CNRS Nantes University UFIP UFIP
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***  PROTEIN BINDING 27-SEP-18 6MLD  ***

elNémo ID: 22060215182887942

Job options:

ID        	=	 22060215182887942
JOBID     	=	 PROTEIN BINDING 27-SEP-18 6MLD
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    PROTEIN BINDING                         27-SEP-18   6MLD              
TITLE     CRYSTAL STRUCTURE OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-   
TITLE    2 BINDING PROTEIN (LAO) F52A MUTANT FROM SALMONELLA TYPHIMURIUM        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE/ARGININE/ORNITHINE-BINDING PERIPLASMIC PROTEIN;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LAO-BINDING PROTEIN;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 / 
SOURCE   3 ATCC 700720);                                                        
SOURCE   4 ORGANISM_TAXID: 99287;                                               
SOURCE   5 STRAIN: LT2 / SGSC1412 / ATCC 700720;                                
SOURCE   6 GENE: ARGT, STM2355;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21-AI;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET12B                                    
KEYWDS    PERIPLASMIC BINDING PROTEIN, LAO, THERMODYNAMICS, PROTEIN LIGAND      
KEYWDS   2 COMPLEX, PROTEIN BINDING                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ROMERO-ROMERO,R.VERGARA,G.ESPINOZA-PEREZ,A.RODRIGUEZ-ROMERO         
JRNL        AUTH   R.VERGARA,S.ROMERO-ROMERO,G.ESPINOZA-PEREZ,                  
JRNL        AUTH 2 A.RODRIGUEZ-ROMERO,A.SOSA-PEINADO,D.A.FERNANDEZ-VELASCO      
JRNL        TITL   STRUCTURAL AND THERMODYNAMIC CONTRIBUTION OF THE BINDING     
JRNL        TITL 2 SITE RESIDUES IN THE LYSINE-ARGININE-ORNITHINE BINDING       
JRNL        TITL 3 PROTEIN (LAO) TO LIGAND AFFINITY                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27544                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1994                            
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 42.6956 -  3.9998    1.00     1972   154  0.1517 0.1966        
REMARK   3     2  3.9998 -  3.1751    1.00     1868   146  0.1310 0.1622        
REMARK   3     3  3.1751 -  2.7738    1.00     1862   145  0.1568 0.2060        
REMARK   3     4  2.7738 -  2.5202    1.00     1833   143  0.1639 0.2409        
REMARK   3     5  2.5202 -  2.3396    1.00     1814   141  0.1618 0.2219        
REMARK   3     6  2.3396 -  2.2017    1.00     1814   142  0.1614 0.1967        
REMARK   3     7  2.2017 -  2.0914    1.00     1821   142  0.1507 0.1984        
REMARK   3     8  2.0914 -  2.0004    1.00     1807   140  0.1589 0.2158        
REMARK   3     9  2.0004 -  1.9234    1.00     1805   142  0.1573 0.2132        
REMARK   3    10  1.9234 -  1.8570    1.00     1806   141  0.1761 0.1880        
REMARK   3    11  1.8570 -  1.7989    1.00     1800   140  0.1863 0.2586        
REMARK   3    12  1.7989 -  1.7475    1.00     1764   138  0.2141 0.2861        
REMARK   3    13  1.7475 -  1.7015    1.00     1817   142  0.2269 0.2833        
REMARK   3    14  1.7015 -  1.6600    1.00     1767   138  0.2516 0.2936        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           1829                                  
REMARK   3   ANGLE     :  0.987           2470                                  
REMARK   3   CHIRALITY :  0.039            275                                  
REMARK   3   PLANARITY :  0.005            326                                  
REMARK   3   DIHEDRAL  : 12.643            652                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7598 -57.9783 107.3088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0350 T22:   0.0290                                     
REMARK   3      T33:   0.0308 T12:  -0.0014                                     
REMARK   3      T13:   0.0015 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3410 L22:   0.3023                                     
REMARK   3      L33:   0.2106 L12:  -0.0313                                     
REMARK   3      L13:  -0.0147 L23:  -0.0765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0127 S12:   0.0288 S13:  -0.0137                       
REMARK   3      S21:  -0.0474 S22:   0.0022 S23:  -0.0181                       
REMARK   3      S31:   0.0249 S32:  -0.0154 S33:   0.0003                       
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 6MLD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237155.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : VARIMAX HF                         
REMARK 200  OPTICS                         : OSMIC VARIMAX CU-HF                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 200K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27708                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.60                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.9_1692                                       
REMARK 200 STARTING MODEL: 2LAO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE TRIHYDRATE. 0.1 M   
REMARK 280  SODIUM CACODYLATE TRIHYDRATE PH 6.5 30% W/V POLYETHYLENE GLYCOL     
REMARK 280  8,000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       17.37900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.68150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.11550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.68150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.37900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.11550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 590 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   4    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  44    CG   CD   CE   NZ                                   
REMARK 470     LYS A  76    CE   NZ                                             
REMARK 470     GLU A  80    OE1  OE2                                            
REMARK 470     GLU A 107    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 110    CD   CE   NZ                                        
REMARK 470     LYS A 171    CD   CE   NZ                                        
REMARK 470     LYS A 176    CD   CE   NZ                                        
REMARK 470     LYS A 212    CE   NZ                                             
REMARK 470     LYS A 225    CD   CE   NZ                                        
REMARK 470     LYS A 228    CG   CD   CE   NZ                                   
REMARK 470     LYS A 229    CE   NZ                                             
REMARK 470     ASP A 238    C    O    CB   CG   OD1  OD2                        
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    THR A  12       44.11    -85.41                                   
REMARK 500    TYR A  14       58.95   -144.76                                   
REMARK 500    SER A  69       50.04   -161.15                                   
REMARK 500    PHE A 169      -49.42   -133.80                                   
REMARK 500    GLU A 177       30.37    -99.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 715        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A 716        DISTANCE =  6.55 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6MKU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DISCUSSED IN THE SAME WORK                                 
REMARK 900 RELATED ID: 6MKW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DISCUSSED IN THE SAME WORK                                 
REMARK 900 RELATED ID: 6MKX   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DISCUSSED IN THE SAME WORK                                 
REMARK 900 RELATED ID: 6ML0   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DISCUSSED IN THE SAME WORK                                 
REMARK 900 RELATED ID: 6ML9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DISCUSSED IN THE SAME WORK                                 
REMARK 900 RELATED ID: 6MLA   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DISCUSSED IN THE SAME WORK                                 
DBREF  6MLD A    1   238  UNP    P02911   ARGT_SALTY      23    260             
SEQADV 6MLD ALA A   52  UNP  P02911    PHE    74 ENGINEERED MUTATION            
SEQRES   1 A  238  ALA LEU PRO GLN THR VAL ARG ILE GLY THR ASP THR THR          
SEQRES   2 A  238  TYR ALA PRO PHE SER SER LYS ASP ALA LYS GLY GLU PHE          
SEQRES   3 A  238  ILE GLY PHE ASP ILE ASP LEU GLY ASN GLU MET CYS LYS          
SEQRES   4 A  238  ARG MET GLN VAL LYS CYS THR TRP VAL ALA SER ASP ALA          
SEQRES   5 A  238  ASP ALA LEU ILE PRO SER LEU LYS ALA LYS LYS ILE ASP          
SEQRES   6 A  238  ALA ILE ILE SER SER LEU SER ILE THR ASP LYS ARG GLN          
SEQRES   7 A  238  GLN GLU ILE ALA PHE SER ASP LYS LEU TYR ALA ALA ASP          
SEQRES   8 A  238  SER ARG LEU ILE ALA ALA LYS GLY SER PRO ILE GLN PRO          
SEQRES   9 A  238  THR LEU GLU SER LEU LYS GLY LYS HIS VAL GLY VAL LEU          
SEQRES  10 A  238  GLN GLY SER THR GLN GLU ALA TYR ALA ASN ASP ASN TRP          
SEQRES  11 A  238  ARG THR LYS GLY VAL ASP VAL VAL ALA TYR ALA ASN GLN          
SEQRES  12 A  238  ASP LEU ILE TYR SER ASP LEU THR ALA GLY ARG LEU ASP          
SEQRES  13 A  238  ALA ALA LEU GLN ASP GLU VAL ALA ALA SER GLU GLY PHE          
SEQRES  14 A  238  LEU LYS GLN PRO ALA GLY LYS GLU TYR ALA PHE ALA GLY          
SEQRES  15 A  238  PRO SER VAL LYS ASP LYS LYS TYR PHE GLY ASP GLY THR          
SEQRES  16 A  238  GLY VAL GLY LEU ARG LYS ASP ASP THR GLU LEU LYS ALA          
SEQRES  17 A  238  ALA PHE ASP LYS ALA LEU THR GLU LEU ARG GLN ASP GLY          
SEQRES  18 A  238  THR TYR ASP LYS MET ALA LYS LYS TYR PHE ASP PHE ASN          
SEQRES  19 A  238  VAL TYR GLY ASP                                              
HET    ACT  A 301       4                                                       
HET    ACT  A 302       4                                                       
HET    ACT  A 303       4                                                       
HET    ACT  A 304       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   2  ACT    4(C2 H3 O2 1-)                                               
FORMUL   6  HOH   *316(H2 O)                                                    
HELIX    1 AA1 GLY A   28  GLN A   42  1                                  15    
HELIX    2 AA2 ASP A   51  ASP A   53  5                                   3    
HELIX    3 AA3 ALA A   54  ALA A   61  1                                   8    
HELIX    4 AA4 LYS A   76  GLU A   80  5                                   5    
HELIX    5 AA5 THR A  105  LYS A  110  1                                   6    
HELIX    6 AA6 SER A  120  TRP A  130  1                                  11    
HELIX    7 AA7 ARG A  131  GLY A  134  5                                   4    
HELIX    8 AA8 ASN A  142  ALA A  152  1                                  11    
HELIX    9 AA9 GLU A  162  PHE A  169  1                                   8    
HELIX   10 AB1 GLN A  172  LYS A  176  5                                   5    
HELIX   11 AB2 ASP A  203  ASP A  220  1                                  18    
HELIX   12 AB3 GLY A  221  LYS A  228  1                                   8    
SHEET    1 AA1 3 LYS A  44  ALA A  49  0                                        
SHEET    2 AA1 3 THR A   5  THR A  10  1  N  ILE A   8   O  THR A  46           
SHEET    3 AA1 3 ALA A  66  ILE A  67  1  O  ALA A  66   N  GLY A   9           
SHEET    1 AA2 3 THR A  13  TYR A  14  0                                        
SHEET    2 AA2 3 SER A  18  LYS A  20 -1  O  SER A  18   N  TYR A  14           
SHEET    3 AA2 3 PHE A  26  ILE A  27 -1  O  ILE A  27   N  SER A  19           
SHEET    1 AA3 2 ALA A  82  PHE A  83  0                                        
SHEET    2 AA3 2 GLY A 198  LEU A 199 -1  O  LEU A 199   N  ALA A  82           
SHEET    1 AA4 5 ASP A 136  TYR A 140  0                                        
SHEET    2 AA4 5 HIS A 113  LEU A 117  1  N  VAL A 114   O  ASP A 136           
SHEET    3 AA4 5 ALA A 157  ASP A 161  1  O  LEU A 159   N  GLY A 115           
SHEET    4 AA4 5 SER A  92  ALA A  97 -1  N  ARG A  93   O  GLN A 160           
SHEET    5 AA4 5 TYR A 178  PHE A 180 -1  O  ALA A 179   N  ALA A  96           
SSBOND   1 CYS A   38    CYS A   45                          1555   1555  2.03  
CISPEP   1 ALA A   15    PRO A   16          0         5.11                     
SITE     1 AC1  3 LYS A 228  TYR A 230  ASP A 232                               
SITE     1 AC2  3 ASN A 129  ASP A 187  TYR A 190                               
SITE     1 AC3  1 ASP A 136                                                     
SITE     1 AC4  3 GLY A 153  ARG A 154  ASP A 156                               
CRYST1   34.758   76.231   85.363  90.00  90.00  90.00 P 21 21 21    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      0.028770  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013118  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011715        0.00000                         
ATOM      1  N   ALA A   1     -17.568 -43.337  93.134  1.00 21.19           N  
ANISOU    1  N   ALA A   1     2532   2957   2565    119   -240    272       N  
ATOM      2  CA  ALA A   1     -16.847 -43.959  92.027  1.00 29.73           C  
ANISOU    2  CA  ALA A   1     3643   4051   3602    107   -252    261       C  
ATOM      3  C   ALA A   1     -15.372 -44.160  92.359  1.00 30.28           C  
ANISOU    3  C   ALA A   1     3741   4098   3665    102   -222    236       C  
