.456  55.051  1.00 27.21           C  
ANISOU 1581  CB  ALA A 211     2035   3543   4760    222    758    569       C  
ATOM   1582  N   ALA A 212      22.171   5.793  52.387  1.00 22.74           N  
ANISOU 1582  N   ALA A 212     1707   3047   3885    113   1021    571       N  
ATOM   1583  CA  ALA A 212      21.408   5.620  51.156  1.00 37.66           C  
ANISOU 1583  CA  ALA A 212     3737   4975   5598    108   1140    545       C  
ATOM   1584  C   ALA A 212      20.619   6.881  50.843  1.00 30.98           C  
ANISOU 1584  C   ALA A 212     2997   4132   4644     23   1089    604       C  
ATOM   1585  O   ALA A 212      20.321   7.678  51.721  1.00 31.44           O  
ANISOU 1585  O   ALA A 212     3057   4146   4743    -12    949    634       O  
ATOM   1586  CB  ALA A 212      20.462   4.436  51.263  1.00 28.35           C  
ANISOU 1586  CB  ALA A 212     2670   3780   4321    182   1113    462       C  
ATOM   1587  N   LYS A 213      20.277   7.038  49.577  1.00 26.00           N  
ANISOU 1587  N   LYS A 213     2457   3550   3872    -12   1204    620       N  
ATOM   1588  CA  LYS A 213      19.533   8.194  49.128  1.00 30.74           C  
ANISOU 1588  CA  LYS A 213     3156   4151   4374    -88   1162    696       C  
ATOM   1589  C   LYS A 213      18.706   7.766  47.933  1.00 34.66           C  
ANISOU 1589  C   LYS A 213     3799   4706   4665    -92   1238    679       C  
ATOM   1590  O   LYS A 213      19.238   7.175  46.989  1.00 31.42           O  
ANISOU 1590  O   LYS A 213     3386   4356   4194    -91   1399    649       O  
ATOM   1591  CB  LYS A 213      20.484   9.336  48.758  1.00 34.67           C  
ANISOU 1591  CB  LYS A 213     3562   4653   4959   -173   1226    795       C  
ATOM   1592  CG  LYS A 213      19.797  10.532  48.131  1.00 36.99           C  
ANISOU 1592  CG  LYS A 213     3957   4940   5160   -253   1199    894       C  
ATOM   1593  CD  LYS A 213      20.803  11.524  47.604  1.00 33.80           C  
ANISOU 1593  CD  LYS A 213     3466   4542   4836   -343   1293    997       C  
ATOM   1594  CE  LYS A 213      20.095  12.662  46.902  1.00 42.09           C  
ANISOU 1594  CE  LYS A 213     4624   5576   5791   -421   1266   1113       C  
ATOM   1595  NZ  LYS A 213      19.209  12.152  45.818  1.00 42.48           N  
ANISOU 1595  NZ  LYS A 213     4825   5700   5614   -412   1315   1114       N  
ATOM   1596  N   THR A 214      17.409   8.054  47.959  1.00 28.92           N  
ANISOU 1596  N   THR A 214     3195   3963   3830   -101   1126    693       N  
ATOM   1597  CA  THR A 214      16.569   7.646  46.847  1.00 21.90           C  
ANISOU 1597  CA  THR A 214     2444   3135   2741   -115   1170    681       C  
ATOM   1598  C   THR A 214      16.520   8.742  45.776  1.00 23.02           C  
ANISOU 1598  C   THR A 214     2641   3319   2786   -207   1212    803       C  
ATOM   1599  O   THR A 214      17.140   9.791  45.923  1.00 29.51           O  
ANISOU 1599  O   THR A 214     3389   4111   3712   -256   1215    894       O  
ATOM   1600  CB  THR A 214      15.140   7.284  47.330  1.00 20.49           C  
ANISOU 1600  CB  THR A 214     2362   2926   2498    -78   1026    638       C  
ATOM   1601  OG1 THR A 214      14.623   8.340  48.139  1.00 24.95           O  
ANISOU 1601  OG1 THR A 214     2912   3422   3144    -93    891    702       O  
ATOM   1602  CG2 THR A 214      15.190   6.020  48.165  1.00 24.79           C  
ANISOU 1602  CG2 THR A 214     2874   3441   3105      4   1011    524       C  
ATOM   1603  N   ASP A 215      15.796   8.486  44.693  1.00 32.30           N  
ANISOU 1603  N   ASP A 215     3948   4564   3762   -237   1240    811       N  
ATOM   1604  CA  ASP A 215      15.770   9.407  43.561  1.00 31.72           C  
ANISOU 1604  CA  ASP A 215     3940   4545   3566   -331   1285    939       C  
ATOM   1605  C   ASP A 215      14.429  10.089  43.388  1.00 28.63           C  
ANISOU 1605  C   ASP A 215     3651   4135   3092   -357   1127   1029       C  
ATOM   1606  O   ASP A 215      14.224  10.832  42.441  1.00 31.61           O  
ANISOU 1606  O   ASP A 215     4098   4555   3357   -433   1133   1153       O  
ATOM   1607  CB  ASP A 215      16.147   8.666  42.284  1.00 35.50           C  
ANISOU 1607  CB  ASP A 215     4493   5138   3858   -366   1458    895       C  
ATOM   1608  CG  ASP A 215      17.520   8.055  42.377  1.00 40.99           C  
ANISOU 1608  CG  ASP A 215     5069   5845   4660   -335   1636    813       C  
ATOM   1609  OD1 ASP A 215      18.453   8.806  42.719  1.00 40.49           O  
ANISOU 1609  OD1 ASP A 215     4883   5748   4753   -359   1662    877       O  
ATOM   1610  OD2 ASP A 215      17.654   6.830  42.172  1.00 37.32           O  
ANISOU 1610  OD2 ASP A 215     4624   5409   4147   -286   1722    674       O  
ATOM   1611  N   GLY A 216      13.515   9.858  44.312  1.00 28.01           N  
ANISOU 1611  N   GLY A 216     3574   3991   3078   -295    985    975       N  
ATOM   1612  CA  GLY A 216      12.240  10.543  44.234  1.00 27.34           C  
ANISOU 1612  CA  GLY A 216     3558   3876   2956   -310    835   1060       C  
ATOM   1613  C   GLY A 216      11.141   9.828  44.979  1.00 27.13           C  
ANISOU 1613  C   GLY A 216     3551   3815   2941   -242    720    965       C  
ATOM   1614  O   GLY A 216      11.395   8.853  45.700  1.00 23.63           O  
ANISOU 1614  O   GLY A 216     3070   3358   2550   -184    747    839       O  
ATOM   1615  N   VAL A 217       9.922  10.338  44.808  1.00 22.96           N  
ANISOU 1615  N   VAL A 217     3077   3268   2380   -251    592   1037       N  
ATOM   1616  CA  VAL A 217       8.720   9.801  45.449  1.00 30.91           C  
ANISOU 1616  CA  VAL A 217     4097   4242   3404   -198    478    968       C  
ATOM   1617  C   VAL A 217       7.579   9.842  44.444  1.00 29.34           C  
ANISOU 1617  C   VAL A 217     3990   4102   3058   -237    390   1040       C  
ATOM   1618  O   VAL A 217       7.454  10.811  43.692  1.00 28.93           O  
ANISOU 1618  O   VAL A 217     3966   4060   2966   -290    356   1186       O  
ATOM   1619  CB  VAL A 217       8.296  10.620  46.706  1.00 28.79           C  
ANISOU 1619  CB  VAL A 217     3755   3855   3331   -153    384    981       C  
ATOM   1620  CG1 VAL A 217       7.048  10.005  47.379  1.00 21.27           C  
ANISOU 1620  CG1 VAL A 217     2809   2877   2396   -100    289    905       C  
ATOM   1621  CG2 VAL A 217       9.414  10.719  47.686  1.00 32.66           C  
ANISOU 1621  CG2 VAL A 217     4159   4294   3958   -132    445    925       C  
ATOM   1622  N   ARG A 218       6.746   8.806  44.423  1.00 29.31           N  
ANISOU 1622  N   ARG A 218     4029   4132   2975   -218    344    949       N  
ATOM   1623  CA  ARG A 218       5.563   8.812  43.565  1.00 26.69           C  
ANISOU 1623  CA  ARG A 218     3772   3855   2515   -259    231   1014       C  
ATOM   1624  C   ARG A 218       4.321   8.565  44.398  1.00 27.65           C  
ANISOU 1624  C   ARG A 218     3852   3917   2737   -206    109    971       C  
ATOM   1625  O   ARG A 218       4.375   7.873  45.422  1.00 26.44           O  
ANISOU 1625  O   ARG A 218     3654   3716   2675   -150    137    851       O  
ATOM   1626  CB  ARG A 218       5.660   7.750  42.470  1.00 29.17           C  
ANISOU 1626  CB  ARG A 218     4192   4287   2603   -315    290    944       C  
ATOM   1627  CG  ARG A 218       6.783   7.947  41.469  1.00 39.59           C  
ANISOU 1627  CG  ARG A 218     5567   5686   3790   -380    428    984       C  
ATOM   1628  CD  ARG A 218       6.521   9.129  40.558  1.00 57.15           C  
ANISOU 1628  CD  ARG A 218     7836   7947   5931   -453    359   1180       C  
ATOM   1629  NE  ARG A 218       7.493   9.203  39.473  1.00 68.50           N  
ANISOU 1629  NE  ARG A 218     9346   9482   7198   -532    500   1218       N  
ATOM   1630  CZ  ARG A 218       8.580   9.966  39.490  1.00 70.37           C  
ANISOU 1630  CZ  ARG A 218     9533   9694   7512   -545    609   1287       C  
ATOM   1631  NH1 ARG A 218       8.844  10.733  40.541  1.00 69.68           N  
ANISOU 1631  NH1 ARG A 218     9329   9489   7659   -492    583   1329       N  
ATOM   1632  NH2 ARG A 218       9.403   9.962  38.452  1.00 71.68           N  
ANISOU 1632  NH2 ARG A 218     9762   9920   7552   -594    741   1280       N  
ATOM   1633  N   GLN A 219       3.204   9.140  43.964  1.00 30.52           N  
ANISOU 1633  N   GLN A 219     4225   4282   3091   -226    -26   1080       N  
ATOM   1634  CA  GLN A 219       1.915   8.843  44.571  1.00 23.79           C  
ANISOU 1634  CA  GLN A 219     3328   3389   2321   -186   -138   1045       C  
ATOM   1635  C   GLN A 219       1.145   7.881  43.685  1.00 27.89           C  
ANISOU 1635  C   GLN A 219     3923   4006   2666   -239   -203   1011       C  
ATOM   1636  O   GLN A 219       1.069   8.078  42.474  1.00 28.26           O  
ANISOU 1636  O   GLN A 219     4048   4139   2549   -313   -244   1100       O  
ATOM   1637  CB  GLN A 219       1.078  10.109  44.780  1.00 25.59           C  
ANISOU 1637  CB  GLN A 219     3489   3537   2698   -161   -253   1182       C  
ATOM   1638  CG  GLN A 219      -0.164   9.830  45.639  1.00 25.20           C  
ANISOU 1638  CG  GLN A 219     3366   3432   2779   -106   -336   1128       C  
ATOM   1639  CD  GLN A 219      -1.065  11.031  45.817  1.00 30.49           C  
ANISOU 1639  CD  GLN A 219     3956   4014   3616    -71   -441   1254       C  
ATOM   1640  OE1 GLN A 219      -0.787  12.116  45.313  1.00 37.34           O  
ANISOU 1640  OE1 GLN A 219     4825   4850   4512    -87   -466   1393       O  
ATOM   1641  NE2 GLN A 219      -2.153  10.840  46.546  1.00 34.61           N  
ANISOU 1641  NE2 GLN A 219     4400   4487   4263    -22   -497   1208       N  
ATOM   1642  N   VAL A 220       0.552   6.858  44.286  1.00 29.15           N  
ANISOU 1642  N   VAL A 220     4065   4153   2856   -212   -218    886       N  
ATOM   1643  CA  VAL A 220      -0.379   6.012  43.553  1.00 24.67           C  
ANISOU 1643  CA  VAL A 220     3556   3662   2157   -268   -307    854       C  
ATOM   1644  C   VAL A 220      -1.666   6.816  43.338  1.00 25.47           C  
ANISOU 1644  C   VAL A 220     3601   3752   2324   -275   -480    992       C  
ATOM   1645  O   VAL A 220      -2.081   7.555  44.231  1.00 26.84           O  
ANISOU 1645  O   VAL A 220     3670   3830   2697   -208   -510   1037       O  
ATOM   1646  CB  VAL A 220      -0.686   4.689  44.319  1.00 27.51           C  
ANISOU 1646  CB  VAL A 220     3902   3993   2556   -241   -275    689       C  
ATOM   1647  CG1 VAL A 220      -1.696   3.830  43.530  1.00 26.94           C  
ANISOU 1647  CG1 VAL A 220     3888   3992   2356   -314   -378    652       C  
ATOM   1648  CG2 VAL A 220       0.588   3.913  44.571  1.00 29.80           C  
ANISOU 1648  CG2 VAL A 220     4232   4278   2814   -222   -113    566       C  
ATOM   1649  N   GLN A 221      -2.296   6.697  42.175  1.00 28.04           N  
ANISOU 1649  N   GLN A 221     3992   4173   2491   -356   -594   1059       N  
ATOM   1650  CA  GLN A 221      -3.606   7.328  41.997  1.00 31.98           C  
ANISOU 1650  CA  GLN A 221     4418   4660   3073   -358   -777   1191       C  
ATOM   1651  C   GLN A 221      -4.560   6.834  43.097  1.00 25.71           C  
ANISOU 1651  C   GLN A 221     3512   3792   2463   -298   -809   1103       C  
ATOM   1652  O   GLN A 221      -4.760   5.636  43.257  1.00 32.56           O  
ANISOU 1652  O   GLN A 221     4408   4686   3277   -321   -785    965       O  
ATOM   1653  CB  GLN A 221      -4.166   7.044  40.608  1.00 37.60           C  
ANISOU 1653  CB  GLN A 221     5223   5501   3564   -468   -911   1258       C  
ATOM   1654  CG  GLN A 221      -5.677   7.113  40.530  1.00 51.18           C  
ANISOU 1654  CG  GLN A 221     6852   7214   5380   -473  -1100   1322       C  
ATOM   1655  CD  GLN A 221      -6.206   6.641  39.191  1.00 70.76           C  
ANISOU 1655  CD  GLN A 221     9417   9802   7669   -573  -1197   1311       C  
ATOM   1656  OE1 GLN A 221      -5.786   5.603  38.677  1.00 77.08           O  
ANISOU 1656  OE1 GLN A 221    10338  10683   8267   -644  -1139   1183       O  
ATOM   1657  NE2 GLN A 221      -7.146   7.390  38.628  1.00 78.75           N  
ANISOU 1657  NE2 GLN A 221    10363  10807   8751   -579  -1341   1439       N  
ATOM   1658  N   PRO A 222      -5.111   7.761  43.896  1.00 28.57           N  
ANISOU 1658  N   PRO A 222     3749   4053   3054   -221   -847   1178       N  
ATOM   1659  CA  PRO A 222      -5.875   7.369  45.086  1.00 27.37           C  
ANISOU 1659  CA  PRO A 222     3489   3826   3084   -159   -834   1086       C  
ATOM   1660  C   PRO A 222      -7.255   6.812  44.755  1.00 30.06           C  
ANISOU 1660  C   PRO A 222     3776   4208   3435   -199   -979   1098       C  
ATOM   1661  O   PRO A 222      -7.745   7.019  43.652  1.00 28.84           O  
ANISOU 1661  O   PRO A 222     3647   4129   3183   -262  -1121   1209       O  
ATOM   1662  CB  PRO A 222      -5.995   8.676  45.863  1.00 29.32           C  
ANISOU 1662  CB  PRO A 222     3630   3956   3556    -74   -823   1168       C  
ATOM   1663  CG  PRO A 222      -5.925   9.727  44.828  1.00 31.61           C  
ANISOU 1663  CG  PRO A 222     3940   4262   3806   -101   -916   1350       C  
ATOM   1664  CD  PRO A 222      -4.987   9.225  43.776  1.00 27.54           C  
ANISOU 1664  CD  PRO A 222     3573   3861   3029   -187   -882   1343       C  
ATOM   1665  N   TYR A 223      -7.851   6.107  45.711  1.00 28.76           N  
ANISOU 1665  N   TYR A 223     3540   4001   3385   -169   -945    988       N  
ATOM   1666  CA  TYR A 223      -9.178   5.506  45.559  1.00 28.87           C  
ANISOU 1666  CA  TYR A 223     3481   4045   3442   -208  -1068    985       C  
ATOM   1667  C   TYR A 223      -9.267   4.618  44.328  1.00 31.82           C  
ANISOU 1667  C   TYR A 223     3967   4537   3587   -323  -1161    964       C  
ATOM   1668  O   TYR A 223     -10.268   4.618  43.618  1.00 33.31           O  
ANISOU 1668  O   TYR A 223     4114   4781   3763   -381  -1330   1043       O  
ATOM   1669  CB  TYR A 223     -10.252   6.592  45.510  1.00 29.91           C  
ANISOU 1669  CB  TYR A 223     3468   4135   3762   -167  -1198   1138       C  
ATOM   1670  CG  TYR A 223     -10.054   7.632  46.583  1.00 33.54           C  
ANISOU 1670  CG  TYR A 223     3839   4471   4433    -57  -1098   1156       C  
ATOM   1671  CD1 TYR A 223     -10.180   7.295  47.923  1.00 29.80           C  
ANISOU 1671  CD1 TYR A 223     3303   3926   4093      0   -972   1033       C  
ATOM   1672  CD2 TYR A 223      -9.707   8.942  46.263  1.00 36.12           C  
ANISOU 1672  CD2 TYR A 223     4156   4751   4818    -18  -1124   1293       C  
ATOM   1673  CE1 TYR A 223      -9.989   8.232  48.913  1.00 23.69           C  
ANISOU 1673  CE1 TYR A 223     2463   3043   3493     89   -876   1030       C  
ATOM   1674  CE2 TYR A 223      -9.510   9.892  47.254  1.00 34.55           C  
ANISOU 1674  CE2 TYR A 223     3884   4427   4816     75  -1028   1291       C  
ATOM   1675  CZ  TYR A 223      -9.650   9.524  48.579  1.00 29.98           C  
ANISOU 1675  CZ  TYR A 223     3250   3786   4354    127   -903   1150       C  
ATOM   1676  OH  TYR A 223      -9.465  10.451  49.580  1.00 39.70           O  
ANISOU 1676  OH  TYR A 223     4422   4898   5763    209   -805   1129       O  
ATOM   1677  N   ASN A 224      -8.217   3.843  44.096  1.00 31.89           N  
ANISOU 1677  N   ASN A 224     4113   4582   3420   -359  -1049    851       N  
ATOM   1678  CA  ASN A 224      -8.162   2.980  42.933  1.00 36.94           C  
ANISOU 1678  CA  ASN A 224     4882   5329   3825   -471  -1106    802       C  
ATOM   1679  C   ASN A 224      -7.406   1.717  43.287  1.00 23.34           C  
ANISOU 1679  C   ASN A 224     3249   3591   2029   -481   -956    614       C  
ATOM   1680  O   ASN A 224      -6.189   1.738  43.413  1.00 23.89           O  
ANISOU 1680  O   ASN A 224     3387   3645   2044   -447   -812    568       O  
ATOM   1681  CB  ASN A 224      -7.504   3.707  41.753  1.00 33.56           C  
ANISOU 1681  CB  ASN A 224     4559   4983   3211   -519  -1139    912       C  
ATOM   1682  CG  ASN A 224      -7.523   2.892  40.467  1.00 37.37           C  
ANISOU 1682  CG  ASN A 224     5187   5589   3422   -649  -1204    861       C  
ATOM   1683  OD1 ASN A 224      -7.299   1.681  40.467  1.00 33.51           O  
ANISOU 1683  OD1 ASN A 224     4774   5110   2846   -690  -1131    692       O  
ATOM   1684  ND2 ASN A 224      -7.784   3.566  39.359  1.00 49.20           N  
ANISOU 1684  ND2 ASN A 224     6722   7162   4810   -705  -1320    992       N  
ATOM   1685  N   GLU A 225      -8.142   0.620  43.420  1.00 26.93           N  
ANISOU 1685  N   GLU A 225     3695   4043   2496   -530   -996    513       N  
ATOM   1686  CA  GLU A 225      -7.565  -0.648  43.842  1.00 28.71           C  
ANISOU 1686  CA  GLU A 225     3990   4229   2689   -534   -864    341       C  
ATOM   1687  C   GLU A 225      -6.568  -1.226  42.839  1.00 30.40           C  
ANISOU 1687  C   GLU A 225     4372   4505   2674   -595   -791    252       C  
ATOM   1688  O   GLU A 225      -5.491  -1.665  43.231  1.00 33.06           O  
ANISOU 1688  O   GLU A 225     4760   4796   3006   -548   -630    161       O  
ATOM   1689  CB  GLU A 225      -8.670  -1.673  44.110  1.00 27.64           C  
ANISOU 1689  CB  GLU A 225     3807   4071   2623   -589   -936    265       C  
ATOM   1690  CG  GLU A 225      -8.133  -2.983  44.648  1.00 31.56           C  
ANISOU 1690  CG  GLU A 225     4368   4501   3122   -588   -802    101       C  
ATOM   1691  CD  GLU A 225      -9.231  -3.938  45.074  1.00 35.14           C  
ANISOU 1691  CD  GLU A 225     4761   4914   3677   -640   -861     39       C  
ATOM   1692  OE1 GLU A 225      -9.383  -4.991  44.424  1.00 30.01           O  
ANISOU 1692  OE1 GLU A 225     4201   4279   2922   -734   -889    -69       O  
ATOM   1693  OE2 GLU A 225      -9.922  -3.642  46.070  1.00 35.15           O  
ANISOU 1693  OE2 GLU A 225     4627   4864   3865   -590   -868     92       O  
ATOM   1694  N   GLY A 226      -6.934  -1.249  41.559  1.00 25.87           N  
ANISOU 1694  N   GLY A 226     3883   4036   1911   -702   -908    278       N  
ATOM   1695  CA  GLY A 226      -6.050  -1.756  40.512  1.00 26.43           C  
ANISOU 1695  CA  GLY A 226     4124   4178   1740   -772   -830    187       C  
ATOM   1696  C   GLY A 226      -4.721  -1.012  40.468  1.00 31.91           C  
ANISOU 1696  C   GLY A 226     4855   4876   2393   -708   -684    232       C  
ATOM   1697  O   GLY A 226      -3.656  -1.593  40.267  1.00 31.83           O  
ANISOU 1697  O   GLY A 226     4937   4863   2293   -705   -525    116       O  
ATOM   1698  N   ALA A 227      -4.794   0.294  40.666  1.00 32.66           N  
ANISOU 1698  N   ALA A 227     4866   4970   2573   -658   -737    403       N  
ATOM   1699  CA  ALA A 227      -3.621   1.135  40.663  1.00 30.14           C  
ANISOU 1699  CA  ALA A 227     4563   4647   2240   -606   -616    467       C  
ATOM   1700  C   ALA A 227      -2.693   0.707  41.787  1.00 27.13           C  
ANISOU 1700  C   ALA A 227     4142   4166   2001   -509   -440    361       C  
ATOM   1701  O   ALA A 227      -1.496   0.536  41.584  1.00 27.67           O  
ANISOU 1701  O   ALA A 227     4273   4243   1999   -497   -290    303       O  
ATOM   1702  CB  ALA A 227      -4.015   2.582  40.813  1.00 27.15           C  
ANISOU 1702  CB  ALA A 227     4088   4255   1972   -567   -717    666       C  
ATOM   1703  N   LEU A 228      -3.254   0.523  42.976  1.00 23.35           N  
ANISOU 1703  N   LEU A 228     3553   3596   1722   -444   -458    340       N  
ATOM   1704  CA  LEU A 228      -2.445   0.157  44.130  1.00 23.98           C  
ANISOU 1704  CA  LEU A 228     3592   3584   1936   -357   -316    259       C  
ATOM   1705  C   LEU A 228      -1.830  -1.236  43.944  1.00 23.58           C  
ANISOU 1705  C   LEU A 228     3631   3523   1808   -377   -206     93       C  
ATOM   1706  O   LEU A 228      -0.661  -1.451  44.268  1.00 25.95           O  
ANISOU 1706  O   LEU A 228     3942   3787   2132   -325    -64     39       O  
ATOM   1707  CB  LEU A 228      -3.277   0.210  45.413  1.00 20.33           C  
ANISOU 1707  CB  LEU A 228     3009   3038   1679   -299   -362    272       C  
ATOM   1708  CG  LEU A 228      -2.542  -0.146  46.702  1.00 24.95           C  
ANISOU 1708  CG  LEU A 228     3553   3534   2394   -217   -238    205       C  
ATOM   1709  CD1 LEU A 228      -1.308   0.739  46.859  1.00 20.76           C  
ANISOU 1709  CD1 LEU A 228     3016   2996   1877   -166   -149    256       C  
ATOM   1710  CD2 LEU A 228      -3.456  -0.022  47.943  1.00 19.41           C  
ANISOU 1710  CD2 LEU A 228     2742   2765   1868   -174   -279    224       C  
ATOM   1711  N   LEU A 229      -2.615  -2.180  43.433  1.00 23.09           N  
ANISOU 1711  N   LEU A 229     3624   3483   1668   -453   -273     11       N  
ATOM   1712  CA  LEU A 229      -2.106  -3.538  43.184  1.00 23.81           C  
ANISOU 1712  CA  LEU A 229     3807   3547   1693   -477   -169   -159       C  
ATOM   1713  C   LEU A 229      -0.922  -3.534  42.223  1.00 30.21           C  
ANISOU 1713  C   LEU A 229     4724   4417   2339   -497    -43   -206       C  
ATOM   1714  O   LEU A 229       0.062  -4.258  42.408  1.00 24.62           O  
ANISOU 1714  O   LEU A 229     4045   3655   1656   -454    110   -316       O  
ATOM   1715  CB  LEU A 229      -3.200  -4.436  42.598  1.00 28.91           C  
ANISOU 1715  CB  LEU A 229     4509   4216   2260   -580   -279   -238       C  
ATOM   1716  CG  LEU A 229      -4.480  -4.593  43.411  1.00 30.76           C  
ANISOU 1716  CG  LEU A 229     4636   4400   2651   -581   -401   -203       C  
ATOM   1717  CD1 LEU A 229      -5.435  -5.545  42.712  1.00 28.69           C  
ANISOU 1717  CD1 LEU A 229     4435   4163   2303   -699   -505   -293       C  
ATOM   1718  CD2 LEU A 229      -4.152  -5.071  44.808  1.00 34.16           C  
ANISOU 1718  CD2 LEU A 229     4994   4710   3274   -488   -300   -241       C  
ATOM   1719  N   TYR A 230      -1.037  -2.723  41.180  1.00 28.77           N  
ANISOU 1719  N   TYR A 230     4597   4345   1991   -564   -106   -117       N  
ATOM   1720  CA  TYR A 230       0.020  -2.628  40.201  1.00 31.68           C  
ANISOU 1720  CA  TYR A 230     5069   4786   2183   -597     20   -148       C  
ATOM   1721  C   TYR A 230       1.292  -2.100  40.858  1.00 31.66           C  
ANISOU 1721  C   TYR A 230     4996   4733   2302   -497    170   -112       C  
ATOM   1722  O   TYR A 230       2.390  -2.619  40.614  1.00 29.17           O  
ANISOU 1722  O   TYR A 230     4724   4409   1950   -478    340   -213       O  
ATOM   1723  CB  TYR A 230      -0.398  -1.735  39.036  1.00 34.18           C  
ANISOU 1723  CB  TYR A 230     5454   5234   2299   -694    -92    -23       C  
ATOM   1724  CG  TYR A 230       0.673  -1.623  37.993  1.00 40.25           C  
ANISOU 1724  CG  TYR A 230     6335   6087   2871   -738     51    -51       C  
ATOM   1725  CD1 TYR A 230       1.017  -2.716  37.209  1.00 44.56           C  
ANISOU 1725  CD1 TYR A 230     6973   6641   3317   -769    151   -225       C  
ATOM   1726  CD2 TYR A 230       1.365  -0.436  37.809  1.00 45.35           C  
ANISOU 1726  CD2 TYR A 230     6949   6768   3515   -713     96     96       C  
ATOM   1727  CE1 TYR A 230       2.016  -2.620  36.263  1.00 52.46           C  
ANISOU 1727  CE1 TYR A 230     8030   7693   4209   -774    293   -251       C  
ATOM   1728  CE2 TYR A 230       2.362  -0.333  36.861  1.00 44.25           C  
ANISOU 1728  CE2 TYR A 230     6867   6679   3266   -724    236     74       C  
ATOM   1729  CZ  TYR A 230       2.683  -1.426  36.099  1.00 47.55           C  
ANISOU 1729  CZ  TYR A 230     7373   7114   3579   -753    336    -99       C  
ATOM   1730  OH  TYR A 230       3.672  -1.323  35.159  1.00 62.08           O  
ANISOU 1730  OH  TYR A 230     9265   9010   5313   -763    481   -121       O  
ATOM   1731  N   SER A 231       1.141  -1.088  41.710  1.00 22.90           N  
ANISOU 1731  N   SER A 231     3769   3584   1348   -433    108     24       N  
ATOM   1732  CA  SER A 231       2.289  -0.526  42.403  1.00 31.53           C  
ANISOU 1732  CA  SER A 231     4787   4627   2566   -348    226     63       C  
ATOM   1733  C   SER A 231       2.923  -1.567  43.298  1.00 25.40           C  
ANISOU 1733  C   SER A 231     3974   3755   1921   -274    338    -65       C  
ATOM   1734  O   SER A 231       4.138  -1.713  43.310  1.00 29.62           O  
ANISOU 1734  O   SER A 231     4500   4274   2478   -234    483   -106       O  
ATOM   1735  CB  SER A 231       1.904   0.699  43.219  1.00 26.62           C  
ANISOU 1735  CB  SER A 231     4055   3967   2092   -301    132    211       C  
ATOM   1736  OG  SER A 231       1.768   1.825  42.374  1.00 34.96           O  
ANISOU 1736  OG  SER A 231     5137   5097   3050   -353     69    352       O  
ATOM   1737  N   ILE A 232       2.099  -2.293  44.042  1.00 20.29           N  
ANISOU 1737  N   ILE A 232     3297   3040   1370   -257    268   -117       N  
ATOM   1738  CA  ILE A 232       2.611  -3.317  44.953  1.00 25.72           C  
ANISOU 1738  CA  ILE A 232     3952   3628   2192   -188    355   -218       C  
ATOM   1739  C   ILE A 232       3.395  -4.408  44.209  1.00 26.58           C  
ANISOU 1739  C   ILE A 232     4147   3731   2221   -201    493   -363       C  
ATOM   1740  O   ILE A 232       4.426  -4.872  44.686  1.00 27.61           O  
ANISOU 1740  O   ILE A 232     4240   3796   2455   -130    614   -414       O  
ATOM   1741  CB  ILE A 232       1.471  -3.960  45.765  1.00 26.42           C  
ANISOU 1741  CB  ILE A 232     4009   3651   2378   -188    256   -242       C  
ATOM   1742  CG1 ILE A 232       0.951  -2.964  46.814  1.00 26.59           C  
ANISOU 1742  CG1 ILE A 232     3925   3652   2528   -146    170   -120       C  
ATOM   1743  CG2 ILE A 232       1.951  -5.194  46.480  1.00 25.34           C  
ANISOU 1743  CG2 ILE A 232     3866   3412   2351   -136    342   -347       C  
ATOM   1744  CD1 ILE A 232      -0.515  -3.154  47.158  1.00 24.59           C  
ANISOU 1744  CD1 ILE A 232     3641   3385   2317   -180     45   -106       C  
ATOM   1745  N   ALA A 233       2.908  -4.800  43.039  1.00 26.11           N  
ANISOU 1745  N   ALA A 233     4202   3739   1980   -294    474   -431       N  
ATOM   1746  CA  ALA A 233       3.601  -5.773  42.200  1.00 29.75           C  
ANISOU 1746  CA  ALA A 233     4762   4199   2342   -318    618   -588       C  
ATOM   1747  C   ALA A 233       4.999  -5.295  41.794  1.00 34.81           C  
ANISOU 1747  C   ALA A 233     5394   4879   2954   -283    784   -577       C  
ATOM   1748  O   ALA A 233       5.872  -6.103  41.488  1.00 28.60           O  
ANISOU 1748  O   ALA A 233     4640   4056   2172   -257    946   -705       O  
ATOM   1749  CB  ALA A 233       2.776  -6.077  40.964  1.00 28.03           C  
ANISOU 1749  CB  ALA A 233     4680   4070   1900   -445    550   -653       C  
ATOM   1750  N   ASN A 234       5.219  -3.983  41.798  1.00 33.18           N  
ANISOU 1750  N   ASN A 234     5136   4738   2734   -281    750   -424       N  
ATOM   1751  CA  ASN A 234       6.535  -3.465  41.465  1.00 35.86           C  
ANISOU 1751  CA  ASN A 234     5451   5112   3064   -255    905   -398       C  
ATOM   1752  C   ASN A 234       7.421  -3.255  42.690  1.00 30.70           C  
ANISOU 1752  C   ASN A 234     4651   4368   2646   -144    956   -353       C  
ATOM   1753  O   ASN A 234       8.619  -3.533  42.641  1.00 30.30           O  
ANISOU 1753  O   ASN A 234     4561   4296   2655    -96   1116   -405       O  
ATOM   1754  CB  ASN A 234       6.392  -2.177  40.655  1.00 39.23           C  
ANISOU 1754  CB  ASN A 234     5913   5657   3335   -330    854   -256       C  
ATOM   1755  CG  ASN A 234       5.875  -2.444  39.242  1.00 50.60           C  
ANISOU 1755  CG  ASN A 234     7514   7209   4502   -451    842   -309       C  
ATOM   1756  OD1 ASN A 234       6.281  -3.409  38.592  1.00 57.04           O  
ANISOU 1756  OD1 ASN A 234     8385   8021   5266   -455    948   -455       O  
ATOM   1757  ND2 ASN A 234       4.960  -1.609  38.777  1.00 53.70           N  
ANISOU 1757  ND2 ASN A 234     7943   7681   4778   -526    680   -178       N  
ATOM   1758  N   GLN A 235       6.825  -2.812  43.795  1.00 26.03           N  
ANISOU 1758  N   GLN A 235     3978   3725   2188   -105    821   -264       N  
ATOM   1759  CA  GLN A 235       7.548  -2.604  45.054  1.00 27.31           C  
ANISOU 1759  CA  GLN A 235     4011   3807   2557    -13    839   -219       C  
ATOM   1760  C   GLN A 235       6.576  -2.312  46.201  1.00 21.80           C  
ANISOU 1760  C   GLN A 235     3261   3060   1964      8    686   -153       C  
ATOM   1761  O   GLN A 235       5.459  -1.847  45.969  1.00 20.96           O  
ANISOU 1761  O   GLN A 235     3188   2990   1785    -43    568   -101       O  
ATOM   1762  CB  GLN A 235       8.527  -1.440  44.936  1.00 32.15           C  
ANISOU 1762  CB  GLN A 235     4561   4464   3191     -8    899   -118       C  
ATOM   1763  CG  GLN A 235       7.837  -0.092  45.076  1.00 35.88           C  
ANISOU 1763  CG  GLN A 235     5016   4970   3646    -44    767     25       C  
ATOM   1764  CD  GLN A 235       8.309   0.902  44.061  1.00 50.95           C  
ANISOU 1764  CD  GLN A 235     6953   6965   5441   -104    818    112       C  
ATOM   1765  OE1 GLN A 235       7.748   1.012  42.971  1.00 47.38           O  
ANISOU 1765  OE1 GLN A 235     6602   6593   4806   -181    793    127       O  
ATOM   1766  NE2 GLN A 235       9.351   1.643  44.409  1.00 68.47           N  
ANISOU 1766  NE2 GLN A 235     9083   9169   7762    -78    883    177       N  
ATOM   1767  N   PRO A 236       6.989  -2.602  47.437  1.00 20.12           N  
ANISOU 1767  N   PRO A 236     2963   2763   1918     82    688   -153       N  
ATOM   1768  CA  PRO A 236       6.182  -2.199  48.591  1.00 20.42           C  
ANISOU 1768  CA  PRO A 236     2950   2762   2046    100    565    -88       C  
ATOM   1769  C   PRO A 236       5.803  -0.709  48.588  1.00 24.56           C  
ANISOU 1769  C   PRO A 236     3446   3331   2553     73    487     29       C  
ATOM   1770  O   PRO A 236       6.576   0.161  48.156  1.00 24.45           O  
ANISOU 1770  O   PRO A 236     3412   3356   2522     63    533     87       O  
ATOM   1771  CB  PRO A 236       7.079  -2.538  49.762  1.00 17.22           C  
ANISOU 1771  CB  PRO A 236     2463   2285   1796    175    601    -90       C  
ATOM   1772  CG  PRO A 236       7.841  -3.736  49.278  1.00 16.71           C  
ANISOU 1772  CG  PRO A 236     2421   2187   1741    202    716   -191       C  
ATOM   1773  CD  PRO A 236       8.135  -3.436  47.841  1.00 17.89           C  
ANISOU 1773  CD  PRO A 236     2632   2417   1750    152    799   -217       C  
ATOM   1774  N   VAL A 237       4.599  -0.441  49.085  1.00 21.16           N  
ANISOU 1774  N   VAL A 237     3008   2887   2144     60    375     63       N  
ATOM   1775  CA  VAL A 237       3.976   0.872  48.984  1.00 20.33           C  
ANISOU 1775  CA  VAL A 237     2881   2810   2034     36    292    167       C  
ATOM   1776  C   VAL A 237       3.556   1.339  50.358  1.00 23.17           C  
ANISOU 1776  C   VAL A 237     3168   3108   2526     76    237    197       C  
ATOM   1777  O   VAL A 237       3.005   0.560  51.131  1.00 19.35           O  
ANISOU 1777  O   VAL A 237     2677   2585   2089     93    216    147       O  
ATOM   1778  CB  VAL A 237       2.735   0.840  48.060  1.00 21.05           C  
ANISOU 1778  CB  VAL A 237     3028   2951   2018    -26    204    182       C  
ATOM   1779  CG1 VAL A 237       2.009   2.194  48.075  1.00 22.01           C  
ANISOU 1779  CG1 VAL A 237     3107   3080   2175    -36    107    302       C  
ATOM   1780  CG2 VAL A 237       3.120   0.437  46.644  1.00 23.13           C  
ANISOU 1780  CG2 VAL A 237     3384   3289   2114    -82    257    147       C  
ATOM   1781  N   SER A 238       3.833   2.601  50.672  1.00 16.17           N  
ANISOU 1781  N   SER A 238     2234   2211   1698     85    221    273       N  
ATOM   1782  CA  SER A 238       3.358   3.197  51.916  1.00 14.33           C  
ANISOU 1782  CA  SER A 238     1944   1923   1578    114    174    292       C  
ATOM   1783  C   SER A 238       1.861   3.486  51.786  1.00 15.93           C  
ANISOU 1783  C   SER A 238     2142   2125   1786     98     88    322       C  
ATOM   1784  O   SER A 238       1.469   4.155  50.846  1.00 15.51           O  
ANISOU 1784  O   SER A 238     2100   2104   1691     69     43    391       O  
ATOM   1785  CB  SER A 238       4.100   4.501  52.212  1.00 18.90           C  
ANISOU 1785  CB  SER A 238     2478   2478   2224    121    184    354       C  
ATOM   1786  OG  SER A 238       3.449   5.187  53.270  1.00 22.69           O  
ANISOU 1786  OG  SER A 238     2918   2904   2800    140    138    361       O  
ATOM   1787  N   VAL A 239       1.045   2.976  52.699  1.00 17.06           N  
ANISOU 1787  N   VAL A 239     2263   2235   1984    113     65    279       N  
ATOM   1788  CA  VAL A 239      -0.406   3.212  52.639  1.00 15.40           C  
ANISOU 1788  CA  VAL A 239     2024   2022   1805    100     -9    305       C  
ATOM   1789  C   VAL A 239      -0.933   3.595  54.015  1.00 17.94           C  
ANISOU 1789  C   VAL A 239     2288   2287   2241    133     -4    290       C  
ATOM   1790  O   VAL A 239      -0.240   3.441  55.024  1.00 15.56           O  
ANISOU 1790  O   VAL A 239     1988   1959   1967    155     47    250       O  
ATOM   1791  CB  VAL A 239      -1.186   1.967  52.130  1.00 13.67           C  
ANISOU 1791  CB  VAL A 239     1839   1832   1522     64    -39    257       C  
ATOM   1792  CG1 VAL A 239      -0.741   1.586  50.709  1.00 16.40           C  
ANISOU 1792  CG1 VAL A 239     2259   2241   1733     20    -39    255       C  
ATOM   1793  CG2 VAL A 239      -1.039   0.794  53.088  1.00 13.26           C  
ANISOU 1793  CG2 VAL A 239     1798   1745   1495     78     12    178       C  
ATOM   1794  N   VAL A 240      -2.165   4.102  54.061  1.00 17.77           N  
ANISOU 1794  N   VAL A 240     2214   2251   2287    135    -55    321       N  
ATOM   1795  CA  VAL A 240      -2.732   4.529  55.325  1.00 17.67           C  
ANISOU 1795  CA  VAL A 240     2146   2186   2382    164    -30    296       C  
ATOM   1796  C   VAL A 240      -4.089   3.858  55.516  1.00 20.41           C  
ANISOU 1796  C   VAL A 240     2452   2537   2765    150    -54    276       C  
ATOM   1797  O   VAL A 240      -4.728   3.454  54.548  1.00 19.91           O  
ANISOU 1797  O   VAL A 240     2385   2510   2668    119   -119    303       O  
ATOM   1798  CB  VAL A 240      -2.868   6.090  55.404  1.00 17.95           C  
ANISOU 1798  CB  VAL A 240     2130   2171   2519    193    -43    351       C  
ATOM   1799  CG1 VAL A 240      -1.471   6.746  55.341  1.00 18.34           C  
ANISOU 1799  CG1 VAL A 240     2215   2209   2545    195    -13    367       C  
ATOM   1800  CG2 VAL A 240      -3.791   6.648  54.292  1.00 16.39           C  
ANISOU 1800  CG2 VAL A 240     1890   1983   2354    186   -130    441       C  
ATOM   1801  N   LEU A 241      -4.508   3.729  56.768  1.00 15.06           N  
ANISOU 1801  N   LEU A 241     1746   1828   2149    165      0    228       N  
ATOM   1802  CA  LEU A 241      -5.804   3.147  57.076  1.00 19.07           C  
ANISOU 1802  CA  LEU A 241     2201   2336   2710    148     -4    211       C  
ATOM   1803  C   LEU A 241      -6.306   3.603  58.436  1.00 18.03           C  
ANISOU 1803  C   LEU A 241     2021   2163   2666    172     72    173       C  
ATOM   1804  O   LEU A 241      -5.569   4.209  59.221  1.00 19.33           O  
ANISOU 1804  O   LEU A 241     2214   2302   2829    194    124    145       O  
ATOM   1805  CB  LEU A 241      -5.726   1.606  57.021  1.00 18.76           C  
ANISOU 1805  CB  LEU A 241     2215   2322   2590    106      2    171       C  
ATOM   1806  CG  LEU A 241      -4.537   0.906  57.686  1.00 26.49           C  
ANISOU 1806  CG  LEU A 241     3273   3294   3500    111     60    131       C  
ATOM   1807  CD1 LEU A 241      -4.499   1.093  59.194  1.00 24.07           C  
ANISOU 1807  CD1 LEU A 241     2959   2961   3225    126    129    103       C  
ATOM   1808  CD2 LEU A 241      -4.537  -0.591  57.349  1.00 27.94           C  
ANISOU 1808  CD2 LEU A 241     3504   3484   3628     73     53    101       C  
ATOM   1809  N   GLU A 242      -7.573   3.300  58.700  1.00 15.34           N  
ANISOU 1809  N   GLU A 242     1608   1820   2401    160     81    166       N  
ATOM   1810  CA  GLU A 242      -8.171   3.582  59.993  1.00 14.76           C  
ANISOU 1810  CA  GLU A 242     1489   1716   2402    175    176    118       C  
ATOM   1811  C   GLU A 242      -7.933   2.370  60.894  1.00 19.49           C  
ANISOU 1811  C   GLU A 242     2153   2335   2915    135    237     74       C  
ATOM   1812  O   GLU A 242      -8.571   1.334  60.718  1.00 21.44           O  
ANISOU 1812  O   GLU A 242     2385   2600   3159     95    223     79       O  
ATOM   1813  CB  GLU A 242      -9.667   3.879  59.831  1.00 17.49           C  
ANISOU 1813  CB  GLU A 242     1705   2048   2892    183    167    140       C  
ATOM   1814  CG  GLU A 242     -10.368   4.288  61.110  1.00 15.39           C  
ANISOU 1814  CG  GLU A 242     1380   1749   2719    202    289     83       C  
ATOM   1815  CD  GLU A 242     -11.883   4.418  60.905  1.00 25.57           C  
ANISOU 1815  CD  GLU A 242     2518   3027   4172    210    285    108       C  
ATOM   1816  OE1 GLU A 242     -12.628   3.516  61.345  1.00 29.64           O  
ANISOU 1816  OE1 GLU A 242     2997   3567   4700    167    330     88       O  
ATOM   1817  OE2 GLU A 242     -12.315   5.409  60.285  1.00 24.74           O  
ANISOU 1817  OE2 GLU A 242     2324   2885   4192    257    231    156       O  
ATOM   1818  N   ALA A 243      -7.014   2.517  61.851  1.00 19.98           N  
ANISOU 1818  N   ALA A 243     2287   2392   2913    141    293     38       N  
ATOM   1819  CA  ALA A 243      -6.531   1.428  62.705  1.00 14.67           C  
ANISOU 1819  CA  ALA A 243     1691   1736   2146    107    333     18       C  
ATOM   1820  C   ALA A 243      -7.006   1.490  64.160  1.00 16.62           C  
ANISOU 1820  C   ALA A 243     1942   1984   2390     88    436    -25       C  
ATOM   1821  O   ALA A 243      -6.634   0.649  64.959  1.00 25.80           O  
ANISOU 1821  O   ALA A 243     3173   3163   3468     55    465    -26       O  
ATOM   1822  CB  ALA A 243      -4.987   1.403  62.686  1.00 16.39           C  
ANISOU 1822  CB  ALA A 243     1993   1959   2275    118    302     24       C  
ATOM   1823  N   ALA A 244      -7.822   2.482  64.494  1.00 28.19           N  
ANISOU 1823  N   ALA A 244     3336   3429   3947    110    494    -58       N  
ATOM   1824  CA  ALA A 244      -8.180   2.770  65.884  1.00 29.27           C  
ANISOU 1824  CA  ALA A 244     3486   3566   4068     94    613   -119       C  
ATOM   1825  C   ALA A 244      -9.277   1.868  66.499  1.00 22.44           C  
ANISOU 1825  C   ALA A 244     2587   2724   3215     48    695   -121       C  
ATOM   1826  O   ALA A 244      -9.451   1.859  67.720  1.00 22.95           O  
ANISOU 1826  O   ALA A 244     2690   2806   3224     17    802   -165       O  
ATOM   1827  CB  ALA A 244      -8.615   4.238  65.993  1.00 34.66           C  
ANISOU 1827  CB  ALA A 244     4102   4202   4866    142    663   -168       C  
ATOM   1828  N   GLY A 245     -10.019   1.141  65.662  1.00 18.43           N  
ANISOU 1828  N   GLY A 245     2009   2217   2774     33    646    -74       N  
ATOM   1829  CA  GLY A 245     -11.116   0.293  66.127  1.00 20.28           C  
ANISOU 1829  CA  GLY A 245     2193   2466   3046    -18    718    -68       C  
ATOM   1830  C   GLY A 245     -10.694  -0.876  67.016  1.00 18.89           C  
ANISOU 1830  C   GLY A 245     2124   2315   2740    -81    758    -51       C  
ATOM   1831  O   GLY A 245      -9.572  -1.370  66.926  1.00 15.90           O  
ANISOU 1831  O   GLY A 245     1846   1938   2259    -84    690    -25       O  
ATOM   1832  N   LYS A 246     -11.618  -1.335  67.849  1.00 17.16           N  
ANISOU 1832  N   LYS A 246     1874   2111   2537   -132    869    -56       N  
ATOM   1833  CA  LYS A 246     -11.333  -2.397  68.800  1.00 18.67           C  
ANISOU 1833  CA  LYS A 246     2165   2323   2607   -200    916    -24       C  
ATOM   1834  C   LYS A 246     -11.057  -3.713  68.092  1.00 19.11           C  
ANISOU 1834  C   LYS A 246     2253   2353   2656   -231    817     42       C  
ATOM   1835  O   LYS A 246     -10.242  -4.507  68.550  1.00 21.51           O  
ANISOU 1835  O   LYS A 246     2665   2653   2854   -257    795     83       O  
ATOM   1836  CB  LYS A 246     -12.491  -2.545  69.797  1.00 24.96           C  
ANISOU 1836  CB  LYS A 246     2911   3143   3430   -255   1074    -40       C  
ATOM   1837  CG  LYS A 246     -12.241  -3.582  70.875  1.00 35.35           C  
ANISOU 1837  CG  LYS A 246     4341   4485   4608   -335   1131      9       C  
ATOM   1838  CD  LYS A 246     -12.859  -3.204  72.225  1.00 36.48           C  
ANISOU 1838  CD  LYS A 246     4495   4674   4690   -380   1313    -35       C  
ATOM   1839  CE  LYS A 246     -14.306  -3.595  72.329  1.00 34.51           C  
ANISOU 1839  CE  LYS A 246     4120   4428   4564   -428   1430    -27       C  
ATOM   1840  NZ  LYS A 246     -14.910  -3.224  73.661  1.00 32.90           N  
ANISOU 1840  NZ  LYS A 246     3931   4276   4295   -475   1634    -79       N  
ATOM   1841  N   ASP A 247     -11.706  -3.942  66.957  1.00 21.25           N  
ANISOU 1841  N   ASP A 247     2432   2602   3041   -230    750     51       N  
ATOM   1842  CA  ASP A 247     -11.445  -5.165  66.194  1.00 17.90           C  
ANISOU 1842  CA  ASP A 247     2044   2144   2612   -263    658     91       C  
ATOM   1843  C   ASP A 247     -10.072  -5.183  65.520  1.00 21.31           C  
ANISOU 1843  C   ASP A 247     2565   2560   2971   -214    556     93       C  
ATOM   1844  O   ASP A 247      -9.460  -6.246  65.386  1.00 23.20           O  
ANISOU 1844  O   ASP A 247     2879   2766   3170   -235    516    121       O  
ATOM   1845  CB  ASP A 247     -12.521  -5.388  65.155  1.00 20.21           C  
ANISOU 1845  CB  ASP A 247     2220   2425   3033   -289    605     90       C  
ATOM   1846  CG  ASP A 247     -13.917  -5.466  65.787  1.00 29.39           C  
ANISOU 1846  CG  ASP A 247     3271   3600   4296   -342    709     93       C  
ATOM   1847  OD1 ASP A 247     -14.158  -6.405  66.558  1.00 26.20           O  
ANISOU 1847  OD1 ASP A 247     2902   3186   3866   -411    779    123       O  
ATOM   1848  OD2 ASP A 247     -14.752  -4.582  65.527  1.00 39.89           O  
ANISOU 1848  OD2 ASP A 247     4472   4946   5737   -314    724     72       O  
ATOM   1849  N   PHE A 248      -9.612  -4.013  65.088  1.00 14.94           N  
ANISOU 1849  N   PHE A 248     1743   1772   2163   -150    523     65       N  
ATOM   1850  CA  PHE A 248      -8.295  -3.860  64.524  1.00 14.06           C  
ANISOU 1850  CA  PHE A 248     1701   1653   1987   -105    447     66       C  
ATOM   1851  C   PHE A 248      -7.250  -4.031  65.626  1.00 14.05           C  
ANISOU 1851  C   PHE A 248     1797   1656   1884   -102    477     82       C  
ATOM   1852  O   PHE A 248      -6.248  -4.718  65.446  1.00 20.83           O  
ANISOU 1852  O   PHE A 248     2724   2494   2698    -92    427    108       O  
ATOM   1853  CB  PHE A 248      -8.157  -2.485  63.859  1.00 13.68           C  
ANISOU 1853  CB  PHE A 248     1605   1620   1974    -48    413     43       C  
ATOM   1854  CG  PHE A 248      -7.075  -2.424  62.820  1.00 19.67           C  
ANISOU 1854  CG  PHE A 248     2407   2374   2692    -14    327     51       C  
ATOM   1855  CD1 PHE A 248      -5.755  -2.235  63.183  1.00 17.33           C  
ANISOU 1855  CD1 PHE A 248     2182   2077   2324     15    323     53       C  
ATOM   1856  CD2 PHE A 248      -7.381  -2.591  61.476  1.00 19.78           C  
ANISOU 1856  CD2 PHE A 248     2390   2389   2737    -19    253     56       C  
ATOM   1857  CE1 PHE A 248      -4.757  -2.189  62.219  1.00 17.34           C  
ANISOU 1857  CE1 PHE A 248     2213   2077   2299     44    263     59       C  
ATOM   1858  CE2 PHE A 248      -6.396  -2.537  60.516  1.00 23.33           C  
ANISOU 1858  CE2 PHE A 248     2886   2841   3136      5    195     59       C  
ATOM   1859  CZ  PHE A 248      -5.077  -2.339  60.893  1.00 22.12           C  
ANISOU 1859  CZ  PHE A 248     2795   2685   2926     40    209     59       C  
ATOM   1860  N   GLN A 249      -7.501  -3.392  66.761  1.00 14.35           N  
ANISOU 1860  N   GLN A 249     1840   1723   1890   -112    558     64       N  
ATOM   1861  CA  GLN A 249      -6.648  -3.505  67.941  1.00 21.78           C  
ANISOU 1861  CA  GLN A 249     2877   2684   2716   -127    581     81       C  
ATOM   1862  C   GLN A 249      -6.432  -4.955  68.350  1.00 21.20           C  
ANISOU 1862  C   GLN A 249     2867   2588   2599   -172    569    151       C  
ATOM   1863  O   GLN A 249      -5.296  -5.395  68.598  1.00 16.94           O  
ANISOU 1863  O   GLN A 249     2400   2039   1999   -161    512    193       O  
ATOM   1864  CB  GLN A 249      -7.262  -2.720  69.122  1.00 19.89           C  
ANISOU 1864  CB  GLN A 249     2635   2482   2439   -153    692     37       C  
ATOM   1865  CG  GLN A 249      -6.574  -3.010  70.484  1.00 16.40           C  
ANISOU 1865  CG  GLN A 249     2308   2077   1849   -197    717     63       C  
ATOM   1866  CD  GLN A 249      -7.314  -2.409  71.668  1.00 25.48           C  
ANISOU 1866  CD  GLN A 249     3470   3270   2940   -240    850      9       C  
ATOM   1867  OE1 GLN A 249      -8.292  -1.659  71.492  1.00 20.04           O  
ANISOU 1867  OE1 GLN A 249     2694   2577   2345   -223    932    -56       O  
ATOM   1868  NE2 GLN A 249      -6.857  -2.731  72.886  1.00 18.12           N  
ANISOU 1868  NE2 GLN A 249     2647   2383   1855   -298    874     38       N  
ATOM   1869  N   LEU A 250      -7.526  -5.702  68.440  1.00 19.77           N  
ANISOU 1869  N   LEU A 250     2652   2393   2467   -225    621    169       N  
ATOM   1870  CA  LEU A 250      -7.451  -7.067  68.963  1.00 17.00           C  
ANISOU 1870  CA  LEU A 250     2364   2009   2087   -279    624    244       C  
ATOM   1871  C   LEU A 250      -7.336  -8.118  67.865  1.00 16.65           C  
ANISOU 1871  C   LEU A 250     2311   1892   2123   -275    551    263       C  
ATOM   1872  O   LEU A 250      -7.496  -9.302  68.132  1.00 17.90           O  
ANISOU 1872  O   LEU A 250     2505   2000   2296   -323    557    320       O  
ATOM   1873  CB  LEU A 250      -8.671  -7.363  69.845  1.00 17.30           C  
ANISOU 1873  CB  LEU A 250     2380   2069   2126   -356    739    262       C  
ATOM   1874  CG  LEU A 250      -8.814  -6.399  71.037  1.00 27.26           C  
ANISOU 1874  CG  LEU A 250     3666   3402   3290   -370    838    229       C  
ATOM   1875  CD1 LEU A 250     -10.156  -6.613  71.744  1.00 23.57           C  
ANISOU 1875  CD1 LEU A 250     3153   2959   2844   -444    977    231       C  
ATOM   1876  CD2 LEU A 250      -7.619  -6.530  72.022  1.00 19.23           C  
ANISOU 1876  CD2 LEU A 250     2777   2411   2117   -380    802    280       C  
ATOM   1877  N   TYR A 251      -7.042  -7.676  66.647  1.00 17.93           N  
ANISOU 1877  N   TYR A 251     2435   2047   2331   -223    486    213       N  
ATOM   1878  CA  TYR A 251      -6.922  -8.576  65.508  1.00 21.07           C  
ANISOU 1878  CA  TYR A 251     2834   2382   2790   -222    423    204       C  
ATOM   1879  C   TYR A 251      -5.834  -9.634  65.731  1.00 23.62           C  
ANISOU 1879  C   TYR A 251     3241   2641   3093   -209    391    255       C  
ATOM   1880  O   TYR A 251      -4.710  -9.312  66.146  1.00 15.45           O  
ANISOU 1880  O   TYR A 251     2247   1620   2002   -161    367    278       O  
ATOM   1881  CB  TYR A 251      -6.644  -7.772  64.225  1.00 21.89           C  
ANISOU 1881  CB  TYR A 251     2899   2507   2911   -170    364    147       C  
ATOM   1882  CG  TYR A 251      -6.213  -8.619  63.041  1.00 21.41           C  
ANISOU 1882  CG  TYR A 251     2866   2392   2876   -165    305    122       C  
ATOM   1883  CD1 TYR A 251      -7.156  -9.277  62.244  1.00 16.95           C  
ANISOU 1883  CD1 TYR A 251     2271   1799   2370   -220    283     93       C  
ATOM   1884  CD2 TYR A 251      -4.859  -8.761  62.719  1.00 17.88           C  
ANISOU 1884  CD2 TYR A 251     2473   1922   2399   -108    276    120       C  
ATOM   1885  CE1 TYR A 251      -6.764 -10.059  61.141  1.00 18.07           C  
ANISOU 1885  CE1 TYR A 251     2453   1889   2522   -224    236     50       C  
ATOM   1886  CE2 TYR A 251      -4.446  -9.540  61.622  1.00 17.65           C  
ANISOU 1886  CE2 TYR A 251     2473   1840   2393   -102    244     80       C  
ATOM   1887  CZ  TYR A 251      -5.402 -10.185  60.840  1.00 14.56           C  
ANISOU 1887  CZ  TYR A 251     2068   1420   2043   -161    227     39       C  
ATOM   1888  OH  TYR A 251      -5.019 -10.945  59.755  1.00 14.92           O  
ANISOU 1888  OH  TYR A 251     2157   1414   2099   -164    203    -20       O  
ATOM   1889  N   ARG A 252      -6.189 -10.888  65.432  1.00 20.79           N  
ANISOU 1889  N   ARG A 252     2898   2203   2798   -252    385    270       N  
ATOM   1890  CA  ARG A 252      -5.297 -12.049  65.565  1.00 18.58           C  
ANISOU 1890  CA  ARG A 252     2688   1832   2539   -238    358    320       C  
ATOM   1891  C   ARG A 252      -4.928 -12.682  64.199  1.00 21.36           C  
ANISOU 1891  C   ARG A 252     3047   2110   2959   -213    315    254       C  
ATOM   1892  O   ARG A 252      -3.751 -12.919  63.918  1.00 22.73           O  
ANISOU 1892  O   ARG A 252     3253   2242   3140   -149    289    253       O  
ATOM   1893  CB  ARG A 252      -5.949 -13.098  66.500  1.00 17.34           C  
ANISOU 1893  CB  ARG A 252     2560   1620   2407   -315    399    402       C  
ATOM   1894  CG  ARG A 252      -5.148 -14.389  66.711  1.00 34.60           C  
ANISOU 1894  CG  ARG A 252     4815   3688   4642   -304    370    473       C  
ATOM   1895  CD  ARG A 252      -3.673 -14.097  66.940  1.00 49.38           C  
ANISOU 1895  CD  ARG A 252     6719   5569   6475   -217    321    506       C  
ATOM   1896  NE  ARG A 252      -3.300 -14.011  68.346  1.00 60.29           N  
ANISOU 1896  NE  ARG A 252     8145   6990   7773   -231    319    618       N  
ATOM   1897  CZ  ARG A 252      -2.269 -13.302  68.795  1.00 60.33           C  
ANISOU 1897  CZ  ARG A 252     8162   7056   7706   -178    276    643       C  
ATOM   1898  NH1 ARG A 252      -1.527 -12.591  67.949  1.00 59.77           N  
ANISOU 1898  NH1 ARG A 252     8052   7009   7648   -105    244    566       N  
ATOM   1899  NH2 ARG A 252      -1.991 -13.290  70.088  1.00 57.50           N  
ANISOU 1899  NH2 ARG A 252     7854   6738   7255   -207    263    746       N  
ATOM   1900  N   GLY A 253      -5.911 -12.951  63.344  1.00 23.40           N  
ANISOU 1900  N   GLY A 253     3271   2352   3266   -266    310    192       N  
ATOM   1901  CA  GLY A 253      -5.592 -13.533  62.049  1.00 17.10           C  
ANISOU 1901  CA  GLY A 253     2496   1493   2507   -256    275    113       C  
ATOM   1902  C   GLY A 253      -6.785 -13.585  61.119  1.00 24.92           C  
ANISOU 1902  C   GLY A 253     3445   2498   3527   -329    250     44       C  
ATOM   1903  O   GLY A 253      -7.921 -13.308  61.535  1.00 20.64           O  
ANISOU 1903  O   GLY A 253     2840   1999   3004   -387    263     69       O  
ATOM   1904  N   GLY A 254      -6.536 -13.931  59.856  1.00 19.17           N  
ANISOU 1904  N   GLY A 254     2745   1738   2800   -329    214    -43       N  
ATOM   1905  CA  GLY A 254      -7.623 -14.085  58.903  1.00 22.12           C  
ANISOU 1905  CA  GLY A 254     3088   2125   3192   -412    167   -110       C  
ATOM   1906  C   GLY A 254      -7.738 -12.834  58.056  1.00 21.67           C  
ANISOU 1906  C   GLY A 254     2989   2186   3061   -388    120   -142       C  
ATOM   1907  O   GLY A 254      -6.962 -11.885  58.225  1.00 22.28           O  
ANISOU 1907  O   GLY A 254     3063   2321   3082   -310    134   -116       O  
ATOM   1908  N   ILE A 255      -8.698 -12.830  57.140  1.00 19.81           N  
ANISOU 1908  N   ILE A 255     2718   1980   2828   -462     55   -190       N  
ATOM   1909  CA  ILE A 255      -8.859 -11.703  56.241  1.00 23.61           C  
ANISOU 1909  CA  ILE A 255     3162   2567   3241   -448     -7   -205       C  
ATOM   1910  C   ILE A 255      -9.825 -10.688  56.856  1.00 20.37           C  
ANISOU 1910  C   ILE A 255     2635   2230   2876   -448    -15   -135       C  
ATOM   1911  O   ILE A 255     -10.990 -11.009  57.123  1.00 21.66           O  
ANISOU 1911  O   ILE A 255     2724   2385   3120   -519    -28   -119       O  
ATOM   1912  CB  ILE A 255      -9.350 -12.154  54.866  1.00 23.98           C  
ANISOU 1912  CB  ILE A 255     3236   2622   3253   -529    -92   -287       C  
ATOM   1913  CG1 ILE A 255      -8.283 -13.009  54.181  1.00 31.09           C  
ANISOU 1913  CG1 ILE A 255     4259   3453   4100   -516    -62   -377       C  
ATOM   1914  CG2 ILE A 255      -9.648 -10.935  54.002  1.00 21.22           C  
ANISOU 1914  CG2 ILE A 255     2840   2389   2833   -523   -172   -271       C  
ATOM   1915  CD1 ILE A 255      -8.693 -13.513  52.803  1.00 28.85           C  
ANISOU 1915  CD1 ILE A 255     4029   3177   3756   -608   -136   -482       C  
ATOM   1916  N   PHE A 256      -9.320  -9.487  57.130  1.00 19.34           N  
ANISOU 1916  N   PHE A 256     2482   2159   2708   -368      4    -95       N  
ATOM   1917  CA  PHE A 256     -10.061  -8.458  57.873  1.00 20.61           C  
ANISOU 1917  CA  PHE A 256     2539   2372   2922   -349     25    -38       C  
ATOM   1918  C   PHE A 256     -10.999  -7.692  56.948  1.00 16.65           C  
ANISOU 1918  C   PHE A 256     1947   1933   2446   -373    -67    -31       C  
ATOM   1919  O   PHE A 256     -10.575  -7.106  55.961  1.00 18.39           O  
ANISOU 1919  O   PHE A 256     2193   2196   2599   -351   -130    -38       O  
ATOM   1920  CB  PHE A 256      -9.079  -7.504  58.567  1.00 15.78           C  
ANISOU 1920  CB  PHE A 256     1948   1781   2265   -258     80     -9       C  
ATOM   1921  CG  PHE A 256      -9.711  -6.546  59.538  1.00 18.84           C  
ANISOU 1921  CG  PHE A 256     2250   2201   2706   -236    131     29       C  
ATOM   1922  CD1 PHE A 256      -9.878  -6.895  60.865  1.00 22.65           C  
ANISOU 1922  CD1 PHE A 256     2735   2662   3209   -248    220     51       C  
ATOM   1923  CD2 PHE A 256     -10.082  -5.271  59.140  1.00 20.20           C  
ANISOU 1923  CD2 PHE A 256     2347   2422   2905   -201     98     44       C  
ATOM   1924  CE1 PHE A 256     -10.441  -6.001  61.774  1.00 22.82           C  
ANISOU 1924  CE1 PHE A 256     2687   2715   3268   -230    287     68       C  
ATOM   1925  CE2 PHE A 256     -10.648  -4.383  60.036  1.00 20.64           C  
ANISOU 1925  CE2 PHE A 256     2324   2493   3026   -173    161     63       C  
ATOM   1926  CZ  PHE A 256     -10.822  -4.744  61.360  1.00 22.39           C  
ANISOU 1926  CZ  PHE A 256     2552   2697   3257   -189    263     65       C  
ATOM   1927  N   VAL A 257     -12.288  -7.721  57.261  1.00 17.42           N  
ANISOU 1927  N   VAL A 257     1934   2038   2647   -424    -75     -8       N  
ATOM   1928  CA  VAL A 257     -13.288  -7.125  56.386  1.00 20.89           C  
ANISOU 1928  CA  VAL A 257     2268   2531   3137   -455   -180     12       C  
ATOM   1929  C   VAL A 257     -13.905  -5.885  57.034  1.00 30.21           C  
ANISOU 1929  C   VAL A 257     3321   3743   4416   -397   -143     67       C  
ATOM   1930  O   VAL A 257     -14.784  -5.242  56.463  1.00 32.80           O  
ANISOU 1930  O   VAL A 257     3535   4109   4820   -405   -225    102       O  
ATOM   1931  CB  VAL A 257     -14.413  -8.137  56.062  1.00 23.56           C  
ANISOU 1931  CB  VAL A 257     2550   2851   3550   -568   -239     -7       C  
ATOM   1932  CG1 VAL A 257     -13.848  -9.336  55.278  1.00 21.89           C  
ANISOU 1932  CG1 VAL A 257     2470   2597   3249   -630   -282    -81       C  
ATOM   1933  CG2 VAL A 257     -15.084  -8.602  57.349  1.00 27.77           C  
ANISOU 1933  CG2 VAL A 257     3014   3343   4193   -595   -130     14       C  
ATOM   1934  N   GLY A 258     -13.452  -5.569  58.240  1.00 27.09           N  
ANISOU 1934  N   GLY A 258     2944   3328   4021   -341    -19     72       N  
ATOM   1935  CA  GLY A 258     -14.074  -4.522  59.032  1.00 35.77           C  
ANISOU 1935  CA  GLY A 258     3930   4441   5219   -293     50    100       C  
ATOM   1936  C   GLY A 258     -14.615  -5.119  60.322  1.00 34.60           C  
ANISOU 1936  C   GLY A 258     3752   4268   5124   -330    176     95       C  
ATOM   1937  O   GLY A 258     -14.416  -6.303  60.588  1.00 31.85           O  
ANISOU 1937  O   GLY A 258     3479   3889   4736   -388    199     85       O  
ATOM   1938  N   PRO A 259     -15.336  -4.320  61.116  1.00 27.26           N  
ANISOU 1938  N   PRO A 259     2715   3350   4294   -300    266    105       N  
ATOM   1939  CA  PRO A 259     -15.786  -2.972  60.754  1.00 28.45           C  
ANISOU 1939  CA  PRO A 259     2751   3518   4541   -233    236    122       C  
ATOM   1940  C   PRO A 259     -14.681  -1.936  60.921  1.00 23.25           C  
ANISOU 1940  C   PRO A 259     2176   2855   3803   -147    257    110       C  
ATOM   1941  O   PRO A 259     -13.865  -2.066  61.821  1.00 27.23           O  
ANISOU 1941  O   PRO A 259     2784   3351   4212   -134    346     82       O  
ATOM   1942  CB  PRO A 259     -16.930  -2.712  61.744  1.00 27.93           C  
ANISOU 1942  CB  PRO A 259     2546   3449   4618   -238    363    119       C  
ATOM   1943  CG  PRO A 259     -16.486  -3.447  62.982  1.00 37.50           C  
ANISOU 1943  CG  PRO A 259     3865   4652   5732   -273    499     93       C  
ATOM   1944  CD  PRO A 259     -15.718  -4.675  62.495  1.00 34.64           C  
ANISOU 1944  CD  PRO A 259     3637   4274   5249   -328    419     98       C  
ATOM   1945  N   CYS A 260     -14.663  -0.946  60.036  1.00 21.64           N  
ANISOU 1945  N   CYS A 260     1924   2657   3639    -96    165    140       N  
ATOM   1946  CA  CYS A 260     -13.783   0.208  60.149  1.00 26.14           C  
ANISOU 1946  CA  CYS A 260     2545   3213   4175    -17    184    135       C  
ATOM   1947  C   CYS A 260     -14.289   1.283  59.199  1.00 22.17           C  
ANISOU 1947  C   CYS A 260     1936   2706   3782     27     84    192       C  
ATOM   1948  O   CYS A 260     -14.818   0.974  58.130  1.00 26.87           O  
ANISOU 1948  O   CYS A 260     2482   3328   4399    -10    -44    240       O  
ATOM   1949  CB  CYS A 260     -12.324  -0.164  59.817  1.00 28.67           C  
ANISOU 1949  CB  CYS A 260     3028   3542   4325    -18    148    124       C  
ATOM   1950  SG  CYS A 260     -12.144  -1.092  58.280  1.00 29.75           S  
ANISOU 1950  SG  CYS A 260     3216   3708   4378    -76      1    147       S  
ATOM   1951  N   GLY A 261     -14.134   2.541  59.582  1.00 22.39           N  
ANISOU 1951  N   GLY A 261     1931   2696   3879    102    136    190       N  
ATOM   1952  CA  GLY A 261     -14.475   3.630  58.681  1.00 21.43           C  
ANISOU 1952  CA  GLY A 261     1721   2555   3867    152     35    261       C  
ATOM   1953  C   GLY A 261     -13.320   4.078  57.802  1.00 26.95           C  
ANISOU 1953  C   GLY A 261     2531   3261   4446    168    -54    300       C  
ATOM   1954  O   GLY A 261     -12.347   3.344  57.610  1.00 27.15           O  
ANISOU 1954  O   GLY A 261     2690   3321   4306    130    -64    276       O  
ATOM   1955  N   ASN A 262     -13.425   5.303  57.297  1.00 20.28           N  
ANISOU 1955  N   ASN A 262     1625   2379   3701    225   -109    365       N  
ATOM   1956  CA  ASN A 262     -12.485   5.853  56.329  1.00 23.98           C  
ANISOU 1956  CA  ASN A 262     2179   2856   4079    234   -201    427       C  
ATOM   1957  C   ASN A 262     -11.644   6.986  56.881  1.00 20.22           C  
ANISOU 1957  C   ASN A 262     1744   2312   3628    294   -124    408       C  
ATOM   1958  O   ASN A 262     -11.043   7.743  56.116  1.00 20.29           O  
ANISOU 1958  O   ASN A 262     1787   2307   3616    311   -192    477       O  
ATOM   1959  CB  ASN A 262     -13.239   6.370  55.105  1.00 24.68           C  
ANISOU 1959  CB  ASN A 262     2173   2954   4251    236   -358    548       C  
ATOM   1960  CG  ASN A 262     -13.871   5.267  54.314  1.00 30.59           C  
ANISOU 1960  CG  ASN A 262     2906   3780   4935    156   -469    570       C  
ATOM   1961  OD1 ASN A 262     -14.965   5.421  53.760  1.00 38.86           O  
ANISOU 1961  OD1 ASN A 262     3826   4839   6102    148   -578    645       O  
ATOM   1962  ND2 ASN A 262     -13.190   4.134  54.257  1.00 30.13           N  
ANISOU 1962  ND2 ASN A 262     2977   3773   4699     94   -448    504       N  
ATOM   1963  N   LYS A 263     -11.660   7.140  58.200  1.00 18.82           N  
ANISOU 1963  N   LYS A 263     1560   2092   3499    320     18    315       N  
ATOM   1964  CA  LYS A 263     -10.969   8.242  58.854  1.00 19.25           C  
ANISOU 1964  CA  LYS A 263     1649   2074   3591    369     96    276       C  
ATOM   1965  C   LYS A 263      -9.564   7.729  59.162  1.00 21.24           C  
ANISOU 1965  C   LYS A 263     2054   2365   3652    332    125    227       C  
ATOM   1966  O   LYS A 263      -9.247   7.336  60.291  1.00 21.92           O  
ANISOU 1966  O   LYS A 263     2193   2456   3678    317    226    139       O  
ATOM   1967  CB  LYS A 263     -11.712   8.692  60.115  1.00 21.57           C  
ANISOU 1967  CB  LYS A 263     1866   2307   4021    407    237    189       C  
ATOM   1968  CG  LYS A 263     -11.208  10.017  60.718  1.00 24.58           C  
ANISOU 1968  CG  LYS A 263     2266   2592   4481    460    312    139       C  
ATOM   1969  CD  LYS A 263     -11.895  10.273  62.063  1.00 30.80           C  
ANISOU 1969  CD  LYS A 263     3004   3335   5365    483    478     22       C  
ATOM   1970  CE  LYS A 263     -11.409  11.544  62.740  1.00 38.38           C  
ANISOU 1970  CE  LYS A 263     3995   4192   6396    525    563    -55       C  
ATOM   1971  NZ  LYS A 263     -11.618  12.734  61.887  1.00 49.02           N  
ANISOU 1971  NZ  LYS A 263     5258   5438   7930    591    487     31       N  
ATOM   1972  N   VAL A 264      -8.757   7.648  58.112  1.00 21.93           N  
ANISOU 1972  N   VAL A 264     2206   2486   3639    312     32    292       N  
ATOM   1973  CA  VAL A 264      -7.437   7.039  58.218  1.00 18.50           C  
ANISOU 1973  CA  VAL A 264     1896   2093   3040    279     49    258       C  
ATOM   1974  C   VAL A 264      -6.596   7.760  59.278  1.00 18.30           C  
ANISOU 1974  C   VAL A 264     1916   2018   3019    298    134    193       C  
ATOM   1975  O   VAL A 264      -6.677   8.982  59.437  1.00 19.18           O  
ANISOU 1975  O   VAL A 264     1989   2056   3244    336    151    197       O  
ATOM   1976  CB  VAL A 264      -6.707   7.035  56.846  1.00 16.41           C  
ANISOU 1976  CB  VAL A 264     1683   1867   2684    258    -46    338       C  
ATOM   1977  CG1 VAL A 264      -7.484   6.178  55.855  1.00 17.50           C  
ANISOU 1977  CG1 VAL A 264     1800   2066   2783    220   -134    382       C  
ATOM   1978  CG2 VAL A 264      -6.527   8.471  56.303  1.00 19.15           C  
ANISOU 1978  CG2 VAL A 264     2000   2157   3120    292    -86    415       C  
ATOM   1979  N   ASP A 265      -5.808   6.995  60.021  1.00 17.56           N  
ANISOU 1979  N   ASP A 265     1903   1958   2810    269    182    133       N  
ATOM   1980  CA  ASP A 265      -5.121   7.537  61.180  1.00 17.18           C  
ANISOU 1980  CA  ASP A 265     1900   1878   2751    272    253     62       C  
ATOM   1981  C   ASP A 265      -3.744   6.905  61.406  1.00 14.67           C  
ANISOU 1981  C   ASP A 265     1674   1602   2298    241    244     50       C  
ATOM   1982  O   ASP A 265      -3.060   7.227  62.376  1.00 17.86           O  
ANISOU 1982  O   ASP A 265     2122   1994   2671    230    283     -4       O  
ATOM   1983  CB  ASP A 265      -5.991   7.351  62.432  1.00 19.11           C  
ANISOU 1983  CB  ASP A 265     2122   2113   3026    269    350    -17       C  
ATOM   1984  CG  ASP A 265      -6.407   5.888  62.657  1.00 17.60           C  
ANISOU 1984  CG  ASP A 265     1947   1985   2754    231    362    -19       C  
ATOM   1985  OD1 ASP A 265      -5.658   4.973  62.268  1.00 17.38           O  
ANISOU 1985  OD1 ASP A 265     1980   2000   2622    206    313      9       O  
ATOM   1986  OD2 ASP A 265      -7.498   5.637  63.221  1.00 22.65           O  
ANISOU 1986  OD2 ASP A 265     2534   2624   3448    226    426    -48       O  
ATOM   1987  N   HIS A 266      -3.343   6.005  60.515  1.00 15.74           N  
ANISOU 1987  N   HIS A 266     1835   1786   2358    226    191     97       N  
ATOM   1988  CA  HIS A 266      -2.174   5.160  60.766  1.00 16.46           C  
ANISOU 1988  CA  HIS A 266     1996   1914   2344    205    190     85       C  
ATOM   1989  C   HIS A 266      -1.521   4.788  59.450  1.00 20.02           C  
ANISOU 1989  C   HIS A 266     2464   2395   2749    202    140    138       C  
ATOM   1990  O   HIS A 266      -2.219   4.436  58.508  1.00 19.58           O  
ANISOU 1990  O   HIS A 266     2389   2357   2691    197    105    169       O  
ATOM   1991  CB  HIS A 266      -2.614   3.897  61.540  1.00 17.91           C  
ANISOU 1991  CB  HIS A 266     2204   2123   2478    183    222     54       C  
ATOM   1992  CG  HIS A 266      -1.502   2.970  61.949  1.00 18.23           C  
ANISOU 1992  CG  HIS A 266     2307   2187   2433    169    218     52       C  
ATOM   1993  ND1 HIS A 266      -0.416   3.370  62.705  1.00 16.93           N  
ANISOU 1993  ND1 HIS A 266     2173   2020   2238    166    219     37       N  
ATOM   1994  CD2 HIS A 266      -1.353   1.639  61.765  1.00 14.86           C  
ANISOU 1994  CD2 HIS A 266     1910   1777   1959    157    208     64       C  
ATOM   1995  CE1 HIS A 266       0.369   2.336  62.926  1.00 17.06           C  
ANISOU 1995  CE1 HIS A 266     2227   2056   2198    159    204     53       C  
ATOM   1996  NE2 HIS A 266      -0.181   1.268  62.375  1.00 14.93           N  
ANISOU 1996  NE2 HIS A 266     1960   1791   1922    157    203     67       N  
ATOM   1997  N   ALA A 267      -0.189   4.878  59.377  1.00 17.28           N  
ANISOU 1997  N   ALA A 267     2149   2056   2363    201    139    145       N  
ATOM   1998  CA  ALA A 267       0.525   4.450  58.180  1.00 18.41           C  
ANISOU 1998  CA  ALA A 267     2311   2231   2454    196    118    183       C  
ATOM   1999  C   ALA A 267       1.146   3.055  58.353  1.00 16.54           C  
ANISOU 1999  C   ALA A 267     2111   2017   2155    193    135    156       C  
ATOM   2000  O   ALA A 267       1.636   2.703  59.421  1.00 16.20           O  
ANISOU 2000  O   ALA A 267     2081   1966   2109    195    150    132       O  
ATOM   2001  CB  ALA A 267       1.609   5.467  57.822  1.00 16.46           C  
ANISOU 2001  CB  ALA A 267     2057   1974   2225    196    117    217       C  
ATOM   2002  N   VAL A 268       1.129   2.276  57.282  1.00 18.88           N  
ANISOU 2002  N   VAL A 268     2430   2340   2405    185    129    162       N  
ATOM   2003  CA  VAL A 268       1.656   0.921  57.271  1.00 15.55           C  
ANISOU 2003  CA  VAL A 268     2042   1921   1946    188    151    132       C  
ATOM   2004  C   VAL A 268       2.304   0.681  55.913  1.00 14.53           C  
ANISOU 2004  C   VAL A 268     1936   1820   1766    183    167    136       C  
ATOM   2005  O   VAL A 268       2.333   1.587  55.083  1.00 18.40           O  
ANISOU 2005  O   VAL A 268     2418   2334   2238    172    155    173       O  
ATOM   2006  CB  VAL A 268       0.544  -0.118  57.511  1.00 17.41           C  
ANISOU 2006  CB  VAL A 268     2293   2146   2177    169    144    104       C  
ATOM   2007  CG1 VAL A 268       0.011  -0.033  58.959  1.00 17.71           C  
ANISOU 2007  CG1 VAL A 268     2316   2163   2251    168    153     98       C  
ATOM   2008  CG2 VAL A 268      -0.561   0.109  56.540  1.00 18.36           C  
ANISOU 2008  CG2 VAL A 268     2402   2288   2287    144    106    115       C  
ATOM   2009  N   ALA A 269       2.802  -0.527  55.671  1.00 22.17           N  
ANISOU 2009  N   ALA A 269     2934   2779   2711    190    200     98       N  
ATOM   2010  CA  ALA A 269       3.380  -0.843  54.370  1.00 19.58           C  