ATOM      4  O   ALA A   1     -14.870 -43.612  93.346  1.00 27.85           O  
ANISOU    4  O   ALA A   1     3431   3765   3387    109   -192    231       O  
ATOM      5  CB  ALA A   1     -16.993 -43.121  90.766  1.00 35.02           C  
ANISOU    5  CB  ALA A   1     4319   4738   4248    122   -264    295       C  
ATOM      6  N   LEU A   2     -14.687 -44.959  91.541  1.00 32.44           N  
ANISOU    6  N   LEU A   2     4041   4382   3900     89   -230    218       N  
ATOM      7  CA  LEU A   2     -13.239 -45.130  91.664  1.00 25.69           C  
ANISOU    7  CA  LEU A   2     3214   3510   3038     86   -202    198       C  
ATOM      8  C   LEU A   2     -12.522 -44.046  90.872  1.00 27.41           C  
ANISOU    8  C   LEU A   2     3447   3725   3243    103   -184    223       C  
ATOM      9  O   LEU A   2     -12.953 -43.698  89.776  1.00 33.83           O  
ANISOU    9  O   LEU A   2     4264   4559   4030    110   -201    247       O  
ATOM     10  CB  LEU A   2     -12.791 -46.509  91.163  1.00 17.94           C  
ANISOU   10  CB  LEU A   2     2255   2539   2024     66   -215    167       C  
ATOM     11  CG  LEU A   2     -13.384 -47.777  91.785  1.00 18.48           C  
ANISOU   11  CG  LEU A   2     2312   2608   2099     46   -234    140       C  
ATOM     12  CD1 LEU A   2     -12.610 -49.004  91.332  1.00 25.16           C  
ANISOU   12  CD1 LEU A   2     3186   3457   2917     30   -237    108       C  
ATOM     13  CD2 LEU A   2     -13.407 -47.673  93.300  1.00 23.54           C  
ANISOU   13  CD2 LEU A   2     2934   3226   2783     46   -214    133       C  
ATOM     14  N   PRO A   3     -11.410 -43.525  91.415  1.00 29.74           N  
ANISOU   14  N   PRO A   3     3752   3994   3555    108   -150    218       N  
ATOM     15  CA  PRO A   3     -10.628 -42.517  90.694  1.00 28.00           C  
ANISOU   15  CA  PRO A   3     3547   3768   3326    122   -130    241       C  
ATOM     16  C   PRO A   3     -10.085 -43.077  89.384  1.00 29.98           C  
ANISOU   16  C   PRO A   3     3824   4041   3527    117   -138    239       C  
ATOM     17  O   PRO A   3      -9.984 -44.302  89.236  1.00 29.41           O  
ANISOU   17  O   PRO A   3     3763   3980   3433    101   -150    210       O  
ATOM     18  CB  PRO A   3      -9.497 -42.188  91.666  1.00 36.35           C  
ANISOU   18  CB  PRO A   3     4608   4793   4411    122    -96    226       C  
ATOM     19  CG  PRO A   3      -9.362 -43.407  92.508  1.00 34.29           C  
ANISOU   19  CG  PRO A   3     4346   4528   4154    105    -99    189       C  
ATOM     20  CD  PRO A   3     -10.761 -43.926  92.673  1.00 32.04           C  
ANISOU   20  CD  PRO A   3     4042   4261   3872    100   -129    189       C  
ATOM     21  N   GLN A   4      -9.759 -42.193  88.445  1.00 31.22           N  
ANISOU   21  N   GLN A   4     3992   4204   3668    130   -129    269       N  
ATOM     22  CA  GLN A   4      -9.226 -42.612  87.153  1.00 32.61           C  
ANISOU   22  CA  GLN A   4     4194   4403   3793    128   -132    270       C  
ATOM     23  C   GLN A   4      -7.912 -43.353  87.359  1.00 27.35           C  
ANISOU   23  C   GLN A   4     3549   3724   3120    118   -109    237       C  
ATOM     24  O   GLN A   4      -7.641 -44.377  86.722  1.00 27.28           O  
ANISOU   24  O   GLN A   4     3558   3732   3073    108   -118    215       O  
ATOM     25  CB  GLN A   4      -9.028 -41.405  86.229  1.00 32.71           C  
ANISOU   25  CB  GLN A   4     4214   4421   3795    146   -121    313       C  
ATOM     26  N   THR A   5      -7.106 -42.820  88.268  1.00 25.95           N  
ANISOU   26  N   THR A   5     3365   3517   2980    120    -78    234       N  
ATOM     27  CA  THR A   5      -5.857 -43.448  88.656  1.00 23.82           C  
ANISOU   27  CA  THR A   5     3108   3231   2711    111    -55    205       C  
ATOM     28  C   THR A   5      -5.769 -43.551  90.172  1.00 22.15           C  
ANISOU   28  C   THR A   5     2879   2992   2544    105    -46    184       C  
ATOM     29  O   THR A   5      -5.968 -42.569  90.897  1.00 22.79           O  
ANISOU   29  O   THR A   5     2944   3055   2661    113    -37    199       O  
ATOM     30  CB  THR A   5      -4.645 -42.672  88.127  1.00 28.29           C  
ANISOU   30  CB  THR A   5     3688   3788   3273    120    -23    223       C  
ATOM     31  OG1 THR A   5      -4.799 -42.456  86.720  1.00 25.66           O  
ANISOU   31  OG1 THR A   5     3370   3482   2897    128    -30    247       O  
ATOM     32  CG2 THR A   5      -3.357 -43.454  88.391  1.00 26.49           C  
ANISOU   32  CG2 THR A   5     3473   3550   3043    110     -1    192       C  
ATOM     33  N   VAL A   6      -5.486 -44.757  90.640  1.00 15.66           N  
ANISOU   33  N   VAL A   6     2063   2169   1719     91    -50    149       N  
ATOM     34  CA  VAL A   6      -5.299 -45.020  92.057  1.00 11.48           C  
ANISOU   34  CA  VAL A   6     1520   1617   1225     84    -42    128       C  
ATOM     35  C   VAL A   6      -3.820 -44.866  92.393  1.00 16.36           C  
ANISOU   35  C   VAL A   6     2146   2214   1855     83    -11    118       C  
ATOM     36  O   VAL A   6      -2.991 -45.572  91.828  1.00 15.59           O  
ANISOU   36  O   VAL A   6     2067   2123   1735     79     -3    104       O  
ATOM     37  CB  VAL A   6      -5.796 -46.439  92.418  1.00 13.61           C  
ANISOU   37  CB  VAL A   6     1789   1895   1487     69    -64     98       C  
ATOM     38  CG1 VAL A   6      -5.438 -46.791  93.848  1.00 14.92           C  
ANISOU   38  CG1 VAL A   6     1944   2038   1685     61    -53     76       C  
ATOM     39  CG2 VAL A   6      -7.296 -46.533  92.201  1.00 15.74           C  
ANISOU   39  CG2 VAL A   6     2046   2184   1752     67    -95    109       C  
ATOM     40  N   ARG A   7      -3.493 -43.934  93.291  1.00 10.67           N  
ANISOU   40  N   ARG A   7     1413   1470   1171     88      7    125       N  
ATOM     41  CA  ARG A   7      -2.111 -43.758  93.748  1.00  7.25           C  
ANISOU   41  CA  ARG A   7      984   1016    755     86     34    115       C  
ATOM     42  C   ARG A   7      -1.849 -44.647  94.946  1.00 12.31           C  
ANISOU   42  C   ARG A   7     1619   1645   1413     75     33     84       C  
ATOM     43  O   ARG A   7      -2.543 -44.547  95.963  1.00  8.44           O  
ANISOU   43  O   ARG A   7     1114   1147    945     74     24     78       O  
ATOM     44  CB  ARG A   7      -1.831 -42.296  94.109  1.00 11.92           C  
ANISOU   44  CB  ARG A   7     1565   1585   1378     95     52    137       C  
ATOM     45  CG  ARG A   7      -1.744 -41.395  92.890  1.00 18.96           C  
ANISOU   45  CG  ARG A   7     2465   2484   2255    106     61    171       C  
ATOM     46  CD  ARG A   7      -1.778 -39.922  93.264  1.00 17.47           C  
ANISOU   46  CD  ARG A   7     2264   2271   2101    116     74    196       C  
ATOM     47  NE  ARG A   7      -0.779 -39.561  94.260  1.00 23.07           N  
ANISOU   47  NE  ARG A   7     2968   2953   2845    111     95    181       N  
ATOM     48  CZ  ARG A   7       0.506 -39.347  93.996  1.00 29.15           C  
ANISOU   48  CZ  ARG A   7     3745   3712   3620    107    117    183       C  
ATOM     49  NH1 ARG A   7       0.963 -39.473  92.755  1.00 27.54           N  
ANISOU   49  NH1 ARG A   7     3554   3524   3385    110    125    199       N  
ATOM     50  NH2 ARG A   7       1.337 -39.016  94.980  1.00 29.35           N  
ANISOU   50  NH2 ARG A   7     3762   3711   3678    101    132    169       N  
ATOM     51  N   ILE A   8      -0.858 -45.526  94.820  1.00 12.05           N  
ANISOU   51  N   ILE A   8     1597   1612   1368     68     41     64       N  
ATOM     52  CA  ILE A   8      -0.539 -46.446  95.908  1.00  9.13           C  
ANISOU   52  CA  ILE A   8     1223   1232   1013     58     40     36       C  
ATOM     53  C   ILE A   8       0.814 -46.129  96.515  1.00  9.70           C  
ANISOU   53  C   ILE A   8     1294   1284   1108     57     64     29       C  
ATOM     54  O   ILE A   8       1.835 -46.216  95.825  1.00 11.13           O  
ANISOU   54  O   ILE A   8     1485   1466   1278     59     80     30       O  
ATOM     55  CB  ILE A   8      -0.519 -47.915  95.433  1.00  8.98           C  
ANISOU   55  CB  ILE A   8     1218   1227    967     50     28     14       C  
ATOM     56  CG1 ILE A   8      -1.750 -48.233  94.591  1.00 13.05           C  
ANISOU   56  CG1 ILE A   8     1738   1764   1455     49      3     21       C  
ATOM     57  CG2 ILE A   8      -0.367 -48.854  96.651  1.00  9.54           C  
ANISOU   57  CG2 ILE A   8     1282   1286   1056     40     24    -11       C  
ATOM     58  CD1 ILE A   8      -1.784 -49.677  94.098  1.00 11.21           C  
ANISOU   58  CD1 ILE A   8     1520   1543   1197     40    -11     -3       C  
ATOM     59  N   GLY A   9       0.819 -45.787  97.805  1.00  7.56           N  
ANISOU   59  N   GLY A   9     1009    996    867     55     66     22       N  
ATOM     60  CA  GLY A   9       2.061 -45.529  98.512  1.00 12.36           C  
ANISOU   60  CA  GLY A   9     1612   1584   1498     52     84     13       C  
ATOM     61  C   GLY A   9       2.713 -46.811  98.992  1.00 11.60           C  
ANISOU   61  C   GLY A   9     1520   1488   1399     44     82    -12       C  
ATOM     62  O   GLY A   9       2.033 -47.751  99.417  1.00  6.79           O  
ANISOU   62  O   GLY A   9      910    886    783     38     66    -26       O  
ATOM     63  N   THR A  10       4.042 -46.852  98.939  1.00  9.20           N  
ANISOU   63  N   THR A  10     1218   1176   1103     42    100    -16       N  
ATOM     64  CA  THR A  10       4.777 -48.005  99.432  1.00  7.91           C  
ANISOU   64  CA  THR A  10     1055   1010    941     36    100    -38       C  
ATOM     65  C   THR A  10       6.170 -47.572  99.877  1.00 12.02           C  
ANISOU   65  C   THR A  10     1568   1515   1485     35    119    -40       C  
ATOM     66  O   THR A  10       6.766 -46.666  99.305  1.00  9.64           O  
ANISOU   66  O   THR A  10     1265   1208   1189     39    135    -24       O  
ATOM     67  CB  THR A  10       4.872 -49.120  98.362  1.00  7.04           C  
ANISOU   67  CB  THR A  10      960    914    800     37     99    -46       C  
ATOM     68  OG1 THR A  10       5.367 -50.324  98.959  1.00  9.70           O  
ANISOU   68  OG1 THR A  10     1298   1247   1142     32     95    -68       O  
ATOM     69  CG2 THR A  10       5.767 -48.720  97.178  1.00  7.22           C  
ANISOU   69  CG2 THR A  10      992    940    810     44    120    -34       C  
ATOM     70  N   ASP A  11       6.660 -48.218 100.925  1.00  9.08           N  
ANISOU   70  N   ASP A  11     1189   1135   1127     30    115    -57       N  
ATOM     71  CA  ASP A  11       7.993 -47.964 101.447  1.00  8.57           C  
ANISOU   71  CA  ASP A  11     1114   1057   1085     27    128    -61       C  
ATOM     72  C   ASP A  11       8.953 -48.982 100.815  1.00 10.04           C  
ANISOU   72  C   ASP A  11     1306   1248   1262     29    139    -68       C  
ATOM     73  O   ASP A  11       8.949 -50.158 101.176  1.00 10.57           O  
ANISOU   73  O   ASP A  11     1376   1317   1323     27    130    -84       O  
ATOM     74  CB  ASP A  11       7.973 -48.051 102.977  1.00  8.97           C  
ANISOU   74  CB  ASP A  11     1154   1098   1157     21    117    -74       C  
ATOM     75  CG  ASP A  11       9.362 -48.037 103.597  1.00 18.32           C  
ANISOU   75  CG  ASP A  11     2327   2271   2363     17    126    -81       C  
ATOM     76  OD1 ASP A  11      10.344 -47.754 102.889  1.00 14.99           O  
ANISOU   76  OD1 ASP A  11     1903   1847   1947     19    143    -73       O  
ATOM     77  OD2 ASP A  11       9.464 -48.308 104.813  1.00 20.87           O  
ANISOU   77  OD2 ASP A  11     2642   2589   2698     12    115    -93       O  
ATOM     78  N   THR A  12       9.760 -48.516  99.860  1.00  6.96           N  
ANISOU   78  N   THR A  12      917    857    869     33    159    -56       N  
ATOM     79  CA  THR A  12      10.536 -49.427  99.008  1.00  8.06           C  
ANISOU   79  CA  THR A  12     1065   1004    994     38    173    -62       C  
ATOM     80  C   THR A  12      11.867 -49.844  99.627  1.00 12.47           C  
ANISOU   80  C   THR A  12     1609   1552   1575     37    183    -71       C  
ATOM     81  O   THR A  12      12.899 -49.883  98.945  1.00 14.48           O  
ANISOU   81  O   THR A  12     1862   1808   1831     41    204    -66       O  
ATOM     82  CB  THR A  12      10.813 -48.799  97.627  1.00 16.06           C  
ANISOU   82  CB  THR A  12     2086   2026   1991     45    193    -42       C  
ATOM     83  OG1 THR A  12      11.302 -47.465  97.801  1.00 14.94           O  
ANISOU   83  OG1 THR A  12     1931   1872   1873     43    205    -24       O  
ATOM     84  CG2 THR A  12       9.549 -48.758  96.784  1.00 11.71           C  
ANISOU   84  CG2 THR A  12     1552   1491   1408     49    181    -35       C  
ATOM     85  N   THR A  13      11.838 -50.177 100.910  1.00  9.93           N  
ANISOU   85  N   THR A  13     1279   1223   1272     30    168    -83       N  
ATOM     86  CA  THR A  13      13.056 -50.567 101.611  1.00  8.82           C  
ANISOU   86  CA  THR A  13     1123   1073   1154     29    173    -91       C  
ATOM     87  C   THR A  13      12.834 -51.920 102.267  1.00 14.61           C  
ANISOU   87  C   THR A  13     1859   1807   1883     28    157   -108       C  