ANISOU 2010  CA  ALA A 269     2636   2479   2324    183    236     80       C  
ATOM   2011  C   ALA A 269       2.648  -2.007  53.682  1.00 17.00           C  
ANISOU 2011  C   ALA A 269     2363   2149   1947    155    235     24       C  
ATOM   2012  O   ALA A 269       2.442  -3.085  54.263  1.00 16.70           O  
ANISOU 2012  O   ALA A 269     2338   2064   1943    162    242    -14       O  
ATOM   2013  CB  ALA A 269       4.896  -1.156  54.509  1.00 12.90           C  
ANISOU 2013  CB  ALA A 269     1770   1618   1512    220    299     72       C  
ATOM   2014  N   ALA A 270       2.255  -1.789  52.433  1.00 17.31           N  
ANISOU 2014  N   ALA A 270     2439   2238   1901    114    220     21       N  
ATOM   2015  CA  ALA A 270       1.632  -2.849  51.652  1.00 21.79           C  
ANISOU 2015  CA  ALA A 270     3066   2809   2405     73    213    -45       C  
ATOM   2016  C   ALA A 270       2.740  -3.651  50.980  1.00 23.54           C  
ANISOU 2016  C   ALA A 270     3335   3022   2589     86    306   -114       C  
ATOM   2017  O   ALA A 270       3.368  -3.155  50.048  1.00 20.40           O  
ANISOU 2017  O   ALA A 270     2958   2677   2115     74    348   -106       O  
ATOM   2018  CB  ALA A 270       0.670  -2.270  50.620  1.00 21.51           C  
ANISOU 2018  CB  ALA A 270     3052   2838   2283     13    138    -14       C  
ATOM   2019  N   VAL A 271       3.010  -4.859  51.479  1.00 18.68           N  
ANISOU 2019  N   VAL A 271     2730   2334   2035    112    348   -175       N  
ATOM   2020  CA  VAL A 271       4.132  -5.642  50.963  1.00 20.62           C  
ANISOU 2020  CA  VAL A 271     3001   2550   2282    142    451   -246       C  
ATOM   2021  C   VAL A 271       3.687  -6.795  50.098  1.00 25.42           C  
ANISOU 2021  C   VAL A 271     3693   3133   2831     99    477   -355       C  
ATOM   2022  O   VAL A 271       4.482  -7.657  49.738  1.00 18.95           O  
ANISOU 2022  O   VAL A 271     2902   2265   2035    127    573   -436       O  
ATOM   2023  CB  VAL A 271       5.011  -6.192  52.091  1.00 27.57           C  
ANISOU 2023  CB  VAL A 271     3825   3350   3299    216    488   -233       C  
ATOM   2024  CG1 VAL A 271       5.612  -5.050  52.860  1.00 21.82           C  
ANISOU 2024  CG1 VAL A 271     3022   2652   2617    248    465   -142       C  
ATOM   2025  CG2 VAL A 271       4.202  -7.137  53.034  1.00 22.99           C  
ANISOU 2025  CG2 VAL A 271     3255   2693   2789    213    438   -239       C  
ATOM   2026  N   GLY A 272       2.410  -6.835  49.755  1.00 23.25           N  
ANISOU 2026  N   GLY A 272     3457   2887   2491     28    391   -363       N  
ATOM   2027  CA  GLY A 272       1.963  -7.920  48.899  1.00 23.67           C  
ANISOU 2027  CA  GLY A 272     3598   2918   2479    -30    404   -478       C  
ATOM   2028  C   GLY A 272       0.460  -7.974  48.786  1.00 27.29           C  
ANISOU 2028  C   GLY A 272     4070   3399   2901   -110    284   -470       C  
ATOM   2029  O   GLY A 272      -0.231  -7.069  49.294  1.00 21.31           O  
ANISOU 2029  O   GLY A 272     3247   2681   2167   -113    200   -371       O  
ATOM   2030  N   TYR A 273      -0.032  -9.028  48.120  1.00 24.26           N  
ANISOU 2030  N   TYR A 273     3763   2984   2470   -175    280   -579       N  
ATOM   2031  CA  TYR A 273      -1.466  -9.238  47.954  1.00 21.21           C  
ANISOU 2031  CA  TYR A 273     3384   2615   2061   -264    160   -582       C  
ATOM   2032  C   TYR A 273      -1.800 -10.624  47.403  1.00 21.30           C  
ANISOU 2032  C   TYR A 273     3482   2558   2053   -333    173   -724       C  
ATOM   2033  O   TYR A 273      -0.925 -11.361  46.947  1.00 26.33           O  
ANISOU 2033  O   TYR A 273     4190   3142   2673   -314    282   -832       O  
ATOM   2034  CB  TYR A 273      -2.073  -8.163  47.033  1.00 20.87           C  
ANISOU 2034  CB  TYR A 273     3346   2702   1881   -327     62   -521       C  
ATOM   2035  CG  TYR A 273      -1.604  -8.248  45.614  1.00 26.24           C  
ANISOU 2035  CG  TYR A 273     4137   3452   2380   -383     97   -600       C  
ATOM   2036  CD1 TYR A 273      -2.150  -9.186  44.727  1.00 27.65           C  
ANISOU 2036  CD1 TYR A 273     4415   3633   2459   -482     66   -723       C  
ATOM   2037  CD2 TYR A 273      -0.609  -7.395  45.144  1.00 24.12           C  
ANISOU 2037  CD2 TYR A 273     3882   3251   2032   -346    168   -557       C  
ATOM   2038  CE1 TYR A 273      -1.706  -9.270  43.420  1.00 28.23           C  
ANISOU 2038  CE1 TYR A 273     4607   3780   2342   -543    110   -807       C  
ATOM   2039  CE2 TYR A 273      -0.166  -7.469  43.833  1.00 30.16           C  
ANISOU 2039  CE2 TYR A 273     4756   4090   2612   -406    218   -628       C  
ATOM   2040  CZ  TYR A 273      -0.712  -8.410  42.978  1.00 32.24           C  
ANISOU 2040  CZ  TYR A 273     5128   4361   2763   -504    192   -757       C  
ATOM   2041  OH  TYR A 273      -0.256  -8.485  41.673  1.00 33.41           O  
ANISOU 2041  OH  TYR A 273     5400   4591   2703   -571    253   -840       O  
ATOM   2042  N   GLY A 274      -3.095 -10.930  47.400  1.00 20.98           N  
ANISOU 2042  N   GLY A 274     3431   2517   2023   -417     62   -726       N  
ATOM   2043  CA  GLY A 274      -3.621 -12.143  46.807  1.00 28.92           C  
ANISOU 2043  CA  GLY A 274     4519   3465   3005   -509     45   -859       C  
ATOM   2044  C   GLY A 274      -5.001 -11.816  46.262  1.00 35.97           C  
ANISOU 2044  C   GLY A 274     5396   4445   3827   -623   -115   -831       C  
ATOM   2045  O   GLY A 274      -5.431 -10.660  46.316  1.00 33.80           O  
ANISOU 2045  O   GLY A 274     5046   4267   3529   -614   -197   -708       O  
ATOM   2046  N   PRO A 275      -5.708 -12.822  45.734  1.00 40.51           N  
ANISOU 2046  N   PRO A 275     6032   4980   4380   -731   -166   -943       N  
ATOM   2047  CA  PRO A 275      -7.011 -12.600  45.086  1.00 35.71           C  
ANISOU 2047  CA  PRO A 275     5408   4460   3700   -855   -336   -925       C  
ATOM   2048  C   PRO A 275      -8.002 -11.797  45.940  1.00 34.85           C  
ANISOU 2048  C   PRO A 275     5142   4386   3713   -837   -436   -766       C  
ATOM   2049  O   PRO A 275      -8.759 -10.991  45.398  1.00 41.17           O  
ANISOU 2049  O   PRO A 275     5897   5298   4449   -889   -569   -690       O  
ATOM   2050  CB  PRO A 275      -7.529 -14.023  44.863  1.00 41.17           C  
ANISOU 2050  CB  PRO A 275     6166   5049   4427   -958   -350  -1071       C  
ATOM   2051  CG  PRO A 275      -6.295 -14.854  44.740  1.00 39.15           C  
ANISOU 2051  CG  PRO A 275     6019   4689   4168   -902   -182  -1202       C  
ATOM   2052  CD  PRO A 275      -5.301 -14.240  45.691  1.00 35.68           C  
ANISOU 2052  CD  PRO A 275     5507   4228   3820   -747    -72  -1095       C  
ATOM   2053  N   ASN A 276      -7.976 -12.013  47.252  1.00 26.77           N  
ANISOU 2053  N   ASN A 276     4038   3270   2865   -765   -369   -716       N  
ATOM   2054  CA  ASN A 276      -9.001 -11.498  48.159  1.00 32.88           C  
ANISOU 2054  CA  ASN A 276     4667   4056   3772   -759   -435   -597       C  
ATOM   2055  C   ASN A 276      -8.513 -10.484  49.166  1.00 29.37           C  
ANISOU 2055  C   ASN A 276     4142   3623   3395   -637   -369   -481       C  
ATOM   2056  O   ASN A 276      -9.295  -9.989  49.967  1.00 24.24           O  
ANISOU 2056  O   ASN A 276     3376   2982   2854   -623   -399   -391       O  
ATOM   2057  CB  ASN A 276      -9.648 -12.650  48.944  1.00 35.94           C  
ANISOU 2057  CB  ASN A 276     5024   4326   4305   -807   -418   -633       C  
ATOM   2058  CG  ASN A 276     -10.629 -13.436  48.116  1.00 57.88           C  
ANISOU 2058  CG  ASN A 276     7828   7103   7060   -954   -529   -718       C  
ATOM   2059  OD1 ASN A 276     -11.724 -12.958  47.816  1.00 63.71           O  
ANISOU 2059  OD1 ASN A 276     8479   7921   7806  -1023   -661   -661       O  
ATOM   2060  ND2 ASN A 276     -10.251 -14.656  47.745  1.00 65.54           N  
ANISOU 2060  ND2 ASN A 276     8914   7974   8013  -1004   -480   -856       N  
ATOM   2061  N   TYR A 277      -7.219 -10.179  49.151  1.00 29.31           N  
ANISOU 2061  N   TYR A 277     4193   3614   3331   -551   -272   -488       N  
ATOM   2062  CA  TYR A 277      -6.671  -9.354  50.210  1.00 18.69           C  
ANISOU 2062  CA  TYR A 277     2780   2264   2058   -444   -207   -393       C  
ATOM   2063  C   TYR A 277      -5.453  -8.574  49.735  1.00 18.50           C  
ANISOU 2063  C   TYR A 277     2800   2290   1937   -378   -153   -380       C  
ATOM   2064  O   TYR A 277      -4.859  -8.882  48.698  1.00 22.40           O  
ANISOU 2064  O   TYR A 277     3388   2806   2315   -404   -130   -456       O  
ATOM   2065  CB  TYR A 277      -6.274 -10.227  51.409  1.00 23.53           C  
ANISOU 2065  CB  TYR A 277     3391   2763   2787   -400   -113   -406       C  
ATOM   2066  CG  TYR A 277      -5.164 -11.176  51.020  1.00 26.02           C  
ANISOU 2066  CG  TYR A 277     3810   3006   3071   -378    -28   -504       C  
ATOM   2067  CD1 TYR A 277      -5.450 -12.408  50.434  1.00 26.77           C  
ANISOU 2067  CD1 TYR A 277     3977   3031   3162   -454    -32   -616       C  
ATOM   2068  CD2 TYR A 277      -3.830 -10.811  51.173  1.00 24.08           C  
ANISOU 2068  CD2 TYR A 277     3583   2758   2808   -285     58   -491       C  
ATOM   2069  CE1 TYR A 277      -4.427 -13.259  50.038  1.00 29.63           C  
ANISOU 2069  CE1 TYR A 277     4431   3314   3512   -427     61   -717       C  
ATOM   2070  CE2 TYR A 277      -2.808 -11.646  50.784  1.00 24.59           C  
ANISOU 2070  CE2 TYR A 277     3723   2753   2865   -256    146   -581       C  
ATOM   2071  CZ  TYR A 277      -3.107 -12.862  50.217  1.00 27.82           C  
ANISOU 2071  CZ  TYR A 277     4206   3086   3277   -322    153   -697       C  
ATOM   2072  OH  TYR A 277      -2.073 -13.675  49.838  1.00 27.40           O  
ANISOU 2072  OH  TYR A 277     4224   2951   3237   -284    255   -795       O  
ATOM   2073  N   ILE A 278      -5.077  -7.599  50.549  1.00 23.30           N  
ANISOU 2073  N   ILE A 278     3341   2911   2600   -298   -123   -290       N  
ATOM   2074  CA  ILE A 278      -3.827  -6.874  50.417  1.00 19.04           C  
ANISOU 2074  CA  ILE A 278     2824   2400   2012   -227    -57   -266       C  
ATOM   2075  C   ILE A 278      -3.028  -7.202  51.675  1.00 21.30           C  
ANISOU 2075  C   ILE A 278     3088   2606   2397   -151     33   -257       C  
ATOM   2076  O   ILE A 278      -3.571  -7.207  52.771  1.00 18.03           O  
ANISOU 2076  O   ILE A 278     2616   2159   2075   -139     25   -214       O  
ATOM   2077  CB  ILE A 278      -4.078  -5.351  50.244  1.00 16.18           C  
ANISOU 2077  CB  ILE A 278     2401   2116   1629   -210   -116   -161       C  
ATOM   2078  CG1 ILE A 278      -4.724  -5.114  48.868  1.00 22.00           C  
ANISOU 2078  CG1 ILE A 278     3174   2936   2249   -291   -216   -158       C  
ATOM   2079  CG2 ILE A 278      -2.788  -4.556  50.374  1.00 17.32           C  
ANISOU 2079  CG2 ILE A 278     2550   2273   1758   -139    -42   -125       C  
ATOM   2080  CD1 ILE A 278      -5.115  -3.676  48.599  1.00 26.21           C  
ANISOU 2080  CD1 ILE A 278     3645   3535   2779   -280   -294    -39       C  
ATOM   2081  N   LEU A 279      -1.749  -7.513  51.511  1.00 18.93           N  
ANISOU 2081  N   LEU A 279     2834   2279   2078   -103    117   -296       N  
ATOM   2082  CA  LEU A 279      -0.912  -7.915  52.631  1.00 25.32           C  
ANISOU 2082  CA  LEU A 279     3623   3015   2983    -33    185   -281       C  
ATOM   2083  C   LEU A 279      -0.226  -6.707  53.254  1.00 20.76           C  
ANISOU 2083  C   LEU A 279     2989   2477   2423     28    197   -199       C  
ATOM   2084  O   LEU A 279       0.546  -5.988  52.585  1.00 20.89           O  
ANISOU 2084  O   LEU A 279     3010   2544   2384     47    222   -190       O  
ATOM   2085  CB  LEU A 279       0.134  -8.958  52.171  1.00 18.68           C  
ANISOU 2085  CB  LEU A 279     2842   2108   2147     -6    271   -367       C  
ATOM   2086  CG  LEU A 279       1.135  -9.471  53.201  1.00 21.64           C  
ANISOU 2086  CG  LEU A 279     3190   2399   2632     72    330   -342       C  
ATOM   2087  CD1 LEU A 279       0.429 -10.292  54.292  1.00 22.34           C  
ANISOU 2087  CD1 LEU A 279     3268   2407   2812     58    302   -314       C  
ATOM   2088  CD2 LEU A 279       2.236 -10.308  52.506  1.00 21.58           C  
ANISOU 2088  CD2 LEU A 279     3226   2333   2642    110    425   -430       C  
ATOM   2089  N   ILE A 280      -0.455  -6.522  54.548  1.00 19.47           N  
ANISOU 2089  N   ILE A 280     2776   2288   2334     51    186   -143       N  
ATOM   2090  CA  ILE A 280      -0.086  -5.289  55.221  1.00 17.79           C  
ANISOU 2090  CA  ILE A 280     2512   2112   2137     90    181    -75       C  
ATOM   2091  C   ILE A 280       0.893  -5.527  56.361  1.00 18.85           C  
ANISOU 2091  C   ILE A 280     2632   2203   2328    142    216    -49       C  
ATOM   2092  O   ILE A 280       0.618  -6.309  57.250  1.00 17.90           O  
ANISOU 2092  O   ILE A 280     2517   2032   2252    138    218    -40       O  
ATOM   2093  CB  ILE A 280      -1.325  -4.574  55.784  1.00 15.45           C  
ANISOU 2093  CB  ILE A 280     2165   1839   1864     64    132    -34       C  
ATOM   2094  CG1 ILE A 280      -2.257  -4.095  54.658  1.00 16.26           C  
ANISOU 2094  CG1 ILE A 280     2260   1994   1924     18     72    -33       C  
ATOM   2095  CG2 ILE A 280      -0.891  -3.444  56.718  1.00 17.24           C  
ANISOU 2095  CG2 ILE A 280     2350   2080   2120    104    142     17       C  
ATOM   2096  CD1 ILE A 280      -1.657  -3.040  53.710  1.00 16.39           C  
ANISOU 2096  CD1 ILE A 280     2282   2067   1880     30     61     -4       C  
ATOM   2097  N   ARG A 281       2.042  -4.857  56.296  1.00 15.63           N  
ANISOU 2097  N   ARG A 281     2205   1817   1919    182    239    -28       N  
ATOM   2098  CA  ARG A 281       3.056  -4.875  57.355  1.00 12.67           C  
ANISOU 2098  CA  ARG A 281     1803   1416   1597    227    251      9       C  
ATOM   2099  C   ARG A 281       2.817  -3.750  58.344  1.00 18.68           C  
ANISOU 2099  C   ARG A 281     2530   2209   2360    221    217     56       C  
ATOM   2100  O   ARG A 281       2.866  -2.567  57.964  1.00 18.75           O  
ANISOU 2100  O   ARG A 281     2516   2259   2350    217    208     69       O  
ATOM   2101  CB  ARG A 281       4.461  -4.738  56.740  1.00 16.26           C  
ANISOU 2101  CB  ARG A 281     2237   1877   2064    267    295      3       C  
ATOM   2102  CG  ARG A 281       5.579  -4.459  57.745  1.00 16.86           C  
ANISOU 2102  CG  ARG A 281     2263   1943   2201    307    285     54       C  
ATOM   2103  CD  ARG A 281       6.858  -4.341  56.985  1.00 17.65           C  
ANISOU 2103  CD  ARG A 281     2328   2052   2328    342    339     44       C  
ATOM   2104  NE  ARG A 281       8.038  -3.921  57.748  1.00 18.00           N  
ANISOU 2104  NE  ARG A 281     2303   2098   2439    373    322     96       N  
ATOM   2105  CZ  ARG A 281       8.883  -4.746  58.361  1.00 22.53           C  
ANISOU 2105  CZ  ARG A 281     2839   2621   3098    418    317    120       C  
ATOM   2106  NH1 ARG A 281       8.633  -6.056  58.417  1.00 17.10           N  
ANISOU 2106  NH1 ARG A 281     2185   1865   2448    440    332    100       N  
ATOM   2107  NH2 ARG A 281       9.964  -4.255  58.963  1.00 19.90           N  
ANISOU 2107  NH2 ARG A 281     2433   2302   2825    437    286    171       N  
ATOM   2108  N   ASN A 282       2.540  -4.109  59.601  1.00 14.28           N  
ANISOU 2108  N   ASN A 282     1976   1627   1821    216    202     81       N  
ATOM   2109  CA  ASN A 282       2.296  -3.117  60.666  1.00 16.85           C  
ANISOU 2109  CA  ASN A 282     2285   1982   2137    203    183    106       C  
ATOM   2110  C   ASN A 282       3.575  -2.928  61.505  1.00 17.16           C  
ANISOU 2110  C   ASN A 282     2311   2021   2187    227    165    140       C  
ATOM   2111  O   ASN A 282       4.553  -3.674  61.334  1.00 18.20           O  
ANISOU 2111  O   ASN A 282     2436   2126   2354    259    166    155       O  
ATOM   2112  CB  ASN A 282       1.118  -3.554  61.549  1.00 12.33           C  
ANISOU 2112  CB  ASN A 282     1730   1398   1557    168    187    110       C  
ATOM   2113  CG  ASN A 282       0.402  -2.389  62.200  1.00 16.72           C  
ANISOU 2113  CG  ASN A 282     2265   1986   2101    149    193    104       C  
ATOM   2114  OD1 ASN A 282       0.908  -1.271  62.242  1.00 17.86           O  
ANISOU 2114  OD1 ASN A 282     2391   2150   2245    162    185    102       O  
ATOM   2115  ND2 ASN A 282      -0.827  -2.636  62.661  1.00 15.19           N  
ANISOU 2115  ND2 ASN A 282     2070   1790   1911    116    216     96       N  
ATOM   2116  N   SER A 283       3.572  -1.941  62.395  1.00 18.82           N  
ANISOU 2116  N   SER A 283     2514   2258   2378    210    146    148       N  
ATOM   2117  CA  SER A 283       4.758  -1.612  63.207  1.00 17.27           C  
ANISOU 2117  CA  SER A 283     2303   2072   2185    216    109    178       C  
ATOM   2118  C   SER A 283       4.427  -1.650  64.693  1.00 20.75           C  
ANISOU 2118  C   SER A 283     2784   2527   2575    180     87    192       C  
ATOM   2119  O   SER A 283       4.815  -0.763  65.465  1.00 15.28           O  
ANISOU 2119  O   SER A 283     2092   1861   1853    156     59    186       O  
ATOM   2120  CB  SER A 283       5.298  -0.241  62.808  1.00 11.61           C  
ANISOU 2120  CB  SER A 283     1548   1377   1484    215    104    165       C  
ATOM   2121  OG  SER A 283       4.228   0.699  62.765  1.00 16.44           O  
ANISOU 2121  OG  SER A 283     2168   1996   2083    193    124    133       O  
ATOM   2122  N   TRP A 284       3.680  -2.689  65.066  1.00 22.24           N  
ANISOU 2122  N   TRP A 284     3009   2697   2745    167    102    208       N  
ATOM   2123  CA  TRP A 284       3.246  -2.938  66.438  1.00 18.55           C  
ANISOU 2123  CA  TRP A 284     2591   2246   2211    123     96    233       C  
ATOM   2124  C   TRP A 284       3.889  -4.193  66.998  1.00 16.58           C  
ANISOU 2124  C   TRP A 284     2366   1969   1967    130     52    310       C  
ATOM   2125  O   TRP A 284       3.372  -4.790  67.928  1.00 16.51           O  
ANISOU 2125  O   TRP A 284     2407   1962   1906     92     55    348       O  
ATOM   2126  CB  TRP A 284       1.721  -3.080  66.500  1.00 18.21           C  
ANISOU 2126  CB  TRP A 284     2565   2201   2151     91    159    202       C  
ATOM   2127  CG  TRP A 284       0.998  -1.814  66.159  1.00 16.05           C  
ANISOU 2127  CG  TRP A 284     2262   1948   1889     87    196    139       C  
ATOM   2128  CD1 TRP A 284       1.532  -0.554  66.074  1.00 20.33           C  
ANISOU 2128  CD1 TRP A 284     2783   2506   2438     97    182    109       C  
ATOM   2129  CD2 TRP A 284      -0.396  -1.682  65.845  1.00 17.22           C  
ANISOU 2129  CD2 TRP A 284     2386   2092   2063     73    250    106       C  
ATOM   2130  NE1 TRP A 284       0.550   0.353  65.727  1.00 18.00           N  
ANISOU 2130  NE1 TRP A 284     2456   2206   2175     97    225     62       N  
ATOM   2131  CE2 TRP A 284      -0.642  -0.316  65.585  1.00 14.71           C  
ANISOU 2131  CE2 TRP A 284     2032   1783   1774     85    265     61       C  
ATOM   2132  CE3 TRP A 284      -1.454  -2.586  65.752  1.00 16.23           C  
ANISOU 2132  CE3 TRP A 284     2259   1950   1955     50    282    114       C  
ATOM   2133  CZ2 TRP A 284      -1.916   0.173  65.254  1.00 13.73           C  
ANISOU 2133  CZ2 TRP A 284     1862   1652   1702     83    308     30       C  
ATOM   2134  CZ3 TRP A 284      -2.734  -2.097  65.419  1.00 14.63           C  
ANISOU 2134  CZ3 TRP A 284     2008   1753   1800     39    325     79       C  
ATOM   2135  CH2 TRP A 284      -2.940  -0.729  65.166  1.00 15.30           C  
ANISOU 2135  CH2 TRP A 284     2049   1846   1919     61    335     41       C  
ATOM   2136  N   GLY A 285       5.004  -4.604  66.399  1.00 17.71           N  
ANISOU 2136  N   GLY A 285     2467   2081   2182    181     19    337       N  
ATOM   2137  CA  GLY A 285       5.699  -5.814  66.813  1.00 17.45           C  
ANISOU 2137  CA  GLY A 285     2439   2002   2191    204    -26    417       C  
ATOM   2138  C   GLY A 285       5.036  -7.101  66.328  1.00 18.72           C  
ANISOU 2138  C   GLY A 285     2622   2087   2402    216     17    423       C  
ATOM   2139  O   GLY A 285       3.996  -7.073  65.673  1.00 20.61           O  
ANISOU 2139  O   GLY A 285     2874   2322   2635    198     74    363       O  
ATOM   2140  N   THR A 286       5.650  -8.238  66.649  1.00 16.57           N  
ANISOU 2140  N   THR A 286     2352   1750   2193    245    -20    500       N  
ATOM   2141  CA  THR A 286       5.174  -9.518  66.156  1.00 18.34           C  
ANISOU 2141  CA  THR A 286     2597   1880   2491    258     19    501       C  
ATOM   2142  C   THR A 286       4.029 -10.073  67.016  1.00 24.25           C  
ANISOU 2142  C   THR A 286     3414   2620   3182    190     30    545       C  
ATOM   2143  O   THR A 286       3.383 -11.044  66.620  1.00 22.40           O  
ANISOU 2143  O   THR A 286     3201   2307   3001    180     68    536       O  
ATOM   2144  CB  THR A 286       6.324 -10.565  66.091  1.00 23.25           C  
ANISOU 2144  CB  THR A 286     3184   2409   3240    328    -16    566       C  
ATOM   2145  OG1 THR A 286       6.931 -10.696  67.376  1.00 19.54           O  
ANISOU 2145  OG1 THR A 286     2720   1954   2749    319   -107    688       O  
ATOM   2146  CG2 THR A 286       7.404 -10.118  65.093  1.00 19.51           C  
ANISOU 2146  CG2 THR A 286     2633   1939   2842    395      3    512       C  
ATOM   2147  N   GLY A 287       3.769  -9.463  68.173  1.00 19.13           N  
ANISOU 2147  N   GLY A 287     2799   2048   2420    136      6    585       N  
ATOM   2148  CA  GLY A 287       2.688  -9.937  69.043  1.00 23.52           C  
ANISOU 2148  CA  GLY A 287     3419   2607   2909     63     35    629       C  
ATOM   2149  C   GLY A 287       1.288  -9.434  68.687  1.00 18.98           C  
ANISOU 2149  C   GLY A 287     2844   2067   2300     16    120    541       C  
ATOM   2150  O   GLY A 287       0.313  -9.643  69.432  1.00 21.19           O  
ANISOU 2150  O   GLY A 287     3163   2365   2522    -51    164    566       O  
ATOM   2151  N   TRP A 288       1.187  -8.771  67.536  1.00 22.65           N  
ANISOU 2151  N   TRP A 288     3259   2543   2805     49    144    445       N  
ATOM   2152  CA  TRP A 288      -0.081  -8.296  66.999  1.00 21.76           C  
ANISOU 2152  CA  TRP A 288     3124   2454   2688     17    205    369       C  
ATOM   2153  C   TRP A 288      -0.373  -9.000  65.694  1.00 19.41           C  
ANISOU 2153  C   TRP A 288     2806   2092   2478     34    216    323       C  
ATOM   2154  O   TRP A 288       0.542  -9.251  64.933  1.00 20.27           O  
ANISOU 2154  O   TRP A 288     2903   2163   2635     87    193    307       O  
ATOM   2155  CB  TRP A 288      -0.054  -6.773  66.760  1.00 14.65           C  
ANISOU 2155  CB  TRP A 288     2188   1628   1751     31    212    303       C  
ATOM   2156  CG  TRP A 288      -1.350  -6.260  66.172  1.00 15.62           C  
ANISOU 2156  CG  TRP A 288     2273   1770   1894      8    263    238       C  
ATOM   2157  CD1 TRP A 288      -2.482  -5.913  66.862  1.00 15.11           C  
ANISOU 2157  CD1 TRP A 288     2202   1738   1801    -40    320    226       C  
ATOM   2158  CD2 TRP A 288      -1.648  -6.048  64.782  1.00 16.92           C  
ANISOU 2158  CD2 TRP A 288     2393   1924   2113     30    257    185       C  
ATOM   2159  NE1 TRP A 288      -3.468  -5.498  65.985  1.00 13.38           N  
ANISOU 2159  NE1 TRP A 288     1922   1522   1640    -42    343    174       N  
ATOM   2160  CE2 TRP A 288      -2.985  -5.585  64.705  1.00 12.60           C  
ANISOU 2160  CE2 TRP A 288     1806   1401   1582     -4    295    153       C  
ATOM   2161  CE3 TRP A 288      -0.927  -6.236  63.592  1.00 14.75           C  
ANISOU 2161  CE3 TRP A 288     2109   1624   1871     71    228    162       C  
ATOM   2162  CZ2 TRP A 288      -3.610  -5.270  63.481  1.00 14.53           C  
ANISOU 2162  CZ2 TRP A 288     2001   1648   1872      0    280    112       C  
ATOM   2163  CZ3 TRP A 288      -1.552  -5.930  62.380  1.00 20.17           C  
ANISOU 2163  CZ3 TRP A 288     2764   2320   2579     67    225    114       C  
ATOM   2164  CH2 TRP A 288      -2.876  -5.439  62.340  1.00 14.20           C  
ANISOU 2164  CH2 TRP A 288     1968   1591   1835     31    240     96       C  
ATOM   2165  N   GLY A 289      -1.637  -9.309  65.424  1.00 15.09           N  
ANISOU 2165  N   GLY A 289     2251   1533   1951    -16    255    294       N  
ATOM   2166  CA  GLY A 289      -1.983  -9.855  64.126  1.00 14.03           C  
ANISOU 2166  CA  GLY A 289     2101   1349   1881    -15    254    234       C  
ATOM   2167  C   GLY A 289      -1.198 -11.103  63.738  1.00 23.50           C  
ANISOU 2167  C   GLY A 289     3334   2446   3148     14    239    246       C  
ATOM   2168  O   GLY A 289      -0.835 -11.911  64.602  1.00 20.85           O  
ANISOU 2168  O   GLY A 289     3032   2055   2836     13    232    325       O  
ATOM   2169  N   GLU A 290      -0.951 -11.273  62.437  1.00 17.80           N  
ANISOU 2169  N   GLU A 290     2607   1698   2460     39    239    169       N  
ATOM   2170  CA  GLU A 290      -0.298 -12.482  61.923  1.00 17.93           C  
ANISOU 2170  CA  GLU A 290     2653   1603   2556     68    245    152       C  
ATOM   2171  C   GLU A 290       1.211 -12.261  61.927  1.00 19.93           C  
ANISOU 2171  C   GLU A 290     2891   1853   2828    153    237    173       C  
ATOM   2172  O   GLU A 290       1.806 -11.918  60.897  1.00 20.41           O  
ANISOU 2172  O   GLU A 290     2936   1930   2887    192    255    104       O  
ATOM   2173  CB  GLU A 290      -0.819 -12.832  60.517  1.00 18.74           C  
ANISOU 2173  CB  GLU A 290     2768   1680   2671     40    259     42       C  
ATOM   2174  CG  GLU A 290      -2.318 -13.207  60.511  1.00 20.89           C  
ANISOU 2174  CG  GLU A 290     3042   1945   2952    -53    254     27       C  
ATOM   2175  CD  GLU A 290      -2.910 -13.504  59.120  1.00 24.39           C  
ANISOU 2175  CD  GLU A 290     3498   2376   3392    -99    244    -82       C  
ATOM   2176  OE1 GLU A 290      -2.404 -13.000  58.098  1.00 25.99           O  
ANISOU 2176  OE1 GLU A 290     3707   2624   3545    -70    242   -147       O  
ATOM   2177  OE2 GLU A 290      -3.916 -14.245  59.053  1.00 22.72           O  
ANISOU 2177  OE2 GLU A 290     3294   2115   3223   -177    236   -101       O  
ATOM   2178  N   ASN A 291       1.801 -12.457  63.106  1.00 24.04           N  
ANISOU 2178  N   ASN A 291     3413   2357   3364    174    208    274       N  
ATOM   2179  CA  ASN A 291       3.211 -12.150  63.364  1.00 20.81           C  
ANISOU 2179  CA  ASN A 291     2969   1957   2979    247    180    318       C  
ATOM   2180  C   ASN A 291       3.597 -10.748  62.908  1.00 21.00           C  
ANISOU 2180  C   ASN A 291     2952   2089   2937    264    180    272       C  
ATOM   2181  O   ASN A 291       4.683 -10.522  62.392  1.00 16.69           O  
ANISOU 2181  O   ASN A 291     2367   1543   2430    322    186    256       O  
ATOM   2182  CB  ASN A 291       4.082 -13.187  62.706  1.00 25.48           C  
ANISOU 2182  CB  ASN A 291     3553   2434   3695    312    203    297       C  
ATOM   2183  CG  ASN A 291       3.864 -14.562  63.303  1.00 36.88           C  
ANISOU 2183  CG  ASN A 291     5034   3749   5228    303    193    365       C  
ATOM   2184  OD1 ASN A 291       3.709 -14.692  64.512  1.00 35.05           O  
ANISOU 2184  OD1 ASN A 291     4820   3526   4972    274    147    479       O  
ATOM   2185  ND2 ASN A 291       3.816 -15.582  62.463  1.00 42.79           N  
ANISOU 2185  ND2 ASN A 291     5803   4379   6076    318    240    296       N  
ATOM   2186  N   GLY A 292       2.692  -9.797  63.128  1.00 21.92           N  
ANISOU 2186  N   GLY A 292     3073   2290   2966    213    180    255       N  
ATOM   2187  CA  GLY A 292       2.954  -8.418  62.781  1.00 19.27           C  
ANISOU 2187  CA  GLY A 292     2701   2042   2577    223    177    222       C  
ATOM   2188  C   GLY A 292       2.225  -7.893  61.556  1.00 12.72           C  
ANISOU 2188  C   GLY A 292     1866   1246   1722    204    205    142       C  
ATOM   2189  O   GLY A 292       2.252  -6.677  61.298  1.00 15.47           O  
ANISOU 2189  O   GLY A 292     2187   1662   2031    205    200    127       O  
ATOM   2190  N   TYR A 293       1.587  -8.802  60.810  1.00 20.20           N  
ANISOU 2190  N   TYR A 293     2839   2142   2695    182    225     97       N  
ATOM   2191  CA  TYR A 293       0.921  -8.484  59.541  1.00 24.41           C  
ANISOU 2191  CA  TYR A 293     3373   2707   3195    155    234     25       C  
ATOM   2192  C   TYR A 293      -0.581  -8.614  59.654  1.00 13.03           C  
ANISOU 2192  C   TYR A 293     1934   1273   1745     88    222     17       C  
ATOM   2193  O   TYR A 293      -1.067  -9.282  60.554  1.00 17.08           O  
ANISOU 2193  O   TYR A 293     2458   1746   2286     60    226     54       O  
ATOM   2194  CB  TYR A 293       1.433  -9.406  58.429  1.00 22.75           C  
ANISOU 2194  CB  TYR A 293     3193   2437   3012    172    266    -41       C  
ATOM   2195  CG  TYR A 293       2.896  -9.173  58.135  1.00 15.65           C  
ANISOU 2195  CG  TYR A 293     2273   1540   2134    240    296    -42       C  
ATOM   2196  CD1 TYR A 293       3.884  -9.666  58.984  1.00 20.73           C  
ANISOU 2196  CD1 TYR A 293     2895   2129   2853    293    295     14       C  
ATOM   2197  CD2 TYR A 293       3.286  -8.420  57.030  1.00 17.44           C  
ANISOU 2197  CD2 TYR A 293     2491   1827   2307    247    320    -85       C  
ATOM   2198  CE1 TYR A 293       5.234  -9.432  58.721  1.00 17.99           C  
ANISOU 2198  CE1 TYR A 293     2504   1784   2546    356    321     18       C  
ATOM   2199  CE2 TYR A 293       4.617  -8.171  56.769  1.00 15.62           C  
ANISOU 2199  CE2 TYR A 293     2228   1602   2104    303    359    -82       C  
ATOM   2200  CZ  TYR A 293       5.585  -8.667  57.613  1.00 24.12           C  
ANISOU 2200  CZ  TYR A 293     3269   2623   3274    359    361    -34       C  
ATOM   2201  OH  TYR A 293       6.916  -8.400  57.336  1.00 24.55           O  
ANISOU 2201  OH  TYR A 293     3268   2684   3374    414    399    -28       O  
ATOM   2202  N   ILE A 294      -1.295  -7.965  58.747  1.00 15.24           N  
ANISOU 2202  N   ILE A 294     2195   1606   1988     59    204    -21       N  
ATOM   2203  CA  ILE A 294      -2.738  -8.165  58.609  1.00 16.32           C  
ANISOU 2203  CA  ILE A 294     2316   1749   2137     -7    183    -35       C  
ATOM   2204  C   ILE A 294      -3.073  -8.280  57.118  1.00 16.03           C  
ANISOU 2204  C   ILE A 294     2295   1730   2066    -39    153    -98       C  
ATOM   2205  O   ILE A 294      -2.449  -7.643  56.270  1.00 21.74           O  
ANISOU 2205  O   ILE A 294     3027   2497   2735    -14    148   -115       O  
ATOM   2206  CB  ILE A 294      -3.542  -7.022  59.281  1.00 15.25           C  
ANISOU 2206  CB  ILE A 294     2120   1674   2000    -16    177      4       C  
ATOM   2207  CG1 ILE A 294      -5.066  -7.184  59.116  1.00 19.62           C  
ANISOU 2207  CG1 ILE A 294     2629   2236   2591    -80    157     -4       C  
ATOM   2208  CG2 ILE A 294      -3.118  -5.636  58.743  1.00 12.28           C  
ANISOU 2208  CG2 ILE A 294     1717   1360   1590     22    158      8       C  
ATOM   2209  CD1 ILE A 294      -5.826  -6.234  60.047  1.00 14.98           C  
ANISOU 2209  CD1 ILE A 294     1975   1687   2030    -80    181     30       C  
ATOM   2210  N   ARG A 295      -3.995  -9.172  56.795  1.00 20.14           N  
ANISOU 2210  N   ARG A 295     2827   2214   2610   -105    133   -134       N  
ATOM   2211  CA  ARG A 295      -4.499  -9.288  55.437  1.00 20.96           C  
ANISOU 2211  CA  ARG A 295     2951   2346   2667   -158     85   -196       C  
ATOM   2212  C   ARG A 295      -5.841  -8.591  55.397  1.00 23.99           C  
ANISOU 2212  C   ARG A 295     3259   2790   3066   -206     23   -162       C  
ATOM   2213  O   ARG A 295      -6.790  -8.995  56.075  1.00 20.92           O  
ANISOU 2213  O   ARG A 295     2827   2375   2748   -248     21   -142       O  
ATOM   2214  CB  ARG A 295      -4.601 -10.753  55.009  1.00 19.08           C  
ANISOU 2214  CB  ARG A 295     2776   2020   2453   -207     94   -272       C  
ATOM   2215  CG  ARG A 295      -3.200 -11.368  54.750  1.00 18.80           C  
ANISOU 2215  CG  ARG A 295     2808   1922   2414   -147    161   -319       C  
ATOM   2216  CD  ARG A 295      -3.264 -12.854  54.452  1.00 19.90           C  
ANISOU 2216  CD  ARG A 295     3011   1946   2605   -187    184   -400       C  
ATOM   2217  NE  ARG A 295      -3.768 -13.565  55.622  1.00 26.03           N  
ANISOU 2217  NE  ARG A 295     3765   2641   3483   -205    189   -341       N  
ATOM   2218  CZ  ARG A 295      -4.568 -14.623  55.586  1.00 23.88           C  
ANISOU 2218  CZ  ARG A 295     3515   2285   3272   -282    175   -378       C  
ATOM   2219  NH1 ARG A 295      -4.959 -15.133  54.422  1.00 29.89           N  
ANISOU 2219  NH1 ARG A 295     4325   3031   4001   -352    149   -488       N  
ATOM   2220  NH2 ARG A 295      -4.980 -15.173  56.728  1.00 22.10           N  
ANISOU 2220  NH2 ARG A 295     3268   1994   3134   -300    188   -304       N  
ATOM   2221  N   ILE A 296      -5.890  -7.504  54.637  1.00 24.62           N  
ANISOU 2221  N   ILE A 296     3316   2948   3092   -196    -24   -144       N  
ATOM   2222  CA  ILE A 296      -7.084  -6.692  54.551  1.00 17.71           C  
ANISOU 2222  CA  ILE A 296     2352   2127   2251   -225    -89    -99       C  
ATOM   2223  C   ILE A 296      -7.837  -7.014  53.286  1.00 23.50           C  
ANISOU 2223  C   ILE A 296     3095   2894   2941   -304   -183   -132       C  
ATOM   2224  O   ILE A 296      -7.260  -7.048  52.201  1.00 22.60           O  
ANISOU 2224  O   ILE A 296     3055   2811   2722   -317   -207   -170       O  
ATOM   2225  CB  ILE A 296      -6.750  -5.207  54.609  1.00 20.34           C  
ANISOU 2225  CB  ILE A 296     2643   2511   2574   -163    -93    -38       C  
ATOM   2226  CG1 ILE A 296      -6.210  -4.888  56.014  1.00 25.42           C  
ANISOU 2226  CG1 ILE A 296     3271   3123   3265   -103    -10    -13       C  
ATOM   2227  CG2 ILE A 296      -7.994  -4.389  54.342  1.00 15.47           C  
ANISOU 2227  CG2 ILE A 296     1928   1938   2013   -186   -169     11       C  
ATOM   2228  CD1 ILE A 296      -5.639  -3.547  56.134  1.00 36.17           C  
ANISOU 2228  CD1 ILE A 296     4610   4515   4618    -45     -2     28       C  
ATOM   2229  N   LYS A 297      -9.130  -7.287  53.454  1.00 25.29           N  
ANISOU 2229  N   LYS A 297     3245   3118   3245   -366   -235   -121       N  
ATOM   2230  CA  LYS A 297     -10.028  -7.583  52.353  1.00 25.03           C  
ANISOU 2230  CA  LYS A 297     3202   3124   3185   -457   -349   -144       C  
ATOM   2231  C   LYS A 297      -9.901  -6.590  51.209  1.00 21.50           C  
ANISOU 2231  C   LYS A 297     2764   2763   2640   -454   -435   -109       C  
ATOM   2232  O   LYS A 297      -9.813  -5.379  51.427  1.00 21.39           O  
ANISOU 2232  O   LYS A 297     2692   2784   2652   -389   -437    -31       O  
ATOM   2233  CB  LYS A 297     -11.479  -7.597  52.862  1.00 24.38           C  
ANISOU 2233  CB  LYS A 297     2988   3040   3235   -506   -393   -103       C  
ATOM   2234  CG  LYS A 297     -12.528  -8.020  51.840  1.00 29.83           C  
ANISOU 2234  CG  LYS A 297     3647   3766   3921   -616   -528   -124       C  
ATOM   2235  CD  LYS A 297     -12.339  -9.451  51.399  1.00 35.06           C  
ANISOU 2235  CD  LYS A 297     4418   4372   4533   -699   -528   -230       C  
ATOM   2236  CE  LYS A 297     -13.493  -9.902  50.500  1.00 41.97           C  
ANISOU 2236  CE  LYS A 297     5253   5279   5413   -827   -672   -256       C  
ATOM   2237  NZ  LYS A 297     -14.647 -10.410  51.279  1.00 46.79           N  
ANISOU 2237  NZ  LYS A 297     5741   5846   6190   -884   -674   -234       N  
ATOM   2238  N   ARG A 298      -9.893  -7.095  49.980  1.00 24.55           N  
ANISOU 2238  N   ARG A 298     3233   3185   2911   -530   -508   -166       N  
ATOM   2239  CA  ARG A 298      -9.988  -6.200  48.841  1.00 25.82           C  
ANISOU 2239  CA  ARG A 298     3402   3441   2968   -551   -612   -115       C  
ATOM   2240  C   ARG A 298     -11.107  -6.657  47.933  1.00 34.53           C  
ANISOU 2240  C   ARG A 298     4490   4590   4038   -670   -761   -133       C  
ATOM   2241  O   ARG A 298     -11.755  -7.673  48.198  1.00 35.03           O  
ANISOU 2241  O   ARG A 298     4536   4604   4169   -737   -772   -194       O  
ATOM   2242  CB  ARG A 298      -8.660  -6.122  48.077  1.00 22.76           C  
ANISOU 2242  CB  ARG A 298     3148   3081   2419   -529   -553   -157       C  
ATOM   2243  CG  ARG A 298      -8.344  -7.293  47.190  1.00 28.77           C  
ANISOU 2243  CG  ARG A 298     4040   3836   3055   -609   -545   -286       C  
ATOM   2244  CD  ARG A 298      -7.146  -6.961  46.307  1.00 30.92           C  
ANISOU 2244  CD  ARG A 298     4425   4160   3163   -590   -487   -312       C  
ATOM   2245  NE  ARG A 298      -6.711  -8.095  45.485  1.00 32.69           N  
ANISOU 2245  NE  ARG A 298     4786   4369   3267   -657   -444   -458       N  
ATOM   2246  CZ  ARG A 298      -7.154  -8.360  44.257  1.00 34.55           C  
ANISOU 2246  CZ  ARG A 298     5104   4678   3346   -770   -538   -512       C  
ATOM   2247  NH1 ARG A 298      -8.081  -7.595  43.692  1.00 35.22           N  
ANISOU 2247  NH1 ARG A 298     5142   4860   3382   -830   -699   -414       N  
ATOM   2248  NH2 ARG A 298      -6.687  -9.409  43.598  1.00 34.06           N  
ANISOU 2248  NH2 ARG A 298     5173   4588   3182   -826   -474   -668       N  
ATOM   2249  N   GLY A 299     -11.345  -5.897  46.870  1.00 31.40           N  
ANISOU 2249  N   GLY A 299     4099   4288   3542   -705   -884    -70       N  
ATOM   2250  CA  GLY A 299     -12.300  -6.307  45.860  1.00 38.45           C  
ANISOU 2250  CA  GLY A 299     4996   5243   4370   -832  -1049    -85       C  
ATOM   2251  C   GLY A 299     -13.749  -6.045  46.209  1.00 45.12           C  
ANISOU 2251  C   GLY A 299     5662   6095   5387   -861  -1168     -2       C  
ATOM   2252  O   GLY A 299     -14.650  -6.628  45.606  1.00 55.99           O  
ANISOU 2252  O   GLY A 299     7020   7504   6752   -977  -1303    -28       O  
ATOM   2253  N   THR A 300     -13.990  -5.165  47.174  1.00 45.57           N  
ANISOU 2253  N   THR A 300     5585   6122   5610   -761  -1119     93       N  
ATOM   2254  CA  THR A 300     -15.362  -4.875  47.578  1.00 48.12           C  
ANISOU 2254  CA  THR A 300     5716   6443   6123   -775  -1207    171       C  
ATOM   2255  C   THR A 300     -16.005  -3.814  46.682  1.00 50.78           C  
ANISOU 2255  C   THR A 300     5971   6864   6459   -786  -1388    302       C  
ATOM   2256  O   THR A 300     -17.153  -3.427  46.898  1.00 51.07           O  
ANISOU 2256  O   THR A 300     5828   6904   6671   -788  -1476    384       O  
ATOM   2257  CB  THR A 300     -15.437  -4.407  49.043  1.00 44.22           C  
ANISOU 2257  CB  THR A 300     5109   5876   5818   -665  -1062    203       C  
ATOM   2258  OG1 THR A 300     -14.750  -3.159  49.184  1.00 42.90           O  
ANISOU 2258  OG1 THR A 300     4945   5715   5642   -557  -1015    277       O  
ATOM   2259  CG2 THR A 300     -14.812  -5.440  49.974  1.00 41.75           C  
ANISOU 2259  CG2 THR A 300     4877   5483   5503   -657   -898     98       C  
ATOM   2260  N   GLY A 301     -15.269  -3.347  45.675  1.00 55.25           N  
ANISOU 2260  N   GLY A 301     6660   7497   6835   -794  -1441    331       N  
ATOM   2261  CA  GLY A 301     -15.769  -2.315  44.781  1.00 63.50           C  
ANISOU 2261  CA  GLY A 301     7647   8621   7860   -807  -1619    477       C  
ATOM   2262  C   GLY A 301     -15.678  -0.928  45.390  1.00 65.52           C  
ANISOU 2262  C   GLY A 301     7791   8836   8267   -672  -1570    603       C  
ATOM   2263  O   GLY A 301     -15.582   0.069  44.672  1.00 71.27           O  
ANISOU 2263  O   GLY A 301     8521   9611   8947   -654  -1669    728       O  
ATOM   2264  N   ASN A 302     -15.709  -0.881  46.720  1.00 54.23           N  
ANISOU 2264  N   ASN A 302     6273   7315   7016   -584  -1417    568       N  
ATOM   2265  CA  ASN A 302     -15.603   0.350  47.501  1.00 47.69           C  
ANISOU 2265  CA  ASN A 302     5346   6429   6347   -455  -1337    650       C  
ATOM   2266  C   ASN A 302     -14.296   1.103  47.227  1.00 43.12           C  
ANISOU 2266  C   ASN A 302     4896   5851   5635   -397  -1271    676       C  
ATOM   2267  O   ASN A 302     -13.206   0.626  47.565  1.00 34.52           O  
ANISOU 2267  O   ASN A 302     3935   4743   4439   -383  -1132    579       O  
ATOM   2268  CB  ASN A 302     -15.740   0.006  48.991  1.00 52.16           C  
ANISOU 2268  CB  ASN A 302     5839   6908   7070   -397  -1163    570       C  
ATOM   2269  CG  ASN A 302     -15.415   1.172  49.914  1.00 50.65           C  
ANISOU 2269  CG  ASN A 302     5586   6649   7010   -270  -1044    611       C  
ATOM   2270  OD1 ASN A 302     -15.353   2.333  49.495  1.00 55.16           O  
ANISOU 2270  OD1 ASN A 302     6121   7219   7617   -217  -1106    717       O  
ATOM   2271  ND2 ASN A 302     -15.226   0.861  51.195  1.00 37.43           N  
ANISOU 2271  ND2 ASN A 302     3902   4913   5406   -227   -875    529       N  
ATOM   2272  N   SER A 303     -14.427   2.296  46.648  1.00 30.91           N  
ANISOU 2272  N   SER A 303     3303   4323   4120   -363  -1372    819       N  
ATOM   2273  CA  SER A 303     -13.282   3.058  46.160  1.00 31.99           C  
ANISOU 2273  CA  SER A 303     3558   4472   4125   -331  -1338    869       C  
ATOM   2274  C   SER A 303     -12.352   3.526  47.282  1.00 25.18           C  
ANISOU 2274  C   SER A 303     2711   3522   3336   -228  -1145    819       C  
ATOM   2275  O   SER A 303     -11.159   3.706  47.059  1.00 29.40           O  
ANISOU 2275  O   SER A 303     3368   4065   3738   -219  -1069    803       O  
ATOM   2276  CB  SER A 303     -13.765   4.249  45.324  1.00 41.36           C  
ANISOU 2276  CB  SER A 303     4676   5684   5354   -321  -1503   1055       C  
ATOM   2277  OG  SER A 303     -14.465   5.198  46.113  1.00 55.19           O  
ANISOU 2277  OG  SER A 303     6249   7344   7377   -221  -1494   1132       O  
ATOM   2278  N   TYR A 304     -12.871   3.692  48.495  1.00 24.45           N  
ANISOU 2278  N   TYR A 304     2495   3350   3446   -160  -1060    788       N  
ATOM   2279  CA  TYR A 304     -12.015   4.032  49.637  1.00 26.85           C  
ANISOU 2279  CA  TYR A 304     2824   3578   3801    -78   -882    723       C  
ATOM   2280  C   TYR A 304     -11.058   2.914  50.019  1.00 26.34           C  
ANISOU 2280  C   TYR A 304     2890   3523   3595   -107   -765    592       C  
ATOM   2281  O   TYR A 304     -10.014   3.154  50.615  1.00 27.04           O  
ANISOU 2281  O   TYR A 304     3041   3575   3658    -59   -647    552       O  
ATOM   2282  CB  TYR A 304     -12.861   4.376  50.860  1.00 33.60           C  
ANISOU 2282  CB  TYR A 304     3527   4354   4883    -12   -810    706       C  
ATOM   2283  CG  TYR A 304     -13.596   5.692  50.783  1.00 41.88           C  
ANISOU 2283  CG  TYR A 304     4435   5353   6125     54   -875    824       C  
ATOM   2284  CD1 TYR A 304     -14.953   5.729  50.481  1.00 49.52           C  
ANISOU 2284  CD1 TYR A 304     5248   6330   7238     42   -994    894       C  
ATOM   2285  CD2 TYR A 304     -12.943   6.899  51.037  1.00 36.50           C  
ANISOU 2285  CD2 TYR A 304     3764   4603   5501    130   -819    866       C  
ATOM   2286  CE1 TYR A 304     -15.642   6.922  50.422  1.00 50.15           C  
ANISOU 2286  CE1 TYR A 304     5183   6350   7524    113  -1054   1008       C  
ATOM   2287  CE2 TYR A 304     -13.631   8.105  50.972  1.00 42.05           C  
ANISOU 2287  CE2 TYR A 304     4334   5237   6406    197   -876    975       C  
ATOM   2288  CZ  TYR A 304     -14.982   8.104  50.664  1.00 50.05           C  
ANISOU 2288  CZ  TYR A 304     5189   6257   7569    194   -992   1047       C  
ATOM   2289  OH  TYR A 304     -15.689   9.283  50.599  1.00 58.86           O  
ANISOU 2289  OH  TYR A 304     6186   7293   8884    260  -1025   1138       O  
ATOM   2290  N   GLY A 305     -11.435   1.684  49.697  1.00 21.62           N  
ANISOU 2290  N   GLY A 305     2326   2966   2921   -186   -802    526       N  
ATOM   2291  CA  GLY A 305     -10.796   0.524  50.284  1.00 18.71           C  
ANISOU 2291  CA  GLY A 305     2047   2579   2484   -203   -687    403       C  
ATOM   2292  C   GLY A 305     -11.297   0.280  51.695  1.00 22.08           C  
ANISOU 2292  C   GLY A 305     2386   2941   3061   -166   -588    358       C  
ATOM   2293  O   GLY A 305     -11.784   1.183  52.364  1.00 25.57           O  
ANISOU 2293  O   GLY A 305     2721   3346   3650   -106   -562    403       O  
ATOM   2294  N   VAL A 306     -11.197  -0.962  52.137  1.00 23.02           N  
ANISOU 2294  N   VAL A 306     2557   3044   3147   -206   -527    269       N  
ATOM   2295  CA  VAL A 306     -11.532  -1.327  53.500  1.00 20.73           C  
ANISOU 2295  CA  VAL A 306     2211   2699   2964   -184   -419    228       C  
ATOM   2296  C   VAL A 306     -10.644  -0.541  54.465  1.00 21.39           C  
ANISOU 2296  C   VAL A 306     2317   2745   3064    -99   -305    227       C  
ATOM   2297  O   VAL A 306      -9.427  -0.439  54.262  1.00 21.76           O  
ANISOU 2297  O   VAL A 306     2465   2796   3007    -76   -275    213       O  
ATOM   2298  CB  VAL A 306     -11.376  -2.860  53.687  1.00 23.04           C  
ANISOU 2298  CB  VAL A 306     2583   2974   3200   -247   -380    145       C  
ATOM   2299  CG1 VAL A 306     -11.552  -3.270  55.131  1.00 23.11           C  
ANISOU 2299  CG1 VAL A 306     2559   2929   3291   -230   -260    118       C  
ATOM   2300  CG2 VAL A 306     -12.367  -3.592  52.783  1.00 26.68           C  
ANISOU 2300  CG2 VAL A 306     3013   3464   3660   -344   -500    137       C  
ATOM   2301  N   CYS A 307     -11.259   0.034  55.496  1.00 20.10           N  
ANISOU 2301  N   CYS A 307     2056   2549   3032    -58   -240    236       N  
ATOM   2302  CA  CYS A 307     -10.572   0.927  56.439  1.00 21.08           C  
ANISOU 2302  CA  CYS A 307     2193   2637   3180     13   -141    227       C  
ATOM   2303  C   CYS A 307      -9.931   2.141  55.727  1.00 23.11           C  
ANISOU 2303  C   CYS A 307     2466   2895   3420     58   -191    283       C  
ATOM   2304  O   CYS A 307      -8.983   2.729  56.243  1.00 19.13           O  
ANISOU 2304  O   CYS A 307     2011   2365   2892    100   -126    268       O  
ATOM   2305  CB  CYS A 307      -9.502   0.164  57.233  1.00 21.87           C  
ANISOU 2305  CB  CYS A 307     2405   2723   3182     11    -50    166       C  
ATOM   2306  SG  CYS A 307     -10.099  -1.366  58.060  1.00 28.07           S  
ANISOU 2306  SG  CYS A 307     3195   3494   3974    -51      9    120       S  
ATOM   2307  N   GLY A 308     -10.453   2.518  54.557  1.00 19.92           N  
ANISOU 2307  N   GLY A 308     2019   2520   3029     42   -312    355       N  
ATOM   2308  CA  GLY A 308      -9.904   3.639  53.789  1.00 19.19           C  
ANISOU 2308  CA  GLY A 308     1945   2429   2918     73   -367    430       C  
ATOM   2309  C   GLY A 308      -8.491   3.415  53.244  1.00 21.11           C  
ANISOU 2309  C   GLY A 308     2325   2702   2994     58   -351    414       C  
ATOM   2310  O   GLY A 308      -7.738   4.359  53.035  1.00 22.65           O  
ANISOU 2310  O   GLY A 308     2545   2882   3178     91   -344    458       O  
ATOM   2311  N   LEU A 309      -8.156   2.156  52.979  1.00 21.02           N  
ANISOU 2311  N   LEU A 309     2395   2727   2865      7   -343    352       N  
ATOM   2312  CA  LEU A 309      -6.812   1.738  52.571  1.00 18.09           C  
ANISOU 2312  CA  LEU A 309     2143   2377   2353     -3   -302    317       C  
ATOM   2313  C   LEU A 309      -6.315   2.417  51.292  1.00 18.37           C  
ANISOU 2313  C   LEU A 309     2225   2460   2296    -19   -365    388       C  
ATOM   2314  O   LEU A 309      -5.114   2.485  51.067  1.00 22.07           O  
ANISOU 2314  O   LEU A 309     2767   2937   2680    -11   -309    376       O  
ATOM   2315  CB  LEU A 309      -6.792   0.219  52.379  1.00 14.96           C  
ANISOU 2315  CB  LEU A 309     1812   1998   1875    -58   -292    237       C  
ATOM   2316  CG  LEU A 309      -5.488  -0.509  52.095  1.00 20.29           C  
ANISOU 2316  CG  LEU A 309     2598   2678   2433    -62   -227    177       C  
ATOM   2317  CD1 LEU A 309      -4.519  -0.200  53.213  1.00 17.04           C  
ANISOU 2317  CD1 LEU A 309     2187   2222   2065      0   -130    165       C  
ATOM   2318  CD2 LEU A 309      -5.760  -2.018  51.967  1.00 17.16           C  
ANISOU 2318  CD2 LEU A 309     2250   2273   1999   -115   -223     95       C  
ATOM   2319  N   TYR A 310      -7.223   2.924  50.460  1.00 21.37           N  
ANISOU 2319  N   TYR A 310     2556   2871   2693    -45   -482    471       N  
ATOM   2320  CA  TYR A 310      -6.807   3.472  49.155  1.00 24.03           C  
ANISOU 2320  CA  TYR A 310     2953   3266   2912    -77   -552    552       C  
ATOM   2321  C   TYR A 310      -6.675   4.991  49.190  1.00 22.34           C  
ANISOU 2321  C   TYR A 310     2685   3012   2792    -25   -568    664       C  
ATOM   2322  O   TYR A 310      -6.532   5.629  48.149  1.00 22.81           O  
ANISOU 2322  O   TYR A 310     2775   3111   2781    -52   -642    765       O  
ATOM   2323  CB  TYR A 310      -7.790   3.051  48.037  1.00 23.90           C  
ANISOU 2323  CB  TYR A 310     2937   3321   2822   -156   -695    591       C  
ATOM   2324  CG  TYR A 310      -8.000   1.552  47.959  1.00 26.90           C  
ANISOU 2324  CG  TYR A 310     3372   3727   3123   -219   -686    473       C  
ATOM   2325  CD1 TYR A 310      -7.056   0.677  48.482  1.00 22.37           C  
ANISOU 2325  CD1 TYR A 310     2874   3125   2501   -206   -557    360       C  
ATOM   2326  CD2 TYR A 310      -9.136   1.008  47.366  1.00 22.14           C  
ANISOU 2326  CD2 TYR A 310     2738   3167   2506   -292   -813    479       C  
ATOM   2327  CE1 TYR A 310      -7.236  -0.674  48.428  1.00 24.99           C  
ANISOU 2327  CE1 TYR A 310     3255   3458   2782   -259   -545    256       C  
ATOM   2328  CE2 TYR A 310      -9.324  -0.366  47.310  1.00 23.84           C  
ANISOU 2328  CE2 TYR A 310     3007   3390   2662   -357   -802    364       C  
ATOM   2329  CZ  TYR A 310      -8.361  -1.198  47.852  1.00 27.99           C  
ANISOU 2329  CZ  TYR A 310     3613   3874   3149   -337   -662    252       C  
ATOM   2330  OH  TYR A 310      -8.497  -2.565  47.829  1.00 25.43           O  
ANISOU 2330  OH  TYR A 310     3343   3534   2785   -395   -642    139       O  
ATOM   2331  N   THR A 311      -6.702   5.563  50.389  1.00 18.79           N  
ANISOU 2331  N   THR A 311     2164   2480   2497     43   -496    644       N  
ATOM   2332  CA  THR A 311      -6.780   7.014  50.551  1.00 21.24           C  
ANISOU 2332  CA  THR A 311     2407   2724   2939     97   -510    736       C  
ATOM   2333  C   THR A 311      -5.491   7.774  50.174  1.00 23.07           C  
ANISOU 2333  C   THR A 311     2710   2948   3106    100   -470    782       C  
ATOM   2334  O   THR A 311      -5.553   8.865  49.596  1.00 21.37           O  
ANISOU 2334  O   THR A 311     2473   2708   2939    108   -530    902       O  
ATOM   2335  CB  THR A 311      -7.155   7.410  52.022  1.00 21.36           C  
ANISOU 2335  CB  THR A 311     2336   2647   3131    163   -425    674       C  
ATOM   2336  OG1 THR A 311      -8.440   6.863  52.373  1.00 20.45           O  
ANISOU 2336  OG1 THR A 311     2134   2534   3104    161   -453    648       O  
ATOM   2337  CG2 THR A 311      -7.213   8.957  52.162  1.00 23.77           C  
ANISOU 2337  CG2 THR A 311     2578   2863   3590    220   -433    756       C  
ATOM   2338  N   SER A 312      -4.328   7.230  50.504  1.00 23.21           N  
ANISOU 2338  N   SER A 312     2805   2982   3034     92   -371    699       N  
ATOM   2339  CA  SER A 312      -3.103   8.010  50.325  1.00 22.73           C  
ANISOU 2339  CA  SER A 312     2786   2904   2948     97   -320    738       C  
ATOM   2340  C   SER A 312      -1.864   7.121  50.323  1.00 23.94           C  
ANISOU 2340  C   SER A 312     3019   3102   2975     75   -229    655       C  
ATOM   2341  O   SER A 312      -1.374   6.729  51.379  1.00 19.46           O  
ANISOU 2341  O   SER A 312     2446   2502   2447    102   -154    566       O  
ATOM   2342  CB  SER A 312      -2.994   9.067  51.426  1.00 23.48           C  
ANISOU 2342  CB  SER A 312     2816   2892   3211    153   -273    733       C  
ATOM   2343  OG  SER A 312      -1.864   9.893  51.232  1.00 30.31           O  
ANISOU 2343  OG  SER A 312     3712   3733   4072    148   -236    778       O  
ATOM   2344  N   SER A 313      -1.359   6.814  49.134  1.00 21.01           N  
ANISOU 2344  N   SER A 313     2723   2808   2454     24   -236    686       N  
ATOM   2345  CA  SER A 313      -0.320   5.793  49.008  1.00 20.36           C  
ANISOU 2345  CA  SER A 313     2707   2768   2259      7   -145    596       C  
ATOM   2346  C   SER A 313       0.858   6.312  48.203  1.00 23.16           C  
ANISOU 2346  C   SER A 313     3109   3158   2532    -20    -90    650       C  
ATOM   2347  O   SER A 313       0.673   6.855  47.120  1.00 23.18           O  
ANISOU 2347  O   SER A 313     3145   3208   2454    -64   -142    749       O  
ATOM   2348  CB  SER A 313      -0.888   4.523  48.345  1.00 23.69           C  
ANISOU 2348  CB  SER A 313     3186   3255   2561    -38   -176    533       C  
ATOM   2349  OG  SER A 313      -2.134   4.123  48.909  1.00 18.28           O  
ANISOU 2349  OG  SER A 313     2449   2544   1954    -30   -241    506       O  
ATOM   2350  N   PHE A 314       2.066   6.117  48.727  1.00 21.09           N  
ANISOU 2350  N   PHE A 314     2844   2877   2291      2     13    594       N  
ATOM   2351  CA  PHE A 314       3.276   6.684  48.144  1.00 22.48           C  
ANISOU 2351  CA  PHE A 314     3039   3077   2426    -21     84    644       C  
ATOM   2352  C   PHE A 314       4.373   5.629  48.146  1.00 21.86           C  
ANISOU 2352  C   PHE A 314     2985   3028   2293    -16    196    545       C  
ATOM   2353  O   PHE A 314       4.375   4.737  48.994  1.00 18.08           O  
ANISOU 2353  O   PHE A 314     2489   2518   1862     22    215    451       O  
ATOM   2354  CB  PHE A 314       3.773   7.905  48.923  1.00 25.41           C  
ANISOU 2354  CB  PHE A 314     3343   3370   2942      5     92    698       C  
ATOM   2355  CG  PHE A 314       2.883   9.101  48.832  1.00 21.95           C  
ANISOU 2355  CG  PHE A 314     2874   2881   2583      5      1    805       C  
ATOM   2356  CD1 PHE A 314       1.795   9.238  49.683  1.00 20.80           C  
ANISOU 2356  CD1 PHE A 314     2679   2675   2549     47    -62    781       C  
ATOM   2357  CD2 PHE A 314       3.143  10.103  47.905  1.00 23.97           C  
ANISOU 2357  CD2 PHE A 314     3148   3146   2815    -35    -16    936       C  
ATOM   2358  CE1 PHE A 314       0.970  10.363  49.597  1.00 20.77           C  
ANISOU 2358  CE1 PHE A 314     2634   2610   2649     59   -139    879       C  
ATOM   2359  CE2 PHE A 314       2.324  11.222  47.817  1.00 25.80           C  
ANISOU 2359  CE2 PHE A 314     3345   3313   3144    -26   -106   1048       C  
ATOM   2360  CZ  PHE A 314       1.240  11.342  48.671  1.00 25.56           C  
ANISOU 2360  CZ  PHE A 314     3256   3215   3243     26   -166   1014       C  
ATOM   2361  N   TYR A 315       5.296   5.732  47.196  1.00 19.94           N  
ANISOU 2361  N   TYR A 315     2778   2840   1956    -53    275    572       N  
ATOM   2362  CA  TYR A 315       6.438   4.829  47.192  1.00 21.20           C  
ANISOU 2362  CA  TYR A 315     2941   3017   2097    -38    398    481       C  
ATOM   2363  C   TYR A 315       7.695   5.538  46.715  1.00 17.66           C  
ANISOU 2363  C   TYR A 315     2470   2592   1648    -61    494    540       C  
ATOM   2364  O   TYR A 315       7.633   6.491  45.930  1.00 25.11           O  
ANISOU 2364  O   TYR A 315     3439   3567   2533   -112    477    649       O  
ATOM   2365  CB  TYR A 315       6.156   3.590  46.332  1.00 18.69           C  
ANISOU 2365  CB  TYR A 315     2710   2758   1633    -64    432    392       C  
ATOM   2366  CG  TYR A 315       5.853   3.870  44.889  1.00 23.13           C  
ANISOU 2366  CG  TYR A 315     3363   3412   2015   -142    422    447       C  
ATOM   2367  CD1 TYR A 315       6.879   3.964  43.948  1.00 22.51           C  
ANISOU 2367  CD1 TYR A 315     3323   3397   1831   -182    545    457       C  
ATOM   2368  CD2 TYR A 315       4.542   4.029  44.457  1.00 26.47           C  
ANISOU 2368  CD2 TYR A 315     3829   3863   2366   -182    289    495       C  
ATOM   2369  CE1 TYR A 315       6.602   4.212  42.610  1.00 31.20           C  
ANISOU 2369  CE1 TYR A 315     4524   4594   2736   -266    537    513       C  
ATOM   2370  CE2 TYR A 315       4.256   4.272  43.126  1.00 30.21           C  
ANISOU 2370  CE2 TYR A 315     4393   4429   2655   -263    260    558       C  
ATOM   2371  CZ  TYR A 315       5.290   4.360  42.207  1.00 30.07           C  
ANISOU 2371  CZ  TYR A 315     4433   4481   2511   -308    385    566       C  
ATOM   2372  OH  TYR A 315       5.013   4.609  40.889  1.00 33.81           O  
ANISOU 2372  OH  TYR A 315     5011   5059   2777   -400    358    634       O  
ATOM   2373  N   PRO A 316       8.845   5.076  47.208  1.00 20.00           N  
ANISOU 2373  N   PRO A 316     2710   2868   2021    -26    591    479       N  
ATOM   2374  CA  PRO A 316      10.130   5.672  46.837  1.00 20.28           C  
ANISOU 2374  CA  PRO A 316     2700   2923   2082    -48    695    528       C  
ATOM   2375  C   PRO A 316      10.571   5.229  45.446  1.00 27.18           C  
ANISOU 2375  C   PRO A 316     3646   3888   2795    -95    815    511       C  
ATOM   2376  O   PRO A 316      10.267   4.119  45.030  1.00 25.64           O  
ANISOU 2376  O   PRO A 316     3515   3722   2504    -90    848    412       O  
ATOM   2377  CB  PRO A 316      11.083   5.137  47.904  1.00 21.72           C  
ANISOU 2377  CB  PRO A 316     2787   3054   2412     12    740    459       C  
ATOM   2378  CG  PRO A 316      10.491   3.761  48.273  1.00 19.28           C  
ANISOU 2378  CG  PRO A 316     2514   2728   2082     59    720    349       C  
ATOM   2379  CD  PRO A 316       8.986   3.984  48.191  1.00 18.46           C  
ANISOU 2379  CD  PRO A 316     2479   2626   1908     37    600    373       C  
ATOM   2380  N   VAL A 317      11.286   6.105  44.748  1.00 26.19           N  
ANISOU 2380  N   VAL A 317     3511   3801   2639   -149    886    603       N  
ATOM   2381  CA  VAL A 317      11.876   5.788  43.462  1.00 32.66           C  
ANISOU 2381  CA  VAL A 317     4394   4714   3302   -202   1029    590       C  
ATOM   2382  C   VAL A 317      13.387   5.670  43.632  1.00 33.90           C  
ANISOU 2382  C   VAL A 317     4447   4864   3570   -180   1187    560       C  
ATOM   2383  O   VAL A 317      14.008   6.513  44.283  1.00 29.43           O  
ANISOU 2383  O   VAL A 317     3776   4248   3157   -175   1172    632       O  
ATOM   2384  CB  VAL A 317      11.551   6.867  42.408  1.00 28.30           C  
ANISOU 2384  CB  VAL A 317     3916   4225   2611   -293   1003    737       C  
ATOM   2385  CG1 VAL A 317      12.310   6.600  41.100  1.00 29.82           C  
ANISOU 2385  CG1 VAL A 317     4178   4526   2627   -361   1177    726       C  
ATOM   2386  CG2 VAL A 317      10.054   6.919  42.159  1.00 26.47           C  
ANISOU 2386  CG2 VAL A 317     3775   4006   2276   -314    839    773       C  
ATOM   2387  N   LYS A 318      13.965   4.620  43.059  1.00 32.00           N  
ANISOU 2387  N   LYS A 318     4228   4667   3266   -167   1337    448       N  
ATOM   2388  CA  LYS A 318      15.410   4.400  43.118  1.00 31.98           C  
ANISOU 2388  CA  LYS A 318     4110   4660   3380   -140   1504    413       C  
ATOM   2389  C   LYS A 318      15.908   3.890  41.771  1.00 38.98           C  
ANISOU 2389  C   LYS A 318     5072   5641   4099   -186   1701    352       C  
ATOM   2390  O   LYS A 318      15.581   2.774  41.361  1.00 42.37           O  
ANISOU 2390  O   LYS A 318     5581   6086   4433   -166   1740    220       O  
ATOM   2391  CB  LYS A 318      15.758   3.410  44.232  1.00 27.88           C  
ANISOU 2391  CB  LYS A 318     3495   4057   3042    -37   1492    308       C  
ATOM   2392  CG  LYS A 318      17.248   3.081  44.328  1.00 32.16           C  
ANISOU 2392  CG  LYS A 318     3896   4587   3734      5   1655    273       C  
ATOM   2393  CD  LYS A 318      18.065   4.280  44.783  1.00 35.62           C  
ANISOU 2393  CD  LYS A 318     4206   5014   4315    -25   1639    394       C  
ATOM   2394  CE  LYS A 318      19.550   3.926  44.846  1.00 44.37           C  
ANISOU 2394  CE  LYS A 318     5155   6116   5589     13   1795    362       C  
ATOM   2395  NZ  LYS A 318      20.381   5.095  45.222  1.00 42.27           N  
ANISOU 2395  NZ  LYS A 318     4760   5840   5462    -32   1773    477       N  
ATOM   2396  N   ASN A 319      16.683   4.717  41.077  1.00 39.87           N  
ANISOU 2396  N   ASN A 319     5150   5813   4183   -253   1781    437       N  
ATOM   2397  CA  ASN A 319      17.184   4.366  39.754  1.00 42.39           C  
ANISOU 2397  CA  ASN A 319     5519   6239   4349   -300   1901    383       C  
ATOM   2398  C   ASN A 319      18.243   3.268  39.803  1.00 50.22           C  
ANISOU 2398  C   ASN A 319     6416   7209   5458   -223   2039    235       C  
ATOM   2399  O   ASN A 319      18.576   2.652  38.785  1.00 51.74           O  
ANISOU 2399  O   ASN A 319     6656   7468   5533   -233   2149    150       O  
ATOM   2400  CB  ASN A 319      17.758   5.603  39.062  1.00 47.74           C  
ANISOU 2400  CB  ASN A 319     6173   6986   4981   -393   1940    530       C  
ATOM   2401  CG  ASN A 319      16.747   6.718  38.916  1.00 47.02           C  
ANISOU 2401  CG  ASN A 319     6175   6904   4785   -468   1797    693       C  
ATOM   2402  OD1 ASN A 319      15.557   6.475  38.713  1.00 47.47           O  
ANISOU 2402  OD1 ASN A 319     6358   6975   4704   -471   1691    692       O  
ATOM   2403  ND2 ASN A 319      17.219   7.954  39.009  1.00 52.60           N  
ANISOU 2403  ND2 ASN A 319     6820   7591   5574   -532   1786    834       N  
ATOM   2404  OXT ASN A 319      18.805   2.981  40.861  1.00 48.20           O  
ANISOU 2404  OXT ASN A 319     6027   6862   5425   -145   2039    205       O  
TER    2405      ASN A 319                                                      
ATOM   2406  N   SER B   3      30.313   5.735 -11.086  1.00 76.70           N  
ANISOU 2406  N   SER B   3    11461   7858   9824   -831   2018  -1245       N  
ATOM   2407  CA  SER B   3      30.422   5.641  -9.631  1.00 76.17           C  
ANISOU 2407  CA  SER B   3    11395   7971   9576  -1061   2076  -1563       C  
ATOM   2408  C   SER B   3      29.180   4.984  -9.040  1.00 75.84           C  
ANISOU 2408  C   SER B   3    11275   7934   9608   -753   1983  -1395       C  
ATOM   2409  O   SER B   3      29.279   3.971  -8.345  1.00 77.69           O  
ANISOU 2409  O   SER B   3    11329   8550   9641   -755   1711  -1441       O  
ATOM   2410  CB  SER B   3      30.638   7.022  -9.011  1.00 78.44           C  
ANISOU 2410  CB  SER B   3    11988   7916   9898  -1408   2585  -1897       C  
ATOM   2411  OG  SER B   3      31.716   7.706  -9.632  1.00 81.30           O  
ANISOU 2411  OG  SER B   3    12424   8253  10214  -1710   2704  -2021       O  
ATOM   2412  N   ILE B   4      28.017   5.573  -9.311  1.00 69.67           N  
ANISOU 2412  N   ILE B   4    10621   6741   9112   -475   2234  -1176       N  
ATOM   2413  CA  ILE B   4      26.745   4.945  -8.969  1.00 58.40           C  
ANISOU 2413  CA  ILE B   4     9074   5338   7777   -154   2138   -958       C  
ATOM   2414  C   ILE B   4      26.702   3.545  -9.578  1.00 52.93           C  
ANISOU 2414  C   ILE B   4     8111   5017   6984     11   1660   -733       C  
ATOM   2415  O   ILE B   4      26.468   2.557  -8.879  1.00 43.19           O  
ANISOU 2415  O   ILE B   4     6747   4046   5617     36   1454   -759       O  
ATOM   2416  CB  ILE B   4      25.531   5.754  -9.480  1.00 54.71           C  
ANISOU 2416  CB  ILE B   4     8705   4452   7632    190   2447   -653       C  
ATOM   2417  CG1 ILE B   4      25.527   7.180  -8.901  1.00 55.50           C  
ANISOU 2417  CG1 ILE B   4     9128   4098   7861     55   3010   -855       C  
ATOM   2418  CG2 ILE B   4      24.228   5.015  -9.181  1.00 53.81           C  
ANISOU 2418  CG2 ILE B   4     8397   4464   7583    497   2310   -417       C  
ATOM   2419  CD1 ILE B   4      25.508   7.243  -7.393  1.00 53.02           C  
ANISOU 2419  CD1 ILE B   4     8865   3887   7394   -201   3130  -1184       C  
ATOM   2420  N   VAL B   5      26.948   3.478 -10.884  1.00 54.46           N  
ANISOU 2420  N   VAL B   5     8250   5210   7233    106   1524   -523       N  
ATOM   2421  CA  VAL B   5      26.983   2.209 -11.613  1.00 53.56           C  
ANISOU 2421  CA  VAL B   5     7930   5403   7019    216   1128   -344       C  
ATOM   2422  C   VAL B   5      28.399   1.846 -12.068  1.00 49.75           C  
ANISOU 2422  C   VAL B   5     7412   5141   6351     17    949   -475       C  
ATOM   2423  O   VAL B   5      28.659   0.708 -12.440  1.00 45.43           O  
ANISOU 2423  O   VAL B   5     6729   4851   5682     67    666   -402       O  
ATOM   2424  CB  VAL B   5      26.060   2.236 -12.851  1.00 54.47           C  
ANISOU 2424  CB  VAL B   5     7962   5441   7293    484   1077     26       C  
ATOM   2425  CG1 VAL B   5      24.603   2.305 -12.425  1.00 56.68           C  
ANISOU 2425  CG1 VAL B   5     8176   5641   7718    718   1186    207       C  
ATOM   2426  CG2 VAL B   5      26.420   3.400 -13.766  1.00 53.25           C  
ANISOU 2426  CG2 VAL B   5     7942   5030   7261    494   1295    124       C  
ATOM   2427  N   GLY B   6      29.307   2.816 -12.054  1.00 52.01           N  
ANISOU 2427  N   GLY B   6     7827   5318   6616   -217   1150   -672       N  
ATOM   2428  CA  GLY B   6      30.704   2.528 -12.308  1.00 48.00           C  
ANISOU 2428  CA  GLY B   6     7247   5084   5908   -434   1005   -825       C  
ATOM   2429  C   GLY B   6      31.232   3.048 -13.630  1.00 44.72           C  
ANISOU 2429  C   GLY B   6     6883   4547   5563   -460   1044   -718       C  
ATOM   2430  O   GLY B   6      32.386   2.803 -13.978  1.00 46.40           O  
ANISOU 2430  O   GLY B   6     7014   4996   5618   -624    928   -820       O  
ATOM   2431  N   TYR B   7      30.397   3.773 -14.365  1.00 42.93           N  
ANISOU 2431  N   TYR B   7     6773   3979   5560   -281   1220   -488       N  
ATOM   2432  CA  TYR B   7      30.804   4.311 -15.655  1.00 41.67           C  
ANISOU 2432  CA  TYR B   7     6675   3695   5463   -277   1280   -337       C  
ATOM   2433  C   TYR B   7      29.944   5.499 -16.067  1.00 50.66           C  
ANISOU 2433  C   TYR B   7     8001   4397   6852    -99   1626   -113       C  
ATOM   2434  O   TYR B   7      28.804   5.637 -15.624  1.00 51.46           O  
ANISOU 2434  O   TYR B   7     8111   4352   7090    125   1734     26       O  
ATOM   2435  CB  TYR B   7      30.729   3.222 -16.725  1.00 39.13           C  
ANISOU 2435  CB  TYR B   7     6173   3632   5062   -108    933   -107       C  
ATOM   2436  CG  TYR B   7      29.314   2.776 -17.030  1.00 46.83           C  
ANISOU 2436  CG  TYR B   7     7056   4604   6133    190    829    191       C  
ATOM   2437  CD1 TYR B   7      28.661   1.852 -16.215  1.00 51.50           C  
ANISOU 2437  CD1 TYR B   7     7539   5349   6681    263    677    157       C  
ATOM   2438  CD2 TYR B   7      28.627   3.284 -18.128  1.00 49.90           C  
ANISOU 2438  CD2 TYR B   7     7446   4882   6632    387    890    522       C  
ATOM   2439  CE1 TYR B   7      27.367   1.451 -16.489  1.00 47.54           C  
ANISOU 2439  CE1 TYR B   7     6926   4892   6246    481    591    408       C  