ATOM     88  O   THR A  13      13.407 -52.226 103.314  1.00 16.84           O  
ANISOU   88  O   THR A  13     2130   2083   2186     25    151   -115       O  
ATOM     89  CB  THR A  13      13.475 -49.519 102.680  1.00 14.04           C  
ANISOU   89  CB  THR A  13     1766   1722   1846     21    169    -87       C  
ATOM     90  OG1 THR A  13      12.465 -49.412 103.687  1.00 14.15           O  
ANISOU   90  OG1 THR A  13     1781   1734   1860     16    148    -94       O  
ATOM     91  CG2 THR A  13      13.701 -48.145 102.047  1.00 14.28           C  
ANISOU   91  CG2 THR A  13     1793   1748   1886     20    185    -68       C  
ATOM     92  N   TYR A  14      12.012 -52.750 101.637  1.00 10.64           N  
ANISOU   92  N   TYR A  14     1375   1314   1356     31    151   -115       N  
ATOM     93  CA  TYR A  14      11.558 -53.965 102.298  1.00  8.06           C  
ANISOU   93  CA  TYR A  14     1052    986   1026     29    134   -130       C  
ATOM     94  C   TYR A  14      11.391 -55.148 101.346  1.00  8.61           C  
ANISOU   94  C   TYR A  14     1139   1060   1073     34    136   -140       C  
ATOM     95  O   TYR A  14      10.295 -55.693 101.213  1.00 11.37           O  
ANISOU   95  O   TYR A  14     1500   1414   1406     31    121   -147       O  
ATOM     96  CB  TYR A  14      10.236 -53.674 103.020  1.00 15.51           C  
ANISOU   96  CB  TYR A  14     1996   1932   1966     22    113   -129       C  
ATOM     97  CG  TYR A  14       9.988 -54.472 104.280  1.00 17.15           C  
ANISOU   97  CG  TYR A  14     2198   2134   2182     17     96   -138       C  
ATOM     98  CD1 TYR A  14      10.879 -54.422 105.347  1.00 19.89           C  
ANISOU   98  CD1 TYR A  14     2531   2474   2552     15     96   -140       C  
ATOM     99  CD2 TYR A  14       8.842 -55.249 104.418  1.00 12.82           C  
ANISOU   99  CD2 TYR A  14     1659   1591   1622     13     80   -144       C  
ATOM    100  CE1 TYR A  14      10.646 -55.140 106.512  1.00 21.44           C  
ANISOU  100  CE1 TYR A  14     2723   2668   2755     11     81   -146       C  
ATOM    101  CE2 TYR A  14       8.597 -55.973 105.581  1.00 18.00           C  
ANISOU  101  CE2 TYR A  14     2309   2242   2286      8     67   -149       C  
ATOM    102  CZ  TYR A  14       9.504 -55.911 106.624  1.00 21.93           C  
ANISOU  102  CZ  TYR A  14     2795   2734   2804      8     67   -150       C  
ATOM    103  OH  TYR A  14       9.276 -56.621 107.784  1.00 19.69           O  
ANISOU  103  OH  TYR A  14     2507   2449   2527      4     54   -153       O  
ATOM    104  N   ALA A  15      12.472 -55.528 100.673  1.00  8.75           N  
ANISOU  104  N   ALA A  15     1157   1075   1091     43    156   -143       N  
ATOM    105  CA  ALA A  15      12.484 -56.754  99.891  1.00  9.85           C  
ANISOU  105  CA  ALA A  15     1314   1217   1213     49    160   -158       C  
ATOM    106  C   ALA A  15      12.210 -57.922 100.837  1.00 17.31           C  
ANISOU  106  C   ALA A  15     2257   2151   2168     45    141   -171       C  
ATOM    107  O   ALA A  15      12.603 -57.882 102.004  1.00 15.02           O  
ANISOU  107  O   ALA A  15     1951   1854   1902     42    135   -168       O  
ATOM    108  CB  ALA A  15      13.822 -56.926  99.171  1.00 13.27           C  
ANISOU  108  CB  ALA A  15     1744   1648   1650     61    187   -158       C  
ATOM    109  N   PRO A  16      11.526 -58.966 100.353  1.00 12.98           N  
ANISOU  109  N   PRO A  16     1727   1603   1602     45    132   -185       N  
ATOM    110  CA  PRO A  16      11.072 -59.203  98.977  1.00 13.04           C  
ANISOU  110  CA  PRO A  16     1756   1620   1578     49    137   -192       C  
ATOM    111  C   PRO A  16       9.656 -58.682  98.696  1.00  8.66           C  
ANISOU  111  C   PRO A  16     1210   1078   1004     40    118   -187       C  
ATOM    112  O   PRO A  16       9.029 -59.134  97.743  1.00 13.24           O  
ANISOU  112  O   PRO A  16     1809   1666   1558     40    112   -196       O  
ATOM    113  CB  PRO A  16      11.098 -60.723  98.883  1.00 13.18           C  
ANISOU  113  CB  PRO A  16     1784   1628   1595     51    129   -209       C  
ATOM    114  CG  PRO A  16      10.660 -61.151 100.270  1.00 13.30           C  
ANISOU  114  CG  PRO A  16     1788   1632   1632     42    109   -209       C  
ATOM    115  CD  PRO A  16      11.219 -60.112 101.233  1.00 12.48           C  
ANISOU  115  CD  PRO A  16     1664   1529   1551     40    115   -195       C  
ATOM    116  N   PHE A  17       9.157 -57.772  99.524  1.00  8.50           N  
ANISOU  116  N   PHE A  17     1175   1059    996     33    108   -173       N  
ATOM    117  CA  PHE A  17       7.790 -57.297  99.351  1.00 10.02           C  
ANISOU  117  CA  PHE A  17     1372   1263   1174     26     91   -166       C  
ATOM    118  C   PHE A  17       7.737 -56.023  98.528  1.00 11.26           C  
ANISOU  118  C   PHE A  17     1530   1431   1317     31    101   -149       C  
ATOM    119  O   PHE A  17       6.968 -55.931  97.568  1.00  9.75           O  
ANISOU  119  O   PHE A  17     1352   1253   1100     31     95   -147       O  
ATOM    120  CB  PHE A  17       7.128 -57.093 100.711  1.00  9.49           C  
ANISOU  120  CB  PHE A  17     1290   1191   1125     17     74   -161       C  
ATOM    121  CG  PHE A  17       6.921 -58.376 101.450  1.00  7.88           C  
ANISOU  121  CG  PHE A  17     1087    977    931     11     61   -174       C  
ATOM    122  CD1 PHE A  17       5.957 -59.282 101.022  1.00  6.55           C  
ANISOU  122  CD1 PHE A  17      931    811    748      5     45   -184       C  
ATOM    123  CD2 PHE A  17       7.708 -58.695 102.541  1.00 10.47           C  
ANISOU  123  CD2 PHE A  17     1402   1294   1282     12     64   -175       C  
ATOM    124  CE1 PHE A  17       5.776 -60.483 101.691  1.00 10.10           C  
ANISOU  124  CE1 PHE A  17     1380   1249   1209     -1     34   -194       C  
ATOM    125  CE2 PHE A  17       7.525 -59.895 103.220  1.00 13.48           C  
ANISOU  125  CE2 PHE A  17     1784   1665   1673      7     52   -184       C  
ATOM    126  CZ  PHE A  17       6.558 -60.783 102.792  1.00 13.19           C  
ANISOU  126  CZ  PHE A  17     1760   1629   1624      1     38   -193       C  
ATOM    127  N   SER A  18       8.577 -55.057  98.886  1.00  6.68           N  
ANISOU  127  N   SER A  18      936    846    755     34    117   -137       N  
ATOM    128  CA  SER A  18       8.618 -53.792  98.172  1.00  7.73           C  
ANISOU  128  CA  SER A  18     1069    987    881     38    129   -118       C  
ATOM    129  C   SER A  18      10.015 -53.216  98.226  1.00  5.48           C  
ANISOU  129  C   SER A  18      773    695    615     43    153   -110       C  
ATOM    130  O   SER A  18      10.531 -52.910  99.300  1.00  8.71           O  
ANISOU  130  O   SER A  18     1165   1092   1053     39    153   -109       O  
ATOM    131  CB  SER A  18       7.614 -52.802  98.762  1.00 10.63           C  
ANISOU  131  CB  SER A  18     1428   1356   1256     33    115   -105       C  
ATOM    132  OG  SER A  18       7.636 -51.560  98.075  1.00 10.22           O  
ANISOU  132  OG  SER A  18     1375   1308   1199     38    126    -84       O  
ATOM    133  N   SER A  19      10.636 -53.089  97.064  1.00  7.90           N  
ANISOU  133  N   SER A  19     1088   1009    906     51    174   -104       N  
ATOM    134  CA  SER A  19      11.921 -52.406  96.980  1.00  6.95           C  
ANISOU  134  CA  SER A  19      955    883    804     55    199    -92       C  
ATOM    135  C   SER A  19      12.087 -51.862  95.586  1.00 12.37           C  
ANISOU  135  C   SER A  19     1652   1581   1466     63    219    -77       C  
ATOM    136  O   SER A  19      11.215 -52.025  94.737  1.00 11.80           O  
ANISOU  136  O   SER A  19     1599   1523   1361     65    211    -77       O  
ATOM    137  CB  SER A  19      13.083 -53.344  97.338  1.00 11.80           C  
ANISOU  137  CB  SER A  19     1561   1487   1434     59    210   -106       C  
ATOM    138  OG  SER A  19      13.215 -54.409  96.413  1.00 12.79           O  
ANISOU  138  OG  SER A  19     1704   1619   1534     67    218   -120       O  
ATOM    139  N   LYS A  20      13.209 -51.202  95.355  1.00 11.19           N  
ANISOU  139  N   LYS A  20     1491   1428   1332     67    245    -63       N  
ATOM    140  CA  LYS A  20      13.535 -50.712  94.030  1.00 15.45           C  
ANISOU  140  CA  LYS A  20     2041   1981   1849     75    268    -46       C  
ATOM    141  C   LYS A  20      14.795 -51.382  93.543  1.00 12.98           C  
ANISOU  141  C   LYS A  20     1727   1669   1536     84    296    -53       C  
ATOM    142  O   LYS A  20      15.787 -51.436  94.270  1.00 14.69           O  
ANISOU  142  O   LYS A  20     1924   1873   1786     82    304    -55       O  
ATOM    143  CB  LYS A  20      13.709 -49.198  94.042  1.00 15.76           C  
ANISOU  143  CB  LYS A  20     2067   2014   1907     72    279    -18       C  
ATOM    144  CG  LYS A  20      12.386 -48.457  94.015  1.00 17.94           C  
ANISOU  144  CG  LYS A  20     2350   2294   2173     68    258     -7       C  
ATOM    145  CD  LYS A  20      12.609 -46.973  93.866  1.00 19.67           C  
ANISOU  145  CD  LYS A  20     2558   2506   2410     67    272     23       C  
ATOM    146  CE  LYS A  20      11.297 -46.260  93.638  1.00 25.57           C  
ANISOU  146  CE  LYS A  20     3314   3259   3143     67    255     37       C  
ATOM    147  NZ  LYS A  20      11.525 -44.810  93.396  1.00 30.57           N  
ANISOU  147  NZ  LYS A  20     3938   3882   3794     67    269     67       N  
ATOM    148  N   ASP A  21      14.761 -51.904  92.321  1.00 14.27           N  
ANISOU  148  N   ASP A  21     1911   1848   1662     94    308    -57       N  
ATOM    149  CA  ASP A  21      15.955 -52.540  91.761  1.00 15.90           C  
ANISOU  149  CA  ASP A  21     2117   2057   1867    105    335    -63       C  
ATOM    150  C   ASP A  21      16.959 -51.506  91.229  1.00 12.17           C  
ANISOU  150  C   ASP A  21     1630   1587   1407    108    364    -35       C  
ATOM    151  O   ASP A  21      16.773 -50.294  91.402  1.00 15.95           O  
ANISOU  151  O   ASP A  21     2100   2062   1898    103    370    -12       O  
ATOM    152  CB  ASP A  21      15.569 -53.562  90.675  1.00 13.43           C  
ANISOU  152  CB  ASP A  21     1829   1760   1513    112    328    -81       C  
ATOM    153  CG  ASP A  21      14.999 -52.930  89.391  1.00 14.34           C  
ANISOU  153  CG  ASP A  21     1964   1897   1588    116    334    -65       C  
ATOM    154  OD1 ASP A  21      15.085 -51.704  89.173  1.00 15.55           O  
ANISOU  154  OD1 ASP A  21     2110   2053   1744    115    348    -36       O  
ATOM    155  OD2 ASP A  21      14.481 -53.707  88.560  1.00 16.75           O  
ANISOU  155  OD2 ASP A  21     2290   2216   1857    119    323    -81       O  
ATOM    156  N   ALA A  22      18.019 -51.989  90.581  1.00 13.46           N  
ANISOU  156  N   ALA A  22     1789   1756   1570    115    381    -37       N  
ATOM    157  CA  ALA A  22      19.108 -51.123  90.128  1.00 14.98           C  
ANISOU  157  CA  ALA A  22     1964   1949   1778    117    409    -12       C  
ATOM    158  C   ALA A  22      18.674 -50.100  89.084  1.00 18.15           C  
ANISOU  158  C   ALA A  22     2378   2365   2154    118    420     14       C  
ATOM    159  O   ALA A  22      19.347 -49.089  88.896  1.00 20.49           O  
ANISOU  159  O   ALA A  22     2659   2658   2470    116    439     41       O  
ATOM    160  CB  ALA A  22      20.266 -51.973  89.582  1.00 21.64           C  
ANISOU  160  CB  ALA A  22     2803   2797   2622    126    425    -21       C  
ATOM    161  N   LYS A  23      17.550 -50.348  88.415  1.00 15.72           N  
ANISOU  161  N   LYS A  23     2097   2073   1803    121    406      8       N  
ATOM    162  CA  LYS A  23      17.023 -49.388  87.444  1.00 16.68           C  
ANISOU  162  CA  LYS A  23     2231   2209   1897    123    412     35       C  
ATOM    163  C   LYS A  23      15.927 -48.513  88.036  1.00 16.87           C  
ANISOU  163  C   LYS A  23     2256   2226   1926    117    396     49       C  
ATOM    164  O   LYS A  23      15.276 -47.756  87.320  1.00 15.22           O  
ANISOU  164  O   LYS A  23     2059   2030   1694    119    396     72       O  
ATOM    165  CB  LYS A  23      16.483 -50.112  86.215  1.00 16.85           C  
ANISOU  165  CB  LYS A  23     2281   2255   1867    131    406     22       C  
ATOM    166  CG  LYS A  23      17.534 -50.914  85.460  1.00 15.89           C  
ANISOU  166  CG  LYS A  23     2160   2141   1736    139    425      9       C  
ATOM    167  CD  LYS A  23      16.980 -51.444  84.150  1.00 21.54           C  
ANISOU  167  CD  LYS A  23     2903   2881   2399    145    421     -1       C  
ATOM    168  CE  LYS A  23      17.986 -52.346  83.462  1.00 26.14           C  
ANISOU  168  CE  LYS A  23     3489   3471   2974    154    440    -18       C  
ATOM    169  NZ  LYS A  23      19.275 -51.637  83.290  1.00 27.41           N  
ANISOU  169  NZ  LYS A  23     3627   3628   3158    157    472      7       N  
ATOM    170  N   GLY A  24      15.718 -48.636  89.341  1.00 14.37           N  
ANISOU  170  N   GLY A  24     1928   1892   1640    109    383     36       N  
ATOM    171  CA  GLY A  24      14.719 -47.841  90.032  1.00 16.42           C  
ANISOU  171  CA  GLY A  24     2182   2143   1915    100    357     45       C  
ATOM    172  C   GLY A  24      13.302 -48.368  89.906  1.00 13.43           C  
ANISOU  172  C   GLY A  24     1824   1776   1504     99    325     31       C  
ATOM    173  O   GLY A  24      12.351 -47.682  90.290  1.00 15.95           O  
ANISOU  173  O   GLY A  24     2141   2091   1830     93    303     41       O  
ATOM    174  N   GLU A  25      13.149 -49.578  89.373  1.00 11.81           N  
ANISOU  174  N   GLU A  25     1639   1583   1265    105    321      7       N  
ATOM    175  CA  GLU A  25      11.823 -50.164  89.202  1.00 11.09           C  
ANISOU  175  CA  GLU A  25     1566   1504   1144    103    289     -8       C  
ATOM    176  C   GLU A  25      11.292 -50.716  90.522  1.00 13.68           C  
ANISOU  176  C   GLU A  25     1883   1815   1499     92    261    -30       C  
ATOM    177  O   GLU A  25      12.038 -51.305  91.302  1.00 10.84           O  
ANISOU  177  O   GLU A  25     1512   1440   1166     90    266    -46       O  
ATOM    178  CB  GLU A  25      11.864 -51.264  88.141  1.00 11.91           C  
ANISOU  178  CB  GLU A  25     1696   1626   1203    112    295    -28       C  
ATOM    179  CG  GLU A  25      12.357 -50.744  86.802  1.00 17.88           C  
ANISOU  179  CG  GLU A  25     2461   2401   1934    120    317     -7       C  
ATOM    180  CD  GLU A  25      12.573 -51.834  85.763  1.00 18.99           C  
ANISOU  180  CD  GLU A  25     2618   2556   2042    124    317    -30       C  
ATOM    181  OE1 GLU A  25      13.553 -51.721  85.003  1.00 16.80           O  
ANISOU  181  OE1 GLU A  25     2338   2286   1761    130    342    -22       O  
ATOM    182  OE2 GLU A  25      11.770 -52.787  85.693  1.00 24.54           O  
ANISOU  182  OE2 GLU A  25     3336   3264   2725    120    291    -57       O  
ATOM    183  N   PHE A  26      10.004 -50.499  90.777  1.00 11.37           N  
ANISOU  183  N   PHE A  26     1593   1525   1201     86    231    -28       N  
ATOM    184  CA  PHE A  26       9.332 -51.107  91.925  1.00 12.10           C  
ANISOU  184  CA  PHE A  26     1678   1606   1312     76    204    -47       C  
ATOM    185  C   PHE A  26       9.222 -52.623  91.751  1.00 11.91           C  
ANISOU  185  C   PHE A  26     1670   1586   1270     76    194    -78       C  
ATOM    186  O   PHE A  26       8.663 -53.096  90.763  1.00 13.04           O  
ANISOU  186  O   PHE A  26     1834   1745   1374     79    187    -85       O  
ATOM    187  CB  PHE A  26       7.924 -50.542  92.111  1.00  9.17           C  
ANISOU  187  CB  PHE A  26     1307   1241    938     71    177    -36       C  
ATOM    188  CG  PHE A  26       7.862 -49.090  92.511  1.00 10.92           C  
ANISOU  188  CG  PHE A  26     1511   1453   1184     70    182     -9       C  
ATOM    189  CD1 PHE A  26       7.969 -48.084  91.561  1.00 17.26           C  
ANISOU  189  CD1 PHE A  26     2319   2265   1973     77    197     19       C  
ATOM    190  CD2 PHE A  26       7.607 -48.735  93.829  1.00 14.77           C  
ANISOU  190  CD2 PHE A  26     1981   1924   1707     63    170    -12       C  
ATOM    191  CE1 PHE A  26       7.873 -46.735  91.932  1.00 18.54           C  
ANISOU  191  CE1 PHE A  26     2466   2416   2162     77    201     44       C  
ATOM    192  CE2 PHE A  26       7.503 -47.396  94.211  1.00 15.95           C  
ANISOU  192  CE2 PHE A  26     2117   2063   1881     62    175     10       C  
ATOM    193  CZ  PHE A  26       7.636 -46.395  93.262  1.00 13.70           C  
ANISOU  193  CZ  PHE A  26     1836   1784   1586     69    190     38       C  
ATOM    194  N   ILE A  27       9.745 -53.383  92.710  1.00  9.32           N  
ANISOU  194  N   ILE A  27     1332   1242    968     72    193    -97       N  
ATOM    195  CA  ILE A  27       9.711 -54.837  92.628  1.00  8.54           C  
ANISOU  195  CA  ILE A  27     1247   1141    858     72    185   -126       C  
ATOM    196  C   ILE A  27       9.320 -55.455  93.962  1.00 10.21           C  
ANISOU  196  C   ILE A  27     1446   1336   1097     62    164   -139       C  
ATOM    197  O   ILE A  27       9.538 -54.869  95.031  1.00 12.37           O  
ANISOU  197  O   ILE A  27     1699   1598   1402     58    163   -129       O  
ATOM    198  CB  ILE A  27      11.072 -55.433  92.192  1.00 14.48           C  
ANISOU  198  CB  ILE A  27     2003   1890   1610     83    215   -136       C  
ATOM    199  CG1 ILE A  27      12.185 -54.991  93.150  1.00 14.50           C  
ANISOU  199  CG1 ILE A  27     1979   1876   1654     83    231   -127       C  
ATOM    200  CG2 ILE A  27      11.397 -55.044  90.752  1.00 14.52           C  
ANISOU  200  CG2 ILE A  27     2025   1914   1580     94    238   -126       C  
ATOM    201  CD1 ILE A  27      13.461 -55.842  93.042  1.00 14.96           C  
ANISOU  201  CD1 ILE A  27     2034   1926   1723     93    254   -140       C  
ATOM    202  N   GLY A  28       8.729 -56.641  93.898  1.00  9.39           N  
ANISOU  202  N   GLY A  28     1356   1231    981     58    146   -161       N  
ATOM    203  CA  GLY A  28       8.363 -57.352  95.104  1.00  9.91           C  
ANISOU  203  CA  GLY A  28     1411   1282   1071     49    127   -173       C  
ATOM    204  C   GLY A  28       6.960 -57.923  95.077  1.00  9.26           C  
ANISOU  204  C   GLY A  28     1338   1205    975     38     97   -182       C  
ATOM    205  O   GLY A  28       6.142 -57.585  94.216  1.00 11.20           O  
ANISOU  205  O   GLY A  28     1595   1467   1192     37     86   -177       O  
ATOM    206  N   PHE A  29       6.680 -58.781  96.045  1.00 10.85           N  
ANISOU  206  N   PHE A  29     1533   1392   1196     30     82   -194       N  
ATOM    207  CA  PHE A  29       5.388 -59.437  96.131  1.00  9.67           C  
ANISOU  207  CA  PHE A  29     1390   1246   1040     18     53   -203       C  
ATOM    208  C   PHE A  29       4.237 -58.441  96.351  1.00  9.33           C  
ANISOU  208  C   PHE A  29     1335   1214    994     12     37   -184       C  
ATOM    209  O   PHE A  29       3.135 -58.657  95.853  1.00  9.15           O  
ANISOU  209  O   PHE A  29     1320   1202    953      5     16   -186       O  
ATOM    210  CB  PHE A  29       5.412 -60.477  97.248  1.00  9.04           C  
ANISOU  210  CB  PHE A  29     1303   1147    986     11     44   -215       C  
ATOM    211  CG  PHE A  29       4.214 -61.384  97.261  1.00  9.05           C  
ANISOU  211  CG  PHE A  29     1311   1147    982     -2     17   -227       C  
ATOM    212  CD1 PHE A  29       3.762 -61.978  96.088  1.00 12.59           C  
ANISOU  212  CD1 PHE A  29     1778   1603   1404     -3      7   -241       C  
ATOM    213  CD2 PHE A  29       3.562 -61.669  98.453  1.00 10.47           C  
ANISOU  213  CD2 PHE A  29     1475   1318   1184    -12      2   -222       C  
ATOM    214  CE1 PHE A  29       2.667 -62.815  96.101  1.00 12.91           C  
ANISOU  214  CE1 PHE A  29     1818   1642   1445    -16    -19   -250       C  
ATOM    215  CE2 PHE A  29       2.463 -62.515  98.475  1.00 11.27           C  
ANISOU  215  CE2 PHE A  29     1580   1418   1284    -26    -22   -231       C  
ATOM    216  CZ  PHE A  29       2.019 -63.088  97.296  1.00 12.28           C  
ANISOU  216  CZ  PHE A  29     1725   1551   1389    -28    -34   -245       C  
ATOM    217  N   ASP A  30       4.484 -57.370  97.106  1.00  8.56           N  
ANISOU  217  N   ASP A  30     1220   1115    917     15     46   -165       N  
ATOM    218  CA  ASP A  30       3.488 -56.298  97.242  1.00  9.22           C  
ANISOU  218  CA  ASP A  30     1294   1209   1000     12     35   -146       C  
ATOM    219  C   ASP A  30       3.158 -55.660  95.896  1.00  7.39           C  
ANISOU  219  C   ASP A  30     1074    995    738     18     36   -135       C  
ATOM    220  O   ASP A  30       1.982 -55.402  95.569  1.00  9.89           O  
ANISOU  220  O   ASP A  30     1391   1325   1043     14     16   -128       O  
ATOM    221  CB  ASP A  30       3.984 -55.202  98.189  1.00  8.78           C  
ANISOU  221  CB  ASP A  30     1219   1145    970     15     47   -131       C  
ATOM    222  CG  ASP A  30       3.631 -55.466  99.633  1.00 12.73           C  
ANISOU  222  CG  ASP A  30     1706   1636   1497      8     37   -134       C  
ATOM    223  OD1 ASP A  30       2.892 -56.432  99.924  1.00  9.62           O  
ANISOU  223  OD1 ASP A  30     1312   1241   1101      0     19   -144       O  
ATOM    224  OD2 ASP A  30       4.089 -54.677 100.476  1.00  9.64           O  
ANISOU  224  OD2 ASP A  30     1301   1237   1126     10     46   -126       O  
ATOM    225  N   ILE A  31       4.206 -55.383  95.129  1.00  6.71           N  
ANISOU  225  N   ILE A  31      997    911    641     28     59   -133       N  
ATOM    226  CA  ILE A  31       4.058 -54.753  93.822  1.00  9.67           C  
ANISOU  226  CA  ILE A  31     1385   1305    985     35     64   -121       C  
ATOM    227  C   ILE A  31       3.276 -55.684  92.889  1.00 12.26           C  
ANISOU  227  C   ILE A  31     1732   1646   1279     30     44   -137       C  
ATOM    228  O   ILE A  31       2.356 -55.244  92.200  1.00 11.53           O  
ANISOU  228  O   ILE A  31     1645   1571   1165     30     28   -125       O  
ATOM    229  CB  ILE A  31       5.432 -54.387  93.214  1.00 11.18           C  
ANISOU  229  CB  ILE A  31     1582   1495   1171     46     96   -115       C  
ATOM    230  CG1 ILE A  31       6.309 -53.675  94.259  1.00 13.22           C  
ANISOU  230  CG1 ILE A  31     1819   1736   1467     47    113   -105       C  
ATOM    231  CG2 ILE A  31       5.255 -53.547  91.950  1.00 10.73           C  
ANISOU  231  CG2 ILE A  31     1536   1457   1083     54    103    -96       C  
ATOM    232  CD1 ILE A  31       5.693 -52.415  94.870  1.00  9.78           C  
ANISOU  232  CD1 ILE A  31     1367   1298   1050     45    106    -83       C  
ATOM    233  N   ASP A  32       3.632 -56.971  92.884  1.00  8.63           N  
ANISOU  233  N   ASP A  32     1285   1178    817     27     43   -163       N  
ATOM    234  CA  ASP A  32       2.887 -57.976  92.116  1.00 12.38           C  
ANISOU  234  CA  ASP A  32     1779   1662   1264     21     21   -184       C  
ATOM    235  C   ASP A  32       1.401 -58.045  92.507  1.00 14.14           C  
ANISOU  235  C   ASP A  32     1992   1889   1492      7    -13   -180       C  
ATOM    236  O   ASP A  32       0.520 -58.067  91.637  1.00 11.06           O  
ANISOU  236  O   ASP A  32     1612   1517   1073      3    -33   -180       O  
ATOM    237  CB  ASP A  32       3.507 -59.367  92.295  1.00 13.43           C  
ANISOU  237  CB  ASP A  32     1922   1776   1403     19     25   -213       C  
ATOM    238  CG  ASP A  32       4.942 -59.446  91.803  1.00 14.50           C  
ANISOU  238  CG  ASP A  32     2064   1910   1537     33     58   -218       C  
ATOM    239  OD1 ASP A  32       5.357 -58.569  91.027  1.00 15.00           O  
ANISOU  239  OD1 ASP A  32     2133   1986   1578     44     76   -203       O  
ATOM    240  OD2 ASP A  32       5.659 -60.400  92.186  1.00 16.85           O  
ANISOU  240  OD2 ASP A  32     2356   2191   1856     34     66   -234       O  
ATOM    241  N   LEU A  33       1.124 -58.119  93.808  1.00 11.30           N  
ANISOU  241  N   LEU A  33     1612   1515   1166      0    -19   -177       N  
ATOM    242  CA  LEU A  33      -0.261 -58.174  94.280  1.00  8.72           C  
ANISOU  242  CA  LEU A  33     1272   1192    848    -12    -47   -171       C  
ATOM    243  C   LEU A  33      -1.019 -56.927  93.876  1.00  9.57           C  
ANISOU  243  C   LEU A  33     1372   1320    946     -8    -54   -145       C  
ATOM    244  O   LEU A  33      -2.133 -57.017  93.368  1.00  9.34           O  
ANISOU  244  O   LEU A  33     1344   1305    901    -15    -79   -143       O  
ATOM    245  CB  LEU A  33      -0.326 -58.339  95.801  1.00  8.06           C  
ANISOU  245  CB  LEU A  33     1169   1093    803    -19    -47   -169       C  
ATOM    246  CG  LEU A  33       0.001 -59.735  96.323  1.00  8.92           C  
ANISOU  246  CG  LEU A  33     1282   1183    925    -26    -50   -192       C  
ATOM    247  CD1 LEU A  33       0.257 -59.688  97.831  1.00 12.70           C  
ANISOU  247  CD1 LEU A  33     1741   1646   1438    -28    -43   -185       C  
ATOM    248  CD2 LEU A  33      -1.119 -60.715  95.974  1.00 15.77           C  
ANISOU  248  CD2 LEU A  33     2155   2053   1783    -41    -79   -206       C  
ATOM    249  N   GLY A  34      -0.413 -55.767  94.124  1.00  9.48           N  
ANISOU  249  N   GLY A  34     1351   1306    945      3    -33   -125       N  
ATOM    250  CA  GLY A  34      -1.036 -54.505  93.766  1.00  8.12           C  
ANISOU  250  CA  GLY A  34     1171   1148    767      9    -36    -99       C  
ATOM    251  C   GLY A  34      -1.336 -54.437  92.282  1.00 13.24           C  
ANISOU  251  C   GLY A  34     1838   1818   1374     13    -45    -95       C  
ATOM    252  O   GLY A  34      -2.460 -54.150  91.867  1.00 13.07           O  
ANISOU  252  O   GLY A  34     1812   1813   1340     10    -68    -83       O  
ATOM    253  N   ASN A  35      -0.327 -54.719  91.471  1.00 10.79           N  
ANISOU  253  N   ASN A  35     1548   1510   1042     20    -27   -105       N  
ATOM    254  CA  ASN A  35      -0.504 -54.666  90.025  1.00 11.91           C  
ANISOU  254  CA  ASN A  35     1710   1674   1139     24    -32   -102       C  
ATOM    255  C   ASN A  35      -1.555 -55.648  89.523  1.00 14.38           C  