ATOM   2440  CE2 TYR B   7      27.335   2.888 -18.409  1.00 47.72           C  
ANISOU 2440  CE2 TYR B   7     7023   4708   6399    629    783    800       C  
ATOM   2441  CZ  TYR B   7      26.713   1.974 -17.589  1.00 42.62           C  
ANISOU 2441  CZ  TYR B   7     6264   4220   5711    653    634    724       C  
ATOM   2442  OH  TYR B   7      25.432   1.584 -17.873  1.00 38.51           O  
ANISOU 2442  OH  TYR B   7     5570   3847   5213    842    535    981       O  
ATOM   2443  N   SER B   8      30.500   6.351 -16.924  1.00 54.48           N  
ANISOU 2443  N   SER B   8     8629   4678   7394   -175   1825    -52       N  
ATOM   2444  CA  SER B   8      29.760   7.470 -17.494  1.00 67.07           C  
ANISOU 2444  CA  SER B   8    10409   5850   9223     57   2183    246       C  
ATOM   2445  C   SER B   8      29.354   7.138 -18.924  1.00 69.41           C  
ANISOU 2445  C   SER B   8    10558   6302   9514    334   1968    671       C  
ATOM   2446  O   SER B   8      29.898   6.208 -19.527  1.00 57.07           O  
ANISOU 2446  O   SER B   8     8822   5095   7768    250   1611    649       O  
ATOM   2447  CB  SER B   8      30.600   8.746 -17.465  1.00 70.77           C  
ANISOU 2447  CB  SER B   8    11191   5934   9765   -225   2634     47       C  
ATOM   2448  OG  SER B   8      31.819   8.545 -18.157  1.00 70.15           O  
ANISOU 2448  OG  SER B   8    11064   6067   9523   -487   2478    -71       O  
ATOM   2449  N   GLN B   9      28.408   7.899 -19.468  1.00 76.24           N  
ANISOU 2449  N   GLN B   9    11486   6922  10561    669   2208   1067       N  
ATOM   2450  CA  GLN B   9      27.927   7.654 -20.825  1.00 73.67           C  
ANISOU 2450  CA  GLN B   9    10986   6818  10185    933   2010   1507       C  
ATOM   2451  C   GLN B   9      29.033   7.908 -21.847  1.00 65.45           C  
ANISOU 2451  C   GLN B   9    10040   5781   9049    747   2011   1498       C  
ATOM   2452  O   GLN B   9      29.039   7.313 -22.927  1.00 63.74           O  
ANISOU 2452  O   GLN B   9     9648   5892   8678    809   1720   1704       O  
ATOM   2453  CB  GLN B   9      26.700   8.516 -21.132  1.00 76.74           C  
ANISOU 2453  CB  GLN B   9    11339   7080  10739   1340   2256   1925       C  
ATOM   2454  CG  GLN B   9      25.439   8.086 -20.383  1.00 78.72           C  
ANISOU 2454  CG  GLN B   9    11385   7486  11039   1561   2170   2010       C  
ATOM   2455  CD  GLN B   9      25.048   6.633 -20.646  1.00 76.10           C  
ANISOU 2455  CD  GLN B   9    10766   7619  10532   1577   1689   2100       C  
ATOM   2456  OE1 GLN B   9      24.922   5.834 -19.717  1.00 75.21           O  
ANISOU 2456  OE1 GLN B   9    10575   7634  10368   1444   1519   1826       O  
ATOM   2457  NE2 GLN B   9      24.843   6.292 -21.912  1.00 74.42           N  
ANISOU 2457  NE2 GLN B   9    10358   7748  10169   1676   1451   2413       N  
ATOM   2458  N   ASN B  10      29.974   8.777 -21.493  1.00 61.45           N  
ANISOU 2458  N   ASN B  10     9809   4928   8610    476   2352   1230       N  
ATOM   2459  CA  ASN B  10      31.140   9.027 -22.334  1.00 60.97           C  
ANISOU 2459  CA  ASN B  10     9838   4874   8452    234   2379   1159       C  
ATOM   2460  C   ASN B  10      31.933   7.754 -22.615  1.00 54.80           C  
ANISOU 2460  C   ASN B  10     8815   4591   7416     31   1907    955       C  
ATOM   2461  O   ASN B  10      32.437   7.562 -23.725  1.00 46.21           O  
ANISOU 2461  O   ASN B  10     7675   3671   6210      3   1779   1082       O  
ATOM   2462  CB  ASN B  10      32.059  10.070 -21.689  1.00 65.87           C  
ANISOU 2462  CB  ASN B  10    10776   5095   9156   -130   2824    805       C  
ATOM   2463  CG  ASN B  10      33.444  10.104 -22.328  1.00 75.38           C  
ANISOU 2463  CG  ASN B  10    12006   6426  10209   -487   2787    613       C  
ATOM   2464  OD1 ASN B  10      33.603  10.517 -23.481  1.00 75.86           O  
ANISOU 2464  OD1 ASN B  10    12140   6401  10281   -395   2880    895       O  
ATOM   2465  ND2 ASN B  10      34.453   9.663 -21.580  1.00 75.20           N  
ANISOU 2465  ND2 ASN B  10    11896   6654  10023   -885   2653    155       N  
ATOM   2466  N   ASP B  11      32.028   6.889 -21.604  1.00 49.16           N  
ANISOU 2466  N   ASP B  11     7964   4100   6614    -87   1684    660       N  
ATOM   2467  CA  ASP B  11      32.813   5.656 -21.699  1.00 48.30           C  
ANISOU 2467  CA  ASP B  11     7650   4420   6281   -241   1306    466       C  
ATOM   2468  C   ASP B  11      32.342   4.711 -22.805  1.00 48.19           C  
ANISOU 2468  C   ASP B  11     7458   4697   6155    -43    985    738       C  
ATOM   2469  O   ASP B  11      33.102   3.845 -23.233  1.00 39.25           O  
ANISOU 2469  O   ASP B  11     6219   3844   4850   -158    761    624       O  
ATOM   2470  CB  ASP B  11      32.788   4.896 -20.367  1.00 45.03           C  
ANISOU 2470  CB  ASP B  11     7129   4176   5804   -316   1160    190       C  
ATOM   2471  CG  ASP B  11      33.309   5.716 -19.208  1.00 54.98           C  
ANISOU 2471  CG  ASP B  11     8536   5254   7101   -586   1446   -137       C  
ATOM   2472  OD1 ASP B  11      34.200   6.569 -19.417  1.00 51.08           O  
ANISOU 2472  OD1 ASP B  11     8183   4623   6603   -849   1687   -282       O  
ATOM   2473  OD2 ASP B  11      32.824   5.496 -18.078  1.00 63.00           O  
ANISOU 2473  OD2 ASP B  11     9528   6282   8127   -570   1444   -268       O  
ATOM   2474  N   LEU B  12      31.098   4.878 -23.258  1.00 50.25           N  
ANISOU 2474  N   LEU B  12     7679   4920   6495    242    986   1091       N  
ATOM   2475  CA  LEU B  12      30.486   3.950 -24.212  1.00 50.71           C  
ANISOU 2475  CA  LEU B  12     7543   5322   6402    373    681   1321       C  
ATOM   2476  C   LEU B  12      30.657   4.362 -25.675  1.00 50.91           C  
ANISOU 2476  C   LEU B  12     7582   5419   6342    419    699   1605       C  
ATOM   2477  O   LEU B  12      30.171   3.677 -26.576  1.00 48.10           O  
ANISOU 2477  O   LEU B  12     7068   5390   5817    480    465   1791       O  
ATOM   2478  CB  LEU B  12      28.985   3.803 -23.931  1.00 55.30           C  
ANISOU 2478  CB  LEU B  12     7988   5971   7051    629    628   1565       C  
ATOM   2479  CG  LEU B  12      28.450   3.174 -22.640  1.00 55.90           C  
ANISOU 2479  CG  LEU B  12     7999   6063   7176    632    554   1369       C  
ATOM   2480  CD1 LEU B  12      29.147   1.869 -22.338  1.00 41.32           C  
ANISOU 2480  CD1 LEU B  12     6095   4441   5163    429    302   1062       C  
ATOM   2481  CD2 LEU B  12      28.562   4.126 -21.470  1.00 61.44           C  
ANISOU 2481  CD2 LEU B  12     8879   6392   8074    624    874   1213       C  
ATOM   2482  N   THR B  13      31.328   5.477 -25.922  1.00 55.79           N  
ANISOU 2482  N   THR B  13     8396   5745   7055    361    997   1633       N  
ATOM   2483  CA  THR B  13      31.283   6.065 -27.259  1.00 68.58           C  
ANISOU 2483  CA  THR B  13    10051   7387   8620    473   1079   1993       C  
ATOM   2484  C   THR B  13      32.437   5.647 -28.183  1.00 67.54           C  
ANISOU 2484  C   THR B  13     9920   7451   8290    238    955   1864       C  
ATOM   2485  O   THR B  13      32.575   6.195 -29.281  1.00 72.82           O  
ANISOU 2485  O   THR B  13    10645   8125   8897    289   1051   2134       O  
ATOM   2486  CB  THR B  13      31.238   7.606 -27.173  1.00 70.88           C  
ANISOU 2486  CB  THR B  13    10599   7194   9140    590   1551   2185       C  
ATOM   2487  OG1 THR B  13      32.345   8.083 -26.398  1.00 71.64           O  
ANISOU 2487  OG1 THR B  13    10904   6990   9325    271   1788   1776       O  
ATOM   2488  CG2 THR B  13      29.937   8.055 -26.515  1.00 69.45           C  
ANISOU 2488  CG2 THR B  13    10403   6838   9149    916   1710   2426       C  
ATOM   2489  N   SER B  14      33.248   4.678 -27.749  1.00 48.00           N  
ANISOU 2489  N   SER B  14     7377   5150   5712     13    763   1485       N  
ATOM   2490  CA  SER B  14      34.302   4.116 -28.601  1.00 45.44           C  
ANISOU 2490  CA  SER B  14     7022   5049   5193   -173    644   1362       C  
ATOM   2491  C   SER B  14      34.902   2.886 -27.946  1.00 41.16           C  
ANISOU 2491  C   SER B  14     6370   4712   4558   -303    439   1012       C  
ATOM   2492  O   SER B  14      34.750   2.688 -26.751  1.00 33.80           O  
ANISOU 2492  O   SER B  14     5413   3713   3716   -300    430    835       O  
ATOM   2493  CB  SER B  14      35.406   5.145 -28.891  1.00 49.37           C  
ANISOU 2493  CB  SER B  14     7688   5330   5741   -354    927   1300       C  
ATOM   2494  OG  SER B  14      36.245   5.350 -27.765  1.00 39.21           O  
ANISOU 2494  OG  SER B  14     6444   3919   4536   -574   1052    935       O  
ATOM   2495  N   THR B  15      35.593   2.056 -28.715  1.00 34.14           N  
ANISOU 2495  N   THR B  15     5423   4066   3481   -398    303    928       N  
ATOM   2496  CA  THR B  15      36.205   0.875 -28.124  1.00 34.41           C  
ANISOU 2496  CA  THR B  15     5367   4270   3436   -458    167    648       C  
ATOM   2497  C   THR B  15      37.386   1.333 -27.285  1.00 33.41           C  
ANISOU 2497  C   THR B  15     5235   4093   3367   -611    306    401       C  
ATOM   2498  O   THR B  15      37.722   0.701 -26.284  1.00 35.21           O  
ANISOU 2498  O   THR B  15     5372   4424   3583   -616    241    204       O  
ATOM   2499  CB  THR B  15      36.666  -0.155 -29.174  1.00 34.17           C  
ANISOU 2499  CB  THR B  15     5304   4481   3197   -502     52    617       C  
ATOM   2500  OG1 THR B  15      37.731   0.398 -29.949  1.00 50.12           O  
ANISOU 2500  OG1 THR B  15     7362   6524   5157   -629    177    607       O  
ATOM   2501  CG2 THR B  15      35.516  -0.522 -30.093  1.00 34.67           C  
ANISOU 2501  CG2 THR B  15     5362   4668   3143   -440    -76    836       C  
ATOM   2502  N   GLU B  16      37.993   2.452 -27.669  1.00 34.42           N  
ANISOU 2502  N   GLU B  16     5452   4089   3536   -754    513    422       N  
ATOM   2503  CA  GLU B  16      39.119   2.972 -26.895  1.00 37.18           C  
ANISOU 2503  CA  GLU B  16     5778   4444   3903   -985    664    158       C  
ATOM   2504  C   GLU B  16      38.651   3.378 -25.507  1.00 37.23           C  
ANISOU 2504  C   GLU B  16     5812   4298   4036  -1005    738     32       C  
ATOM   2505  O   GLU B  16      39.317   3.103 -24.510  1.00 37.92           O  
ANISOU 2505  O   GLU B  16     5778   4567   4062  -1133    711   -218       O  
ATOM   2506  CB  GLU B  16      39.783   4.160 -27.598  1.00 37.79           C  
ANISOU 2506  CB  GLU B  16     5987   4365   4006  -1187    925    193       C  
ATOM   2507  CG  GLU B  16      40.712   3.772 -28.738  1.00 40.55           C  
ANISOU 2507  CG  GLU B  16     6272   4944   4193  -1262    885    206       C  
ATOM   2508  CD  GLU B  16      40.085   3.993 -30.098  1.00 48.59           C  
ANISOU 2508  CD  GLU B  16     7409   5873   5179  -1131    893    530       C  
ATOM   2509  OE1 GLU B  16      38.837   3.919 -30.213  1.00 53.03           O  
ANISOU 2509  OE1 GLU B  16     8012   6347   5789   -913    805    760       O  
ATOM   2510  OE2 GLU B  16      40.839   4.256 -31.052  1.00 51.36           O  
ANISOU 2510  OE2 GLU B  16     7790   6288   5435  -1253    988    567       O  
ATOM   2511  N   ARG B  17      37.500   4.034 -25.441  1.00 42.74           N  
ANISOU 2511  N   ARG B  17     6652   4697   4892   -866    842    224       N  
ATOM   2512  CA  ARG B  17      36.976   4.488 -24.156  1.00 46.47           C  
ANISOU 2512  CA  ARG B  17     7182   4979   5493   -878    961    107       C  
ATOM   2513  C   ARG B  17      36.505   3.314 -23.296  1.00 33.66           C  
ANISOU 2513  C   ARG B  17     5402   3569   3817   -740    705     29       C  
ATOM   2514  O   ARG B  17      36.673   3.323 -22.087  1.00 35.61           O  
ANISOU 2514  O   ARG B  17     5615   3852   4063   -840    736   -189       O  
ATOM   2515  CB  ARG B  17      35.850   5.503 -24.366  1.00 51.65           C  
ANISOU 2515  CB  ARG B  17     8031   5246   6347   -705   1188    378       C  
ATOM   2516  CG  ARG B  17      36.291   6.915 -24.010  1.00 61.70           C  
ANISOU 2516  CG  ARG B  17     9542   6152   7750   -930   1610    256       C  
ATOM   2517  CD  ARG B  17      35.417   7.990 -24.626  1.00 64.09           C  
ANISOU 2517  CD  ARG B  17    10068   6040   8242   -710   1912    616       C  
ATOM   2518  NE  ARG B  17      35.635   8.130 -26.059  1.00 66.66           N  
ANISOU 2518  NE  ARG B  17    10411   6415   8501   -635   1900    900       N  
ATOM   2519  CZ  ARG B  17      35.211   9.168 -26.772  1.00 68.74           C  
ANISOU 2519  CZ  ARG B  17    10878   6348   8890   -474   2210   1241       C  
ATOM   2520  NH1 ARG B  17      34.547  10.151 -26.178  1.00 72.14           N  
ANISOU 2520  NH1 ARG B  17    11530   6332   9546   -353   2588   1336       N  
ATOM   2521  NH2 ARG B  17      35.450   9.224 -28.076  1.00 64.23           N  
ANISOU 2521  NH2 ARG B  17    10302   5887   8214   -416   2174   1504       N  
ATOM   2522  N   LEU B  18      35.941   2.294 -23.922  1.00 31.94           N  
ANISOU 2522  N   LEU B  18     5099   3504   3533   -542    472    195       N  
ATOM   2523  CA  LEU B  18      35.592   1.078 -23.206  1.00 29.90           C  
ANISOU 2523  CA  LEU B  18     4722   3425   3214   -432    266    120       C  
ATOM   2524  C   LEU B  18      36.835   0.439 -22.571  1.00 32.99           C  
ANISOU 2524  C   LEU B  18     4987   4080   3468   -544    210   -123       C  
ATOM   2525  O   LEU B  18      36.808  -0.004 -21.414  1.00 31.14           O  
ANISOU 2525  O   LEU B  18     4678   3945   3208   -520    160   -246       O  
ATOM   2526  CB  LEU B  18      34.896   0.102 -24.147  1.00 28.84           C  
ANISOU 2526  CB  LEU B  18     4552   3405   3003   -284     80    301       C  
ATOM   2527  CG  LEU B  18      33.449   0.478 -24.490  1.00 41.74           C  
ANISOU 2527  CG  LEU B  18     6211   4922   4726   -136     74    564       C  
ATOM   2528  CD1 LEU B  18      32.837  -0.485 -25.507  1.00 38.75           C  
ANISOU 2528  CD1 LEU B  18     5768   4752   4202    -88   -112    704       C  
ATOM   2529  CD2 LEU B  18      32.615   0.508 -23.227  1.00 39.45           C  
ANISOU 2529  CD2 LEU B  18     5906   4526   4558    -48     96    526       C  
ATOM   2530  N   ILE B  19      37.933   0.429 -23.323  1.00 31.73           N  
ANISOU 2530  N   ILE B  19     4782   4068   3205   -653    231   -168       N  
ATOM   2531  CA  ILE B  19      39.186  -0.157 -22.857  1.00 30.25           C  
ANISOU 2531  CA  ILE B  19     4419   4206   2867   -721    190   -343       C  
ATOM   2532  C   ILE B  19      39.749   0.600 -21.661  1.00 45.66           C  
ANISOU 2532  C   ILE B  19     6299   6253   4795   -942    298   -559       C  
ATOM   2533  O   ILE B  19      40.262  -0.016 -20.708  1.00 31.77           O  
ANISOU 2533  O   ILE B  19     4359   4802   2909   -924    216   -669       O  
ATOM   2534  CB  ILE B  19      40.231  -0.197 -23.983  1.00 31.97           C  
ANISOU 2534  CB  ILE B  19     4592   4571   2985   -800    225   -335       C  
ATOM   2535  CG1 ILE B  19      39.843  -1.263 -25.016  1.00 33.00           C  
ANISOU 2535  CG1 ILE B  19     4768   4704   3067   -607    114   -186       C  
ATOM   2536  CG2 ILE B  19      41.593  -0.511 -23.430  1.00 32.14           C  
ANISOU 2536  CG2 ILE B  19     4383   4976   2853   -887    227   -499       C  
ATOM   2537  CD1 ILE B  19      40.611  -1.149 -26.348  1.00 30.88           C  
ANISOU 2537  CD1 ILE B  19     4515   4507   2711   -688    176   -147       C  
ATOM   2538  N   GLN B  20      39.634   1.930 -21.700  1.00 33.40           N  
ANISOU 2538  N   GLN B  20     4898   4445   3348  -1155    508   -612       N  
ATOM   2539  CA  GLN B  20      40.144   2.757 -20.616  1.00 35.47           C  
ANISOU 2539  CA  GLN B  20     5139   4769   3569  -1457    668   -872       C  
ATOM   2540  C   GLN B  20      39.275   2.580 -19.383  1.00 41.50           C  
ANISOU 2540  C   GLN B  20     5922   5472   4374  -1367    633   -921       C  
ATOM   2541  O   GLN B  20      39.793   2.501 -18.272  1.00 35.76           O  
ANISOU 2541  O   GLN B  20     5053   5037   3499  -1528    619  -1130       O  
ATOM   2542  CB  GLN B  20      40.222   4.232 -21.029  1.00 40.11           C  
ANISOU 2542  CB  GLN B  20     5956   5007   4275  -1725    987   -926       C  
ATOM   2543  CG  GLN B  20      41.300   4.517 -22.082  1.00 43.66           C  
ANISOU 2543  CG  GLN B  20     6370   5571   4647  -1904   1060   -934       C  
ATOM   2544  CD  GLN B  20      42.681   3.994 -21.680  1.00 49.29           C  
ANISOU 2544  CD  GLN B  20     6766   6850   5112  -2099    952  -1145       C  
ATOM   2545  OE1 GLN B  20      43.109   4.161 -20.543  1.00 52.42           O  
ANISOU 2545  OE1 GLN B  20     7030   7503   5384  -2331    978  -1386       O  
ATOM   2546  NE2 GLN B  20      43.379   3.355 -22.620  1.00 44.67           N  
ANISOU 2546  NE2 GLN B  20     6037   6500   4434  -1998    840  -1042       N  
ATOM   2547  N   LEU B  21      37.961   2.497 -19.590  1.00 33.40           N  
ANISOU 2547  N   LEU B  21     5044   4124   3522  -1116    615   -719       N  
ATOM   2548  CA  LEU B  21      37.022   2.245 -18.504  1.00 33.49           C  
ANISOU 2548  CA  LEU B  21     5071   4068   3584   -996    581   -735       C  
ATOM   2549  C   LEU B  21      37.294   0.884 -17.858  1.00 31.08           C  
ANISOU 2549  C   LEU B  21     4556   4142   3112   -857    337   -755       C  
ATOM   2550  O   LEU B  21      37.230   0.746 -16.636  1.00 31.96           O  
ANISOU 2550  O   LEU B  21     4603   4394   3146   -899    327   -884       O  
ATOM   2551  CB  LEU B  21      35.574   2.313 -19.010  1.00 32.82           C  
ANISOU 2551  CB  LEU B  21     5124   3647   3697   -732    589   -470       C  
ATOM   2552  CG  LEU B  21      34.553   1.632 -18.095  1.00 30.85           C  
ANISOU 2552  CG  LEU B  21     4836   3407   3479   -547    481   -434       C  
ATOM   2553  CD1 LEU B  21      34.396   2.404 -16.799  1.00 40.25           C  
ANISOU 2553  CD1 LEU B  21     6104   4485   4704   -700    681   -639       C  
ATOM   2554  CD2 LEU B  21      33.209   1.434 -18.780  1.00 31.57           C  
ANISOU 2554  CD2 LEU B  21     4969   3320   3707   -290    425   -147       C  
ATOM   2555  N   PHE B  22      37.600  -0.116 -18.688  1.00 29.75           N  
ANISOU 2555  N   PHE B  22     4301   4123   2879   -685    176   -619       N  
ATOM   2556  CA  PHE B  22      37.968  -1.450 -18.199  1.00 34.09           C  
ANISOU 2556  CA  PHE B  22     4686   4986   3281   -509     13   -598       C  
ATOM   2557  C   PHE B  22      39.259  -1.408 -17.378  1.00 30.81           C  
ANISOU 2557  C   PHE B  22     4044   5008   2652   -662     16   -766       C  
ATOM   2558  O   PHE B  22      39.346  -2.014 -16.309  1.00 31.23           O  
ANISOU 2558  O   PHE B  22     3967   5318   2580   -575    -55   -785       O  
ATOM   2559  CB  PHE B  22      38.114  -2.425 -19.381  1.00 27.80           C  
ANISOU 2559  CB  PHE B  22     3895   4202   2466   -326    -74   -444       C  
ATOM   2560  CG  PHE B  22      38.596  -3.792 -18.996  1.00 34.07           C  
ANISOU 2560  CG  PHE B  22     4567   5250   3128   -111   -154   -397       C  
ATOM   2561  CD1 PHE B  22      37.940  -4.528 -18.029  1.00 33.24           C  
ANISOU 2561  CD1 PHE B  22     4470   5140   3019     49   -202   -356       C  
ATOM   2562  CD2 PHE B  22      39.693  -4.355 -19.627  1.00 33.84           C  
ANISOU 2562  CD2 PHE B  22     4429   5443   2985    -42   -145   -369       C  
ATOM   2563  CE1 PHE B  22      38.374  -5.798 -17.695  1.00 27.22           C  
ANISOU 2563  CE1 PHE B  22     3632   4564   2148    288   -221   -268       C  
ATOM   2564  CE2 PHE B  22      40.134  -5.615 -19.291  1.00 33.70           C  
ANISOU 2564  CE2 PHE B  22     4321   5619   2864    218   -156   -281       C  
ATOM   2565  CZ  PHE B  22      39.462  -6.341 -18.320  1.00 29.35           C  
ANISOU 2565  CZ  PHE B  22     3805   5031   2318    391   -186   -220       C  
ATOM   2566  N   GLU B  23      40.254  -0.672 -17.868  1.00 32.35           N  
ANISOU 2566  N   GLU B  23     4175   5332   2784   -905    105   -876       N  
ATOM   2567  CA  GLU B  23      41.514  -0.531 -17.152  1.00 34.74           C  
ANISOU 2567  CA  GLU B  23     4209   6144   2847  -1115    108  -1046       C  
ATOM   2568  C   GLU B  23      41.272   0.142 -15.799  1.00 41.32           C  
ANISOU 2568  C   GLU B  23     5039   7054   3608  -1359    179  -1255       C  
ATOM   2569  O   GLU B  23      41.860  -0.232 -14.785  1.00 37.75           O  
ANISOU 2569  O   GLU B  23     4335   7093   2914  -1401     99  -1328       O  
ATOM   2570  CB  GLU B  23      42.524   0.283 -17.975  1.00 36.58           C  
ANISOU 2570  CB  GLU B  23     4396   6464   3037  -1406    228  -1154       C  
ATOM   2571  CG  GLU B  23      43.087  -0.410 -19.219  1.00 43.85           C  
ANISOU 2571  CG  GLU B  23     5256   7454   3953  -1208    171   -986       C  
ATOM   2572  CD  GLU B  23      44.053  -1.546 -18.895  1.00 53.56           C  
ANISOU 2572  CD  GLU B  23     6158   9225   4969   -990     54   -907       C  
ATOM   2573  OE1 GLU B  23      44.190  -1.913 -17.711  1.00 57.77           O  
ANISOU 2573  OE1 GLU B  23     6503  10096   5351   -939    -20   -930       O  
ATOM   2574  OE2 GLU B  23      44.681  -2.086 -19.829  1.00 36.73           O  
ANISOU 2574  OE2 GLU B  23     3954   7190   2810   -844     56   -797       O  
ATOM   2575  N   SER B  24      40.406   1.147 -15.794  1.00 36.27           N  
ANISOU 2575  N   SER B  24     4676   5945   3161  -1510    353  -1337       N  
ATOM   2576  CA  SER B  24      40.058   1.846 -14.563  1.00 42.70           C  
ANISOU 2576  CA  SER B  24     5555   6737   3931  -1753    483  -1560       C  
ATOM   2577  C   SER B  24      39.343   0.905 -13.596  1.00 38.64           C  
ANISOU 2577  C   SER B  24     4978   6334   3370  -1480    326  -1461       C  
ATOM   2578  O   SER B  24      39.615   0.925 -12.396  1.00 38.21           O  
ANISOU 2578  O   SER B  24     4789   6627   3103  -1642    319  -1625       O  
ATOM   2579  CB  SER B  24      39.189   3.066 -14.864  1.00 40.99           C  
ANISOU 2579  CB  SER B  24     5689   5907   3977  -1880    763  -1611       C  
ATOM   2580  OG  SER B  24      39.922   4.017 -15.614  1.00 51.60           O  
ANISOU 2580  OG  SER B  24     7117   7146   5343  -2180    964  -1721       O  
ATOM   2581  N   TRP B  25      38.451   0.072 -14.131  1.00 33.68           N  
ANISOU 2581  N   TRP B  25     4441   5444   2913  -1097    211  -1200       N  
ATOM   2582  CA  TRP B  25      37.729  -0.915 -13.328  1.00 34.24           C  
ANISOU 2582  CA  TRP B  25     4478   5573   2957   -830     86  -1083       C  
ATOM   2583  C   TRP B  25      38.663  -1.943 -12.691  1.00 35.75           C  
ANISOU 2583  C   TRP B  25     4385   6326   2871   -711    -67  -1032       C  
ATOM   2584  O   TRP B  25      38.468  -2.345 -11.550  1.00 33.75           O  
ANISOU 2584  O   TRP B  25     4051   6291   2481   -654   -111  -1039       O  
ATOM   2585  CB  TRP B  25      36.679  -1.642 -14.178  1.00 29.70           C  
ANISOU 2585  CB  TRP B  25     4048   4643   2594   -511     12   -834       C  
ATOM   2586  CG  TRP B  25      35.964  -2.718 -13.419  1.00 35.04           C  
ANISOU 2586  CG  TRP B  25     4710   5359   3246   -267    -85   -718       C  
ATOM   2587  CD1 TRP B  25      34.836  -2.575 -12.662  1.00 34.89           C  
ANISOU 2587  CD1 TRP B  25     4796   5142   3320   -237    -37   -726       C  
ATOM   2588  CD2 TRP B  25      36.330  -4.102 -13.334  1.00 34.55           C  
ANISOU 2588  CD2 TRP B  25     4540   5525   3061    -12   -200   -567       C  
ATOM   2589  NE1 TRP B  25      34.474  -3.782 -12.118  1.00 27.41           N  
ANISOU 2589  NE1 TRP B  25     3810   4295   2309    -10   -132   -598       N  
ATOM   2590  CE2 TRP B  25      35.376  -4.736 -12.514  1.00 27.45           C  
ANISOU 2590  CE2 TRP B  25     3704   4539   2187    139   -216   -493       C  
ATOM   2591  CE3 TRP B  25      37.365  -4.870 -13.886  1.00 35.62           C  
ANISOU 2591  CE3 TRP B  25     4549   5907   3079    123   -251   -472       C  
ATOM   2592  CZ2 TRP B  25      35.431  -6.099 -12.219  1.00 30.77           C  
ANISOU 2592  CZ2 TRP B  25     4094   5077   2521    407   -263   -326       C  
ATOM   2593  CZ3 TRP B  25      37.418  -6.226 -13.591  1.00 31.36           C  
ANISOU 2593  CZ3 TRP B  25     3977   5475   2462    424   -283   -297       C  
ATOM   2594  CH2 TRP B  25      36.453  -6.825 -12.773  1.00 34.60           C  
ANISOU 2594  CH2 TRP B  25     4483   5759   2905    557   -280   -224       C  
ATOM   2595  N   MET B  26      39.661  -2.390 -13.444  1.00 37.57           N  
ANISOU 2595  N   MET B  26     4460   6800   3015   -636   -129   -948       N  
ATOM   2596  CA  MET B  26      40.637  -3.333 -12.915  1.00 38.10           C  
ANISOU 2596  CA  MET B  26     4225   7433   2817   -462   -236   -843       C  
ATOM   2597  C   MET B  26      41.421  -2.691 -11.787  1.00 44.46           C  
ANISOU 2597  C   MET B  26     4777   8787   3326   -785   -232  -1052       C  
ATOM   2598  O   MET B  26      41.729  -3.333 -10.780  1.00 50.41           O  
ANISOU 2598  O   MET B  26     5306  10009   3836   -652   -319   -967       O  
ATOM   2599  CB  MET B  26      41.607  -3.798 -13.999  1.00 39.09           C  
ANISOU 2599  CB  MET B  26     4226   7712   2915   -330   -254   -724       C  
ATOM   2600  CG  MET B  26      40.984  -4.491 -15.185  1.00 37.43           C  
ANISOU 2600  CG  MET B  26     4249   7039   2932    -66   -244   -550       C  
ATOM   2601  SD  MET B  26      42.300  -4.903 -16.350  1.00 41.37           S  
ANISOU 2601  SD  MET B  26     4584   7781   3353     33   -218   -461       S  
ATOM   2602  CE  MET B  26      43.380  -5.841 -15.296  1.00 36.66           C  
ANISOU 2602  CE  MET B  26     3602   7869   2457    301   -263   -308       C  
ATOM   2603  N   LEU B  27      41.749  -1.416 -11.961  1.00 40.61           N  
ANISOU 2603  N   LEU B  27     4332   8259   2838  -1230   -107  -1324       N  
ATOM   2604  CA  LEU B  27      42.527  -0.711 -10.955  1.00 53.10           C  
ANISOU 2604  CA  LEU B  27     5686  10296   4194  -1620    -50  -1545       C  
ATOM   2605  C   LEU B  27      41.741  -0.606  -9.653  1.00 57.39           C  
ANISOU 2605  C   LEU B  27     6305  10781   4719  -1664    -20  -1613       C  
ATOM   2606  O   LEU B  27      42.269  -0.900  -8.584  1.00 55.18           O  
ANISOU 2606  O   LEU B  27     5741  10972   4251  -1679    -70  -1571       O  
ATOM   2607  CB  LEU B  27      42.934   0.678 -11.453  1.00 54.22           C  
ANISOU 2607  CB  LEU B  27     5940  10262   4401  -2114    158  -1826       C  
ATOM   2608  CG  LEU B  27      44.086   0.675 -12.457  1.00 61.49           C  
ANISOU 2608  CG  LEU B  27     6666  11445   5255  -2177    143  -1793       C  
ATOM   2609  CD1 LEU B  27      44.467   2.094 -12.869  1.00 68.22           C  
ANISOU 2609  CD1 LEU B  27     7661  12091   6170  -2700    399  -2073       C  
ATOM   2610  CD2 LEU B  27      45.279  -0.058 -11.872  1.00 64.86           C  
ANISOU 2610  CD2 LEU B  27     6600  12611   5433  -2061     23  -1645       C  
ATOM   2611  N   LYS B  28      40.475  -0.204  -9.755  1.00 54.77           N  
ANISOU 2611  N   LYS B  28     6342   9896   4572  -1672     77  -1706       N  
ATOM   2612  CA  LYS B  28      39.623  -0.044  -8.581  1.00 53.72           C  
ANISOU 2612  CA  LYS B  28     6317   9654   4439  -1715    140  -1787       C  
ATOM   2613  C   LYS B  28      39.478  -1.343  -7.805  1.00 52.00           C  
ANISOU 2613  C   LYS B  28     5919   9755   4082  -1336    -50  -1531       C  
ATOM   2614  O   LYS B  28      39.239  -1.323  -6.604  1.00 59.17           O  
ANISOU 2614  O   LYS B  28     6774  10817   4891  -1405    -31  -1575       O  
ATOM   2615  CB  LYS B  28      38.233   0.456  -8.978  1.00 57.28           C  
ANISOU 2615  CB  LYS B  28     7167   9387   5211  -1653    298  -1816       C  
ATOM   2616  CG  LYS B  28      38.188   1.810  -9.656  1.00 64.30           C  
ANISOU 2616  CG  LYS B  28     8301   9831   6297  -1967    566  -2013       C  
ATOM   2617  CD  LYS B  28      36.742   2.279  -9.773  1.00 71.99           C  
ANISOU 2617  CD  LYS B  28     9609  10135   7610  -1813    747  -1948       C  
ATOM   2618  CE  LYS B  28      36.578   3.417 -10.775  1.00 78.35           C  
ANISOU 2618  CE  LYS B  28    10675  10416   8678  -1937   1012  -1978       C  
ATOM   2619  NZ  LYS B  28      36.729   2.981 -12.195  1.00 75.34           N  
ANISOU 2619  NZ  LYS B  28    10259   9933   8433  -1686    866  -1706       N  
ATOM   2620  N   HIS B  29      39.615  -2.469  -8.500  1.00 53.93           N  
ANISOU 2620  N   HIS B  29     6096  10068   4328   -936   -197  -1254       N  
ATOM   2621  CA  HIS B  29      39.331  -3.774  -7.911  1.00 50.10           C  
ANISOU 2621  CA  HIS B  29     5530   9734   3770   -519   -310   -967       C  
ATOM   2622  C   HIS B  29      40.538  -4.704  -7.818  1.00 60.03           C  
ANISOU 2622  C   HIS B  29     6440  11487   4880   -263   -396   -711       C  
ATOM   2623  O   HIS B  29      40.358  -5.923  -7.829  1.00 62.68           O  
ANISOU 2623  O   HIS B  29     6783  11804   5227    168   -435   -418       O  
ATOM   2624  CB  HIS B  29      38.230  -4.489  -8.706  1.00 35.71           C  
ANISOU 2624  CB  HIS B  29     3990   7318   2260   -180   -305   -768       C  
ATOM   2625  CG  HIS B  29      36.899  -3.813  -8.647  1.00 42.97           C  
ANISOU 2625  CG  HIS B  29     5200   7694   3434   -302   -200   -891       C  
ATOM   2626  ND1 HIS B  29      36.427  -3.010  -9.662  1.00 39.20           N  
ANISOU 2626  ND1 HIS B  29     4922   6745   3227   -421   -108   -967       N  
ATOM   2627  CD2 HIS B  29      35.933  -3.827  -7.699  1.00 44.20           C  
ANISOU 2627  CD2 HIS B  29     5461   7726   3608   -289   -154   -919       C  
ATOM   2628  CE1 HIS B  29      35.230  -2.555  -9.340  1.00 36.29           C  
ANISOU 2628  CE1 HIS B  29     4751   5999   3037   -450     -6  -1017       C  
ATOM   2629  NE2 HIS B  29      34.904  -3.041  -8.157  1.00 39.94           N  
ANISOU 2629  NE2 HIS B  29     5164   6653   3358   -382    -31  -1005       N  
ATOM   2630  N   ASN B  30      41.748  -4.139  -7.741  1.00 67.63           N  
ANISOU 2630  N   ASN B  30     7110  12875   5713   -523   -381   -815       N  
ATOM   2631  CA  ASN B  30      42.999  -4.909  -7.594  1.00 73.51           C  
ANISOU 2631  CA  ASN B  30     7456  14187   6288   -296   -422   -581       C  
ATOM   2632  C   ASN B  30      43.190  -6.035  -8.613  1.00 72.65           C  
ANISOU 2632  C   ASN B  30     7378  13961   6263    181   -442   -286       C  
ATOM   2633  O   ASN B  30      44.051  -6.892  -8.432  1.00 82.95           O  
ANISOU 2633  O   ASN B  30     8401  15665   7452    493   -426    -29       O  
ATOM   2634  CB  ASN B  30      43.100  -5.507  -6.173  1.00 81.14           C  
ANISOU 2634  CB  ASN B  30     8198  15555   7076   -149   -439   -425       C  
ATOM   2635  CG  ASN B  30      42.330  -6.823  -6.018  1.00 86.91           C  
ANISOU 2635  CG  ASN B  30     9099  16030   7891    368   -453   -111       C  
ATOM   2636  OD1 ASN B  30      42.842  -7.907  -6.308  1.00 85.53           O  
ANISOU 2636  OD1 ASN B  30     8809  15982   7706    795   -423    195       O  
ATOM   2637  ND2 ASN B  30      41.098  -6.725  -5.544  1.00 90.72           N  
ANISOU 2637  ND2 ASN B  30     9871  16141   8458    326   -453   -189       N  
ATOM   2638  N   LYS B  31      42.398  -6.036  -9.680  1.00 58.27           N  
ANISOU 2638  N   LYS B  31     5902  11607   4632    243   -440   -317       N  
ATOM   2639  CA  LYS B  31      42.395  -7.157 -10.617  1.00 52.99           C  
ANISOU 2639  CA  LYS B  31     5340  10748   4046    685   -420    -52       C  
ATOM   2640  C   LYS B  31      43.741  -7.328 -11.324  1.00 55.75           C  
ANISOU 2640  C   LYS B  31     5410  11465   4307    772   -396     40       C  
ATOM   2641  O   LYS B  31      44.307  -6.380 -11.868  1.00 62.43           O  
ANISOU 2641  O   LYS B  31     6164  12433   5124    427   -405   -169       O  
ATOM   2642  CB  LYS B  31      41.266  -6.994 -11.635  1.00 47.47           C  
ANISOU 2642  CB  LYS B  31     5053   9327   3654    643   -379   -134       C  
ATOM   2643  CG  LYS B  31      39.909  -7.360 -11.059  1.00 50.30           C  
ANISOU 2643  CG  LYS B  31     5673   9288   4153    739   -364    -96       C  
ATOM   2644  CD  LYS B  31      39.871  -8.824 -10.627  1.00 55.64           C  
ANISOU 2644  CD  LYS B  31     6353  10021   4766   1195   -318    214       C  
ATOM   2645  CE  LYS B  31      38.564  -9.168  -9.917  1.00 57.13           C  
ANISOU 2645  CE  LYS B  31     6773   9877   5059   1247   -293    239       C  
ATOM   2646  NZ  LYS B  31      38.396 -10.634  -9.705  1.00 60.42           N  
ANISOU 2646  NZ  LYS B  31     7295  10189   5474   1673   -181    539       N  
ATOM   2647  N   ILE B  32      44.242  -8.557 -11.269  1.00 50.17           N  
ANISOU 2647  N   ILE B  32     4578  10924   3559   1246   -326    363       N  
ATOM   2648  CA  ILE B  32      45.531  -8.937 -11.818  1.00 54.32           C  
ANISOU 2648  CA  ILE B  32     4811  11847   3983   1444   -259    519       C  
ATOM   2649  C   ILE B  32      45.358 -10.261 -12.546  1.00 55.24           C  
ANISOU 2649  C   ILE B  32     5151  11630   4206   1981   -117    816       C  
ATOM   2650  O   ILE B  32      45.140 -11.295 -11.919  1.00 59.63           O  
ANISOU 2650  O   ILE B  32     5764  12112   4782   2353      4   1063       O  
ATOM   2651  CB  ILE B  32      46.604  -9.083 -10.712  1.00 65.94           C  
ANISOU 2651  CB  ILE B  32     5814  14021   5220   1494   -219    645       C  
ATOM   2652  CG1 ILE B  32      46.934  -7.722 -10.087  1.00 77.03           C  
ANISOU 2652  CG1 ILE B  32     6998  15781   6489    901   -306    321       C  
ATOM   2653  CG2 ILE B  32      47.868  -9.751 -11.250  1.00 63.20           C  
ANISOU 2653  CG2 ILE B  32     5192  14075   4746   1830    -86    895       C  
ATOM   2654  CD1 ILE B  32      47.523  -6.722 -11.063  1.00 78.44           C  
ANISOU 2654  CD1 ILE B  32     7117  16021   6666    514   -322     76       C  
ATOM   2655  N   TYR B  33      45.443 -10.230 -13.869  1.00 51.06           N  
ANISOU 2655  N   TYR B  33     4795  10817   3788   1978    -67    767       N  
ATOM   2656  CA  TYR B  33      45.206 -11.425 -14.669  1.00 50.83           C  
ANISOU 2656  CA  TYR B  33     5066  10300   3948   2380    149    962       C  
ATOM   2657  C   TYR B  33      46.484 -12.241 -14.878  1.00 57.60           C  
ANISOU 2657  C   TYR B  33     5644  11576   4666   2836    314   1265       C  
ATOM   2658  O   TYR B  33      47.581 -11.782 -14.555  1.00 62.39           O  
ANISOU 2658  O   TYR B  33     5793  12867   5044   2779    238   1296       O  
ATOM   2659  CB  TYR B  33      44.580 -11.025 -16.000  1.00 45.09           C  
ANISOU 2659  CB  TYR B  33     4690   8968   3472   2095    176    724       C  
ATOM   2660  CG  TYR B  33      43.230 -10.388 -15.800  1.00 45.19           C  
ANISOU 2660  CG  TYR B  33     4975   8559   3636   1761     57    513       C  
ATOM   2661  CD1 TYR B  33      42.300 -10.968 -14.953  1.00 44.97           C  
ANISOU 2661  CD1 TYR B  33     5113   8327   3648   1901     70    600       C  
ATOM   2662  CD2 TYR B  33      42.889  -9.198 -16.431  1.00 42.15           C  
ANISOU 2662  CD2 TYR B  33     4670   7993   3352   1333    -41    256       C  
ATOM   2663  CE1 TYR B  33      41.061 -10.391 -14.747  1.00 42.06           C  
ANISOU 2663  CE1 TYR B  33     4956   7612   3414   1622    -24    426       C  
ATOM   2664  CE2 TYR B  33      41.654  -8.618 -16.229  1.00 38.41           C  
ANISOU 2664  CE2 TYR B  33     4418   7157   3019   1094   -117    114       C  
ATOM   2665  CZ  TYR B  33      40.749  -9.218 -15.375  1.00 32.56           C  
ANISOU 2665  CZ  TYR B  33     3807   6254   2312   1239   -115    194       C  
ATOM   2666  OH  TYR B  33      39.518  -8.656 -15.173  1.00 30.53           O  
ANISOU 2666  OH  TYR B  33     3737   5669   2193   1026   -175     71       O  
ATOM   2667  N   LYS B  34      46.340 -13.462 -15.390  1.00 52.59           N  
ANISOU 2667  N   LYS B  34     5293  10514   4175   3262    587   1476       N  
ATOM   2668  CA  LYS B  34      47.498 -14.335 -15.579  1.00 59.05           C  
ANISOU 2668  CA  LYS B  34     5948  11600   4889   3706    825   1785       C  
ATOM   2669  C   LYS B  34      48.343 -13.842 -16.737  1.00 68.13           C  
ANISOU 2669  C   LYS B  34     6921  12913   6050   3603    839   1669       C  
ATOM   2670  O   LYS B  34      49.445 -13.331 -16.546  1.00 70.22           O  
ANISOU 2670  O   LYS B  34     6780  13806   6092   3494    726   1704       O  
ATOM   2671  CB  LYS B  34      47.067 -15.779 -15.838  1.00 59.95           C  
ANISOU 2671  CB  LYS B  34     6542  11071   5165   4075   1169   1998       C  
ATOM   2672  CG  LYS B  34      48.228 -16.726 -16.065  1.00 67.32           C  
ANISOU 2672  CG  LYS B  34     7447  12129   6004   4434   1427   2321       C  
ATOM   2673  CD  LYS B  34      47.861 -17.833 -17.041  1.00 69.98           C  
ANISOU 2673  CD  LYS B  34     8305  11698   6586   4621   1779   2363       C  
ATOM   2674  CE  LYS B  34      49.061 -18.711 -17.357  1.00 73.01           C  
ANISOU 2674  CE  LYS B  34     8655  12189   6897   4981   2050   2682       C  
ATOM   2675  NZ  LYS B  34      48.873 -19.471 -18.625  1.00 74.46           N  
ANISOU 2675  NZ  LYS B  34     9290  11676   7324   5026   2372   2599       N  
ATOM   2676  N   ASN B  35      47.808 -13.999 -17.944  1.00 67.91           N  
ANISOU 2676  N   ASN B  35     7305  12244   6254   3487    980   1489       N  
ATOM   2677  CA  ASN B  35      48.498 -13.555 -19.144  1.00 63.74           C  
ANISOU 2677  CA  ASN B  35     6714  11757   5747   3314   1024   1346       C  
ATOM   2678  C   ASN B  35      47.659 -12.584 -19.961  1.00 61.61           C  
ANISOU 2678  C   ASN B  35     6724  11066   5619   2740    857    975       C  
ATOM   2679  O   ASN B  35      46.546 -12.216 -19.584  1.00 56.84           O  
ANISOU 2679  O   ASN B  35     6333  10161   5102   2484    704    832       O  
ATOM   2680  CB  ASN B  35      48.913 -14.754 -20.010  1.00 61.38           C  
ANISOU 2680  CB  ASN B  35     6650  11124   5547   3736   1404   1525       C  
ATOM   2681  CG  ASN B  35      47.753 -15.691 -20.341  1.00 65.29           C  
ANISOU 2681  CG  ASN B  35     7735  10830   6244   3818   1638   1482       C  
ATOM   2682  OD1 ASN B  35      46.612 -15.264 -20.549  1.00 51.62           O  
ANISOU 2682  OD1 ASN B  35     6292   8703   4617   3417   1488   1222       O  
ATOM   2683  ND2 ASN B  35      48.052 -16.984 -20.404  1.00 77.82           N  
ANISOU 2683  ND2 ASN B  35     9565  12100   7902   4164   1921   1735       N  
ATOM   2684  N   ILE B  36      48.211 -12.182 -21.093  1.00 61.46           N  
ANISOU 2684  N   ILE B  36     6688  11048   5615   2571    908    852       N  
ATOM   2685  CA  ILE B  36      47.611 -11.170 -21.938  1.00 54.68           C  
ANISOU 2685  CA  ILE B  36     6031   9892   4854   2063    766    561       C  
ATOM   2686  C   ILE B  36      46.312 -11.654 -22.590  1.00 46.16           C  
ANISOU 2686  C   ILE B  36     5464   8124   3951   1986    835    465       C  
ATOM   2687  O   ILE B  36      45.348 -10.895 -22.709  1.00 42.89           O  
ANISOU 2687  O   ILE B  36     5211   7467   3617   1630    658    296       O  
ATOM   2688  CB  ILE B  36      48.637 -10.730 -22.993  1.00 68.02           C  
ANISOU 2688  CB  ILE B  36     7560  11798   6487   1947    841    498       C  
ATOM   2689  CG1 ILE B  36      48.218  -9.458 -23.696  1.00 69.79           C  
ANISOU 2689  CG1 ILE B  36     7899  11850   6767   1419    684    244       C  
ATOM   2690  CG2 ILE B  36      48.938 -11.837 -24.003  1.00 68.36           C  
ANISOU 2690  CG2 ILE B  36     7824  11567   6582   2266   1157    593       C  
ATOM   2691  CD1 ILE B  36      49.340  -8.960 -24.556  1.00 78.86           C  
ANISOU 2691  CD1 ILE B  36     8837  13295   7830   1290    759    197       C  
ATOM   2692  N   ASP B  37      46.280 -12.929 -22.970  1.00 47.26           N  
ANISOU 2692  N   ASP B  37     5849   7969   4138   2318   1119    579       N  
ATOM   2693  CA  ASP B  37      45.105 -13.533 -23.583  1.00 50.07           C  
ANISOU 2693  CA  ASP B  37     6681   7730   4615   2207   1226    466       C  
ATOM   2694  C   ASP B  37      43.915 -13.469 -22.630  1.00 49.11           C  
ANISOU 2694  C   ASP B  37     6670   7434   4558   2107   1061    449       C  
ATOM   2695  O   ASP B  37      42.756 -13.323 -23.055  1.00 39.72           O  
ANISOU 2695  O   ASP B  37     5750   5896   3446   1815    985    295       O  
ATOM   2696  CB  ASP B  37      45.406 -14.986 -23.978  1.00 58.11           C  
ANISOU 2696  CB  ASP B  37     7954   8467   5658   2591   1642    586       C  
ATOM   2697  CG  ASP B  37      46.401 -15.084 -25.112  1.00 67.22           C  
ANISOU 2697  CG  ASP B  37     9078   9699   6764   2651   1847    563       C  
ATOM   2698  OD1 ASP B  37      46.930 -14.028 -25.513  1.00 73.46           O  
ANISOU 2698  OD1 ASP B  37     9606  10813   7491   2409   1647    478       O  
ATOM   2699  OD2 ASP B  37      46.667 -16.208 -25.597  1.00 69.33           O  
ANISOU 2699  OD2 ASP B  37     9599   9686   7058   2934   2244    625       O  
ATOM   2700  N   GLU B  38      44.211 -13.562 -21.336  1.00 46.28           N  
ANISOU 2700  N   GLU B  38     6069   7376   4141   2347   1005    619       N  
ATOM   2701  CA  GLU B  38      43.177 -13.519 -20.317  1.00 43.91           C  
ANISOU 2701  CA  GLU B  38     5845   6955   3882   2282    868    619       C  
ATOM   2702  C   GLU B  38      42.586 -12.122 -20.198  1.00 41.91           C  
ANISOU 2702  C   GLU B  38     5499   6774   3653   1844    559    422       C  
ATOM   2703  O   GLU B  38      41.370 -11.971 -20.075  1.00 39.37           O  
ANISOU 2703  O   GLU B  38     5381   6150   3427   1653    472    330       O  
ATOM   2704  CB  GLU B  38      43.724 -13.982 -18.964  1.00 52.96           C  
ANISOU 2704  CB  GLU B  38     6740   8467   4917   2662    899    875       C  
ATOM   2705  CG  GLU B  38      42.665 -14.059 -17.870  1.00 64.92           C  
ANISOU 2705  CG  GLU B  38     8356   9849   6462   2624    797    890       C  
ATOM   2706  CD  GLU B  38      41.708 -15.242 -18.018  1.00 73.85           C  
ANISOU 2706  CD  GLU B  38     9928  10408   7723   2749   1043    929       C  
ATOM   2707  OE1 GLU B  38      42.019 -16.199 -18.760  1.00 73.55           O  
ANISOU 2707  OE1 GLU B  38    10116  10101   7728   2961   1355    993       O  
ATOM   2708  OE2 GLU B  38      40.633 -15.209 -17.380  1.00 79.49           O  
ANISOU 2708  OE2 GLU B  38    10775  10935   8492   2611    954    879       O  
ATOM   2709  N   LYS B  39      43.444 -11.104 -20.248  1.00 44.59           N  
ANISOU 2709  N   LYS B  39     5534   7504   3904   1685    431    361       N  
ATOM   2710  CA  LYS B  39      42.986  -9.720 -20.200  1.00 33.75           C  
ANISOU 2710  CA  LYS B  39     4115   6144   2566   1274    221    175       C  
ATOM   2711  C   LYS B  39      42.054  -9.387 -21.358  1.00 40.46           C  
ANISOU 2711  C   LYS B  39     5260   6565   3549   1025    205     55       C  
ATOM   2712  O   LYS B  39      41.031  -8.739 -21.166  1.00 45.81           O  
ANISOU 2712  O   LYS B  39     6041   7052   4315    818     87    -20       O  
ATOM   2713  CB  LYS B  39      44.167  -8.763 -20.211  1.00 38.45           C  
ANISOU 2713  CB  LYS B  39     4376   7198   3035   1106    162    110       C  
ATOM   2714  CG  LYS B  39      43.789  -7.319 -20.035  1.00 34.00           C  
ANISOU 2714  CG  LYS B  39     3795   6618   2507    687     25    -83       C  
ATOM   2715  CD  LYS B  39      45.007  -6.531 -19.585  1.00 41.26           C  
ANISOU 2715  CD  LYS B  39     4346   8084   3247    505     -5   -161       C  
ATOM   2716  CE  LYS B  39      44.618  -5.165 -19.069  1.00 41.44           C  
ANISOU 2716  CE  LYS B  39     4382   8074   3289     86    -75   -372       C  
ATOM   2717  NZ  LYS B  39      45.758  -4.451 -18.424  1.00 46.14           N  
ANISOU 2717  NZ  LYS B  39     4615   9254   3662   -168    -89   -496       N  
ATOM   2718  N   ILE B  40      42.415  -9.825 -22.557  1.00 34.17           N  
ANISOU 2718  N   ILE B  40     4581   5656   2747   1056    335     53       N  
ATOM   2719  CA  ILE B  40      41.549  -9.647 -23.712  1.00 33.91           C  
ANISOU 2719  CA  ILE B  40     4807   5297   2779    828    322    -35       C  
ATOM   2720  C   ILE B  40      40.227 -10.382 -23.502  1.00 30.05           C  
ANISOU 2720  C   ILE B  40     4571   4487   2360    839    331    -34       C  
ATOM   2721  O   ILE B  40      39.160  -9.833 -23.748  1.00 32.04           O  
ANISOU 2721  O   ILE B  40     4916   4590   2668    616    206    -82       O  
ATOM   2722  CB  ILE B  40      42.221 -10.140 -25.022  1.00 34.63           C  
ANISOU 2722  CB  ILE B  40     4994   5354   2809    855    495    -53       C  
ATOM   2723  CG1 ILE B  40      43.486  -9.330 -25.309  1.00 34.61           C  
ANISOU 2723  CG1 ILE B  40     4728   5687   2736    798    487    -63       C  
ATOM   2724  CG2 ILE B  40      41.261 -10.004 -26.199  1.00 31.46           C  
ANISOU 2724  CG2 ILE B  40     4845   4693   2417    592    466   -138       C  
ATOM   2725  CD1 ILE B  40      44.289  -9.832 -26.489  1.00 35.13           C  
ANISOU 2725  CD1 ILE B  40     4850   5766   2732    863    683    -69       C  
ATOM   2726  N   TYR B  41      40.301 -11.620 -23.040  1.00 31.26           N  
ANISOU 2726  N   TYR B  41     4825   4547   2504   1105    504     42       N  
ATOM   2727  CA  TYR B  41      39.096 -12.407 -22.788  1.00 30.83           C  
ANISOU 2727  CA  TYR B  41     5022   4184   2506   1087    558     28       C  
ATOM   2728  C   TYR B  41      38.230 -11.710 -21.735  1.00 33.33           C  
ANISOU 2728  C   TYR B  41     5239   4538   2886    994    350     35       C  
ATOM   2729  O   TYR B  41      37.011 -11.600 -21.891  1.00 27.99           O  
ANISOU 2729  O   TYR B  41     4689   3681   2263    797    272    -20       O  
ATOM   2730  CB  TYR B  41      39.454 -13.831 -22.346  1.00 36.75           C  
ANISOU 2730  CB  TYR B  41     5918   4799   3247   1427    845    137       C  
ATOM   2731  CG  TYR B  41      38.269 -14.655 -21.887  1.00 42.34           C  
ANISOU 2731  CG  TYR B  41     6886   5190   4011   1396    936    124       C  
ATOM   2732  CD1 TYR B  41      37.374 -15.192 -22.799  1.00 44.39           C  
ANISOU 2732  CD1 TYR B  41     7446   5149   4269   1131   1045    -28       C  
ATOM   2733  CD2 TYR B  41      38.036 -14.878 -20.536  1.00 48.63           C  
ANISOU 2733  CD2 TYR B  41     7614   6029   4834   1590    917    252       C  
ATOM   2734  CE1 TYR B  41      36.283 -15.935 -22.380  1.00 46.69           C  
ANISOU 2734  CE1 TYR B  41     7963   5180   4598   1043   1144    -63       C  
ATOM   2735  CE2 TYR B  41      36.951 -15.623 -20.106  1.00 52.14           C  
ANISOU 2735  CE2 TYR B  41     8300   6181   5331   1542   1020    240       C  
ATOM   2736  CZ  TYR B  41      36.079 -16.151 -21.031  1.00 55.51           C  
ANISOU 2736  CZ  TYR B  41     9023   6301   5769   1259   1138     75       C  
ATOM   2737  OH  TYR B  41      34.997 -16.890 -20.602  1.00 61.54           O  
ANISOU 2737  OH  TYR B  41    10013   6800   6570   1155   1257     41       O  
ATOM   2738  N   ARG B  42      38.861 -11.220 -20.673  1.00 32.54           N  
ANISOU 2738  N   ARG B  42     4891   4714   2758   1118    268     99       N  
ATOM   2739  CA  ARG B  42      38.126 -10.531 -19.611  1.00 34.73           C  
ANISOU 2739  CA  ARG B  42     5085   5033   3080   1023    110     82       C  
ATOM   2740  C   ARG B  42      37.464  -9.252 -20.122  1.00 33.19           C  
ANISOU 2740  C   ARG B  42     4883   4767   2961    718    -38    -19       C  
ATOM   2741  O   ARG B  42      36.338  -8.917 -19.736  1.00 28.92           O  
ANISOU 2741  O   ARG B  42     4400   4087   2502    618   -113    -34       O  
ATOM   2742  CB  ARG B  42      39.053 -10.217 -18.438  1.00 31.92           C  
ANISOU 2742  CB  ARG B  42     4449   5059   2620   1157     66    138       C  
ATOM   2743  CG  ARG B  42      39.469 -11.455 -17.689  1.00 41.23           C  
ANISOU 2743  CG  ARG B  42     5617   6328   3722   1523    210    318       C  
ATOM   2744  CD  ARG B  42      38.252 -12.225 -17.196  1.00 41.08           C  
ANISOU 2744  CD  ARG B  42     5842   5980   3784   1575    273    356       C  
ATOM   2745  NE  ARG B  42      38.613 -13.551 -16.702  1.00 39.05           N  
ANISOU 2745  NE  ARG B  42     5665   5694   3478   1952    496    558       N  
ATOM   2746  CZ  ARG B  42      37.737 -14.479 -16.330  1.00 41.79           C  
ANISOU 2746  CZ  ARG B  42     6267   5724   3886   2037    641    617       C  
ATOM   2747  NH1 ARG B  42      36.430 -14.232 -16.379  1.00 38.38           N  
ANISOU 2747  NH1 ARG B  42     5991   5039   3554   1756    554    479       N  
ATOM   2748  NH2 ARG B  42      38.170 -15.659 -15.910  1.00 45.99           N  
ANISOU 2748  NH2 ARG B  42     6897   6201   4379   2416    901    833       N  
ATOM   2749  N   PHE B  43      38.155  -8.537 -21.000  1.00 26.69           N  
ANISOU 2749  N   PHE B  43     3992   4037   2113    595    -52    -63       N  
ATOM   2750  CA  PHE B  43      37.575  -7.320 -21.555  1.00 25.83           C  
ANISOU 2750  CA  PHE B  43     3902   3835   2078    354   -141   -105       C  
ATOM   2751  C   PHE B  43      36.269  -7.598 -22.307  1.00 28.96           C  
ANISOU 2751  C   PHE B  43     4476   4002   2524    270   -172    -71       C  
ATOM   2752  O   PHE B  43      35.285  -6.859 -22.177  1.00 24.51           O  
ANISOU 2752  O   PHE B  43     3917   3352   2046    175   -247    -40       O  
ATOM   2753  CB  PHE B  43      38.577  -6.627 -22.482  1.00 26.60           C  
ANISOU 2753  CB  PHE B  43     3927   4053   2126    240   -112   -138       C  
ATOM   2754  CG  PHE B  43      37.996  -5.460 -23.211  1.00 28.51           C  
ANISOU 2754  CG  PHE B  43     4231   4161   2441     37   -151   -126       C  
ATOM   2755  CD1 PHE B  43      37.660  -4.288 -22.526  1.00 27.98           C  
ANISOU 2755  CD1 PHE B  43     4127   4040   2465    -73   -162   -151       C  
ATOM   2756  CD2 PHE B  43      37.754  -5.536 -24.573  1.00 26.44           C  
ANISOU 2756  CD2 PHE B  43     4077   3824   2144    -35   -144    -75       C  
ATOM   2757  CE1 PHE B  43      37.096  -3.208 -23.192  1.00 29.66           C  
ANISOU 2757  CE1 PHE B  43     4419   4087   2763   -196   -140    -84       C  
ATOM   2758  CE2 PHE B  43      37.205  -4.444 -25.246  1.00 34.31           C  
ANISOU 2758  CE2 PHE B  43     5114   4731   3192   -170   -167      4       C  
ATOM   2759  CZ  PHE B  43      36.887  -3.282 -24.546  1.00 26.67           C  
ANISOU 2759  CZ  PHE B  43     4117   3671   2344   -223   -151     18       C  
ATOM   2760  N   GLU B  44      36.263  -8.659 -23.105  1.00 26.70           N  
ANISOU 2760  N   GLU B  44     4327   3648   2169    295    -91    -77       N  
ATOM   2761  CA  GLU B  44      35.091  -8.989 -23.905  1.00 28.68           C  
ANISOU 2761  CA  GLU B  44     4718   3778   2402    143   -118    -75       C  
ATOM   2762  C   GLU B  44      33.887  -9.289 -23.018  1.00 26.03           C  
ANISOU 2762  C   GLU B  44     4408   3348   2135    147   -162    -55       C  
ATOM   2763  O   GLU B  44      32.757  -8.914 -23.339  1.00 30.14           O  
ANISOU 2763  O   GLU B  44     4914   3865   2670      8   -256    -13       O  
ATOM   2764  CB  GLU B  44      35.380 -10.184 -24.818  1.00 29.62           C  
ANISOU 2764  CB  GLU B  44     5018   3830   2407    120     37   -144       C  
ATOM   2765  CG  GLU B  44      36.467  -9.922 -25.845  1.00 29.81           C  
ANISOU 2765  CG  GLU B  44     5024   3952   2349     96     95   -166       C  
ATOM   2766  CD  GLU B  44      36.122  -8.793 -26.786  1.00 39.95           C  
ANISOU 2766  CD  GLU B  44     6246   5332   3602   -105    -39   -119       C  
ATOM   2767  OE1 GLU B  44      34.934  -8.593 -27.070  1.00 35.94           O  
ANISOU 2767  OE1 GLU B  44     5754   4824   3077   -246   -144    -73       O  
ATOM   2768  OE2 GLU B  44      37.049  -8.101 -27.250  1.00 53.37           O  
ANISOU 2768  OE2 GLU B  44     7866   7131   5281   -112    -26   -104       O  
ATOM   2769  N   ILE B  45      34.137  -9.984 -21.916  1.00 25.16           N  
ANISOU 2769  N   ILE B  45     4315   3196   2049    323    -84    -59       N  
ATOM   2770  CA  ILE B  45      33.087 -10.322 -20.983  1.00 24.77           C  
ANISOU 2770  CA  ILE B  45     4296   3058   2058    335   -100    -41       C  
ATOM   2771  C   ILE B  45      32.609  -9.066 -20.266  1.00 27.48           C  
ANISOU 2771  C   ILE B  45     4482   3463   2497    311   -231     -4       C  
ATOM   2772  O   ILE B  45      31.401  -8.853 -20.096  1.00 26.15           O  
ANISOU 2772  O   ILE B  45     4303   3245   2387    231   -288     29       O  
ATOM   2773  CB  ILE B  45      33.567 -11.345 -19.957  1.00 26.60           C  
ANISOU 2773  CB  ILE B  45     4589   3241   2275    563     41    -14       C  
ATOM   2774  CG1 ILE B  45      33.884 -12.670 -20.638  1.00 30.58           C  
ANISOU 2774  CG1 ILE B  45     5318   3588   2714    608    260    -43       C  
ATOM   2775  CG2 ILE B  45      32.535 -11.515 -18.866  1.00 28.43           C  
ANISOU 2775  CG2 ILE B  45     4833   3404   2567    573     19     12       C  
ATOM   2776  CD1 ILE B  45      34.099 -13.789 -19.660  1.00 40.82           C  
ANISOU 2776  CD1 ILE B  45     6730   4768   4013    861    458     37       C  
ATOM   2777  N   PHE B  46      33.574  -8.254 -19.849  1.00 23.65           N  
ANISOU 2777  N   PHE B  46     3874   3094   2017    366   -248    -19       N  
ATOM   2778  CA  PHE B  46      33.326  -6.935 -19.247  1.00 23.29           C  
ANISOU 2778  CA  PHE B  46     3725   3066   2056    305   -300    -27       C  
ATOM   2779  C   PHE B  46      32.399  -6.098 -20.107  1.00 25.61           C  
ANISOU 2779  C   PHE B  46     4034   3268   2430    190   -344     46       C  
ATOM   2780  O   PHE B  46      31.413  -5.555 -19.637  1.00 26.66           O  
ANISOU 2780  O   PHE B  46     4143   3327   2660    189   -354     96       O  
ATOM   2781  CB  PHE B  46      34.657  -6.187 -19.064  1.00 27.67           C  
ANISOU 2781  CB  PHE B  46     4169   3784   2563    277   -277    -98       C  
ATOM   2782  CG  PHE B  46      34.526  -4.803 -18.441  1.00 30.51           C  
ANISOU 2782  CG  PHE B  46     4477   4118   2997    156   -255   -159       C  
ATOM   2783  CD1 PHE B  46      34.416  -4.651 -17.069  1.00 24.38           C  
ANISOU 2783  CD1 PHE B  46     3648   3407   2209    166   -238   -230       C  
ATOM   2784  CD2 PHE B  46      34.553  -3.661 -19.235  1.00 24.62           C  
ANISOU 2784  CD2 PHE B  46     3761   3271   2323     25   -211   -148       C  
ATOM   2785  CE1 PHE B  46      34.325  -3.391 -16.498  1.00 25.15           C  
ANISOU 2785  CE1 PHE B  46     3743   3448   2366     16   -158   -330       C  
ATOM   2786  CE2 PHE B  46      34.441  -2.405 -18.676  1.00 31.25           C  
ANISOU 2786  CE2 PHE B  46     4615   4012   3247    -90   -110   -215       C  
ATOM   2787  CZ  PHE B  46      34.333  -2.272 -17.297  1.00 32.49           C  
ANISOU 2787  CZ  PHE B  46     4738   4216   3392   -111    -74   -328       C  
ATOM   2788  N   LYS B  47      32.768  -5.984 -21.377  1.00 26.65           N  
ANISOU 2788  N   LYS B  47     4189   3430   2506    118   -353     76       N  
ATOM   2789  CA  LYS B  47      31.983  -5.290 -22.386  1.00 24.33           C  
ANISOU 2789  CA  LYS B  47     3888   3120   2234     37   -395    203       C  
ATOM   2790  C   LYS B  47      30.535  -5.772 -22.418  1.00 30.43           C  
ANISOU 2790  C   LYS B  47     4646   3907   3007     18   -459    286       C  
ATOM   2791  O   LYS B  47      29.594  -4.974 -22.459  1.00 33.37           O  
ANISOU 2791  O   LYS B  47     4940   4282   3456     40   -482    431       O  
ATOM   2792  CB  LYS B  47      32.614  -5.510 -23.761  1.00 24.84           C  
ANISOU 2792  CB  LYS B  47     3995   3269   2174    -48   -397    209       C  
ATOM   2793  CG  LYS B  47      33.246  -4.322 -24.403  1.00 46.32           C  
ANISOU 2793  CG  LYS B  47     6694   5992   4915    -91   -359    269       C  
ATOM   2794  CD  LYS B  47      33.784  -4.707 -25.788  1.00 46.25           C  
ANISOU 2794  CD  LYS B  47     6731   6090   4752   -182   -361    274       C  
ATOM   2795  CE  LYS B  47      32.685  -5.258 -26.681  1.00 57.41           C  
ANISOU 2795  CE  LYS B  47     8161   7607   6044   -269   -445    363       C  
ATOM   2796  NZ  LYS B  47      33.214  -6.008 -27.856  1.00 66.42           N  
ANISOU 2796  NZ  LYS B  47     9386   8856   6994   -394   -419    289       N  
ATOM   2797  N   ASP B  48      30.364  -7.088 -22.418  1.00 29.79           N  
ANISOU 2797  N   ASP B  48     4641   3842   2837    -25   -454    203       N  
ATOM   2798  CA  ASP B  48      29.053  -7.667 -22.602  1.00 31.20           C  
ANISOU 2798  CA  ASP B  48     4803   4083   2970   -131   -501    243       C  
ATOM   2799  C   ASP B  48      28.217  -7.441 -21.357  1.00 34.13           C  
ANISOU 2799  C   ASP B  48     5104   4395   3469    -39   -501    281       C  
ATOM   2800  O   ASP B  48      27.027  -7.113 -21.438  1.00 31.37           O  
ANISOU 2800  O   ASP B  48     4635   4142   3143    -71   -557    400       O  
ATOM   2801  CB  ASP B  48      29.162  -9.146 -22.938  1.00 43.45           C  
ANISOU 2801  CB  ASP B  48     6514   5606   4389   -251   -424    104       C  
ATOM   2802  CG  ASP B  48      29.705  -9.376 -24.340  1.00 73.21           C  
ANISOU 2802  CG  ASP B  48    10355   9460   8001   -393   -408     60       C  
ATOM   2803  OD1 ASP B  48      29.714  -8.410 -25.137  1.00 82.41           O  
ANISOU 2803  OD1 ASP B  48    11412  10762   9136   -422   -499    175       O  
ATOM   2804  OD2 ASP B  48      30.119 -10.514 -24.650  1.00 82.15           O  
ANISOU 2804  OD2 ASP B  48    11669  10506   9038   -467   -273    -81       O  
ATOM   2805  N   ASN B  49      28.842  -7.599 -20.200  1.00 23.68           N  
ANISOU 2805  N   ASN B  49     3829   2959   2209     83   -435    195       N  
ATOM   2806  CA  ASN B  49      28.160  -7.285 -18.973  1.00 27.65           C  
ANISOU 2806  CA  ASN B  49     4276   3410   2820    164   -417    215       C  
ATOM   2807  C   ASN B  49      27.786  -5.811 -18.917  1.00 30.17           C  
ANISOU 2807  C   ASN B  49     4492   3708   3262    216   -414    319       C  
ATOM   2808  O   ASN B  49      26.712  -5.467 -18.431  1.00 36.19           O  
ANISOU 2808  O   ASN B  49     5179   4462   4112    260   -400    403       O  
ATOM   2809  CB  ASN B  49      29.018  -7.667 -17.771  1.00 30.29           C  
ANISOU 2809  CB  ASN B  49     4664   3698   3148    276   -350    116       C  
ATOM   2810  CG  ASN B  49      28.952  -9.139 -17.458  1.00 26.30           C  
ANISOU 2810  CG  ASN B  49     4277   3148   2568    297   -285     81       C  
ATOM   2811  OD1 ASN B  49      28.010  -9.812 -17.839  1.00 27.95           O  
ANISOU 2811  OD1 ASN B  49     4535   3328   2756    181   -275     89       O  
ATOM   2812  ND2 ASN B  49      29.946  -9.642 -16.737  1.00 27.03           N  
ANISOU 2812  ND2 ASN B  49     4409   3253   2606    440   -217     53       N  
ATOM   2813  N   LEU B  50      28.662  -4.942 -19.418  1.00 30.60           N  
ANISOU 2813  N   LEU B  50     4557   3738   3330    217   -389    322       N  
ATOM   2814  CA  LEU B  50      28.388  -3.512 -19.404  1.00 24.73           C  
ANISOU 2814  CA  LEU B  50     3779   2898   2718    271   -307    425       C  
ATOM   2815  C   LEU B  50      27.142  -3.186 -20.208  1.00 29.57           C  
ANISOU 2815  C   LEU B  50     4287   3589   3357    318   -345    664       C  
ATOM   2816  O   LEU B  50      26.305  -2.377 -19.783  1.00 32.55           O  
ANISOU 2816  O   LEU B  50     4607   3891   3868    440   -253    797       O  
ATOM   2817  CB  LEU B  50      29.575  -2.732 -19.960  1.00 26.08           C  
ANISOU 2817  CB  LEU B  50     4005   3024   2880    218   -245    384       C  
ATOM   2818  CG  LEU B  50      29.392  -1.211 -20.020  1.00 32.05           C  
ANISOU 2818  CG  LEU B  50     4794   3601   3783    260    -80    489       C  
ATOM   2819  CD1 LEU B  50      28.919  -0.691 -18.683  1.00 32.82           C  
ANISOU 2819  CD1 LEU B  50     4918   3547   4006    309     58    415       C  
ATOM   2820  CD2 LEU B  50      30.685  -0.526 -20.422  1.00 33.03           C  
ANISOU 2820  CD2 LEU B  50     4996   3671   3884    145     14    394       C  
ATOM   2821  N   LYS B  51      27.049  -3.793 -21.385  1.00 26.38           N  
ANISOU 2821  N   LYS B  51     3848   3369   2807    225   -460    728       N  
ATOM   2822  CA  LYS B  51      25.894  -3.636 -22.242  1.00 34.89           C  
ANISOU 2822  CA  LYS B  51     4768   4661   3827    232   -535    967       C  
ATOM   2823  C   LYS B  51      24.643  -4.057 -21.497  1.00 38.68           C  
ANISOU 2823  C   LYS B  51     5127   5227   4343    256   -556   1006       C  
ATOM   2824  O   LYS B  51      23.636  -3.348 -21.526  1.00 36.63           O  
ANISOU 2824  O   LYS B  51     4702   5063   4154    394   -532   1244       O  
ATOM   2825  CB  LYS B  51      26.045  -4.458 -23.518  1.00 33.90           C  
ANISOU 2825  CB  LYS B  51     4637   4772   3472     41   -657    949       C  
ATOM   2826  CG  LYS B  51      24.861  -4.378 -24.453  1.00 47.11           C  
ANISOU 2826  CG  LYS B  51     6095   6799   5004     -7   -765   1191       C  
ATOM   2827  CD  LYS B  51      24.843  -5.566 -25.403  1.00 60.57           C  
ANISOU 2827  CD  LYS B  51     7818   8757   6437   -305   -869   1056       C  
ATOM   2828  CE  LYS B  51      26.192  -5.771 -26.069  1.00 60.67           C  
ANISOU 2828  CE  LYS B  51     8026   8650   6375   -383   -830    905       C  
ATOM   2829  NZ  LYS B  51      26.285  -7.094 -26.744  1.00 58.94           N  
ANISOU 2829  NZ  LYS B  51     7911   8560   5923   -679   -846    691       N  
ATOM   2830  N   TYR B  52      24.713  -5.208 -20.829  1.00 32.96           N  
ANISOU 2830  N   TYR B  52     4484   4468   3572    144   -574    797       N  
ATOM   2831  CA  TYR B  52      23.567  -5.723 -20.090  1.00 31.75           C  
ANISOU 2831  CA  TYR B  52     4234   4391   3440    126   -577    807       C  
ATOM   2832  C   TYR B  52      23.164  -4.762 -18.979  1.00 35.89           C  
ANISOU 2832  C   TYR B  52     4714   4756   4166    338   -459    881       C  
ATOM   2833  O   TYR B  52      21.972  -4.514 -18.749  1.00 30.23           O  
ANISOU 2833  O   TYR B  52     3821   4163   3502    412   -444   1040       O  
ATOM   2834  CB  TYR B  52      23.866  -7.102 -19.486  1.00 36.16           C  
ANISOU 2834  CB  TYR B  52     4950   4860   3928     -8   -555    576       C  
ATOM   2835  CG  TYR B  52      22.677  -7.678 -18.736  1.00 38.74           C  
ANISOU 2835  CG  TYR B  52     5196   5257   4269    -65   -535    578       C  
ATOM   2836  CD1 TYR B  52      21.590  -8.199 -19.427  1.00 38.74           C  
ANISOU 2836  CD1 TYR B  52     5042   5543   4133   -272   -606    637       C  
ATOM   2837  CD2 TYR B  52      22.634  -7.686 -17.343  1.00 33.31           C  
ANISOU 2837  CD2 TYR B  52     4564   4394   3698     56   -441    517       C  
ATOM   2838  CE1 TYR B  52      20.496  -8.715 -18.762  1.00 40.52           C  
ANISOU 2838  CE1 TYR B  52     5171   5863   4361   -360   -576    632       C  
ATOM   2839  CE2 TYR B  52      21.538  -8.200 -16.661  1.00 27.24           C  
ANISOU 2839  CE2 TYR B  52     3721   3690   2940     -2   -406    524       C  
ATOM   2840  CZ  TYR B  52      20.470  -8.717 -17.386  1.00 37.70           C  
ANISOU 2840  CZ  TYR B  52     4891   5285   4149   -213   -470    581       C  
ATOM   2841  OH  TYR B  52      19.366  -9.231 -16.752  1.00 32.08           O  
ANISOU 2841  OH  TYR B  52     4082   4674   3435   -311   -426    580       O  
ATOM   2842  N   ILE B  53      24.170  -4.221 -18.303  1.00 28.89           N  
ANISOU 2842  N   ILE B  53     3978   3625   3374    415   -358    756       N  
ATOM   2843  CA  ILE B  53      23.960  -3.344 -17.172  1.00 29.92           C  
ANISOU 2843  CA  ILE B  53     4128   3571   3670    554   -199    748       C  
ATOM   2844  C   ILE B  53      23.293  -2.062 -17.619  1.00 35.84           C  
ANISOU 2844  C   ILE B  53     4785   4281   4553    728    -84   1002       C  
ATOM   2845  O   ILE B  53      22.324  -1.594 -17.017  1.00 31.47           O  
ANISOU 2845  O   ILE B  53     4145   3692   4121    875     34   1118       O  
ATOM   2846  CB  ILE B  53      25.293  -3.026 -16.480  1.00 28.84           C  
ANISOU 2846  CB  ILE B  53     4158   3259   3542    518   -115    530       C  
ATOM   2847  CG1 ILE B  53      25.733  -4.217 -15.623  1.00 27.00           C  
ANISOU 2847  CG1 ILE B  53     3984   3076   3199    449   -174    347       C  
ATOM   2848  CG2 ILE B  53      25.164  -1.773 -15.614  1.00 27.03           C  
ANISOU 2848  CG2 ILE B  53     3983   2819   3470    605    104    508       C  
ATOM   2849  CD1 ILE B  53      27.229  -4.223 -15.276  1.00 23.84           C  
ANISOU 2849  CD1 ILE B  53     3674   2671   2715    398   -161    171       C  
ATOM   2850  N   ASP B  54      23.823  -1.506 -18.698  1.00 29.64           N  
ANISOU 2850  N   ASP B  54     4021   3499   3742    737    -92   1112       N  
ATOM   2851  CA  ASP B  54      23.328  -0.258 -19.248  1.00 41.47           C  
ANISOU 2851  CA  ASP B  54     5461   4935   5360    943     57   1407       C  
ATOM   2852  C   ASP B  54      21.864  -0.371 -19.681  1.00 43.99           C  
ANISOU 2852  C   ASP B  54     5501   5562   5651   1083    -15   1722       C  
ATOM   2853  O   ASP B  54      21.057   0.516 -19.405  1.00 45.34           O  
ANISOU 2853  O   ASP B  54     5589   5660   5979   1339    172   1960       O  
ATOM   2854  CB  ASP B  54      24.216   0.158 -20.421  1.00 38.32           C  
ANISOU 2854  CB  ASP B  54     5138   4531   4893    897     38   1474       C  
ATOM   2855  CG  ASP B  54      24.101   1.625 -20.751  1.00 54.60           C  
ANISOU 2855  CG  ASP B  54     7257   6371   7116   1116    297   1733       C  
ATOM   2856  OD1 ASP B  54      23.462   1.957 -21.774  1.00 59.16           O  
ANISOU 2856  OD1 ASP B  54     7679   7151   7648   1274    267   2091       O  
ATOM   2857  OD2 ASP B  54      24.658   2.442 -19.992  1.00 59.58           O  
ANISOU 2857  OD2 ASP B  54     8095   6640   7903   1119    551   1581       O  
ATOM   2858  N   GLU B  55      21.530  -1.474 -20.347  1.00 41.68           N  
ANISOU 2858  N   GLU B  55     5060   5630   5146    900   -258   1717       N  
ATOM   2859  CA  GLU B  55      20.179  -1.690 -20.850  1.00 45.09           C  
ANISOU 2859  CA  GLU B  55     5170   6483   5477    946   -363   1991       C  
ATOM   2860  C   GLU B  55      19.193  -1.977 -19.722  1.00 38.53           C  
ANISOU 2860  C   GLU B  55     4227   5674   4741    998   -304   1962       C  
ATOM   2861  O   GLU B  55      18.054  -1.519 -19.748  1.00 46.73           O  
ANISOU 2861  O   GLU B  55     4999   6936   5821   1198   -254   2261       O  
ATOM   2862  CB  GLU B  55      20.167  -2.837 -21.869  1.00 52.88           C  
ANISOU 2862  CB  GLU B  55     6066   7856   6170    632   -610   1913       C  
ATOM   2863  CG  GLU B  55      21.011  -2.571 -23.116  1.00 64.46           C  
ANISOU 2863  CG  GLU B  55     7606   9379   7507    576   -673   1974       C  
ATOM   2864  CD  GLU B  55      21.059  -3.755 -24.075  1.00 75.54           C  
ANISOU 2864  CD  GLU B  55     8970  11129   8604    220   -871   1833       C  
ATOM   2865  OE1 GLU B  55      21.004  -4.916 -23.608  1.00 77.91           O  
ANISOU 2865  OE1 GLU B  55     9351  11413   8838    -21   -908   1552       O  
ATOM   2866  OE2 GLU B  55      21.171  -3.522 -25.298  1.00 77.53           O  
ANISOU 2866  OE2 GLU B  55     9136  11649   8672    173   -957   1998       O  
ATOM   2867  N   THR B  56      19.635  -2.726 -18.722  1.00 38.68           N  
ANISOU 2867  N   THR B  56     4433   5481   4783    842   -295   1631       N  
ATOM   2868  CA  THR B  56      18.755  -3.131 -17.637  1.00 35.25           C  
ANISOU 2868  CA  THR B  56     3914   5069   4410    852   -240   1578       C  