ANISOU  255  C   ASN A  35     2033   1999   1430     12    -66   -121       C  
ATOM    256  O   ASN A  35      -2.366 -55.314  88.656  1.00 13.56           O  
ANISOU  256  O   ASN A  35     1935   1918   1298     13    -85   -109       O  
ATOM    257  CB  ASN A  35       0.833 -54.916  89.319  1.00  9.26           C  
ANISOU  257  CB  ASN A  35     1395   1338    785     34     -3   -112       C  
ATOM    258  CG  ASN A  35       1.747 -53.698  89.353  1.00 13.20           C  
ANISOU  258  CG  ASN A  35     1886   1835   1296     47     29    -86       C  
ATOM    259  OD1 ASN A  35       1.278 -52.566  89.468  1.00 13.14           O  
ANISOU  259  OD1 ASN A  35     1865   1831   1298     50     26    -58       O  
ATOM    260  ND2 ASN A  35       3.056 -53.925  89.227  1.00 14.78           N  
ANISOU  260  ND2 ASN A  35     2093   2026   1498     54     58    -95       N  
ATOM    261  N   GLU A  36      -1.548 -56.858  90.070  1.00 12.53           N  
ANISOU  261  N   GLU A  36     1801   1750   1209      1    -74   -149       N  
ATOM    262  CA  GLU A  36      -2.522 -57.864  89.669  1.00 13.99           C  
ANISOU  262  CA  GLU A  36     1995   1943   1378    -13   -107   -169       C  
ATOM    263  C   GLU A  36      -3.950 -57.447  90.058  1.00 15.84           C  
ANISOU  263  C   GLU A  36     2207   2187   1626    -22   -137   -150       C  
ATOM    264  O   GLU A  36      -4.893 -57.613  89.280  1.00 13.55           O  
ANISOU  264  O   GLU A  36     1922   1916   1311    -29   -165   -151       O  
ATOM    265  CB  GLU A  36      -2.162 -59.223  90.281  1.00  9.14           C  
ANISOU  265  CB  GLU A  36     1384   1305    785    -23   -106   -199       C  
ATOM    266  CG  GLU A  36      -3.100 -60.368  89.871  1.00 10.88           C  
ANISOU  266  CG  GLU A  36     1601   1530   1004    -42   -133   -218       C  
ATOM    267  CD  GLU A  36      -3.067 -60.671  88.380  1.00 17.08           C  
ANISOU  267  CD  GLU A  36     2402   2334   1752    -41   -135   -228       C  
ATOM    268  OE1 GLU A  36      -2.098 -60.273  87.681  1.00 16.58           O  
ANISOU  268  OE1 GLU A  36     2355   2278   1668    -28   -110   -226       O  
ATOM    269  OE2 GLU A  36      -4.020 -61.327  87.915  1.00 15.40           O  
ANISOU  269  OE2 GLU A  36     2186   2132   1533    -55   -161   -240       O  
ATOM    270  N   MET A  37      -4.122 -56.895  91.251  1.00 11.89           N  
ANISOU  270  N   MET A  37     1681   1674   1163    -22   -130   -134       N  
ATOM    271  CA  MET A  37      -5.453 -56.457  91.663  1.00 11.75           C  
ANISOU  271  CA  MET A  37     1640   1665   1160    -29   -154   -116       C  
ATOM    272  C   MET A  37      -5.931 -55.292  90.801  1.00 14.67           C  
ANISOU  272  C   MET A  37     2009   2058   1509    -18   -160    -88       C  
ATOM    273  O   MET A  37      -7.072 -55.284  90.334  1.00 14.87           O  
ANISOU  273  O   MET A  37     2027   2101   1521    -24   -189    -80       O  
ATOM    274  CB  MET A  37      -5.473 -56.074  93.150  1.00 11.25           C  
ANISOU  274  CB  MET A  37     1551   1584   1139    -29   -142   -105       C  
ATOM    275  CG  MET A  37      -5.338 -57.279  94.095  1.00 11.91           C  
ANISOU  275  CG  MET A  37     1632   1648   1247    -41   -144   -128       C  
ATOM    276  SD  MET A  37      -5.453 -56.843  95.855  1.00 10.63           S  
ANISOU  276  SD  MET A  37     1442   1469   1130    -41   -132   -115       S  
ATOM    277  CE  MET A  37      -3.963 -55.856  96.033  1.00  8.20           C  
ANISOU  277  CE  MET A  37     1139   1151    825    -24    -95   -107       C  
ATOM    278  N   CYS A  38      -5.055 -54.322  90.568  1.00 13.47           N  
ANISOU  278  N   CYS A  38     1861   1905   1351     -2   -132    -71       N  
ATOM    279  CA  CYS A  38      -5.414 -53.184  89.726  1.00 11.62           C  
ANISOU  279  CA  CYS A  38     1626   1691   1097     10   -135    -42       C  
ATOM    280  C   CYS A  38      -5.822 -53.629  88.325  1.00 14.93           C  
ANISOU  280  C   CYS A  38     2067   2136   1469      7   -157    -48       C  
ATOM    281  O   CYS A  38      -6.772 -53.101  87.754  1.00 15.61           O  
ANISOU  281  O   CYS A  38     2147   2243   1540      9   -180    -28       O  
ATOM    282  CB  CYS A  38      -4.262 -52.199  89.641  1.00 12.18           C  
ANISOU  282  CB  CYS A  38     1703   1755   1172     25   -100    -25       C  
ATOM    283  SG  CYS A  38      -3.935 -51.390  91.225  1.00 17.45           S  
ANISOU  283  SG  CYS A  38     2343   2395   1893     29    -78    -13       S  
ATOM    284  N   LYS A  39      -5.101 -54.604  87.779  1.00 13.45           N  
ANISOU  284  N   LYS A  39     1905   1947   1257      4   -152    -77       N  
ATOM    285  CA  LYS A  39      -5.469 -55.170  86.486  1.00 17.19           C  
ANISOU  285  CA  LYS A  39     2402   2444   1683      0   -174    -90       C  
ATOM    286  C   LYS A  39      -6.914 -55.683  86.494  1.00 16.19           C  
ANISOU  286  C   LYS A  39     2264   2325   1564    -19   -216    -93       C  
ATOM    287  O   LYS A  39      -7.708 -55.366  85.603  1.00 16.24           O  
ANISOU  287  O   LYS A  39     2273   2349   1549    -20   -238    -78       O  
ATOM    288  CB  LYS A  39      -4.505 -56.294  86.104  1.00 15.38           C  
ANISOU  288  CB  LYS A  39     2195   2202   1446     -8   -156   -123       C  
ATOM    289  CG  LYS A  39      -4.977 -57.121  84.918  1.00 16.05           C  
ANISOU  289  CG  LYS A  39     2293   2303   1502    -24   -175   -139       C  
ATOM    290  CD  LYS A  39      -3.838 -57.917  84.314  1.00 27.87           C  
ANISOU  290  CD  LYS A  39     3810   3795   2986    -22   -149   -166       C  
ATOM    291  CE  LYS A  39      -3.458 -59.094  85.176  1.00 25.02           C  
ANISOU  291  CE  LYS A  39     3441   3408   2656    -30   -142   -197       C  
ATOM    292  NZ  LYS A  39      -2.212 -59.762  84.686  1.00 17.66           N  
ANISOU  292  NZ  LYS A  39     2526   2469   1717    -23   -113   -220       N  
ATOM    293  N   ARG A  40      -7.262 -56.459  87.512  1.00 13.64           N  
ANISOU  293  N   ARG A  40     1926   1984   1272    -32   -226   -111       N  
ATOM    294  CA  ARG A  40      -8.592 -57.047  87.590  1.00 14.10           C  
ANISOU  294  CA  ARG A  40     1968   2045   1344    -43   -262   -116       C  
ATOM    295  C   ARG A  40      -9.662 -56.006  87.909  1.00 19.79           C  
ANISOU  295  C   ARG A  40     2660   2781   2077    -43   -279    -81       C  
ATOM    296  O   ARG A  40     -10.820 -56.150  87.502  1.00 18.59           O  
ANISOU  296  O   ARG A  40     2497   2639   1926    -48   -310    -76       O  
ATOM    297  CB  ARG A  40      -8.605 -58.172  88.622  1.00 14.41           C  
ANISOU  297  CB  ARG A  40     1994   2062   1418    -58   -262   -142       C  
ATOM    298  CG  ARG A  40      -7.742 -59.354  88.179  1.00 16.11           C  
ANISOU  298  CG  ARG A  40     2226   2269   1625    -63   -246   -176       C  
ATOM    299  CD  ARG A  40      -7.599 -60.405  89.248  1.00 20.71           C  
ANISOU  299  CD  ARG A  40     2800   2824   2245    -75   -241   -196       C  
ATOM    300  NE  ARG A  40      -6.697 -61.471  88.813  1.00 20.76           N  
ANISOU  300  NE  ARG A  40     2824   2819   2245    -78   -224   -226       N  
ATOM    301  CZ  ARG A  40      -7.065 -62.732  88.627  1.00 20.17           C  
ANISOU  301  CZ  ARG A  40     2749   2737   2179    -91   -237   -251       C  
ATOM    302  NH1 ARG A  40      -8.317 -63.099  88.852  1.00 20.21           N  
ANISOU  302  NH1 ARG A  40     2734   2744   2199   -104   -266   -250       N  
ATOM    303  NH2 ARG A  40      -6.173 -63.629  88.230  1.00 19.00           N  
ANISOU  303  NH2 ARG A  40     2617   2577   2025    -91   -219   -276       N  
ATOM    304  N   MET A  41      -9.270 -54.956  88.625  1.00 17.91           N  
ANISOU  304  N   MET A  41     2407   2537   1860    -31   -253    -57       N  
ATOM    305  CA  MET A  41     -10.178 -53.848  88.921  1.00 18.83           C  
ANISOU  305  CA  MET A  41     2496   2663   1996    -23   -261    -22       C  
ATOM    306  C   MET A  41     -10.340 -52.941  87.707  1.00 22.39           C  
ANISOU  306  C   MET A  41     2955   3140   2411     -9   -268      4       C  
ATOM    307  O   MET A  41     -11.234 -52.098  87.668  1.00 15.29           O  
ANISOU  307  O   MET A  41     2036   2254   1521     -3   -282     33       O  
ATOM    308  CB  MET A  41      -9.663 -53.039  90.113  1.00 16.26           C  
ANISOU  308  CB  MET A  41     2154   2316   1710    -12   -229     -8       C  
ATOM    309  CG  MET A  41      -9.535 -53.854  91.391  1.00 12.69           C  
ANISOU  309  CG  MET A  41     1690   1839   1291    -24   -222    -29       C  
ATOM    310  SD  MET A  41      -8.265 -53.199  92.500  1.00 14.70           S  
ANISOU  310  SD  MET A  41     1943   2068   1577    -12   -179    -26       S  
ATOM    311  CE  MET A  41      -9.018 -51.637  92.973  1.00 18.06           C  
ANISOU  311  CE  MET A  41     2340   2495   2026      3   -174     12       C  
ATOM    312  N   GLN A  42      -9.461 -53.131  86.727  1.00 20.98           N  
ANISOU  312  N   GLN A  42     2809   2970   2194     -4   -257     -7       N  
ATOM    313  CA  GLN A  42      -9.409 -52.304  85.527  1.00 20.73           C  
ANISOU  313  CA  GLN A  42     2790   2960   2125     10   -258     17       C  
ATOM    314  C   GLN A  42      -9.301 -50.831  85.860  1.00 22.74           C  
ANISOU  314  C   GLN A  42     3028   3212   2401     28   -237     57       C  
ATOM    315  O   GLN A  42     -10.021 -49.996  85.307  1.00 26.51           O  
ANISOU  315  O   GLN A  42     3496   3708   2868     37   -252     88       O  
ATOM    316  CB  GLN A  42     -10.625 -52.567  84.650  1.00 22.34           C  
ANISOU  316  CB  GLN A  42     2996   3176   2316      3   -297     20       C  
ATOM    317  CG  GLN A  42     -10.812 -54.036  84.354  1.00 21.88           C  
ANISOU  317  CG  GLN A  42     2955   3108   2251    -13   -317    -21       C  
ATOM    318  CD  GLN A  42     -11.544 -54.263  83.060  1.00 24.77           C  
ANISOU  318  CD  GLN A  42     3337   3489   2587    -13   -347    -22       C  
ATOM    319  OE1 GLN A  42     -10.933 -54.575  82.035  1.00 23.81           O  
ANISOU  319  OE1 GLN A  42     3250   3369   2430    -12   -341    -34       O  
ATOM    320  NE2 GLN A  42     -12.861 -54.106  83.093  1.00 23.46           N  
ANISOU  320  NE2 GLN A  42     3145   3333   2436    -14   -378    -10       N  
ATOM    321  N   VAL A  43      -8.398 -50.527  86.783  1.00 19.87           N  
ANISOU  321  N   VAL A  43     2659   2821   2069     33   -202     55       N  
ATOM    322  CA  VAL A  43      -8.042 -49.159  87.101  1.00 20.40           C  
ANISOU  322  CA  VAL A  43     2715   2877   2159     50   -176     87       C  
ATOM    323  C   VAL A  43      -6.541 -49.005  86.902  1.00 18.44           C  
ANISOU  323  C   VAL A  43     2487   2618   1903     57   -139     82       C  
ATOM    324  O   VAL A  43      -5.787 -49.963  87.074  1.00 24.54           O  
ANISOU  324  O   VAL A  43     3274   3380   2672     49   -128     50       O  
ATOM    325  CB  VAL A  43      -8.421 -48.783  88.552  1.00 29.08           C  
ANISOU  325  CB  VAL A  43     3784   3953   3311     49   -170     91       C  
ATOM    326  CG1 VAL A  43      -9.925 -48.837  88.744  1.00 29.90           C  
ANISOU  326  CG1 VAL A  43     3865   4071   3426     44   -204    101       C  
ATOM    327  CG2 VAL A  43      -7.720 -49.709  89.539  1.00 27.15           C  
ANISOU  327  CG2 VAL A  43     3542   3686   3088     38   -156     58       C  
ATOM    328  N   LYS A  44      -6.112 -47.807  86.523  1.00 16.36           N  
ANISOU  328  N   LYS A  44     2225   2354   1639     73   -118    113       N  
ATOM    329  CA  LYS A  44      -4.694 -47.510  86.430  1.00 21.43           C  
ANISOU  329  CA  LYS A  44     2880   2983   2281     80    -80    113       C  
ATOM    330  C   LYS A  44      -4.160 -47.260  87.826  1.00 21.90           C  
ANISOU  330  C   LYS A  44     2921   3009   2390     78    -58    106       C  
ATOM    331  O   LYS A  44      -4.802 -46.580  88.629  1.00 19.72           O  
ANISOU  331  O   LYS A  44     2623   2722   2148     80    -63    120       O  
ATOM    332  CB  LYS A  44      -4.439 -46.296  85.537  1.00 23.05           C  
ANISOU  332  CB  LYS A  44     3090   3198   2469     96    -65    153       C  
ATOM    333  N   CYS A  45      -2.992 -47.819  88.117  1.00 17.98           N  
ANISOU  333  N   CYS A  45     2434   2498   1898     74    -35     83       N  
ATOM    334  CA  CYS A  45      -2.380 -47.628  89.419  1.00 14.53           C  
ANISOU  334  CA  CYS A  45     1982   2032   1506     72    -16     75       C  
ATOM    335  C   CYS A  45      -0.985 -47.066  89.297  1.00 17.39           C  
ANISOU  335  C   CYS A  45     2350   2381   1874     79     20     83       C  
ATOM    336  O   CYS A  45      -0.185 -47.513  88.472  1.00 23.28           O  
ANISOU  336  O   CYS A  45     3116   3137   2593     81     34     75       O  
ATOM    337  CB  CYS A  45      -2.355 -48.936  90.198  1.00 18.85           C  
ANISOU  337  CB  CYS A  45     2529   2571   2063     58    -25     39       C  
ATOM    338  SG  CYS A  45      -3.992 -49.416  90.765  1.00 19.33           S  
ANISOU  338  SG  CYS A  45     2573   2639   2134     48    -63     33       S  
ATOM    339  N   THR A  46      -0.708 -46.064  90.117  1.00 15.94           N  