ATOM   2869  C   THR B  56      18.447  -1.962 -16.698  1.00 45.25           C  
ANISOU 2869  C   THR B  56     5210   6063   5920   1149     21   1677       C  
ATOM   2870  O   THR B  56      17.322  -1.838 -16.208  1.00 52.34           O  
ANISOU 2870  O   THR B  56     5912   7088   6888   1281    102   1825       O  
ATOM   2871  CB  THR B  56      19.360  -4.311 -16.845  1.00 42.93           C  
ANISOU 2871  CB  THR B  56     5099   5898   5316    621   -282   1231       C  
ATOM   2872  OG1 THR B  56      19.613  -5.406 -17.739  1.00 34.02           O  
ANISOU 2872  OG1 THR B  56     3988   4961   3976    351   -449   1134       O  
ATOM   2873  CG2 THR B  56      18.410  -4.775 -15.745  1.00 47.66           C  
ANISOU 2873  CG2 THR B  56     5618   6531   5960    613   -215   1190       C  
ATOM   2874  N   ASN B  57      19.427  -1.090 -16.470  1.00 37.39           N  
ANISOU 2874  N   ASN B  57     4459   4702   5045   1234    183   1586       N  
ATOM   2875  CA  ASN B  57      19.223   0.072 -15.601  1.00 37.66           C  
ANISOU 2875  CA  ASN B  57     4591   4414   5304   1466    501   1627       C  
ATOM   2876  C   ASN B  57      18.352   1.154 -16.227  1.00 48.88           C  
ANISOU 2876  C   ASN B  57     5842   5875   6856   1805    678   2049       C  
ATOM   2877  O   ASN B  57      18.044   2.160 -15.587  1.00 55.06           O  
ANISOU 2877  O   ASN B  57     6715   6360   7847   2042   1010   2127       O  
ATOM   2878  CB  ASN B  57      20.559   0.701 -15.209  1.00 36.16           C  
ANISOU 2878  CB  ASN B  57     4722   3845   5172   1380    654   1370       C  
ATOM   2879  CG  ASN B  57      21.298  -0.095 -14.162  1.00 35.20           C  
ANISOU 2879  CG  ASN B  57     4747   3675   4954   1148    580    999       C  
ATOM   2880  OD1 ASN B  57      20.742  -0.994 -13.533  1.00 41.95           O  
ANISOU 2880  OD1 ASN B  57     5516   4677   5746   1093    485    935       O  
ATOM   2881  ND2 ASN B  57      22.567   0.229 -13.972  1.00 33.33           N  
ANISOU 2881  ND2 ASN B  57     4715   3263   4684   1008    633    769       N  
ATOM   2882  N   LYS B  58      17.984   0.977 -17.487  1.00 47.33           N  
ANISOU 2882  N   LYS B  58     5408   6049   6526   1839    488   2333       N  
ATOM   2883  CA  LYS B  58      17.135   1.961 -18.147  1.00 59.49           C  
ANISOU 2883  CA  LYS B  58     6733   7716   8153   2213    644   2816       C  
ATOM   2884  C   LYS B  58      15.698   1.773 -17.697  1.00 68.02           C  
ANISOU 2884  C   LYS B  58     7485   9112   9248   2354    668   3000       C  
ATOM   2885  O   LYS B  58      14.920   2.724 -17.641  1.00 78.88           O  
ANISOU 2885  O   LYS B  58     8774  10462  10734   2606    932   3216       O  
ATOM   2886  CB  LYS B  58      17.241   1.853 -19.668  1.00 56.22           C  
ANISOU 2886  CB  LYS B  58     6157   7679   7525   2144    424   3025       C  
ATOM   2887  CG  LYS B  58      18.531   2.403 -20.227  1.00 55.24           C  
ANISOU 2887  CG  LYS B  58     6333   7230   7423   2095    491   2944       C  
ATOM   2888  CD  LYS B  58      18.509   2.415 -21.746  1.00 59.14           C  
ANISOU 2888  CD  LYS B  58     6655   8111   7704   2043    317   3155       C  
ATOM   2889  CE  LYS B  58      19.794   2.992 -22.311  1.00 62.50           C  
ANISOU 2889  CE  LYS B  58     7376   8215   8156   1998    404   3089       C  
ATOM   2890  NZ  LYS B  58      19.722   3.118 -23.791  1.00 68.37           N  
ANISOU 2890  NZ  LYS B  58     7954   9325   8700   1978    274   3312       N  
ATOM   2891  N   LYS B  59      15.362   0.531 -17.371  1.00 62.09           N  
ANISOU 2891  N   LYS B  59     6594   8653   8344   2084    421   2813       N  
ATOM   2892  CA  LYS B  59      14.043   0.197 -16.860  1.00 64.95           C  
ANISOU 2892  CA  LYS B  59     6630   9342   8704   2160    428   2951       C  
ATOM   2893  C   LYS B  59      13.858   0.775 -15.456  1.00 63.84           C  
ANISOU 2893  C   LYS B  59     6669   8766   8821   2356    764   2838       C  
ATOM   2894  O   LYS B  59      14.807   0.865 -14.675  1.00 65.07           O  
ANISOU 2894  O   LYS B  59     7204   8458   9062   2234    878   2488       O  
ATOM   2895  CB  LYS B  59      13.857  -1.316 -16.849  1.00 65.67           C  
ANISOU 2895  CB  LYS B  59     6619   9777   8555   1720    127   2689       C  
ATOM   2896  CG  LYS B  59      14.216  -1.975 -18.174  1.00 69.23           C  
ANISOU 2896  CG  LYS B  59     6989  10584   8731   1438   -166   2689       C  
ATOM   2897  CD  LYS B  59      14.480  -3.470 -18.011  1.00 70.83           C  
ANISOU 2897  CD  LYS B  59     7309  10860   8745    964   -354   2298       C  
ATOM   2898  CE  LYS B  59      15.074  -4.056 -19.292  1.00 70.23           C  
ANISOU 2898  CE  LYS B  59     7263  11007   8415    674   -574   2229       C  
ATOM   2899  NZ  LYS B  59      15.115  -5.544 -19.268  1.00 67.19           N  
ANISOU 2899  NZ  LYS B  59     6970  10726   7831    213   -695   1894       N  
ATOM   2900  N   ASN B  60      12.634   1.171 -15.139  1.00 62.63           N  
ANISOU 2900  N   ASN B  60     6243   8802   8752   2615    932   3104       N  
ATOM   2901  CA  ASN B  60      12.332   1.759 -13.841  1.00 57.73           C  
ANISOU 2901  CA  ASN B  60     5790   7793   8352   2787   1287   2997       C  
ATOM   2902  C   ASN B  60      12.219   0.684 -12.760  1.00 48.90           C  
ANISOU 2902  C   ASN B  60     4691   6701   7187   2532   1188   2673       C  
ATOM   2903  O   ASN B  60      11.145   0.462 -12.213  1.00 56.02           O  
ANISOU 2903  O   ASN B  60     5338   7835   8112   2614   1256   2776       O  
ATOM   2904  CB  ASN B  60      11.043   2.589 -13.940  1.00 59.93           C  
ANISOU 2904  CB  ASN B  60     5835   8266   8670   3059   1514   3343       C  
ATOM   2905  CG  ASN B  60      10.715   3.343 -12.656  1.00 58.06           C  
ANISOU 2905  CG  ASN B  60     5810   7601   8647   3233   1926   3245       C  
ATOM   2906  OD1 ASN B  60      11.576   3.570 -11.805  1.00 59.85           O  
ANISOU 2906  OD1 ASN B  60     6420   7325   8994   3147   2101   2911       O  
ATOM   2907  ND2 ASN B  60       9.458   3.738 -12.520  1.00 63.44           N  
ANISOU 2907  ND2 ASN B  60     6244   8511   9347   3452   2088   3533       N  
ATOM   2908  N   ASN B  61      13.335   0.011 -12.472  1.00 56.94           N  
ANISOU 2908  N   ASN B  61     6027   7503   8104   2183   1034   2267       N  
ATOM   2909  CA  ASN B  61      13.407  -0.985 -11.399  1.00 53.90           C  
ANISOU 2909  CA  ASN B  61     5758   7082   7639   1905    968   1926       C  
ATOM   2910  C   ASN B  61      13.667  -0.331 -10.047  1.00 45.78           C  
ANISOU 2910  C   ASN B  61     5010   5616   6768   2002   1292   1716       C  
ATOM   2911  O   ASN B  61      14.181   0.777  -9.988  1.00 43.75           O  
ANISOU 2911  O   ASN B  61     4965   5003   6656   2169   1544   1714       O  
ATOM   2912  CB  ASN B  61      14.514  -2.006 -11.679  1.00 58.67           C  
ANISOU 2912  CB  ASN B  61     6569   7670   8053   1545    693   1636       C  
ATOM   2913  CG  ASN B  61      14.323  -2.737 -12.991  1.00 65.26           C  
ANISOU 2913  CG  ASN B  61     7184   8913   8701   1374    402   1768       C  
ATOM   2914  OD1 ASN B  61      13.223  -3.187 -13.306  1.00 72.08           O  
ANISOU 2914  OD1 ASN B  61     7716  10193   9479   1326    314   1940       O  
ATOM   2915  ND2 ASN B  61      15.398  -2.859 -13.766  1.00 59.72           N  
ANISOU 2915  ND2 ASN B  61     6654   8126   7911   1248    262   1673       N  
ATOM   2916  N   SER B  62      13.344  -1.020  -8.959  1.00 41.91           N  
ANISOU 2916  N   SER B  62     4545   5149   6229   1862   1311   1521       N  
ATOM   2917  CA  SER B  62      13.641  -0.491  -7.632  1.00 42.00           C  
ANISOU 2917  CA  SER B  62     4830   4803   6327   1890   1602   1280       C  
ATOM   2918  C   SER B  62      15.099  -0.761  -7.245  1.00 39.13           C  
ANISOU 2918  C   SER B  62     4803   4234   5832   1627   1506    927       C  
ATOM   2919  O   SER B  62      15.552  -0.350  -6.184  1.00 39.27           O  
ANISOU 2919  O   SER B  62     5055   4016   5851   1572   1711    682       O  
ATOM   2920  CB  SER B  62      12.696  -1.078  -6.579  1.00 43.44           C  
ANISOU 2920  CB  SER B  62     4895   5123   6488   1858   1679   1234       C  
ATOM   2921  OG  SER B  62      12.958  -2.452  -6.359  1.00 43.61           O  
ANISOU 2921  OG  SER B  62     4941   5323   6306   1547   1411   1061       O  
ATOM   2922  N   TYR B  63      15.830  -1.458  -8.105  1.00 36.94           N  
ANISOU 2922  N   TYR B  63     4529   4089   5416   1457   1205    904       N  
ATOM   2923  CA  TYR B  63      17.262  -1.636  -7.876  1.00 34.72           C  
ANISOU 2923  CA  TYR B  63     4513   3668   5011   1259   1120    628       C  
ATOM   2924  C   TYR B  63      18.041  -1.365  -9.151  1.00 34.36           C  
ANISOU 2924  C   TYR B  63     4489   3610   4956   1246    983    704       C  
ATOM   2925  O   TYR B  63      17.464  -1.191 -10.219  1.00 35.04           O  
ANISOU 2925  O   TYR B  63     4387   3830   5098   1368    919    971       O  
ATOM   2926  CB  TYR B  63      17.574  -3.040  -7.345  1.00 37.67           C  
ANISOU 2926  CB  TYR B  63     4925   4202   5185   1049    918    474       C  
ATOM   2927  CG  TYR B  63      17.372  -4.147  -8.353  1.00 31.67           C  
ANISOU 2927  CG  TYR B  63     4030   3672   4330    943    658    590       C  
ATOM   2928  CD1 TYR B  63      16.106  -4.663  -8.595  1.00 36.93           C  
ANISOU 2928  CD1 TYR B  63     4461   4563   5008    936    622    755       C  
ATOM   2929  CD2 TYR B  63      18.443  -4.675  -9.059  1.00 29.92           C  
ANISOU 2929  CD2 TYR B  63     3914   3463   3990    820    475    517       C  
ATOM   2930  CE1 TYR B  63      15.910  -5.668  -9.516  1.00 32.59           C  
ANISOU 2930  CE1 TYR B  63     3809   4236   4339    760    420    811       C  
ATOM   2931  CE2 TYR B  63      18.257  -5.688  -9.979  1.00 38.26           C  
ANISOU 2931  CE2 TYR B  63     4892   4697   4949    688    291    584       C  
ATOM   2932  CZ  TYR B  63      16.988  -6.180 -10.204  1.00 38.15           C  
ANISOU 2932  CZ  TYR B  63     4667   4895   4931    632    268    714       C  
ATOM   2933  OH  TYR B  63      16.790  -7.193 -11.114  1.00 41.11           O  
ANISOU 2933  OH  TYR B  63     4984   5460   5177    421    118    730       O  
ATOM   2934  N   TRP B  64      19.360  -1.318  -9.043  1.00 32.55           N  
ANISOU 2934  N   TRP B  64     4465   3271   4632   1094    940    482       N  
ATOM   2935  CA  TRP B  64      20.165  -1.121 -10.232  1.00 31.85           C  
ANISOU 2935  CA  TRP B  64     4402   3179   4521   1061    816    537       C  
ATOM   2936  C   TRP B  64      21.393  -2.000 -10.193  1.00 34.12           C  
ANISOU 2936  C   TRP B  64     4791   3559   4613    856    613    334       C  
ATOM   2937  O   TRP B  64      21.831  -2.447  -9.125  1.00 28.93           O  
ANISOU 2937  O   TRP B  64     4220   2930   3843    759    619    140       O  
ATOM   2938  CB  TRP B  64      20.566   0.349 -10.383  1.00 33.67           C  
ANISOU 2938  CB  TRP B  64     4780   3115   4897   1145   1087    534       C  
ATOM   2939  CG  TRP B  64      21.260   0.922  -9.185  1.00 34.24           C  
ANISOU 2939  CG  TRP B  64     5079   2986   4946   1005   1310    220       C  
ATOM   2940  CD1 TRP B  64      22.609   1.048  -8.999  1.00 33.53           C  
ANISOU 2940  CD1 TRP B  64     5141   2878   4721    774   1285    -40       C  
ATOM   2941  CD2 TRP B  64      20.640   1.473  -8.012  1.00 37.61           C  
ANISOU 2941  CD2 TRP B  64     5587   3249   5454   1053   1609    118       C  
ATOM   2942  NE1 TRP B  64      22.865   1.636  -7.779  1.00 35.04           N  
ANISOU 2942  NE1 TRP B  64     5493   2943   4876    636   1533   -312       N  
ATOM   2943  CE2 TRP B  64      21.674   1.901  -7.154  1.00 36.61           C  
ANISOU 2943  CE2 TRP B  64     5675   3023   5210    803   1745   -231       C  
ATOM   2944  CE3 TRP B  64      19.311   1.641  -7.602  1.00 37.89           C  
ANISOU 2944  CE3 TRP B  64     5518   3246   5634   1270   1785    284       C  
ATOM   2945  CZ2 TRP B  64      21.419   2.485  -5.911  1.00 38.71           C  
ANISOU 2945  CZ2 TRP B  64     6088   3135   5484    736   2058   -445       C  
ATOM   2946  CZ3 TRP B  64      19.063   2.219  -6.367  1.00 39.80           C  
ANISOU 2946  CZ3 TRP B  64     5911   3296   5915   1248   2109     89       C  
ATOM   2947  CH2 TRP B  64      20.112   2.637  -5.539  1.00 40.20           C  
ANISOU 2947  CH2 TRP B  64     6210   3229   5835    970   2248   -284       C  
ATOM   2948  N   LEU B  65      21.915  -2.263 -11.381  1.00 28.70           N  
ANISOU 2948  N   LEU B  65     4077   2953   3874    815    443    410       N  
ATOM   2949  CA  LEU B  65      23.116  -3.055 -11.562  1.00 26.94           C  
ANISOU 2949  CA  LEU B  65     3935   2817   3484    673    278    266       C  
ATOM   2950  C   LEU B  65      24.296  -2.116 -11.691  1.00 27.19           C  
ANISOU 2950  C   LEU B  65     4084   2733   3515    610    363    140       C  
ATOM   2951  O   LEU B  65      24.106  -0.904 -11.794  1.00 29.46           O  
ANISOU 2951  O   LEU B  65     4420   2831   3944    666    560    178       O  
ATOM   2952  CB  LEU B  65      23.000  -3.935 -12.806  1.00 26.21           C  
ANISOU 2952  CB  LEU B  65     3762   2879   3319    631     80    392       C  
ATOM   2953  CG  LEU B  65      21.737  -4.791 -12.884  1.00 26.72           C  
ANISOU 2953  CG  LEU B  65     3693   3091   3367    616     16    507       C  
ATOM   2954  CD1 LEU B  65      21.735  -5.587 -14.162  1.00 26.93           C  
ANISOU 2954  CD1 LEU B  65     3671   3280   3281    495   -146    571       C  
ATOM   2955  CD2 LEU B  65      21.665  -5.718 -11.663  1.00 31.19           C  
ANISOU 2955  CD2 LEU B  65     4333   3652   3865    570     46    377       C  
ATOM   2956  N   GLY B  66      25.505  -2.671 -11.701  1.00 26.07           N  
ANISOU 2956  N   GLY B  66     3986   2705   3215    498    247      5       N  
ATOM   2957  CA  GLY B  66      26.710  -1.870 -11.843  1.00 26.55           C  
ANISOU 2957  CA  GLY B  66     4121   2728   3238    384    312   -135       C  
ATOM   2958  C   GLY B  66      27.929  -2.713 -12.160  1.00 30.47           C  
ANISOU 2958  C   GLY B  66     4593   3430   3553    315    144   -200       C  
ATOM   2959  O   GLY B  66      27.876  -3.941 -12.079  1.00 27.04           O  
ANISOU 2959  O   GLY B  66     4124   3123   3025    373     17   -152       O  
ATOM   2960  N   LEU B  67      29.021  -2.053 -12.536  1.00 25.95           N  
ANISOU 2960  N   LEU B  67     4046   2876   2938    196    180   -301       N  
ATOM   2961  CA  LEU B  67      30.294  -2.716 -12.749  1.00 26.28           C  
ANISOU 2961  CA  LEU B  67     4031   3154   2802    145     56   -363       C  
ATOM   2962  C   LEU B  67      30.914  -3.071 -11.412  1.00 27.54           C  
ANISOU 2962  C   LEU B  67     4130   3563   2772     95     49   -506       C  
ATOM   2963  O   LEU B  67      31.929  -2.495 -11.014  1.00 27.36           O  
ANISOU 2963  O   LEU B  67     4060   3718   2618    -78     95   -674       O  
ATOM   2964  CB  LEU B  67      31.250  -1.829 -13.546  1.00 27.30           C  
ANISOU 2964  CB  LEU B  67     4178   3263   2933      6    112   -428       C  
ATOM   2965  CG  LEU B  67      30.756  -1.425 -14.927  1.00 26.01           C  
ANISOU 2965  CG  LEU B  67     4065   2902   2917     65    122   -253       C  
ATOM   2966  CD1 LEU B  67      31.699  -0.395 -15.587  1.00 27.22           C  
ANISOU 2966  CD1 LEU B  67     4269   2995   3078    -92    235   -322       C  
ATOM   2967  CD2 LEU B  67      30.585  -2.680 -15.782  1.00 24.59           C  
ANISOU 2967  CD2 LEU B  67     3836   2828   2678    176    -63   -111       C  
ATOM   2968  N   ASN B  68      30.306  -4.028 -10.719  1.00 25.52           N  
ANISOU 2968  N   ASN B  68     3861   3360   2474    225     -1   -432       N  
ATOM   2969  CA  ASN B  68      30.804  -4.398  -9.405  1.00 26.48           C  
ANISOU 2969  CA  ASN B  68     3914   3758   2388    211     -6   -516       C  
ATOM   2970  C   ASN B  68      31.942  -5.394  -9.572  1.00 29.46           C  
ANISOU 2970  C   ASN B  68     4187   4428   2579    319   -119   -435       C  
ATOM   2971  O   ASN B  68      32.433  -5.583 -10.689  1.00 32.03           O  
ANISOU 2971  O   ASN B  68     4511   4714   2945    351   -166   -376       O  
ATOM   2972  CB  ASN B  68      29.687  -4.961  -8.518  1.00 26.28           C  
ANISOU 2972  CB  ASN B  68     3933   3662   2391    316     26   -452       C  
ATOM   2973  CG  ASN B  68      29.096  -6.259  -9.039  1.00 25.06           C  
ANISOU 2973  CG  ASN B  68     3819   3411   2292    493    -44   -258       C  
ATOM   2974  OD1 ASN B  68      29.690  -6.963  -9.858  1.00 24.57           O  
ANISOU 2974  OD1 ASN B  68     3759   3382   2196    565   -111   -176       O  
ATOM   2975  ND2 ASN B  68      27.899  -6.591  -8.541  1.00 24.92           N  
ANISOU 2975  ND2 ASN B  68     3848   3268   2354    539      6   -203       N  
ATOM   2976  N   VAL B  69      32.328  -6.055  -8.484  1.00 27.63           N  
ANISOU 2976  N   VAL B  69     3868   4494   2138    404   -142   -403       N  
ATOM   2977  CA  VAL B  69      33.501  -6.945  -8.481  1.00 28.57           C  
ANISOU 2977  CA  VAL B  69     3850   4953   2053    566   -210   -280       C  
ATOM   2978  C   VAL B  69      33.398  -8.132  -9.468  1.00 28.36           C  
ANISOU 2978  C   VAL B  69     3927   4717   2130    802   -210    -82       C  
ATOM   2979  O   VAL B  69      34.399  -8.764  -9.788  1.00 33.57           O  
ANISOU 2979  O   VAL B  69     4502   5574   2677    959   -218     28       O  
ATOM   2980  CB  VAL B  69      33.759  -7.476  -7.047  1.00 34.57           C  
ANISOU 2980  CB  VAL B  69     4492   6090   2553    667   -216   -213       C  
ATOM   2981  CG1 VAL B  69      32.696  -8.484  -6.654  1.00 31.10           C  
ANISOU 2981  CG1 VAL B  69     4208   5411   2199    871   -161    -47       C  
ATOM   2982  CG2 VAL B  69      35.145  -8.075  -6.915  1.00 33.86           C  
ANISOU 2982  CG2 VAL B  69     4177   6484   2203    830   -272    -74       C  
ATOM   2983  N   PHE B  70      32.201  -8.422  -9.968  1.00 32.77           N  
ANISOU 2983  N   PHE B  70     4662   4899   2889    809   -176    -45       N  
ATOM   2984  CA  PHE B  70      32.009  -9.578 -10.860  1.00 25.53           C  
ANISOU 2984  CA  PHE B  70     3882   3775   2043    951   -135     88       C  
ATOM   2985  C   PHE B  70      31.775  -9.171 -12.314  1.00 24.39           C  
ANISOU 2985  C   PHE B  70     3799   3425   2042    818   -167     36       C  
ATOM   2986  O   PHE B  70      31.357  -9.987 -13.147  1.00 35.78           O  
ANISOU 2986  O   PHE B  70     5375   4676   3542    838   -125     91       O  
ATOM   2987  CB  PHE B  70      30.840 -10.425 -10.356  1.00 26.12           C  
ANISOU 2987  CB  PHE B  70     4101   3646   2177   1011    -57    166       C  
ATOM   2988  CG  PHE B  70      31.077 -11.030  -8.993  1.00 26.88           C  
ANISOU 2988  CG  PHE B  70     4166   3936   2113   1186      0    272       C  
ATOM   2989  CD1 PHE B  70      32.258 -11.711  -8.723  1.00 31.71           C  
ANISOU 2989  CD1 PHE B  70     4704   4798   2547   1421     38    420       C  
ATOM   2990  CD2 PHE B  70      30.141 -10.901  -7.982  1.00 38.94           C  
ANISOU 2990  CD2 PHE B  70     5714   5433   3646   1137     26    252       C  
ATOM   2991  CE1 PHE B  70      32.492 -12.272  -7.459  1.00 33.75           C  
ANISOU 2991  CE1 PHE B  70     4905   5297   2620   1619     91    576       C  
ATOM   2992  CE2 PHE B  70      30.356 -11.460  -6.731  1.00 28.55           C  
ANISOU 2992  CE2 PHE B  70     4370   4327   2153   1298     80    370       C  
ATOM   2993  CZ  PHE B  70      31.534 -12.141  -6.465  1.00 32.27           C  
ANISOU 2993  CZ  PHE B  70     4760   5072   2429   1543    106    544       C  
ATOM   2994  N   ALA B  71      32.048  -7.913 -12.629  1.00 24.14           N  
ANISOU 2994  N   ALA B  71     3684   3438   2048    660   -217    -72       N  
ATOM   2995  CA  ALA B  71      31.757  -7.403 -13.981  1.00 23.38           C  
ANISOU 2995  CA  ALA B  71     3637   3170   2075    548   -243    -81       C  
ATOM   2996  C   ALA B  71      32.581  -8.102 -15.055  1.00 23.50           C  
ANISOU 2996  C   ALA B  71     3683   3213   2032    604   -241    -38       C  
ATOM   2997  O   ALA B  71      32.162  -8.177 -16.200  1.00 23.08           O  
ANISOU 2997  O   ALA B  71     3707   3024   2039    532   -254    -16       O  
ATOM   2998  CB  ALA B  71      31.986  -5.878 -14.038  1.00 24.88           C  
ANISOU 2998  CB  ALA B  71     3767   3367   2321    388   -233   -184       C  
ATOM   2999  N   ASP B  72      33.742  -8.638 -14.686  1.00 35.18           N  
ANISOU 2999  N   ASP B  72     5088   4904   3373    741   -213    -12       N  
ATOM   3000  CA  ASP B  72      34.589  -9.333 -15.659  1.00 36.81           C  
ANISOU 3000  CA  ASP B  72     5326   5130   3528    834   -163     38       C  
ATOM   3001  C   ASP B  72      34.316 -10.833 -15.734  1.00 34.66           C  
ANISOU 3001  C   ASP B  72     5231   4692   3246   1013    -31    139       C  
ATOM   3002  O   ASP B  72      35.071 -11.569 -16.355  1.00 32.81           O  
ANISOU 3002  O   ASP B  72     5052   4452   2963   1143     78    190       O  
ATOM   3003  CB  ASP B  72      36.076  -9.105 -15.354  1.00 39.19           C  
ANISOU 3003  CB  ASP B  72     5422   5787   3682    914   -167     42       C  
ATOM   3004  CG  ASP B  72      36.547  -9.819 -14.088  1.00 41.38           C  
ANISOU 3004  CG  ASP B  72     5588   6324   3811   1148   -130    158       C  
ATOM   3005  OD1 ASP B  72      35.703 -10.259 -13.283  1.00 43.61           O  
ANISOU 3005  OD1 ASP B  72     5961   6494   4116   1212   -106    207       O  
ATOM   3006  OD2 ASP B  72      37.779  -9.917 -13.888  1.00 39.94           O  
ANISOU 3006  OD2 ASP B  72     5200   6508   3470   1272   -122    221       O  
ATOM   3007  N   MET B  73      33.238 -11.280 -15.109  1.00 25.35           N  
ANISOU 3007  N   MET B  73     4159   3356   2118   1010     -1    163       N  
ATOM   3008  CA  MET B  73      32.895 -12.700 -15.125  1.00 29.99           C  
ANISOU 3008  CA  MET B  73     4963   3729   2703   1131    181    240       C  
ATOM   3009  C   MET B  73      31.632 -12.963 -15.910  1.00 25.91           C  
ANISOU 3009  C   MET B  73     4614   2960   2269    891    198    156       C  
ATOM   3010  O   MET B  73      30.661 -12.265 -15.743  1.00 24.90           O  
ANISOU 3010  O   MET B  73     4414   2839   2207    729     77    114       O  
ATOM   3011  CB  MET B  73      32.718 -13.227 -13.704  1.00 34.74           C  
ANISOU 3011  CB  MET B  73     5565   4379   3256   1317    249    353       C  
ATOM   3012  CG  MET B  73      34.017 -13.439 -12.981  1.00 49.26           C  
ANISOU 3012  CG  MET B  73     7248   6521   4947   1610    286    499       C  
ATOM   3013  SD  MET B  73      33.785 -14.421 -11.505  1.00 57.45           S  
ANISOU 3013  SD  MET B  73     8346   7586   5897   1887    432    708       S  
ATOM   3014  CE  MET B  73      33.254 -15.971 -12.221  1.00 53.02           C  
ANISOU 3014  CE  MET B  73     8187   6517   5441   1967    755    772       C  
ATOM   3015  N   SER B  74      31.646 -13.972 -16.775  1.00 34.74           N  
ANISOU 3015  N   SER B  74     5948   3883   3367    856    369    131       N  
ATOM   3016  CA  SER B  74      30.418 -14.381 -17.439  1.00 33.60           C  
ANISOU 3016  CA  SER B  74     5953   3569   3245    569    405     31       C  
ATOM   3017  C   SER B  74      29.498 -15.005 -16.391  1.00 38.72           C  
ANISOU 3017  C   SER B  74     6693   4094   3926    574    501     67       C  
ATOM   3018  O   SER B  74      29.977 -15.536 -15.385  1.00 41.89           O  
ANISOU 3018  O   SER B  74     7145   4456   4315    837    628    183       O  
ATOM   3019  CB  SER B  74      30.705 -15.363 -18.576  1.00 31.64           C  
ANISOU 3019  CB  SER B  74     5951   3136   2933    474    618    -54       C  
ATOM   3020  OG  SER B  74      30.835 -16.689 -18.087  1.00 36.38           O  
ANISOU 3020  OG  SER B  74     6819   3472   3530    624    934    -12       O  
ATOM   3021  N   ASN B  75      28.186 -14.928 -16.601  1.00 34.60           N  
ANISOU 3021  N   ASN B  75     6164   3556   3427    293    442     -8       N  
ATOM   3022  CA  ASN B  75      27.267 -15.508 -15.632  1.00 32.54           C  
ANISOU 3022  CA  ASN B  75     5982   3188   3195    263    546     15       C  
ATOM   3023  C   ASN B  75      27.409 -17.018 -15.583  1.00 36.43           C  
ANISOU 3023  C   ASN B  75     6815   3376   3652    287    888      6       C  
ATOM   3024  O   ASN B  75      27.198 -17.624 -14.540  1.00 37.30           O  
ANISOU 3024  O   ASN B  75     7033   3358   3780    421   1044     95       O  
ATOM   3025  CB  ASN B  75      25.816 -15.140 -15.929  1.00 38.69           C  
ANISOU 3025  CB  ASN B  75     6640   4072   3989    -56    425    -53       C  
ATOM   3026  CG  ASN B  75      24.862 -15.666 -14.864  1.00 39.17           C  
ANISOU 3026  CG  ASN B  75     6752   4050   4082    -96    533    -30       C  
ATOM   3027  OD1 ASN B  75      24.067 -16.568 -15.116  1.00 36.29           O  
ANISOU 3027  OD1 ASN B  75     6544   3571   3675   -361    694   -120       O  
ATOM   3028  ND2 ASN B  75      24.969 -15.121 -13.649  1.00 28.17           N  
ANISOU 3028  ND2 ASN B  75     5239   2721   2743    137    469     72       N  
ATOM   3029  N   ASP B  76      27.781 -17.628 -16.705  1.00 36.61           N  
ANISOU 3029  N   ASP B  76     7032   3258   3620    163   1045    -99       N  
ATOM   3030  CA  ASP B  76      28.013 -19.058 -16.713  1.00 42.10           C  
ANISOU 3030  CA  ASP B  76     8111   3587   4297    205   1456   -114       C  
ATOM   3031  C   ASP B  76      29.205 -19.361 -15.829  1.00 39.63           C  
ANISOU 3031  C   ASP B  76     7829   3218   4009    719   1595    119       C  
ATOM   3032  O   ASP B  76      29.225 -20.361 -15.126  1.00 44.29           O  
ANISOU 3032  O   ASP B  76     8664   3548   4615    902   1909    234       O  
ATOM   3033  CB  ASP B  76      28.246 -19.577 -18.133  1.00 50.34           C  
ANISOU 3033  CB  ASP B  76     9369   4493   5264    -42   1626   -300       C  
ATOM   3034  CG  ASP B  76      26.970 -19.642 -18.947  1.00 57.78           C  
ANISOU 3034  CG  ASP B  76    10327   5511   6116   -601   1573   -530       C  
ATOM   3035  OD1 ASP B  76      25.896 -19.320 -18.403  1.00 57.12           O  
ANISOU 3035  OD1 ASP B  76    10078   5576   6050   -766   1417   -523       O  
ATOM   3036  OD2 ASP B  76      27.039 -20.026 -20.133  1.00 67.38           O  
ANISOU 3036  OD2 ASP B  76    11704   6677   7221   -887   1695   -717       O  
ATOM   3037  N   GLU B  77      30.193 -18.477 -15.855  1.00 33.99           N  
ANISOU 3037  N   GLU B  77     6848   2785   3281    948   1371    206       N  
ATOM   3038  CA  GLU B  77      31.382 -18.658 -15.045  1.00 37.59           C  
ANISOU 3038  CA  GLU B  77     7236   3338   3710   1421   1456    443       C  
ATOM   3039  C   GLU B  77      30.981 -18.497 -13.588  1.00 34.45           C  
ANISOU 3039  C   GLU B  77     6718   3067   3304   1562   1376    586       C  
ATOM   3040  O   GLU B  77      31.296 -19.310 -12.722  1.00 36.55           O  
ANISOU 3040  O   GLU B  77     7103   3247   3539   1877   1607    797       O  
ATOM   3041  CB  GLU B  77      32.445 -17.638 -15.442  1.00 43.90           C  
ANISOU 3041  CB  GLU B  77     7734   4479   4467   1526   1211    455       C  
ATOM   3042  CG  GLU B  77      33.874 -18.026 -15.154  1.00 61.74           C  
ANISOU 3042  CG  GLU B  77     9929   6869   6659   1970   1358    672       C  
ATOM   3043  CD  GLU B  77      34.845 -17.140 -15.911  1.00 74.85           C  
ANISOU 3043  CD  GLU B  77    11343   8817   8279   1958   1169    617       C  
ATOM   3044  OE1 GLU B  77      34.444 -16.013 -16.287  1.00 64.64           O  
ANISOU 3044  OE1 GLU B  77     9883   7669   7007   1656    881    455       O  
ATOM   3045  OE2 GLU B  77      35.995 -17.574 -16.144  1.00 87.18           O  
ANISOU 3045  OE2 GLU B  77    12883  10451   9790   2260   1338    751       O  
ATOM   3046  N   PHE B  78      30.242 -17.431 -13.347  1.00 32.06           N  
ANISOU 3046  N   PHE B  78     6189   2968   3026   1331   1071    480       N  
ATOM   3047  CA  PHE B  78      29.774 -17.089 -12.025  1.00 39.95           C  
ANISOU 3047  CA  PHE B  78     7056   4113   4010   1401    974    564       C  
ATOM   3048  C   PHE B  78      28.894 -18.173 -11.417  1.00 41.57           C  
ANISOU 3048  C   PHE B  78     7525   4031   4238   1379   1235    620       C  
ATOM   3049  O   PHE B  78      29.034 -18.524 -10.239  1.00 34.45           O  
ANISOU 3049  O   PHE B  78     6631   3180   3280   1630   1328    806       O  
ATOM   3050  CB  PHE B  78      29.017 -15.771 -12.115  1.00 39.73           C  
ANISOU 3050  CB  PHE B  78     6793   4266   4036   1129    673    415       C  
ATOM   3051  CG  PHE B  78      28.513 -15.275 -10.807  1.00 28.62           C  
ANISOU 3051  CG  PHE B  78     5251   3008   2615   1168    585    459       C  
ATOM   3052  CD1 PHE B  78      29.354 -14.585  -9.953  1.00 28.45           C  
ANISOU 3052  CD1 PHE B  78     5021   3292   2495   1348    466    524       C  
ATOM   3053  CD2 PHE B  78      27.192 -15.482 -10.439  1.00 29.65           C  
ANISOU 3053  CD2 PHE B  78     5449   3009   2808    987    630    417       C  
ATOM   3054  CE1 PHE B  78      28.881 -14.101  -8.752  1.00 34.39           C  
ANISOU 3054  CE1 PHE B  78     5667   4191   3208   1342    406    530       C  
ATOM   3055  CE2 PHE B  78      26.715 -15.010  -9.234  1.00 30.72           C  
ANISOU 3055  CE2 PHE B  78     5468   3277   2928   1022    572    449       C  
ATOM   3056  CZ  PHE B  78      27.558 -14.322  -8.390  1.00 28.22           C  
ANISOU 3056  CZ  PHE B  78     4976   3236   2509   1198    467    498       C  
ATOM   3057  N   LYS B  79      28.004 -18.709 -12.249  1.00 44.39           N  
ANISOU 3057  N   LYS B  79     8096   4116   4653   1050   1365    455       N  
ATOM   3058  CA  LYS B  79      26.956 -19.630 -11.818  1.00 47.24           C  
ANISOU 3058  CA  LYS B  79     8704   4206   5040    886   1612    437       C  
ATOM   3059  C   LYS B  79      27.451 -21.057 -11.630  1.00 48.75           C  
ANISOU 3059  C   LYS B  79     9283   4020   5220   1117   2067    578       C  
ATOM   3060  O   LYS B  79      26.747 -21.872 -11.050  1.00 50.37           O  
ANISOU 3060  O   LYS B  79     9724   3973   5442   1049   2329    613       O  
ATOM   3061  CB  LYS B  79      25.820 -19.625 -12.840  1.00 54.88           C  
ANISOU 3061  CB  LYS B  79     9713   5109   6029    378   1577    183       C  
ATOM   3062  CG  LYS B  79      24.569 -20.383 -12.462  1.00 62.31           C  
ANISOU 3062  CG  LYS B  79    10833   5861   6981     86   1782    110       C  
ATOM   3063  CD  LYS B  79      23.894 -20.964 -13.689  1.00 70.08           C  
ANISOU 3063  CD  LYS B  79    11997   6711   7919   -404   1925   -143       C  
ATOM   3064  CE  LYS B  79      23.764 -19.936 -14.794  1.00 70.48           C  
ANISOU 3064  CE  LYS B  79    11747   7102   7929   -619   1574   -267       C  
ATOM   3065  NZ  LYS B  79      23.252 -20.557 -16.045  1.00 77.33           N  
ANISOU 3065  NZ  LYS B  79    12784   7909   8688  -1108   1717   -515       N  
ATOM   3066  N   GLU B  80      28.649 -21.361 -12.124  1.00 46.46           N  
ANISOU 3066  N   GLU B  80     9069   3675   4908   1399   2199    672       N  
ATOM   3067  CA  GLU B  80      29.134 -22.742 -12.156  1.00 58.91           C  
ANISOU 3067  CA  GLU B  80    10936   4974   6472   1579   2655    774       C  
ATOM   3068  C   GLU B  80      29.059 -23.393 -10.780  1.00 70.29           C  
ANISOU 3068  C   GLU B  80    12377   6451   7880   1845   2829    994       C  
ATOM   3069  O   GLU B  80      28.523 -24.490 -10.629  1.00 75.71           O  
ANISOU 3069  O   GLU B  80    13334   6854   8578   1736   3187    964       O  
ATOM   3070  CB  GLU B  80      30.568 -22.802 -12.689  1.00 63.48           C  
ANISOU 3070  CB  GLU B  80    11431   5678   7009   1902   2706    894       C  
ATOM   3071  CG  GLU B  80      30.723 -23.538 -14.026  1.00 69.72           C  
ANISOU 3071  CG  GLU B  80    12498   6178   7813   1677   2989    726       C  
ATOM   3072  CD  GLU B  80      30.549 -25.043 -13.889  1.00 87.17           C  
ANISOU 3072  CD  GLU B  80    15042   8071  10010   1662   3499    778       C  
ATOM   3073  OE1 GLU B  80      30.565 -25.544 -12.742  1.00 89.55           O  
ANISOU 3073  OE1 GLU B  80    15336   8399  10289   1938   3648    988       O  
ATOM   3074  OE2 GLU B  80      30.411 -25.729 -14.928  1.00 95.31           O  
ANISOU 3074  OE2 GLU B  80    16341   8834  11037   1370   3770    605       O  
ATOM   3075  N   LYS B  81      29.566 -22.696  -9.770  1.00 80.57           N  
ANISOU 3075  N   LYS B  81    13367   8125   9121   2162   2578   1195       N  
ATOM   3076  CA  LYS B  81      29.377 -23.130  -8.390  1.00 95.85           C  
ANISOU 3076  CA  LYS B  81    15257  10154  11008   2373   2677   1382       C  
ATOM   3077  C   LYS B  81      28.124 -22.511  -7.785  1.00 95.22           C  
ANISOU 3077  C   LYS B  81    15145  10082  10954   2098   2478   1293       C  
ATOM   3078  O   LYS B  81      27.883 -22.635  -6.587  1.00 97.87           O  
ANISOU 3078  O   LYS B  81    15406  10541  11239   2238   2492   1432       O  
ATOM   3079  CB  LYS B  81      30.603 -22.785  -7.537  1.00104.03           C  
ANISOU 3079  CB  LYS B  81    15944  11665  11918   2820   2535   1638       C  
ATOM   3080  CG  LYS B  81      31.688 -23.847  -7.568  1.00109.96           C  
ANISOU 3080  CG  LYS B  81    16752  12409  12619   3190   2886   1845       C  
ATOM   3081  CD  LYS B  81      31.346 -24.994  -6.628  1.00107.92           C  
ANISOU 3081  CD  LYS B  81    16677  11979  12350   3361   3249   2007       C  
ATOM   3082  CE  LYS B  81      32.577 -25.827  -6.332  1.00105.40           C  
ANISOU 3082  CE  LYS B  81    16299  11813  11935   3837   3551   2309       C  
ATOM   3083  NZ  LYS B  81      33.773 -24.952  -6.229  1.00102.64           N  
ANISOU 3083  NZ  LYS B  81    15511  12023  11466   4068   3238   2433       N  
ATOM   3084  N   TYR B  82      27.347 -21.834  -8.629  1.00 88.95           N  
ANISOU 3084  N   TYR B  82    14394   9176  10225   1708   2304   1075       N  
ATOM   3085  CA  TYR B  82      26.028 -21.296  -8.271  1.00 81.57           C  
ANISOU 3085  CA  TYR B  82    13375   8292   9325   1356   2138    932       C  
ATOM   3086  C   TYR B  82      26.073 -20.225  -7.197  1.00 77.53           C  
ANISOU 3086  C   TYR B  82    12507   8208   8743   1494   1817   1011       C  
ATOM   3087  O   TYR B  82      25.035 -19.851  -6.660  1.00 84.53           O  
ANISOU 3087  O   TYR B  82    13303   9160   9654   1281   1727    928       O  
ATOM   3088  CB  TYR B  82      25.093 -22.430  -7.825  1.00 83.33           C  
ANISOU 3088  CB  TYR B  82    13928   8154   9579   1203   2510    941       C  
ATOM   3089  CG  TYR B  82      24.802 -23.433  -8.921  1.00 93.96           C  
ANISOU 3089  CG  TYR B  82    15576   9149  10977    896   2820    724       C  
ATOM   3090  CD1 TYR B  82      23.749 -23.238  -9.808  1.00 99.17           C  
ANISOU 3090  CD1 TYR B  82    16302   9707  11671    346   2773    454       C  
ATOM   3091  CD2 TYR B  82      25.594 -24.567  -9.083  1.00 97.47           C  
ANISOU 3091  CD2 TYR B  82    16215   9419  11399   1130   3174    788       C  
ATOM   3092  CE1 TYR B  82      23.486 -24.150 -10.819  1.00105.37           C  
ANISOU 3092  CE1 TYR B  82    17331  10263  12441      4   3049    214       C  
ATOM   3093  CE2 TYR B  82      25.339 -25.483 -10.089  1.00104.25           C  
ANISOU 3093  CE2 TYR B  82    17366   9983  12261    821   3495    576       C  
ATOM   3094  CZ  TYR B  82      24.285 -25.272 -10.954  1.00109.36           C  
ANISOU 3094  CZ  TYR B  82    18067  10568  12916    243   3421    272       C  
ATOM   3095  OH  TYR B  82      24.033 -26.189 -11.953  1.00114.13           O  
ANISOU 3095  OH  TYR B  82    18936  10959  13471   -113   3738     38       O  
ATOM   3096  N   THR B  83      27.260 -19.702  -6.901  1.00 75.35           N  
ANISOU 3096  N   THR B  83    12017   8247   8365   1815   1658   1150       N  
ATOM   3097  CA  THR B  83      27.442 -18.983  -5.642  1.00 74.44           C  
ANISOU 3097  CA  THR B  83    11639   8526   8119   1970   1467   1255       C  
ATOM   3098  C   THR B  83      28.515 -17.923  -5.504  1.00 65.97           C  
ANISOU 3098  C   THR B  83    10227   7913   6924   2100   1181   1256       C  
ATOM   3099  O   THR B  83      29.009 -17.702  -4.396  1.00 48.12           O  
ANISOU 3099  O   THR B  83     7797   6010   4478   2302   1117   1408       O  
ATOM   3100  CB  THR B  83      27.743 -19.968  -4.542  1.00 88.57           C  
ANISOU 3100  CB  THR B  83    13537  10314   9801   2301   1716   1539       C  
ATOM   3101  OG1 THR B  83      28.546 -21.038  -5.063  1.00 97.30           O  
ANISOU 3101  OG1 THR B  83    14770  11238  10960   2513   1979   1620       O  
ATOM   3102  CG2 THR B  83      26.489 -20.512  -4.035  1.00 92.02           C  
ANISOU 3102  CG2 THR B  83    14189  10477  10299   2117   1903   1519       C  
ATOM   3103  N   GLY B  84      28.879 -17.275  -6.598  1.00 77.17           N  
ANISOU 3103  N   GLY B  84    11544   9356   8419   1957   1021   1084       N  
ATOM   3104  CA  GLY B  84      29.796 -16.157  -6.526  1.00 82.40           C  
ANISOU 3104  CA  GLY B  84    11896  10433   8979   1985    765   1030       C  
ATOM   3105  C   GLY B  84      31.187 -16.469  -6.036  1.00 87.76           C  
ANISOU 3105  C   GLY B  84    12434  11462   9450   2350    794   1271       C  
ATOM   3106  O   GLY B  84      31.670 -17.605  -6.155  1.00 99.01           O  
ANISOU 3106  O   GLY B  84    14010  12743  10867   2640   1037   1489       O  
ATOM   3107  N   SER B  85      31.831 -15.436  -5.499  1.00 82.93           N  
ANISOU 3107  N   SER B  85    11508  11325   8674   2308    568   1211       N  
ATOM   3108  CA  SER B  85      33.156 -15.564  -4.921  1.00 81.71           C  
ANISOU 3108  CA  SER B  85    11083  11650   8313   2563    544   1389       C  
ATOM   3109  C   SER B  85      33.536 -14.300  -4.146  1.00 79.09           C  
ANISOU 3109  C   SER B  85    10427  11837   7786   2351    302   1229       C  
ATOM   3110  O   SER B  85      34.478 -13.593  -4.507  1.00 80.78           O  
ANISOU 3110  O   SER B  85    10407  12362   7925   2260    169   1130       O  
ATOM   3111  CB  SER B  85      34.199 -15.867  -6.010  1.00 85.59           C  
ANISOU 3111  CB  SER B  85    11533  12131   8857   2711    598   1440       C  
ATOM   3112  OG  SER B  85      34.994 -14.737  -6.322  1.00 86.40           O  
ANISOU 3112  OG  SER B  85    11357  12617   8854   2550    371   1290       O  
ATOM   3113  N   TYR B  90      26.755 -25.353  -5.671  1.00 95.41           N  
ANISOU 3113  N   TYR B  90    15704   9551  10996   2230   3359   1499       N  
ATOM   3114  CA  TYR B  90      26.155 -24.449  -4.695  1.00 82.15           C  
ANISOU 3114  CA  TYR B  90    13800   8133   9279   2178   3048   1544       C  
ATOM   3115  C   TYR B  90      26.984 -24.404  -3.416  1.00 74.69           C  
ANISOU 3115  C   TYR B  90    12611   7560   8210   2635   2984   1837       C  
ATOM   3116  O   TYR B  90      27.627 -25.387  -3.069  1.00 80.61           O  
ANISOU 3116  O   TYR B  90    13442   8256   8930   2962   3284   2023       O  
ATOM   3117  CB  TYR B  90      24.725 -24.878  -4.390  1.00 82.98           C  
ANISOU 3117  CB  TYR B  90    14120   7962   9448   1822   3212   1415       C  
ATOM   3118  N   THR B  91      26.983 -23.262  -2.727  1.00 68.83           N  
ANISOU 3118  N   THR B  91    11562   7222   7370   2642   2614   1875       N  
ATOM   3119  CA  THR B  91      27.538 -23.192  -1.379  1.00 60.82           C  
ANISOU 3119  CA  THR B  91    10302   6607   6199   2965   2539   2112       C  
ATOM   3120  C   THR B  91      26.619 -23.950  -0.417  1.00 59.86           C  
ANISOU 3120  C   THR B  91    10370   6285   6091   2943   2775   2193       C  
ATOM   3121  O   THR B  91      27.052 -24.410   0.634  1.00 56.51           O  
ANISOU 3121  O   THR B  91     9853   6056   5560   3253   2868   2429       O  
ATOM   3122  CB  THR B  91      27.722 -21.742  -0.866  1.00 65.35           C  
ANISOU 3122  CB  THR B  91    10516   7691   6624   2898   2109   2074       C  
ATOM   3123  OG1 THR B  91      26.545 -20.975  -1.119  1.00 67.17           O  
ANISOU 3123  OG1 THR B  91    10822   7793   6906   2517   1976   1868       O  
ATOM   3124  CG2 THR B  91      28.893 -21.056  -1.513  1.00 47.03           C  
ANISOU 3124  CG2 THR B  91     7947   5679   4246   2996   1890   2049       C  
ATOM   3125  N   THR B  92      25.347 -24.080  -0.776  1.00 57.88           N  
ANISOU 3125  N   THR B  92    10364   5669   5959   2562   2876   2000       N  
ATOM   3126  CA  THR B  92      24.432 -24.904   0.011  1.00 59.16           C  
ANISOU 3126  CA  THR B  92    10738   5591   6150   2496   3146   2047       C  
ATOM   3127  C   THR B  92      23.786 -25.995  -0.836  1.00 61.72           C  
ANISOU 3127  C   THR B  92    11451   5374   6625   2247   3529   1877       C  
ATOM   3128  O   THR B  92      22.886 -25.727  -1.624  1.00 59.02           O  
ANISOU 3128  O   THR B  92    11205   4852   6368   1803   3491   1622       O  
ATOM   3129  CB  THR B  92      23.326 -24.057   0.667  1.00 59.95           C  
ANISOU 3129  CB  THR B  92    10736   5836   6208   2209   2945   1966       C  
ATOM   3130  OG1 THR B  92      22.593 -23.351  -0.336  1.00 57.05           O  
ANISOU 3130  OG1 THR B  92    10384   5364   5927   1801   2810   1714       O  
ATOM   3131  CG2 THR B  92      23.928 -23.071   1.608  1.00 51.54           C  
ANISOU 3131  CG2 THR B  92     9323   5312   4949   2415   2629   2096       C  
ATOM   3132  N   THR B  93      24.244 -27.231  -0.676  1.00 79.93           N  
ANISOU 3132  N   THR B  93    13974   7453   8944   2515   3922   2011       N  
ATOM   3133  CA  THR B  93      23.671 -28.331  -1.438  1.00 92.64           C  
ANISOU 3133  CA  THR B  93    15982   8560  10658   2258   4344   1819       C  
ATOM   3134  C   THR B  93      22.239 -28.602  -0.973  1.00 99.47           C  
ANISOU 3134  C   THR B  93    17011   9216  11569   1873   4460   1681       C  
ATOM   3135  O   THR B  93      21.805 -28.059   0.049  1.00 94.45           O  
ANISOU 3135  O   THR B  93    16196   8810  10883   1897   4262   1794       O  
ATOM   3136  CB  THR B  93      24.528 -29.598  -1.322  1.00101.01           C  
ANISOU 3136  CB  THR B  93    17256   9422  11700   2671   4808   2017       C  
ATOM   3137  OG1 THR B  93      25.086 -29.677  -0.005  1.00103.96           O  
ANISOU 3137  OG1 THR B  93    17445  10077  11977   3141   4788   2367       O  
ATOM   3138  CG2 THR B  93      25.659 -29.547  -2.340  1.00101.21           C  
ANISOU 3138  CG2 THR B  93    17235   9509  11712   2841   4815   2022       C  
ATOM   3139  N   GLU B  94      21.530 -29.437  -1.736  1.00104.59           N  
ANISOU 3139  N   GLU B  94    17987   9466  12287   1495   4792   1424       N  
ATOM   3140  CA  GLU B  94      20.084 -29.667  -1.605  1.00100.43           C  
ANISOU 3140  CA  GLU B  94    17594   8764  11799    993   4894   1205       C  
ATOM   3141  C   GLU B  94      19.303 -28.456  -2.100  1.00 94.59           C  
ANISOU 3141  C   GLU B  94    16592   8272  11074    552   4482   1007       C  
ATOM   3142  O   GLU B  94      19.148 -28.260  -3.306  1.00 92.79           O  
ANISOU 3142  O   GLU B  94    16377   8012  10867    212   4419    761       O  
ATOM   3143  CB  GLU B  94      19.685 -29.995  -0.163  1.00 97.20           C  
ANISOU 3143  CB  GLU B  94    17201   8366  11363   1180   5003   1420       C  
ATOM   3144  CG  GLU B  94      20.416 -31.184   0.421  1.00 97.77           C  
ANISOU 3144  CG  GLU B  94    17515   8218  11416   1649   5433   1664       C  
ATOM   3145  CD  GLU B  94      19.497 -32.097   1.200  1.00102.44           C  
ANISOU 3145  CD  GLU B  94    18372   8525  12023   1517   5793   1662       C  
ATOM   3146  OE1 GLU B  94      18.367 -31.670   1.526  1.00103.28           O  
ANISOU 3146  OE1 GLU B  94    18397   8705  12140   1122   5637   1528       O  
ATOM   3147  OE2 GLU B  94      19.905 -33.241   1.483  1.00104.80           O  
ANISOU 3147  OE2 GLU B  94    18961   8537  12322   1813   6257   1805       O  
ATOM   3148  N   VAL B 106       5.034 -10.030  20.243  1.00 98.23           N  
ANISOU 3148  N   VAL B 106    13432  13876  10013    -64   4802   -432       N  
ATOM   3149  CA  VAL B 106       4.376  -9.933  18.947  1.00 93.65           C  
ANISOU 3149  CA  VAL B 106    12663  13079   9841     17   4820   -357       C  
ATOM   3150  C   VAL B 106       4.790  -8.651  18.217  1.00 98.95           C  
ANISOU 3150  C   VAL B 106    13297  13586  10716    126   4789   -543       C  
ATOM   3151  O   VAL B 106       4.992  -8.656  16.998  1.00 98.21           O  
ANISOU 3151  O   VAL B 106    13119  13362  10835    197   4670   -466       O  
ATOM   3152  CB  VAL B 106       2.835  -9.996  19.096  1.00 87.16           C  
ANISOU 3152  CB  VAL B 106    11619  12256   9241     22   5061   -290       C  
ATOM   3153  CG1 VAL B 106       2.352  -9.045  20.181  1.00 85.00           C  
ANISOU 3153  CG1 VAL B 106    11351  12027   8917     52   5284   -486       C  
ATOM   3154  CG2 VAL B 106       2.149  -9.710  17.767  1.00 85.65           C  
ANISOU 3154  CG2 VAL B 106    11149  11949   9444    122   5071   -207       C  
ATOM   3155  N   ASN B 107       4.943  -7.562  18.965  1.00 99.53           N  
ANISOU 3155  N   ASN B 107    13451  13650  10716    122   4906   -788       N  
ATOM   3156  CA  ASN B 107       5.345  -6.291  18.373  1.00 96.48           C  
ANISOU 3156  CA  ASN B 107    13082  13052  10522    202   4920   -973       C  
ATOM   3157  C   ASN B 107       6.861  -6.183  18.179  1.00 87.92           C  
ANISOU 3157  C   ASN B 107    12170  12028   9208    108   4675  -1085       C  
ATOM   3158  O   ASN B 107       7.632  -6.147  19.142  1.00 88.78           O  
ANISOU 3158  O   ASN B 107    12427  12353   8953    -38   4616  -1220       O  
ATOM   3159  CB  ASN B 107       4.834  -5.118  19.220  1.00101.24           C  
ANISOU 3159  CB  ASN B 107    13738  13557  11172    212   5198  -1196       C  
ATOM   3160  CG  ASN B 107       5.298  -5.188  20.662  1.00104.30           C  
ANISOU 3160  CG  ASN B 107    14312  14178  11141     20   5227  -1362       C  
ATOM   3161  OD1 ASN B 107       5.676  -6.249  21.153  1.00108.94           O  
ANISOU 3161  OD1 ASN B 107    14937  15038  11418    -72   5077  -1238       O  
ATOM   3162  ND2 ASN B 107       5.269  -4.051  21.348  1.00104.25           N  
ANISOU 3162  ND2 ASN B 107    14428  14064  11118    -38   5437  -1624       N  
ATOM   3163  N   ILE B 108       7.283  -6.136  16.920  1.00 79.47           N  
ANISOU 3163  N   ILE B 108    11048  10811   8336    191   4527  -1015       N  
ATOM   3164  CA  ILE B 108       8.697  -6.009  16.597  1.00 65.02           C  
ANISOU 3164  CA  ILE B 108     9347   9042   6318    112   4294  -1110       C  
ATOM   3165  C   ILE B 108       8.973  -4.649  15.954  1.00 72.26           C  
ANISOU 3165  C   ILE B 108    10287   9690   7478    152   4355  -1303       C  
ATOM   3166  O   ILE B 108       8.081  -4.064  15.336  1.00 65.50           O  
ANISOU 3166  O   ILE B 108     9312   8580   6993    321   4523  -1246       O  
ATOM   3167  CB  ILE B 108       9.168  -7.166  15.662  1.00 71.35           C  
ANISOU 3167  CB  ILE B 108    10120   9888   7100    159   4060   -862       C  
ATOM   3168  CG1 ILE B 108       8.394  -7.169  14.341  1.00 60.40           C  
ANISOU 3168  CG1 ILE B 108     8553   8265   6130    313   4100   -708       C  
ATOM   3169  CG2 ILE B 108       9.026  -8.509  16.367  1.00 75.62           C  
ANISOU 3169  CG2 ILE B 108    10705  10647   7381    111   4023   -652       C  
ATOM   3170  CD1 ILE B 108       8.915  -8.197  13.325  1.00 56.83           C  
ANISOU 3170  CD1 ILE B 108     8074   7817   5702    329   3791   -485       C  
ATOM   3171  N   PRO B 109      10.208  -4.133  16.113  1.00 70.10           N  
ANISOU 3171  N   PRO B 109    10156   9494   6987     -2   4225  -1507       N  
ATOM   3172  CA  PRO B 109      10.578  -2.819  15.575  1.00 68.66           C  
ANISOU 3172  CA  PRO B 109    10045   9031   7012    -18   4305  -1703       C  
ATOM   3173  C   PRO B 109      10.317  -2.687  14.079  1.00 63.15           C  
ANISOU 3173  C   PRO B 109     9230   8062   6702    199   4272  -1531       C  
ATOM   3174  O   PRO B 109      10.371  -3.670  13.339  1.00 60.19           O  
ANISOU 3174  O   PRO B 109     8748   7777   6346    287   4088  -1314       O  
ATOM   3175  CB  PRO B 109      12.079  -2.732  15.868  1.00 65.76           C  
ANISOU 3175  CB  PRO B 109     9792   8911   6283   -255   4083  -1880       C  
ATOM   3176  CG  PRO B 109      12.271  -3.579  17.056  1.00 67.14           C  
ANISOU 3176  CG  PRO B 109     9976   9497   6038   -363   3996  -1845       C  
ATOM   3177  CD  PRO B 109      11.305  -4.721  16.902  1.00 69.53           C  
ANISOU 3177  CD  PRO B 109    10168   9811   6439   -178   4015  -1547       C  
ATOM   3178  N   GLU B 110      10.025  -1.469  13.644  1.00 47.14           N  
ANISOU 3178  N   GLU B 110     7032   4488   6391   1329   3578    -63       N  
ATOM   3179  CA  GLU B 110       9.762  -1.235  12.242  1.00 45.96           C  
ANISOU 3179  CA  GLU B 110     6604   4342   6516   1392   3461     50       C  
ATOM   3180  C   GLU B 110      11.032  -1.504  11.448  1.00 42.39           C  
ANISOU 3180  C   GLU B 110     6206   3951   5950   1230   3184    -69       C  
ATOM   3181  O   GLU B 110      10.991  -2.054  10.351  1.00 47.87           O  
ANISOU 3181  O   GLU B 110     6627   4738   6822   1222   3026     27       O  
ATOM   3182  CB  GLU B 110       9.271   0.192  12.009  1.00 48.40           C  
ANISOU 3182  CB  GLU B 110     6978   4462   6951   1543   3601     78       C  
ATOM   3183  CG  GLU B 110       8.803   0.428  10.594  1.00 52.00           C  
ANISOU 3183  CG  GLU B 110     7113   4927   7718   1630   3485    240       C  
ATOM   3184  CD  GLU B 110       8.327   1.842  10.376  1.00 59.23           C  
ANISOU 3184  CD  GLU B 110     8093   5655   8756   1781   3623    281       C  
ATOM   3185  OE1 GLU B 110       8.610   2.702  11.235  1.00 62.26           O  
ANISOU 3185  OE1 GLU B 110     8818   5889   8950   1790   3781    140       O  
ATOM   3186  OE2 GLU B 110       7.668   2.098   9.346  1.00 65.18           O  
ANISOU 3186  OE2 GLU B 110     8560   6411   9794   1885   3562    462       O  
ATOM   3187  N   TYR B 111      12.159  -1.115  12.031  1.00 41.98           N  
ANISOU 3187  N   TYR B 111     6508   3843   5600   1094   3120   -269       N  
ATOM   3188  CA  TYR B 111      13.466  -1.278  11.415  1.00 39.13           C  
ANISOU 3188  CA  TYR B 111     6239   3525   5105    924   2866   -389       C  
ATOM   3189  C   TYR B 111      14.403  -2.032  12.342  1.00 47.96           C  
ANISOU 3189  C   TYR B 111     7558   4743   5921    739   2768   -509       C  
ATOM   3190  O   TYR B 111      14.417  -1.788  13.549  1.00 48.06           O  
ANISOU 3190  O   TYR B 111     7807   4707   5747    717   2874   -578       O  
ATOM   3191  CB  TYR B 111      14.077   0.079  11.081  1.00 48.41           C  
ANISOU 3191  CB  TYR B 111     7635   4527   6234    904   2819   -492       C  
ATOM   3192  CG  TYR B 111      13.442   0.817   9.920  1.00 47.63           C  
ANISOU 3192  CG  TYR B 111     7342   4336   6421   1057   2840   -371       C  
ATOM   3193  CD1 TYR B 111      12.383   1.698  10.124  1.00 51.91           C  
ANISOU 3193  CD1 TYR B 111     7855   4750   7117   1240   3057   -280       C  
ATOM   3194  CD2 TYR B 111      13.928   0.662   8.628  1.00 47.98           C  
ANISOU 3194  CD2 TYR B 111     7244   4410   6574   1020   2638   -339       C  
ATOM   3195  CE1 TYR B 111      11.811   2.387   9.068  1.00 48.24           C  
ANISOU 3195  CE1 TYR B 111     7206   4209   6916   1377   3052   -147       C  
ATOM   3196  CE2 TYR B 111      13.367   1.350   7.566  1.00 49.93           C  
ANISOU 3196  CE2 TYR B 111     7322   4572   7075   1157   2627   -208       C  
ATOM   3197  CZ  TYR B 111      12.306   2.209   7.794  1.00 54.61           C  
ANISOU 3197  CZ  TYR B 111     7872   5056   7823   1332   2826   -107       C  
ATOM   3198  OH  TYR B 111      11.744   2.886   6.737  1.00 59.54           O  
ANISOU 3198  OH  TYR B 111     8316   5608   8698   1463   2793     45       O  
ATOM   3199  N   VAL B 112      15.185  -2.951  11.786  1.00 43.48           N  
ANISOU 3199  N   VAL B 112     6902   4314   5306    608   2563   -525       N  
ATOM   3200  CA  VAL B 112      16.242  -3.588  12.564  1.00 43.25           C  
ANISOU 3200  CA  VAL B 112     7060   4379   4992    416   2423   -626       C  
ATOM   3201  C   VAL B 112      17.511  -3.631  11.717  1.00 35.33           C  
ANISOU 3201  C   VAL B 112     6090   3412   3923    260   2169   -701       C  
ATOM   3202  O   VAL B 112      17.445  -3.846  10.514  1.00 36.90           O  
ANISOU 3202  O   VAL B 112     6033   3669   4320    272   2013   -600       O  
ATOM   3203  CB  VAL B 112      15.834  -5.014  13.042  1.00 40.15           C  
ANISOU 3203  CB  VAL B 112     6510   4155   4589    405   2456   -530       C  
ATOM   3204  CG1 VAL B 112      17.030  -5.771  13.603  1.00 36.43           C  
ANISOU 3204  CG1 VAL B 112     6189   3799   3854    206   2263   -603       C  
ATOM   3205  CG2 VAL B 112      14.738  -4.930  14.094  1.00 43.15           C  
ANISOU 3205  CG2 VAL B 112     6913   4493   4989    530   2702   -467       C  
ATOM   3206  N   ASP B 113      18.657  -3.390  12.351  1.00 35.71           N  
ANISOU 3206  N   ASP B 113     6382   3455   3731     82   2017   -813       N  
ATOM   3207  CA  ASP B 113      19.957  -3.422  11.686  1.00 33.30           C  
ANISOU 3207  CA  ASP B 113     6090   3197   3366    -91   1749   -856       C  
ATOM   3208  C   ASP B 113      21.037  -3.707  12.726  1.00 34.09           C  
ANISOU 3208  C   ASP B 113     6392   3362   3199   -286   1598   -926       C  
ATOM   3209  O   ASP B 113      21.492  -2.809  13.426  1.00 40.24           O  
ANISOU 3209  O   ASP B 113     7400   4040   3851   -364   1566  -1004       O  
ATOM   3210  CB  ASP B 113      20.231  -2.094  10.966  1.00 41.24           C  
ANISOU 3210  CB  ASP B 113     7184   4032   4455    -85   1727   -909       C  
ATOM   3211  CG  ASP B 113      21.494  -2.128  10.119  1.00 45.51           C  
ANISOU 3211  CG  ASP B 113     7650   4641   5001   -253   1439   -892       C  
ATOM   3212  OD1 ASP B 113      22.358  -3.006  10.343  1.00 43.04           O  
ANISOU 3212  OD1 ASP B 113     7294   4482   4579   -395   1260   -875       O  
ATOM   3213  OD2 ASP B 113      21.622  -1.261   9.227  1.00 48.10           O  
ANISOU 3213  OD2 ASP B 113     7960   4865   5452   -234   1406   -880       O  
ATOM   3214  N   TRP B 114      21.463  -4.955  12.809  1.00 34.85           N  
ANISOU 3214  N   TRP B 114     6372   3635   3236   -366   1473   -868       N  
ATOM   3215  CA  TRP B 114      22.335  -5.367  13.889  1.00 38.14           C  
ANISOU 3215  CA  TRP B 114     6946   4129   3418   -525   1335   -894       C  
ATOM   3216  C   TRP B 114      23.743  -4.776  13.800  1.00 38.48           C  
ANISOU 3216  C   TRP B 114     7096   4155   3371   -721   1085   -946       C  
ATOM   3217  O   TRP B 114      24.475  -4.782  14.791  1.00 33.49           O  
ANISOU 3217  O   TRP B 114     6614   3551   2560   -857    957   -963       O  
ATOM   3218  CB  TRP B 114      22.387  -6.899  13.949  1.00 33.59           C  
ANISOU 3218  CB  TRP B 114     6192   3740   2832   -543   1269   -787       C  
ATOM   3219  CG  TRP B 114      21.198  -7.443  14.669  1.00 34.65           C  
ANISOU 3219  CG  TRP B 114     6314   3889   2964   -413   1505   -739       C  
ATOM   3220  CD1 TRP B 114      20.112  -8.060  14.124  1.00 29.17           C  
ANISOU 3220  CD1 TRP B 114     5370   3231   2484   -271   1637   -632       C  
ATOM   3221  CD2 TRP B 114      20.949  -7.362  16.071  1.00 36.28           C  
ANISOU 3221  CD2 TRP B 114     6711   4070   3004   -411   1592   -757       C  
ATOM   3222  NE1 TRP B 114      19.220  -8.390  15.101  1.00 30.86           N  
ANISOU 3222  NE1 TRP B 114     5634   3445   2647   -188   1851   -595       N  
ATOM   3223  CE2 TRP B 114      19.704  -7.964  16.308  1.00 34.39           C  
ANISOU 3223  CE2 TRP B 114     6346   3854   2865   -263   1818   -669       C  
ATOM   3224  CE3 TRP B 114      21.664  -6.841  17.152  1.00 40.71           C  
ANISOU 3224  CE3 TRP B 114     7535   4589   3343   -529   1496   -832       C  
ATOM   3225  CZ2 TRP B 114      19.163  -8.075  17.584  1.00 36.14           C  
ANISOU 3225  CZ2 TRP B 114     6706   4063   2964   -221   1965   -657       C  
ATOM   3226  CZ3 TRP B 114      21.127  -6.950  18.413  1.00 36.76           C  
ANISOU 3226  CZ3 TRP B 114     7192   4071   2703   -487   1637   -831       C  
ATOM   3227  CH2 TRP B 114      19.886  -7.557  18.622  1.00 40.54           C  
ANISOU 3227  CH2 TRP B 114     7549   4576   3277   -329   1878   -747       C  
ATOM   3228  N   ARG B 115      24.112  -4.261  12.627  1.00 33.28           N  
ANISOU 3228  N   ARG B 115     6348   3448   2850   -738   1012   -953       N  
ATOM   3229  CA  ARG B 115      25.383  -3.547  12.455  1.00 34.56           C  
ANISOU 3229  CA  ARG B 115     6587   3572   2971   -923    798   -984       C  
ATOM   3230  C   ARG B 115      25.499  -2.328  13.367  1.00 40.77           C  
ANISOU 3230  C   ARG B 115     7634   4206   3649   -977    820  -1065       C  
ATOM   3231  O   ARG B 115      26.584  -1.990  13.847  1.00 37.98           O  
ANISOU 3231  O   ARG B 115     7384   3859   3188  -1164    624  -1077       O  
ATOM   3232  CB  ARG B 115      25.554  -3.087  11.008  1.00 32.14           C  
ANISOU 3232  CB  ARG B 115     6100   3227   2885   -887    753   -935       C  
ATOM   3233  CG  ARG B 115      25.534  -4.222   9.984  1.00 29.62           C  
ANISOU 3233  CG  ARG B 115     5444   3075   2734   -811    684   -791       C  
ATOM   3234  CD  ARG B 115      25.603  -3.658   8.558  1.00 33.09           C  
ANISOU 3234  CD  ARG B 115     5744   3464   3365   -760    660   -737       C  
ATOM   3235  NE  ARG B 115      24.410  -2.884   8.210  1.00 33.22           N  
ANISOU 3235  NE  ARG B 115     5796   3337   3488   -598    846   -762       N  
ATOM   3236  CZ  ARG B 115      24.193  -2.329   7.017  1.00 36.68           C  
ANISOU 3236  CZ  ARG B 115     6134   3714   4089   -523    851   -706       C  
ATOM   3237  NH1 ARG B 115      25.088  -2.451   6.039  1.00 29.01           N  
ANISOU 3237  NH1 ARG B 115     5039   2810   3173   -597    702   -633       N  
ATOM   3238  NH2 ARG B 115      23.081  -1.639   6.805  1.00 34.79           N  
ANISOU 3238  NH2 ARG B 115     5918   3344   3955   -367   1015   -708       N  
ATOM   3239  N   GLN B 116      24.379  -1.652  13.581  1.00 38.52           N  
ANISOU 3239  N   GLN B 116     7450   3782   3406   -812   1060  -1110       N  
ATOM   3240  CA  GLN B 116      24.392  -0.435  14.382  1.00 42.73           C  
ANISOU 3240  CA  GLN B 116     8252   4147   3836   -845   1112  -1195       C  
ATOM   3241  C   GLN B 116      24.586  -0.779  15.860  1.00 48.77           C  
ANISOU 3241  C   GLN B 116     9209   4956   4364   -928   1083  -1224       C  
ATOM   3242  O   GLN B 116      25.075   0.037  16.639  1.00 48.17           O  
ANISOU 3242  O   GLN B 116     9380   4779   4143  -1043   1021  -1294       O  
ATOM   3243  CB  GLN B 116      23.105   0.359  14.156  1.00 42.43           C  
ANISOU 3243  CB  GLN B 116     8249   3945   3926   -626   1393  -1216       C  
ATOM   3244  CG  GLN B 116      22.922   0.793  12.701  1.00 46.97           C  
ANISOU 3244  CG  GLN B 116     8652   4459   4735   -543   1408  -1176       C  
ATOM   3245  CD  GLN B 116      21.703   1.672  12.485  1.00 55.80           C  
ANISOU 3245  CD  GLN B 116     9794   5408   5998   -325   1667  -1171       C  
ATOM   3246  OE1 GLN B 116      20.608   1.373  12.964  1.00 55.28           O  
ANISOU 3246  OE1 GLN B 116     9698   5344   5960   -160   1879  -1141       O  
ATOM   3247  NE2 GLN B 116      21.893   2.770  11.764  1.00 62.45           N  
ANISOU 3247  NE2 GLN B 116    10677   6102   6947   -323   1651  -1183       N  
ATOM   3248  N   LYS B 117      24.224  -2.002  16.237  1.00 44.65           N  
ANISOU 3248  N   LYS B 117     8583   4582   3800   -877   1119  -1165       N  
ATOM   3249  CA  LYS B 117      24.407  -2.443  17.616  1.00 47.87           C  
ANISOU 3249  CA  LYS B 117     9163   5042   3981   -951   1086  -1174       C  
ATOM   3250  C   LYS B 117      25.842  -2.912  17.865  1.00 40.45           C  
ANISOU 3250  C   LYS B 117     8212   4229   2929  -1182    764  -1134       C  
ATOM   3251  O   LYS B 117      26.195  -3.275  18.971  1.00 45.42           O  
ANISOU 3251  O   LYS B 117     8981   4909   3366  -1273    680  -1128       O  
ATOM   3252  CB  LYS B 117      23.418  -3.561  17.955  1.00 41.80           C  
ANISOU 3252  CB  LYS B 117     8284   4377   3223   -803   1263  -1106       C  
ATOM   3253  CG  LYS B 117      21.942  -3.175  17.856  1.00 39.84           C  
ANISOU 3253  CG  LYS B 117     8018   4018   3103   -571   1591  -1110       C  
ATOM   3254  CD  LYS B 117      21.480  -2.329  19.025  1.00 55.47           C  
ANISOU 3254  CD  LYS B 117    10300   5847   4930   -531   1761  -1189       C  
ATOM   3255  CE  LYS B 117      19.968  -2.097  18.992  1.00 55.22           C  
ANISOU 3255  CE  LYS B 117    10210   5725   5046   -286   2101  -1156       C  
ATOM   3256  NZ  LYS B 117      19.185  -3.323  19.306  1.00 58.00           N  
ANISOU 3256  NZ  LYS B 117    10393   6214   5433   -185   2229  -1051       N  
ATOM   3257  N   GLY B 118      26.667  -2.900  16.827  1.00 37.63           N  
ANISOU 3257  N   GLY B 118     7678   3921   2699  -1272    584  -1093       N  
ATOM   3258  CA  GLY B 118      28.029  -3.380  16.949  1.00 42.58           C  
ANISOU 3258  CA  GLY B 118     8233   4678   3267  -1477    283  -1021       C  
ATOM   3259  C   GLY B 118      28.073  -4.895  17.007  1.00 39.20           C  
ANISOU 3259  C   GLY B 118     7620   4445   2827  -1453    231   -913       C  
ATOM   3260  O   GLY B 118      28.953  -5.472  17.636  1.00 41.99           O  
ANISOU 3260  O   GLY B 118     7967   4911   3075  -1590     25   -840       O  
ATOM   3261  N   ALA B 119      27.121  -5.545  16.344  1.00 33.69           N  
ANISOU 3261  N   ALA B 119     6768   3786   2248  -1280    412   -890       N  
ATOM   3262  CA  ALA B 119      26.989  -6.999  16.441  1.00 40.51           C  
ANISOU 3262  CA  ALA B 119     7478   4817   3097  -1239    401   -787       C  
ATOM   3263  C   ALA B 119      27.471  -7.735  15.193  1.00 36.92           C  
ANISOU 3263  C   ALA B 119     6758   4478   2791  -1251    292   -702       C  
ATOM   3264  O   ALA B 119      27.446  -8.969  15.143  1.00 32.86           O  
ANISOU 3264  O   ALA B 119     6073   4096   2315  -1206    268   -588       O  
ATOM   3265  CB  ALA B 119      25.536  -7.371  16.741  1.00 43.83           C  
ANISOU 3265  CB  ALA B 119     7912   5211   3532  -1046    687   -796       C  
ATOM   3266  N   VAL B 120      27.916  -6.972  14.197  1.00 36.89           N  
ANISOU 3266  N   VAL B 120     6679   4412   2926  -1285    230   -727       N  
ATOM   3267  CA  VAL B 120      28.345  -7.529  12.910  1.00 33.89           C  
ANISOU 3267  CA  VAL B 120     5972   4117   2788  -1232    151   -606       C  
ATOM   3268  C   VAL B 120      29.797  -7.165  12.565  1.00 35.94           C  
ANISOU 3268  C   VAL B 120     6156   4412   3087  -1404    -83   -550       C  
ATOM   3269  O   VAL B 120      30.147  -5.989  12.514  1.00 34.42           O  
ANISOU 3269  O   VAL B 120     6100   4104   2873  -1510   -125   -627       O  
ATOM   3270  CB  VAL B 120      27.439  -7.034  11.762  1.00 26.11           C  
ANISOU 3270  CB  VAL B 120     4889   3035   1996  -1071    319   -636       C  
ATOM   3271  CG1 VAL B 120      27.795  -7.748  10.464  1.00 25.31           C  
ANISOU 3271  CG1 VAL B 120     4496   3024   2098  -1010    252   -517       C  
ATOM   3272  CG2 VAL B 120      25.967  -7.239  12.097  1.00 26.78           C  
ANISOU 3272  CG2 VAL B 120     5022   3074   2079   -908    554   -672       C  
ATOM   3273  N   THR B 121      30.631  -8.173  12.318  1.00 35.23           N  
ANISOU 3273  N   THR B 121     5841   4470   3075  -1426   -223   -403       N  
ATOM   3274  CA  THR B 121      32.028  -7.953  11.933  1.00 34.94           C  
ANISOU 3274  CA  THR B 121     5666   4486   3123  -1569   -425   -304       C  
ATOM   3275  C   THR B 121      32.109  -7.392  10.507  1.00 32.53           C  
ANISOU 3275  C   THR B 121     5215   4121   3022  -1502   -356   -292       C  
ATOM   3276  O   THR B 121      31.128  -7.457   9.772  1.00 31.05           O  
ANISOU 3276  O   THR B 121     4998   3884   2917  -1334   -183   -334       O  
ATOM   3277  CB  THR B 121      32.844  -9.273  12.035  1.00 30.16           C  
ANISOU 3277  CB  THR B 121     4837   4051   2571  -1568   -554   -126       C  
ATOM   3278  OG1 THR B 121      32.261 -10.259  11.187  1.00 27.37           O  
ANISOU 3278  OG1 THR B 121     4309   3731   2359  -1367   -410    -76       O  
ATOM   3279  CG2 THR B 121      32.853  -9.792  13.467  1.00 33.27           C  
ANISOU 3279  CG2 THR B 121     5385   4509   2748  -1651   -650   -113       C  
ATOM   3280  N   PRO B 122      33.271  -6.838  10.109  1.00 32.57           N  
ANISOU 3280  N   PRO B 122     5126   4135   3115  -1639   -496   -218       N  
ATOM   3281  CA  PRO B 122      33.382  -6.346   8.723  1.00 28.45           C  
ANISOU 3281  CA  PRO B 122     4471   3563   2776  -1571   -414   -186       C  
ATOM   3282  C   PRO B 122      33.082  -7.428   7.675  1.00 23.47           C  
ANISOU 3282  C   PRO B 122     3631   3011   2275  -1369   -298   -103       C  
ATOM   3283  O   PRO B 122      33.263  -8.606   7.938  1.00 29.49           O  
ANISOU 3283  O   PRO B 122     4284   3884   3037  -1317   -326    -24       O  
ATOM   3284  CB  PRO B 122      34.846  -5.883   8.629  1.00 33.24           C  
ANISOU 3284  CB  PRO B 122     4960   4208   3464  -1764   -595    -68       C  
ATOM   3285  CG  PRO B 122      35.224  -5.529  10.045  1.00 34.17           C  
ANISOU 3285  CG  PRO B 122     5266   4316   3401  -1977   -782   -117       C  
ATOM   3286  CD  PRO B 122      34.488  -6.552  10.897  1.00 33.33           C  
ANISOU 3286  CD  PRO B 122     5238   4278   3145  -1876   -738   -152       C  
ATOM   3287  N   VAL B 123      32.611  -7.023   6.505  1.00 27.02           N  
ANISOU 3287  N   VAL B 123     4051   3392   2825  -1261   -174   -122       N  
ATOM   3288  CA  VAL B 123      32.247  -7.957   5.439  1.00 29.98           C  
ANISOU 3288  CA  VAL B 123     4285   3815   3291  -1084    -73    -67       C  
ATOM   3289  C   VAL B 123      33.423  -8.829   4.988  1.00 26.06           C  
ANISOU 3289  C   VAL B 123     3580   3434   2888  -1076   -120     87       C  
ATOM   3290  O   VAL B 123      34.538  -8.328   4.800  1.00 25.58           O  
ANISOU 3290  O   VAL B 123     3427   3396   2898  -1182   -188    178       O  
ATOM   3291  CB  VAL B 123      31.678  -7.180   4.221  1.00 36.24           C  
ANISOU 3291  CB  VAL B 123     5105   4510   4155  -1000     33    -99       C  
ATOM   3292  CG1 VAL B 123      31.639  -8.056   2.978  1.00 21.63           C  
ANISOU 3292  CG1 VAL B 123     3129   2711   2380   -859    103    -26       C  
ATOM   3293  CG2 VAL B 123      30.288  -6.669   4.553  1.00 33.81           C  
ANISOU 3293  CG2 VAL B 123     4954   4097   3794   -936    117   -222       C  
ATOM   3294  N   LYS B 124      33.161 -10.127   4.820  1.00 23.68           N  
ANISOU 3294  N   LYS B 124     3202   3194   2600   -949    -74    125       N  
ATOM   3295  CA  LYS B 124      34.191 -11.098   4.442  1.00 29.43           C  
ANISOU 3295  CA  LYS B 124     3747   4014   3422   -902    -83    271       C  
ATOM   3296  C   LYS B 124      34.034 -11.531   2.996  1.00 25.35           C  
ANISOU 3296  C   LYS B 124     3186   3471   2976   -747     55    290       C  
ATOM   3297  O   LYS B 124      33.029 -11.241   2.354  1.00 25.09           O  
ANISOU 3297  O   LYS B 124     3259   3364   2910   -682    126    196       O  
ATOM   3298  CB  LYS B 124      34.135 -12.353   5.333  1.00 30.95           C  