ANISOU  339  N   THR A  46     2150   2177   1730     83     36     98       N  
ATOM    340  CA  THR A  46       0.611 -45.458  90.164  1.00 16.52           C  
ANISOU  340  CA  THR A  46     2224   2234   1818     87     69    106       C  
ATOM    341  C   THR A  46       1.242 -45.684  91.523  1.00 15.33           C  
ANISOU  341  C   THR A  46     2060   2058   1707     80     79     85       C  
ATOM    342  O   THR A  46       0.672 -45.314  92.549  1.00 14.96           O  
ANISOU  342  O   THR A  46     1997   1998   1690     77     70     84       O  
ATOM    343  CB  THR A  46       0.555 -43.952  89.888  1.00 18.05           C  
ANISOU  343  CB  THR A  46     2410   2422   2025     98     81    144       C  
ATOM    344  OG1 THR A  46       0.089 -43.726  88.550  1.00 19.23           O  
ANISOU  344  OG1 THR A  46     2574   2598   2136    106     74    167       O  
ATOM    345  CG2 THR A  46       1.945 -43.332  90.058  1.00 18.11           C  
ANISOU  345  CG2 THR A  46     2415   2409   2055     99    115    151       C  
ATOM    346  N   TRP A  47       2.422 -46.286  91.523  1.00 13.08           N  
ANISOU  346  N   TRP A  47     1782   1767   1420     77     98     68       N  
ATOM    347  CA  TRP A  47       3.176 -46.494  92.752  1.00 13.17           C  
ANISOU  347  CA  TRP A  47     1782   1756   1467     70    108     49       C  
ATOM    348  C   TRP A  47       3.940 -45.247  93.127  1.00 13.73           C  
ANISOU  348  C   TRP A  47     1840   1807   1569     74    131     68       C  
ATOM    349  O   TRP A  47       4.555 -44.598  92.273  1.00 17.53           O  
ANISOU  349  O   TRP A  47     2326   2291   2042     80    150     90       O  
ATOM    350  CB  TRP A  47       4.143 -47.664  92.598  1.00 12.05           C  
ANISOU  350  CB  TRP A  47     1650   1616   1314     67    118     24       C  
ATOM    351  CG  TRP A  47       3.443 -48.963  92.405  1.00 14.66           C  
ANISOU  351  CG  TRP A  47     1992   1959   1620     62     96      1       C  
ATOM    352  CD1 TRP A  47       3.149 -49.573  91.219  1.00 12.41           C  
ANISOU  352  CD1 TRP A  47     1727   1695   1294     64     88     -3       C  
ATOM    353  CD2 TRP A  47       2.929 -49.812  93.435  1.00 11.47           C  
ANISOU  353  CD2 TRP A  47     1580   1547   1231     52     77    -21       C  
ATOM    354  NE1 TRP A  47       2.498 -50.763  91.451  1.00 11.13           N  
ANISOU  354  NE1 TRP A  47     1569   1536   1123     56     65    -29       N  
ATOM    355  CE2 TRP A  47       2.352 -50.931  92.803  1.00 11.50           C  
ANISOU  355  CE2 TRP A  47     1599   1566   1205     48     58    -38       C  
ATOM    356  CE3 TRP A  47       2.922 -49.747  94.836  1.00 10.04           C  
ANISOU  356  CE3 TRP A  47     1382   1348   1085     47     74    -28       C  
ATOM    357  CZ2 TRP A  47       1.760 -51.966  93.519  1.00 13.18           C  
ANISOU  357  CZ2 TRP A  47     1809   1774   1426     38     38    -60       C  
ATOM    358  CZ3 TRP A  47       2.344 -50.773  95.540  1.00 11.78           C  
ANISOU  358  CZ3 TRP A  47     1599   1566   1310     38     55    -48       C  
ATOM    359  CH2 TRP A  47       1.765 -51.871  94.882  1.00 11.57           C  
ANISOU  359  CH2 TRP A  47     1587   1554   1257     33     38    -63       C  
ATOM    360  N   VAL A  48       3.912 -44.933  94.414  1.00 10.88           N  
ANISOU  360  N   VAL A  48     1463   1427   1244     69    128     60       N  
ATOM    361  CA  VAL A  48       4.514 -43.727  94.958  1.00 11.70           C  
ANISOU  361  CA  VAL A  48     1554   1508   1383     70    145     74       C  
ATOM    362  C   VAL A  48       5.406 -44.118  96.121  1.00 16.08           C  
ANISOU  362  C   VAL A  48     2099   2046   1965     61    150     51       C  
ATOM    363  O   VAL A  48       4.915 -44.621  97.127  1.00 11.80           O  
ANISOU  363  O   VAL A  48     1550   1499   1432     56    135     32       O  
ATOM    364  CB  VAL A  48       3.436 -42.729  95.442  1.00 13.97           C  
ANISOU  364  CB  VAL A  48     1831   1787   1688     74    133     89       C  
ATOM    365  CG1 VAL A  48       4.082 -41.499  96.055  1.00 14.33           C  
ANISOU  365  CG1 VAL A  48     1866   1807   1773     74    150     99       C  
ATOM    366  CG2 VAL A  48       2.491 -42.349  94.300  1.00 17.66           C  
ANISOU  366  CG2 VAL A  48     2307   2273   2130     83    124    114       C  
ATOM    367  N   ALA A  49       6.716 -43.920  95.989  1.00 13.96           N  
ANISOU  367  N   ALA A  49     1828   1768   1709     60    173     54       N  
ATOM    368  CA  ALA A  49       7.628 -44.313  97.056  1.00 14.51           C  
ANISOU  368  CA  ALA A  49     1887   1823   1804     52    177     33       C  
ATOM    369  C   ALA A  49       7.518 -43.342  98.215  1.00 14.52           C  
ANISOU  369  C   ALA A  49     1874   1803   1841     48    173     33       C  
ATOM    370  O   ALA A  49       7.562 -42.126  98.027  1.00 19.43           O  
ANISOU  370  O   ALA A  49     2491   2413   2480     50    183     53       O  
ATOM    371  CB  ALA A  49       9.067 -44.377  96.547  1.00 16.85           C  
ANISOU  371  CB  ALA A  49     2182   2117   2105     52    201     37       C  
ATOM    372  N   SER A  50       7.378 -43.888  99.416  1.00 13.42           N  
ANISOU  372  N   SER A  50     1728   1658   1713     42    159     10       N  
ATOM    373  CA  SER A  50       7.143 -43.075 100.598  1.00 12.64           C  
ANISOU  373  CA  SER A  50     1618   1541   1643     38    154      6       C  
ATOM    374  C   SER A  50       7.925 -43.598 101.795  1.00 15.26           C  
ANISOU  374  C   SER A  50     1940   1864   1992     30    150    -17       C  
ATOM    375  O   SER A  50       8.164 -44.799 101.927  1.00 17.75           O  
ANISOU  375  O   SER A  50     2259   2190   2295     27    145    -32       O  
ATOM    376  CB  SER A  50       5.642 -43.049 100.923  1.00 16.69           C  
ANISOU  376  CB  SER A  50     2133   2061   2147     42    136      5       C  
ATOM    377  OG  SER A  50       5.390 -42.503 102.209  1.00 22.14           O  
ANISOU  377  OG  SER A  50     2814   2738   2862     40    130     -6       O  
ATOM    378  N   ASP A  51       8.340 -42.685 102.662  1.00 14.82           N  
ANISOU  378  N   ASP A  51     1875   1790   1966     25    153    -20       N  
ATOM    379  CA  ASP A  51       8.847 -43.066 103.968  1.00 17.72           C  
ANISOU  379  CA  ASP A  51     2234   2151   2349     17    144    -42       C  
ATOM    380  C   ASP A  51       7.754 -43.821 104.720  1.00 14.56           C  
ANISOU  380  C   ASP A  51     1838   1761   1934     18    126    -56       C  
ATOM    381  O   ASP A  51       6.571 -43.499 104.585  1.00 14.73           O  
ANISOU  381  O   ASP A  51     1863   1787   1947     24    120    -49       O  
ATOM    382  CB  ASP A  51       9.287 -41.828 104.747  1.00 23.76           C  
ANISOU  382  CB  ASP A  51     2990   2893   3146     12    148    -44       C  
ATOM    383  CG  ASP A  51       9.966 -42.170 106.043  1.00 39.35           C  
ANISOU  383  CG  ASP A  51     4956   4862   5135      3    138    -66       C  
ATOM    384  OD1 ASP A  51      11.194 -42.407 106.024  1.00 46.62           O  
ANISOU  384  OD1 ASP A  51     5867   5779   6066     -3    144    -69       O  
ATOM    385  OD2 ASP A  51       9.275 -42.192 107.084  1.00 43.60           O  
ANISOU  385  OD2 ASP A  51     5495   5400   5672      3    125    -81       O  
ATOM    386  N   ALA A  52       8.144 -44.829 105.495  1.00 13.66           N  
ANISOU  386  N   ALA A  52     1721   1652   1817     13    117    -74       N  
ATOM    387  CA  ALA A  52       7.183 -45.650 106.232  1.00 15.27           C  
ANISOU  387  CA  ALA A  52     1928   1867   2008     14    101    -85       C  
ATOM    388  C   ALA A  52       6.262 -44.811 107.118  1.00 11.90           C  
ANISOU  388  C   ALA A  52     1499   1434   1590     16     95    -88       C  
ATOM    389  O   ALA A  52       5.050 -45.035 107.158  1.00 14.41           O  
ANISOU  389  O   ALA A  52     1818   1761   1894     20     87    -85       O  
ATOM    390  CB  ALA A  52       7.906 -46.675 107.071  1.00 22.36           C  
ANISOU  390  CB  ALA A  52     2822   2767   2908      8     95   -101       C  
ATOM    391  N   ASP A  53       6.839 -43.830 107.798  1.00 11.80           N  
ANISOU  391  N   ASP A  53     1479   1404   1599     13     99    -93       N  
ATOM    392  CA  ASP A  53       6.073 -43.022 108.738  1.00 14.88           C  
ANISOU  392  CA  ASP A  53     1868   1787   1998     15     95    -99       C  
ATOM    393  C   ASP A  53       5.173 -42.015 108.046  1.00 15.52           C  
ANISOU  393  C   ASP A  53     1951   1862   2082     24    102    -83       C  
ATOM    394  O   ASP A  53       4.337 -41.397 108.689  1.00 17.12           O  
ANISOU  394  O   ASP A  53     2153   2060   2291     30     99    -87       O  
ATOM    395  CB  ASP A  53       7.015 -42.304 109.702  1.00 20.75           C  
ANISOU  395  CB  ASP A  53     2606   2514   2765      8     96   -113       C  
ATOM    396  CG  ASP A  53       7.684 -43.258 110.665  1.00 31.05           C  
ANISOU  396  CG  ASP A  53     3908   3826   4065      1     86   -130       C  
ATOM    397  OD1 ASP A  53       7.049 -44.272 111.022  1.00 34.36           O  
ANISOU  397  OD1 ASP A  53     4329   4260   4465      3     77   -134       O  
ATOM    398  OD2 ASP A  53       8.842 -43.000 111.059  1.00 35.60           O  
ANISOU  398  OD2 ASP A  53     4477   4392   4658     -7     86   -138       O  
ATOM    399  N   ALA A  54       5.331 -41.863 106.735  1.00 13.27           N  
ANISOU  399  N   ALA A  54     1669   1579   1793     27    110    -64       N  
ATOM    400  CA  ALA A  54       4.518 -40.912 105.992  1.00 13.31           C  
ANISOU  400  CA  ALA A  54     1676   1580   1801     37    115    -44       C  
ATOM    401  C   ALA A  54       3.341 -41.588 105.281  1.00 12.36           C  
ANISOU  401  C   ALA A  54     1560   1481   1654     44    107    -34       C  
ATOM    402  O   ALA A  54       2.482 -40.910 104.735  1.00 11.33           O  
ANISOU  402  O   ALA A  54     1430   1351   1525     53    108    -17       O  
ATOM    403  CB  ALA A  54       5.380 -40.156 104.986  1.00 13.82           C  
ANISOU  403  CB  ALA A  54     1741   1633   1877     36    130    -26       C  
ATOM    404  N   LEU A  55       3.304 -42.918 105.292  1.00  8.20           N  
ANISOU  404  N   LEU A  55     1036    971   1108     39     97    -43       N  
ATOM    405  CA  LEU A  55       2.272 -43.646 104.548  1.00  8.09           C  
ANISOU  405  CA  LEU A  55     1026    977   1070     42     87    -35       C  
ATOM    406  C   LEU A  55       0.849 -43.347 105.017  1.00  7.37           C  
ANISOU  406  C   LEU A  55      929    890    980     49     78    -31       C  
ATOM    407  O   LEU A  55       0.019 -42.906 104.229  1.00  8.09           O  
ANISOU  407  O   LEU A  55     1020    988   1065     57     76    -13       O  
ATOM    408  CB  LEU A  55       2.523 -45.146 104.624  1.00  8.02           C  
ANISOU  408  CB  LEU A  55     1021    982   1045     35     79    -49       C  
ATOM    409  CG  LEU A  55       3.685 -45.626 103.751  1.00 10.93           C  
ANISOU  409  CG  LEU A  55     1396   1351   1405     32     87    -48       C  
ATOM    410  CD1 LEU A  55       4.023 -47.069 104.097  1.00 13.17           C  
ANISOU  410  CD1 LEU A  55     1683   1642   1679     25     80    -65       C  
ATOM    411  CD2 LEU A  55       3.336 -45.488 102.270  1.00 13.91           C  
ANISOU  411  CD2 LEU A  55     1782   1739   1763     37     90    -30       C  
ATOM    412  N   ILE A  56       0.568 -43.594 106.292  1.00  8.22           N  
ANISOU  412  N   ILE A  56     1031    997   1094     47     74    -47       N  
ATOM    413  CA  ILE A  56      -0.780 -43.373 106.814  1.00  7.34           C  
ANISOU  413  CA  ILE A  56      912    891    984     54     68    -44       C  
ATOM    414  C   ILE A  56      -1.141 -41.881 106.811  1.00  7.04           C  
ANISOU  414  C   ILE A  56      871    838    966     65     77    -33       C  
ATOM    415  O   ILE A  56      -2.242 -41.535 106.395  1.00  5.38           O  
ANISOU  415  O   ILE A  56      655    635    755     74     74    -18       O  
ATOM    416  CB  ILE A  56      -0.942 -43.990 108.218  1.00 13.31           C  
ANISOU  416  CB  ILE A  56     1664   1651   1741     49     63    -63       C  
ATOM    417  CG1 ILE A  56      -0.895 -45.520 108.083  1.00 13.85           C  
ANISOU  417  CG1 ILE A  56     1736   1735   1792     39     52    -69       C  
ATOM    418  CG2 ILE A  56      -2.250 -43.534 108.878  1.00 12.41           C  
ANISOU  418  CG2 ILE A  56     1542   1541   1634     58     63    -60       C  
ATOM    419  CD1 ILE A  56      -1.147 -46.279 109.379  1.00 14.20           C  
ANISOU  419  CD1 ILE A  56     1776   1785   1835     34     47    -82       C  
ATOM    420  N   PRO A  57      -0.211 -40.991 107.225  1.00 12.08           N  
ANISOU  420  N   PRO A  57     1511   1455   1624     64     88    -40       N  
ATOM    421  CA  PRO A  57      -0.556 -39.572 107.056  1.00 12.46           C  
ANISOU  421  CA  PRO A  57     1556   1485   1692     75     98    -28       C  
ATOM    422  C   PRO A  57      -0.886 -39.183 105.609  1.00  8.92           C  
ANISOU  422  C   PRO A  57     1109   1041   1238     82     99      1       C  