ANISOU 3298  CB  LYS B 124     3908   4275   3576   -868   -129    312       C  
ATOM   3299  CG  LYS B 124      33.992 -12.095   6.822  1.00 34.06           C  
ANISOU 3299  CG  LYS B 124     4409   4691   3842  -1001   -251    273       C  
ATOM   3300  CD  LYS B 124      35.042 -11.146   7.312  1.00 51.04           C  
ANISOU 3300  CD  LYS B 124     6538   6866   5988  -1187   -399    324       C  
ATOM   3301  CE  LYS B 124      34.946 -10.962   8.821  1.00 62.10           C  
ANISOU 3301  CE  LYS B 124     8090   8285   7219  -1331   -538    281       C  
ATOM   3302  NZ  LYS B 124      35.798  -9.836   9.281  1.00 64.30           N  
ANISOU 3302  NZ  LYS B 124     8410   8551   7468  -1548   -703    292       N  
ATOM   3303  N   ASN B 125      35.026 -12.254   2.496  1.00 21.21           N  
ANISOU 3303  N   ASN B 125     2511   3003   2543   -683     95    422       N  
ATOM   3304  CA  ASN B 125      35.015 -12.698   1.115  1.00 21.77           C  
ANISOU 3304  CA  ASN B 125     2578   3042   2653   -536    242    440       C  
ATOM   3305  C   ASN B 125      35.356 -14.171   1.084  1.00 28.56           C  
ANISOU 3305  C   ASN B 125     3365   3931   3553   -412    294    513       C  
ATOM   3306  O   ASN B 125      36.450 -14.576   1.483  1.00 25.32           O  
ANISOU 3306  O   ASN B 125     2792   3592   3236   -417    273    656       O  
ATOM   3307  CB  ASN B 125      36.004 -11.891   0.272  1.00 29.75           C  
ANISOU 3307  CB  ASN B 125     3498   4060   3746   -562    305    540       C  
ATOM   3308  CG  ASN B 125      35.786 -12.064  -1.223  1.00 31.98           C  
ANISOU 3308  CG  ASN B 125     3852   4288   4010   -421    468    529       C  
ATOM   3309  OD1 ASN B 125      35.226 -13.065  -1.667  1.00 28.82           O  
ANISOU 3309  OD1 ASN B 125     3534   3857   3559   -295    531    478       O  
ATOM   3310  ND2 ASN B 125      36.229 -11.076  -2.009  1.00 33.64           N  
ANISOU 3310  ND2 ASN B 125     4051   4479   4250   -454    530    580       N  
ATOM   3311  N   GLN B 126      34.399 -14.972   0.631  1.00 29.67           N  
ANISOU 3311  N   GLN B 126     3626   4010   3637   -306    353    424       N  
ATOM   3312  CA  GLN B 126      34.575 -16.414   0.558  1.00 28.91           C  
ANISOU 3312  CA  GLN B 126     3510   3902   3573   -185    412    470       C  
ATOM   3313  C   GLN B 126      35.498 -16.826  -0.592  1.00 24.10           C  
ANISOU 3313  C   GLN B 126     2855   3273   3029    -52    573    559       C  
ATOM   3314  O   GLN B 126      35.962 -17.967  -0.646  1.00 24.86           O  
ANISOU 3314  O   GLN B 126     2913   3351   3181     64    650    629       O  
ATOM   3315  CB  GLN B 126      33.216 -17.090   0.405  1.00 24.03           C  
ANISOU 3315  CB  GLN B 126     3049   3203   2877   -142    409    344       C  
ATOM   3316  CG  GLN B 126      32.606 -16.899  -0.952  1.00 20.24           C  
ANISOU 3316  CG  GLN B 126     2707   2645   2340    -83    480    261       C  
ATOM   3317  CD  GLN B 126      31.218 -17.501  -1.019  1.00 26.59           C  
ANISOU 3317  CD  GLN B 126     3639   3377   3088    -79    431    154       C  
ATOM   3318  OE1 GLN B 126      30.248 -16.895  -0.567  1.00 23.55           O  
ANISOU 3318  OE1 GLN B 126     3274   2994   2679   -154    354     92       O  
ATOM   3319  NE2 GLN B 126      31.121 -18.708  -1.566  1.00 26.40           N  
ANISOU 3319  NE2 GLN B 126     3699   3278   3055      9    482    141       N  
ATOM   3320  N   GLY B 127      35.763 -15.892  -1.503  1.00 27.55           N  
ANISOU 3320  N   GLY B 127     3307   3702   3457    -61    644    563       N  
ATOM   3321  CA  GLY B 127      36.608 -16.159  -2.660  1.00 33.23           C  
ANISOU 3321  CA  GLY B 127     4008   4402   4217     69    834    649       C  
ATOM   3322  C   GLY B 127      36.086 -17.261  -3.568  1.00 30.12           C  
ANISOU 3322  C   GLY B 127     3805   3903   3736    222    954    567       C  
ATOM   3323  O   GLY B 127      34.893 -17.507  -3.629  1.00 30.98           O  
ANISOU 3323  O   GLY B 127     4081   3949   3742    200    874    428       O  
ATOM   3324  N   SER B 128      36.983 -17.948  -4.262  1.00 33.21           N  
ANISOU 3324  N   SER B 128     4177   4266   4177    375   1149    658       N  
ATOM   3325  CA  SER B 128      36.584 -19.001  -5.192  1.00 43.18           C  
ANISOU 3325  CA  SER B 128     5670   5401   5336    520   1279    570       C  
ATOM   3326  C   SER B 128      36.474 -20.344  -4.471  1.00 46.50           C  
ANISOU 3326  C   SER B 128     6087   5770   5813    584   1255    570       C  
ATOM   3327  O   SER B 128      37.170 -21.308  -4.789  1.00 55.93           O  
ANISOU 3327  O   SER B 128     7289   6899   7065    747   1428    639       O  
ATOM   3328  CB  SER B 128      37.581 -19.097  -6.347  1.00 44.99           C  
ANISOU 3328  CB  SER B 128     5927   5598   5570    677   1547    659       C  
ATOM   3329  OG  SER B 128      38.898 -19.225  -5.850  1.00 55.71           O  
ANISOU 3329  OG  SER B 128     7002   7035   7130    738   1645    862       O  
ATOM   3330  N   CYS B 129      35.598 -20.379  -3.483  1.00 41.34           N  
ANISOU 3330  N   CYS B 129     5423   5137   5147    462   1054    503       N  
ATOM   3331  CA  CYS B 129      35.375 -21.554  -2.657  1.00 32.02           C  
ANISOU 3331  CA  CYS B 129     4236   3914   4017    492   1004    513       C  
ATOM   3332  C   CYS B 129      33.898 -21.528  -2.343  1.00 26.65           C  
ANISOU 3332  C   CYS B 129     3690   3197   3238    372    840    365       C  
ATOM   3333  O   CYS B 129      33.377 -20.486  -1.963  1.00 24.71           O  
ANISOU 3333  O   CYS B 129     3403   3027   2960    245    722    326       O  
ATOM   3334  CB  CYS B 129      36.234 -21.508  -1.389  1.00 30.73           C  
ANISOU 3334  CB  CYS B 129     3809   3871   3996    454    930    678       C  
ATOM   3335  SG  CYS B 129      35.978 -22.841  -0.154  1.00 31.02           S  
ANISOU 3335  SG  CYS B 129     3818   3876   4093    471    840    728       S  
ATOM   3336  N   GLY B 130      33.210 -22.646  -2.529  1.00 27.60           N  
ANISOU 3336  N   GLY B 130     3972   3191   3322    413    841    289       N  
ATOM   3337  CA  GLY B 130      31.790 -22.692  -2.222  1.00 27.44           C  
ANISOU 3337  CA  GLY B 130     4044   3139   3243    294    687    178       C  
ATOM   3338  C   GLY B 130      31.510 -22.870  -0.740  1.00 26.25           C  
ANISOU 3338  C   GLY B 130     3757   3057   3160    213    578    234       C  
ATOM   3339  O   GLY B 130      30.916 -23.871  -0.326  1.00 27.11           O  
ANISOU 3339  O   GLY B 130     3923   3089   3289    206    541    221       O  
ATOM   3340  N   SER B 131      31.915 -21.880   0.054  1.00 30.37           N  
ANISOU 3340  N   SER B 131     4120   3715   3704    141    523    294       N  
ATOM   3341  CA  SER B 131      31.935 -22.002   1.512  1.00 27.70           C  
ANISOU 3341  CA  SER B 131     3667   3455   3401     72    433    368       C  
ATOM   3342  C   SER B 131      30.951 -21.085   2.260  1.00 23.81           C  
ANISOU 3342  C   SER B 131     3178   3023   2847    -64    328    299       C  
ATOM   3343  O   SER B 131      31.061 -20.920   3.470  1.00 25.42           O  
ANISOU 3343  O   SER B 131     3312   3304   3041   -132    262    352       O  
ATOM   3344  CB  SER B 131      33.350 -21.714   2.013  1.00 29.20           C  
ANISOU 3344  CB  SER B 131     3682   3749   3663     90    440    516       C  
ATOM   3345  OG  SER B 131      33.749 -20.408   1.626  1.00 27.73           O  
ANISOU 3345  OG  SER B 131     3445   3631   3461     34    437    505       O  
ATOM   3346  N   ALA B 132      29.995 -20.494   1.553  1.00 21.45           N  
ANISOU 3346  N   ALA B 132     2967   2683   2501    -95    319    190       N  
ATOM   3347  CA  ALA B 132      29.101 -19.515   2.167  1.00 23.56           C  
ANISOU 3347  CA  ALA B 132     3229   2994   2730   -193    258    135       C  
ATOM   3348  C   ALA B 132      28.282 -20.094   3.324  1.00 23.20           C  
ANISOU 3348  C   ALA B 132     3178   2953   2684   -241    223    146       C  
ATOM   3349  O   ALA B 132      27.871 -19.360   4.228  1.00 23.24           O  
ANISOU 3349  O   ALA B 132     3168   3011   2650   -309    202    132       O  
ATOM   3350  CB  ALA B 132      28.176 -18.931   1.134  1.00 15.98           C  
ANISOU 3350  CB  ALA B 132     2346   1979   1747   -197    251     46       C  
ATOM   3351  N   TRP B 133      28.053 -21.402   3.285  1.00 17.47           N  
ANISOU 3351  N   TRP B 133     2482   2158   1998   -203    231    173       N  
ATOM   3352  CA  TRP B 133      27.369 -22.096   4.378  1.00 21.36           C  
ANISOU 3352  CA  TRP B 133     2965   2650   2501   -246    214    213       C  
ATOM   3353  C   TRP B 133      28.137 -21.903   5.682  1.00 23.71           C  
ANISOU 3353  C   TRP B 133     3204   3051   2754   -277    193    299       C  
ATOM   3354  O   TRP B 133      27.535 -21.701   6.737  1.00 21.34           O  
ANISOU 3354  O   TRP B 133     2913   2794   2403   -341    186    308       O  
ATOM   3355  CB  TRP B 133      27.220 -23.585   4.067  1.00 22.88           C  
ANISOU 3355  CB  TRP B 133     3209   2730   2756   -201    225    244       C  
ATOM   3356  CG  TRP B 133      28.514 -24.301   3.787  1.00 25.22           C  
ANISOU 3356  CG  TRP B 133     3501   2998   3084   -101    268    314       C  
ATOM   3357  CD1 TRP B 133      29.138 -24.416   2.581  1.00 21.94           C  
ANISOU 3357  CD1 TRP B 133     3141   2518   2679    -13    326    281       C  
ATOM   3358  CD2 TRP B 133      29.342 -24.996   4.734  1.00 23.38           C  
ANISOU 3358  CD2 TRP B 133     3202   2798   2884    -65    271    446       C  
ATOM   3359  NE1 TRP B 133      30.294 -25.149   2.712  1.00 27.40           N  
ANISOU 3359  NE1 TRP B 133     3790   3193   3427     90    388    387       N  
ATOM   3360  CE2 TRP B 133      30.444 -25.515   4.022  1.00 20.04           C  
ANISOU 3360  CE2 TRP B 133     2773   2323   2520     58    340    496       C  
ATOM   3361  CE3 TRP B 133      29.250 -25.241   6.111  1.00 25.54           C  
ANISOU 3361  CE3 TRP B 133     3429   3139   3138   -120    227    539       C  
ATOM   3362  CZ2 TRP B 133      31.451 -26.262   4.637  1.00 21.58           C  
ANISOU 3362  CZ2 TRP B 133     2884   2531   2784    135    357    650       C  
ATOM   3363  CZ3 TRP B 133      30.247 -25.981   6.722  1.00 22.24           C  
ANISOU 3363  CZ3 TRP B 133     2950   2739   2763    -60    219    687       C  
ATOM   3364  CH2 TRP B 133      31.339 -26.484   5.983  1.00 25.51           C  
ANISOU 3364  CH2 TRP B 133     3327   3101   3266     70    279    748       C  
ATOM   3365  N   ALA B 134      29.470 -21.946   5.608  1.00 23.31           N  
ANISOU 3365  N   ALA B 134     3096   3043   2720   -235    184    373       N  
ATOM   3366  CA  ALA B 134      30.289 -21.686   6.797  1.00 24.34           C  
ANISOU 3366  CA  ALA B 134     3164   3281   2804   -289    118    470       C  
ATOM   3367  C   ALA B 134      30.280 -20.199   7.145  1.00 23.51           C  
ANISOU 3367  C   ALA B 134     3074   3246   2612   -387     78    404       C  
ATOM   3368  O   ALA B 134      30.186 -19.831   8.311  1.00 22.97           O  
ANISOU 3368  O   ALA B 134     3044   3239   2447   -472     26    417       O  
ATOM   3369  CB  ALA B 134      31.730 -22.172   6.587  1.00 24.19           C  
ANISOU 3369  CB  ALA B 134     3038   3289   2866   -216    110    601       C  
ATOM   3370  N   PHE B 135      30.391 -19.342   6.131  1.00 20.84           N  
ANISOU 3370  N   PHE B 135     2733   2887   2298   -375    106    334       N  
ATOM   3371  CA  PHE B 135      30.348 -17.900   6.370  1.00 20.68           C  
ANISOU 3371  CA  PHE B 135     2746   2900   2210   -465     76    266       C  
ATOM   3372  C   PHE B 135      29.038 -17.455   7.007  1.00 20.25           C  
ANISOU 3372  C   PHE B 135     2791   2820   2081   -507    107    175       C  
ATOM   3373  O   PHE B 135      29.041 -16.651   7.936  1.00 24.66           O  
ANISOU 3373  O   PHE B 135     3415   3411   2542   -591     79    146       O  
ATOM   3374  CB  PHE B 135      30.589 -17.136   5.066  1.00 20.20           C  
ANISOU 3374  CB  PHE B 135     2672   2804   2199   -434    116    220       C  
ATOM   3375  CG  PHE B 135      32.034 -17.031   4.727  1.00 24.92           C  
ANISOU 3375  CG  PHE B 135     3160   3450   2856   -428     98    321       C  
ATOM   3376  CD1 PHE B 135      32.680 -18.072   4.089  1.00 21.66           C  
ANISOU 3376  CD1 PHE B 135     2678   3023   2528   -318    155    406       C  
ATOM   3377  CD2 PHE B 135      32.769 -15.912   5.105  1.00 29.00           C  
ANISOU 3377  CD2 PHE B 135     3643   4020   3357   -537     28    343       C  
ATOM   3378  CE1 PHE B 135      34.034 -17.996   3.814  1.00 22.03           C  
ANISOU 3378  CE1 PHE B 135     2590   3121   2658   -296    164    529       C  
ATOM   3379  CE2 PHE B 135      34.117 -15.827   4.824  1.00 26.27           C  
ANISOU 3379  CE2 PHE B 135     3156   3727   3097   -545      6    468       C  
ATOM   3380  CZ  PHE B 135      34.751 -16.864   4.182  1.00 25.75           C  
ANISOU 3380  CZ  PHE B 135     2989   3661   3132   -416     83    570       C  
ATOM   3381  N   SER B 136      27.926 -17.958   6.479  1.00 20.89           N  
ANISOU 3381  N   SER B 136     2890   2836   2212   -450    167    133       N  
ATOM   3382  CA  SER B 136      26.609 -17.648   7.019  1.00 19.96           C  
ANISOU 3382  CA  SER B 136     2823   2692   2067   -469    223     79       C  
ATOM   3383  C   SER B 136      26.508 -18.061   8.489  1.00 26.00           C  
ANISOU 3383  C   SER B 136     3632   3506   2741   -515    230    127       C  
ATOM   3384  O   SER B 136      26.071 -17.277   9.331  1.00 29.30           O  
ANISOU 3384  O   SER B 136     4132   3935   3065   -557    275     82       O  
ATOM   3385  CB  SER B 136      25.520 -18.345   6.198  1.00 22.16           C  
ANISOU 3385  CB  SER B 136     3074   2900   2445   -418    253     67       C  
ATOM   3386  OG  SER B 136      24.274 -18.312   6.864  1.00 27.19           O  
ANISOU 3386  OG  SER B 136     3715   3525   3092   -431    317     62       O  
ATOM   3387  N   ALA B 137      26.932 -19.283   8.802  1.00 26.33           N  
ANISOU 3387  N   ALA B 137     3638   3565   2800   -500    197    223       N  
ATOM   3388  CA  ALA B 137      26.867 -19.768  10.185  1.00 25.56           C  
ANISOU 3388  CA  ALA B 137     3592   3516   2604   -544    197    293       C  
ATOM   3389  C   ALA B 137      27.751 -18.947  11.122  1.00 21.11           C  
ANISOU 3389  C   ALA B 137     3099   3031   1890   -629    119    299       C  
ATOM   3390  O   ALA B 137      27.313 -18.566  12.219  1.00 20.82           O  
ANISOU 3390  O   ALA B 137     3183   3018   1708   -684    154    278       O  
ATOM   3391  CB  ALA B 137      27.261 -21.244  10.257  1.00 24.58           C  
ANISOU 3391  CB  ALA B 137     3414   3381   2544   -504    165    415       C  
ATOM   3392  N   VAL B 138      28.987 -18.682  10.696  1.00 23.53           N  
ANISOU 3392  N   VAL B 138     3339   3375   2227   -647     17    333       N  
ATOM   3393  CA  VAL B 138      29.941 -17.966  11.546  1.00 24.85           C  
ANISOU 3393  CA  VAL B 138     3555   3616   2269   -760   -105    360       C  
ATOM   3394  C   VAL B 138      29.450 -16.542  11.851  1.00 25.10           C  
ANISOU 3394  C   VAL B 138     3736   3617   2185   -834    -69    219       C  
ATOM   3395  O   VAL B 138      29.569 -16.052  12.982  1.00 24.46           O  
ANISOU 3395  O   VAL B 138     3804   3565   1926   -936   -120    200       O  
ATOM   3396  CB  VAL B 138      31.345 -17.910  10.901  1.00 32.46           C  
ANISOU 3396  CB  VAL B 138     4373   4623   3338   -766   -212    447       C  
ATOM   3397  CG1 VAL B 138      32.209 -16.860  11.579  1.00 31.38           C  
ANISOU 3397  CG1 VAL B 138     4282   4546   3095   -917   -357    452       C  
ATOM   3398  CG2 VAL B 138      32.022 -19.277  10.968  1.00 29.74           C  
ANISOU 3398  CG2 VAL B 138     3905   4313   3083   -695   -254    614       C  
ATOM   3399  N   SER B 139      28.868 -15.896  10.847  1.00 24.48           N  
ANISOU 3399  N   SER B 139     3639   3465   2198   -779     21    122       N  
ATOM   3400  CA  SER B 139      28.333 -14.554  11.038  1.00 29.23           C  
ANISOU 3400  CA  SER B 139     4378   4006   2720   -821     81     -5       C  
ATOM   3401  C   SER B 139      27.294 -14.524  12.163  1.00 29.93           C  
ANISOU 3401  C   SER B 139     4624   4076   2673   -820    195    -51       C  
ATOM   3402  O   SER B 139      27.303 -13.628  13.018  1.00 29.09           O  
ANISOU 3402  O   SER B 139     4704   3947   2403   -897    204   -127       O  
ATOM   3403  CB  SER B 139      27.713 -14.027   9.739  1.00 26.28           C  
ANISOU 3403  CB  SER B 139     3943   3555   2487   -737    167    -71       C  
ATOM   3404  OG  SER B 139      27.536 -12.621   9.836  1.00 28.35           O  
ANISOU 3404  OG  SER B 139     4327   3750   2695   -780    201   -173       O  
ATOM   3405  N   THR B 140      26.407 -15.510  12.178  1.00 25.89           N  
ANISOU 3405  N   THR B 140     4050   3564   2223   -738    291     -3       N  
ATOM   3406  CA  THR B 140      25.380 -15.550  13.224  1.00 27.78           C  
ANISOU 3406  CA  THR B 140     4415   3789   2352   -724    435    -20       C  
ATOM   3407  C   THR B 140      25.982 -15.900  14.590  1.00 25.44           C  
ANISOU 3407  C   THR B 140     4261   3564   1841   -815    364     36       C  
ATOM   3408  O   THR B 140      25.472 -15.473  15.631  1.00 28.07           O  
ANISOU 3408  O   THR B 140     4789   3883   1994   -840    469    -12       O  
ATOM   3409  CB  THR B 140      24.255 -16.551  12.887  1.00 27.95           C  
ANISOU 3409  CB  THR B 140     4309   3791   2521   -632    549     43       C  
ATOM   3410  OG1 THR B 140      24.780 -17.886  12.858  1.00 29.83           O  
ANISOU 3410  OG1 THR B 140     4454   4074   2805   -637    454    160       O  
ATOM   3411  CG2 THR B 140      23.638 -16.224  11.539  1.00 24.92           C  
ANISOU 3411  CG2 THR B 140     3796   3342   2332   -559    581      1       C  
ATOM   3412  N   ILE B 141      27.064 -16.674  14.596  1.00 23.71           N  
ANISOU 3412  N   ILE B 141     3955   3420   1635   -859    193    146       N  
ATOM   3413  CA  ILE B 141      27.733 -17.013  15.855  1.00 31.64           C  
ANISOU 3413  CA  ILE B 141     5081   4503   2437   -955     79    228       C  
ATOM   3414  C   ILE B 141      28.416 -15.769  16.417  1.00 30.76           C  
ANISOU 3414  C   ILE B 141     5153   4395   2139  -1091    -31    139       C  
ATOM   3415  O   ILE B 141      28.339 -15.488  17.612  1.00 31.74           O  
ANISOU 3415  O   ILE B 141     5511   4533   2014  -1174    -35    114       O  
ATOM   3416  CB  ILE B 141      28.783 -18.146  15.682  1.00 30.04           C  
ANISOU 3416  CB  ILE B 141     4710   4375   2330   -955    -86    397       C  
ATOM   3417  CG1 ILE B 141      28.146 -19.408  15.093  1.00 29.96           C  
ANISOU 3417  CG1 ILE B 141     4553   4328   2501   -832     16    473       C  
ATOM   3418  CG2 ILE B 141      29.465 -18.468  17.014  1.00 31.33           C  
ANISOU 3418  CG2 ILE B 141     4994   4628   2281  -1060   -232    508       C  
ATOM   3419  CD1 ILE B 141      27.234 -20.086  16.031  1.00 38.78           C  
ANISOU 3419  CD1 ILE B 141     5766   5445   3524   -819    131    525       C  
ATOM   3420  N   GLU B 142      29.095 -15.025  15.551  1.00 28.94           N  
ANISOU 3420  N   GLU B 142     4835   4143   2019  -1124   -122     94       N  
ATOM   3421  CA  GLU B 142      29.777 -13.812  15.986  1.00 33.82           C  
ANISOU 3421  CA  GLU B 142     5618   4741   2489  -1275   -246     13       C  
ATOM   3422  C   GLU B 142      28.775 -12.845  16.609  1.00 32.36           C  
ANISOU 3422  C   GLU B 142     5712   4452   2130  -1276    -71   -155       C  
ATOM   3423  O   GLU B 142      29.049 -12.240  17.644  1.00 33.87           O  
ANISOU 3423  O   GLU B 142     6158   4627   2084  -1402   -140   -215       O  
ATOM   3424  CB  GLU B 142      30.510 -13.159  14.815  1.00 36.35           C  
ANISOU 3424  CB  GLU B 142     5778   5036   2996  -1294   -326      0       C  
ATOM   3425  CG  GLU B 142      31.676 -13.980  14.310  1.00 28.82           C  
ANISOU 3425  CG  GLU B 142     4570   4182   2198  -1298   -487    173       C  
ATOM   3426  CD  GLU B 142      32.265 -13.443  13.013  1.00 32.30           C  
ANISOU 3426  CD  GLU B 142     4837   4595   2841  -1280   -501    175       C  
ATOM   3427  OE1 GLU B 142      31.566 -12.697  12.293  1.00 28.78           O  
ANISOU 3427  OE1 GLU B 142     4435   4053   2449  -1223   -366     53       O  
ATOM   3428  OE2 GLU B 142      33.422 -13.793  12.703  1.00 33.83           O  
ANISOU 3428  OE2 GLU B 142     4842   4863   3147  -1313   -636    317       O  
ATOM   3429  N   SER B 143      27.605 -12.742  15.984  1.00 33.66           N  
ANISOU 3429  N   SER B 143     5825   4539   2425  -1127    156   -218       N  
ATOM   3430  CA  SER B 143      26.548 -11.848  16.441  1.00 34.06           C  
ANISOU 3430  CA  SER B 143     6097   4477   2369  -1079    374   -357       C  
ATOM   3431  C   SER B 143      25.953 -12.239  17.789  1.00 30.95           C  
ANISOU 3431  C   SER B 143     5896   4096   1765  -1068    492   -346       C  
ATOM   3432  O   SER B 143      25.834 -11.405  18.677  1.00 38.35           O  
ANISOU 3432  O   SER B 143     7046   4950   2576  -1088    533   -437       O  
ATOM   3433  CB  SER B 143      25.436 -11.791  15.394  1.00 33.55           C  
ANISOU 3433  CB  SER B 143     5859   4344   2544   -910    567   -375       C  
ATOM   3434  OG  SER B 143      25.929 -11.262  14.176  1.00 31.56           O  
ANISOU 3434  OG  SER B 143     5464   4060   2467   -911    474   -393       O  
ATOM   3435  N   ILE B 144      25.578 -13.505  17.944  1.00 29.70           N  
ANISOU 3435  N   ILE B 144     5626   4025   1636  -1012    542   -219       N  
ATOM   3436  CA  ILE B 144      24.915 -13.931  19.169  1.00 32.53           C  
ANISOU 3436  CA  ILE B 144     6113   4389   1859   -969    674   -185       C  
ATOM   3437  C   ILE B 144      25.887 -13.869  20.356  1.00 35.53           C  
ANISOU 3437  C   ILE B 144     6668   4811   2020  -1098    472   -168       C  
ATOM   3438  O   ILE B 144      25.474 -13.597  21.483  1.00 36.33           O  
ANISOU 3438  O   ILE B 144     6970   4874   1961  -1084    569   -209       O  
ATOM   3439  CB  ILE B 144      24.307 -15.344  19.033  1.00 35.17           C  
ANISOU 3439  CB  ILE B 144     6282   4794   2286   -897    771    -32       C  
ATOM   3440  CG1 ILE B 144      23.265 -15.584  20.133  1.00 37.00           C  
ANISOU 3440  CG1 ILE B 144     6616   5005   2437   -814    990     -8       C  
ATOM   3441  CG2 ILE B 144      25.387 -16.427  19.052  1.00 33.52           C  
ANISOU 3441  CG2 ILE B 144     5960   4696   2081   -975    526    118       C  
ATOM   3442  CD1 ILE B 144      22.151 -14.548  20.169  1.00 36.95           C  
ANISOU 3442  CD1 ILE B 144     6676   4883   2481   -701   1243   -126       C  
ATOM   3443  N   ILE B 145      27.179 -14.076  20.108  1.00 35.51           N  
ANISOU 3443  N   ILE B 145     6587   4886   2018  -1223    192    -99       N  
ATOM   3444  CA  ILE B 145      28.165 -13.923  21.174  1.00 35.81           C  
ANISOU 3444  CA  ILE B 145     6767   4961   1877  -1362    -29    -72       C  
ATOM   3445  C   ILE B 145      28.318 -12.448  21.556  1.00 42.52           C  
ANISOU 3445  C   ILE B 145     7838   5687   2630  -1440    -42   -237       C  
ATOM   3446  O   ILE B 145      28.551 -12.115  22.727  1.00 44.05           O  
ANISOU 3446  O   ILE B 145     8255   5858   2626  -1519   -102   -266       O  
ATOM   3447  CB  ILE B 145      29.533 -14.520  20.785  1.00 38.68           C  
ANISOU 3447  CB  ILE B 145     6940   5442   2314  -1471   -329     79       C  
ATOM   3448  CG1 ILE B 145      29.403 -16.032  20.565  1.00 39.29           C  
ANISOU 3448  CG1 ILE B 145     6832   5621   2474  -1389   -314    262       C  
ATOM   3449  CG2 ILE B 145      30.579 -14.253  21.872  1.00 38.12           C  
ANISOU 3449  CG2 ILE B 145     6996   5403   2085  -1629   -577    118       C  
ATOM   3450  CD1 ILE B 145      28.785 -16.778  21.737  1.00 36.50           C  
ANISOU 3450  CD1 ILE B 145     6605   5287   1977  -1339   -209    325       C  
ATOM   3451  N   LYS B 146      28.164 -11.560  20.583  1.00 36.26           N  
ANISOU 3451  N   LYS B 146     7001   4805   1971  -1417     20   -341       N  
ATOM   3452  CA  LYS B 146      28.154 -10.133  20.883  1.00 45.38           C  
ANISOU 3452  CA  LYS B 146     8374   5813   3057  -1469     49   -494       C  
ATOM   3453  C   LYS B 146      26.928  -9.780  21.698  1.00 49.51           C  
ANISOU 3453  C   LYS B 146     9109   6234   3470  -1347    328   -585       C  
ATOM   3454  O   LYS B 146      27.030  -9.119  22.735  1.00 51.77           O  
ANISOU 3454  O   LYS B 146     9660   6443   3569  -1414    319   -659       O  
ATOM   3455  CB  LYS B 146      28.186  -9.293  19.607  1.00 46.94           C  
ANISOU 3455  CB  LYS B 146     8467   5930   3439  -1453     73   -567       C  
ATOM   3456  CG  LYS B 146      27.781  -7.834  19.822  1.00 46.78           C  
ANISOU 3456  CG  LYS B 146     8673   5722   3379  -1445    195   -723       C  
ATOM   3457  CD  LYS B 146      28.757  -7.081  20.708  1.00 51.60           C  
ANISOU 3457  CD  LYS B 146     9496   6284   3826  -1636    -11   -758       C  
ATOM   3458  CE  LYS B 146      28.248  -5.663  21.001  1.00 59.16           C  
ANISOU 3458  CE  LYS B 146    10715   7036   4726  -1615    140   -912       C  
ATOM   3459  NZ  LYS B 146      29.209  -4.869  21.819  1.00 63.30           N  
ANISOU 3459  NZ  LYS B 146    11467   7497   5087  -1820    -69   -950       N  
ATOM   3460  N   ILE B 147      25.767 -10.223  21.227  1.00 48.54           N  
ANISOU 3460  N   ILE B 147     8866   6108   3470  -1171    580   -571       N  
ATOM   3461  CA  ILE B 147      24.512  -9.931  21.919  1.00 44.12           C  
ANISOU 3461  CA  ILE B 147     8454   5458   2853  -1032    876   -628       C  
ATOM   3462  C   ILE B 147      24.549 -10.413  23.373  1.00 42.66           C  
ANISOU 3462  C   ILE B 147     8463   5320   2425  -1072    869   -589       C  
ATOM   3463  O   ILE B 147      24.190  -9.673  24.288  1.00 52.58           O  
ANISOU 3463  O   ILE B 147     9982   6473   3524  -1062    987   -681       O  
ATOM   3464  CB  ILE B 147      23.318 -10.560  21.174  1.00 43.33           C  
ANISOU 3464  CB  ILE B 147     8127   5379   2957   -852   1116   -565       C  
ATOM   3465  CG1 ILE B 147      23.105  -9.830  19.846  1.00 39.19           C  
ANISOU 3465  CG1 ILE B 147     7469   4774   2648   -795   1161   -627       C  
ATOM   3466  CG2 ILE B 147      22.048 -10.516  22.023  1.00 41.14           C  
ANISOU 3466  CG2 ILE B 147     7954   5044   2634   -711   1416   -570       C  
ATOM   3467  CD1 ILE B 147      22.368 -10.634  18.827  1.00 35.97           C  
ANISOU 3467  CD1 ILE B 147     6783   4423   2460   -681   1275   -537       C  
ATOM   3468  N   ARG B 148      25.026 -11.634  23.584  1.00 51.83           N  
ANISOU 3468  N   ARG B 148     9510   6632   3551  -1120    727   -448       N  
ATOM   3469  CA  ARG B 148      25.055 -12.228  24.922  1.00 55.96           C  
ANISOU 3469  CA  ARG B 148    10198   7216   3848  -1152    715   -385       C  
ATOM   3470  C   ARG B 148      26.151 -11.676  25.841  1.00 59.32           C  
ANISOU 3470  C   ARG B 148    10864   7628   4045  -1335    466   -428       C  
ATOM   3471  O   ARG B 148      25.910 -11.464  27.026  1.00 60.87           O  
ANISOU 3471  O   ARG B 148    11324   7788   4016  -1350    536   -467       O  
ATOM   3472  CB  ARG B 148      25.213 -13.744  24.815  1.00 55.38           C  
ANISOU 3472  CB  ARG B 148     9915   7298   3830  -1138    641   -196       C  
ATOM   3473  CG  ARG B 148      23.971 -14.448  24.340  1.00 61.54           C  
ANISOU 3473  CG  ARG B 148    10516   8089   4780   -972    913   -129       C  
ATOM   3474  CD  ARG B 148      22.800 -14.129  25.250  1.00 70.40           C  
ANISOU 3474  CD  ARG B 148    11805   9142   5802   -863   1210   -175       C  
ATOM   3475  NE  ARG B 148      21.631 -13.749  24.468  1.00 73.10           N  
ANISOU 3475  NE  ARG B 148    12008   9401   6365   -714   1475   -216       N  
ATOM   3476  CZ  ARG B 148      20.676 -14.595  24.104  1.00 73.42           C  
ANISOU 3476  CZ  ARG B 148    11833   9482   6583   -606   1656    -99       C  
ATOM   3477  NH1 ARG B 148      20.748 -15.866  24.470  1.00 76.28           N  
ANISOU 3477  NH1 ARG B 148    12111   9953   6917   -628   1614     61       N  
ATOM   3478  NH2 ARG B 148      19.647 -14.170  23.385  1.00 70.81           N  
ANISOU 3478  NH2 ARG B 148    11360   9073   6470   -480   1871   -126       N  
ATOM   3479  N   THR B 149      27.348 -11.453  25.304  1.00 55.52           N  
ANISOU 3479  N   THR B 149    10291   7178   3627  -1481    176   -410       N  
ATOM   3480  CA  THR B 149      28.497 -11.102  26.142  1.00 51.96           C  
ANISOU 3480  CA  THR B 149    10013   6738   2992  -1679   -106   -405       C  
ATOM   3481  C   THR B 149      29.000  -9.668  25.970  1.00 55.91           C  
ANISOU 3481  C   THR B 149    10661   7099   3483  -1798   -197   -543       C  
ATOM   3482  O   THR B 149      29.812  -9.202  26.766  1.00 63.00           O  
ANISOU 3482  O   THR B 149    11752   7974   4210  -1971   -404   -558       O  
ATOM   3483  CB  THR B 149      29.687 -12.054  25.878  1.00 53.26           C  
ANISOU 3483  CB  THR B 149     9942   7063   3233  -1786   -417   -222       C  
ATOM   3484  OG1 THR B 149      30.190 -11.853  24.548  1.00 45.50           O  
ANISOU 3484  OG1 THR B 149     8708   6089   2492  -1804   -510   -208       O  
ATOM   3485  CG2 THR B 149      29.260 -13.498  26.046  1.00 50.10           C  
ANISOU 3485  CG2 THR B 149     9403   6787   2847  -1674   -341    -67       C  
ATOM   3486  N   GLY B 150      28.540  -8.975  24.932  1.00 58.32           N  
ANISOU 3486  N   GLY B 150    10878   7308   3972  -1715    -54   -633       N  
ATOM   3487  CA  GLY B 150      28.958  -7.603  24.690  1.00 49.49           C  
ANISOU 3487  CA  GLY B 150     9893   6046   2865  -1816   -119   -753       C  
ATOM   3488  C   GLY B 150      30.286  -7.479  23.961  1.00 48.48           C  
ANISOU 3488  C   GLY B 150     9572   5979   2868  -1983   -429   -677       C  
ATOM   3489  O   GLY B 150      30.792  -6.376  23.750  1.00 53.36           O  
ANISOU 3489  O   GLY B 150    10281   6489   3505  -2094   -520   -750       O  
ATOM   3490  N   ASN B 151      30.855  -8.617  23.577  1.00 56.88           N  
ANISOU 3490  N   ASN B 151    10365   7214   4032  -1997   -582   -516       N  
ATOM   3491  CA  ASN B 151      32.125  -8.642  22.860  1.00 54.48           C  
ANISOU 3491  CA  ASN B 151     9831   6989   3881  -2136   -861   -407       C  
ATOM   3492  C   ASN B 151      31.967  -9.185  21.449  1.00 45.38           C  
ANISOU 3492  C   ASN B 151     8363   5904   2975  -2022   -793   -348       C  
ATOM   3493  O   ASN B 151      31.505 -10.311  21.260  1.00 42.81           O  
ANISOU 3493  O   ASN B 151     7897   5677   2691  -1901   -706   -265       O  
ATOM   3494  CB  ASN B 151      33.152  -9.486  23.616  1.00 47.54           C  
ANISOU 3494  CB  ASN B 151     8885   6254   2923  -2266  -1138   -235       C  
ATOM   3495  CG  ASN B 151      33.435  -8.955  24.996  1.00 53.56           C  
ANISOU 3495  CG  ASN B 151     9968   6957   3427  -2409  -1248   -284       C  
ATOM   3496  OD1 ASN B 151      33.548  -7.746  25.198  1.00 59.44           O  
ANISOU 3496  OD1 ASN B 151    10925   7561   4099  -2507  -1262   -409       O  
ATOM   3497  ND2 ASN B 151      33.536  -9.857  25.964  1.00 58.32           N  
ANISOU 3497  ND2 ASN B 151    10623   7660   3877  -2422  -1325   -183       N  
ATOM   3498  N   LEU B 152      32.353  -8.382  20.463  1.00 49.20           N  
ANISOU 3498  N   LEU B 152     8750   6329   3615  -2065   -833   -386       N  
ATOM   3499  CA  LEU B 152      32.310  -8.796  19.061  1.00 43.06           C  
ANISOU 3499  CA  LEU B 152     7691   5610   3060  -1977   -788   -335       C  
ATOM   3500  C   LEU B 152      33.617  -9.470  18.676  1.00 41.16           C  
ANISOU 3500  C   LEU B 152     7175   5521   2942  -2083  -1055   -142       C  
ATOM   3501  O   LEU B 152      34.670  -8.838  18.688  1.00 42.29           O  
ANISOU 3501  O   LEU B 152     7280   5657   3130  -2242  -1257    -94       O  
ATOM   3502  CB  LEU B 152      32.053  -7.598  18.149  1.00 44.07           C  
ANISOU 3502  CB  LEU B 152     7847   5596   3302  -1959   -684   -460       C  
ATOM   3503  CG  LEU B 152      31.848  -7.945  16.670  1.00 41.27           C  
ANISOU 3503  CG  LEU B 152     7242   5283   3156  -1858   -607   -432       C  
ATOM   3504  CD1 LEU B 152      30.575  -8.753  16.492  1.00 32.08           C  
ANISOU 3504  CD1 LEU B 152     6060   4139   1991  -1662   -365   -457       C  
ATOM   3505  CD2 LEU B 152      31.824  -6.704  15.807  1.00 39.52           C  
ANISOU 3505  CD2 LEU B 152     7043   4921   3050  -1871   -552   -530       C  
ATOM   3506  N   ASN B 153      33.560 -10.753  18.345  1.00 42.50           N  
ANISOU 3506  N   ASN B 153     7143   5825   3181  -1989  -1050    -13       N  
ATOM   3507  CA  ASN B 153      34.762 -11.455  17.924  1.00 41.31           C  
ANISOU 3507  CA  ASN B 153     6698   5818   3181  -2051  -1275    197       C  
ATOM   3508  C   ASN B 153      34.628 -11.992  16.510  1.00 36.91           C  
ANISOU 3508  C   ASN B 153     5881   5314   2831  -1927  -1188    250       C  
ATOM   3509  O   ASN B 153      33.531 -12.100  15.978  1.00 34.69           O  
ANISOU 3509  O   ASN B 153     5618   4957   2603  -1754   -933    147       O  
ATOM   3510  CB  ASN B 153      35.083 -12.605  18.873  1.00 41.74           C  
ANISOU 3510  CB  ASN B 153     6718   5987   3155  -2050  -1388    358       C  
ATOM   3511  CG  ASN B 153      35.216 -12.153  20.309  1.00 51.55           C  
ANISOU 3511  CG  ASN B 153     8227   7182   4178  -2169  -1477    310       C  
ATOM   3512  OD1 ASN B 153      36.261 -11.648  20.718  1.00 53.41           O  
ANISOU 3512  OD1 ASN B 153     8456   7425   4412  -2337  -1702    374       O  
ATOM   3513  ND2 ASN B 153      34.152 -12.337  21.087  1.00 47.44           N  
ANISOU 3513  ND2 ASN B 153     7942   6612   3471  -2085  -1297    209       N  
ATOM   3514  N   GLU B 154      35.762 -12.327  15.910  1.00 37.24           N  
ANISOU 3514  N   GLU B 154     5623   5442   3086  -1949  -1335    428       N  
ATOM   3515  CA  GLU B 154      35.776 -12.999  14.630  1.00 36.54           C  
ANISOU 3515  CA  GLU B 154     5243   5364   3276  -1752  -1185    506       C  
ATOM   3516  C   GLU B 154      36.168 -14.453  14.806  1.00 34.84           C  
ANISOU 3516  C   GLU B 154     4836   5258   3143  -1650  -1227    708       C  
ATOM   3517  O   GLU B 154      37.228 -14.765  15.370  1.00 34.58           O  
ANISOU 3517  O   GLU B 154     4690   5331   3119  -1756  -1456    890       O  
ATOM   3518  CB  GLU B 154      36.726 -12.284  13.670  1.00 47.65           C  
ANISOU 3518  CB  GLU B 154     6453   6765   4886  -1813  -1250    561       C  
ATOM   3519  CG  GLU B 154      36.247 -10.881  13.337  1.00 56.51           C  
ANISOU 3519  CG  GLU B 154     7762   7751   5958  -1885  -1175    366       C  
ATOM   3520  CD  GLU B 154      37.067 -10.209  12.266  1.00 58.80           C  
ANISOU 3520  CD  GLU B 154     7856   8023   6462  -1926  -1197    428       C  
ATOM   3521  OE1 GLU B 154      38.311 -10.247  12.355  1.00 70.25           O  
ANISOU 3521  OE1 GLU B 154     9113   9564   8016  -2052  -1394    605       O  
ATOM   3522  OE2 GLU B 154      36.465  -9.636  11.337  1.00 43.93           O  
ANISOU 3522  OE2 GLU B 154     6004   6038   4651  -1832  -1016    317       O  
ATOM   3523  N   TYR B 155      35.304 -15.343  14.329  1.00 32.29           N  
ANISOU 3523  N   TYR B 155     4477   4900   2891  -1450  -1017    685       N  
ATOM   3524  CA  TYR B 155      35.551 -16.775  14.445  1.00 31.95           C  
ANISOU 3524  CA  TYR B 155     4281   4923   2937  -1333  -1023    862       C  
ATOM   3525  C   TYR B 155      35.883 -17.426  13.102  1.00 32.64           C  
ANISOU 3525  C   TYR B 155     4117   4988   3298  -1157   -900    939       C  
ATOM   3526  O   TYR B 155      35.749 -16.811  12.042  1.00 26.45           O  
ANISOU 3526  O   TYR B 155     3295   4141   2615  -1113   -789    843       O  
ATOM   3527  CB  TYR B 155      34.343 -17.452  15.098  1.00 29.87           C  
ANISOU 3527  CB  TYR B 155     4196   4625   2528  -1260   -893    800       C  
ATOM   3528  CG  TYR B 155      34.128 -16.963  16.513  1.00 30.30           C  
ANISOU 3528  CG  TYR B 155     4519   4709   2285  -1419   -999    752       C  
ATOM   3529  CD1 TYR B 155      35.044 -17.256  17.509  1.00 32.69           C  
ANISOU 3529  CD1 TYR B 155     4827   5118   2474  -1547  -1244    916       C  
ATOM   3530  CD2 TYR B 155      33.023 -16.198  16.847  1.00 33.22           C  
ANISOU 3530  CD2 TYR B 155     5145   4996   2482  -1438   -851    553       C  
ATOM   3531  CE1 TYR B 155      34.865 -16.809  18.804  1.00 37.84           C  
ANISOU 3531  CE1 TYR B 155     5768   5789   2822  -1699  -1345    864       C  
ATOM   3532  CE2 TYR B 155      32.833 -15.745  18.143  1.00 32.09           C  
ANISOU 3532  CE2 TYR B 155     5291   4863   2038  -1573   -918    497       C  
ATOM   3533  CZ  TYR B 155      33.759 -16.053  19.114  1.00 34.87           C  
ANISOU 3533  CZ  TYR B 155     5662   5305   2280  -1695  -1155    639       C  
ATOM   3534  OH  TYR B 155      33.576 -15.615  20.399  1.00 36.77           O  
ANISOU 3534  OH  TYR B 155     6160   5500   2309  -1774  -1171    558       O  
ATOM   3535  N   SER B 156      36.324 -18.678  13.161  1.00 33.63           N  
ANISOU 3535  N   SER B 156     4093   5154   3531  -1050   -913   1118       N  
ATOM   3536  CA  SER B 156      36.918 -19.333  12.002  1.00 30.67           C  
ANISOU 3536  CA  SER B 156     3489   4757   3407   -886   -810   1221       C  
ATOM   3537  C   SER B 156      35.930 -20.031  11.072  1.00 28.29           C  
ANISOU 3537  C   SER B 156     3237   4339   3172   -707   -578   1112       C  
ATOM   3538  O   SER B 156      35.354 -21.068  11.431  1.00 25.88           O  
ANISOU 3538  O   SER B 156     2988   3998   2845   -629   -526   1138       O  
ATOM   3539  CB  SER B 156      37.955 -20.359  12.462  1.00 33.28           C  
ANISOU 3539  CB  SER B 156     3628   5168   3851   -838   -925   1485       C  
ATOM   3540  OG  SER B 156      38.454 -21.074  11.345  1.00 34.10           O  
ANISOU 3540  OG  SER B 156     3540   5224   4193   -646   -774   1576       O  
ATOM   3541  N   GLU B 157      35.770 -19.480   9.869  1.00 24.34           N  
ANISOU 3541  N   GLU B 157     2720   3775   2753   -653   -453   1002       N  
ATOM   3542  CA  GLU B 157      35.038 -20.168   8.804  1.00 28.62           C  
ANISOU 3542  CA  GLU B 157     3296   4207   3372   -492   -265    921       C  
ATOM   3543  C   GLU B 157      35.805 -21.392   8.330  1.00 31.79           C  
ANISOU 3543  C   GLU B 157     3554   4585   3939   -334   -201   1079       C  
ATOM   3544  O   GLU B 157      35.208 -22.407   7.964  1.00 27.04           O  
ANISOU 3544  O   GLU B 157     3016   3886   3371   -216    -92   1051       O  
ATOM   3545  CB  GLU B 157      34.787 -19.250   7.604  1.00 25.30           C  
ANISOU 3545  CB  GLU B 157     2902   3731   2980   -477   -166    788       C  
ATOM   3546  CG  GLU B 157      33.758 -18.154   7.847  1.00 25.14           C  
ANISOU 3546  CG  GLU B 157     3042   3685   2824   -581   -172    614       C  
ATOM   3547  CD  GLU B 157      34.394 -16.859   8.297  1.00 25.09           C  
ANISOU 3547  CD  GLU B 157     3034   3736   2764   -736   -289    611       C  
ATOM   3548  OE1 GLU B 157      35.646 -16.776   8.317  1.00 28.29           O  
ANISOU 3548  OE1 GLU B 157     3284   4210   3253   -777   -379    753       O  
ATOM   3549  OE2 GLU B 157      33.642 -15.921   8.628  1.00 30.50           O  
ANISOU 3549  OE2 GLU B 157     3869   4385   3334   -818   -290    475       O  
ATOM   3550  N   GLN B 158      37.133 -21.283   8.319  1.00 27.27           N  
ANISOU 3550  N   GLN B 158     2786   4091   3484   -331   -265   1252       N  
ATOM   3551  CA  GLN B 158      37.970 -22.353   7.802  1.00 31.93           C  
ANISOU 3551  CA  GLN B 158     3220   4651   4260   -153   -169   1420       C  
ATOM   3552  C   GLN B 158      37.780 -23.597   8.656  1.00 30.03           C  
ANISOU 3552  C   GLN B 158     3004   4390   4017    -96   -208   1524       C  
ATOM   3553  O   GLN B 158      37.800 -24.729   8.150  1.00 31.32           O  
ANISOU 3553  O   GLN B 158     3164   4447   4290     79    -70   1572       O  
ATOM   3554  CB  GLN B 158      39.452 -21.931   7.762  1.00 28.32           C  
ANISOU 3554  CB  GLN B 158     2503   4301   3957   -172   -239   1626       C  
ATOM   3555  CG  GLN B 158      40.381 -23.018   7.216  1.00 31.49           C  
ANISOU 3555  CG  GLN B 158     2718   4666   4580     45   -102   1825       C  
ATOM   3556  CD  GLN B 158      40.284 -23.189   5.705  1.00 32.94           C  
ANISOU 3556  CD  GLN B 158     2956   4726   4833    220    167   1728       C  
ATOM   3557  OE1 GLN B 158      40.060 -22.228   4.978  1.00 30.04           O  
ANISOU 3557  OE1 GLN B 158     2648   4354   4410    162    220   1596       O  
ATOM   3558  NE2 GLN B 158      40.458 -24.423   5.231  1.00 32.51           N  
ANISOU 3558  NE2 GLN B 158     2904   4559   4889    436    341   1794       N  
ATOM   3559  N   GLU B 159      37.568 -23.387   9.951  1.00 27.59           N  
ANISOU 3559  N   GLU B 159     2748   4167   3568   -244   -388   1554       N  
ATOM   3560  CA  GLU B 159      37.389 -24.502  10.869  1.00 29.01           C  
ANISOU 3560  CA  GLU B 159     2961   4339   3725   -208   -438   1674       C  
ATOM   3561  C   GLU B 159      36.163 -25.336  10.477  1.00 30.84           C  
ANISOU 3561  C   GLU B 159     3365   4419   3933   -115   -274   1539       C  
ATOM   3562  O   GLU B 159      36.220 -26.561  10.424  1.00 33.09           O  
ANISOU 3562  O   GLU B 159     3638   4615   4320     17   -204   1639       O  
ATOM   3563  CB  GLU B 159      37.243 -24.001  12.310  1.00 31.84           C  
ANISOU 3563  CB  GLU B 159     3404   4813   3879   -401   -647   1702       C  
ATOM   3564  CG  GLU B 159      37.359 -25.109  13.363  1.00 35.69           C  
ANISOU 3564  CG  GLU B 159     3894   5324   4344   -375   -735   1893       C  
ATOM   3565  CD  GLU B 159      37.492 -24.566  14.784  1.00 43.79           C  
ANISOU 3565  CD  GLU B 159     5005   6484   5148   -574   -970   1955       C  
ATOM   3566  OE1 GLU B 159      36.989 -23.458  15.056  1.00 45.55           O  
ANISOU 3566  OE1 GLU B 159     5384   6738   5187   -726  -1008   1779       O  
ATOM   3567  OE2 GLU B 159      38.115 -25.238  15.631  1.00 45.84           O  
ANISOU 3567  OE2 GLU B 159     5193   6813   5411   -578  -1119   2184       O  
ATOM   3568  N   LEU B 160      35.060 -24.662  10.203  1.00 27.93           N  
ANISOU 3568  N   LEU B 160     3153   4014   3446   -189   -221   1322       N  
ATOM   3569  CA  LEU B 160      33.840 -25.351   9.808  1.00 25.73           C  
ANISOU 3569  CA  LEU B 160     3017   3600   3160   -134    -95   1201       C  
ATOM   3570  C   LEU B 160      34.021 -26.001   8.445  1.00 31.85           C  
ANISOU 3570  C   LEU B 160     3779   4240   4084     25     53   1171       C  
ATOM   3571  O   LEU B 160      33.608 -27.146   8.239  1.00 27.20           O  
ANISOU 3571  O   LEU B 160     3260   3520   3555    112    131   1182       O  
ATOM   3572  CB  LEU B 160      32.656 -24.385   9.791  1.00 24.70           C  
ANISOU 3572  CB  LEU B 160     3018   3471   2895   -244    -76   1003       C  
ATOM   3573  CG  LEU B 160      32.438 -23.621  11.099  1.00 31.97           C  
ANISOU 3573  CG  LEU B 160     4005   4503   3639   -393   -185   1001       C  
ATOM   3574  CD1 LEU B 160      31.130 -22.852  11.081  1.00 29.80           C  
ANISOU 3574  CD1 LEU B 160     3863   4197   3262   -458   -114    820       C  
ATOM   3575  CD2 LEU B 160      32.524 -24.544  12.315  1.00 35.59           C  
ANISOU 3575  CD2 LEU B 160     4484   4996   4041   -408   -252   1160       C  
ATOM   3576  N   LEU B 161      34.661 -25.270   7.530  1.00 27.82           N  
ANISOU 3576  N   LEU B 161     3196   3751   3622     57     97   1136       N  
ATOM   3577  CA  LEU B 161      34.964 -25.782   6.199  1.00 24.06           C  
ANISOU 3577  CA  LEU B 161     2732   3153   3256    215    258   1108       C  
ATOM   3578  C   LEU B 161      35.725 -27.114   6.250  1.00 26.16           C  
ANISOU 3578  C   LEU B 161     2932   3339   3667    379    328   1281       C  
ATOM   3579  O   LEU B 161      35.358 -28.068   5.561  1.00 30.24           O  
ANISOU 3579  O   LEU B 161     3577   3686   4228    493    455   1225       O  
ATOM   3580  CB  LEU B 161      35.773 -24.746   5.405  1.00 24.53           C  
ANISOU 3580  CB  LEU B 161     2691   3280   3350    222    296   1103       C  
ATOM   3581  CG  LEU B 161      36.109 -25.146   3.966  1.00 34.77           C  
ANISOU 3581  CG  LEU B 161     4031   4456   4725    389    492   1068       C  
ATOM   3582  CD1 LEU B 161      34.907 -24.912   3.092  1.00 36.04           C  
ANISOU 3582  CD1 LEU B 161     4405   4517   4771    356    537    848       C  
ATOM   3583  CD2 LEU B 161      37.308 -24.362   3.441  1.00 42.69           C  
ANISOU 3583  CD2 LEU B 161     4860   5545   5813    424    547   1167       C  
ATOM   3584  N   ASP B 162      36.782 -27.173   7.067  1.00 30.74           N  
ANISOU 3584  N   ASP B 162     3322   4034   4326    387    238   1496       N  
ATOM   3585  CA  ASP B 162      37.570 -28.399   7.227  1.00 29.35           C  
ANISOU 3585  CA  ASP B 162     3051   3789   4312    557    298   1700       C  
ATOM   3586  C   ASP B 162      36.887 -29.493   8.053  1.00 33.75           C  
ANISOU 3586  C   ASP B 162     3720   4262   4843    557    257   1743       C  
ATOM   3587  O   ASP B 162      37.067 -30.678   7.782  1.00 33.19           O  
ANISOU 3587  O   ASP B 162     3682   4035   4894    719    374   1820       O  
ATOM   3588  CB  ASP B 162      38.913 -28.111   7.901  1.00 31.20           C  
ANISOU 3588  CB  ASP B 162     3012   4186   4656    554    178   1956       C  
ATOM   3589  CG  ASP B 162      39.782 -27.175   7.107  1.00 35.91           C  
ANISOU 3589  CG  ASP B 162     3451   4860   5335    568    233   1976       C  
ATOM   3590  OD1 ASP B 162      39.466 -26.904   5.929  1.00 40.69           O  
ANISOU 3590  OD1 ASP B 162     4165   5375   5921    627    402   1808       O  
ATOM   3591  OD2 ASP B 162      40.792 -26.717   7.677  1.00 39.53           O  
ANISOU 3591  OD2 ASP B 162     3674   5470   5877    509     94   2174       O  
ATOM   3592  N   CYS B 163      36.141 -29.094   9.080  1.00 28.85           N  
ANISOU 3592  N   CYS B 163     3164   3734   4065    380    108   1704       N  
ATOM   3593  CA  CYS B 163      35.789 -30.025  10.148  1.00 29.76           C  
ANISOU 3593  CA  CYS B 163     3328   3821   4157    365     42   1825       C  
ATOM   3594  C   CYS B 163      34.343 -30.539  10.127  1.00 28.66           C  
ANISOU 3594  C   CYS B 163     3400   3549   3941    313    104   1673       C  
ATOM   3595  O   CYS B 163      34.034 -31.527  10.793  1.00 29.62           O  
ANISOU 3595  O   CYS B 163     3575   3598   4080    329     97   1779       O  
ATOM   3596  CB  CYS B 163      36.074 -29.379  11.505  1.00 30.37           C  
ANISOU 3596  CB  CYS B 163     3338   4098   4102    208   -168   1942       C  
ATOM   3597  SG  CYS B 163      37.842 -29.023  11.789  1.00 41.21           S  
ANISOU 3597  SG  CYS B 163     4424   5633   5601    240   -309   2203       S  
ATOM   3598  N   ASP B 164      33.463 -29.877   9.386  1.00 28.21           N  
ANISOU 3598  N   ASP B 164     3446   3460   3812    245    156   1448       N  
ATOM   3599  CA  ASP B 164      32.065 -30.306   9.342  1.00 34.35           C  
ANISOU 3599  CA  ASP B 164     4384   4122   4544    178    197   1325       C  
ATOM   3600  C   ASP B 164      31.897 -31.503   8.395  1.00 29.62           C  
ANISOU 3600  C   ASP B 164     3889   3290   4073    300    317   1293       C  
ATOM   3601  O   ASP B 164      31.854 -31.338   7.183  1.00 30.10           O  
ANISOU 3601  O   ASP B 164     4015   3264   4157    351    395   1154       O  
ATOM   3602  CB  ASP B 164      31.159 -29.140   8.917  1.00 24.30           C  
ANISOU 3602  CB  ASP B 164     3165   2903   3164     62    191   1121       C  
ATOM   3603  CG  ASP B 164      29.686 -29.544   8.838  1.00 28.32           C  
ANISOU 3603  CG  ASP B 164     3796   3305   3660    -13    224   1020       C  
ATOM   3604  OD1 ASP B 164      29.348 -30.678   9.256  1.00 30.29           O  
ANISOU 3604  OD1 ASP B 164     4094   3448   3965     -2    242   1107       O  
ATOM   3605  OD2 ASP B 164      28.879 -28.732   8.350  1.00 29.02           O  
ANISOU 3605  OD2 ASP B 164     3918   3411   3699    -85    228    870       O  
ATOM   3606  N   ARG B 165      31.772 -32.704   8.954  1.00 29.82           N  
ANISOU 3606  N   ARG B 165     3960   3203   4168    338    329   1417       N  
ATOM   3607  CA  ARG B 165      31.725 -33.921   8.135  1.00 30.83           C  
ANISOU 3607  CA  ARG B 165     4215   3077   4422    457    442   1398       C  
ATOM   3608  C   ARG B 165      30.435 -34.141   7.325  1.00 33.78           C  
ANISOU 3608  C   ARG B 165     4771   3290   4774    365    468   1197       C  
ATOM   3609  O   ARG B 165      30.397 -35.028   6.469  1.00 31.75           O  
ANISOU 3609  O   ARG B 165     4664   2806   4593    445    552   1138       O  
ATOM   3610  CB  ARG B 165      31.963 -35.147   9.013  1.00 34.49           C  
ANISOU 3610  CB  ARG B 165     4680   3448   4979    519    442   1606       C  
ATOM   3611  CG  ARG B 165      33.417 -35.425   9.327  1.00 44.13           C  
ANISOU 3611  CG  ARG B 165     5745   4717   6304    687    454   1826       C  
ATOM   3612  CD  ARG B 165      33.591 -36.909   9.644  1.00 58.58           C  
ANISOU 3612  CD  ARG B 165     7640   6341   8277    808    515   1993       C  
ATOM   3613  NE  ARG B 165      34.852 -37.193  10.318  1.00 71.23           N  
ANISOU 3613  NE  ARG B 165     9057   8026   9983    945    482   2268       N  
ATOM   3614  CZ  ARG B 165      34.980 -37.312  11.635  1.00 81.02           C  
ANISOU 3614  CZ  ARG B 165    10209   9396  11178    881    343   2478       C  
ATOM   3615  NH1 ARG B 165      33.919 -37.178  12.419  1.00 82.42           N  
ANISOU 3615  NH1 ARG B 165    10482   9631  11205    694    260   2434       N  
ATOM   3616  NH2 ARG B 165      36.167 -37.571  12.169  1.00 83.18           N  
ANISOU 3616  NH2 ARG B 165    10298   9745  11559   1006    289   2746       N  
ATOM   3617  N   ARG B 166      29.391 -33.355   7.594  1.00 27.10           N  
ANISOU 3617  N   ARG B 166     3918   2551   3828    198    395   1101       N  
ATOM   3618  CA  ARG B 166      28.138 -33.454   6.842  1.00 26.88           C  
ANISOU 3618  CA  ARG B 166     4017   2399   3797     92    386    937       C  
ATOM   3619  C   ARG B 166      28.174 -32.588   5.609  1.00 31.17           C  
ANISOU 3619  C   ARG B 166     4599   2960   4284    104    395    764       C  
ATOM   3620  O   ARG B 166      27.407 -32.796   4.676  1.00 38.04           O  
ANISOU 3620  O   ARG B 166     5603   3695   5155     50    381    630       O  
ATOM   3621  CB  ARG B 166      26.925 -33.039   7.685  1.00 29.36           C  
ANISOU 3621  CB  ARG B 166     4282   2813   4062    -77    324    941       C  
ATOM   3622  CG  ARG B 166      26.518 -34.016   8.771  1.00 39.00           C  
ANISOU 3622  CG  ARG B 166     5507   3977   5332   -123    327   1099       C  
ATOM   3623  CD  ARG B 166      26.880 -33.494  10.148  1.00 49.38           C  
ANISOU 3623  CD  ARG B 166     6715   5501   6547   -139    305   1238       C  
ATOM   3624  NE  ARG B 166      26.714 -34.520  11.171  1.00 58.01           N  
ANISOU 3624  NE  ARG B 166     7829   6535   7675   -156    317   1419       N  
ATOM   3625  CZ  ARG B 166      25.607 -34.682  11.884  1.00 62.21           C  
ANISOU 3625  CZ  ARG B 166     8370   7075   8192   -279    336   1465       C  
ATOM   3626  NH1 ARG B 166      24.573 -33.873  11.692  1.00 66.38           N  
ANISOU 3626  NH1 ARG B 166     8869   7668   8686   -384    347   1346       N  
ATOM   3627  NH2 ARG B 166      25.536 -35.653  12.784  1.00 59.24           N  
ANISOU 3627  NH2 ARG B 166     8023   6638   7848   -288    356   1648       N  
ATOM   3628  N   SER B 167      29.052 -31.596   5.617  1.00 27.52           N  
ANISOU 3628  N   SER B 167     4021   2665   3769    160    403    777       N  
ATOM   3629  CA  SER B 167      29.159 -30.682   4.492  1.00 28.40           C  
ANISOU 3629  CA  SER B 167     4162   2807   3822    173    421    635       C  
ATOM   3630  C   SER B 167      30.254 -31.158   3.539  1.00 27.64           C  
ANISOU 3630  C   SER B 167     4131   2599   3771    348    542    638       C  
ATOM   3631  O   SER B 167      30.893 -32.177   3.777  1.00 27.61           O  
ANISOU 3631  O   SER B 167     4140   2490   3860    464    612    750       O  
ATOM   3632  CB  SER B 167      29.427 -29.257   4.992  1.00 22.61           C  
ANISOU 3632  CB  SER B 167     3278   2301   3011    118    371    643       C  
ATOM   3633  OG  SER B 167      28.302 -28.741   5.699  1.00 24.97           O  
ANISOU 3633  OG  SER B 167     3554   2677   3255    -25    300    611       O  
ATOM   3634  N   TYR B 168      30.463 -30.416   2.460  1.00 29.92           N  
ANISOU 3634  N   TYR B 168     4466   2904   3998    378    584    527       N  
ATOM   3635  CA  TYR B 168      31.345 -30.863   1.391  1.00 31.59           C  
ANISOU 3635  CA  TYR B 168     4783   2988   4231    548    737    507       C  
ATOM   3636  C   TYR B 168      32.448 -29.861   1.109  1.00 32.99           C  
ANISOU 3636  C   TYR B 168     4811   3319   4404    628    808    561       C  
ATOM   3637  O   TYR B 168      32.890 -29.732  -0.026  1.00 34.26           O  
ANISOU 3637  O   TYR B 168     5073   3414   4528    727    933    496       O  
ATOM   3638  CB  TYR B 168      30.535 -31.106   0.118  1.00 32.35           C  
ANISOU 3638  CB  TYR B 168     5145   2910   4236    512    744    318       C  
ATOM   3639  CG  TYR B 168      29.443 -32.128   0.299  1.00 37.91           C  
ANISOU 3639  CG  TYR B 168     5998   3442   4964    408    659    270       C  
ATOM   3640  CD1 TYR B 168      29.712 -33.483   0.154  1.00 42.34           C  
ANISOU 3640  CD1 TYR B 168     6722   3772   5595    507    749    292       C  
ATOM   3641  CD2 TYR B 168      28.146 -31.744   0.614  1.00 36.25           C  
ANISOU 3641  CD2 TYR B 168     5759   3288   4727    214    498    217       C  
ATOM   3642  CE1 TYR B 168      28.724 -34.423   0.319  1.00 41.73           C  
ANISOU 3642  CE1 TYR B 168     6783   3520   5552    391    663    256       C  
ATOM   3643  CE2 TYR B 168      27.142 -32.683   0.781  1.00 36.77           C  
ANISOU 3643  CE2 TYR B 168     5932   3197   4841    102    417    197       C  
ATOM   3644  CZ  TYR B 168      27.444 -34.022   0.632  1.00 44.29           C  
ANISOU 3644  CZ  TYR B 168     7055   3917   5857    180    491    214       C  
ATOM   3645  OH  TYR B 168      26.465 -34.973   0.795  1.00 50.19           O  
ANISOU 3645  OH  TYR B 168     7915   4490   6665     50    403    202       O  
ATOM   3646  N   GLY B 169      32.880 -29.153   2.145  1.00 31.80           N  
ANISOU 3646  N   GLY B 169     4434   3367   4281    574    725    682       N  
ATOM   3647  CA  GLY B 169      33.945 -28.176   2.020  1.00 34.80           C  
ANISOU 3647  CA  GLY B 169     4643   3899   4681    614    761    758       C  
ATOM   3648  C   GLY B 169      33.645 -27.106   0.988  1.00 29.12           C  
ANISOU 3648  C   GLY B 169     3997   3210   3859    566    780    614       C  
ATOM   3649  O   GLY B 169      32.621 -26.435   1.057  1.00 32.51           O  
ANISOU 3649  O   GLY B 169     4477   3679   4195    424    669    501       O  
ATOM   3650  N   CYS B 170      34.548 -26.954   0.019  1.00 30.43           N  
ANISOU 3650  N   CYS B 170     4165   3352   4048    697    937    636       N  
ATOM   3651  CA  CYS B 170      34.402 -25.935  -1.010  1.00 30.22           C  
ANISOU 3651  CA  CYS B 170     4210   3354   3919    665    972    528       C  
ATOM   3652  C   CYS B 170      33.362 -26.309  -2.044  1.00 26.78           C  
ANISOU 3652  C   CYS B 170     4063   2758   3353    650    981    343       C  
ATOM   3653  O   CYS B 170      33.071 -25.532  -2.935  1.00 27.85           O  
ANISOU 3653  O   CYS B 170     4294   2906   3383    614    986    250       O  
ATOM   3654  CB  CYS B 170      35.746 -25.673  -1.691  1.00 30.44           C  
ANISOU 3654  CB  CYS B 170     4140   3412   4014    812   1159    636       C  
ATOM   3655  SG  CYS B 170      36.819 -24.612  -0.690  1.00 40.09           S  
ANISOU 3655  SG  CYS B 170     5004   4866   5361    738   1072    834       S  
ATOM   3656  N   ASN B 171      32.791 -27.500  -1.918  1.00 32.61           N  
ANISOU 3656  N   ASN B 171     4945   3342   4101    663    966    301       N  
ATOM   3657  CA  ASN B 171      31.750 -27.931  -2.848  1.00 33.11           C  
ANISOU 3657  CA  ASN B 171     5292   3242   4046    613    929    130       C  
ATOM   3658  C   ASN B 171      30.355 -27.761  -2.285  1.00 34.45           C  
ANISOU 3658  C   ASN B 171     5454   3439   4194    421    719     66       C  
ATOM   3659  O   ASN B 171      29.399 -28.317  -2.816  1.00 42.78           O  
ANISOU 3659  O   ASN B 171     6708   4355   5193    349    645    -43       O  
ATOM   3660  CB  ASN B 171      31.973 -29.390  -3.265  1.00 32.46           C  
ANISOU 3660  CB  ASN B 171     5422   2927   3985    740   1055    109       C  
ATOM   3661  CG  ASN B 171      33.156 -29.535  -4.193  1.00 39.08           C  
ANISOU 3661  CG  ASN B 171     6342   3696   4809    948   1306    136       C  
ATOM   3662  OD1 ASN B 171      33.153 -28.997  -5.296  1.00 49.75           O  
ANISOU 3662  OD1 ASN B 171     7848   5033   6021    963   1370     42       O  
ATOM   3663  ND2 ASN B 171      34.181 -30.236  -3.745  1.00 39.20           N  
ANISOU 3663  ND2 ASN B 171     6245   3676   4974   1118   1459    282       N  
ATOM   3664  N   GLY B 172      30.235 -26.992  -1.211  1.00 25.73           N  
ANISOU 3664  N   GLY B 172     4128   2509   3138    333    627    139       N  
ATOM   3665  CA  GLY B 172      28.929 -26.742  -0.631  1.00 24.69           C  
ANISOU 3665  CA  GLY B 172     3968   2414   2999    173    470     96       C  
ATOM   3666  C   GLY B 172      28.733 -27.399   0.719  1.00 23.93           C  
ANISOU 3666  C   GLY B 172     3766   2336   2990    134    428    194       C  
ATOM   3667  O   GLY B 172      29.477 -28.304   1.096  1.00 30.94           O  
ANISOU 3667  O   GLY B 172     4644   3166   3945    229    500    285       O  
ATOM   3668  N   GLY B 173      27.727 -26.937   1.457  1.00 25.49           N  
ANISOU 3668  N   GLY B 173     3886   2612   3187      5    327    189       N  
ATOM   3669  CA  GLY B 173      27.437 -27.510   2.759  1.00 25.80           C  
ANISOU 3669  CA  GLY B 173     3846   2675   3284    -42    299    286       C  
ATOM   3670  C   GLY B 173      26.160 -26.992   3.387  1.00 24.11           C  
ANISOU 3670  C   GLY B 173     3571   2526   3064   -175    225    268       C  
ATOM   3671  O   GLY B 173      25.310 -26.431   2.704  1.00 27.44           O  
ANISOU 3671  O   GLY B 173     4019   2937   3469   -235    175    181       O  
ATOM   3672  N   TYR B 174      26.032 -27.173   4.698  1.00 25.82           N  
ANISOU 3672  N   TYR B 174     3705   2810   3295   -212    225    366       N  
ATOM   3673  CA  TYR B 174      24.794 -26.861   5.395  1.00 27.68           C  
ANISOU 3673  CA  TYR B 174     3888   3091   3539   -319    201    372       C  
ATOM   3674  C   TYR B 174      25.031 -25.965   6.593  1.00 23.99           C  
ANISOU 3674  C   TYR B 174     3339   2783   2991   -338    225    421       C  
ATOM   3675  O   TYR B 174      25.789 -26.322   7.492  1.00 24.41           O  
ANISOU 3675  O   TYR B 174     3377   2885   3013   -315    233    520       O  
ATOM   3676  CB  TYR B 174      24.108 -28.139   5.873  1.00 25.64           C  
ANISOU 3676  CB  TYR B 174     3654   2724   3364   -368    199    448       C  
ATOM   3677  CG  TYR B 174      23.924 -29.219   4.829  1.00 28.98           C  
ANISOU 3677  CG  TYR B 174     4201   2952   3858   -366    166    402       C  
ATOM   3678  CD1 TYR B 174      22.920 -29.128   3.870  1.00 27.12           C  
ANISOU 3678  CD1 TYR B 174     4011   2639   3654   -449     89    312       C  
ATOM   3679  CD2 TYR B 174      24.725 -30.351   4.835  1.00 28.11           C  
ANISOU 3679  CD2 TYR B 174     4174   2722   3783   -286    204    457       C  
ATOM   3680  CE1 TYR B 174      22.734 -30.138   2.925  1.00 31.50           C  
ANISOU 3680  CE1 TYR B 174     4725   2996   4246   -472     36    256       C  
ATOM   3681  CE2 TYR B 174      24.549 -31.364   3.901  1.00 38.93           C  
ANISOU 3681  CE2 TYR B 174     5706   3881   5204   -285    186    399       C  
ATOM   3682  CZ  TYR B 174      23.555 -31.252   2.949  1.00 40.06           C  
ANISOU 3682  CZ  TYR B 174     5925   3945   5350   -389     95    289       C  
ATOM   3683  OH  TYR B 174      23.389 -32.263   2.026  1.00 40.48           O  
ANISOU 3683  OH  TYR B 174     6182   3773   5426   -409     58    218       O  
ATOM   3684  N   PRO B 175      24.378 -24.795   6.618  1.00 24.64           N  
ANISOU 3684  N   PRO B 175     3387   2938   3038   -382    231    356       N  
ATOM   3685  CA  PRO B 175      24.551 -23.910   7.775  1.00 24.62           C  
ANISOU 3685  CA  PRO B 175     3360   3060   2935   -408    262    380       C  
ATOM   3686  C   PRO B 175      24.085 -24.570   9.068  1.00 26.63           C  
ANISOU 3686  C   PRO B 175     3617   3333   3167   -447    306    483       C  
ATOM   3687  O   PRO B 175      24.699 -24.346  10.107  1.00 29.14           O  
ANISOU 3687  O   PRO B 175     3959   3739   3373   -458    307    538       O  
ATOM   3688  CB  PRO B 175      23.682 -22.697   7.427  1.00 23.31           C  
ANISOU 3688  CB  PRO B 175     3175   2917   2767   -432    287    291       C  
ATOM   3689  CG  PRO B 175      23.608 -22.706   5.897  1.00 21.69           C  
ANISOU 3689  CG  PRO B 175     2978   2633   2629   -405    233    220       C  
ATOM   3690  CD  PRO B 175      23.599 -24.167   5.531  1.00 22.60           C  
ANISOU 3690  CD  PRO B 175     3130   2642   2816   -400    203    260       C  
ATOM   3691  N   TRP B 176      23.037 -25.392   9.008  1.00 26.93           N  
ANISOU 3691  N   TRP B 176     3636   3288   3306   -480    331    519       N  
ATOM   3692  CA  TRP B 176      22.538 -26.019  10.227  1.00 27.86           C  
ANISOU 3692  CA  TRP B 176     3755   3422   3408   -519    396    634       C  
ATOM   3693  C   TRP B 176      23.547 -27.014  10.808  1.00 27.43           C  
ANISOU 3693  C   TRP B 176     3744   3358   3320   -491    361    746       C  
ATOM   3694  O   TRP B 176      23.686 -27.127  12.023  1.00 26.86           O  
ANISOU 3694  O   TRP B 176     3702   3357   3146   -510    394    843       O  
ATOM   3695  CB  TRP B 176      21.173 -26.694   9.985  1.00 32.46           C  
ANISOU 3695  CB  TRP B 176     4281   3910   4142   -578    426    671       C  
ATOM   3696  CG  TRP B 176      21.148 -27.713   8.891  1.00 31.25           C  
ANISOU 3696  CG  TRP B 176     4149   3609   4117   -589    337    655       C  
ATOM   3697  CD1 TRP B 176      20.733 -27.526   7.606  1.00 32.55           C  
ANISOU 3697  CD1 TRP B 176     4308   3702   4356   -606    261    558       C  
ATOM   3698  CD2 TRP B 176      21.540 -29.086   8.992  1.00 28.37           C  
ANISOU 3698  CD2 TRP B 176     3843   3131   3805   -586    315    736       C  
ATOM   3699  NE1 TRP B 176      20.854 -28.693   6.893  1.00 34.42           N  
ANISOU 3699  NE1 TRP B 176     4624   3784   4670   -622    192    556       N  
ATOM   3700  CE2 TRP B 176      21.345 -29.668   7.722  1.00 36.77           C  
ANISOU 3700  CE2 TRP B 176     4959   4043   4968   -603    234    663       C  
ATOM   3701  CE3 TRP B 176      22.039 -29.880  10.033  1.00 28.10           C  
ANISOU 3701  CE3 TRP B 176     3839   3099   3738   -568    352    869       C  
ATOM   3702  CZ2 TRP B 176      21.643 -30.999   7.461  1.00 39.28           C  
ANISOU 3702  CZ2 TRP B 176     5373   4195   5357   -598    207    703       C  
ATOM   3703  CZ3 TRP B 176      22.338 -31.198   9.771  1.00 37.69           C  
ANISOU 3703  CZ3 TRP B 176     5120   4158   5044   -554    323    929       C  
ATOM   3704  CH2 TRP B 176      22.138 -31.749   8.497  1.00 42.17           C  
ANISOU 3704  CH2 TRP B 176     5750   4557   5715   -566    260    839       C  
ATOM   3705  N   SER B 177      24.264 -27.727   9.948  1.00 22.40           N  
ANISOU 3705  N   SER B 177     3121   2630   2761   -435    304    742       N  
ATOM   3706  CA  SER B 177      25.302 -28.632  10.410  1.00 26.11           C  
ANISOU 3706  CA  SER B 177     3611   3082   3229   -379    278    864       C  
ATOM   3707  C   SER B 177      26.485 -27.886  11.028  1.00 24.23           C  
ANISOU 3707  C   SER B 177     3350   2990   2867   -354    231    903       C  
ATOM   3708  O   SER B 177      27.049 -28.321  12.037  1.00 26.27           O  
ANISOU 3708  O   SER B 177     3613   3301   3066   -352    201   1043       O  
ATOM   3709  CB  SER B 177      25.805 -29.500   9.261  1.00 30.55           C  
ANISOU 3709  CB  SER B 177     4206   3492   3910   -301    262    841       C  
ATOM   3710  OG  SER B 177      26.769 -30.391   9.759  1.00 37.07           O  
ANISOU 3710  OG  SER B 177     5035   4290   4760   -226    256    983       O  
ATOM   3711  N   ALA B 178      26.882 -26.794  10.390  1.00 27.17           N  
ANISOU 3711  N   ALA B 178     3698   3421   3206   -345    208    794       N  
ATOM   3712  CA  ALA B 178      27.947 -25.946  10.923  1.00 30.38           C  
ANISOU 3712  CA  ALA B 178     4077   3961   3505   -356    142    823       C  
ATOM   3713  C   ALA B 178      27.552 -25.370  12.284  1.00 24.17           C  
ANISOU 3713  C   ALA B 178     3353   3279   2551   -447    139    847       C  
ATOM   3714  O   ALA B 178      28.360 -25.348  13.209  1.00 26.47           O  
ANISOU 3714  O   ALA B 178     3658   3662   2739   -476     58    950       O  
ATOM   3715  CB  ALA B 178      28.286 -24.826   9.938  1.00 26.30           C  
ANISOU 3715  CB  ALA B 178     3531   3467   2995   -346    132    698       C  
ATOM   3716  N   LEU B 179      26.312 -24.897  12.402  1.00 23.92           N  
ANISOU 3716  N   LEU B 179     3366   3232   2490   -490    229    760       N  
ATOM   3717  CA  LEU B 179      25.806 -24.384  13.676  1.00 22.87           C  
ANISOU 3717  CA  LEU B 179     3327   3177   2188   -557    279    773       C  
ATOM   3718  C   LEU B 179      25.747 -25.476  14.738  1.00 27.61           C  
ANISOU 3718  C   LEU B 179     3969   3785   2738   -571    290    935       C  
ATOM   3719  O   LEU B 179      26.002 -25.233  15.911  1.00 32.77           O  
ANISOU 3719  O   LEU B 179     4723   4525   3201   -622    271    995       O  
ATOM   3720  CB  LEU B 179      24.414 -23.760  13.496  1.00 26.27           C  
ANISOU 3720  CB  LEU B 179     3766   3572   2645   -568    414    672       C  
ATOM   3721  CG  LEU B 179      24.352 -22.465  12.667  1.00 26.21           C  
ANISOU 3721  CG  LEU B 179     3743   3563   2653   -559    415    522       C  
ATOM   3722  CD1 LEU B 179      22.920 -22.077  12.332  1.00 24.44           C  
ANISOU 3722  CD1 LEU B 179     3481   3288   2519   -546    540    464       C  
ATOM   3723  CD2 LEU B 179      25.054 -21.310  13.385  1.00 26.10           C  
ANISOU 3723  CD2 LEU B 179     3836   3630   2449   -607    378    470       C  
ATOM   3724  N   GLN B 180      25.392 -26.683  14.319  1.00 27.34           N  
ANISOU 3724  N   GLN B 180     3880   3646   2862   -533    317   1008       N  
ATOM   3725  CA  GLN B 180      25.314 -27.807  15.236  1.00 32.32           C  
ANISOU 3725  CA  GLN B 180     4547   4259   3474   -542    333   1179       C  
ATOM   3726  C   GLN B 180      26.710 -28.148  15.754  1.00 30.27           C  
ANISOU 3726  C   GLN B 180     4293   4065   3144   -518    198   1310       C  
ATOM   3727  O   GLN B 180      26.890 -28.441  16.934  1.00 33.37           O  
ANISOU 3727  O   GLN B 180     4760   4524   3394   -555    172   1445       O  
ATOM   3728  CB  GLN B 180      24.667 -29.015  14.550  1.00 31.55           C  
ANISOU 3728  CB  GLN B 180     4398   4003   3586   -518    378   1219       C  
ATOM   3729  CG  GLN B 180      24.722 -30.287  15.357  1.00 44.17           C  
ANISOU 3729  CG  GLN B 180     6030   5552   5199   -518    387   1412       C  
ATOM   3730  CD  GLN B 180      24.136 -30.102  16.741  1.00 65.74           C  
ANISOU 3730  CD  GLN B 180     8843   8379   7757   -584    472   1502       C  
ATOM   3731  OE1 GLN B 180      23.112 -29.438  16.909  1.00 63.15           O  
ANISOU 3731  OE1 GLN B 180     8523   8080   7392   -628    591   1428       O  
ATOM   3732  NE2 GLN B 180      24.783 -30.689  17.744  1.00 78.79           N  
ANISOU 3732  NE2 GLN B 180    10561  10077   9297   -582    422   1675       N  
ATOM   3733  N   LEU B 181      27.698 -28.085  14.867  1.00 30.17           N  
ANISOU 3733  N   LEU B 181     4195   4037   3232   -455    112   1285       N  
ATOM   3734  CA  LEU B 181      29.084 -28.385  15.245  1.00 30.28           C  
ANISOU 3734  CA  LEU B 181     4159   4115   3231   -420    -21   1434       C  
ATOM   3735  C   LEU B 181      29.562 -27.447  16.367  1.00 28.10           C  
ANISOU 3735  C   LEU B 181     3953   4004   2721   -521   -130   1462       C  
ATOM   3736  O   LEU B 181      30.158 -27.890  17.365  1.00 34.62           O  
ANISOU 3736  O   LEU B 181     4806   4900   3449   -546   -234   1638       O  
ATOM   3737  CB  LEU B 181      29.999 -28.274  14.016  1.00 32.23           C  
ANISOU 3737  CB  LEU B 181     4288   4323   3635   -330    -53   1391       C  
ATOM   3738  CG  LEU B 181      31.351 -29.005  13.957  1.00 39.57           C  
ANISOU 3738  CG  LEU B 181     5105   5252   4679   -230   -133   1574       C  
ATOM   3739  CD1 LEU B 181      32.093 -28.640  12.679  1.00 36.45           C  
ANISOU 3739  CD1 LEU B 181     4604   4826   4419   -143   -110   1501       C  
ATOM   3740  CD2 LEU B 181      32.238 -28.707  15.148  1.00 47.34           C  
ANISOU 3740  CD2 LEU B 181     6062   6396   5529   -297   -298   1736       C  
ATOM   3741  N   VAL B 182      29.293 -26.154  16.198  1.00 29.52           N  
ANISOU 3741  N   VAL B 182     4179   4234   2805   -585   -115   1292       N  
ATOM   3742  CA  VAL B 182      29.704 -25.143  17.168  1.00 28.23           C  
ANISOU 3742  CA  VAL B 182     4126   4196   2405   -699   -218   1277       C  
ATOM   3743  C   VAL B 182      29.009 -25.327  18.513  1.00 33.24           C  
ANISOU 3743  C   VAL B 182     4943   4869   2817   -765   -166   1335       C  
ATOM   3744  O   VAL B 182      29.618 -25.135  19.559  1.00 36.75           O  
ANISOU 3744  O   VAL B 182     5495   5413   3054   -850   -300   1424       O  
ATOM   3745  CB  VAL B 182      29.435 -23.719  16.625  1.00 31.10           C  
ANISOU 3745  CB  VAL B 182     4526   4563   2730   -744   -180   1067       C  
ATOM   3746  CG1 VAL B 182      29.839 -22.659  17.639  1.00 33.45           C  
ANISOU 3746  CG1 VAL B 182     4983   4957   2769   -876   -288   1032       C  
ATOM   3747  CG2 VAL B 182      30.203 -23.509  15.334  1.00 26.59           C  
ANISOU 3747  CG2 VAL B 182     3786   3963   2353   -685   -228   1031       C  
ATOM   3748  N   ALA B 183      27.742 -25.726  18.489  1.00 34.83           N  
ANISOU 3748  N   ALA B 183     5180   4992   3060   -732     26   1299       N  
ATOM   3749  CA  ALA B 183      26.991 -25.930  19.726  1.00 35.08           C  
ANISOU 3749  CA  ALA B 183     5381   5054   2894   -780    128   1365       C  
ATOM   3750  C   ALA B 183      27.467 -27.169  20.467  1.00 39.52           C  
ANISOU 3750  C   ALA B 183     5950   5633   3431   -772     46   1601       C  
ATOM   3751  O   ALA B 183      27.415 -27.230  21.688  1.00 45.32           O  
ANISOU 3751  O   ALA B 183     6854   6439   3925   -834     38   1698       O  
ATOM   3752  CB  ALA B 183      25.493 -26.035  19.440  1.00 32.52           C  
ANISOU 3752  CB  ALA B 183     5044   4641   2669   -746    366   1293       C  
ATOM   3753  N   GLN B 184      27.932 -28.157  19.719  1.00 36.38           N  
ANISOU 3753  N   GLN B 184     5388   5159   3276   -689     -7   1697       N  
ATOM   3754  CA  GLN B 184      28.370 -29.401  20.324  1.00 36.63           C  
ANISOU 3754  CA  GLN B 184     5411   5177   3328   -658    -73   1936       C  
ATOM   3755  C   GLN B 184      29.816 -29.298  20.781  1.00 39.07           C  
ANISOU 3755  C   GLN B 184     5692   5600   3554   -677   -314   2073       C  
ATOM   3756  O   GLN B 184      30.153 -29.683  21.892  1.00 38.37           O  
ANISOU 3756  O   GLN B 184     5692   5576   3311   -711   -406   2228       O  
ATOM   3757  CB  GLN B 184      28.201 -30.558  19.339  1.00 37.86           C  
ANISOU 3757  CB  GLN B 184     5430   5168   3788   -552     -6   1980       C  
ATOM   3758  CG  GLN B 184      28.323 -31.920  19.976  1.00 51.32           C  
ANISOU 3758  CG  GLN B 184     7152   6812   5537   -515    -17   2222       C  
ATOM   3759  CD  GLN B 184      27.276 -32.153  21.060  1.00 51.59           C  
ANISOU 3759  CD  GLN B 184     7335   6863   5405   -591    110   2296       C  
ATOM   3760  OE1 GLN B 184      26.185 -31.571  21.040  1.00 55.31           O  
ANISOU 3760  OE1 GLN B 184     7856   7333   5827   -642    266   2157       O  
ATOM   3761  NE2 GLN B 184      27.610 -33.000  22.011  1.00 45.38           N  
ANISOU 3761  NE2 GLN B 184     6608   6078   4557   -575     60   2480       N  
ATOM   3762  N   TYR B 185      30.668 -28.759  19.921  1.00 37.76           N  
ANISOU 3762  N   TYR B 185     5386   5452   3511   -649   -414   2002       N  
ATOM   3763  CA  TYR B 185      32.101 -28.772  20.176  1.00 42.30           C  
ANISOU 3763  CA  TYR B 185     5859   6124   4090   -655   -646   2167       C  
ATOM   3764  C   TYR B 185      32.641 -27.383  20.487  1.00 44.24           C  
ANISOU 3764  C   TYR B 185     6161   6501   4146   -791   -798   2067       C  
ATOM   3765  O   TYR B 185      33.272 -27.175  21.521  1.00 53.96           O  
ANISOU 3765  O   TYR B 185     7461   7831   5212   -879   -975   2143       O  
ATOM   3766  CB  TYR B 185      32.836 -29.386  18.979  1.00 42.54           C  
ANISOU 3766  CB  TYR B 185     5659   6064   4441   -505   -638   2220       C  
ATOM   3767  CG  TYR B 185      32.377 -30.803  18.711  1.00 40.75           C  
ANISOU 3767  CG  TYR B 185     5414   5677   4393   -380   -505   2320       C  
ATOM   3768  CD1 TYR B 185      32.932 -31.872  19.402  1.00 40.61           C  
ANISOU 3768  CD1 TYR B 185     5366   5652   4411   -325   -588   2588       C  
ATOM   3769  CD2 TYR B 185      31.365 -31.066  17.797  1.00 39.04           C  
ANISOU 3769  CD2 TYR B 185     5219   5307   4306   -332   -312   2155       C  
ATOM   3770  CE1 TYR B 185      32.504 -33.164  19.178  1.00 40.92           C  
ANISOU 3770  CE1 TYR B 185     5412   5518   4618   -219   -463   2679       C  
ATOM   3771  CE2 TYR B 185      30.930 -32.354  17.566  1.00 42.03           C  
ANISOU 3771  CE2 TYR B 185     5606   5519   4845   -246   -207   2238       C  
ATOM   3772  CZ  TYR B 185      31.500 -33.398  18.262  1.00 45.27           C  
ANISOU 3772  CZ  TYR B 185     6001   5908   5293   -188   -274   2495       C  
ATOM   3773  OH  TYR B 185      31.069 -34.685  18.035  1.00 46.30           O  
ANISOU 3773  OH  TYR B 185     6157   5844   5589   -108   -166   2578       O  
ATOM   3774  N   GLY B 186      32.376 -26.432  19.600  1.00 38.49           N  
ANISOU 3774  N   GLY B 186     5405   5741   3476   -798   -718   1845       N  
ATOM   3775  CA  GLY B 186      32.851 -25.079  19.785  1.00 34.12           C  
ANISOU 3775  CA  GLY B 186     4914   5278   2770   -931   -848   1735       C  
ATOM   3776  C   GLY B 186      33.481 -24.557  18.510  1.00 35.79           C  
ANISOU 3776  C   GLY B 186     4926   5464   3207   -883   -859   1657       C  
ATOM   3777  O   GLY B 186      33.376 -25.195  17.458  1.00 33.62           O  
ANISOU 3777  O   GLY B 186     4506   5094   3174   -739   -733   1653       O  
ATOM   3778  N   ILE B 187      34.132 -23.399  18.603  1.00 36.75           N  
ANISOU 3778  N   ILE B 187     5062   5662   3240  -1010  -1008   1596       N  
ATOM   3779  CA  ILE B 187      34.788 -22.781  17.449  1.00 33.81           C  
ANISOU 3779  CA  ILE B 187     4505   5275   3066   -984  -1019   1538       C  
ATOM   3780  C   ILE B 187      35.974 -21.930  17.906  1.00 36.42           C  
ANISOU 3780  C   ILE B 187     4790   5720   3326  -1150  -1284   1616       C  
ATOM   3781  O   ILE B 187      35.993 -21.417  19.031  1.00 35.64           O  
ANISOU 3781  O   ILE B 187     4890   5689   2963  -1317  -1437   1609       O  
ATOM   3782  CB  ILE B 187      33.806 -21.921  16.629  1.00 29.82           C  
ANISOU 3782  CB  ILE B 187     4086   4677   2567   -966   -826   1278       C  
ATOM   3783  CG1 ILE B 187      34.360 -21.670  15.228  1.00 32.26           C  
ANISOU 3783  CG1 ILE B 187     4192   4946   3118   -884   -781   1248       C  
ATOM   3784  CG2 ILE B 187      33.465 -20.623  17.354  1.00 30.46           C  
ANISOU 3784  CG2 ILE B 187     4397   4784   2393  -1130   -873   1122       C  
ATOM   3785  CD1 ILE B 187      33.345 -21.090  14.250  1.00 33.41           C  
ANISOU 3785  CD1 ILE B 187     4398   4989   3307   -830   -587   1029       C  
ATOM   3786  N   HIS B 188      36.976 -21.811  17.040  1.00 33.87           N  
ANISOU 3786  N   HIS B 188     4213   5417   3240  -1110  -1339   1701       N  
ATOM   3787  CA  HIS B 188      38.174 -21.039  17.369  1.00 43.06           C  
ANISOU 3787  CA  HIS B 188     5276   6689   4395  -1278  -1604   1809       C  
ATOM   3788  C   HIS B 188      38.124 -19.670  16.713  1.00 39.21           C  
ANISOU 3788  C   HIS B 188     4829   6162   3906  -1374  -1572   1610       C  
ATOM   3789  O   HIS B 188      37.321 -19.444  15.806  1.00 32.74           O  
ANISOU 3789  O   HIS B 188     4051   5240   3149  -1268  -1339   1428       O  
ATOM   3790  CB  HIS B 188      39.435 -21.778  16.931  1.00 37.16           C  
ANISOU 3790  CB  HIS B 188     4183   6000   3935  -1178  -1691   2085       C  
ATOM   3791  CG  HIS B 188      39.762 -22.966  17.777  1.00 44.01           C  
ANISOU 3791  CG  HIS B 188     5000   6914   4807  -1121  -1791   2320       C  
ATOM   3792  ND1 HIS B 188      39.361 -24.244  17.453  1.00 42.96           N  
ANISOU 3792  ND1 HIS B 188     4820   6704   4799   -907  -1614   2402       N  
ATOM   3793  CD2 HIS B 188      40.451 -23.071  18.938  1.00 47.97           C  
ANISOU 3793  CD2 HIS B 188     5511   7474   5242  -1238  -1984   2427       C  
ATOM   3794  CE1 HIS B 188      39.797 -25.087  18.373  1.00 41.44           C  
ANISOU 3794  CE1 HIS B 188     4595   6544   4605   -895  -1723   2585       C  
ATOM   3795  NE2 HIS B 188      40.458 -24.401  19.287  1.00 46.74           N  
ANISOU 3795  NE2 HIS B 188     5298   7301   5160  -1092  -1943   2596       N  
ATOM   3796  N   TYR B 189      38.978 -18.760  17.175  1.00 38.14           N  
ANISOU 3796  N   TYR B 189     4685   6103   3702  -1584  -1821   1656       N  
ATOM   3797  CA  TYR B 189      39.066 -17.424  16.594  1.00 36.30           C  
ANISOU 3797  CA  TYR B 189     4486   5823   3485  -1696  -1816   1495       C  
ATOM   3798  C   TYR B 189      39.579 -17.485  15.170  1.00 38.95           C  
ANISOU 3798  C   TYR B 189     4527   6132   4141  -1554  -1675   1550       C  
ATOM   3799  O   TYR B 189      40.285 -18.424  14.805  1.00 41.17           O  
ANISOU 3799  O   TYR B 189     4543   6460   4640  -1419  -1666   1763       O  
ATOM   3800  CB  TYR B 189      39.991 -16.518  17.423  1.00 39.21           C  
ANISOU 3800  CB  TYR B 189     4902   6214   3781  -1934  -2063   1524       C  
ATOM   3801  CG  TYR B 189      39.445 -16.156  18.784  1.00 44.83           C  
ANISOU 3801  CG  TYR B 189     5973   6875   4187  -2054  -2108   1382       C  
ATOM   3802  CD1 TYR B 189      38.236 -15.478  18.910  1.00 47.84           C  
ANISOU 3802  CD1 TYR B 189     6666   7153   4356  -2058  -1941   1120       C  
ATOM   3803  CD2 TYR B 189      40.141 -16.474  19.939  1.00 46.48           C  
ANISOU 3803  CD2 TYR B 189     6204   7132   4325  -2151  -2301   1517       C  
ATOM   3804  CE1 TYR B 189      37.732 -15.145  20.157  1.00 47.70           C  
ANISOU 3804  CE1 TYR B 189     6974   7079   4071  -2138  -1942    997       C  
ATOM   3805  CE2 TYR B 189      39.648 -16.141  21.188  1.00 51.00           C  
ANISOU 3805  CE2 TYR B 189     7115   7658   4606  -2252  -2332   1389       C  
ATOM   3806  CZ  TYR B 189      38.441 -15.479  21.292  1.00 51.42           C  
ANISOU 3806  CZ  TYR B 189     7475   7604   4457  -2237  -2141   1129       C  
ATOM   3807  OH  TYR B 189      37.941 -15.150  22.535  1.00 48.40           O  
ANISOU 3807  OH  TYR B 189     7429   7167   3793  -2312  -2138   1008       O  
ATOM   3808  N   ARG B 190      39.233 -16.473  14.376  1.00 39.27           N  
ANISOU 3808  N   ARG B 190     4628   6088   4204  -1575  -1555   1365       N  
ATOM   3809  CA  ARG B 190      39.824 -16.290  13.050  1.00 37.86           C  
ANISOU 3809  CA  ARG B 190     4202   5890   4294  -1480  -1439   1418       C  
ATOM   3810  C   ARG B 190      41.348 -16.387  13.072  1.00 39.68           C  
ANISOU 3810  C   ARG B 190     4116   6235   4727  -1551  -1633   1697       C  
ATOM   3811  O   ARG B 190      41.929 -17.134  12.292  1.00 42.12           O  
ANISOU 3811  O   ARG B 190     4161   6562   5280  -1373  -1515   1860       O  
ATOM   3812  CB  ARG B 190      39.430 -14.940  12.461  1.00 44.65           C  
ANISOU 3812  CB  ARG B 190     5192   6659   5114  -1567  -1367   1214       C  
ATOM   3813  CG  ARG B 190      40.555 -14.300  11.632  1.00 53.31           C  
ANISOU 3813  CG  ARG B 190     6040   7783   6434  -1625  -1408   1336       C  
ATOM   3814  CD  ARG B 190      40.136 -13.000  11.006  1.00 48.06           C  
ANISOU 3814  CD  ARG B 190     5512   7011   5737  -1700  -1324   1148       C  
ATOM   3815  NE  ARG B 190      39.044 -13.221  10.072  1.00 48.81           N  
ANISOU 3815  NE  ARG B 190     5703   7009   5836  -1493  -1046    988       N  
ATOM   3816  CZ  ARG B 190      38.636 -12.321   9.191  1.00 52.80           C  
ANISOU 3816  CZ  ARG B 190     6279   7419   6365  -1481   -916    858       C  
ATOM   3817  NH1 ARG B 190      39.232 -11.135   9.131  1.00 48.14           N  
ANISOU 3817  NH1 ARG B 190     5682   6806   5805  -1661  -1021    862       N  
ATOM   3818  NH2 ARG B 190      37.637 -12.610   8.375  1.00 49.49           N  
ANISOU 3818  NH2 ARG B 190     5938   6923   5945  -1300   -699    736       N  
ATOM   3819  N   ASN B 191      41.984 -15.633  13.969  1.00 42.56           N  
ANISOU 3819  N   ASN B 191     4510   6669   4991  -1813  -1928   1757       N  
ATOM   3820  CA  ASN B 191      43.444 -15.543  14.012  1.00 48.02           C  
ANISOU 3820  CA  ASN B 191     4930   7420   5897  -1879  -2068   2000       C  
ATOM   3821  C   ASN B 191      44.123 -16.884  14.259  1.00 49.83           C  
ANISOU 3821  C   ASN B 191     4920   7726   6288  -1727  -2086   2267       C  
ATOM   3822  O   ASN B 191      45.244 -17.116  13.817  1.00 58.50           O  
ANISOU 3822  O   ASN B 191     5717   8859   7653  -1665  -2075   2490       O  
ATOM   3823  CB  ASN B 191      43.885 -14.549  15.088  1.00 61.84           C  
ANISOU 3823  CB  ASN B 191     6875   9138   7481  -2138  -2292   1953       C  
ATOM   3824  CG  ASN B 191      43.411 -13.136  14.810  1.00 78.23           C  
ANISOU 3824  CG  ASN B 191     9175  11108   9443  -2277  -2261   1714       C  
ATOM   3825  OD1 ASN B 191      43.107 -12.783  13.669  1.00 81.09           O  
ANISOU 3825  OD1 ASN B 191     9459  11432   9919  -2203  -2095   1638       O  
ATOM   3826  ND2 ASN B 191      43.362 -12.312  15.853  1.00 87.13           N  
ANISOU 3826  ND2 ASN B 191    10587  12171  10347  -2473  -2411   1598       N  
ATOM   3827  N   THR B 192      43.433 -17.762  14.974  1.00 51.09           N  
ANISOU 3827  N   THR B 192     5228   7896   6287  -1659  -2093   2247       N  
ATOM   3828  CA  THR B 192      43.940 -19.098  15.271  1.00 55.59           C  
ANISOU 3828  CA  THR B 192     5614   8513   6996  -1503  -2093   2485       C  
ATOM   3829  C   THR B 192      43.917 -20.014  14.047  1.00 50.48           C  
ANISOU 3829  C   THR B 192     4729   7848   6604  -1213  -1849   2585       C  
ATOM   3830  O   THR B 192      44.841 -20.793  13.808  1.00 46.43           O  
ANISOU 3830  O   THR B 192     3952   7349   6342  -1069  -1795   2818       O  
ATOM   3831  CB  THR B 192      43.108 -19.755  16.389  1.00 56.81           C  
ANISOU 3831  CB  THR B 192     6032   8663   6891  -1510  -2143   2423       C  
ATOM   3832  OG1 THR B 192      42.979 -18.845  17.489  1.00 62.18           O  
ANISOU 3832  OG1 THR B 192     6988   9335   7304  -1757  -2320   2287       O  
ATOM   3833  CG2 THR B 192      43.753 -21.044  16.856  1.00 57.59           C  
ANISOU 3833  CG2 THR B 192     5953   8799   7131  -1385  -2177   2679       C  
ATOM   3834  N   TYR B 193      42.843 -19.891  13.277  1.00 44.82           N  
ANISOU 3834  N   TYR B 193     4186   7029   5815  -1109  -1613   2344       N  
ATOM   3835  CA  TYR B 193      42.513 -20.799  12.190  1.00 38.70           C  
ANISOU 3835  CA  TYR B 193     3356   6147   5202   -824  -1297   2317       C  
ATOM   3836  C   TYR B 193      41.986 -19.917  11.052  1.00 38.46           C  
ANISOU 3836  C   TYR B 193     3421   6026   5166   -810  -1098   2082       C  
ATOM   3837  O   TYR B 193      40.770 -19.864  10.822  1.00 32.81           O  
ANISOU 3837  O   TYR B 193     2958   5212   4298   -772   -958   1841       O  
ATOM   3838  CB  TYR B 193      41.429 -21.786  12.652  1.00 35.22           C  
ANISOU 3838  CB  TYR B 193     3139   5631   4612   -720  -1208   2224       C  
ATOM   3839  CG  TYR B 193      41.317 -23.141  11.976  1.00 36.70           C  
ANISOU 3839  CG  TYR B 193     3259   5715   4970   -445   -977   2292       C  
ATOM   3840  CD1 TYR B 193      40.836 -24.246  12.696  1.00 35.04           C  
ANISOU 3840  CD1 TYR B 193     3149   5470   4695   -374   -985   2352       C  
ATOM   3841  CD2 TYR B 193      41.721 -23.341  10.657  1.00 34.43           C  
ANISOU 3841  CD2 TYR B 193     2829   5353   4899   -260   -748   2306       C  
ATOM   3842  CE1 TYR B 193      40.708 -25.496  12.103  1.00 34.87           C  
ANISOU 3842  CE1 TYR B 193     3099   5322   4826   -136   -778   2404       C  
ATOM   3843  CE2 TYR B 193      41.602 -24.596  10.057  1.00 37.31           C  
ANISOU 3843  CE2 TYR B 193     3186   5594   5395    -12   -532   2348       C  
ATOM   3844  CZ  TYR B 193      41.096 -25.667  10.786  1.00 40.03           C  
ANISOU 3844  CZ  TYR B 193     3639   5889   5682     44   -555   2394       C  
ATOM   3845  OH  TYR B 193      40.980 -26.911  10.193  1.00 38.60           O  
ANISOU 3845  OH  TYR B 193     3475   5556   5636    279   -344   2429       O  
ATOM   3846  N   PRO B 194      42.876 -19.173  10.376  1.00 39.62           N  
ANISOU 3846  N   PRO B 194     3364   6209   5479   -854  -1097   2166       N  
ATOM   3847  CA  PRO B 194      42.419 -18.222   9.351  1.00 38.12           C  
ANISOU 3847  CA  PRO B 194     3277   5938   5268   -864   -933   1961       C  
ATOM   3848  C   PRO B 194      41.940 -18.891   8.072  1.00 34.12           C  
ANISOU 3848  C   PRO B 194     2805   5316   4843   -606   -612   1874       C  
ATOM   3849  O   PRO B 194      42.240 -20.066   7.848  1.00 33.91           O  
ANISOU 3849  O   PRO B 194     2671   5269   4945   -409   -498   2005       O  
ATOM   3850  CB  PRO B 194      43.666 -17.366   9.081  1.00 38.30           C  
ANISOU 3850  CB  PRO B 194     3038   6043   5472   -991  -1035   2136       C  
ATOM   3851  CG  PRO B 194      44.812 -18.228   9.479  1.00 40.18           C  
ANISOU 3851  CG  PRO B 194     2960   6385   5920   -928  -1136   2461       C  
ATOM   3852  CD  PRO B 194      44.334 -19.099  10.599  1.00 39.51           C  
ANISOU 3852  CD  PRO B 194     3010   6320   5682   -922  -1269   2472       C  
ATOM   3853  N   TYR B 195      41.206 -18.139   7.254  1.00 29.88           N  
ANISOU 3853  N   TYR B 195     2434   4697   4224   -611   -479   1660       N  
ATOM   3854  CA  TYR B 195      40.577 -18.662   6.046  1.00 28.30           C  
ANISOU 3854  CA  TYR B 195     2334   4378   4041   -404   -211   1541       C  
ATOM   3855  C   TYR B 195      41.587 -18.856   4.931  1.00 41.04           C  
ANISOU 3855  C   TYR B 195     3741   5988   5865   -252    -25   1693       C  
ATOM   3856  O   TYR B 195      42.422 -17.983   4.687  1.00 43.28           O  
ANISOU 3856  O   TYR B 195     3858   6335   6252   -345    -58   1796       O  
ATOM   3857  CB  TYR B 195      39.471 -17.721   5.578  1.00 39.10           C  
ANISOU 3857  CB  TYR B 195     3937   5670   5250   -473   -161   1289       C  
ATOM   3858  CG  TYR B 195      38.626 -18.239   4.429  1.00 34.16           C  
ANISOU 3858  CG  TYR B 195     3459   4924   4598   -297     59   1148       C  
ATOM   3859  CD1 TYR B 195      37.892 -19.410   4.554  1.00 30.56           C  
ANISOU 3859  CD1 TYR B 195     3113   4399   4099   -184    115   1097       C  
ATOM   3860  CD2 TYR B 195      38.538 -17.531   3.231  1.00 26.73           C  
ANISOU 3860  CD2 TYR B 195     2564   3931   3662   -265    193   1071       C  
ATOM   3861  CE1 TYR B 195      37.105 -19.880   3.510  1.00 26.75           C  
ANISOU 3861  CE1 TYR B 195     2784   3797   3582    -56    278    966       C  
ATOM   3862  CE2 TYR B 195      37.765 -17.994   2.184  1.00 25.07           C  
ANISOU 3862  CE2 TYR B 195     2514   3613   3400   -126    359    946       C  
ATOM   3863  CZ  TYR B 195      37.045 -19.164   2.328  1.00 27.92           C  
ANISOU 3863  CZ  TYR B 195     2986   3905   3719    -30    390    888       C  
ATOM   3864  OH  TYR B 195      36.256 -19.616   1.285  1.00 29.43           O  
ANISOU 3864  OH  TYR B 195     3354   3979   3850     77    520    760       O  
ATOM   3865  N   GLU B 196      41.502 -19.990   4.242  1.00 38.58           N  
ANISOU 3865  N   GLU B 196     3453   5589   5617    -20    184   1706       N  
ATOM   3866  CA  GLU B 196      42.452 -20.304   3.178  1.00 32.40           C  
ANISOU 3866  CA  GLU B 196     2503   4785   5023    164    414   1852       C  
ATOM   3867  C   GLU B 196      41.764 -20.543   1.839  1.00 33.07           C  
ANISOU 3867  C   GLU B 196     2816   4727   5023    322    671   1671       C  
ATOM   3868  O   GLU B 196      42.416 -20.665   0.805  1.00 33.70           O  
ANISOU 3868  O   GLU B 196     2828   4770   5206    475    901   1749       O  
ATOM   3869  CB  GLU B 196      43.288 -21.517   3.576  1.00 37.01           C  
ANISOU 3869  CB  GLU B 196     2886   5385   5792    325    448   2090       C  
ATOM   3870  CG  GLU B 196      44.046 -21.304   4.879  1.00 37.98           C  
ANISOU 3870  CG  GLU B 196     2770   5662   6000    161    161   2304       C  
ATOM   3871  CD  GLU B 196      44.765 -22.544   5.357  1.00 39.76           C  
ANISOU 3871  CD  GLU B 196     2801   5899   6405    324    169   2554       C  
ATOM   3872  OE1 GLU B 196      45.658 -23.027   4.634  1.00 41.86           O  
ANISOU 3872  OE1 GLU B 196     2866   6143   6897    530    385   2736       O  
ATOM   3873  OE2 GLU B 196      44.431 -23.033   6.459  1.00 44.90           O  
ANISOU 3873  OE2 GLU B 196     3507   6579   6973    256    -26   2578       O  
ATOM   3874  N   GLY B 197      40.440 -20.613   1.851  1.00 31.54           N  
ANISOU 3874  N   GLY B 197     2895   4451   4636    281    633   1438       N  
ATOM   3875  CA  GLY B 197      39.699 -20.776   0.613  1.00 30.59           C  
ANISOU 3875  CA  GLY B 197     3010   4200   4412    391    819   1262       C  
ATOM   3876  C   GLY B 197      39.901 -22.119  -0.071  1.00 37.19           C  
ANISOU 3876  C   GLY B 197     3915   4910   5304    628   1036   1292       C  
ATOM   3877  O   GLY B 197      39.682 -22.246  -1.277  1.00 44.75           O  
ANISOU 3877  O   GLY B 197     5046   5762   6194    740   1226   1193       O  
ATOM   3878  N   VAL B 198      40.321 -23.117   0.702  1.00 31.48           N  
ANISOU 3878  N   VAL B 198     3080   4188   4695    705   1008   1430       N  
ATOM   3879  CA  VAL B 198      40.432 -24.492   0.233  1.00 37.38           C  
ANISOU 3879  CA  VAL B 198     3920   4783   5499    929   1203   1453       C  
ATOM   3880  C   VAL B 198      40.266 -25.393   1.437  1.00 36.95           C  
ANISOU 3880  C   VAL B 198     3820   4727   5491    918   1058   1534       C  
ATOM   3881  O   VAL B 198      40.673 -25.033   2.541  1.00 39.15           O  
ANISOU 3881  O   VAL B 198     3897   5151   5825    795    860   1673       O  
ATOM   3882  CB  VAL B 198      41.806 -24.815  -0.442  1.00 47.28           C  
ANISOU 3882  CB  VAL B 198     4985   6027   6951   1144   1455   1662       C  
ATOM   3883  CG1 VAL B 198      41.886 -24.258  -1.857  1.00 56.32           C  
ANISOU 3883  CG1 VAL B 198     6258   7118   8021   1215   1680   1570       C  
ATOM   3884  CG2 VAL B 198      42.962 -24.319   0.421  1.00 48.88           C  
ANISOU 3884  CG2 VAL B 198     4802   6415   7355   1075   1327   1934       C  
ATOM   3885  N   GLN B 199      39.687 -26.568   1.242  1.00 37.61           N  
ANISOU 3885  N   GLN B 199     4105   4641   5546   1034   1147   1454       N  
ATOM   3886  CA  GLN B 199      39.517 -27.472   2.368  1.00 30.86           C  
ANISOU 3886  CA  GLN B 199     3217   3771   4738   1028   1024   1547       C  
ATOM   3887  C   GLN B 199      40.781 -28.292   2.608  1.00 38.36           C  
ANISOU 3887  C   GLN B 199     3942   4713   5919   1223   1127   1819       C  
ATOM   3888  O   GLN B 199      41.354 -28.862   1.677  1.00 47.40           O  
ANISOU 3888  O   GLN B 199     5112   5733   7165   1444   1386   1859       O  
ATOM   3889  CB  GLN B 199      38.321 -28.402   2.150  1.00 38.53           C  
ANISOU 3889  CB  GLN B 199     4487   4551   5601   1044   1054   1365       C  
ATOM   3890  CG  GLN B 199      38.073 -29.326   3.326  1.00 40.59           C  
ANISOU 3890  CG  GLN B 199     4728   4788   5906   1027    934   1467       C  
ATOM   3891  CD  GLN B 199      36.997 -30.357   3.049  1.00 40.90           C  
ANISOU 3891  CD  GLN B 199     5047   4613   5881   1048    982   1317       C  
ATOM   3892  OE1 GLN B 199      35.947 -30.363   3.690  1.00 38.38           O  
ANISOU 3892  OE1 GLN B 199     4817   4304   5464    892    836   1233       O  
ATOM   3893  NE2 GLN B 199      37.257 -31.238   2.097  1.00 43.17           N  
ANISOU 3893  NE2 GLN B 199     5481   4696   6226   1238   1194   1288       N  
ATOM   3894  N   ARG B 200      41.222 -28.327   3.862  1.00 36.81           N  
ANISOU 3894  N   ARG B 200     3533   4652   5802   1145    927   2016       N  
ATOM   3895  CA  ARG B 200      42.313 -29.200   4.279  1.00 37.97           C  
ANISOU 3895  CA  ARG B 200     3450   4796   6181   1322    977   2307       C  
ATOM   3896  C   ARG B 200      41.740 -30.115   5.343  1.00 42.28           C  
ANISOU 3896  C   ARG B 200     4082   5292   6690   1290    833   2347       C  
ATOM   3897  O   ARG B 200      40.534 -30.120   5.561  1.00 45.99           O  
ANISOU 3897  O   ARG B 200     4792   5711   6971   1157    751   2140       O  
ATOM   3898  CB  ARG B 200      43.497 -28.402   4.820  1.00 42.77           C  
ANISOU 3898  CB  ARG B 200     3689   5625   6936   1247    835   2562       C  
ATOM   3899  CG  ARG B 200      43.798 -27.136   4.035  1.00 48.56           C  
ANISOU 3899  CG  ARG B 200     4354   6449   7648   1164    888   2491       C  
ATOM   3900  CD  ARG B 200      45.222 -26.665   4.271  1.00 60.52           C  
ANISOU 3900  CD  ARG B 200     5464   8129   9400   1165    836   2801       C  
ATOM   3901  NE  ARG B 200      46.091 -27.072   3.176  1.00 70.39           N  
ANISOU 3901  NE  ARG B 200     6635   9285  10826   1404   1166   2901       N  
ATOM   3902  CZ  ARG B 200      46.351 -26.320   2.113  1.00 68.85           C  
ANISOU 3902  CZ  ARG B 200     6456   9086  10619   1416   1343   2831       C  
ATOM   3903  NH1 ARG B 200      45.826 -25.110   2.013  1.00 58.10           N  
ANISOU 3903  NH1 ARG B 200     5125   7822   9129   1223   1227   2690       N  
ATOM   3904  NH2 ARG B 200      47.153 -26.774   1.159  1.00 77.04           N  
ANISOU 3904  NH2 ARG B 200     7513  10010  11750   1600   1632   2899       N  
ATOM   3905  N   TYR B 201      42.586 -30.876   6.019  1.00 47.15           N  
ANISOU 3905  N   TYR B 201     4493   5926   7495   1409    802   2630       N  
ATOM   3906  CA  TYR B 201      42.092 -31.716   7.103  1.00 51.36           C  
ANISOU 3906  CA  TYR B 201     5102   6423   7989   1370    654   2699       C  
ATOM   3907  C   TYR B 201      41.713 -30.850   8.305  1.00 46.56           C  
ANISOU 3907  C   TYR B 201     4462   6026   7202   1084    333   2695       C  
ATOM   3908  O   TYR B 201      42.218 -29.737   8.478  1.00 41.46           O  
ANISOU 3908  O   TYR B 201     3652   5564   6535    943    197   2733       O  
ATOM   3909  CB  TYR B 201      43.126 -32.785   7.490  1.00 52.01           C  
ANISOU 3909  CB  TYR B 201     4990   6467   8306   1560    708   2991       C  
ATOM   3910  CG  TYR B 201      44.399 -32.256   8.101  1.00 59.18           C  
ANISOU 3910  CG  TYR B 201     5553   7603   9330   1473    554   3229       C  
ATOM   3911  CD1 TYR B 201      45.349 -31.604   7.323  1.00 67.38           C  
ANISOU 3911  CD1 TYR B 201     6399   8710  10493   1513    677   3284       C  
ATOM   3912  CD2 TYR B 201      44.667 -32.432   9.454  1.00 63.32           C  
ANISOU 3912  CD2 TYR B 201     5965   8261   9834   1335    287   3402       C  
ATOM   3913  CE1 TYR B 201      46.523 -31.123   7.878  1.00 69.73           C  
ANISOU 3913  CE1 TYR B 201     6390   9194  10909   1405    526   3514       C  
ATOM   3914  CE2 TYR B 201      45.837 -31.958  10.018  1.00 71.87           C  
ANISOU 3914  CE2 TYR B 201     6757   9533  11019   1229    126   3617       C  
ATOM   3915  CZ  TYR B 201      46.763 -31.303   9.224  1.00 73.14           C  
ANISOU 3915  CZ  TYR B 201     6721   9749  11322   1260    242   3677       C  
ATOM   3916  OH  TYR B 201      47.930 -30.824   9.776  1.00 76.96           O  
ANISOU 3916  OH  TYR B 201     6924  10400  11917   1133     73   3903       O  
ATOM   3917  N   CYS B 202      40.787 -31.354   9.109  1.00 43.18           N  
ANISOU 3917  N   CYS B 202     4217   5555   6636    994    229   2638       N  
ATOM   3918  CA  CYS B 202      40.350 -30.666  10.313  1.00 42.12           C  
ANISOU 3918  CA  CYS B 202     4107   5593   6302    744    -38   2630       C  
ATOM   3919  C   CYS B 202      41.514 -30.498  11.283  1.00 43.87           C  
ANISOU 3919  C   CYS B 202     4057   6002   6609    699   -262   2939       C  
ATOM   3920  O   CYS B 202      42.089 -31.484  11.765  1.00 50.09           O  
ANISOU 3920  O   CYS B 202     4728   6760   7543    830   -285   3194       O  
ATOM   3921  CB  CYS B 202      39.204 -31.441  10.970  1.00 47.87           C  
ANISOU 3921  CB  CYS B 202     5069   6220   6898    696    -58   2558       C  
ATOM   3922  SG  CYS B 202      38.601 -30.768  12.531  1.00 43.11           S  
ANISOU 3922  SG  CYS B 202     4550   5805   6024    422   -333   2559       S  
ATOM   3923  N   ARG B 203      41.852 -29.246  11.572  1.00 42.61           N  
ANISOU 3923  N   ARG B 203     3802   6026   6360    505   -441   2923       N  
ATOM   3924  CA  ARG B 203      43.004 -28.928  12.412  1.00 45.21           C  
ANISOU 3924  CA  ARG B 203     3864   6545   6769    418   -695   3212       C  
ATOM   3925  C   ARG B 203      42.609 -28.339  13.766  1.00 44.68           C  
ANISOU 3925  C   ARG B 203     3929   6620   6426    144   -991   3184       C  
ATOM   3926  O   ARG B 203      43.450 -27.825  14.492  1.00 46.86           O  
ANISOU 3926  O   ARG B 203     4079   7035   6691    -22  -1201   3287       O  
ATOM   3927  CB  ARG B 203      43.933 -27.958  11.674  1.00 47.01           C  
ANISOU 3927  CB  ARG B 203     3860   6862   7140    393   -678   3246       C  
ATOM   3928  CG  ARG B 203      44.831 -28.629  10.643  1.00 49.10           C  
ANISOU 3928  CG  ARG B 203     3936   7022   7697    647   -397   3356       C  
ATOM   3929  CD  ARG B 203      45.363 -27.641   9.620  1.00 46.88           C  
ANISOU 3929  CD  ARG B 203     3512   6784   7518    645   -289   3320       C  
ATOM   3930  NE  ARG B 203      44.306 -27.150   8.745  1.00 43.15           N  
ANISOU 3930  NE  ARG B 203     3292   6216   6888    642   -132   3007       N  
ATOM   3931  CZ  ARG B 203      44.411 -26.058   7.994  1.00 48.47           C  
ANISOU 3931  CZ  ARG B 203     3944   6929   7543    561    -75   2887       C  
ATOM   3932  NH1 ARG B 203      45.536 -25.344   8.012  1.00 43.75           N  
ANISOU 3932  NH1 ARG B 203     3042   6473   7107    489   -171   3091       N  
ATOM   3933  NH2 ARG B 203      43.397 -25.680   7.222  1.00 36.72           N  
ANISOU 3933  NH2 ARG B 203     2726   5337   5887    544     68   2582       N  
ATOM   3934  N   SER B 204      41.332 -28.434  14.118  1.00 41.59           N  
ANISOU 3934  N   SER B 204     3837   6163   5804     75   -958   2981       N  
ATOM   3935  CA  SER B 204      40.842 -27.846  15.362  1.00 40.47           C  
ANISOU 3935  CA  SER B 204     3871   6139   5367   -166  -1187   2934       C  
ATOM   3936  C   SER B 204      41.556 -28.379  16.616  1.00 51.02           C  
ANISOU 3936  C   SER B 204     5140   7560   6687   -231  -1387   3141       C  
ATOM   3937  O   SER B 204      41.683 -27.672  17.610  1.00 59.15           O  
ANISOU 3937  O   SER B 204     6254   8706   7514   -451  -1603   3114       O  
ATOM   3938  CB  SER B 204      39.326 -28.071  15.473  1.00 40.82           C  
ANISOU 3938  CB  SER B 204     4226   6070   5215   -185  -1041   2690       C  
ATOM   3939  OG  SER B 204      39.003 -29.432  15.277  1.00 48.78           O  
ANISOU 3939  OG  SER B 204     5260   6928   6348      1   -883   2766       O  
ATOM   3940  N   ARG B 205      42.034 -29.617  16.560  1.00 44.18           N  
ANISOU 3940  N   ARG B 205     4146   6612   6029    -41  -1295   3315       N  
ATOM   3941  CA  ARG B 205      42.721 -30.221  17.688  1.00 47.27           C  
ANISOU 3941  CA  ARG B 205     4469   7065   6424    -84  -1459   3508       C  
ATOM   3942  C   ARG B 205      44.192 -29.811  17.768  1.00 60.19           C  
ANISOU 3942  C   ARG B 205     5815   8818   8236   -144  -1605   3689       C  
ATOM   3943  O   ARG B 205      44.911 -30.241  18.669  1.00 60.75           O  
ANISOU 3943  O   ARG B 205     5797   8951   8333   -190  -1764   3877       O  
ATOM   3944  CB  ARG B 205      42.614 -31.742  17.611  1.00 49.68           C  
ANISOU 3944  CB  ARG B 205     4769   7222   6887    142  -1295   3625       C  
ATOM   3945  CG  ARG B 205      41.191 -32.240  17.633  1.00 49.97           C  
ANISOU 3945  CG  ARG B 205     5090   7128   6769    175  -1160   3476       C  
ATOM   3946  CD  ARG B 205      41.143 -33.734  17.439  1.00 58.07           C  
ANISOU 3946  CD  ARG B 205     6113   7972   7977    392   -989   3580       C  
ATOM   3947  NE  ARG B 205      39.801 -34.253  17.679  1.00 59.74           N  
ANISOU 3947  NE  ARG B 205     6598   8063   8038    379   -893   3467       N  
ATOM   3948  CZ  ARG B 205      39.394 -34.757  18.839  1.00 63.63           C  
ANISOU 3948  CZ  ARG B 205     7229   8575   8373    300   -984   3531       C  
ATOM   3949  NH1 ARG B 205      40.227 -34.813  19.872  1.00 61.10           N  
ANISOU 3949  NH1 ARG B 205     6817   8387   8010    231  -1187   3703       N  
ATOM   3950  NH2 ARG B 205      38.154 -35.208  18.965  1.00 71.98           N  
ANISOU 3950  NH2 ARG B 205     8517   9514   9320    284   -866   3432       N  
ATOM   3951  N   GLU B 206      44.635 -29.001  16.813  1.00 57.58           N  
ANISOU 3951  N   GLU B 206     5335   8510   8033   -144  -1544   3646       N  
ATOM   3952  CA  GLU B 206      45.976 -28.420  16.839  1.00 58.23           C  
ANISOU 3952  CA  GLU B 206     5151   8698   8275   -240  -1675   3808       C  
ATOM   3953  C   GLU B 206      45.910 -26.990  17.352  1.00 53.07           C  
ANISOU 3953  C   GLU B 206     4610   8158   7397   -539  -1908   3678       C  
ATOM   3954  O   GLU B 206      46.929 -26.336  17.523  1.00 55.90           O  
ANISOU 3954  O   GLU B 206     4801   8600   7840   -681  -2061   3791       O  
ATOM   3955  CB  GLU B 206      46.609 -28.421  15.448  1.00 60.31           C  
ANISOU 3955  CB  GLU B 206     5179   8901   8835    -51  -1433   3859       C  
ATOM   3956  CG  GLU B 206      46.489 -29.719  14.688  1.00 68.10           C  
ANISOU 3956  CG  GLU B 206     6132   9725  10016    263  -1134   3907       C  
ATOM   3957  CD  GLU B 206      47.113 -29.633  13.308  1.00 75.59           C  
ANISOU 3957  CD  GLU B 206     6897  10607  11218    446   -866   3931       C  
ATOM   3958  OE1 GLU B 206      47.383 -28.502  12.839  1.00 73.42           O  
ANISOU 3958  OE1 GLU B 206     6548  10406  10943    330   -899   3876       O  
ATOM   3959  OE2 GLU B 206      47.337 -30.698  12.694  1.00 78.30           O  
ANISOU 3959  OE2 GLU B 206     7192  10809  11748    703   -611   4000       O  
ATOM   3960  N   LYS B 207      44.698 -26.505  17.579  1.00 48.95           N  
ANISOU 3960  N   LYS B 207     4388   7621   6589   -635  -1918   3438       N  
ATOM   3961  CA  LYS B 207      44.486 -25.100  17.881  1.00 51.26           C  
ANISOU 3961  CA  LYS B 207     4835   7979   6663   -893  -2075   3262       C  
ATOM   3962  C   LYS B 207      44.266 -24.846  19.369  1.00 54.42           C  
ANISOU 3962  C   LYS B 207     5480   8435   6763  -1110  -2306   3219       C  
ATOM   3963  O   LYS B 207      43.960 -23.723  19.780  1.00 56.76           O  
ANISOU 3963  O   LYS B 207     5980   8754   6831  -1323  -2420   3041       O  
ATOM   3964  CB  LYS B 207      43.295 -24.577  17.088  1.00 44.69           C  
ANISOU 3964  CB  LYS B 207     4188   7085   5706   -859  -1911   3009       C  
ATOM   3965  CG  LYS B 207      43.428 -24.733  15.574  1.00 54.19           C  
ANISOU 3965  CG  LYS B 207     5191   8225   7173   -645  -1677   3026       C  
ATOM   3966  CD  LYS B 207      44.733 -24.153  15.058  1.00 49.98           C  
ANISOU 3966  CD  LYS B 207     4367   7746   6878   -682  -1712   3159       C  
ATOM   3967  CE  LYS B 207      44.762 -24.112  13.532  1.00 45.79           C  
ANISOU 3967  CE  LYS B 207     3687   7149   6564   -482  -1450   3131       C  
ATOM   3968  NZ  LYS B 207      46.121 -23.762  13.027  1.00 45.46           N  
ANISOU 3968  NZ  LYS B 207     3349   7143   6782   -481  -1428   3303       N  
ATOM   3969  N   GLY B 208      44.418 -25.889  20.175  1.00 53.12           N  
ANISOU 3969  N   GLY B 208     5313   8278   6594  -1048  -2359   3376       N  
ATOM   3970  CA  GLY B 208      44.168 -25.776  21.599  1.00 53.88           C  
ANISOU 3970  CA  GLY B 208     5658   8421   6394  -1225  -2553   3346       C  
ATOM   3971  C   GLY B 208      42.680 -25.669  21.868  1.00 51.37           C  
ANISOU 3971  C   GLY B 208     5694   8045   5779  -1232  -2428   3102       C  
ATOM   3972  O   GLY B 208      41.875 -25.919  20.970  1.00 48.38           O  
ANISOU 3972  O   GLY B 208     5336   7589   5456  -1082  -2203   3001       O  
ATOM   3973  N   PRO B 209      42.308 -25.325  23.115  1.00 55.69           N  
ANISOU 3973  N   PRO B 209     6526   8622   6010  -1399  -2561   3018       N  
ATOM   3974  CA  PRO B 209      40.916 -25.150  23.549  1.00 51.20           C  
ANISOU 3974  CA  PRO B 209     6312   8001   5139  -1417  -2426   2794       C  
ATOM   3975  C   PRO B 209      40.128 -24.141  22.721  1.00 55.53           C  
ANISOU 3975  C   PRO B 209     6976   8498   5626  -1446  -2276   2537       C  
ATOM   3976  O   PRO B 209      40.668 -23.104  22.330  1.00 48.18           O  
ANISOU 3976  O   PRO B 209     5979   7586   4739  -1565  -2366   2471       O  
ATOM   3977  CB  PRO B 209      41.068 -24.663  24.986  1.00 54.31           C  
ANISOU 3977  CB  PRO B 209     6950   8447   5239  -1619  -2629   2766       C  
ATOM   3978  CG  PRO B 209      42.313 -25.340  25.450  1.00 58.36           C  
ANISOU 3978  CG  PRO B 209     7229   9033   5911  -1626  -2842   3054       C  
ATOM   3979  CD  PRO B 209      43.236 -25.317  24.259  1.00 57.21           C  
ANISOU 3979  CD  PRO B 209     6706   8896   6134  -1550  -2831   3177       C  
ATOM   3980  N   TYR B 210      38.858 -24.453  22.463  1.00 46.77           N  
ANISOU 3980  N   TYR B 210     6032   7316   4423  -1341  -2047   2406       N  
ATOM   3981  CA  TYR B 210      37.980 -23.571  21.699  1.00 42.89           C  
ANISOU 3981  CA  TYR B 210     5661   6769   3865  -1355  -1885   2168       C  
ATOM   3982  C   TYR B 210      37.876 -22.169  22.288  1.00 43.77           C  
ANISOU 3982  C   TYR B 210     6009   6884   3737  -1558  -1968   1961       C  
ATOM   3983  O   TYR B 210      38.122 -21.954  23.480  1.00 46.46           O  
ANISOU 3983  O   TYR B 210     6516   7253   3884  -1683  -2110   1966       O  
ATOM   3984  CB  TYR B 210      36.577 -24.175  21.596  1.00 40.91           C  
ANISOU 3984  CB  TYR B 210     5577   6439   3528  -1236  -1630   2080       C  
ATOM   3985  CG  TYR B 210      36.512 -25.447  20.779  1.00 56.99           C  
ANISOU 3985  CG  TYR B 210     7415   8420   5818  -1033  -1504   2240       C  
ATOM   3986  CD1 TYR B 210      36.560 -25.405  19.392  1.00 48.89           C  
ANISOU 3986  CD1 TYR B 210     6216   7350   5010   -928  -1400   2230       C  
ATOM   3987  CD2 TYR B 210      36.390 -26.691  21.394  1.00 62.53           C  
ANISOU 3987  CD2 TYR B 210     8125   9092   6540   -941  -1476   2398       C  
ATOM   3988  CE1 TYR B 210      36.495 -26.559  18.638  1.00 50.92           C  
ANISOU 3988  CE1 TYR B 210     6325   7500   5523   -723  -1239   2313       C  
ATOM   3989  CE2 TYR B 210      36.327 -27.857  20.645  1.00 61.82           C  
ANISOU 3989  CE2 TYR B 210     7881   8912   6697   -753  -1345   2529       C  
ATOM   3990  CZ  TYR B 210      36.382 -27.783  19.265  1.00 60.42           C  
ANISOU 3990  CZ  TYR B 210     7549   8674   6734   -647  -1236   2502       C  
ATOM   3991  OH  TYR B 210      36.319 -28.931  18.502  1.00 66.42           O  
ANISOU 3991  OH  TYR B 210     8192   9296   7749   -448  -1073   2576       O  
ATOM   3992  N   ALA B 211      37.504 -21.221  21.432  1.00 41.69           N  
ANISOU 3992  N   ALA B 211     5773   6577   3490  -1583  -1873   1781       N  
ATOM   3993  CA  ALA B 211      37.329 -19.827  21.823  1.00 52.82           C  
ANISOU 3993  CA  ALA B 211     7415   7948   4706  -1752  -1909   1563       C  
ATOM   3994  C   ALA B 211      35.902 -19.567  22.290  1.00 48.18           C  
ANISOU 3994  C   ALA B 211     7149   7280   3876  -1722  -1686   1351       C  
ATOM   3995  O   ALA B 211      35.666 -18.748  23.174  1.00 43.23           O  
ANISOU 3995  O   ALA B 211     6788   6613   3026  -1834  -1702   1207       O  
ATOM   3996  CB  ALA B 211      37.679 -18.897  20.658  1.00 40.81           C  
ANISOU 3996  CB  ALA B 211     5756   6406   3343  -1788  -1910   1484       C  
ATOM   3997  N   ALA B 212      34.955 -20.261  21.674  1.00 39.15           N  
ANISOU 3997  N   ALA B 212     5976   6105   2796  -1565  -1463   1342       N  
ATOM   3998  CA  ALA B 212      33.545 -20.107  22.016  1.00 45.55           C  
ANISOU 3998  CA  ALA B 212     7035   6839   3432  -1514  -1211   1171       C  
ATOM   3999  C   ALA B 212      32.759 -21.362  21.676  1.00 47.19           C  
ANISOU 3999  C   ALA B 212     7163   7032   3736  -1356  -1028   1274       C  
ATOM   4000  O   ALA B 212      33.154 -22.153  20.822  1.00 48.86           O  
ANISOU 4000  O   ALA B 212     7139   7260   4166  -1270  -1053   1423       O  
ATOM   4001  CB  ALA B 212      32.942 -18.908  21.300  1.00 38.50           C  
ANISOU 4001  CB  ALA B 212     6232   5867   2531  -1532  -1073    941       C  
ATOM   4002  N   LYS B 213      31.633 -21.530  22.350  1.00 44.79           N  
ANISOU 4002  N   LYS B 213     7056   6681   3280  -1315   -830   1202       N  
ATOM   4003  CA  LYS B 213      30.751 -22.655  22.106  1.00 37.66           C  
ANISOU 4003  CA  LYS B 213     6097   5741   2471  -1190   -636   1292       C  
ATOM   4004  C   LYS B 213      29.336 -22.166  22.333  1.00 41.75           C  
ANISOU 4004  C   LYS B 213     6798   6187   2878  -1157   -359   1121       C  
ATOM   4005  O   LYS B 213      29.080 -21.430  23.288  1.00 45.61           O  
ANISOU 4005  O   LYS B 213     7504   6668   3156  -1204   -324   1009       O  
ATOM   4006  CB  LYS B 213      31.080 -23.834  23.034  1.00 41.55           C  
ANISOU 4006  CB  LYS B 213     6583   6272   2929  -1162   -718   1501       C  
ATOM   4007  CG  LYS B 213      30.207 -25.069  22.804  1.00 45.96           C  
ANISOU 4007  CG  LYS B 213     7081   6769   3612  -1045   -525   1613       C  
ATOM   4008  CD  LYS B 213      30.500 -26.191  23.803  1.00 48.84           C  
ANISOU 4008  CD  LYS B 213     7469   7157   3931  -1015   -595   1817       C  
ATOM   4009  CE  LYS B 213      30.145 -25.777  25.215  1.00 62.35           C  
ANISOU 4009  CE  LYS B 213     9443   8906   5340  -1075   -566   1762       C  
ATOM   4010  NZ  LYS B 213      28.717 -25.382  25.334  1.00 68.93           N  
ANISOU 4010  NZ  LYS B 213    10422   9681   6086  -1043   -270   1617       N  
ATOM   4011  N   THR B 214      28.416 -22.558  21.463  1.00 34.97           N  
ANISOU 4011  N   THR B 214     5844   5267   2177  -1074   -158   1108       N  
ATOM   4012  CA  THR B 214      27.035 -22.142  21.641  1.00 35.26           C  
ANISOU 4012  CA  THR B 214     6000   5235   2164  -1028    120    977       C  
ATOM   4013  C   THR B 214      26.256 -23.236  22.369  1.00 34.86           C  
ANISOU 4013  C   THR B 214     5973   5171   2100   -969    268   1113       C  
ATOM   4014  O   THR B 214      26.843 -24.218  22.812  1.00 36.14           O  
ANISOU 4014  O   THR B 214     6097   5372   2262   -971    142   1290       O  
ATOM   4015  CB  THR B 214      26.384 -21.793  20.305  1.00 33.76           C  
ANISOU 4015  CB  THR B 214     5635   4956   2236   -943    253    847       C  
ATOM   4016  OG1 THR B 214      26.524 -22.892  19.401  1.00 35.50           O  
ANISOU 4016  OG1 THR B 214     5615   5138   2735   -864    216    949       O  
ATOM   4017  CG2 THR B 214      27.068 -20.580  19.709  1.00 33.03           C  
ANISOU 4017  CG2 THR B 214     5541   4862   2148   -991    135    701       C  
ATOM   4018  N   ASP B 215      24.947 -23.061  22.511  1.00 44.64           N  
ANISOU 4018  N   ASP B 215     7260   6354   3348   -912    538   1046       N  
ATOM   4019  CA  ASP B 215      24.157 -23.971  23.333  1.00 42.13           C  
ANISOU 4019  CA  ASP B 215     6972   6031   3006   -865    698   1180       C  
ATOM   4020  C   ASP B 215      23.067 -24.693  22.560  1.00 39.42           C  
ANISOU 4020  C   ASP B 215     6456   5609   2915   -815    894   1242       C  
ATOM   4021  O   ASP B 215      22.369 -25.526  23.113  1.00 43.76           O  
ANISOU 4021  O   ASP B 215     6988   6142   3494   -786   1029   1374       O  
ATOM   4022  CB  ASP B 215      23.524 -23.213  24.497  1.00 43.28           C  
ANISOU 4022  CB  ASP B 215     7323   6194   2929   -844    857   1090       C  
ATOM   4023  CG  ASP B 215      24.553 -22.628  25.428  1.00 45.34           C  
ANISOU 4023  CG  ASP B 215     7784   6516   2926   -918    652   1042       C  
ATOM   4024  OD1 ASP B 215      25.495 -23.354  25.806  1.00 43.05           O  
ANISOU 4024  OD1 ASP B 215     7487   6283   2585   -963    439   1185       O  
ATOM   4025  OD2 ASP B 215      24.428 -21.436  25.765  1.00 44.62           O  
ANISOU 4025  OD2 ASP B 215     7855   6403   2697   -936    697    867       O  
ATOM   4026  N   GLY B 216      22.910 -24.379  21.284  1.00 39.38           N  
ANISOU 4026  N   GLY B 216     6282   5543   3137   -789    888   1139       N  
ATOM   4027  CA  GLY B 216      21.876 -25.032  20.504  1.00 33.38           C  
ANISOU 4027  CA  GLY B 216     5317   4693   2671   -734   1020   1173       C  
ATOM   4028  C   GLY B 216      21.730 -24.431  19.130  1.00 33.15           C  
ANISOU 4028  C   GLY B 216     5125   4606   2864   -695    983   1023       C  
ATOM   4029  O   GLY B 216      22.388 -23.449  18.800  1.00 31.09           O  
ANISOU 4029  O   GLY B 216     4909   4372   2532   -702    885    892       O  
ATOM   4030  N   VAL B 217      20.882 -25.048  18.317  1.00 30.94           N  
ANISOU 4030  N   VAL B 217     4663   4243   2852   -667   1045   1055       N  
ATOM   4031  CA  VAL B 217      20.530 -24.516  16.999  1.00 31.32           C  
ANISOU 4031  CA  VAL B 217     4564   4233   3105   -634   1019    929       C  
ATOM   4032  C   VAL B 217      19.015 -24.529  16.902  1.00 36.77           C  
ANISOU 4032  C   VAL B 217     5139   4875   3957   -619   1214    963       C  
ATOM   4033  O   VAL B 217      18.364 -25.469  17.362  1.00 31.92           O  
ANISOU 4033  O   VAL B 217     4478   4234   3415   -644   1306   1109       O  
ATOM   4034  CB  VAL B 217      21.122 -25.352  15.843  1.00 32.27           C  
ANISOU 4034  CB  VAL B 217     4564   4284   3415   -629    839    938       C  
ATOM   4035  CG1 VAL B 217      20.900 -24.671  14.513  1.00 26.15           C  
ANISOU 4035  CG1 VAL B 217     3687   3463   2787   -602    794    801       C  
ATOM   4036  CG2 VAL B 217      22.594 -25.608  16.056  1.00 35.51           C  
ANISOU 4036  CG2 VAL B 217     5043   4740   3709   -630    672    970       C  
ATOM   4037  N   ARG B 218      18.437 -23.491  16.326  1.00 34.57           N  
ANISOU 4037  N   ARG B 218     4800   4583   3753   -579   1280    853       N  
ATOM   4038  CA  ARG B 218      17.002 -23.521  16.119  1.00 39.19           C  
ANISOU 4038  CA  ARG B 218     5222   5125   4542   -560   1444    914       C  
ATOM   4039  C   ARG B 218      16.672 -23.187  14.684  1.00 39.69           C  
ANISOU 4039  C   ARG B 218     5119   5133   4829   -549   1331    838       C  
ATOM   4040  O   ARG B 218      17.439 -22.526  13.996  1.00 33.22           O  
ANISOU 4040  O   ARG B 218     4345   4317   3960   -530   1199    710       O  
ATOM   4041  CB  ARG B 218      16.298 -22.577  17.084  1.00 39.10           C  
ANISOU 4041  CB  ARG B 218     5300   5151   4407   -501   1710    906       C  
ATOM   4042  CG  ARG B 218      15.817 -23.317  18.309  1.00 54.83           C  
ANISOU 4042  CG  ARG B 218     7352   7169   6313   -518   1897   1065       C  
ATOM   4043  CD  ARG B 218      15.792 -22.451  19.532  1.00 64.01           C  
ANISOU 4043  CD  ARG B 218     8732   8386   7203   -464   2059   1000       C  
ATOM   4044  NE  ARG B 218      15.437 -23.235  20.709  1.00 71.82           N  
ANISOU 4044  NE  ARG B 218     9774   9415   8099   -480   2148   1127       N  
ATOM   4045  CZ  ARG B 218      15.244 -22.719  21.917  1.00 74.35           C  
ANISOU 4045  CZ  ARG B 218    10273   9779   8197   -435   2286   1094       C  
ATOM   4046  NH1 ARG B 218      15.374 -21.414  22.108  1.00 66.98           N  
ANISOU 4046  NH1 ARG B 218     9491   8837   7120   -372   2342    931       N  
ATOM   4047  NH2 ARG B 218      14.918 -23.509  22.931  1.00 81.46           N  
ANISOU 4047  NH2 ARG B 218    11215  10716   9019   -458   2367   1224       N  
ATOM   4048  N   GLN B 219      15.538 -23.697  14.229  1.00 36.43           N  
ANISOU 4048  N   GLN B 219     4511   4669   4662   -573   1368    935       N  
ATOM   4049  CA  GLN B 219      15.087 -23.451  12.877  1.00 34.95           C  
ANISOU 4049  CA  GLN B 219     4167   4429   4683   -579   1241    887       C  
ATOM   4050  C   GLN B 219      13.868 -22.554  12.909  1.00 37.30           C  
ANISOU 4050  C   GLN B 219     4319   4738   5116   -520   1415    924       C  
ATOM   4051  O   GLN B 219      12.966 -22.753  13.713  1.00 36.18           O  
ANISOU 4051  O   GLN B 219     4096   4610   5042   -510   1620   1055       O  
ATOM   4052  CB  GLN B 219      14.746 -24.756  12.165  1.00 35.68           C  
ANISOU 4052  CB  GLN B 219     4144   4438   4975   -677   1090    973       C  
ATOM   4053  CG  GLN B 219      14.338 -24.552  10.721  1.00 38.71           C  
ANISOU 4053  CG  GLN B 219     4408   4766   5536   -705    918    919       C  
ATOM   4054  CD  GLN B 219      13.898 -25.831  10.056  1.00 42.42           C  
ANISOU 4054  CD  GLN B 219     4796   5131   6189   -825    763    997       C  
ATOM   4055  OE1 GLN B 219      13.769 -26.863  10.705  1.00 49.53           O  
ANISOU 4055  OE1 GLN B 219     5701   5994   7123   -885    808   1108       O  
ATOM   4056  NE2 GLN B 219      13.668 -25.771   8.750  1.00 40.96           N  
ANISOU 4056  NE2 GLN B 219     4561   4888   6115   -870    572    940       N  
ATOM   4057  N   VAL B 220      13.842 -21.572  12.024  1.00 34.61           N  
ANISOU 4057  N   VAL B 220     3938   4386   4824   -471   1346    826       N  
ATOM   4058  CA  VAL B 220      12.662 -20.746  11.857  1.00 36.06           C  
ANISOU 4058  CA  VAL B 220     3948   4565   5186   -401   1484    881       C  
ATOM   4059  C   VAL B 220      11.656 -21.554  11.051  1.00 33.95           C  
ANISOU 4059  C   VAL B 220     3425   4258   5217   -486   1363   1019       C  
ATOM   4060  O   VAL B 220      12.045 -22.270  10.125  1.00 29.26           O  
ANISOU 4060  O   VAL B 220     2837   3620   4660   -581   1112    985       O  
ATOM   4061  CB  VAL B 220      13.006 -19.424  11.136  1.00 36.46           C  
ANISOU 4061  CB  VAL B 220     4050   4607   5195   -322   1431    744       C  
ATOM   4062  CG1 VAL B 220      11.762 -18.545  10.988  1.00 35.85           C  
ANISOU 4062  CG1 VAL B 220     3783   4514   5325   -225   1588    824       C  
ATOM   4063  CG2 VAL B 220      14.114 -18.701  11.878  1.00 28.72           C  
ANISOU 4063  CG2 VAL B 220     3339   3652   3921   -279   1500    603       C  
ATOM   4064  N   GLN B 221      10.372 -21.465  11.398  1.00 33.20           N  
ANISOU 4064  N   GLN B 221     3110   4169   5333   -460   1538   1179       N  
ATOM   4065  CA  GLN B 221       9.355 -22.077  10.552  1.00 32.86           C  
ANISOU 4065  CA  GLN B 221     2793   4091   5601   -560   1387   1324       C  
ATOM   4066  C   GLN B 221       9.524 -21.576   9.114  1.00 31.63           C  
ANISOU 4066  C   GLN B 221     2613   3907   5498   -575   1118   1230       C  
ATOM   4067  O   GLN B 221       9.515 -20.375   8.871  1.00 36.66           O  
ANISOU 4067  O   GLN B 221     3254   4562   6114   -458   1175   1169       O  
ATOM   4068  CB  GLN B 221       7.948 -21.776  11.064  1.00 35.62           C  
ANISOU 4068  CB  GLN B 221     2913   4463   6157   -485   1583   1485       C  
ATOM   4069  CG  GLN B 221       6.886 -22.584  10.360  1.00 42.28           C  
ANISOU 4069  CG  GLN B 221     3510   5274   7281   -603   1377   1628       C  
ATOM   4070  CD  GLN B 221       5.471 -22.201  10.786  1.00 53.28           C  
ANISOU 4070  CD  GLN B 221     4681   6689   8875   -503   1535   1782       C  
ATOM   4071  OE1 GLN B 221       5.246 -21.130  11.355  1.00 48.79           O  
ANISOU 4071  OE1 GLN B 221     4130   6143   8263   -327   1779   1768       O  
ATOM   4072  NE2 GLN B 221       4.512 -23.084  10.515  1.00 57.28           N  
ANISOU 4072  NE2 GLN B 221     4989   7172   9602   -613   1398   1931       N  
ATOM   4073  N   PRO B 222       9.725 -22.502   8.166  1.00 36.91           N  
ANISOU 4073  N   PRO B 222     3291   4518   6214   -718    831   1213       N  
ATOM   4074  CA  PRO B 222       9.970 -22.142   6.763  1.00 32.92           C  
ANISOU 4074  CA  PRO B 222     2816   3982   5710   -745    565   1118       C  
ATOM   4075  C   PRO B 222       8.764 -21.501   6.086  1.00 38.16           C  
ANISOU 4075  C   PRO B 222     3211   4656   6631   -738    501   1246       C  
ATOM   4076  O   PRO B 222       7.632 -21.687   6.546  1.00 37.56           O  
ANISOU 4076  O   PRO B 222     2878   4596   6796   -758    609   1439       O  
ATOM   4077  CB  PRO B 222      10.297 -23.489   6.112  1.00 36.32           C  
ANISOU 4077  CB  PRO B 222     3336   4327   6135   -909    320   1093       C  
ATOM   4078  CG  PRO B 222       9.624 -24.491   6.980  1.00 40.82           C  
ANISOU 4078  CG  PRO B 222     3783   4879   6849   -996    422   1254       C  
ATOM   4079  CD  PRO B 222       9.813 -23.956   8.373  1.00 37.23           C  
ANISOU 4079  CD  PRO B 222     3363   4503   6278   -859    748   1271       C  
ATOM   4080  N   TYR B 223       9.018 -20.753   5.014  1.00 37.14           N  
ANISOU 4080  N   TYR B 223     3131   4520   6459   -707    332   1161       N  
ATOM   4081  CA  TYR B 223       7.956 -20.170   4.202  1.00 42.08           C  
ANISOU 4081  CA  TYR B 223     3513   5154   7320   -709    208   1292       C  
ATOM   4082  C   TYR B 223       7.066 -19.259   5.040  1.00 41.91           C  
ANISOU 4082  C   TYR B 223     3266   5180   7477   -554    503   1435       C  
ATOM   4083  O   TYR B 223       5.867 -19.149   4.806  1.00 41.40           O  
ANISOU 4083  O   TYR B 223     2893   5130   7708   -568    473   1638       O  
ATOM   4084  CB  TYR B 223       7.141 -21.286   3.532  1.00 47.88           C  
ANISOU 4084  CB  TYR B 223     4087   5845   8259   -917    -63   1426       C  
ATOM   4085  CG  TYR B 223       8.030 -22.295   2.838  1.00 49.16           C  
ANISOU 4085  CG  TYR B 223     4520   5928   8229  -1057   -302   1273       C  
ATOM   4086  CD1 TYR B 223       9.104 -21.873   2.065  1.00 48.30           C  
ANISOU 4086  CD1 TYR B 223     4676   5803   7872  -1007   -402   1082       C  
ATOM   4087  CD2 TYR B 223       7.828 -23.663   2.989  1.00 54.57           C  
ANISOU 4087  CD2 TYR B 223     5208   6542   8983  -1228   -397   1323       C  
ATOM   4088  CE1 TYR B 223       9.941 -22.781   1.440  1.00 50.37           C  
ANISOU 4088  CE1 TYR B 223     5195   5984   7959  -1105   -574    945       C  
ATOM   4089  CE2 TYR B 223       8.666 -24.584   2.368  1.00 53.82           C  
ANISOU 4089  CE2 TYR B 223     5390   6349   8711  -1332   -583   1176       C  
ATOM   4090  CZ  TYR B 223       9.721 -24.132   1.593  1.00 50.35           C  
ANISOU 4090  CZ  TYR B 223     5208   5898   8024  -1260   -660    986       C  
ATOM   4091  OH  TYR B 223      10.565 -25.021   0.963  1.00 50.53           O  
ANISOU 4091  OH  TYR B 223     5511   5815   7875  -1334   -803    845       O  
ATOM   4092  N   ASN B 224       7.675 -18.611   6.026  1.00 41.16           N  
ANISOU 4092  N   ASN B 224     3334   5104   7200   -407    791   1332       N  
ATOM   4093  CA  ASN B 224       6.957 -17.766   6.975  1.00 40.52           C  
ANISOU 4093  CA  ASN B 224     3120   5046   7232   -239   1133   1433       C  
ATOM   4094  C   ASN B 224       7.742 -16.484   7.179  1.00 39.75           C  
ANISOU 4094  C   ASN B 224     3253   4931   6918    -79   1279   1261       C  
ATOM   4095  O   ASN B 224       8.738 -16.463   7.906  1.00 44.00           O  
ANISOU 4095  O   ASN B 224     4063   5471   7183    -62   1388   1104       O  
ATOM   4096  CB  ASN B 224       6.748 -18.504   8.309  1.00 39.54           C  
ANISOU 4096  CB  ASN B 224     2997   4941   7084   -247   1386   1500       C  
ATOM   4097  CG  ASN B 224       5.883 -17.723   9.302  1.00 39.71           C  
ANISOU 4097  CG  ASN B 224     2975   4963   7150    -54   1704   1568       C  
ATOM   4098  OD1 ASN B 224       5.736 -16.507   9.209  1.00 44.87           O  
ANISOU 4098  OD1 ASN B 224     3632   5594   7824    102   1827   1542       O  
ATOM   4099  ND2 ASN B 224       5.314 -18.438  10.270  1.00 48.50           N  
ANISOU 4099  ND2 ASN B 224     4064   6088   8276    -62   1844   1655       N  
ATOM   4100  N   GLU B 225       7.288 -15.424   6.520  1.00 38.28           N  
ANISOU 4100  N   GLU B 225     2956   4723   6865     27   1260   1304       N  
ATOM   4101  CA  GLU B 225       7.950 -14.127   6.570  1.00 38.96           C  
ANISOU 4101  CA  GLU B 225     3252   4768   6784    169   1376   1155       C  
ATOM   4102  C   GLU B 225       7.933 -13.535   7.976  1.00 42.83           C  
ANISOU 4102  C   GLU B 225     3865   5234   7175    315   1772   1114       C  
ATOM   4103  O   GLU B 225       8.955 -13.055   8.459  1.00 39.41           O  
ANISOU 4103  O   GLU B 225     3735   4775   6463    341   1849    925       O  
ATOM   4104  CB  GLU B 225       7.290 -13.160   5.589  1.00 38.82           C  
ANISOU 4104  CB  GLU B 225     3057   4718   6974    261   1286   1255       C  
ATOM   4105  CG  GLU B 225       7.846 -11.747   5.649  1.00 44.64           C  
ANISOU 4105  CG  GLU B 225     3998   5385   7580    416   1428   1124       C  
ATOM   4106  CD  GLU B 225       7.346 -10.882   4.510  1.00 46.21           C  
ANISOU 4106  CD  GLU B 225     4047   5547   7961    488   1281   1226       C  
ATOM   4107  OE1 GLU B 225       6.850  -9.764   4.782  1.00 43.69           O  
ANISOU 4107  OE1 GLU B 225     3679   5160   7763    677   1508   1281       O  
ATOM   4108  OE2 GLU B 225       7.456 -11.320   3.343  1.00 42.08           O  
ANISOU 4108  OE2 GLU B 225     3479   5057   7452    359    942   1251       O  
ATOM   4109  N   GLY B 226       6.768 -13.570   8.622  1.00 37.09           N  
ANISOU 4109  N   GLY B 226     2907   4513   6674    405   2022   1298       N  
ATOM   4110  CA  GLY B 226       6.620 -13.054   9.972  1.00 38.62           C  
ANISOU 4110  CA  GLY B 226     3299   4661   6713    543   2349   1239       C  
ATOM   4111  C   GLY B 226       7.515 -13.738  10.996  1.00 44.07           C  
ANISOU 4111  C   GLY B 226     4258   5387   7100    458   2431   1110       C  
ATOM   4112  O   GLY B 226       8.025 -13.103  11.914  1.00 43.16           O  
ANISOU 4112  O   GLY B 226     4434   5231   6735    535   2622    969       O  
ATOM   4113  N   ALA B 227       7.708 -15.040  10.846  1.00 44.09           N  
ANISOU 4113  N   ALA B 227     4180   5456   7117    290   2262   1164       N  
ATOM   4114  CA  ALA B 227       8.511 -15.776  11.806  1.00 45.61           C  
ANISOU 4114  CA  ALA B 227     4608   5682   7039    209   2319   1078       C  
ATOM   4115  C   ALA B 227       9.963 -15.392  11.611  1.00 40.06           C  
ANISOU 4115  C   ALA B 227     4203   4971   6048    167   2186    861       C  
ATOM   4116  O   ALA B 227      10.714 -15.242  12.577  1.00 40.99           O  
ANISOU 4116  O   ALA B 227     4597   5092   5885    173   2307    746       O  
ATOM   4117  CB  ALA B 227       8.325 -17.259  11.643  1.00 35.47           C  
ANISOU 4117  CB  ALA B 227     3176   4442   5858     45   2150   1195       C  
ATOM   4118  N   LEU B 228      10.347 -15.224  10.352  1.00 31.42           N  
ANISOU 4118  N   LEU B 228     3065   3864   5009    117   1901    807       N  
ATOM   4119  CA  LEU B 228      11.721 -14.851  10.036  1.00 34.67           C  
ANISOU 4119  CA  LEU B 228     3735   4266   5172     74   1737    614       C  
ATOM   4120  C   LEU B 228      12.008 -13.463  10.587  1.00 29.73           C  
ANISOU 4120  C   LEU B 228     3312   3582   4401    195   1935    495       C  
ATOM   4121  O   LEU B 228      13.057 -13.228  11.171  1.00 36.44           O  
ANISOU 4121  O   LEU B 228     4431   4432   4984    159   1938    353       O  
ATOM   4122  CB  LEU B 228      11.981 -14.892   8.534  1.00 30.17           C  
ANISOU 4122  CB  LEU B 228     3082   3689   4694     12   1430    596       C  
ATOM   4123  CG  LEU B 228      13.427 -14.542   8.161  1.00 30.74           C  
ANISOU 4123  CG  LEU B 228     3393   3756   4532    -31   1280    421       C  
ATOM   4124  CD1 LEU B 228      14.398 -15.468   8.899  1.00 27.76           C  
ANISOU 4124  CD1 LEU B 228     3175   3424   3950   -122   1250    365       C  
ATOM   4125  CD2 LEU B 228      13.637 -14.629   6.665  1.00 27.78           C  
ANISOU 4125  CD2 LEU B 228     2953   3371   4231    -82   1011    415       C  
ATOM   4126  N   LEU B 229      11.065 -12.550  10.417  1.00 31.38           N  
ANISOU 4126  N   LEU B 229     3395   3732   4795    335   2097    563       N  
ATOM   4127  CA  LEU B 229      11.242 -11.190  10.913  1.00 32.31           C  
ANISOU 4127  CA  LEU B 229     3723   3757   4795    462   2308    449       C  
ATOM   4128  C   LEU B 229      11.371 -11.162  12.431  1.00 39.83           C  
ANISOU 4128  C   LEU B 229     4918   4699   5519    495   2589    386       C  
ATOM   4129  O   LEU B 229      12.203 -10.442  12.982  1.00 39.65           O  
ANISOU 4129  O   LEU B 229     5210   4621   5236    490   2638    217       O  
ATOM   4130  CB  LEU B 229      10.076 -10.307  10.471  1.00 39.83           C  
ANISOU 4130  CB  LEU B 229     4466   4636   6032    633   2458    570       C  
ATOM   4131  CG  LEU B 229       9.998 -10.108   8.957  1.00 40.06           C  
ANISOU 4131  CG  LEU B 229     4308   4665   6247    607   2168    625       C  
ATOM   4132  CD1 LEU B 229       8.741  -9.346   8.585  1.00 40.01           C  
ANISOU 4132  CD1 LEU B 229     4049   4599   6555    779   2308    794       C  
ATOM   4133  CD2 LEU B 229      11.244  -9.388   8.465  1.00 35.85           C  
ANISOU 4133  CD2 LEU B 229     4032   4085   5503    558   2007    440       C  
ATOM   4134  N   TYR B 230      10.553 -11.962  13.100  1.00 35.27           N  
ANISOU 4134  N   TYR B 230     4212   4168   5021    504   2708    521       N  
ATOM   4135  CA  TYR B 230      10.588 -12.017  14.550  1.00 36.98           C  
ANISOU 4135  CA  TYR B 230     4670   4377   5004    518   2868    470       C  
ATOM   4136  C   TYR B 230      11.940 -12.519  15.038  1.00 38.98           C  
ANISOU 4136  C   TYR B 230     5189   4687   4933    371   2738    342       C  
ATOM   4137  O   TYR B 230      12.506 -11.988  16.002  1.00 39.02           O  
ANISOU 4137  O   TYR B 230     5507   4656   4665    367   2793    211       O  
ATOM   4138  CB  TYR B 230       9.478 -12.908  15.090  1.00 40.74           C  
ANISOU 4138  CB  TYR B 230     4941   4900   5640    538   2977    654       C  
ATOM   4139  CG  TYR B 230       9.535 -13.001  16.588  1.00 49.67           C  
ANISOU 4139  CG  TYR B 230     6327   6027   6517    552   3149    608       C  
ATOM   4140  CD1 TYR B 230       9.316 -11.879  17.371  1.00 55.82           C  
ANISOU 4140  CD1 TYR B 230     7332   6700   7176    677   3355    521       C  
ATOM   4141  CD2 TYR B 230       9.855 -14.192  17.219  1.00 49.32           C  
ANISOU 4141  CD2 TYR B 230     6321   6074   6344    437   3097    652       C  
ATOM   4142  CE1 TYR B 230       9.389 -11.948  18.743  1.00 60.43           C  
ANISOU 4142  CE1 TYR B 230     8171   7277   7513    682   3503    476       C  
ATOM   4143  CE2 TYR B 230       9.922 -14.268  18.596  1.00 50.79           C  
ANISOU 4143  CE2 TYR B 230     6748   6262   6286    448   3244    618       C  
ATOM   4144  CZ  TYR B 230       9.694 -13.143  19.346  1.00 50.42           C  
ANISOU 4144  CZ  TYR B 230     6924   6116   6116    568   3443    526       C  
ATOM   4145  OH  TYR B 230       9.765 -13.205  20.709  1.00 62.28           O  
ANISOU 4145  OH  TYR B 230     8683   7617   7364    573   3584    491       O  
ATOM   4146  N   SER B 231      12.452 -13.541  14.356  1.00 38.47           N  
ANISOU 4146  N   SER B 231     4999   4706   4913    243   2549    391       N  
ATOM   4147  CA  SER B 231      13.739 -14.121  14.704  1.00 38.81           C  
ANISOU 4147  CA  SER B 231     5251   4806   4691    103   2359    301       C  
ATOM   4148  C   SER B 231      14.852 -13.110  14.477  1.00 35.23           C  
ANISOU 4148  C   SER B 231     5027   4307   4050     74   2228    116       C  
ATOM   4149  O   SER B 231      15.726 -12.944  15.327  1.00 38.83           O  
ANISOU 4149  O   SER B 231     5761   4773   4221      9   2218     16       O  
ATOM   4150  CB  SER B 231      14.000 -15.390  13.896  1.00 33.39           C  
ANISOU 4150  CB  SER B 231     4368   4185   4135    -14   2084    384       C  
ATOM   4151  OG  SER B 231      13.285 -16.475  14.441  1.00 44.18           O  
ANISOU 4151  OG  SER B 231     5609   5592   5587    -37   2188    541       O  
ATOM   4152  N   ILE B 232      14.818 -12.441  13.331  1.00 29.52           N  
ANISOU 4152  N   ILE B 232     4189   3534   3491    109   2114     86       N  
ATOM   4153  CA  ILE B 232      15.793 -11.379  13.026  1.00 34.51           C  
ANISOU 4153  CA  ILE B 232     5017   4107   3987     83   2006    -70       C  
ATOM   4154  C   ILE B 232      15.781 -10.272  14.085  1.00 42.56           C  
ANISOU 4154  C   ILE B 232     6334   5029   4806    145   2244   -187       C  
ATOM   4155  O   ILE B 232      16.832  -9.760  14.483  1.00 38.35           O  
ANISOU 4155  O   ILE B 232     6065   4470   4036     55   2154   -322       O  
ATOM   4156  CB  ILE B 232      15.539 -10.750  11.633  1.00 34.68           C  