ATOM    423  O   PRO A  57      -1.847 -38.438 105.398  1.00  9.53           O  
ANISOU  423  O   PRO A  57     1181   1115   1323     95    100     16       O  
ATOM    424  CB  PRO A  57       0.703 -38.847 107.551  1.00 12.26           C  
ANISOU  424  CB  PRO A  57     1534   1436   1688     69    108    -40       C  
ATOM    425  CG  PRO A  57       1.260 -39.766 108.597  1.00 10.74           C  
ANISOU  425  CG  PRO A  57     1342   1250   1488     58    101    -64       C  
ATOM    426  CD  PRO A  57       0.987 -41.168 108.074  1.00 12.09           C  
ANISOU  426  CD  PRO A  57     1515   1447   1633     54     91    -60       C  
ATOM    427  N   SER A  58      -0.137 -39.692 104.635  1.00  8.49           N  
ANISOU  427  N   SER A  58     1062    995   1170     76    100      8       N  
ATOM    428  CA  SER A  58      -0.412 -39.369 103.237  1.00  7.66           C  
ANISOU  428  CA  SER A  58      960    896   1054     83    101     35       C  
ATOM    429  C   SER A  58      -1.758 -39.913 102.798  1.00  9.31           C  
ANISOU  429  C   SER A  58     1166   1128   1244     89     85     45       C  
ATOM    430  O   SER A  58      -2.465 -39.286 102.005  1.00  9.64           O  
ANISOU  430  O   SER A  58     1205   1173   1283     99     83     69       O  
ATOM    431  CB  SER A  58       0.680 -39.908 102.315  1.00 10.62           C  
ANISOU  431  CB  SER A  58     1344   1277   1414     75    106     39       C  
ATOM    432  OG  SER A  58       1.896 -39.219 102.528  1.00 15.26           O  
ANISOU  432  OG  SER A  58     1932   1843   2023     70    121     36       O  
ATOM    433  N   LEU A  59      -2.103 -41.091 103.309  1.00  7.71           N  
ANISOU  433  N   LEU A  59      961    941   1027     81     73     28       N  
ATOM    434  CA  LEU A  59      -3.375 -41.706 102.987  1.00  8.13           C  
ANISOU  434  CA  LEU A  59     1009   1016   1064     84     57     36       C  
ATOM    435  C   LEU A  59      -4.520 -40.860 103.538  1.00 10.28           C  
ANISOU  435  C   LEU A  59     1269   1284   1355     96     57     45       C  
ATOM    436  O   LEU A  59      -5.479 -40.533 102.824  1.00  7.66           O  
ANISOU  436  O   LEU A  59      930    961   1018    106     49     66       O  
ATOM    437  CB  LEU A  59      -3.426 -43.132 103.547  1.00  7.70           C  
ANISOU  437  CB  LEU A  59      956    975    996     72     46     15       C  
ATOM    438  CG  LEU A  59      -4.762 -43.849 103.315  1.00  7.48           C  
ANISOU  438  CG  LEU A  59      920    969    955     71     28     21       C  
ATOM    439  CD1 LEU A  59      -4.979 -44.119 101.823  1.00  5.80           C  
ANISOU  439  CD1 LEU A  59      713    771    718     71     17     37       C  
ATOM    440  CD2 LEU A  59      -4.820 -45.146 104.138  1.00  6.29           C  
ANISOU  440  CD2 LEU A  59      766    824    798     59     20      1       C  
ATOM    441  N   LYS A  60      -4.415 -40.491 104.810  1.00  8.34           N  
ANISOU  441  N   LYS A  60     1018   1023   1127     98     65     28       N  
ATOM    442  CA  LYS A  60      -5.439 -39.668 105.439  1.00  7.17           C  
ANISOU  442  CA  LYS A  60      857    868    997    111     69     33       C  
ATOM    443  C   LYS A  60      -5.626 -38.330 104.721  1.00 10.04           C  
ANISOU  443  C   LYS A  60     1220   1217   1377    126     77     57       C  
ATOM    444  O   LYS A  60      -6.753 -37.835 104.618  1.00 11.15           O  
ANISOU  444  O   LYS A  60     1349   1361   1526    140     74     73       O  
ATOM    445  CB  LYS A  60      -5.094 -39.429 106.907  1.00  7.42           C  
ANISOU  445  CB  LYS A  60      889    885   1045    110     79      9       C  
ATOM    446  CG  LYS A  60      -5.260 -40.664 107.777  1.00 12.82           C  
ANISOU  446  CG  LYS A  60     1571   1585   1715    100     72    -10       C  
ATOM    447  CD  LYS A  60      -4.670 -40.417 109.151  1.00 22.86           C  
ANISOU  447  CD  LYS A  60     2846   2843   2998     98     81    -34       C  
ATOM    448  CE  LYS A  60      -5.252 -41.352 110.196  1.00 31.02           C  
ANISOU  448  CE  LYS A  60     3874   3893   4021     94     76    -47       C  
ATOM    449  NZ  LYS A  60      -4.576 -41.159 111.511  1.00 32.54           N  
ANISOU  449  NZ  LYS A  60     4072   4074   4219     91     84    -71       N  
ATOM    450  N   ALA A  61      -4.525 -37.780 104.206  1.00  9.20           N  
ANISOU  450  N   ALA A  61     1125   1095   1277    123     87     62       N  
ATOM    451  CA  ALA A  61      -4.520 -36.465 103.571  1.00 10.35           C  
ANISOU  451  CA  ALA A  61     1270   1222   1440    135     97     85       C  
ATOM    452  C   ALA A  61      -4.911 -36.540 102.093  1.00 10.20           C  
ANISOU  452  C   ALA A  61     1252   1221   1402    140     88    116       C  
ATOM    453  O   ALA A  61      -4.972 -35.517 101.402  1.00  8.25           O  
ANISOU  453  O   ALA A  61     1005    961   1167    151     95    141       O  
ATOM    454  CB  ALA A  61      -3.140 -35.817 103.724  1.00 11.63           C  
ANISOU  454  CB  ALA A  61     1441   1358   1620    128    112     78       C  
ATOM    455  N   LYS A  62      -5.173 -37.763 101.631  1.00 11.18           N  
ANISOU  455  N   LYS A  62     1378   1373   1497    131     72    113       N  
ATOM    456  CA  LYS A  62      -5.525 -38.079 100.241  1.00  6.73           C  
ANISOU  456  CA  LYS A  62      819    832    907    133     60    136       C  
ATOM    457  C   LYS A  62      -4.419 -37.787  99.213  1.00  8.43           C  
ANISOU  457  C   LYS A  62     1048   1043   1113    130     71    149       C  
ATOM    458  O   LYS A  62      -4.701 -37.655  98.026  1.00 11.06           O  
ANISOU  458  O   LYS A  62     1385   1390   1427    136     65    174       O  
ATOM    459  CB  LYS A  62      -6.817 -37.355  99.837  1.00  8.34           C  
ANISOU  459  CB  LYS A  62     1010   1041   1119    150     52    163       C  
ATOM    460  CG  LYS A  62      -7.961 -37.692 100.786  1.00  5.44           C  
ANISOU  460  CG  LYS A  62      626    681    760    153     43    152       C  
ATOM    461  CD  LYS A  62      -9.313 -37.405 100.173  1.00  8.46           C  
ANISOU  461  CD  LYS A  62      994   1080   1142    167     28    179       C  
ATOM    462  CE  LYS A  62     -10.394 -37.627 101.214  1.00  8.72           C  
ANISOU  462  CE  LYS A  62     1007   1117   1188    171     24    169       C  
ATOM    463  NZ  LYS A  62     -11.741 -37.648 100.613  1.00 10.61           N  
ANISOU  463  NZ  LYS A  62     1229   1378   1425    181      6    194       N  
ATOM    464  N   LYS A  63      -3.173 -37.726  99.666  1.00  8.56           N  
ANISOU  464  N   LYS A  63     1072   1041   1140    121     86    133       N  
ATOM    465  CA  LYS A  63      -2.033 -37.661  98.749  1.00  9.83           C  
ANISOU  465  CA  LYS A  63     1244   1200   1290    116     98    143       C  
ATOM    466  C   LYS A  63      -1.867 -38.967  97.990  1.00 11.59           C  
ANISOU  466  C   LYS A  63     1477   1451   1476    108     87    136       C  
ATOM    467  O   LYS A  63      -1.385 -38.985  96.861  1.00 13.13           O  
ANISOU  467  O   LYS A  63     1682   1655   1650    108     92    152       O  
ATOM    468  CB  LYS A  63      -0.745 -37.346  99.505  1.00 13.47           C  
ANISOU  468  CB  LYS A  63     1707   1636   1775    107    115    126       C  
ATOM    469  CG  LYS A  63      -0.689 -35.945 100.077  1.00 14.79           C  
ANISOU  469  CG  LYS A  63     1868   1772   1981    115    128    133       C  
ATOM    470  CD  LYS A  63       0.499 -35.817 101.014  1.00 20.59           C  
ANISOU  470  CD  LYS A  63     2601   2483   2737    103    139    109       C  
ATOM    471  CE  LYS A  63       1.218 -34.500 100.827  1.00 31.67           C  
ANISOU  471  CE  LYS A  63     4005   3857   4171    104    157    124       C  
ATOM    472  NZ  LYS A  63       2.494 -34.460 101.601  1.00 32.57           N  
ANISOU  472  NZ  LYS A  63     4117   3952   4305     90    166    102       N  
ATOM    473  N   ILE A  64      -2.248 -40.060  98.644  1.00 10.28           N  
ANISOU  473  N   ILE A  64     1308   1296   1300    100     73    112       N  
ATOM    474  CA  ILE A  64      -2.330 -41.372  98.014  1.00 10.41           C  
ANISOU  474  CA  ILE A  64     1334   1338   1284     92     60    102       C  
ATOM    475  C   ILE A  64      -3.718 -41.946  98.301  1.00  8.93           C  
ANISOU  475  C   ILE A  64     1137   1167   1090     92     37     99       C  
ATOM    476  O   ILE A  64      -4.424 -41.443  99.176  1.00  8.92           O  
ANISOU  476  O   ILE A  64     1121   1157   1110     98     36     99       O  
ATOM    477  CB  ILE A  64      -1.241 -42.333  98.527  1.00  8.78           C  
ANISOU  477  CB  ILE A  64     1134   1128   1075     79     66     75       C  
ATOM    478  CG1 ILE A  64      -1.271 -42.426 100.059  1.00  6.79           C  
ANISOU  478  CG1 ILE A  64      871    861    847     75     66     53       C  
ATOM    479  CG2 ILE A  64       0.132 -41.880  98.037  1.00  9.56           C  
ANISOU  479  CG2 ILE A  64     1240   1215   1177     79     87     81       C  
ATOM    480  CD1 ILE A  64      -0.262 -43.466 100.626  1.00  7.60           C  
ANISOU  480  CD1 ILE A  64      979    962    948     63     69     28       C  
ATOM    481  N   ASP A  65      -4.097 -42.992  97.568  1.00  6.88           N  
ANISOU  481  N   ASP A  65      883    930    799     86     20     95       N  
ATOM    482  CA  ASP A  65      -5.407 -43.614  97.720  1.00  7.26           C  
ANISOU  482  CA  ASP A  65      922    996    842     84     -3     93       C  
ATOM    483  C   ASP A  65      -5.343 -44.964  98.409  1.00  8.45           C  
ANISOU  483  C   ASP A  65     1073   1150    988     69    -11     65       C  
ATOM    484  O   ASP A  65      -6.354 -45.473  98.887  1.00  9.31           O  
ANISOU  484  O   ASP A  65     1170   1268   1101     65    -27     60       O  
ATOM    485  CB  ASP A  65      -6.069 -43.773  96.356  1.00 10.38           C  
ANISOU  485  CB  ASP A  65     1322   1415   1207     86    -21    111       C  
ATOM    486  CG  ASP A  65      -6.218 -42.464  95.653  1.00 14.96           C  
ANISOU  486  CG  ASP A  65     1902   1993   1791    102    -14    143       C  
ATOM    487  OD1 ASP A  65      -6.994 -41.629  96.152  1.00 15.19           O  
ANISOU  487  OD1 ASP A  65     1914   2014   1843    112    -15    157       O  
ATOM    488  OD2 ASP A  65      -5.543 -42.256  94.628  1.00 13.54           O  
ANISOU  488  OD2 ASP A  65     1737   1818   1591    104     -7    155       O  
ATOM    489  N   ALA A  66      -4.147 -45.537  98.465  1.00  7.52           N  
ANISOU  489  N   ALA A  66      968   1025    864     62      0     47       N  
ATOM    490  CA  ALA A  66      -3.967 -46.854  99.051  1.00  8.22           C  
ANISOU  490  CA  ALA A  66     1059   1115    949     49     -7     22       C  
ATOM    491  C   ALA A  66      -2.550 -47.009  99.551  1.00  7.78           C  
ANISOU  491  C   ALA A  66     1010   1042    902     46     12      6       C  
ATOM    492  O   ALA A  66      -1.639 -46.337  99.062  1.00  8.11           O  
ANISOU  492  O   ALA A  66     1060   1078    946     51     28     14       O  
ATOM    493  CB  ALA A  66      -4.286 -47.933  98.034  1.00  8.38           C  
ANISOU  493  CB  ALA A  66     1090   1154    939     42    -25     16       C  
ATOM    494  N   ILE A  67      -2.371 -47.902 100.522  1.00  5.83           N  
ANISOU  494  N   ILE A  67      761    791    664     37      9    -14       N  
ATOM    495  CA  ILE A  67      -1.047 -48.313 100.975  1.00  5.32           C  
ANISOU  495  CA  ILE A  67      702    713    605     32     23    -30       C  
ATOM    496  C   ILE A  67      -0.860 -49.802 100.740  1.00  5.71           C  
ANISOU  496  C   ILE A  67      761    769    638     23     13    -47       C  
ATOM    497  O   ILE A  67      -1.630 -50.599 101.263  1.00  7.12           O  
ANISOU  497  O   ILE A  67      934    952    818     16     -1    -55       O  
ATOM    498  CB  ILE A  67      -0.844 -48.066 102.475  1.00  6.75           C  
ANISOU  498  CB  ILE A  67      872    881    811     31     29    -39       C  
ATOM    499  CG1 ILE A  67      -1.114 -46.599 102.827  1.00 10.93           C  
ANISOU  499  CG1 ILE A  67     1393   1400   1359     40     37    -26       C  
ATOM    500  CG2 ILE A  67       0.572 -48.515 102.913  1.00  6.51           C  
ANISOU  500  CG2 ILE A  67      847    840    788     26     40    -54       C  
ATOM    501  CD1 ILE A  67      -1.249 -46.371 104.310  1.00  5.51           C  
ANISOU  501  CD1 ILE A  67      696    705    693     39     40    -36       C  
ATOM    502  N   ILE A  68       0.151 -50.189  99.971  1.00  5.56           N  
ANISOU  502  N   ILE A  68      756    751    608     23     23    -53       N  
ATOM    503  CA  ILE A  68       0.527 -51.601  99.946  1.00  6.27           C  
ANISOU  503  CA  ILE A  68      854    840    687     15     18    -73       C  
ATOM    504  C   ILE A  68       2.007 -51.661 100.276  1.00  7.03           C  
ANISOU  504  C   ILE A  68      952    923    795     17     37    -81       C  
ATOM    505  O   ILE A  68       2.849 -51.370  99.430  1.00  8.10           O  
ANISOU  505  O   ILE A  68     1096   1059    922     23     52    -77       O  
ATOM    506  CB  ILE A  68       0.236 -52.290  98.602  1.00  7.77           C  
ANISOU  506  CB  ILE A  68     1061   1045    848     14      8    -76       C  