ANISOU 4156  CB  ILE B 232     4865   4077   4234    136   1895    -57       C  
ATOM   4157  CG1 ILE B 232      15.830 -11.771  10.522  1.00 31.91           C  
ANISOU 4157  CG1 ILE B 232     4313   3808   4004     48   1621     13       C  
ATOM   4158  CG2 ILE B 232      16.421  -9.531  11.439  1.00 32.25           C  
ANISOU 4158  CG2 ILE B 232     4770   3686   3798    119   1838   -203       C  
ATOM   4159  CD1 ILE B 232      15.264 -11.406   9.169  1.00 28.26           C  
ANISOU 4159  CD1 ILE B 232     3652   3312   3775    100   1519     73       C  
ATOM   4160  N   ALA B 233      14.588  -9.928  14.561  1.00 38.55           N  
ANISOU 4160  N   ALA B 233     5779   4461   4408    291   2512   -124       N  
ATOM   4161  CA  ALA B 233      14.437  -8.926  15.605  1.00 40.43           C  
ANISOU 4161  CA  ALA B 233     6278   4586   4497    354   2657   -216       C  
ATOM   4162  C   ALA B 233      15.109  -9.351  16.915  1.00 44.75           C  
ANISOU 4162  C   ALA B 233     7084   5182   4736    245   2616   -276       C  
ATOM   4163  O   ALA B 233      15.389  -8.513  17.765  1.00 44.04           O  
ANISOU 4163  O   ALA B 233     7277   5000   4456    240   2662   -387       O  
ATOM   4164  CB  ALA B 233      12.970  -8.634  15.836  1.00 37.96           C  
ANISOU 4164  CB  ALA B 233     5814   4209   4399    533   2911    -99       C  
ATOM   4165  N   ASN B 234      15.381 -10.643  17.076  1.00 35.36           N  
ANISOU 4165  N   ASN B 234     5805   4128   3502    154   2520   -193       N  
ATOM   4166  CA  ASN B 234      16.083 -11.101  18.266  1.00 36.27           C  
ANISOU 4166  CA  ASN B 234     6150   4301   3330     48   2451   -228       C  
ATOM   4167  C   ASN B 234      17.576 -11.328  18.036  1.00 38.37           C  
ANISOU 4167  C   ASN B 234     6526   4631   3421   -123   2162   -299       C  
ATOM   4168  O   ASN B 234      18.402 -11.023  18.894  1.00 41.79           O  
ANISOU 4168  O   ASN B 234     7212   5059   3608   -218   2057   -382       O  
ATOM   4169  CB  ASN B 234      15.421 -12.364  18.799  1.00 49.56           C  
ANISOU 4169  CB  ASN B 234     7689   6081   5059     61   2541    -71       C  
ATOM   4170  CG  ASN B 234      14.098 -12.067  19.505  1.00 51.79           C  
ANISOU 4170  CG  ASN B 234     7947   6300   5430    210   2831     -8       C  
ATOM   4171  OD1 ASN B 234      13.040 -12.541  19.097  1.00 51.25           O  
ANISOU 4171  OD1 ASN B 234     7599   6249   5624    291   2949    136       O  
ATOM   4172  ND2 ASN B 234      14.159 -11.258  20.557  1.00 56.97           N  
ANISOU 4172  ND2 ASN B 234     8897   6875   5875    239   2941   -110       N  
ATOM   4173  N   GLN B 235      17.928 -11.825  16.860  1.00 36.65           N  
ANISOU 4173  N   GLN B 235     6115   4469   3342   -168   2028   -258       N  
ATOM   4174  CA  GLN B 235      19.326 -12.086  16.525  1.00 36.87           C  
ANISOU 4174  CA  GLN B 235     6207   4561   3240   -322   1759   -300       C  
ATOM   4175  C   GLN B 235      19.440 -12.317  15.023  1.00 31.72           C  
ANISOU 4175  C   GLN B 235     5266   3924   2864   -311   1581   -256       C  
ATOM   4176  O   GLN B 235      18.455 -12.667  14.392  1.00 27.35           O  
ANISOU 4176  O   GLN B 235     4484   3363   2545   -221   1662   -169       O  
ATOM   4177  CB  GLN B 235      19.826 -13.294  17.300  1.00 43.12           C  
ANISOU 4177  CB  GLN B 235     7028   5467   3887   -414   1657   -207       C  
ATOM   4178  CG  GLN B 235      19.546 -14.611  16.617  1.00 47.04           C  
ANISOU 4178  CG  GLN B 235     7229   6035   4608   -403   1580    -58       C  
ATOM   4179  CD  GLN B 235      19.868 -15.785  17.490  1.00 65.04           C  
ANISOU 4179  CD  GLN B 235     9557   8403   6752   -470   1536     51       C  
ATOM   4180  OE1 GLN B 235      19.283 -15.959  18.564  1.00 69.37           O  
ANISOU 4180  OE1 GLN B 235    10221   8958   7177   -441   1715     93       O  
ATOM   4181  NE2 GLN B 235      20.830 -16.587  17.057  1.00 72.24           N  
ANISOU 4181  NE2 GLN B 235    10372   9378   7700   -546   1287    106       N  
ATOM   4182  N   PRO B 236      20.626 -12.074  14.438  1.00 28.68           N  
ANISOU 4182  N   PRO B 236     4895   3554   2446   -406   1342   -309       N  
ATOM   4183  CA  PRO B 236      20.828 -12.435  13.030  1.00 26.24           C  
ANISOU 4183  CA  PRO B 236     4344   3268   2359   -397   1180   -261       C  
ATOM   4184  C   PRO B 236      20.612 -13.920  12.770  1.00 27.25           C  
ANISOU 4184  C   PRO B 236     4280   3474   2600   -399   1117   -134       C  
ATOM   4185  O   PRO B 236      20.896 -14.757  13.632  1.00 30.79           O  
ANISOU 4185  O   PRO B 236     4785   3985   2929   -449   1104    -78       O  
ATOM   4186  CB  PRO B 236      22.285 -12.046  12.771  1.00 23.61           C  
ANISOU 4186  CB  PRO B 236     4089   2954   1927   -510    966   -319       C  
ATOM   4187  CG  PRO B 236      22.510 -10.891  13.717  1.00 25.41           C  
ANISOU 4187  CG  PRO B 236     4597   3109   1947   -557   1038   -436       C  
ATOM   4188  CD  PRO B 236      21.738 -11.259  14.961  1.00 27.14           C  
ANISOU 4188  CD  PRO B 236     4948   3337   2027   -520   1231   -420       C  
ATOM   4189  N   VAL B 237      20.137 -14.225  11.566  1.00 27.83           N  
ANISOU 4189  N   VAL B 237     4149   3532   2894   -352   1065    -89       N  
ATOM   4190  CA  VAL B 237      19.680 -15.562  11.200  1.00 30.22           C  
ANISOU 4190  CA  VAL B 237     4279   3868   3334   -354   1020     22       C  
ATOM   4191  C   VAL B 237      20.373 -16.044   9.942  1.00 30.01           C  
ANISOU 4191  C   VAL B 237     4159   3848   3396   -382    820     25       C  
ATOM   4192  O   VAL B 237      20.527 -15.280   8.995  1.00 24.36           O  
ANISOU 4192  O   VAL B 237     3424   3098   2735   -360    765    -28       O  
ATOM   4193  CB  VAL B 237      18.148 -15.567  10.970  1.00 28.53           C  
ANISOU 4193  CB  VAL B 237     3909   3615   3316   -276   1162     92       C  
ATOM   4194  CG1 VAL B 237      17.654 -16.958  10.540  1.00 27.85           C  
ANISOU 4194  CG1 VAL B 237     3650   3545   3385   -311   1085    207       C  
ATOM   4195  CG2 VAL B 237      17.435 -15.077  12.210  1.00 29.94           C  
ANISOU 4195  CG2 VAL B 237     4184   3779   3414   -221   1414     98       C  
ATOM   4196  N   SER B 238      20.809 -17.301   9.932  1.00 29.44           N  
ANISOU 4196  N   SER B 238     4048   3808   3329   -422    728     90       N  
ATOM   4197  CA  SER B 238      21.325 -17.905   8.703  1.00 25.69           C  
ANISOU 4197  CA  SER B 238     3501   3316   2943   -428    579     95       C  
ATOM   4198  C   SER B 238      20.174 -18.165   7.751  1.00 25.34           C  
ANISOU 4198  C   SER B 238     3332   3217   3078   -405    568    124       C  
ATOM   4199  O   SER B 238      19.221 -18.847   8.123  1.00 29.43           O  
ANISOU 4199  O   SER B 238     3773   3723   3685   -416    624    200       O  
ATOM   4200  CB  SER B 238      22.048 -19.222   8.986  1.00 19.20           C  
ANISOU 4200  CB  SER B 238     2686   2517   2094   -459    508    163       C  
ATOM   4201  OG  SER B 238      22.392 -19.850   7.763  1.00 24.77           O  
ANISOU 4201  OG  SER B 238     3346   3177   2888   -446    404    161       O  
ATOM   4202  N   VAL B 239      20.247 -17.635   6.533  1.00 20.25           N  
ANISOU 4202  N   VAL B 239     2666   2542   2488   -385    486     78       N  
ATOM   4203  CA  VAL B 239      19.168 -17.850   5.564  1.00 20.32           C  
ANISOU 4203  CA  VAL B 239     2565   2502   2654   -382    430    115       C  
ATOM   4204  C   VAL B 239      19.767 -18.228   4.209  1.00 21.48           C  
ANISOU 4204  C   VAL B 239     2752   2615   2796   -395    280     79       C  
ATOM   4205  O   VAL B 239      20.948 -18.028   3.982  1.00 21.36           O  
ANISOU 4205  O   VAL B 239     2823   2616   2678   -382    259     30       O  
ATOM   4206  CB  VAL B 239      18.251 -16.598   5.406  1.00 29.21           C  
ANISOU 4206  CB  VAL B 239     3626   3613   3861   -327    502    116       C  
ATOM   4207  CG1 VAL B 239      17.572 -16.250   6.727  1.00 28.92           C  
ANISOU 4207  CG1 VAL B 239     3570   3592   3828   -292    695    151       C  
ATOM   4208  CG2 VAL B 239      19.033 -15.387   4.855  1.00 24.12           C  
ANISOU 4208  CG2 VAL B 239     3071   2958   3135   -293    480     34       C  
ATOM   4209  N   VAL B 240      18.966 -18.815   3.327  1.00 21.92           N  
ANISOU 4209  N   VAL B 240     2752   2620   2957   -427    179    112       N  
ATOM   4210  CA  VAL B 240      19.463 -19.191   2.004  1.00 23.30           C  
ANISOU 4210  CA  VAL B 240     3013   2747   3093   -439     47     68       C  
ATOM   4211  C   VAL B 240      18.638 -18.536   0.914  1.00 25.33           C  
ANISOU 4211  C   VAL B 240     3231   2979   3414   -443    -52     78       C  
ATOM   4212  O   VAL B 240      17.498 -18.140   1.139  1.00 22.79           O  
ANISOU 4212  O   VAL B 240     2774   2666   3220   -448    -44    146       O  
ATOM   4213  CB  VAL B 240      19.443 -20.728   1.779  1.00 26.46           C  
ANISOU 4213  CB  VAL B 240     3459   3078   3517   -497    -29     85       C  
ATOM   4214  CG1 VAL B 240      20.369 -21.422   2.765  1.00 25.83           C  
ANISOU 4214  CG1 VAL B 240     3422   3017   3376   -479     57     95       C  
ATOM   4215  CG2 VAL B 240      18.021 -21.281   1.881  1.00 22.19           C  
ANISOU 4215  CG2 VAL B 240     2797   2501   3132   -576    -87    166       C  
ATOM   4216  N   LEU B 241      19.216 -18.432  -0.274  1.00 19.35           N  
ANISOU 4216  N   LEU B 241     2589   2192   2570   -435   -141     27       N  
ATOM   4217  CA  LEU B 241      18.512 -17.852  -1.396  1.00 25.30           C  
ANISOU 4217  CA  LEU B 241     3334   2923   3355   -445   -263     46       C  
ATOM   4218  C   LEU B 241      19.139 -18.334  -2.695  1.00 26.16           C  
ANISOU 4218  C   LEU B 241     3628   2978   3333   -461   -368    -12       C  
ATOM   4219  O   LEU B 241      20.160 -19.044  -2.690  1.00 24.44           O  
ANISOU 4219  O   LEU B 241     3529   2737   3021   -443   -314    -67       O  
ATOM   4220  CB  LEU B 241      18.507 -16.310  -1.315  1.00 27.78           C  
ANISOU 4220  CB  LEU B 241     3599   3276   3678   -373   -187     56       C  
ATOM   4221  CG  LEU B 241      19.749 -15.514  -0.896  1.00 26.50           C  
ANISOU 4221  CG  LEU B 241     3514   3146   3409   -318    -59     -4       C  
ATOM   4222  CD1 LEU B 241      20.884 -15.687  -1.881  1.00 28.03           C  
ANISOU 4222  CD1 LEU B 241     3854   3326   3470   -310    -94    -53       C  
ATOM   4223  CD2 LEU B 241      19.431 -14.007  -0.701  1.00 22.69           C  
ANISOU 4223  CD2 LEU B 241     2983   2665   2972   -262     13     13       C  
ATOM   4224  N   GLU B 242      18.505 -17.968  -3.801  1.00 22.14           N  
ANISOU 4224  N   GLU B 242     3148   2445   2819   -490   -514     10       N  
ATOM   4225  CA  GLU B 242      19.040 -18.277  -5.118  1.00 24.65           C  
ANISOU 4225  CA  GLU B 242     3682   2707   2974   -500   -605    -48       C  
ATOM   4226  C   GLU B 242      19.836 -17.085  -5.634  1.00 30.55           C  
ANISOU 4226  C   GLU B 242     4494   3493   3620   -417   -527    -62       C  
ATOM   4227  O   GLU B 242      19.272 -16.038  -5.930  1.00 32.50           O  
ANISOU 4227  O   GLU B 242     4670   3765   3913   -402   -574     -4       O  
ATOM   4228  CB  GLU B 242      17.911 -18.638  -6.078  1.00 30.27           C  
ANISOU 4228  CB  GLU B 242     4427   3368   3706   -604   -843     -9       C  
ATOM   4229  CG  GLU B 242      18.356 -18.785  -7.515  1.00 40.23           C  
ANISOU 4229  CG  GLU B 242     5956   4570   4760   -617   -945    -71       C  
ATOM   4230  CD  GLU B 242      17.180 -18.842  -8.465  1.00 53.74           C  
ANISOU 4230  CD  GLU B 242     7692   6249   6480   -733  -1221    -12       C  
ATOM   4231  OE1 GLU B 242      17.009 -17.895  -9.269  1.00 55.00           O  
ANISOU 4231  OE1 GLU B 242     7882   6439   6577   -711  -1301     36       O  
ATOM   4232  OE2 GLU B 242      16.428 -19.837  -8.395  1.00 53.22           O  
ANISOU 4232  OE2 GLU B 242     7610   6123   6489   -856  -1369      0       O  
ATOM   4233  N   ALA B 243      21.151 -17.256  -5.738  1.00 26.00           N  
ANISOU 4233  N   ALA B 243     4039   2915   2925   -360   -401   -121       N  
ATOM   4234  CA  ALA B 243      22.073 -16.150  -5.992  1.00 23.47           C  
ANISOU 4234  CA  ALA B 243     3746   2635   2537   -290   -291   -118       C  
ATOM   4235  C   ALA B 243      22.801 -16.265  -7.330  1.00 25.26           C  
ANISOU 4235  C   ALA B 243     4188   2822   2587   -259   -285   -148       C  
ATOM   4236  O   ALA B 243      23.650 -15.446  -7.652  1.00 32.80           O  
ANISOU 4236  O   ALA B 243     5173   3805   3484   -205   -182   -132       O  
ATOM   4237  CB  ALA B 243      23.086 -16.069  -4.859  1.00 21.51           C  
ANISOU 4237  CB  ALA B 243     3415   2436   2323   -252   -130   -128       C  
ATOM   4238  N   ALA B 244      22.474 -17.288  -8.105  1.00 30.16           N  
ANISOU 4238  N   ALA B 244     4975   3369   3117   -298   -387   -190       N  
ATOM   4239  CA  ALA B 244      23.202 -17.569  -9.337  1.00 37.24           C  
ANISOU 4239  CA  ALA B 244     6128   4209   3813   -258   -348   -234       C  
ATOM   4240  C   ALA B 244      22.846 -16.629 -10.499  1.00 37.28           C  
ANISOU 4240  C   ALA B 244     6243   4222   3701   -267   -445   -195       C  
ATOM   4241  O   ALA B 244      23.576 -16.576 -11.496  1.00 28.55           O  
ANISOU 4241  O   ALA B 244     5350   3088   2412   -217   -366   -214       O  
ATOM   4242  CB  ALA B 244      22.964 -19.016  -9.747  1.00 41.61           C  
ANISOU 4242  CB  ALA B 244     6874   4652   4286   -303   -423   -309       C  
ATOM   4243  N   GLY B 245      21.737 -15.897 -10.367  1.00 28.91           N  
ANISOU 4243  N   GLY B 245     5038   3195   2749   -321   -600   -125       N  
ATOM   4244  CA  GLY B 245      21.217 -15.076 -11.444  1.00 25.51           C  
ANISOU 4244  CA  GLY B 245     4697   2767   2228   -338   -736    -61       C  
ATOM   4245  C   GLY B 245      22.104 -13.901 -11.805  1.00 28.15           C  
ANISOU 4245  C   GLY B 245     5061   3137   2498   -254   -583    -17       C  
ATOM   4246  O   GLY B 245      22.812 -13.345 -10.964  1.00 25.17           O  
ANISOU 4246  O   GLY B 245     4539   2800   2225   -201   -411     -9       O  
ATOM   4247  N   LYS B 246      22.043 -13.513 -13.071  1.00 27.12           N  
ANISOU 4247  N   LYS B 246     5128   2987   2188   -255   -662     20       N  
ATOM   4248  CA  LYS B 246      22.886 -12.455 -13.588  1.00 31.70           C  
ANISOU 4248  CA  LYS B 246     5769   3588   2687   -185   -517     77       C  
ATOM   4249  C   LYS B 246      22.584 -11.108 -12.940  1.00 26.83           C  
ANISOU 4249  C   LYS B 246     4922   3007   2265   -164   -501    169       C  
ATOM   4250  O   LYS B 246      23.492 -10.326 -12.689  1.00 24.93           O  
ANISOU 4250  O   LYS B 246     4635   2782   2056   -116   -323    194       O  
ATOM   4251  CB  LYS B 246      22.726 -12.370 -15.099  1.00 32.37           C  
ANISOU 4251  CB  LYS B 246     6140   3641   2518   -199   -625    109       C  
ATOM   4252  CG  LYS B 246      23.765 -11.519 -15.783  1.00 34.33           C  
ANISOU 4252  CG  LYS B 246     6506   3901   2638   -124   -435    167       C  
ATOM   4253  CD  LYS B 246      23.568 -11.645 -17.282  1.00 38.75           C  
ANISOU 4253  CD  LYS B 246     7401   4424   2898   -143   -543    188       C  
ATOM   4254  CE  LYS B 246      24.554 -10.857 -18.078  1.00 40.70           C  
ANISOU 4254  CE  LYS B 246     7794   4678   2991    -68   -342    262       C  
ATOM   4255  NZ  LYS B 246      24.361 -11.255 -19.516  1.00 40.78           N  
ANISOU 4255  NZ  LYS B 246     8084   4647   2764    -88   -424    241       N  
ATOM   4256  N   ASP B 247      21.313 -10.837 -12.660  1.00 24.45           N  
ANISOU 4256  N   ASP B 247     4476   2708   2106   -200   -680    227       N  
ATOM   4257  CA  ASP B 247      20.957  -9.617 -11.934  1.00 25.43           C  
ANISOU 4257  CA  ASP B 247     4390   2839   2431   -160   -637    304       C  
ATOM   4258  C   ASP B 247      21.498  -9.624 -10.515  1.00 23.69           C  
ANISOU 4258  C   ASP B 247     4010   2635   2355   -141   -458    235       C  
ATOM   4259  O   ASP B 247      21.923  -8.591 -10.003  1.00 32.01           O  
ANISOU 4259  O   ASP B 247     4993   3679   3492   -106   -334    258       O  
ATOM   4260  CB  ASP B 247      19.446  -9.421 -11.895  1.00 30.61           C  
ANISOU 4260  CB  ASP B 247     4900   3492   3237   -182   -842    397       C  
ATOM   4261  CG  ASP B 247      18.832  -9.423 -13.281  1.00 38.95           C  
ANISOU 4261  CG  ASP B 247     6109   4540   4150   -222  -1074    485       C  
ATOM   4262  OD1 ASP B 247      18.915  -8.385 -13.960  1.00 40.83           O  
ANISOU 4262  OD1 ASP B 247     6407   4764   4340   -178  -1081    584       O  
ATOM   4263  OD2 ASP B 247      18.286 -10.467 -13.692  1.00 52.17           O  
ANISOU 4263  OD2 ASP B 247     7859   6212   5749   -309  -1259    457       O  
ATOM   4264  N   PHE B 248      21.479 -10.793  -9.885  1.00 24.69           N  
ANISOU 4264  N   PHE B 248     4102   2778   2502   -175   -456    154       N  
ATOM   4265  CA  PHE B 248      22.007 -10.929  -8.552  1.00 19.96           C  
ANISOU 4265  CA  PHE B 248     3376   2202   2007   -167   -309     97       C  
ATOM   4266  C   PHE B 248      23.532 -10.733  -8.584  1.00 19.90           C  
ANISOU 4266  C   PHE B 248     3440   2208   1912   -142   -139     69       C  
ATOM   4267  O   PHE B 248      24.100  -9.982  -7.780  1.00 21.33           O  
ANISOU 4267  O   PHE B 248     3533   2399   2171   -138    -29     71       O  
ATOM   4268  CB  PHE B 248      21.628 -12.293  -7.967  1.00 20.52           C  
ANISOU 4268  CB  PHE B 248     3405   2280   2111   -210   -356     40       C  
ATOM   4269  CG  PHE B 248      21.694 -12.341  -6.459  1.00 20.62           C  
ANISOU 4269  CG  PHE B 248     3260   2320   2255   -208   -249     12       C  
ATOM   4270  CD1 PHE B 248      22.902 -12.466  -5.815  1.00 17.64           C  
ANISOU 4270  CD1 PHE B 248     2888   1968   1845   -197   -109    -33       C  
ATOM   4271  CD2 PHE B 248      20.552 -12.221  -5.697  1.00 21.25           C  
ANISOU 4271  CD2 PHE B 248     3185   2401   2488   -217   -287     47       C  
ATOM   4272  CE1 PHE B 248      22.977 -12.487  -4.426  1.00 22.25           C  
ANISOU 4272  CE1 PHE B 248     3359   2580   2516   -208    -32    -54       C  
ATOM   4273  CE2 PHE B 248      20.618 -12.243  -4.319  1.00 25.82           C  
ANISOU 4273  CE2 PHE B 248     3659   3001   3150   -212   -171     21       C  
ATOM   4274  CZ  PHE B 248      21.829 -12.375  -3.684  1.00 24.21           C  
ANISOU 4274  CZ  PHE B 248     3494   2823   2881   -214    -57    -35       C  
ATOM   4275  N   GLN B 249      24.183 -11.379  -9.542  1.00 21.43           N  
ANISOU 4275  N   GLN B 249     3801   2395   1945   -130   -117     51       N  
ATOM   4276  CA  GLN B 249      25.630 -11.214  -9.734  1.00 25.27           C  
ANISOU 4276  CA  GLN B 249     4337   2898   2365    -94     61     58       C  
ATOM   4277  C   GLN B 249      26.064  -9.745  -9.872  1.00 23.64           C  
ANISOU 4277  C   GLN B 249     4096   2690   2195    -89    130    135       C  
ATOM   4278  O   GLN B 249      27.025  -9.305  -9.231  1.00 24.40           O  
ANISOU 4278  O   GLN B 249     4102   2808   2362   -100    251    148       O  
ATOM   4279  CB  GLN B 249      26.089 -11.993 -10.973  1.00 21.18           C  
ANISOU 4279  CB  GLN B 249     4043   2355   1651    -58     94     42       C  
ATOM   4280  CG  GLN B 249      27.565 -11.737 -11.339  1.00 22.18           C  
ANISOU 4280  CG  GLN B 249     4208   2500   1721     -2    310     85       C  
ATOM   4281  CD  GLN B 249      27.910 -12.220 -12.741  1.00 29.61           C  
ANISOU 4281  CD  GLN B 249     5413   3401   2437     53    374     84       C  
ATOM   4282  OE1 GLN B 249      27.131 -12.941 -13.358  1.00 30.63           O  
ANISOU 4282  OE1 GLN B 249     5720   3483   2437     36    244     25       O  
ATOM   4283  NE2 GLN B 249      29.084 -11.835 -13.244  1.00 27.77           N  
ANISOU 4283  NE2 GLN B 249     5216   3183   2152    111    579    152       N  
ATOM   4284  N   LEU B 250      25.353  -8.990 -10.701  1.00 28.81           N  
ANISOU 4284  N   LEU B 250     4825   3313   2810    -83     38    196       N  
ATOM   4285  CA  LEU B 250      25.763  -7.609 -11.026  1.00 21.48           C  
ANISOU 4285  CA  LEU B 250     3900   2359   1901    -76    105    283       C  
ATOM   4286  C   LEU B 250      25.025  -6.568 -10.186  1.00 21.10           C  
ANISOU 4286  C   LEU B 250     3717   2271   2029    -86     63    304       C  
ATOM   4287  O   LEU B 250      25.074  -5.360 -10.468  1.00 21.75           O  
ANISOU 4287  O   LEU B 250     3816   2301   2149    -78     89    380       O  
ATOM   4288  CB  LEU B 250      25.546  -7.343 -12.518  1.00 23.05           C  
ANISOU 4288  CB  LEU B 250     4290   2537   1933    -51     49    360       C  
ATOM   4289  CG  LEU B 250      26.309  -8.342 -13.408  1.00 23.85           C  
ANISOU 4289  CG  LEU B 250     4579   2657   1828    -25    131    330       C  
ATOM   4290  CD1 LEU B 250      25.965  -8.160 -14.882  1.00 25.73           C  
ANISOU 4290  CD1 LEU B 250     5056   2871   1851    -10     54    395       C  
ATOM   4291  CD2 LEU B 250      27.821  -8.236 -13.175  1.00 26.38           C  
ANISOU 4291  CD2 LEU B 250     4850   3002   2171     -4    366    350       C  
ATOM   4292  N   TYR B 251      24.358  -7.044  -9.144  1.00 20.27           N  
ANISOU 4292  N   TYR B 251     3493   2177   2031    -97     18    240       N  
ATOM   4293  CA  TYR B 251      23.635  -6.165  -8.228  1.00 27.79           C  
ANISOU 4293  CA  TYR B 251     4332   3081   3145    -87     19    246       C  
ATOM   4294  C   TYR B 251      24.544  -5.072  -7.666  1.00 25.46           C  
ANISOU 4294  C   TYR B 251     4032   2741   2902   -114    145    245       C  
ATOM   4295  O   TYR B 251      25.646  -5.355  -7.167  1.00 21.82           O  
ANISOU 4295  O   TYR B 251     3557   2317   2417   -165    226    202       O  
ATOM   4296  CB  TYR B 251      23.015  -6.976  -7.087  1.00 25.50           C  
ANISOU 4296  CB  TYR B 251     3927   2822   2939    -97      2    174       C  
ATOM   4297  CG  TYR B 251      22.464  -6.123  -5.958  1.00 23.19           C  
ANISOU 4297  CG  TYR B 251     3544   2475   2791    -77     66    162       C  
ATOM   4298  CD1 TYR B 251      21.248  -5.468  -6.091  1.00 22.13           C  
ANISOU 4298  CD1 TYR B 251     3350   2284   2772    -13     22    233       C  
ATOM   4299  CD2 TYR B 251      23.157  -5.978  -4.761  1.00 21.86           C  
ANISOU 4299  CD2 TYR B 251     3360   2306   2639   -118    172     86       C  
ATOM   4300  CE1 TYR B 251      20.728  -4.687  -5.069  1.00 23.61           C  
ANISOU 4300  CE1 TYR B 251     3478   2402   3090     31    121    219       C  
ATOM   4301  CE2 TYR B 251      22.640  -5.205  -3.718  1.00 19.08           C  
ANISOU 4301  CE2 TYR B 251     2978   1886   2385    -97    247     57       C  
ATOM   4302  CZ  TYR B 251      21.417  -4.563  -3.886  1.00 22.35           C  
ANISOU 4302  CZ  TYR B 251     3347   2231   2915    -12    241    119       C  
ATOM   4303  OH  TYR B 251      20.872  -3.784  -2.880  1.00 23.46           O  
ANISOU 4303  OH  TYR B 251     3477   2284   3153     36    355     91       O  
ATOM   4304  N   ARG B 252      24.073  -3.824  -7.752  1.00 22.45           N  
ANISOU 4304  N   ARG B 252     3659   2268   2604    -85    152    303       N  
ATOM   4305  CA  ARG B 252      24.801  -2.678  -7.215  1.00 24.40           C  
ANISOU 4305  CA  ARG B 252     3927   2434   2911   -127    254    299       C  
ATOM   4306  C   ARG B 252      24.113  -2.027  -6.005  1.00 25.33           C  
ANISOU 4306  C   ARG B 252     4005   2463   3157   -109    297    241       C  
ATOM   4307  O   ARG B 252      24.761  -1.736  -5.007  1.00 29.47           O  
ANISOU 4307  O   ARG B 252     4543   2958   3696   -179    366    165       O  
ATOM   4308  CB  ARG B 252      25.005  -1.625  -8.299  1.00 31.12           C  
ANISOU 4308  CB  ARG B 252     4866   3210   3746   -111    263    414       C  
ATOM   4309  CG  ARG B 252      25.861  -0.457  -7.852  1.00 46.63           C  
ANISOU 4309  CG  ARG B 252     6867   5075   5777   -181    360    419       C  
ATOM   4310  CD  ARG B 252      27.189  -0.952  -7.306  1.00 58.37           C  
ANISOU 4310  CD  ARG B 252     8318   6635   7226   -287    415    365       C  
ATOM   4311  NE  ARG B 252      28.313  -0.243  -7.906  1.00 73.70           N  
ANISOU 4311  NE  ARG B 252    10297   8545   9162   -358    481    457       N  
ATOM   4312  CZ  ARG B 252      29.587  -0.579  -7.729  1.00 81.63           C  
ANISOU 4312  CZ  ARG B 252    11243   9618  10154   -447    533    469       C  
ATOM   4313  NH1 ARG B 252      29.902  -1.621  -6.969  1.00 78.23           N  
ANISOU 4313  NH1 ARG B 252    10727   9290   9707   -469    517    392       N  
ATOM   4314  NH2 ARG B 252      30.545   0.127  -8.316  1.00 88.76           N  
ANISOU 4314  NH2 ARG B 252    12159  10489  11078   -512    603    579       N  
ATOM   4315  N   GLY B 253      22.811  -1.767  -6.095  1.00 21.95           N  
ANISOU 4315  N   GLY B 253     3534   1987   2820    -14    261    287       N  
ATOM   4316  CA  GLY B 253      22.110  -1.219  -4.948  1.00 24.46           C  
ANISOU 4316  CA  GLY B 253     3822   2215   3258     32    346    235       C  
ATOM   4317  C   GLY B 253      20.605  -1.131  -5.114  1.00 28.08           C  
ANISOU 4317  C   GLY B 253     4179   2643   3847    156    312    319       C  
ATOM   4318  O   GLY B 253      20.091  -1.394  -6.194  1.00 23.78           O  
ANISOU 4318  O   GLY B 253     3594   2144   3299    190    185    427       O  
ATOM   4319  N   GLY B 254      19.904  -0.743  -4.049  1.00 26.23           N  
ANISOU 4319  N   GLY B 254     3909   2330   3727    223    428    279       N  
ATOM   4320  CA  GLY B 254      18.452  -0.614  -4.099  1.00 26.92           C  
ANISOU 4320  CA  GLY B 254     3859   2386   3983    357    428    383       C  
ATOM   4321  C   GLY B 254      17.765  -1.868  -3.598  1.00 28.92           C  
ANISOU 4321  C   GLY B 254     3966   2759   4262    353    395    370       C  
ATOM   4322  O   GLY B 254      18.426  -2.816  -3.178  1.00 33.74           O  
ANISOU 4322  O   GLY B 254     4603   3465   4751    254    378    270       O  
ATOM   4323  N   ILE B 255      16.438  -1.878  -3.632  1.00 26.02           N  
ANISOU 4323  N   ILE B 255     3430   2383   4073    460    386    488       N  
ATOM   4324  CA  ILE B 255      15.683  -3.033  -3.173  1.00 30.66           C  
ANISOU 4324  CA  ILE B 255     3855   3074   4719    448    355    503       C  
ATOM   4325  C   ILE B 255      15.503  -4.039  -4.314  1.00 27.72           C  
ANISOU 4325  C   ILE B 255     3416   2819   4298    367    102    580       C  
ATOM   4326  O   ILE B 255      14.908  -3.721  -5.350  1.00 26.78           O  
ANISOU 4326  O   ILE B 255     3235   2692   4247    402    -46    723       O  
ATOM   4327  CB  ILE B 255      14.316  -2.604  -2.606  1.00 37.70           C  
ANISOU 4327  CB  ILE B 255     4567   3904   5854    599    483    614       C  
ATOM   4328  CG1 ILE B 255      14.521  -1.721  -1.375  1.00 28.35           C  
ANISOU 4328  CG1 ILE B 255     3508   2588   4675    677    761    504       C  
ATOM   4329  CG2 ILE B 255      13.477  -3.814  -2.233  1.00 31.72           C  
ANISOU 4329  CG2 ILE B 255     3610   3258   5184    572    439    666       C  
ATOM   4330  CD1 ILE B 255      13.249  -1.087  -0.852  1.00 37.72           C  
ANISOU 4330  CD1 ILE B 255     4553   3676   6104    865    949    616       C  
ATOM   4331  N   PHE B 256      16.043  -5.240  -4.116  1.00 24.11           N  
ANISOU 4331  N   PHE B 256     2993   2457   3711    256     50    484       N  
ATOM   4332  CA  PHE B 256      16.030  -6.301  -5.118  1.00 29.73           C  
ANISOU 4332  CA  PHE B 256     3708   3255   4334    163   -171    514       C  
ATOM   4333  C   PHE B 256      14.704  -7.070  -5.124  1.00 27.42           C  
ANISOU 4333  C   PHE B 256     3207   3007   4202    154   -291    626       C  
ATOM   4334  O   PHE B 256      14.331  -7.706  -4.132  1.00 24.89           O  
ANISOU 4334  O   PHE B 256     2782   2714   3961    145   -200    600       O  
ATOM   4335  CB  PHE B 256      17.193  -7.252  -4.858  1.00 26.10           C  
ANISOU 4335  CB  PHE B 256     3377   2852   3688     65   -151    371       C  
ATOM   4336  CG  PHE B 256      17.488  -8.202  -5.989  1.00 27.02           C  
ANISOU 4336  CG  PHE B 256     3585   3020   3664    -18   -335    370       C  
ATOM   4337  CD1 PHE B 256      18.295  -7.811  -7.048  1.00 29.44           C  
ANISOU 4337  CD1 PHE B 256     4055   3314   3817    -28   -379    369       C  
ATOM   4338  CD2 PHE B 256      16.997  -9.491  -5.972  1.00 27.31           C  
ANISOU 4338  CD2 PHE B 256     3567   3101   3708    -88   -446    366       C  
ATOM   4339  CE1 PHE B 256      18.593  -8.692  -8.081  1.00 32.24           C  
ANISOU 4339  CE1 PHE B 256     4539   3701   4010    -92   -517    354       C  
ATOM   4340  CE2 PHE B 256      17.282 -10.383  -7.004  1.00 30.86           C  
ANISOU 4340  CE2 PHE B 256     4151   3569   4007   -166   -606    343       C  
ATOM   4341  CZ  PHE B 256      18.080  -9.981  -8.062  1.00 31.25           C  
ANISOU 4341  CZ  PHE B 256     4385   3605   3883   -161   -633    332       C  
ATOM   4342  N   VAL B 257      14.005  -7.004  -6.252  1.00 30.66           N  
ANISOU 4342  N   VAL B 257     3561   3427   4660    145   -505    764       N  
ATOM   4343  CA  VAL B 257      12.687  -7.625  -6.403  1.00 37.94           C  
ANISOU 4343  CA  VAL B 257     4260   4390   5764    117   -667    908       C  
ATOM   4344  C   VAL B 257      12.721  -8.870  -7.285  1.00 42.80           C  
ANISOU 4344  C   VAL B 257     4958   5062   6243    -42   -930    891       C  
ATOM   4345  O   VAL B 257      11.715  -9.561  -7.436  1.00 45.29           O  
ANISOU 4345  O   VAL B 257     5107   5409   6691   -113  -1105    999       O  
ATOM   4346  CB  VAL B 257      11.673  -6.652  -7.031  1.00 37.28           C  
ANISOU 4346  CB  VAL B 257     4019   4274   5873    212   -766   1119       C  
ATOM   4347  CG1 VAL B 257      11.454  -5.435  -6.137  1.00 33.62           C  
ANISOU 4347  CG1 VAL B 257     3471   3722   5580    388   -488   1149       C  
ATOM   4348  CG2 VAL B 257      12.143  -6.239  -8.434  1.00 34.61           C  
ANISOU 4348  CG2 VAL B 257     3869   3927   5354    178   -960   1153       C  
ATOM   4349  N   GLY B 258      13.875  -9.134  -7.886  1.00 44.25           N  
ANISOU 4349  N   GLY B 258     5402   5246   6165    -97   -954    762       N  
ATOM   4350  CA  GLY B 258      14.002 -10.193  -8.871  1.00 50.30           C  
ANISOU 4350  CA  GLY B 258     6319   6035   6758   -230  -1183    730       C  
ATOM   4351  C   GLY B 258      14.575  -9.652 -10.169  1.00 48.59           C  
ANISOU 4351  C   GLY B 258     6328   5803   6332   -228  -1284    741       C  
ATOM   4352  O   GLY B 258      14.941  -8.482 -10.238  1.00 49.56           O  
ANISOU 4352  O   GLY B 258     6473   5898   6458   -130  -1167    775       O  
ATOM   4353  N   PRO B 259      14.627 -10.487 -11.217  1.00 48.50           N  
ANISOU 4353  N   PRO B 259     6504   5796   6129   -340  -1499    718       N  
ATOM   4354  CA  PRO B 259      14.072 -11.841 -11.228  1.00 48.52           C  
ANISOU 4354  CA  PRO B 259     6495   5802   6138   -475  -1674    690       C  
ATOM   4355  C   PRO B 259      15.008 -12.852 -10.577  1.00 42.04           C  
ANISOU 4355  C   PRO B 259     5790   4967   5216   -500  -1504    510       C  
ATOM   4356  O   PRO B 259      16.227 -12.757 -10.707  1.00 43.40           O  
ANISOU 4356  O   PRO B 259     6154   5128   5208   -449  -1340    399       O  
ATOM   4357  CB  PRO B 259      13.911 -12.131 -12.720  1.00 53.74           C  
ANISOU 4357  CB  PRO B 259     7389   6448   6580   -578  -1960    722       C  
ATOM   4358  CG  PRO B 259      15.075 -11.414 -13.336  1.00 56.65           C  
ANISOU 4358  CG  PRO B 259     8001   6804   6718   -491  -1813    662       C  
ATOM   4359  CD  PRO B 259      15.319 -10.176 -12.482  1.00 53.52           C  
ANISOU 4359  CD  PRO B 259     7418   6417   6500   -346  -1567    706       C  
ATOM   4360  N   CYS B 260      14.416 -13.793  -9.854  1.00 43.30           N  
ANISOU 4360  N   CYS B 260     5809   5125   5516   -573  -1538    505       N  
ATOM   4361  CA  CYS B 260      15.141 -14.923  -9.302  1.00 46.26           C  
ANISOU 4361  CA  CYS B 260     6291   5474   5810   -610  -1424    361       C  
ATOM   4362  C   CYS B 260      14.123 -15.998  -8.959  1.00 42.55           C  
ANISOU 4362  C   CYS B 260     5688   4986   5493   -739  -1580    407       C  
ATOM   4363  O   CYS B 260      12.986 -15.702  -8.599  1.00 47.75           O  
ANISOU 4363  O   CYS B 260     6078   5677   6389   -756  -1657    552       O  
ATOM   4364  CB  CYS B 260      15.981 -14.520  -8.076  1.00 48.09           C  
ANISOU 4364  CB  CYS B 260     6448   5734   6090   -498  -1119    295       C  
ATOM   4365  SG  CYS B 260      15.140 -13.546  -6.798  1.00 47.67           S  
ANISOU 4365  SG  CYS B 260     6072   5722   6320   -409   -973    404       S  
ATOM   4366  N   GLY B 261      14.523 -17.251  -9.106  1.00 43.77           N  
ANISOU 4366  N   GLY B 261     6028   5078   5525   -829  -1621    296       N  
ATOM   4367  CA  GLY B 261      13.641 -18.353  -8.784  1.00 44.00           C  
ANISOU 4367  CA  GLY B 261     5956   5068   5696   -972  -1768    335       C  
ATOM   4368  C   GLY B 261      13.840 -18.784  -7.345  1.00 35.96           C  
ANISOU 4368  C   GLY B 261     4781   4064   4818   -927  -1535    314       C  
ATOM   4369  O   GLY B 261      14.480 -18.084  -6.559  1.00 42.57           O  
ANISOU 4369  O   GLY B 261     5555   4956   5665   -791  -1290    289       O  
ATOM   4370  N   ASN B 262      13.308 -19.954  -7.015  1.00 31.45           N  
ANISOU 4370  N   ASN B 262     4168   3437   4342  -1055  -1626    328       N  
ATOM   4371  CA  ASN B 262      13.326 -20.469  -5.653  1.00 35.23           C  
ANISOU 4371  CA  ASN B 262     4495   3929   4963  -1033  -1431    339       C  
ATOM   4372  C   ASN B 262      14.310 -21.608  -5.451  1.00 36.86           C  
ANISOU 4372  C   ASN B 262     4929   4051   5027  -1046  -1343    203       C  
ATOM   4373  O   ASN B 262      14.324 -22.228  -4.390  1.00 35.89           O  
ANISOU 4373  O   ASN B 262     4710   3922   5003  -1049  -1214    221       O  
ATOM   4374  CB  ASN B 262      11.927 -20.948  -5.262  1.00 48.54           C  
ANISOU 4374  CB  ASN B 262     5915   5613   6916  -1163  -1564    497       C  
ATOM   4375  CG  ASN B 262      10.882 -19.866  -5.416  1.00 64.44           C  
ANISOU 4375  CG  ASN B 262     7659   7707   9119  -1133  -1639    666       C  
ATOM   4376  OD1 ASN B 262      11.128 -18.701  -5.087  1.00 66.63           O  
ANISOU 4376  OD1 ASN B 262     7861   8052   9404   -972  -1460    680       O  
ATOM   4377  ND2 ASN B 262       9.707 -20.239  -5.927  1.00 64.30           N  
ANISOU 4377  ND2 ASN B 262     7493   7672   9266  -1292  -1913    807       N  
ATOM   4378  N   LYS B 263      15.099 -21.915  -6.476  1.00 37.51           N  
ANISOU 4378  N   LYS B 263     5314   4059   4878  -1047  -1404     82       N  
ATOM   4379  CA  LYS B 263      16.131 -22.940  -6.343  1.00 43.29           C  
ANISOU 4379  CA  LYS B 263     6269   4699   5482  -1021  -1286    -40       C  
ATOM   4380  C   LYS B 263      17.315 -22.396  -5.554  1.00 33.96           C  
ANISOU 4380  C   LYS B 263     5055   3596   4254   -850  -1007    -76       C  
ATOM   4381  O   LYS B 263      18.300 -21.947  -6.136  1.00 36.20           O  
ANISOU 4381  O   LYS B 263     5496   3889   4371   -754   -922   -146       O  
ATOM   4382  CB  LYS B 263      16.602 -23.422  -7.714  1.00 50.81           C  
ANISOU 4382  CB  LYS B 263     7576   5535   6195  -1057  -1405   -156       C  
ATOM   4383  CG  LYS B 263      15.657 -24.367  -8.414  1.00 63.21           C  
ANISOU 4383  CG  LYS B 263     9269   6977   7769  -1260  -1691   -158       C  
ATOM   4384  CD  LYS B 263      16.195 -24.748  -9.788  1.00 68.60           C  
ANISOU 4384  CD  LYS B 263    10362   7541   8164  -1276  -1777   -290       C  
ATOM   4385  CE  LYS B 263      17.633 -25.252  -9.713  1.00 69.74           C  
ANISOU 4385  CE  LYS B 263    10738   7607   8151  -1125  -1510   -421       C  
ATOM   4386  NZ  LYS B 263      17.766 -26.496  -8.897  1.00 73.29           N  
ANISOU 4386  NZ  LYS B 263    11193   7944   8711  -1152  -1430   -446       N  
ATOM   4387  N   VAL B 264      17.226 -22.437  -4.228  1.00 27.03           N  
ANISOU 4387  N   VAL B 264     3977   2775   3518   -821   -868    -18       N  
ATOM   4388  CA  VAL B 264      18.220 -21.772  -3.405  1.00 26.55           C  
ANISOU 4388  CA  VAL B 264     3865   2802   3419   -687   -645    -35       C  
ATOM   4389  C   VAL B 264      19.577 -22.487  -3.508  1.00 25.74           C  
ANISOU 4389  C   VAL B 264     3956   2644   3180   -618   -537   -120       C  
ATOM   4390  O   VAL B 264      19.646 -23.708  -3.663  1.00 27.04           O  
ANISOU 4390  O   VAL B 264     4246   2696   3332   -663   -574   -151       O  
ATOM   4391  CB  VAL B 264      17.749 -21.681  -1.940  1.00 27.91           C  
ANISOU 4391  CB  VAL B 264     3815   3044   3746   -682   -530     48       C  
ATOM   4392  CG1 VAL B 264      16.419 -20.928  -1.889  1.00 27.80           C  
ANISOU 4392  CG1 VAL B 264     3596   3078   3890   -719   -599    149       C  
ATOM   4393  CG2 VAL B 264      17.582 -23.070  -1.334  1.00 27.71           C  
ANISOU 4393  CG2 VAL B 264     3797   2944   3786   -753   -531     72       C  
ATOM   4394  N   ASP B 265      20.652 -21.717  -3.443  1.00 27.66           N  
ANISOU 4394  N   ASP B 265     4217   2957   3338   -509   -400   -145       N  
ATOM   4395  CA  ASP B 265      21.955 -22.240  -3.811  1.00 23.11           C  
ANISOU 4395  CA  ASP B 265     3806   2332   2643   -427   -297   -202       C  
ATOM   4396  C   ASP B 265      23.078 -21.595  -3.022  1.00 19.95           C  
ANISOU 4396  C   ASP B 265     3310   2033   2238   -333   -134   -177       C  
ATOM   4397  O   ASP B 265      24.219 -21.951  -3.199  1.00 26.07           O  
ANISOU 4397  O   ASP B 265     4164   2788   2953   -253    -32   -190       O  
ATOM   4398  CB  ASP B 265      22.197 -22.046  -5.321  1.00 28.26           C  
ANISOU 4398  CB  ASP B 265     4671   2927   3141   -409   -350   -266       C  
ATOM   4399  CG  ASP B 265      22.079 -20.571  -5.767  1.00 26.96           C  
ANISOU 4399  CG  ASP B 265     4446   2854   2944   -389   -367   -241       C  
ATOM   4400  OD1 ASP B 265      22.306 -19.650  -4.953  1.00 24.98           O  
ANISOU 4400  OD1 ASP B 265     4027   2703   2763   -351   -280   -197       O  
ATOM   4401  OD2 ASP B 265      21.752 -20.332  -6.946  1.00 31.55           O  
ANISOU 4401  OD2 ASP B 265     5170   3398   3420   -415   -475   -263       O  
ATOM   4402  N   HIS B 266      22.740 -20.666  -2.135  1.00 20.85           N  
ANISOU 4402  N   HIS B 266     3255   2246   2421   -345   -110   -133       N  
ATOM   4403  CA  HIS B 266      23.736 -19.806  -1.508  1.00 22.12           C  
ANISOU 4403  CA  HIS B 266     3348   2497   2558   -289      2   -116       C  
ATOM   4404  C   HIS B 266      23.237 -19.402  -0.138  1.00 22.84           C  
ANISOU 4404  C   HIS B 266     3299   2656   2722   -321     34    -77       C  
ATOM   4405  O   HIS B 266      22.065 -19.052   0.027  1.00 25.41           O  
ANISOU 4405  O   HIS B 266     3554   2983   3118   -360     -7    -60       O  
ATOM   4406  CB  HIS B 266      24.004 -18.580  -2.405  1.00 19.32           C  
ANISOU 4406  CB  HIS B 266     3030   2169   2142   -261      4   -135       C  
ATOM   4407  CG  HIS B 266      25.041 -17.625  -1.885  1.00 22.56           C  
ANISOU 4407  CG  HIS B 266     3380   2655   2537   -229     99   -115       C  
ATOM   4408  ND1 HIS B 266      26.325 -18.011  -1.556  1.00 21.74           N  
ANISOU 4408  ND1 HIS B 266     3266   2579   2415   -190    180    -89       N  
ATOM   4409  CD2 HIS B 266      24.986 -16.286  -1.677  1.00 17.34           C  
ANISOU 4409  CD2 HIS B 266     2667   2036   1885   -240    115   -110       C  
ATOM   4410  CE1 HIS B 266      27.009 -16.951  -1.159  1.00 24.48           C  
ANISOU 4410  CE1 HIS B 266     3549   2991   2761   -200    220    -66       C  
ATOM   4411  NE2 HIS B 266      26.221 -15.894  -1.221  1.00 20.15           N  
ANISOU 4411  NE2 HIS B 266     2992   2442   2222   -232    187    -89       N  
ATOM   4412  N   ALA B 267      24.109 -19.476   0.857  1.00 22.72           N  
ANISOU 4412  N   ALA B 267     3247   2695   2689   -304    108    -50       N  
ATOM   4413  CA  ALA B 267      23.733 -19.066   2.208  1.00 20.82           C  
ANISOU 4413  CA  ALA B 267     2925   2517   2471   -336    150    -22       C  
ATOM   4414  C   ALA B 267      24.301 -17.703   2.575  1.00 22.52           C  
ANISOU 4414  C   ALA B 267     3130   2792   2634   -333    192    -42       C  
ATOM   4415  O   ALA B 267      25.420 -17.363   2.212  1.00 25.45           O  
ANISOU 4415  O   ALA B 267     3523   3185   2961   -315    198    -44       O  
ATOM   4416  CB  ALA B 267      24.174 -20.106   3.220  1.00 19.92           C  
ANISOU 4416  CB  ALA B 267     2798   2416   2352   -343    177     32       C  
ATOM   4417  N   VAL B 268      23.510 -16.938   3.316  1.00 21.19           N  
ANISOU 4417  N   VAL B 268     2932   2641   2480   -352    233    -50       N  
ATOM   4418  CA  VAL B 268      23.841 -15.569   3.678  1.00 23.58           C  
ANISOU 4418  CA  VAL B 268     3260   2964   2735   -359    275    -85       C  
ATOM   4419  C   VAL B 268      23.348 -15.316   5.093  1.00 23.48           C  
ANISOU 4419  C   VAL B 268     3259   2973   2689   -381    353    -86       C  
ATOM   4420  O   VAL B 268      22.770 -16.212   5.708  1.00 29.93           O  
ANISOU 4420  O   VAL B 268     4045   3799   3528   -387    379    -44       O  
ATOM   4421  CB  VAL B 268      23.195 -14.561   2.731  1.00 26.59           C  
ANISOU 4421  CB  VAL B 268     3639   3298   3165   -328    269   -108       C  
ATOM   4422  CG1 VAL B 268      23.862 -14.600   1.351  1.00 20.21           C  
ANISOU 4422  CG1 VAL B 268     2865   2474   2340   -309    207   -110       C  
ATOM   4423  CG2 VAL B 268      21.694 -14.843   2.624  1.00 25.03           C  
ANISOU 4423  CG2 VAL B 268     3369   3069   3072   -309    268    -77       C  
ATOM   4424  N   ALA B 269      23.560 -14.111   5.614  1.00 21.87           N  
ANISOU 4424  N   ALA B 269     3120   2764   2424   -397    400   -133       N  
ATOM   4425  CA  ALA B 269      23.072 -13.797   6.963  1.00 23.40           C  
ANISOU 4425  CA  ALA B 269     3377   2961   2551   -410    500   -150       C  
ATOM   4426  C   ALA B 269      22.066 -12.642   6.948  1.00 21.61           C  
ANISOU 4426  C   ALA B 269     3173   2663   2375   -355    610   -189       C  
ATOM   4427  O   ALA B 269      22.323 -11.567   6.390  1.00 23.41           O  
ANISOU 4427  O   ALA B 269     3441   2841   2611   -346    600   -233       O  
ATOM   4428  CB  ALA B 269      24.238 -13.477   7.893  1.00 25.32           C  
ANISOU 4428  CB  ALA B 269     3730   3245   2645   -491    463   -174       C  
ATOM   4429  N   ALA B 270      20.913 -12.871   7.559  1.00 24.26           N  
ANISOU 4429  N   ALA B 270     3471   2987   2759   -309    729   -158       N  
ATOM   4430  CA  ALA B 270      19.913 -11.819   7.688  1.00 28.94           C  
ANISOU 4430  CA  ALA B 270     4072   3505   3418   -229    873   -175       C  
ATOM   4431  C   ALA B 270      20.237 -10.986   8.928  1.00 27.38           C  
ANISOU 4431  C   ALA B 270     4077   3273   3054   -246    995   -258       C  
ATOM   4432  O   ALA B 270      20.111 -11.476  10.046  1.00 26.40           O  
ANISOU 4432  O   ALA B 270     4023   3184   2826   -265   1079   -250       O  
ATOM   4433  CB  ALA B 270      18.517 -12.417   7.775  1.00 25.93           C  
ANISOU 4433  CB  ALA B 270     3537   3126   3190   -166    966    -80       C  
ATOM   4434  N   VAL B 271      20.710  -9.757   8.737  1.00 23.08           N  
ANISOU 4434  N   VAL B 271     3651   2654   2466   -253    994   -338       N  
ATOM   4435  CA  VAL B 271      21.121  -8.958   9.892  1.00 22.83           C  
ANISOU 4435  CA  VAL B 271     3859   2568   2248   -299   1078   -437       C  
ATOM   4436  C   VAL B 271      20.193  -7.797  10.176  1.00 31.28           C  
ANISOU 4436  C   VAL B 271     5030   3502   3355   -189   1289   -488       C  
ATOM   4437  O   VAL B 271      20.519  -6.920  10.974  1.00 31.58           O  
ANISOU 4437  O   VAL B 271     5312   3451   3236   -224   1365   -594       O  
ATOM   4438  CB  VAL B 271      22.551  -8.422   9.737  1.00 28.46           C  
ANISOU 4438  CB  VAL B 271     4683   3278   2852   -427    912   -498       C  
ATOM   4439  CG1 VAL B 271      23.541  -9.582   9.742  1.00 28.00           C  
ANISOU 4439  CG1 VAL B 271     4542   3353   2745   -522    739   -436       C  
ATOM   4440  CG2 VAL B 271      22.711  -7.542   8.462  1.00 26.59           C  
ANISOU 4440  CG2 VAL B 271     4387   2970   2747   -401    859   -502       C  
ATOM   4441  N   GLY B 272      19.023  -7.808   9.545  1.00 32.54           N  
ANISOU 4441  N   GLY B 272     5006   3636   3723    -58   1384   -405       N  
ATOM   4442  CA  GLY B 272      18.023  -6.786   9.800  1.00 36.09           C  
ANISOU 4442  CA  GLY B 272     5506   3952   4252     83   1615   -418       C  
ATOM   4443  C   GLY B 272      16.895  -6.756   8.781  1.00 35.70           C  
ANISOU 4443  C   GLY B 272     5194   3889   4480    213   1639   -289       C  
ATOM   4444  O   GLY B 272      16.766  -7.671   7.956  1.00 30.49           O  
ANISOU 4444  O   GLY B 272     4324   3328   3933    179   1477   -194       O  
ATOM   4445  N   TYR B 273      16.086  -5.693   8.843  1.00 34.31           N  
ANISOU 4445  N   TYR B 273     5044   3579   4413    359   1837   -282       N  
ATOM   4446  CA  TYR B 273      14.956  -5.491   7.930  1.00 32.56           C  
ANISOU 4446  CA  TYR B 273     4565   3333   4475    495   1862   -135       C  
ATOM   4447  C   TYR B 273      14.314  -4.103   8.072  1.00 31.05           C  
ANISOU 4447  C   TYR B 273     4454   2960   4384    666   2092   -142       C  
ATOM   4448  O   TYR B 273      14.582  -3.370   9.020  1.00 34.95           O  
ANISOU 4448  O   TYR B 273     5223   3335   4720    690   2279   -272       O  
ATOM   4449  CB  TYR B 273      13.871  -6.561   8.154  1.00 36.05           C  
ANISOU 4449  CB  TYR B 273     4754   3873   5069    540   1930     12       C  
ATOM   4450  CG  TYR B 273      13.178  -6.450   9.494  1.00 37.01           C  
ANISOU 4450  CG  TYR B 273     4956   3949   5158    645   2257     10       C  
ATOM   4451  CD1 TYR B 273      12.109  -5.568   9.689  1.00 34.14           C  
ANISOU 4451  CD1 TYR B 273     4535   3465   4971    845   2530     80       C  
ATOM   4452  CD2 TYR B 273      13.593  -7.224  10.567  1.00 33.18           C  
ANISOU 4452  CD2 TYR B 273     4611   3535   4462    555   2310    -50       C  
ATOM   4453  CE1 TYR B 273      11.493  -5.466  10.914  1.00 42.85           C  
ANISOU 4453  CE1 TYR B 273     5736   4524   6023    939   2824     82       C  
ATOM   4454  CE2 TYR B 273      12.980  -7.132  11.791  1.00 35.49           C  
ANISOU 4454  CE2 TYR B 273     5009   3787   4689    650   2625    -51       C  
ATOM   4455  CZ  TYR B 273      11.931  -6.252  11.964  1.00 48.51           C  
ANISOU 4455  CZ  TYR B 273     6610   5319   6501    826   2838     16       C  
ATOM   4456  OH  TYR B 273      11.330  -6.166  13.200  1.00 57.88           O  
ANISOU 4456  OH  TYR B 273     7914   6469   7611    886   3039     31       O  
ATOM   4457  N   GLY B 274      13.426  -3.786   7.139  1.00 31.69           N  
ANISOU 4457  N   GLY B 274     4299   3013   4728    786   2076      8       N  
ATOM   4458  CA  GLY B 274      12.636  -2.566   7.190  1.00 34.22           C  
ANISOU 4458  CA  GLY B 274     4634   3160   5208    986   2308     51       C  
ATOM   4459  C   GLY B 274      11.234  -2.911   6.732  1.00 43.98           C  
ANISOU 4459  C   GLY B 274     5500   4446   6764   1125   2354    284       C  
ATOM   4460  O   GLY B 274      10.885  -4.088   6.669  1.00 42.96           O  
ANISOU 4460  O   GLY B 274     5160   4470   6692   1051   2250    378       O  
ATOM   4461  N   PRO B 275      10.421  -1.894   6.405  1.00 52.98           N  
ANISOU 4461  N   PRO B 275     6550   5450   8130   1322   2500    393       N  
ATOM   4462  CA  PRO B 275       9.015  -2.111   6.040  1.00 52.32           C  
ANISOU 4462  CA  PRO B 275     6083   5407   8391   1469   2558    648       C  
ATOM   4463  C   PRO B 275       8.835  -3.039   4.840  1.00 49.23           C  
ANISOU 4463  C   PRO B 275     5401   5184   8120   1337   2186    798       C  
ATOM   4464  O   PRO B 275       7.917  -3.859   4.839  1.00 50.61           O  
ANISOU 4464  O   PRO B 275     5276   5463   8489   1341   2169    971       O  
ATOM   4465  CB  PRO B 275       8.522  -0.703   5.703  1.00 59.03           C  
ANISOU 4465  CB  PRO B 275     6964   6094   9370   1619   2642    718       C  
ATOM   4466  CG  PRO B 275       9.434   0.206   6.460  1.00 60.85           C  
ANISOU 4466  CG  PRO B 275     7623   6173   9323   1591   2781    479       C  
ATOM   4467  CD  PRO B 275      10.770  -0.467   6.415  1.00 56.76           C  
ANISOU 4467  CD  PRO B 275     7282   5718   8567   1415   2624    295       C  
ATOM   4468  N   ASN B 276       9.705  -2.909   3.844  1.00 42.01           N  
ANISOU 4468  N   ASN B 276     4590   4286   7085   1213   1899    735       N  
ATOM   4469  CA  ASN B 276       9.556  -3.640   2.590  1.00 43.98           C  
ANISOU 4469  CA  ASN B 276     4629   4665   7417   1097   1547    863       C  
ATOM   4470  C   ASN B 276      10.839  -4.327   2.129  1.00 35.30           C  
ANISOU 4470  C   ASN B 276     3716   3655   6043    882   1294    708       C  
ATOM   4471  O   ASN B 276      11.032  -4.564   0.936  1.00 35.92           O  
ANISOU 4471  O   ASN B 276     3745   3788   6115    797   1015    764       O  
ATOM   4472  CB  ASN B 276       9.061  -2.695   1.491  1.00 55.39           C  
ANISOU 4472  CB  ASN B 276     5955   6035   9056   1208   1440   1023       C  
ATOM   4473  CG  ASN B 276      10.052  -1.587   1.186  1.00 69.58           C  
ANISOU 4473  CG  ASN B 276     8045   7701  10691   1217   1447    887       C  
ATOM   4474  OD1 ASN B 276      10.848  -1.197   2.042  1.00 72.68           O  
ANISOU 4474  OD1 ASN B 276     8713   8011  10892   1201   1623    690       O  
ATOM   4475  ND2 ASN B 276      10.005  -1.071  -0.039  1.00 72.21           N  
ANISOU 4475  ND2 ASN B 276     8326   8014  11098   1231   1243   1003       N  
ATOM   4476  N   TYR B 277      11.726  -4.641   3.064  1.00 33.75           N  
ANISOU 4476  N   TYR B 277     3740   3469   5615    800   1394    524       N  
ATOM   4477  CA  TYR B 277      12.910  -5.414   2.701  1.00 34.45           C  
ANISOU 4477  CA  TYR B 277     3963   3650   5478    613   1177    406       C  
ATOM   4478  C   TYR B 277      13.422  -6.219   3.882  1.00 33.93           C  
ANISOU 4478  C   TYR B 277     4009   3642   5241    531   1277    289       C  
ATOM   4479  O   TYR B 277      12.985  -6.026   5.019  1.00 32.98           O  
ANISOU 4479  O   TYR B 277     3925   3479   5128    611   1528    270       O  
ATOM   4480  CB  TYR B 277      14.023  -4.499   2.174  1.00 33.73           C  
ANISOU 4480  CB  TYR B 277     4094   3483   5238    578   1110    298       C  
ATOM   4481  CG  TYR B 277      14.553  -3.568   3.232  1.00 36.52           C  
ANISOU 4481  CG  TYR B 277     4690   3713   5474    616   1334    154       C  
ATOM   4482  CD1 TYR B 277      13.985  -2.316   3.419  1.00 37.41           C  
ANISOU 4482  CD1 TYR B 277     4846   3662   5706    775   1527    181       C  
ATOM   4483  CD2 TYR B 277      15.611  -3.947   4.062  1.00 32.20           C  
ANISOU 4483  CD2 TYR B 277     4338   3202   4694    490   1347     -3       C  
ATOM   4484  CE1 TYR B 277      14.449  -1.467   4.400  1.00 41.80           C  
ANISOU 4484  CE1 TYR B 277     5670   4079   6135    797   1730     31       C  
ATOM   4485  CE2 TYR B 277      16.083  -3.102   5.044  1.00 34.48           C  
ANISOU 4485  CE2 TYR B 277     4876   3372   4854    497   1520   -138       C  
ATOM   4486  CZ  TYR B 277      15.497  -1.862   5.208  1.00 36.97           C  
ANISOU 4486  CZ  TYR B 277     5266   3510   5272    645   1713   -133       C  
ATOM   4487  OH  TYR B 277      15.950  -1.013   6.182  1.00 37.12           O  
ANISOU 4487  OH  TYR B 277     5578   3384   5144    642   1883   -284       O  
ATOM   4488  N   ILE B 278      14.360  -7.111   3.589  1.00 30.99           N  
ANISOU 4488  N   ILE B 278     3704   3362   4710    379   1089    219       N  
ATOM   4489  CA  ILE B 278      15.140  -7.801   4.606  1.00 24.54           C  
ANISOU 4489  CA  ILE B 278     3027   2598   3700    286   1140    106       C  
ATOM   4490  C   ILE B 278      16.608  -7.505   4.314  1.00 27.93           C  
ANISOU 4490  C   ILE B 278     3655   3023   3933    188   1023    -18       C  
ATOM   4491  O   ILE B 278      17.015  -7.502   3.165  1.00 26.17           O  
ANISOU 4491  O   ILE B 278     3410   2816   3717    150    850      3       O  
ATOM   4492  CB  ILE B 278      14.859  -9.314   4.601  1.00 24.62           C  
ANISOU 4492  CB  ILE B 278     2895   2720   3741    203   1034    173       C  
ATOM   4493  CG1 ILE B 278      13.450  -9.567   5.158  1.00 27.37           C  
ANISOU 4493  CG1 ILE B 278     3042   3070   4288    288   1192    306       C  
ATOM   4494  CG2 ILE B 278      15.893 -10.070   5.424  1.00 26.10           C  
ANISOU 4494  CG2 ILE B 278     3234   2965   3718     99   1031     71       C  
ATOM   4495  CD1 ILE B 278      12.947 -10.967   4.954  1.00 29.44           C  
ANISOU 4495  CD1 ILE B 278     3124   3417   4644    198   1064    407       C  
ATOM   4496  N   LEU B 279      17.387  -7.215   5.347  1.00 27.60           N  
ANISOU 4496  N   LEU B 279     3811   2959   3718    143   1120   -136       N  
ATOM   4497  CA  LEU B 279      18.768  -6.820   5.154  1.00 29.10           C  
ANISOU 4497  CA  LEU B 279     4163   3140   3754     42   1014   -231       C  
ATOM   4498  C   LEU B 279      19.680  -8.031   5.212  1.00 22.73           C  
ANISOU 4498  C   LEU B 279     3346   2456   2835    -77    875   -243       C  
ATOM   4499  O   LEU B 279      19.787  -8.720   6.236  1.00 24.16           O  
ANISOU 4499  O   LEU B 279     3565   2690   2925   -117    922   -264       O  
ATOM   4500  CB  LEU B 279      19.186  -5.771   6.192  1.00 27.44           C  
ANISOU 4500  CB  LEU B 279     4185   2824   3416     32   1155   -347       C  
ATOM   4501  CG  LEU B 279      20.643  -5.317   6.223  1.00 23.35           C  
ANISOU 4501  CG  LEU B 279     3834   2293   2745   -106   1042   -437       C  
ATOM   4502  CD1 LEU B 279      21.047  -4.580   4.945  1.00 26.85           C  
ANISOU 4502  CD1 LEU B 279     4250   2685   3269   -108    941   -405       C  
ATOM   4503  CD2 LEU B 279      20.841  -4.450   7.434  1.00 36.00           C  
ANISOU 4503  CD2 LEU B 279     5687   3784   4208   -133   1173   -555       C  
ATOM   4504  N   ILE B 280      20.361  -8.260   4.100  1.00 26.09           N  
ANISOU 4504  N   ILE B 280     3732   2917   3262   -122    716   -222       N  
ATOM   4505  CA  ILE B 280      21.135  -9.476   3.897  1.00 27.66           C  
ANISOU 4505  CA  ILE B 280     3898   3216   3396   -200    595   -210       C  
ATOM   4506  C   ILE B 280      22.634  -9.197   3.794  1.00 21.59           C  
ANISOU 4506  C   ILE B 280     3223   2466   2515   -286    524   -254       C  
ATOM   4507  O   ILE B 280      23.068  -8.395   2.981  1.00 23.11           O  
ANISOU 4507  O   ILE B 280     3444   2615   2722   -288    490   -254       O  
ATOM   4508  CB  ILE B 280      20.673 -10.198   2.622  1.00 17.85           C  
ANISOU 4508  CB  ILE B 280     2536   2000   2246   -177    479   -138       C  
ATOM   4509  CG1 ILE B 280      19.230 -10.689   2.768  1.00 22.32           C  
ANISOU 4509  CG1 ILE B 280     2968   2565   2946   -126    512    -66       C  
ATOM   4510  CG2 ILE B 280      21.643 -11.330   2.242  1.00 22.57           C  
ANISOU 4510  CG2 ILE B 280     3142   2665   2767   -240    375   -139       C  
ATOM   4511  CD1 ILE B 280      19.004 -11.603   3.954  1.00 24.68           C  
ANISOU 4511  CD1 ILE B 280     3246   2910   3221   -151    588    -62       C  
ATOM   4512  N   ARG B 281      23.412  -9.858   4.635  1.00 20.84           N  
ANISOU 4512  N   ARG B 281     3161   2437   2321   -358    500   -271       N  
ATOM   4513  CA  ARG B 281      24.871  -9.783   4.571  1.00 20.44           C  
ANISOU 4513  CA  ARG B 281     3147   2425   2196   -446    416   -275       C  
ATOM   4514  C   ARG B 281      25.429 -10.912   3.705  1.00 25.93           C  
ANISOU 4514  C   ARG B 281     3744   3188   2918   -435    337   -213       C  
ATOM   4515  O   ARG B 281      25.200 -12.084   4.004  1.00 22.45           O  
ANISOU 4515  O   ARG B 281     3257   2794   2480   -421    326   -185       O  
ATOM   4516  CB  ARG B 281      25.450  -9.856   5.984  1.00 24.90           C  
ANISOU 4516  CB  ARG B 281     3800   3024   2638   -533    413   -307       C  
ATOM   4517  CG  ARG B 281      26.942 -10.071   6.079  1.00 20.64           C  
ANISOU 4517  CG  ARG B 281     3245   2553   2046   -634    298   -271       C  
ATOM   4518  CD  ARG B 281      27.298 -10.332   7.510  1.00 25.11           C  
ANISOU 4518  CD  ARG B 281     3894   3165   2482   -719    267   -282       C  
ATOM   4519  NE  ARG B 281      28.691 -10.707   7.748  1.00 27.13           N  
ANISOU 4519  NE  ARG B 281     4098   3504   2705   -818    132   -211       N  
ATOM   4520  CZ  ARG B 281      29.691  -9.846   7.908  1.00 23.32           C  
ANISOU 4520  CZ  ARG B 281     3657   3014   2191   -941     40   -213       C  
ATOM   4521  NH1 ARG B 281      29.488  -8.539   7.790  1.00 25.89           N  
ANISOU 4521  NH1 ARG B 281     4101   3232   2505   -980     74   -296       N  
ATOM   4522  NH2 ARG B 281      30.912 -10.292   8.166  1.00 31.71           N  
ANISOU 4522  NH2 ARG B 281     4630   4167   3252  -1027    -91   -115       N  
ATOM   4523  N   ASN B 282      26.151 -10.562   2.635  1.00 27.10           N  
ANISOU 4523  N   ASN B 282     3880   3329   3087   -436    300   -189       N  
ATOM   4524  CA  ASN B 282      26.738 -11.557   1.731  1.00 21.05           C  
ANISOU 4524  CA  ASN B 282     3059   2607   2333   -407    262   -137       C  
ATOM   4525  C   ASN B 282      28.216 -11.746   2.073  1.00 22.94           C  
ANISOU 4525  C   ASN B 282     3264   2908   2544   -465    236    -92       C  
ATOM   4526  O   ASN B 282      28.766 -11.001   2.873  1.00 23.52           O  
ANISOU 4526  O   ASN B 282     3360   2989   2588   -551    215   -101       O  
ATOM   4527  CB  ASN B 282      26.584 -11.124   0.270  1.00 20.50           C  
ANISOU 4527  CB  ASN B 282     3006   2494   2288   -357    259   -121       C  
ATOM   4528  CG  ASN B 282      26.497 -12.294  -0.700  1.00 21.28           C  
ANISOU 4528  CG  ASN B 282     3103   2602   2379   -302    235    -98       C  
ATOM   4529  OD1 ASN B 282      26.894 -13.416  -0.399  1.00 23.89           O  
ANISOU 4529  OD1 ASN B 282     3411   2966   2701   -296    233    -84       O  
ATOM   4530  ND2 ASN B 282      25.955 -12.027  -1.881  1.00 21.23           N  
ANISOU 4530  ND2 ASN B 282     3144   2554   2370   -263    210    -92       N  
ATOM   4531  N   SER B 283      28.849 -12.738   1.461  1.00 22.96           N  
ANISOU 4531  N   SER B 283     3215   2945   2563   -420    236    -37       N  
ATOM   4532  CA  SER B 283      30.245 -13.049   1.750  1.00 29.33           C  
ANISOU 4532  CA  SER B 283     3945   3816   3382   -453    221     42       C  
ATOM   4533  C   SER B 283      31.067 -12.988   0.457  1.00 26.47           C  
ANISOU 4533  C   SER B 283     3551   3449   3055   -399    278    101       C  
ATOM   4534  O   SER B 283      31.847 -13.891   0.149  1.00 19.91           O  
ANISOU 4534  O   SER B 283     2661   2649   2255   -340    318    172       O  
ATOM   4535  CB  SER B 283      30.344 -14.425   2.420  1.00 23.35           C  
ANISOU 4535  CB  SER B 283     3146   3101   2627   -424    204     82       C  
ATOM   4536  OG  SER B 283      29.758 -15.419   1.596  1.00 23.60           O  
ANISOU 4536  OG  SER B 283     3208   3085   2673   -330    244     66       O  
ATOM   4537  N   TRP B 284      30.863 -11.909  -0.297  1.00 26.71           N  
ANISOU 4537  N   TRP B 284     3634   3434   3081   -410    300     79       N  
ATOM   4538  CA  TRP B 284      31.513 -11.703  -1.586  1.00 28.18           C  
ANISOU 4538  CA  TRP B 284     3821   3608   3277   -359    374    136       C  
ATOM   4539  C   TRP B 284      32.357 -10.453  -1.613  1.00 21.96           C  
ANISOU 4539  C   TRP B 284     2989   2824   2531   -447    380    193       C  
ATOM   4540  O   TRP B 284      32.616  -9.906  -2.681  1.00 23.25           O  
ANISOU 4540  O   TRP B 284     3181   2959   2695   -420    447    234       O  
ATOM   4541  CB  TRP B 284      30.478 -11.607  -2.698  1.00 26.15           C  
ANISOU 4541  CB  TRP B 284     3684   3286   2966   -291    390     84       C  
ATOM   4542  CG  TRP B 284      29.775 -12.867  -2.960  1.00 22.11           C  
ANISOU 4542  CG  TRP B 284     3225   2756   2418   -221    376     43       C  
ATOM   4543  CD1 TRP B 284      30.120 -14.114  -2.517  1.00 23.04           C  
ANISOU 4543  CD1 TRP B 284     3307   2898   2550   -188    390     57       C  
ATOM   4544  CD2 TRP B 284      28.585 -13.026  -3.742  1.00 21.25           C  
ANISOU 4544  CD2 TRP B 284     3221   2592   2263   -187    331     -8       C  
ATOM   4545  NE1 TRP B 284      29.207 -15.042  -2.973  1.00 23.85           N  
ANISOU 4545  NE1 TRP B 284     3501   2947   2615   -143    361      3       N  
ATOM   4546  CE2 TRP B 284      28.259 -14.395  -3.732  1.00 23.66           C  
ANISOU 4546  CE2 TRP B 284     3558   2880   2552   -152    312    -35       C  
ATOM   4547  CE3 TRP B 284      27.762 -12.139  -4.446  1.00 20.96           C  
ANISOU 4547  CE3 TRP B 284     3248   2512   2205   -189    288    -18       C  
ATOM   4548  CZ2 TRP B 284      27.143 -14.902  -4.408  1.00 21.53           C  
ANISOU 4548  CZ2 TRP B 284     3385   2554   2242   -141    236    -79       C  
ATOM   4549  CZ3 TRP B 284      26.656 -12.642  -5.115  1.00 21.64           C  
ANISOU 4549  CZ3 TRP B 284     3410   2557   2254   -167    208    -47       C  
ATOM   4550  CH2 TRP B 284      26.357 -14.015  -5.088  1.00 23.62           C  
ANISOU 4550  CH2 TRP B 284     3695   2794   2487   -154    174    -80       C  
ATOM   4551  N   GLY B 285      32.759  -9.984  -0.438  1.00 21.50           N  
ANISOU 4551  N   GLY B 285     2881   2792   2498   -565    302    197       N  
ATOM   4552  CA  GLY B 285      33.565  -8.779  -0.334  1.00 24.11           C  
ANISOU 4552  CA  GLY B 285     3178   3108   2876   -687    276    247       C  
ATOM   4553  C   GLY B 285      32.723  -7.516  -0.412  1.00 22.24           C  
ANISOU 4553  C   GLY B 285     3075   2763   2611   -727    268    162       C  
ATOM   4554  O   GLY B 285      31.535  -7.562  -0.713  1.00 26.16           O  
ANISOU 4554  O   GLY B 285     3663   3209   3067   -642    293     86       O  
ATOM   4555  N   THR B 286      33.344  -6.378  -0.149  1.00 24.04           N  
ANISOU 4555  N   THR B 286     3308   2948   2879   -860    230    187       N  
ATOM   4556  CA  THR B 286      32.620  -5.113  -0.117  1.00 25.50           C  
ANISOU 4556  CA  THR B 286     3636   3003   3050   -898    232    109       C  
ATOM   4557  C   THR B 286      32.407  -4.541  -1.525  1.00 25.50           C  
ANISOU 4557  C   THR B 286     3668   2943   3079   -820    318    160       C  
ATOM   4558  O   THR B 286      31.667  -3.579  -1.705  1.00 27.58           O  
ANISOU 4558  O   THR B 286     4045   3091   3344   -810    334    115       O  
ATOM   4559  CB  THR B 286      33.356  -4.085   0.740  1.00 28.56           C  
ANISOU 4559  CB  THR B 286     4058   3335   3459  -1090    145    105       C  
ATOM   4560  OG1 THR B 286      34.685  -3.935   0.242  1.00 27.55           O  
ANISOU 4560  OG1 THR B 286     3786   3258   3424  -1176    134    249       O  
ATOM   4561  CG2 THR B 286      33.428  -4.544   2.214  1.00 27.80           C  
ANISOU 4561  CG2 THR B 286     3986   3287   3289  -1178     40     42       C  
ATOM   4562  N   GLY B 287      33.033  -5.150  -2.521  1.00 28.79           N  
ANISOU 4562  N   GLY B 287     3998   3431   3510   -754    384    261       N  
ATOM   4563  CA  GLY B 287      32.893  -4.678  -3.896  1.00 28.48           C  
ANISOU 4563  CA  GLY B 287     4015   3345   3463   -682    469    322       C  
ATOM   4564  C   GLY B 287      31.675  -5.225  -4.632  1.00 25.55           C  
ANISOU 4564  C   GLY B 287     3738   2961   3009   -538    483    268       C  
ATOM   4565  O   GLY B 287      31.544  -5.052  -5.848  1.00 30.66           O  
ANISOU 4565  O   GLY B 287     4449   3586   3612   -469    537    324       O  
ATOM   4566  N   TRP B 288      30.798  -5.900  -3.888  1.00 25.51           N  
ANISOU 4566  N   TRP B 288     3743   2972   2979   -503    425    173       N  
ATOM   4567  CA  TRP B 288      29.519  -6.383  -4.399  1.00 24.20           C  
ANISOU 4567  CA  TRP B 288     3643   2789   2764   -398    401    127       C  
ATOM   4568  C   TRP B 288      28.392  -5.667  -3.685  1.00 25.46           C  
ANISOU 4568  C   TRP B 288     3840   2869   2963   -402    361     60       C  
ATOM   4569  O   TRP B 288      28.468  -5.470  -2.482  1.00 25.31           O  
ANISOU 4569  O   TRP B 288     3808   2840   2967   -466    352      3       O  
ATOM   4570  CB  TRP B 288      29.356  -7.899  -4.196  1.00 18.18           C  
ANISOU 4570  CB  TRP B 288     2845   2101   1963   -347    383     92       C  
ATOM   4571  CG  TRP B 288      28.021  -8.416  -4.710  1.00 22.79           C  
ANISOU 4571  CG  TRP B 288     3488   2660   2510   -272    328     55       C  
ATOM   4572  CD1 TRP B 288      27.709  -8.739  -6.006  1.00 22.55           C  
ANISOU 4572  CD1 TRP B 288     3545   2619   2404   -211    315     82       C  
ATOM   4573  CD2 TRP B 288      26.827  -8.640  -3.944  1.00 20.64           C  
ANISOU 4573  CD2 TRP B 288     3191   2373   2277   -263    271     -3       C  
ATOM   4574  NE1 TRP B 288      26.404  -9.166  -6.088  1.00 20.33           N  
ANISOU 4574  NE1 TRP B 288     3282   2318   2124   -183    220     49       N  
ATOM   4575  CE2 TRP B 288      25.842  -9.112  -4.834  1.00 17.01           C  
ANISOU 4575  CE2 TRP B 288     2774   1898   1791   -209    205      6       C  
ATOM   4576  CE3 TRP B 288      26.498  -8.486  -2.587  1.00 22.83           C  
ANISOU 4576  CE3 TRP B 288     3423   2648   2604   -300    274    -53       C  
ATOM   4577  CZ2 TRP B 288      24.548  -9.445  -4.415  1.00 22.09           C  
ANISOU 4577  CZ2 TRP B 288     3372   2529   2492   -193    140    -15       C  
ATOM   4578  CZ3 TRP B 288      25.216  -8.809  -2.173  1.00 22.64           C  
ANISOU 4578  CZ3 TRP B 288     3373   2609   2620   -265    247    -81       C  
ATOM   4579  CH2 TRP B 288      24.255  -9.295  -3.084  1.00 20.16           C  
ANISOU 4579  CH2 TRP B 288     3058   2285   2315   -213    179    -52       C  
ATOM   4580  N   GLY B 289      27.345  -5.294  -4.416  1.00 22.76           N  
ANISOU 4580  N   GLY B 289     3550   2470   2626   -327    342     75       N  
ATOM   4581  CA  GLY B 289      26.167  -4.735  -3.784  1.00 18.61           C  
ANISOU 4581  CA  GLY B 289     3034   1870   2165   -294    332     32       C  
ATOM   4582  C   GLY B 289      26.416  -3.487  -2.965  1.00 25.29           C  
ANISOU 4582  C   GLY B 289     3933   2614   3061   -355    380     -2       C  
ATOM   4583  O   GLY B 289      27.312  -2.689  -3.264  1.00 27.80           O  
ANISOU 4583  O   GLY B 289     4291   2887   3385   -424    400     37       O  
ATOM   4584  N   GLU B 290      25.629  -3.315  -1.911  1.00 21.77           N  
ANISOU 4584  N   GLU B 290     3502   2120   2649   -335    410    -74       N  
ATOM   4585  CA  GLU B 290      25.760  -2.132  -1.063  1.00 24.71           C  
ANISOU 4585  CA  GLU B 290     3978   2363   3046   -388    467   -132       C  
ATOM   4586  C   GLU B 290      26.832  -2.410  -0.018  1.00 27.63           C  
ANISOU 4586  C   GLU B 290     4370   2784   3344   -527    441   -194       C  
ATOM   4587  O   GLU B 290      26.536  -2.730   1.137  1.00 25.31           O  
ANISOU 4587  O   GLU B 290     4109   2500   3006   -542    459   -274       O  
ATOM   4588  CB  GLU B 290      24.406  -1.753  -0.430  1.00 23.60           C  
ANISOU 4588  CB  GLU B 290     3868   2131   2967   -282    546   -175       C  
ATOM   4589  CG  GLU B 290      23.294  -1.546  -1.473  1.00 27.52           C  
ANISOU 4589  CG  GLU B 290     4300   2594   3562   -144    540    -77       C  
ATOM   4590  CD  GLU B 290      21.916  -1.232  -0.880  1.00 28.55           C  
ANISOU 4590  CD  GLU B 290     4408   2643   3798    -18    634    -83       C  
ATOM   4591  OE1 GLU B 290      21.615  -1.675   0.253  1.00 32.78           O  
ANISOU 4591  OE1 GLU B 290     4946   3200   4309    -18    705   -159       O  
ATOM   4592  OE2 GLU B 290      21.120  -0.555  -1.570  1.00 28.30           O  
ANISOU 4592  OE2 GLU B 290     4348   2528   3877     89    645      8       O  
ATOM   4593  N   ASN B 291      28.089  -2.299  -0.452  1.00 33.07           N  
ANISOU 4593  N   ASN B 291     5032   3510   4025   -629    397   -138       N  
ATOM   4594  CA  ASN B 291      29.238  -2.565   0.413  1.00 24.81           C  
ANISOU 4594  CA  ASN B 291     3966   2526   2934   -775    337   -156       C  
ATOM   4595  C   ASN B 291      29.197  -3.956   1.039  1.00 22.48           C  
ANISOU 4595  C   ASN B 291     3588   2369   2582   -752    305   -174       C  
ATOM   4596  O   ASN B 291      29.548  -4.130   2.197  1.00 23.94           O  
ANISOU 4596  O   ASN B 291     3806   2581   2710   -844    260   -223       O  
ATOM   4597  CB  ASN B 291      29.329  -1.505   1.502  1.00 28.98           C  
ANISOU 4597  CB  ASN B 291     4651   2923   3437   -890    330   -247       C  
ATOM   4598  CG  ASN B 291      29.668  -0.138   0.939  1.00 40.95           C  
ANISOU 4598  CG  ASN B 291     6252   4288   5020   -952    347   -216       C  
ATOM   4599  OD1 ASN B 291      30.224  -0.029  -0.152  1.00 42.24           O  
ANISOU 4599  OD1 ASN B 291     6330   4479   5241   -953    346   -104       O  
ATOM   4600  ND2 ASN B 291      29.323   0.903   1.669  1.00 47.70           N  
ANISOU 4600  ND2 ASN B 291     7293   4969   5863   -998    378   -312       N  
ATOM   4601  N   GLY B 292      28.763  -4.937   0.250  1.00 24.19           N  
ANISOU 4601  N   GLY B 292     3719   2664   2808   -637    320   -132       N  
ATOM   4602  CA  GLY B 292      28.671  -6.310   0.700  1.00 22.18           C  
ANISOU 4602  CA  GLY B 292     3392   2519   2518   -605    297   -138       C  
ATOM   4603  C   GLY B 292      27.273  -6.798   1.064  1.00 17.60           C  
ANISOU 4603  C   GLY B 292     2826   1927   1935   -513    327   -190       C  
ATOM   4604  O   GLY B 292      27.085  -7.991   1.314  1.00 21.47           O  
ANISOU 4604  O   GLY B 292     3257   2494   2407   -484    311   -184       O  
ATOM   4605  N   TYR B 293      26.309  -5.882   1.106  1.00 24.38           N  
ANISOU 4605  N   TYR B 293     3750   2681   2830   -466    379   -225       N  
ATOM   4606  CA  TYR B 293      24.939  -6.193   1.549  1.00 23.69           C  
ANISOU 4606  CA  TYR B 293     3649   2576   2775   -377    431   -251       C  
ATOM   4607  C   TYR B 293      23.948  -6.059   0.427  1.00 23.97           C  
ANISOU 4607  C   TYR B 293     3631   2577   2898   -272    425   -192       C  
ATOM   4608  O   TYR B 293      24.217  -5.389  -0.572  1.00 28.27           O  
ANISOU 4608  O   TYR B 293     4199   3079   3462   -263    402   -147       O  
ATOM   4609  CB  TYR B 293      24.518  -5.272   2.706  1.00 27.32           C  
ANISOU 4609  CB  TYR B 293     4227   2936   3217   -386    523   -329       C  
ATOM   4610  CG  TYR B 293      25.348  -5.492   3.944  1.00 29.39           C  
ANISOU 4610  CG  TYR B 293     4568   3238   3361   -503    501   -389       C  
ATOM   4611  CD1 TYR B 293      26.642  -4.988   4.031  1.00 28.76           C  
ANISOU 4611  CD1 TYR B 293     4542   3154   3233   -637    423   -395       C  
ATOM   4612  CD2 TYR B 293      24.847  -6.219   5.020  1.00 27.33           C  
ANISOU 4612  CD2 TYR B 293     4321   3023   3039   -491    546   -421       C  
ATOM   4613  CE1 TYR B 293      27.408  -5.206   5.152  1.00 23.22           C  
ANISOU 4613  CE1 TYR B 293     3904   2497   2421   -762    362   -430       C  
ATOM   4614  CE2 TYR B 293      25.599  -6.444   6.125  1.00 25.97           C  
ANISOU 4614  CE2 TYR B 293     4235   2895   2738   -603    504   -460       C  
ATOM   4615  CZ  TYR B 293      26.886  -5.946   6.189  1.00 27.86           C  
ANISOU 4615  CZ  TYR B 293     4525   3135   2927   -742    397   -464       C  
ATOM   4616  OH  TYR B 293      27.650  -6.172   7.307  1.00 29.29           O  
ANISOU 4616  OH  TYR B 293     4786   3366   2977   -871    315   -486       O  
ATOM   4617  N   ILE B 294      22.799  -6.701   0.583  1.00 23.93           N  
ANISOU 4617  N   ILE B 294     3551   2593   2949   -203    436   -175       N  
ATOM   4618  CA  ILE B 294      21.700  -6.535  -0.368  1.00 20.01           C  
ANISOU 4618  CA  ILE B 294     2984   2064   2554   -115    404   -100       C  
ATOM   4619  C   ILE B 294      20.387  -6.428   0.394  1.00 21.82           C  
ANISOU 4619  C   ILE B 294     3145   2257   2891    -36    493    -85       C  
ATOM   4620  O   ILE B 294      20.190  -7.078   1.429  1.00 30.64           O  
ANISOU 4620  O   ILE B 294     4242   3413   3988    -51    554   -121       O  
ATOM   4621  CB  ILE B 294      21.625  -7.698  -1.395  1.00 24.48           C  
ANISOU 4621  CB  ILE B 294     3491   2709   3100   -123    277    -50       C  
ATOM   4622  CG1 ILE B 294      20.457  -7.518  -2.376  1.00 21.52           C  
ANISOU 4622  CG1 ILE B 294     3050   2307   2820    -58    197     41       C  
ATOM   4623  CG2 ILE B 294      21.496  -9.067  -0.692  1.00 20.11           C  
ANISOU 4623  CG2 ILE B 294     2881   2230   2529   -155    266    -74       C  
ATOM   4624  CD1 ILE B 294      20.517  -8.489  -3.548  1.00 18.57           C  
ANISOU 4624  CD1 ILE B 294     2690   1985   2380    -88     51     74       C  
ATOM   4625  N   ARG B 295      19.508  -5.564  -0.093  1.00 24.58           N  
ANISOU 4625  N   ARG B 295     3454   2525   3360     56    518    -18       N  
ATOM   4626  CA  ARG B 295      18.183  -5.446   0.478  1.00 29.13           C  
ANISOU 4626  CA  ARG B 295     3925   3065   4080    157    620     33       C  
ATOM   4627  C   ARG B 295      17.199  -6.180  -0.430  1.00 32.92           C  
ANISOU 4627  C   ARG B 295     4225   3605   4677    182    481    159       C  
ATOM   4628  O   ARG B 295      16.963  -5.787  -1.573  1.00 26.56           O  
ANISOU 4628  O   ARG B 295     3392   2780   3918    208    365    244       O  
ATOM   4629  CB  ARG B 295      17.814  -3.977   0.679  1.00 30.59           C  
ANISOU 4629  CB  ARG B 295     4173   3100   4348    258    759     40       C  
ATOM   4630  CG  ARG B 295      18.557  -3.338   1.866  1.00 32.63           C  
ANISOU 4630  CG  ARG B 295     4630   3279   4487    219    907   -100       C  
ATOM   4631  CD  ARG B 295      18.300  -1.843   1.994  1.00 34.36           C  
ANISOU 4631  CD  ARG B 295     4965   3312   4776    311   1046   -112       C  
ATOM   4632  NE  ARG B 295      18.744  -1.157   0.787  1.00 33.33           N  
ANISOU 4632  NE  ARG B 295     4857   3135   4673    297    933    -53       N  
ATOM   4633  CZ  ARG B 295      18.186  -0.060   0.296  1.00 29.93           C  
ANISOU 4633  CZ  ARG B 295     4434   2565   4375    411    989     23       C  
ATOM   4634  NH1 ARG B 295      17.153   0.503   0.912  1.00 30.83           N  
ANISOU 4634  NH1 ARG B 295     4529   2563   4622    563   1174     47       N  
ATOM   4635  NH2 ARG B 295      18.656   0.464  -0.825  1.00 28.59           N  
ANISOU 4635  NH2 ARG B 295     4290   2365   4206    385    876     90       N  
ATOM   4636  N   ILE B 296      16.668  -7.283   0.090  1.00 31.43           N  
ANISOU 4636  N   ILE B 296     3929   3489   4524    157    478    176       N  
ATOM   4637  CA  ILE B 296      15.754  -8.140  -0.641  1.00 26.73           C  
ANISOU 4637  CA  ILE B 296     3167   2949   4039    140    322    289       C  
ATOM   4638  C   ILE B 296      14.321  -7.747  -0.315  1.00 31.59           C  
ANISOU 4638  C   ILE B 296     3586   3531   4885    247    409    419       C  
ATOM   4639  O   ILE B 296      13.954  -7.669   0.857  1.00 31.91           O  
ANISOU 4639  O   ILE B 296     3595   3553   4977    303    613    404       O  
ATOM   4640  CB  ILE B 296      15.947  -9.634  -0.277  1.00 24.40           C  
ANISOU 4640  CB  ILE B 296     2855   2736   3681     39    265    253       C  
ATOM   4641  CG1 ILE B 296      17.402 -10.080  -0.471  1.00 25.12           C  
ANISOU 4641  CG1 ILE B 296     3119   2858   3566    -42    215    140       C  
ATOM   4642  CG2 ILE B 296      14.996 -10.496  -1.089  1.00 23.46           C  
ANISOU 4642  CG2 ILE B 296     2588   2651   3675     -7     76    366       C  
ATOM   4643  CD1 ILE B 296      17.767 -10.408  -1.907  1.00 28.06           C  
ANISOU 4643  CD1 ILE B 296     3552   3242   3867    -87     30    155       C  
ATOM   4644  N   LYS B 297      13.521  -7.501  -1.346  1.00 29.49           N  
ANISOU 4644  N   LYS B 297     3189   3258   4757    279    261    561       N  
ATOM   4645  CA  LYS B 297      12.115  -7.147  -1.167  1.00 30.26           C  
ANISOU 4645  CA  LYS B 297     3048   3332   5120    389    323    730       C  
ATOM   4646  C   LYS B 297      11.389  -8.133  -0.239  1.00 28.63           C  
ANISOU 4646  C   LYS B 297     2675   3181   5023    365    410    773       C  
ATOM   4647  O   LYS B 297      11.624  -9.349  -0.302  1.00 28.32           O  
ANISOU 4647  O   LYS B 297     2643   3213   4904    231    281    737       O  
ATOM   4648  CB  LYS B 297      11.424  -7.102  -2.529  1.00 33.82           C  
ANISOU 4648  CB  LYS B 297     3366   3801   5684    374     60    895       C  
ATOM   4649  CG  LYS B 297       9.944  -6.709  -2.487  1.00 42.19           C  
ANISOU 4649  CG  LYS B 297     4126   4844   7060    490     87   1118       C  
ATOM   4650  CD  LYS B 297       9.770  -5.255  -2.091  1.00 44.85           C  
ANISOU 4650  CD  LYS B 297     4475   5061   7503    685    327   1149       C  
ATOM   4651  CE  LYS B 297       8.319  -4.792  -2.270  1.00 53.11           C  
ANISOU 4651  CE  LYS B 297     5202   6085   8891    825    337   1409       C  
ATOM   4652  NZ  LYS B 297       7.943  -4.626  -3.707  1.00 57.50           N  
ANISOU 4652  NZ  LYS B 297     5667   6669   9510    787     10   1579       N  
ATOM   4653  N   ARG B 298      10.533  -7.617   0.643  1.00 34.39           N  
ANISOU 4653  N   ARG B 298     3268   3866   5932    502    651    853       N  
ATOM   4654  CA  ARG B 298       9.664  -8.501   1.424  1.00 37.54           C  
ANISOU 4654  CA  ARG B 298     3465   4321   6478    489    744    946       C  
ATOM   4655  C   ARG B 298       8.209  -8.074   1.288  1.00 40.48           C  
ANISOU 4655  C   ARG B 298     3517   4675   7188    615    798   1186       C  
ATOM   4656  O   ARG B 298       7.924  -7.007   0.764  1.00 34.98           O  
ANISOU 4656  O   ARG B 298     2782   3910   6598    738    804   1263       O  
ATOM   4657  CB  ARG B 298      10.079  -8.534   2.902  1.00 35.45           C  
ANISOU 4657  CB  ARG B 298     3349   4036   6083    527   1044    816       C  
ATOM   4658  CG  ARG B 298       9.640  -7.358   3.746  1.00 37.80           C  
ANISOU 4658  CG  ARG B 298     3672   4229   6461    723   1375    824       C  
ATOM   4659  CD  ARG B 298       9.944  -7.632   5.208  1.00 37.95           C  
ANISOU 4659  CD  ARG B 298     3851   4245   6323    729   1641    708       C  
ATOM   4660  NE  ARG B 298       9.535  -6.535   6.085  1.00 45.15           N  
ANISOU 4660  NE  ARG B 298     4846   5035   7274    919   1988    692       N  
ATOM   4661  CZ  ARG B 298       8.319  -6.396   6.614  1.00 51.18           C  
ANISOU 4661  CZ  ARG B 298     5402   5773   8272   1074   2242    851       C  
ATOM   4662  NH1 ARG B 298       7.360  -7.280   6.358  1.00 47.96           N  
ANISOU 4662  NH1 ARG B 298     4657   5463   8104   1044   2164   1055       N  
ATOM   4663  NH2 ARG B 298       8.056  -5.358   7.396  1.00 52.32           N  
ANISOU 4663  NH2 ARG B 298     5679   5781   8419   1261   2583    811       N  
ATOM   4664  N   GLY B 299       7.298  -8.928   1.741  1.00 39.09           N  
ANISOU 4664  N   GLY B 299     3096   4560   7196    583    832   1323       N  
ATOM   4665  CA  GLY B 299       5.876  -8.636   1.700  1.00 44.52           C  
ANISOU 4665  CA  GLY B 299     3424   5246   8246    698    896   1586       C  
ATOM   4666  C   GLY B 299       5.214  -8.849   0.350  1.00 46.80           C  
ANISOU 4666  C   GLY B 299     3485   5582   8716    609    521   1779       C  
ATOM   4667  O   GLY B 299       4.087  -8.418   0.144  1.00 53.87           O  
ANISOU 4667  O   GLY B 299     4065   6474   9929    714    531   2024       O  
ATOM   4668  N   THR B 300       5.902  -9.520  -0.569  1.00 48.21           N  
ANISOU 4668  N   THR B 300     3824   5802   8690    417    189   1679       N  
ATOM   4669  CA  THR B 300       5.350  -9.779  -1.897  1.00 53.01           C  
ANISOU 4669  CA  THR B 300     4285   6451   9406    301   -203   1839       C  
ATOM   4670  C   THR B 300       4.235 -10.814  -1.857  1.00 65.18           C  
ANISOU 4670  C   THR B 300     5499   8059  11207    172   -349   2042       C  
ATOM   4671  O   THR B 300       3.602 -11.089  -2.873  1.00 67.40           O  
ANISOU 4671  O   THR B 300     5637   8373  11600     52   -693   2199       O  
ATOM   4672  CB  THR B 300       6.418 -10.288  -2.877  1.00 48.18           C  
ANISOU 4672  CB  THR B 300     3985   5851   8470    130   -491   1660       C  
ATOM   4673  OG1 THR B 300       6.858 -11.586  -2.463  1.00 43.88           O  
ANISOU 4673  OG1 THR B 300     3544   5339   7790    -30   -518   1533       O  
ATOM   4674  CG2 THR B 300       7.604  -9.338  -2.936  1.00 47.52           C  
ANISOU 4674  CG2 THR B 300     4213   5708   8136    229   -356   1470       C  
ATOM   4675  N   GLY B 301       4.019 -11.406  -0.687  1.00 72.41           N  
ANISOU 4675  N   GLY B 301     6329   8989  12193    178    -98   2036       N  
ATOM   4676  CA  GLY B 301       2.991 -12.414  -0.523  1.00 74.50           C  
ANISOU 4676  CA  GLY B 301     6388   9288  12630     42   -191   2192       C  
ATOM   4677  C   GLY B 301       3.448 -13.806  -0.915  1.00 73.64           C  
ANISOU 4677  C   GLY B 301     6389   9208  12382   -217   -473   2099       C  
ATOM   4678  O   GLY B 301       2.810 -14.792  -0.552  1.00 77.99           O  
ANISOU 4678  O   GLY B 301     6857   9764  13013   -333   -499   2171       O  
ATOM   4679  N   ASN B 302       4.549 -13.889  -1.658  1.00 70.91           N  
ANISOU 4679  N   ASN B 302     6329   8852  11763   -296   -665   1909       N  
ATOM   4680  CA  ASN B 302       5.087 -15.177  -2.091  1.00 70.00           C  
ANISOU 4680  CA  ASN B 302     6413   8727  11456   -525   -910   1781       C  
ATOM   4681  C   ASN B 302       5.665 -15.960  -0.916  1.00 60.05           C  
ANISOU 4681  C   ASN B 302     5273   7459  10083   -540   -660   1646       C  
ATOM   4682  O   ASN B 302       6.495 -15.436  -0.163  1.00 55.91           O  
ANISOU 4682  O   ASN B 302     4930   6926   9386   -400   -380   1494       O  
ATOM   4683  CB  ASN B 302       6.155 -14.975  -3.164  1.00 75.20           C  
ANISOU 4683  CB  ASN B 302     7423   9357  11792   -562  -1107   1593       C  
ATOM   4684  CG  ASN B 302       6.755 -16.280  -3.639  1.00 77.60           C  
ANISOU 4684  CG  ASN B 302     7969   9628  11887   -769  -1324   1449       C  
ATOM   4685  OD1 ASN B 302       6.148 -17.344  -3.500  1.00 80.13           O  
ANISOU 4685  OD1 ASN B 302     8168   9939  12338   -931  -1447   1529       O  
ATOM   4686  ND2 ASN B 302       7.955 -16.207  -4.201  1.00 76.48           N  
ANISOU 4686  ND2 ASN B 302     8173   9456  11429   -762  -1356   1245       N  
ATOM   4687  N   SER B 303       5.242 -17.217  -0.775  1.00 47.89           N  
ANISOU 4687  N   SER B 303     3644   5915   8637   -723   -782   1708       N  
ATOM   4688  CA  SER B 303       5.563 -18.000   0.419  1.00 47.97           C  
ANISOU 4688  CA  SER B 303     3708   5919   8598   -736   -541   1644       C  
ATOM   4689  C   SER B 303       7.014 -18.483   0.452  1.00 44.03           C  
ANISOU 4689  C   SER B 303     3602   5384   7745   -764   -531   1380       C  
ATOM   4690  O   SER B 303       7.559 -18.722   1.526  1.00 44.23           O  
ANISOU 4690  O   SER B 303     3725   5414   7668   -708   -280   1300       O  
ATOM   4691  CB  SER B 303       4.622 -19.203   0.547  1.00 56.96           C  
ANISOU 4691  CB  SER B 303     4695   7041   9905   -899   -662   1782       C  
ATOM   4692  OG  SER B 303       4.773 -20.095  -0.542  1.00 61.58           O  
ANISOU 4692  OG  SER B 303     5443   7570  10383  -1103  -1031   1719       O  
ATOM   4693  N   TYR B 304       7.638 -18.632  -0.714  1.00 36.63           N  
ANISOU 4693  N   TYR B 304     2887   4410   6622   -846   -796   1261       N  
ATOM   4694  CA  TYR B 304       9.056 -19.005  -0.765  1.00 38.06           C  
ANISOU 4694  CA  TYR B 304     3418   4555   6488   -845   -766   1031       C  
ATOM   4695  C   TYR B 304       9.967 -17.858  -0.330  1.00 34.83           C  
ANISOU 4695  C   TYR B 304     3142   4177   5915   -657   -528    912       C  
ATOM   4696  O   TYR B 304      11.137 -18.064   0.038  1.00 33.85           O  
ANISOU 4696  O   TYR B 304     3244   4044   5573   -629   -423    754       O  
ATOM   4697  CB  TYR B 304       9.449 -19.443  -2.176  1.00 47.56           C  
ANISOU 4697  CB  TYR B 304     4837   5702   7532   -969  -1083    943       C  
ATOM   4698  CG  TYR B 304       8.773 -20.704  -2.685  1.00 53.46           C  
ANISOU 4698  CG  TYR B 304     5554   6383   8374  -1191  -1355   1009       C  
ATOM   4699  CD1 TYR B 304       9.311 -21.959  -2.425  1.00 49.08           C  
ANISOU 4699  CD1 TYR B 304     5178   5749   7720  -1291  -1356    909       C  
ATOM   4700  CD2 TYR B 304       7.620 -20.635  -3.457  1.00 56.61           C  
ANISOU 4700  CD2 TYR B 304     5757   6787   8964  -1309  -1630   1177       C  
ATOM   4701  CE1 TYR B 304       8.700 -23.114  -2.901  1.00 47.47           C  
ANISOU 4701  CE1 TYR B 304     4980   5455   7601  -1509  -1612    959       C  
ATOM   4702  CE2 TYR B 304       7.005 -21.784  -3.939  1.00 56.00           C  
ANISOU 4702  CE2 TYR B 304     5700   6638   8938  -1514  -1883   1223       C  
ATOM   4703  CZ  TYR B 304       7.551 -23.018  -3.657  1.00 52.99           C  
ANISOU 4703  CZ  TYR B 304     5525   6166   8444  -1607  -1861   1101       C  
ATOM   4704  OH  TYR B 304       6.945 -24.160  -4.133  1.00 57.48           O  
ANISOU 4704  OH  TYR B 304     6174   6651   9014  -1758  -2056   1122       O  
ATOM   4705  N   GLY B 305       9.441 -16.641  -0.393  1.00 34.04           N  
ANISOU 4705  N   GLY B 305     2900   4104   5930   -534   -455    998       N  
ATOM   4706  CA  GLY B 305      10.278 -15.453  -0.299  1.00 30.75           C  
ANISOU 4706  CA  GLY B 305     2638   3688   5359   -384   -298    885       C  
ATOM   4707  C   GLY B 305      10.910 -15.138  -1.646  1.00 33.53           C  
ANISOU 4707  C   GLY B 305     3175   4019   5546   -413   -517    808       C  
ATOM   4708  O   GLY B 305      11.022 -16.009  -2.513  1.00 36.87           O  
ANISOU 4708  O   GLY B 305     3696   4421   5893   -548   -755    782       O  
ATOM   4709  N   VAL B 306      11.300 -13.884  -1.837  1.00 33.72           N  
ANISOU 4709  N   VAL B 306     3265   4035   5512   -289   -430    775       N  
ATOM   4710  CA  VAL B 306      12.004 -13.497  -3.047  1.00 33.45           C  
ANISOU 4710  CA  VAL B 306     3424   3982   5302   -304   -592    707       C  
ATOM   4711  C   VAL B 306      13.356 -14.203  -3.063  1.00 32.63           C  
ANISOU 4711  C   VAL B 306     3580   3872   4947   -358   -573    530       C  
ATOM   4712  O   VAL B 306      14.052 -14.230  -2.051  1.00 25.53           O  
ANISOU 4712  O   VAL B 306     2737   2982   3981   -316   -373    443       O  
ATOM   4713  CB  VAL B 306      12.200 -11.974  -3.136  1.00 30.56           C  
ANISOU 4713  CB  VAL B 306     3079   3595   4937   -158   -472    717       C  
ATOM   4714  CG1 VAL B 306      13.052 -11.615  -4.344  1.00 31.94           C  
ANISOU 4714  CG1 VAL B 306     3473   3753   4909   -178   -612    650       C  
ATOM   4715  CG2 VAL B 306      10.860 -11.263  -3.198  1.00 33.06           C  
ANISOU 4715  CG2 VAL B 306     3131   3907   5525    -78   -484    915       C  
ATOM   4716  N   CYS B 307      13.702 -14.791  -4.206  1.00 30.06           N  
ANISOU 4716  N   CYS B 307     3414   3525   4482   -448   -782    487       N  
ATOM   4717  CA  CYS B 307      14.916 -15.594  -4.357  1.00 30.42           C  
ANISOU 4717  CA  CYS B 307     3694   3550   4313   -488   -764    340       C  
ATOM   4718  C   CYS B 307      14.901 -16.821  -3.432  1.00 30.30           C  
ANISOU 4718  C   CYS B 307     3645   3527   4342   -551   -704    315       C  
ATOM   4719  O   CYS B 307      15.947 -17.389  -3.132  1.00 29.30           O  
ANISOU 4719  O   CYS B 307     3663   3389   4081   -545   -616    212       O  
ATOM   4720  CB  CYS B 307      16.175 -14.750  -4.095  1.00 30.29           C  
ANISOU 4720  CB  CYS B 307     3804   3548   4157   -388   -578    246       C  
ATOM   4721  SG  CYS B 307      16.356 -13.281  -5.163  1.00 38.04           S  
ANISOU 4721  SG  CYS B 307     4854   4521   5077   -315   -619    279       S  
ATOM   4722  N   GLY B 308      13.710 -17.232  -2.994  1.00 30.83           N  
ANISOU 4722  N   GLY B 308     3503   3598   4611   -609   -752    431       N  
ATOM   4723  CA  GLY B 308      13.568 -18.405  -2.145  1.00 24.35           C  
ANISOU 4723  CA  GLY B 308     2639   2761   3851   -680   -703    435       C  
ATOM   4724  C   GLY B 308      14.036 -18.165  -0.720  1.00 24.99           C  
ANISOU 4724  C   GLY B 308     2684   2886   3926   -588   -432    408       C  
ATOM   4725  O   GLY B 308      14.369 -19.107  -0.009  1.00 31.27           O  
ANISOU 4725  O   GLY B 308     3517   3669   4694   -627   -366    383       O  
ATOM   4726  N   LEU B 309      14.022 -16.898  -0.302  1.00 30.46           N  
ANISOU 4726  N   LEU B 309     3317   3617   4640   -472   -282    420       N  
ATOM   4727  CA  LEU B 309      14.617 -16.443   0.961  1.00 26.58           C  
ANISOU 4727  CA  LEU B 309     2860   3156   4082   -388    -39    366       C  
ATOM   4728  C   LEU B 309      14.064 -17.092   2.227  1.00 27.30           C  
ANISOU 4728  C   LEU B 309     2840   3267   4266   -403    105    432       C  
ATOM   4729  O   LEU B 309      14.720 -17.083   3.267  1.00 30.12           O  
ANISOU 4729  O   LEU B 309     3284   3648   4514   -370    266    376       O  
ATOM   4730  CB  LEU B 309      14.458 -14.918   1.081  1.00 29.31           C  
ANISOU 4730  CB  LEU B 309     3173   3506   4459   -270     81    374       C  
ATOM   4731  CG  LEU B 309      15.236 -14.244   2.215  1.00 25.73           C  
ANISOU 4731  CG  LEU B 309     2828   3063   3885   -200    300    287       C  
ATOM   4732  CD1 LEU B 309      16.730 -14.504   2.072  1.00 23.98           C  
ANISOU 4732  CD1 LEU B 309     2801   2853   3457   -239    257    167       C  
ATOM   4733  CD2 LEU B 309      14.959 -12.731   2.291  1.00 25.30           C  
ANISOU 4733  CD2 LEU B 309     2763   2974   3877    -87    420    293       C  
ATOM   4734  N   TYR B 310      12.868 -17.660   2.161  1.00 26.40           N  
ANISOU 4734  N   TYR B 310     2535   3145   4352   -464     41    564       N  
ATOM   4735  CA  TYR B 310      12.275 -18.243   3.370  1.00 31.73           C  
ANISOU 4735  CA  TYR B 310     3089   3838   5128   -476    205    653       C  
ATOM   4736  C   TYR B 310      12.419 -19.761   3.420  1.00 32.62           C  
ANISOU 4736  C   TYR B 310     3243   3919   5233   -608    100    662       C  
ATOM   4737  O   TYR B 310      11.728 -20.419   4.191  1.00 33.17           O  
ANISOU 4737  O   TYR B 310     3183   3991   5428   -652    187    773       O  
ATOM   4738  CB  TYR B 310      10.785 -17.857   3.484  1.00 35.94           C  
ANISOU 4738  CB  TYR B 310     3337   4384   5934   -447    260    833       C  
ATOM   4739  CG  TYR B 310      10.549 -16.363   3.389  1.00 38.49           C  
ANISOU 4739  CG  TYR B 310     3615   4712   6297   -298    372    842       C  
ATOM   4740  CD1 TYR B 310      11.554 -15.462   3.738  1.00 35.32           C  
ANISOU 4740  CD1 TYR B 310     3423   4306   5692   -201    505    694       C  
ATOM   4741  CD2 TYR B 310       9.331 -15.851   2.952  1.00 37.85           C  
ANISOU 4741  CD2 TYR B 310     3277   4631   6472   -258    338   1009       C  
ATOM   4742  CE1 TYR B 310      11.359 -14.106   3.649  1.00 38.18           C  
ANISOU 4742  CE1 TYR B 310     3772   4644   6092    -70    611    697       C  
ATOM   4743  CE2 TYR B 310       9.129 -14.492   2.857  1.00 36.76           C  
ANISOU 4743  CE2 TYR B 310     3107   4477   6382   -104    452   1026       C  
ATOM   4744  CZ  TYR B 310      10.149 -13.620   3.208  1.00 39.97           C  
ANISOU 4744  CZ  TYR B 310     3755   4859   6571    -10    595    860       C  
ATOM   4745  OH  TYR B 310       9.967 -12.256   3.119  1.00 36.63           O  
ANISOU 4745  OH  TYR B 310     3328   4393   6198    139    714    870       O  
ATOM   4746  N   THR B 311      13.331 -20.316   2.624  1.00 29.81           N  
ANISOU 4746  N   THR B 311     3076   3519   4730   -663    -62    552       N  
ATOM   4747  CA  THR B 311      13.369 -21.763   2.422  1.00 31.21           C  
ANISOU 4747  CA  THR B 311     3311   3627   4921   -790   -189    560       C  
ATOM   4748  C   THR B 311      13.964 -22.528   3.602  1.00 34.65           C  
ANISOU 4748  C   THR B 311     3816   4065   5285   -782    -35    556       C  
ATOM   4749  O   THR B 311      13.423 -23.542   4.021  1.00 31.94           O  
ANISOU 4749  O   THR B 311     3405   3680   5052   -872    -41    646       O  
ATOM   4750  CB  THR B 311      14.170 -22.143   1.144  1.00 27.64           C  
ANISOU 4750  CB  THR B 311     3074   3105   4324   -830   -383    439       C  
ATOM   4751  OG1 THR B 311      13.536 -21.583  -0.011  1.00 28.48           O  
ANISOU 4751  OG1 THR B 311     3136   3202   4482   -863   -564    462       O  
ATOM   4752  CG2 THR B 311      14.232 -23.668   0.984  1.00 25.06           C  
ANISOU 4752  CG2 THR B 311     2847   2670   4006   -951   -491    434       C  
ATOM   4753  N   SER B 312      15.082 -22.053   4.132  1.00 30.95           N  
ANISOU 4753  N   SER B 312     3481   3643   4636   -687     88    465       N  
ATOM   4754  CA  SER B 312      15.764 -22.803   5.178  1.00 28.52           C  
ANISOU 4754  CA  SER B 312     3255   3342   4239   -683    195    471       C  
ATOM   4755  C   SER B 312      16.551 -21.892   6.106  1.00 30.20           C  
ANISOU 4755  C   SER B 312     3539   3640   4295   -587    356    421       C  
ATOM   4756  O   SER B 312      17.695 -21.519   5.799  1.00 26.83           O  
ANISOU 4756  O   SER B 312     3239   3229   3727   -544    322    325       O  
ATOM   4757  CB  SER B 312      16.688 -23.846   4.548  1.00 26.61           C  
ANISOU 4757  CB  SER B 312     3175   3019   3919   -719     72    407       C  
ATOM   4758  OG  SER B 312      17.259 -24.661   5.546  1.00 32.09           O  
ANISOU 4758  OG  SER B 312     3925   3710   4559   -715    159    447       O  
ATOM   4759  N   SER B 313      15.957 -21.549   7.249  1.00 26.24           N  
ANISOU 4759  N   SER B 313     2968   3188   3813   -559    533    490       N  
ATOM   4760  CA  SER B 313      16.535 -20.518   8.117  1.00 29.93           C  
ANISOU 4760  CA  SER B 313     3533   3721   4120   -481    678    430       C  
ATOM   4761  C   SER B 313      16.876 -21.036   9.512  1.00 31.30           C  
ANISOU 4761  C   SER B 313     3788   3934   4171   -490    802    476       C  
ATOM   4762  O   SER B 313      16.032 -21.603  10.184  1.00 29.32           O  
ANISOU 4762  O   SER B 313     3457   3681   4001   -513    909    588       O  
ATOM   4763  CB  SER B 313      15.571 -19.330   8.230  1.00 29.27           C  
ANISOU 4763  CB  SER B 313     3352   3647   4120   -411    809    447       C  
ATOM   4764  OG  SER B 313      15.308 -18.760   6.955  1.00 28.54           O  
ANISOU 4764  OG  SER B 313     3193   3525   4128   -398    680    418       O  
ATOM   4765  N   PHE B 314      18.111 -20.825   9.956  1.00 25.50           N  
ANISOU 4765  N   PHE B 314     3208   3238   3242   -479    784    408       N  
ATOM   4766  CA  PHE B 314      18.531 -21.350  11.253  1.00 26.73           C  
ANISOU 4766  CA  PHE B 314     3462   3439   3257   -498    861    465       C  
ATOM   4767  C   PHE B 314      19.277 -20.281  12.035  1.00 29.20           C  
ANISOU 4767  C   PHE B 314     3931   3809   3353   -475    917    384       C  
ATOM   4768  O   PHE B 314      19.849 -19.368  11.443  1.00 26.72           O  
ANISOU 4768  O   PHE B 314     3656   3494   3004   -458    850    282       O  
ATOM   4769  CB  PHE B 314      19.440 -22.577  11.097  1.00 30.06           C  
ANISOU 4769  CB  PHE B 314     3918   3841   3661   -536    726    506       C  
ATOM   4770  CG  PHE B 314      18.757 -23.795  10.531  1.00 27.16           C  
ANISOU 4770  CG  PHE B 314     3452   3390   3479   -581    673    585       C  
ATOM   4771  CD1 PHE B 314      18.557 -23.925   9.169  1.00 28.13           C  
ANISOU 4771  CD1 PHE B 314     3518   3440   3729   -594    547    534       C  
ATOM   4772  CD2 PHE B 314      18.357 -24.836  11.366  1.00 29.79           C  
ANISOU 4772  CD2 PHE B 314     3773   3705   3842   -622    738    714       C  
ATOM   4773  CE1 PHE B 314      17.938 -25.064   8.650  1.00 27.19           C  
ANISOU 4773  CE1 PHE B 314     3343   3223   3765   -662    472    597       C  
ATOM   4774  CE2 PHE B 314      17.744 -25.971  10.853  1.00 27.63           C  
ANISOU 4774  CE2 PHE B 314     3421   3331   3746   -686    676    788       C  
ATOM   4775  CZ  PHE B 314      17.537 -26.081   9.500  1.00 29.42           C  
ANISOU 4775  CZ  PHE B 314     3604   3478   4098   -712    535    722       C  
ATOM   4776  N   TYR B 315      19.287 -20.402  13.359  1.00 27.68           N  
ANISOU 4776  N   TYR B 315     3849   3660   3007   -488   1032    431       N  
ATOM   4777  CA  TYR B 315      20.109 -19.516  14.172  1.00 30.85           C  
ANISOU 4777  CA  TYR B 315     4445   4109   3168   -499   1043    353       C  
ATOM   4778  C   TYR B 315      20.667 -20.215  15.407  1.00 31.46           C  
ANISOU 4778  C   TYR B 315     4654   4245   3053   -550   1037    436       C  
ATOM   4779  O   TYR B 315      20.094 -21.196  15.894  1.00 32.07           O  
ANISOU 4779  O   TYR B 315     4691   4324   3171   -555   1115    559       O  
ATOM   4780  CB  TYR B 315      19.314 -18.264  14.568  1.00 25.02           C  
ANISOU 4780  CB  TYR B 315     3780   3344   2383   -444   1238    279       C  
ATOM   4781  CG  TYR B 315      18.054 -18.525  15.334  1.00 26.77           C  
ANISOU 4781  CG  TYR B 315     3971   3557   2644   -399   1479    370       C  
ATOM   4782  CD1 TYR B 315      18.072 -18.602  16.729  1.00 35.04           C  
ANISOU 4782  CD1 TYR B 315     5211   4641   3462   -412   1622    402       C  
ATOM   4783  CD2 TYR B 315      16.841 -18.693  14.683  1.00 32.05           C  
ANISOU 4783  CD2 TYR B 315     4419   4185   3575   -348   1565    441       C  
ATOM   4784  CE1 TYR B 315      16.922 -18.841  17.452  1.00 39.78           C  
ANISOU 4784  CE1 TYR B 315     5785   5234   4094   -361   1881    501       C  
ATOM   4785  CE2 TYR B 315      15.668 -18.942  15.413  1.00 39.82           C  
ANISOU 4785  CE2 TYR B 315     5340   5166   4625   -306   1808    555       C  
ATOM   4786  CZ  TYR B 315      15.723 -19.006  16.796  1.00 39.43           C  
ANISOU 4786  CZ  TYR B 315     5486   5150   4344   -304   1984    584       C  
ATOM   4787  OH  TYR B 315      14.588 -19.250  17.543  1.00 38.03           O  
ANISOU 4787  OH  TYR B 315     5247   4973   4229   -251   2235    703       O  
ATOM   4788  N   PRO B 316      21.807 -19.712  15.908  1.00 30.69           N  
ANISOU 4788  N   PRO B 316     4714   4198   2749   -600    928    385       N  
ATOM   4789  CA  PRO B 316      22.455 -20.279  17.089  1.00 26.64           C  
ANISOU 4789  CA  PRO B 316     4343   3753   2027   -660    877    473       C  
ATOM   4790  C   PRO B 316      21.781 -19.839  18.385  1.00 36.51           C  
ANISOU 4790  C   PRO B 316     5798   5016   3057   -664   1078    467       C  
ATOM   4791  O   PRO B 316      21.262 -18.729  18.462  1.00 34.52           O  
ANISOU 4791  O   PRO B 316     5638   4723   2754   -630   1218    351       O  
ATOM   4792  CB  PRO B 316      23.871 -19.721  17.005  1.00 34.62           C  
ANISOU 4792  CB  PRO B 316     5422   4809   2925   -725    664    419       C  
ATOM   4793  CG  PRO B 316      23.695 -18.393  16.301  1.00 28.05           C  
ANISOU 4793  CG  PRO B 316     4597   3923   2136   -705    701    262       C  
ATOM   4794  CD  PRO B 316      22.621 -18.641  15.290  1.00 27.71           C  
ANISOU 4794  CD  PRO B 316     4369   3815   2344   -617    810    261       C  
ATOM   4795  N   VAL B 317      21.793 -20.706  19.389  1.00 33.40           N  
ANISOU 4795  N   VAL B 317     5490   4670   2532   -695   1105    598       N  
ATOM   4796  CA  VAL B 317      21.324 -20.347  20.711  1.00 38.00           C  
ANISOU 4796  CA  VAL B 317     6304   5273   2863   -697   1281    597       C  
ATOM   4797  C   VAL B 317      22.526 -20.203  21.645  1.00 46.61           C  
ANISOU 4797  C   VAL B 317     7586   6432   3691   -778   1068    592       C  
ATOM   4798  O   VAL B 317      23.461 -21.007  21.602  1.00 46.92           O  
ANISOU 4798  O   VAL B 317     7583   6527   3717   -841    863    708       O  
ATOM   4799  CB  VAL B 317      20.327 -21.398  21.262  1.00 40.56           C  
ANISOU 4799  CB  VAL B 317     6546   5598   3267   -651   1458    757       C  
ATOM   4800  CG1 VAL B 317      20.036 -21.156  22.744  1.00 41.34           C  
ANISOU 4800  CG1 VAL B 317     6837   5735   3134   -627   1565    759       C  
ATOM   4801  CG2 VAL B 317      19.040 -21.378  20.454  1.00 37.28           C  
ANISOU 4801  CG2 VAL B 317     5922   5112   3133   -577   1659    764       C  
ATOM   4802  N   LYS B 318      22.511 -19.164  22.472  1.00 44.62           N  
ANISOU 4802  N   LYS B 318     7539   6165   3248   -778   1107    466       N  
ATOM   4803  CA  LYS B 318      23.570 -18.952  23.447  1.00 46.24           C  
ANISOU 4803  CA  LYS B 318     7939   6423   3205   -873    900    457       C  
ATOM   4804  C   LYS B 318      22.984 -18.488  24.779  1.00 53.14           C  
ANISOU 4804  C   LYS B 318     9047   7280   3865   -844   1058    404       C  
ATOM   4805  O   LYS B 318      22.471 -17.377  24.891  1.00 55.49           O  
ANISOU 4805  O   LYS B 318     9464   7495   4127   -804   1200    250       O  
ATOM   4806  CB  LYS B 318      24.583 -17.938  22.918  1.00 42.91           C  
ANISOU 4806  CB  LYS B 318     7559   5983   2763   -961    691    327       C  
ATOM   4807  CG  LYS B 318      25.722 -17.616  23.878  1.00 42.76           C  
ANISOU 4807  CG  LYS B 318     7720   6008   2520  -1086    447    320       C  
ATOM   4808  CD  LYS B 318      26.535 -18.850  24.213  1.00 49.72           C  
ANISOU 4808  CD  LYS B 318     8515   6996   3381  -1134    246    522       C  
ATOM   4809  CE  LYS B 318      27.864 -18.481  24.850  1.00 51.49           C  
ANISOU 4809  CE  LYS B 318     8841   7269   3454  -1278    -59    532       C  
ATOM   4810  NZ  LYS B 318      28.489 -19.629  25.564  1.00 53.14           N  
ANISOU 4810  NZ  LYS B 318     9016   7574   3600  -1304   -220    739       N  
ATOM   4811  N   ASN B 319      23.061 -19.346  25.789  1.00 52.13           N  
ANISOU 4811  N   ASN B 319     8990   7221   3594   -858   1041    541       N  
ATOM   4812  CA  ASN B 319      22.523 -19.022  27.104  1.00 52.04           C  
ANISOU 4812  CA  ASN B 319     9213   7205   3356   -835   1197    508       C  
ATOM   4813  C   ASN B 319      23.284 -17.909  27.814  1.00 56.36           C  
ANISOU 4813  C   ASN B 319    10039   7719   3657   -930   1051    356       C  
ATOM   4814  O   ASN B 319      23.042 -17.622  28.994  1.00 61.52           O  
ANISOU 4814  O   ASN B 319    10938   8363   4074   -935   1138    323       O  
ATOM   4815  CB  ASN B 319      22.505 -20.273  27.980  1.00 57.12           C  
ANISOU 4815  CB  ASN B 319     9864   7939   3902   -837   1193    711       C  
ATOM   4816  CG  ASN B 319      21.505 -21.291  27.504  1.00 56.97           C  
ANISOU 4816  CG  ASN B 319     9608   7922   4115   -752   1393    859       C  
ATOM   4817  OD1 ASN B 319      20.456 -20.934  26.971  1.00 59.56           O  
ANISOU 4817  OD1 ASN B 319     9826   8186   4616   -673   1620    801       O  
ATOM   4818  ND2 ASN B 319      21.820 -22.567  27.688  1.00 58.16           N  
ANISOU 4818  ND2 ASN B 319     9672   8134   4294   -773   1300   1062       N  
ATOM   4819  OXT ASN B 319      24.160 -17.275  27.233  1.00 57.08           O  
ANISOU 4819  OXT ASN B 319    10121   7786   3781  -1014    842    269       O  
TER    4820      ASN B 319                                                      
HETATM 4821 CL    CL A 401     -14.141   1.608  54.079  1.00 74.87          CL  
HETATM 4822 NA    NA A 402     -13.979  -0.076  55.887  1.00 52.19          NA  
HETATM 4823 CL    CL B 401      38.321 -12.327 -12.296  1.00 69.32          CL  
HETATM 4824 NA    NA B 402      39.856 -18.587 -18.723  1.00 60.56          NA  
HETATM 4825  O   HOH A 501      -3.450   4.494  51.355  1.00 21.62           O  
HETATM 4826  O   HOH A 502       8.281  -2.673  52.892  1.00 25.19           O  
HETATM 4827  O   HOH A 503       7.027  14.354  69.363  1.00 27.72           O  
HETATM 4828  O   HOH A 504       3.016  -5.233  63.807  1.00 17.12           O  
HETATM 4829  O   HOH A 505      -4.119   4.824  47.090  1.00 21.31           O  
HETATM 4830  O   HOH A 506      22.809   1.659  52.079  1.00 31.24           O  
HETATM 4831  O   HOH A 507       8.912  14.884  62.769  1.00 20.42           O  
HETATM 4832  O   HOH A 508      17.772  -2.379  51.802  1.00 21.10           O  
HETATM 4833  O   HOH A 509      12.078   8.381  48.487  1.00 20.54           O  
HETATM 4834  O   HOH A 510       0.178 -11.981  70.755  1.00 35.69           O  
HETATM 4835  O   HOH A 511       3.747   1.077  60.332  1.00 24.57           O  
HETATM 4836  O   HOH A 512       9.322   0.026  47.950  1.00 19.08           O  
HETATM 4837  O   HOH A 513      -2.867   7.369  46.745  1.00 26.36           O  
HETATM 4838  O   HOH A 514      -5.225   3.725  45.012  1.00 25.95           O  
HETATM 4839  O   HOH A 515       2.229 -13.024  58.422  1.00 20.53           O  
HETATM 4840  O   HOH A 516      15.890   4.247  63.959  1.00 22.31           O  
HETATM 4841  O   HOH A 517       9.392  -5.773  66.528  1.00 23.45           O  
HETATM 4842  O   HOH A 518     -13.671  -4.850  75.367  1.00 32.23           O  
HETATM 4843  O   HOH A 519       0.264   9.478  53.014  1.00 23.41           O  
HETATM 4844  O   HOH A 520      11.290 -11.308  58.594  1.00 44.49           O  
HETATM 4845  O   HOH A 521      19.254   7.476  68.299  1.00 24.71           O  
HETATM 4846  O   HOH A 522      21.799   5.314  47.848  1.00 34.42           O  
HETATM 4847  O   HOH A 523      -9.186 -17.005  57.543  1.00 27.32           O  
HETATM 4848  O   HOH A 524       1.142   6.885  52.508  1.00 18.99           O  
HETATM 4849  O   HOH A 525      13.459  17.135  66.226  1.00 26.72           O  
HETATM 4850  O   HOH A 526      10.750  -8.817  64.527  1.00 27.64           O  
HETATM 4851  O   HOH A 527       7.274  -3.412  61.107  1.00 15.96           O  
HETATM 4852  O   HOH A 528      14.365 -14.517  51.316  1.00 62.93           O  
HETATM 4853  O   HOH A 529       7.638  -1.289  59.301  1.00 18.59           O  
HETATM 4854  O   HOH A 530     -10.419   8.321  53.698  1.00 25.53           O  
HETATM 4855  O   HOH A 531     -12.798  -3.344  44.631  1.00 53.61           O  
HETATM 4856  O   HOH A 532      26.857   6.727  57.683  1.00 26.84           O  
HETATM 4857  O   HOH A 533      17.709 -10.403  52.209  1.00 41.14           O  
HETATM 4858  O   HOH A 534       7.005 -11.435  61.360  1.00 22.14           O  
HETATM 4859  O   HOH A 535       4.040  -7.098  69.474  1.00 20.37           O  
HETATM 4860  O   HOH A 536      -4.631 -11.560  42.778  1.00 37.71           O  
HETATM 4861  O   HOH A 537       8.595  17.953  64.249  1.00 28.11           O  
HETATM 4862  O   HOH A 538     -11.725  -2.882  77.517  1.00 45.69           O  
HETATM 4863  O   HOH A 539      10.210  16.615  53.206  1.00 31.23           O  
HETATM 4864  O   HOH A 540     -10.402  -2.466  74.082  1.00 55.89           O  
HETATM 4865  O   HOH A 541     -10.097   0.475  62.801  1.00 23.35           O  
HETATM 4866  O   HOH A 542      -7.328  11.001  61.553  1.00 44.06           O  
HETATM 4867  O   HOH A 543      11.493  -3.544  55.098  1.00 19.91           O  
HETATM 4868  O   HOH A 544       8.042  -7.792  68.133  1.00 20.70           O  
HETATM 4869  O   HOH A 545     -14.686  -0.920  74.412  1.00 41.15           O  
HETATM 4870  O   HOH A 546     -14.021   0.369  68.160  1.00 32.56           O  
HETATM 4871  O   HOH A 547       0.245 -12.491  49.570  1.00 32.34           O  
HETATM 4872  O   HOH A 548      10.183  -9.428  67.545  1.00 44.42           O  
HETATM 4873  O   HOH A 549      20.473   8.901  44.631  1.00 50.42           O  
HETATM 4874  O   HOH A 550      24.612   5.276  58.542  1.00 23.54           O  
HETATM 4875  O   HOH A 551      -4.337 -13.072  38.635  1.00 45.75           O  
HETATM 4876  O   HOH A 552       7.438   8.957  73.047  1.00 42.70           O  
HETATM 4877  O   HOH A 553      10.027   0.437  59.342  1.00 21.09           O  
HETATM 4878  O   HOH A 554       4.760   1.329  40.645  1.00 35.11           O  
HETATM 4879  O   HOH A 555      22.209   2.226  47.932  1.00 46.06           O  
HETATM 4880  O   HOH A 556       5.071  -0.655  58.710  1.00 20.24           O  
HETATM 4881  O   HOH A 557      21.432  -2.653  58.021  1.00 47.67           O  
HETATM 4882  O   HOH A 558       6.040 -15.026  53.235  1.00 28.62           O  
HETATM 4883  O   HOH A 559       1.399   6.705  40.095  1.00 57.64           O  
HETATM 4884  O   HOH A 560      21.741  -0.952  60.606  1.00 33.29           O  
HETATM 4885  O   HOH A 561      -9.552  -0.864  40.449  1.00 35.64           O  
HETATM 4886  O   HOH A 562       3.565   7.676  38.597  1.00 53.87           O  
HETATM 4887  O   HOH A 563      11.588  -0.415  66.518  1.00 36.29           O  
HETATM 4888  O   HOH A 564       0.240 -14.975  38.610  1.00 34.80           O  
HETATM 4889  O   HOH A 565       5.711 -18.665  45.427  1.00 44.16           O  
HETATM 4890  O   HOH A 566     -14.539   0.447  71.625  1.00 38.42           O  
HETATM 4891  O   HOH A 567     -13.846  -2.326  65.435  1.00 28.47           O  
HETATM 4892  O   HOH A 568     -15.227 -17.930  70.839  1.00 45.80           O  
HETATM 4893  O   HOH A 569      20.231  -8.818  51.413  1.00 48.13           O  
HETATM 4894  O   HOH A 570       0.647  19.640  58.903  1.00 30.47           O  
HETATM 4895  O   HOH A 571       7.474  -5.866  70.227  1.00 39.29           O  
HETATM 4896  O   HOH A 572      10.139  -4.444  40.762  1.00 36.76           O  
HETATM 4897  O   HOH A 573     -16.555  -2.867  68.876  1.00 41.70           O  
HETATM 4898  O   HOH A 574      18.072  16.501  57.568  1.00 54.07           O  
HETATM 4899  O   HOH A 575      11.531  -2.554  66.682  1.00 41.59           O  
HETATM 4900  O   HOH A 576     -16.038 -13.248  64.308  1.00 57.06           O  
HETATM 4901  O   HOH A 577       7.233  -8.657  35.764  1.00 47.41           O  
HETATM 4902  O   HOH A 578      10.492  -9.452  34.252  1.00 43.09           O  
HETATM 4903  O   HOH A 579     -14.051 -12.497  80.427  1.00 41.17           O  
HETATM 4904  O   HOH A 580       8.881  -8.079  40.269  1.00 38.05           O  
HETATM 4905  O   HOH A 581      -1.986 -21.095  83.371  1.00 50.05           O  
HETATM 4906  O   HOH A 582       3.990 -17.572  54.378  1.00 54.90           O  
HETATM 4907  O   HOH A 583      11.754   1.802  31.949  1.00 50.50           O  
HETATM 4908  O   HOH A 584     -11.146   0.681  43.146  1.00 33.40           O  
HETATM 4909  O   HOH A 585      10.751  -1.788  58.074  1.00 21.77           O  
HETATM 4910  O   HOH A 586      -9.963  -2.911  50.349  1.00 21.24           O  
HETATM 4911  O   HOH A 587      12.228 -10.393  53.477  1.00 24.82           O  
HETATM 4912  O   HOH A 588       0.528  -2.705  78.817  1.00 36.24           O  
HETATM 4913  O   HOH A 589      13.643  -4.764  61.489  1.00 32.25           O  
HETATM 4914  O   HOH A 590      27.884   6.695  60.226  1.00 31.30           O  
HETATM 4915  O   HOH A 591      13.960 -10.317  57.138  1.00 34.02           O  
HETATM 4916  O   HOH A 592       8.764  -9.872  58.234  1.00 29.21           O  
HETATM 4917  O   HOH A 593      25.960   3.195  52.292  1.00 33.47           O  
HETATM 4918  O   HOH A 594     -11.733  -1.907  63.518  1.00 24.48           O  
HETATM 4919  O   HOH A 595      -9.460   7.404  62.794  1.00 27.38           O  
HETATM 4920  O   HOH A 596     -17.087   1.470  61.260  1.00 35.80           O  
HETATM 4921  O   HOH A 597       6.075 -12.299  45.192  1.00 28.20           O  
HETATM 4922  O   HOH A 598       9.409 -10.395  61.262  1.00 24.46           O  
HETATM 4923  O   HOH A 599      10.355  17.758  55.573  1.00 30.68           O  
HETATM 4924  O   HOH A 600       8.586  12.915  71.362  1.00 30.37           O  
HETATM 4925  O   HOH A 601       5.536  20.310  61.823  1.00 32.44           O  
HETATM 4926  O   HOH A 602      -2.932   3.627  84.239  1.00 43.24           O  
HETATM 4927  O   HOH A 603     -12.474  -1.417  74.962  1.00 43.45           O  
HETATM 4928  O   HOH A 604     -12.371   1.995  63.278  1.00 31.98           O  
HETATM 4929  O   HOH A 605      22.003   8.545  68.135  1.00 31.45           O  
HETATM 4930  O   HOH A 606      -2.556 -15.606  52.166  1.00 29.70           O  
HETATM 4931  O   HOH A 607       6.594  11.652  73.124  1.00 37.96           O  
HETATM 4932  O   HOH A 608     -12.468 -16.988  70.802  1.00 34.91           O  
HETATM 4933  O   HOH A 609      18.142  13.995  57.365  1.00 38.50           O  
HETATM 4934  O   HOH A 610     -13.480 -12.299  53.450  1.00 37.86           O  
HETATM 4935  O   HOH A 611     -13.508  -6.755  83.796  1.00 40.02           O  
HETATM 4936  O   HOH A 612      14.176  -7.070  42.174  1.00 51.21           O  
HETATM 4937  O   HOH A 613      -4.813 -16.974  90.487  1.00 46.21           O  
HETATM 4938  O   HOH A 614       9.805   0.296  70.171  1.00 30.12           O  
HETATM 4939  O   HOH A 615      14.616 -14.839  49.150  1.00 50.69           O  
HETATM 4940  O   HOH A 616      -0.031 -18.376  84.994  1.00 41.54           O  
HETATM 4941  O   HOH A 617      22.424  14.200  50.152  1.00 39.01           O  
HETATM 4942  O   HOH A 618      -1.748 -14.480  74.038  1.00 46.72           O  
HETATM 4943  O   HOH A 619     -12.478   3.113  68.077  1.00 33.88           O  
HETATM 4944  O   HOH A 620     -10.781  10.362  52.068  1.00 39.61           O  
HETATM 4945  O   HOH A 621      -1.912 -15.261  64.674  1.00 49.39           O  
HETATM 4946  O   HOH A 622       9.218 -10.222  41.449  1.00 51.96           O  
HETATM 4947  O   HOH A 623       4.747  -3.005  80.322  1.00 61.83           O  
HETATM 4948  O   HOH A 624      11.597  17.875  69.735  1.00 55.43           O  
HETATM 4949  O   HOH A 625     -19.680  -6.133  81.484  1.00 58.33           O  
HETATM 4950  O   HOH A 626      16.750   0.841  69.400  1.00 42.17           O  
HETATM 4951  O   HOH A 627       3.468   9.526  71.784  1.00 40.78           O  
HETATM 4952  O   HOH A 628      -1.002   5.315  39.930  1.00 31.49           O  
HETATM 4953  O   HOH A 629      13.328  -4.507  65.340  1.00 41.46           O  
HETATM 4954  O   HOH A 630     -12.187 -10.254  46.911  1.00 40.27           O  
HETATM 4955  O   HOH A 631      24.986  13.758  56.806  1.00 52.01           O  
HETATM 4956  O   HOH A 632       3.562 -12.479  85.089  1.00 47.17           O  
HETATM 4957  O   HOH A 633      12.495   2.739  41.632  1.00 33.84           O  
HETATM 4958  O   HOH A 634      10.082  12.662  43.135  1.00 35.02           O  
HETATM 4959  O   HOH A 635      19.821   7.916  38.771  1.00 50.21           O  
HETATM 4960  O   HOH A 636      -6.148  11.379  48.962  1.00 42.62           O  
HETATM 4961  O   HOH A 637       0.030 -12.481  57.043  1.00 28.53           O  
HETATM 4962  O   HOH A 638      15.378  19.201  60.947  1.00 34.95           O  
HETATM 4963  O   HOH A 639      -6.335 -20.502  83.573  1.00 44.09           O  
HETATM 4964  O   HOH A 640      -9.872 -15.489  56.274  1.00 37.67           O  
HETATM 4965  O   HOH A 641       1.646 -12.817  67.402  1.00 37.02           O  
HETATM 4966  O   HOH A 642     -12.424  -0.711  45.451  1.00 57.10           O  
HETATM 4967  O   HOH A 643       6.878   1.252  40.240  1.00 39.11           O  
HETATM 4968  O   HOH A 644      -4.008  -9.606  40.401  1.00 56.44           O  
HETATM 4969  O   HOH A 645      18.628  11.821  42.411  1.00 42.39           O  
HETATM 4970  O   HOH A 646      28.104  15.396  58.200  1.00 42.53           O  
HETATM 4971  O   HOH A 647      -2.615  12.341  50.375  1.00 41.79           O  
HETATM 4972  O   HOH A 648      -0.146   2.499  39.923  1.00 38.04           O  
HETATM 4973  O   HOH A 649     -22.056 -13.263  70.773  1.00 56.26           O  
HETATM 4974  O   HOH A 650     -16.654  -2.614  66.787  1.00 54.04           O  
HETATM 4975  O   HOH A 651      22.018  17.531  62.405  1.00 43.35           O  
HETATM 4976  O   HOH A 652      19.104  10.826  72.836  1.00 46.92           O  
HETATM 4977  O   HOH A 653       2.330 -13.795  70.036  1.00 50.33           O  
HETATM 4978  O   HOH A 654      -1.838   1.257  37.411  1.00 50.60           O  
HETATM 4979  O   HOH A 655      -4.022   0.526  36.642  1.00 54.49           O  
HETATM 4980  O   HOH A 656      -3.200  -2.669  36.406  1.00 58.26           O  
HETATM 4981  O   HOH A 657       4.645  -5.602  37.739  1.00 56.43           O  
HETATM 4982  O   HOH A 658      21.712 -10.818  48.440  1.00 54.67           O  
HETATM 4983  O   HOH A 659      24.409  -2.821  56.330  1.00 55.03           O  
HETATM 4984  O   HOH A 660      18.634  -3.244  39.623  1.00 48.45           O  
HETATM 4985  O   HOH A 661       1.059 -14.473  65.533  1.00 37.57           O  
HETATM 4986  O   HOH A 662     -17.544  -6.109  65.139  1.00 49.24           O  
HETATM 4987  O   HOH A 663      11.654  -3.091  39.279  1.00 50.13           O  
HETATM 4988  O   HOH A 664      12.122  18.331  62.922  1.00 43.99           O  
HETATM 4989  O   HOH A 665      10.376 -12.818  65.972  1.00 41.90           O  
HETATM 4990  O   HOH A 666       0.791  10.411  70.437  1.00 54.37           O  
HETATM 4991  O   HOH A 667      25.941  11.852  52.588  1.00 41.76           O  
HETATM 4992  O   HOH A 668      14.734  -8.692  45.589  1.00 54.24           O  
HETATM 4993  O   HOH A 669      24.268  -7.890  46.505  1.00 56.53           O  
HETATM 4994  O   HOH A 670     -18.357  -7.304  67.792  1.00 45.51           O  
HETATM 4995  O   HOH A 671      -3.325 -20.834  77.051  1.00 56.35           O  
HETATM 4996  O   HOH A 672       5.048  12.878  45.031  1.00 50.69           O  
HETATM 4997  O   HOH A 673      11.882  11.287  40.317  1.00 54.87           O  
HETATM 4998  O   HOH A 674      -4.586 -17.736  64.991  1.00 51.93           O  
HETATM 4999  O   HOH A 675       3.285  14.865  46.286  1.00 54.58           O  
HETATM 5000  O   HOH A 676     -11.783 -18.661  91.662  1.00 49.69           O  
HETATM 5001  O   HOH A 677      -6.098 -20.110  94.108  1.00 36.11           O  
HETATM 5002  O   HOH A 678       4.829  -7.827  37.963  1.00 45.80           O  
HETATM 5003  O   HOH A 679      27.210  -2.513  55.633  1.00 42.56           O  
HETATM 5004  O   HOH A 680       4.371   8.649  75.525  1.00 55.17           O  
HETATM 5005  O   HOH A 681      20.880  -1.870  36.470  1.00 51.18           O  
HETATM 5006  O   HOH A 682      17.531  -7.355  59.341  1.00 47.03           O  
HETATM 5007  O   HOH A 683       9.740   2.714  42.253  1.00 33.22           O  
HETATM 5008  O   HOH A 684     -15.424 -17.657  90.116  1.00 39.64           O  
HETATM 5009  O   HOH A 685       1.700  -6.685  30.556  1.00 63.74           O  
HETATM 5010  O   HOH A 686      17.471 -12.451  47.766  1.00 59.76           O  
HETATM 5011  O   HOH A 687      15.194 -14.708  46.813  1.00 54.27           O  
HETATM 5012  O   HOH A 688      17.115   0.559  66.785  1.00 36.79           O  
HETATM 5013  O   HOH A 689      17.107  -8.006  44.360  1.00 58.23           O  
HETATM 5014  O   HOH A 690       6.704  16.924  69.160  1.00 40.06           O  
HETATM 5015  O   HOH A 691      28.355   7.351  63.534  1.00 40.61           O  
HETATM 5016  O   HOH A 692      27.570   4.504  62.325  1.00 38.52           O  
HETATM 5017  O   HOH A 693      10.653 -11.272  63.269  1.00 44.17           O  
HETATM 5018  O   HOH A 694     -15.029   4.080  64.967  1.00 49.36           O  
HETATM 5019  O   HOH A 695     -12.458   3.844  65.409  1.00 39.20           O  
HETATM 5020  O   HOH A 696     -11.674   6.518  64.630  1.00 44.42           O  
HETATM 5021  O   HOH A 697      21.395   4.840  37.536  1.00 42.25           O  
HETATM 5022  O   HOH A 698      20.129   5.967  42.449  1.00 59.90           O  
HETATM 5023  O   HOH A 699      21.950   7.702  41.313  1.00 50.58           O  
HETATM 5024  O   HOH A 700     -16.566  -0.826  70.486  1.00 56.67           O  
HETATM 5025  O   HOH A 701      -0.062  -3.860  75.898  1.00 32.17           O  
HETATM 5026  O   HOH A 702       3.821 -18.320  67.399  1.00 59.92           O  
HETATM 5027  O   HOH A 703       4.909 -14.431  67.922  1.00 58.59           O  
HETATM 5028  O   HOH A 704       3.146  -0.584  77.467  1.00 49.33           O  
HETATM 5029  O   HOH A 705      15.473   0.511  61.972  1.00 38.27           O  
HETATM 5030  O   HOH A 706       0.335 -23.016  85.901  1.00 34.97           O  
HETATM 5031  O   HOH A 707     -14.041   9.293  46.954  1.00 47.04           O  
HETATM 5032  O   HOH A 708     -12.171  -3.187  48.705  1.00 32.91           O  
HETATM 5033  O   HOH A 709     -18.129  -0.538  59.617  1.00 37.61           O  
HETATM 5034  O   HOH A 710      13.400   0.353  64.618  1.00 29.28           O  
HETATM 5035  O   HOH A 711      -0.133  17.030  66.091  1.00 45.83           O  
HETATM 5036  O   HOH A 712      17.405   7.133  35.040  1.00 46.14           O  
HETATM 5037  O   HOH A 713      16.177   4.728  32.363  1.00 52.83           O  
HETATM 5038  O   HOH A 714      15.502   3.895  35.742  1.00 54.85           O  
HETATM 5039  O   HOH A 715     -17.154  -1.581  58.002  1.00 51.40           O  
HETATM 5040  O   HOH A 716      -3.324  -7.732  92.905  1.00 95.12           O  
HETATM 5041  O   HOH A 717       0.093 -16.543  58.887  1.00 33.91           O  
HETATM 5042  O   HOH B 501      38.322  -6.137  -5.476  1.00 43.16           O  
HETATM 5043  O   HOH B 502      29.365  -9.369  -0.081  1.00 20.89           O  
HETATM 5044  O   HOH B 503      38.307 -23.428  -4.553  1.00 45.17           O  
HETATM 5045  O   HOH B 504      22.845 -14.679  15.673  1.00 36.04           O  
HETATM 5046  O   HOH B 505      31.850  -3.043   9.408  1.00 41.90           O  
HETATM 5047  O   HOH B 506      20.572 -15.112 -14.961  1.00 40.39           O  
HETATM 5048  O   HOH B 507      32.977 -29.535   5.068  1.00 26.83           O  
HETATM 5049  O   HOH B 508      27.168 -14.066   5.120  1.00 27.18           O  
HETATM 5050  O   HOH B 509      16.102 -19.326   4.205  1.00 33.32           O  
HETATM 5051  O   HOH B 510      25.927 -21.697 -21.989  1.00 51.43           O  
HETATM 5052  O   HOH B 511      36.393 -29.049  -0.679  1.00 32.99           O  
HETATM 5053  O   HOH B 512      29.690 -13.355   6.603  1.00 26.49           O  
HETATM 5054  O   HOH B 513      24.731 -27.841  22.828  1.00 41.43           O  
HETATM 5055  O   HOH B 514      32.245  -8.270 -25.858  1.00 43.08           O  
HETATM 5056  O   HOH B 515      16.739  -7.277  20.166  1.00 51.81           O  
HETATM 5057  O   HOH B 516      14.500  -6.542  31.188  1.00 47.30           O  
HETATM 5058  O   HOH B 517      15.163  -4.988  26.429  1.00 46.73           O  
HETATM 5059  O   HOH B 518      16.758  -3.918  31.228  1.00 54.57           O  
HETATM 5060  O   HOH B 519      13.727 -16.057  28.644  1.00 51.53           O  
HETATM 5061  O   HOH B 520      16.281 -11.312  32.687  1.00 54.95           O  
HETATM 5062  O   HOH B 521      30.593 -11.241   4.967  1.00 24.58           O  
HETATM 5063  O   HOH B 522      12.406  -6.730  19.950  1.00 43.73           O  
HETATM 5064  O   HOH B 523      36.028  -6.752   0.593  1.00 28.44           O  
HETATM 5065  O   HOH B 524      25.043 -23.007  17.343  1.00 22.04           O  
HETATM 5066  O   HOH B 525      31.365 -15.041   8.105  1.00 28.12           O  
HETATM 5067  O   HOH B 526      35.922 -10.800 -10.747  1.00 28.34           O  
HETATM 5068  O   HOH B 527      37.511 -14.956   7.046  1.00 30.75           O  
HETATM 5069  O   HOH B 528      34.324 -13.696  10.025  1.00 37.11           O  
HETATM 5070  O   HOH B 529      20.308 -21.457   6.697  1.00 24.05           O  
HETATM 5071  O   HOH B 530      10.332 -18.527   7.425  1.00 28.87           O  
HETATM 5072  O   HOH B 531      34.087  -7.664  -3.172  1.00 24.27           O  
HETATM 5073  O   HOH B 532      30.818 -12.902   9.710  1.00 32.26           O  
HETATM 5074  O   HOH B 533      10.704 -11.893   0.345  1.00 28.07           O  
HETATM 5075  O   HOH B 534      18.762 -12.830 -13.207  1.00 37.98           O  
HETATM 5076  O   HOH B 535      35.887  -8.883   2.524  1.00 29.25           O  
HETATM 5077  O   HOH B 536      35.386  -5.755   4.796  1.00 38.73           O  
HETATM 5078  O   HOH B 537      38.751 -31.899   6.018  1.00 35.96           O  
HETATM 5079  O   HOH B 538      12.815 -22.950  -2.148  1.00 40.20           O  
HETATM 5080  O   HOH B 539      37.102  -8.382  -1.437  1.00 41.52           O  
HETATM 5081  O   HOH B 540      38.866 -27.557  -1.252  1.00 29.27           O  
HETATM 5082  O   HOH B 541      12.700 -19.545   6.788  1.00 33.78           O  
HETATM 5083  O   HOH B 542      19.571 -15.218  -8.398  1.00 29.06           O  
HETATM 5084  O   HOH B 543      24.875  -1.627   3.340  1.00 29.08           O  
HETATM 5085  O   HOH B 544      24.118   0.409   9.347  1.00 36.77           O  
HETATM 5086  O   HOH B 545       9.302   0.308  15.947  1.00 46.65           O  
HETATM 5087  O   HOH B 546      28.573  -4.203  13.888  1.00 34.33           O  
HETATM 5088  O   HOH B 547      36.505  -7.173  13.476  1.00 50.37           O  
HETATM 5089  O   HOH B 548       8.756  -3.442   9.295  1.00 45.03           O  
HETATM 5090  O   HOH B 549      17.179  -5.537  21.344  1.00 48.22           O  
HETATM 5091  O   HOH B 550      42.311   2.647 -24.971  1.00 40.16           O  
HETATM 5092  O   HOH B 551      32.522  -2.613  -6.910  1.00 33.92           O  
HETATM 5093  O   HOH B 552      30.231 -35.127   3.507  1.00 36.42           O  
HETATM 5094  O   HOH B 553      27.400 -15.623   3.146  1.00 28.74           O  
HETATM 5095  O   HOH B 554      29.234 -32.284  11.740  1.00 41.85           O  
HETATM 5096  O   HOH B 555      18.993 -11.953  23.269  1.00 52.31           O  
HETATM 5097  O   HOH B 556      18.254 -35.015  -1.361  1.00 50.20           O  
HETATM 5098  O   HOH B 557      29.244 -10.930  12.106  1.00 36.08           O  
HETATM 5099  O   HOH B 558      23.434   2.116 -16.000  1.00 39.51           O  
HETATM 5100  O   HOH B 559      31.386 -12.126  18.944  1.00 39.20           O  
HETATM 5101  O   HOH B 560      31.390 -19.986  24.468  1.00 43.73           O  
HETATM 5102  O   HOH B 561      34.375   1.030 -12.864  1.00 37.21           O  
HETATM 5103  O   HOH B 562      40.952 -19.723  19.121  1.00 39.87           O  
HETATM 5104  O   HOH B 563      40.690   7.991 -20.723  1.00 50.97           O  
HETATM 5105  O   HOH B 564      27.078   0.119  -4.217  1.00 49.38           O  
HETATM 5106  O   HOH B 565      35.333 -16.007  22.326  1.00 37.70           O  
HETATM 5107  O   HOH B 566      35.854 -28.967  15.395  1.00 41.44           O  
HETATM 5108  O   HOH B 567      18.888 -12.948 -10.236  1.00 42.74           O  
HETATM 5109  O   HOH B 568      37.841 -25.557  24.655  1.00 51.18           O  
HETATM 5110  O   HOH B 569      30.426  -3.052   4.597  1.00 31.22           O  
HETATM 5111  O   HOH B 570      15.023 -19.469  20.376  1.00 51.39           O  
HETATM 5112  O   HOH B 571      37.798   5.484 -17.740  1.00 49.14           O  
HETATM 5113  O   HOH B 572      20.146 -21.976  -8.118  1.00 49.81           O  
HETATM 5114  O   HOH B 573      25.083 -32.335  23.962  1.00 51.78           O  
HETATM 5115  O   HOH B 574      20.559 -18.641 -11.939  1.00 44.25           O  
HETATM 5116  O   HOH B 575      35.214 -19.762 -22.181  1.00 44.12           O  
HETATM 5117  O   HOH B 576      14.660 -16.035  18.265  1.00 46.53           O  
HETATM 5118  O   HOH B 577       4.982 -15.376   4.694  1.00 45.87           O  
HETATM 5119  O   HOH B 578      18.720 -12.002 -17.253  1.00 45.42           O  
HETATM 5120  O   HOH B 579      31.971  -5.150  20.629  1.00 62.17           O  
HETATM 5121  O   HOH B 580      24.630 -22.063 -19.679  1.00 55.26           O  
HETATM 5122  O   HOH B 581      25.436 -11.877  11.525  1.00 43.07           O  
HETATM 5123  O   HOH B 582      38.127 -11.656  17.327  1.00 45.56           O  
HETATM 5124  O   HOH B 583      33.549 -28.687  23.494  1.00 51.18           O  
HETATM 5125  O   HOH B 584      10.412 -17.099  14.755  1.00 41.19           O  
HETATM 5126  O   HOH B 585      34.640 -22.682  24.559  1.00 53.10           O  
HETATM 5127  O   HOH B 586      36.917 -15.469  10.061  1.00 52.61           O  
HETATM 5128  O   HOH B 587      37.922 -30.903  18.764  1.00 47.64           O  
HETATM 5129  O   HOH B 588      41.720 -14.214   8.146  1.00 47.94           O  
HETATM 5130  O   HOH B 589      20.201 -13.787 -18.121  1.00 46.77           O  
HETATM 5131  O   HOH B 590      34.141 -24.872  24.857  1.00 47.99           O  
HETATM 5132  O   HOH B 591      28.939  -0.295  17.415  1.00 54.85           O  
HETATM 5133  O   HOH B 592      27.398  -0.105  18.920  1.00 52.60           O  
HETATM 5134  O   HOH B 593      32.306  -3.801  12.387  1.00 56.67           O  
HETATM 5135  O   HOH B 594      44.119 -14.447 -15.286  1.00 55.00           O  
HETATM 5136  O   HOH B 595      23.955 -23.232  29.573  1.00 59.04           O  
HETATM 5137  O   HOH B 596      21.423 -29.284  13.218  1.00 52.40           O  
HETATM 5138  O   HOH B 597      29.287 -22.887  26.387  1.00 55.07           O  
HETATM 5139  O   HOH B 598      34.682  -5.254  14.463  1.00 51.13           O  
HETATM 5140  O   HOH B 599      36.389  -2.617   1.669  1.00 41.20           O  
HETATM 5141  O   HOH B 600      22.346  -7.211 -23.267  1.00 51.70           O  
HETATM 5142  O   HOH B 601      23.529 -11.107  28.292  1.00 47.47           O  
HETATM 5143  O   HOH B 602      34.041 -32.552   3.764  1.00 44.90           O  
HETATM 5144  O   HOH B 603      38.939 -15.040   0.211  1.00 45.36           O  
HETATM 5145  O   HOH B 604      37.775  -9.613   6.568  1.00 42.45           O  
HETATM 5146  O   HOH B 605      21.731   0.448 -23.961  1.00 68.95           O  
HETATM 5147  O   HOH B 606      39.522   4.994 -33.049  1.00 49.00           O  
HETATM 5148  O   HOH B 607      19.986 -24.297   5.941  1.00 38.11           O  
HETATM 5149  O   HOH B 608       5.461 -25.815   9.466  1.00 45.88           O  
HETATM 5150  O   HOH B 609      27.078 -31.353  12.775  1.00 38.02           O  
HETATM 5151  O   HOH B 610      33.295  -0.054 -10.591  1.00 39.44           O  
HETATM 5152  O   HOH B 611      28.516  -2.336   6.476  1.00 36.39           O  
HETATM 5153  O   HOH B 612      32.019  -4.352   6.100  1.00 43.60           O  
HETATM 5154  O   HOH B 613      42.750 -15.249   5.578  1.00 37.61           O  
HETATM 5155  O   HOH B 614      39.926 -11.619  20.292  1.00 60.89           O  
HETATM 5156  O   HOH B 615       8.160 -11.689  -0.170  1.00 38.29           O  
HETATM 5157  O   HOH B 616      16.760   0.875   4.408  1.00 44.14           O  
HETATM 5158  O   HOH B 617      30.283 -12.837 -22.441  1.00 50.71           O  
HETATM 5159  O   HOH B 618      40.038 -17.075  -0.735  1.00 44.14           O  
HETATM 5160  O   HOH B 619      25.047  -5.352  21.976  1.00 57.48           O  
HETATM 5161  O   HOH B 620      16.382 -35.715   0.492  1.00 54.33           O  
HETATM 5162  O   HOH B 621      18.114 -10.421  21.284  1.00 48.38           O  
HETATM 5163  O   HOH B 622      27.880 -32.083  15.306  1.00 57.12           O  
HETATM 5164  O   HOH B 623      16.121 -27.210  16.278  1.00 61.92           O  
HETATM 5165  O   HOH B 624      11.959 -21.324  -8.859  1.00 44.10           O  
HETATM 5166  O   HOH B 625      21.606 -17.614 -14.201  1.00 51.87           O  
HETATM 5167  O   HOH B 626      35.440 -23.913  -4.967  1.00 45.56           O  
HETATM 5168  O   HOH B 627       6.263  -5.153   0.219  1.00 50.35           O  
HETATM 5169  O   HOH B 628      34.382  -2.968   6.136  1.00 39.83           O  
HETATM 5170  O   HOH B 629      27.523  -2.094  21.617  1.00 61.45           O  
HETATM 5171  O   HOH B 630      12.086 -25.373  -6.083  1.00 53.71           O  
HETATM 5172  O   HOH B 631      25.774  -6.227  24.637  1.00 56.59           O  
HETATM 5173  O   HOH B 632      13.319 -22.070   7.968  1.00 32.79           O  
HETATM 5174  O   HOH B 633      12.234  -9.146  20.064  1.00 51.68           O  
HETATM 5175  O   HOH B 634      41.259 -14.348 -14.581  1.00 57.65           O  
HETATM 5176  O   HOH B 635      22.427  -2.164   2.606  1.00 37.64           O  
HETATM 5177  O   HOH B 636      44.063 -21.644   8.678  1.00 34.55           O  
HETATM 5178  O   HOH B 637      24.605 -13.582 -19.775  1.00 52.69           O  
HETATM 5179  O   HOH B 638      22.342 -15.242 -17.989  1.00 52.70           O  
HETATM 5180  O   HOH B 639      20.468 -17.180  22.366  1.00 39.04           O  
HETATM 5181  O   HOH B 640      20.783 -26.688  30.503  1.00 55.47           O  
HETATM 5182  O   HOH B 641      21.079 -25.976  27.793  1.00 47.87           O  
HETATM 5183  O   HOH B 642      36.376  -4.674  -4.509  1.00 50.87           O  
HETATM 5184  O   HOH B 643      38.742 -23.676  -7.334  1.00 44.35           O  
HETATM 5185  O   HOH B 644      24.531 -34.352   2.121  1.00 38.66           O  
HETATM 5186  O   HOH B 645      17.583   4.220   3.703  1.00 56.97           O  
HETATM 5187  O   HOH B 646      17.147   4.552   6.728  1.00 57.14           O  
HETATM 5188  O   HOH B 647      20.385   7.829   7.330  1.00 55.96           O  
HETATM 5189  O   HOH B 648      18.885   5.430   5.108  1.00 50.64           O  
HETATM 5190  O   HOH B 649      39.438 -13.958  -9.451  1.00 51.88           O  
HETATM 5191  O   HOH B 650       5.519   1.504  13.125  1.00 43.85           O  
HETATM 5192  O   HOH B 651      14.049   0.351  26.528  1.00 56.59           O  
HETATM 5193  O   HOH B 652      18.867   3.946   1.596  1.00 50.07           O  
CONECT  920 1240                                                                
CONECT 1182 1507                                                                
CONECT 1240  920                                                                
CONECT 1507 1182                                                                
CONECT 1948 4822                                                                
CONECT 1950 2306                                                                
CONECT 2306 1950                                                                
CONECT 3335 3655                                                                
CONECT 3597 3922                                                                
CONECT 3655 3335                                                                
CONECT 3922 3597                                                                
CONECT 4365 4721                                                                
CONECT 4721 4365                                                                
CONECT 4822 1948                                                                
MASTER      495    0    4   25   28    0    6    6 5191    2   14   56          
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.