ATOM    507  CG1 ILE A  68      -1.254 -52.149  98.246  1.00  8.69           C  
ANISOU  507  CG1 ILE A  68     1172   1176    954     12    -14    -66       C  
ATOM    508  CG2 ILE A  68       0.627 -53.774  98.700  1.00  7.04           C  
ANISOU  508  CG2 ILE A  68      977    948    751      6      4    -99       C  
ATOM    509  CD1 ILE A  68      -1.630 -52.627  96.834  1.00  9.83           C  
ANISOU  509  CD1 ILE A  68     1333   1338   1065     11    -26    -67       C  
ATOM    510  N   SER A  69       2.309 -52.023 101.521  1.00  6.25           N  
ANISOU  510  N   SER A  69      845    814    717     13     37    -91       N  
ATOM    511  CA  SER A  69       3.646 -51.848 102.060  1.00  8.08           C  
ANISOU  511  CA  SER A  69     1073   1032    965     14     53    -96       C  
ATOM    512  C   SER A  69       3.857 -52.739 103.292  1.00  6.10           C  
ANISOU  512  C   SER A  69      815    774    727      8     46   -110       C  
ATOM    513  O   SER A  69       4.316 -52.269 104.339  1.00  7.21           O  
ANISOU  513  O   SER A  69      946    906    886      8     51   -111       O  
ATOM    514  CB  SER A  69       3.863 -50.367 102.412  1.00  5.58           C  
ANISOU  514  CB  SER A  69      747    709    665     19     63    -83       C  
ATOM    515  OG  SER A  69       5.235 -50.069 102.607  1.00  8.84           O  
ANISOU  515  OG  SER A  69     1156   1111   1093     20     79    -85       O  
ATOM    516  N   SER A  70       3.527 -54.025 103.152  1.00  5.70           N  
ANISOU  516  N   SER A  70      772    726    667      3     36   -120       N  
ATOM    517  CA  SER A  70       3.502 -54.951 104.282  1.00  5.68           C  
ANISOU  517  CA  SER A  70      764    717    675     -3     27   -130       C  
ATOM    518  C   SER A  70       2.832 -54.308 105.494  1.00  6.80           C  
ANISOU  518  C   SER A  70      893    860    831     -5     22   -123       C  
ATOM    519  O   SER A  70       3.336 -54.402 106.610  1.00  6.88           O  
ANISOU  519  O   SER A  70      896    864    854     -6     24   -127       O  
ATOM    520  CB  SER A  70       4.923 -55.408 104.662  1.00  6.45           C  
ANISOU  520  CB  SER A  70      861    804    785     -1     38   -138       C  
ATOM    521  OG  SER A  70       5.549 -56.055 103.583  1.00  9.11           O  
ANISOU  521  OG  SER A  70     1209   1139   1111      3     46   -145       O  
ATOM    522  N   LEU A  71       1.713 -53.634 105.268  1.00  7.76           N  
ANISOU  522  N   LEU A  71     1011    990    947     -4     16   -114       N  
ATOM    523  CA  LEU A  71       1.076 -52.860 106.332  1.00  6.59           C  
ANISOU  523  CA  LEU A  71      851    842    810     -3     15   -108       C  
ATOM    524  C   LEU A  71       0.234 -53.770 107.214  1.00  8.67           C  
ANISOU  524  C   LEU A  71     1108   1110   1075    -10      3   -111       C  
ATOM    525  O   LEU A  71      -0.867 -54.179 106.825  1.00  9.79           O  
ANISOU  525  O   LEU A  71     1249   1260   1210    -14     -9   -106       O  
ATOM    526  CB  LEU A  71       0.217 -51.732 105.736  1.00  5.41           C  
ANISOU  526  CB  LEU A  71      698    700    657      3     15    -94       C  
ATOM    527  CG  LEU A  71      -0.221 -50.651 106.731  1.00  7.87           C  
ANISOU  527  CG  LEU A  71      999   1008    983      8     20    -89       C  
ATOM    528  CD1 LEU A  71       0.990 -49.805 107.159  1.00 11.62           C  
ANISOU  528  CD1 LEU A  71     1474   1470   1471     11     33    -93       C  
ATOM    529  CD2 LEU A  71      -1.299 -49.770 106.122  1.00  7.82           C  
ANISOU  529  CD2 LEU A  71      988   1009    974     15     17    -74       C  
ATOM    530  N   SER A  72       0.748 -54.090 108.402  1.00  7.60           N  
ANISOU  530  N   SER A  72      969    969    949    -12      5   -116       N  
ATOM    531  CA  SER A  72       0.016 -54.972 109.318  1.00  7.70           C  
ANISOU  531  CA  SER A  72      976    986    964    -19     -4   -116       C  
ATOM    532  C   SER A  72      -1.330 -54.383 109.705  1.00  9.33           C  
ANISOU  532  C   SER A  72     1172   1201   1171    -18     -7   -107       C  
ATOM    533  O   SER A  72      -1.435 -53.188 110.008  1.00  7.87           O  
ANISOU  533  O   SER A  72      983   1018    991    -10      0   -104       O  
ATOM    534  CB  SER A  72       0.832 -55.235 110.582  1.00 12.35           C  
ANISOU  534  CB  SER A  72     1562   1569   1561    -19     -1   -122       C  
ATOM    535  OG  SER A  72       2.104 -55.755 110.251  1.00 18.58           O  
ANISOU  535  OG  SER A  72     2358   2349   2353    -19      2   -129       O  
ATOM    536  N   ILE A  73      -2.348 -55.239 109.715  1.00  7.10           N  
ANISOU  536  N   ILE A  73      885    925    886    -25    -18   -103       N  
ATOM    537  CA  ILE A  73      -3.707 -54.828 110.052  1.00  4.40           C  
ANISOU  537  CA  ILE A  73      531    595    547    -25    -21    -92       C  
ATOM    538  C   ILE A  73      -3.833 -54.784 111.577  1.00  5.74           C  
ANISOU  538  C   ILE A  73      692    767    723    -23    -15    -91       C  
ATOM    539  O   ILE A  73      -4.613 -55.517 112.180  1.00  9.38           O  
ANISOU  539  O   ILE A  73     1144   1233   1185    -30    -20    -86       O  
ATOM    540  CB  ILE A  73      -4.747 -55.790 109.427  1.00  8.54           C  
ANISOU  540  CB  ILE A  73     1051   1126   1068    -35    -37    -87       C  
ATOM    541  CG1 ILE A  73      -4.420 -56.038 107.949  1.00  9.88           C  
ANISOU  541  CG1 ILE A  73     1233   1293   1226    -37    -44    -93       C  
ATOM    542  CG2 ILE A  73      -6.166 -55.220 109.541  1.00  9.36           C  
ANISOU  542  CG2 ILE A  73     1139   1242   1175    -33    -40    -74       C  
ATOM    543  CD1 ILE A  73      -5.318 -57.065 107.291  1.00 11.55           C  
ANISOU  543  CD1 ILE A  73     1444   1510   1434    -50    -62    -92       C  
ATOM    544  N   THR A  74      -3.057 -53.918 112.217  1.00  7.87           N  
ANISOU  544  N   THR A  74      965   1032    995    -15     -4    -97       N  
ATOM    545  CA  THR A  74      -3.108 -53.882 113.678  1.00  6.68           C  
ANISOU  545  CA  THR A  74      808    884    846    -14      1    -98       C  
ATOM    546  C   THR A  74      -4.428 -53.283 114.169  1.00  6.78           C  
ANISOU  546  C   THR A  74      808    907    860     -9      6    -89       C  
ATOM    547  O   THR A  74      -5.035 -52.453 113.510  1.00  8.54           O  
ANISOU  547  O   THR A  74     1027   1132   1086     -2      8    -84       O  
ATOM    548  CB  THR A  74      -1.947 -53.071 114.286  1.00  8.21           C  
ANISOU  548  CB  THR A  74     1008   1071   1042     -8     10   -109       C  
ATOM    549  OG1 THR A  74      -2.039 -51.717 113.839  1.00 10.04           O  
ANISOU  549  OG1 THR A  74     1239   1298   1278      1     17   -109       O  
ATOM    550  CG2 THR A  74      -0.590 -53.667 113.885  1.00  9.44           C  
ANISOU  550  CG2 THR A  74     1173   1216   1199    -12      7   -116       C  
ATOM    551  N   ASP A  75      -4.856 -53.720 115.346  1.00  6.92           N  
ANISOU  551  N   ASP A  75      820    933    876    -10      9    -86       N  
ATOM    552  CA  ASP A  75      -6.032 -53.163 116.007  1.00  8.20           C  
ANISOU  552  CA  ASP A  75      969   1106   1039     -3     17    -79       C  
ATOM    553  C   ASP A  75      -5.971 -51.634 116.079  1.00  7.10           C  
ANISOU  553  C   ASP A  75      832    963    904     11     28    -85       C  
ATOM    554  O   ASP A  75      -6.963 -50.947 115.778  1.00  9.65           O  
ANISOU  554  O   ASP A  75     1143   1290   1232     19     32    -77       O  
ATOM    555  CB  ASP A  75      -6.151 -53.788 117.403  1.00  7.65           C  
ANISOU  555  CB  ASP A  75      897   1044    964     -6     22    -77       C  
ATOM    556  CG  ASP A  75      -7.421 -53.383 118.139  1.00 10.21           C  
ANISOU  556  CG  ASP A  75     1208   1384   1289      1     33    -68       C  
ATOM    557  OD1 ASP A  75      -7.287 -52.874 119.271  1.00 14.38           O  
ANISOU  557  OD1 ASP A  75     1737   1915   1809      9     44    -74       O  
ATOM    558  OD2 ASP A  75      -8.543 -53.595 117.618  1.00 11.44           O  
ANISOU  558  OD2 ASP A  75     1350   1546   1452     -2     30    -54       O  
ATOM    559  N   LYS A  76      -4.802 -51.100 116.425  1.00  9.10           N  
ANISOU  559  N   LYS A  76     1096   1206   1156     14     32    -99       N  
ATOM    560  CA  LYS A  76      -4.620 -49.655 116.539  1.00 11.91           C  
ANISOU  560  CA  LYS A  76     1454   1554   1517     26     42   -107       C  
ATOM    561  C   LYS A  76      -4.840 -48.961 115.193  1.00 11.41           C  
ANISOU  561  C   LYS A  76     1389   1484   1463     30     41    -99       C  
ATOM    562  O   LYS A  76      -5.524 -47.929 115.110  1.00 10.78           O  
ANISOU  562  O   LYS A  76     1303   1402   1389     41     49    -96       O  
ATOM    563  CB  LYS A  76      -3.224 -49.328 117.084  1.00 12.31           C  
ANISOU  563  CB  LYS A  76     1516   1595   1567     24     43   -123       C  
ATOM    564  CG  LYS A  76      -3.001 -47.853 117.346  1.00 18.53           C  
ANISOU  564  CG  LYS A  76     2307   2372   2363     35     53   -133       C  
ATOM    565  CD  LYS A  76      -1.563 -47.572 117.794  1.00 19.94           C  
ANISOU  565  CD  LYS A  76     2495   2539   2542     30     51   -149       C  
ATOM    566  N   ARG A  77      -4.280 -49.523 114.129  1.00  9.63           N  
ANISOU  566  N   ARG A  77     1169   1254   1235     22     32    -97       N  
ATOM    567  CA  ARG A  77      -4.441 -48.894 112.830  1.00 11.87           C  
ANISOU  567  CA  ARG A  77     1454   1534   1524     26     30    -88       C  
ATOM    568  C   ARG A  77      -5.888 -48.915 112.350  1.00 11.57           C  
ANISOU  568  C   ARG A  77     1403   1508   1486     30     26    -73       C  
ATOM    569  O   ARG A  77      -6.320 -48.012 111.639  1.00  9.91           O  
ANISOU  569  O   ARG A  77     1189   1295   1281     38     28    -64       O  
ATOM    570  CB  ARG A  77      -3.534 -49.560 111.799  1.00 11.06           C  
ANISOU  570  CB  ARG A  77     1360   1427   1415     18     23    -90       C  
ATOM    571  CG  ARG A  77      -2.101 -49.093 111.916  1.00 11.53           C  
ANISOU  571  CG  ARG A  77     1429   1472   1479     18     29   -101       C  
ATOM    572  CD  ARG A  77      -1.204 -49.886 111.006  1.00 11.02           C  
ANISOU  572  CD  ARG A  77     1373   1405   1409     11     25   -102       C  
ATOM    573  NE  ARG A  77       0.195 -49.521 111.185  1.00 11.09           N  
ANISOU  573  NE  ARG A  77     1387   1402   1424     10     31   -111       N  
ATOM    574  CZ  ARG A  77       1.205 -50.290 110.808  1.00 13.82           C  
ANISOU  574  CZ  ARG A  77     1738   1744   1768      5     29   -116       C  
ATOM    575  NH1 ARG A  77       0.963 -51.451 110.226  1.00 12.67           N  
ANISOU  575  NH1 ARG A  77     1597   1605   1613      0     22   -114       N  
ATOM    576  NH2 ARG A  77       2.457 -49.890 111.000  1.00 14.38           N  
ANISOU  576  NH2 ARG A  77     1811   1805   1847      5     35   -123       N  
ATOM    577  N   GLN A  78      -6.636 -49.939 112.742  1.00  9.53           N  
ANISOU  577  N   GLN A  78     1136   1261   1224     22     19    -69       N  
ATOM    578  CA  GLN A  78      -8.038 -50.020 112.359  1.00 12.73           C  
ANISOU  578  CA  GLN A  78     1526   1679   1632     23     14    -53       C  
ATOM    579  C   GLN A  78      -8.919 -48.979 113.062  1.00 14.56           C  
ANISOU  579  C   GLN A  78     1745   1914   1873     38     27    -48       C  
ATOM    580  O   GLN A  78     -10.064 -48.783 112.676  1.00 15.83           O  
ANISOU  580  O   GLN A  78     1890   2084   2040     43     24    -34       O  
ATOM    581  CB  GLN A  78      -8.559 -51.435 112.610  1.00 12.61           C  
ANISOU  581  CB  GLN A  78     1504   1673   1613      9      3    -50       C  
ATOM    582  CG  GLN A  78      -7.952 -52.417 111.620  1.00 10.14           C  
ANISOU  582  CG  GLN A  78     1203   1357   1293     -3    -11    -53       C  
ATOM    583  CD  GLN A  78      -8.617 -53.772 111.624  1.00 12.31           C  
ANISOU  583  CD  GLN A  78     1471   1639   1568    -18    -24    -49       C  
ATOM    584  OE1 GLN A  78      -8.267 -54.638 112.415  1.00 10.11           O  
ANISOU  584  OE1 GLN A  78     1195   1358   1289    -26    -23    -53       O  
ATOM    585  NE2 GLN A  78      -9.564 -53.971 110.718  1.00 13.10           N  
ANISOU  585  NE2 GLN A  78     1562   1747   1668    -23    -37    -39       N  
ATOM    586  N   GLN A  79      -8.375 -48.293 114.062  1.00 13.32           N  
ANISOU  586  N   GLN A  79     1594   1750   1718     46     41    -60       N  
ATOM    587  CA  GLN A  79      -9.073 -47.162 114.676  1.00 14.27           C  
ANISOU  587  CA  GLN A  79     1706   1869   1847     63     56    -59       C  
ATOM    588  C   GLN A  79      -9.137 -45.997 113.699  1.00 16.56           C  
ANISOU  588  C   GLN A  79     1996   2149   2149     74     57    -52       C  
ATOM    589  O   GLN A  79     -10.045 -45.161 113.766  1.00 16.35           O  
ANISOU  589  O   GLN A  79     1958   2123   2133     88     66    -44       O  
ATOM    590  CB  GLN A  79      -8.371 -46.703 115.957  1.00 17.06           C  
ANISOU  590  CB  GLN A  79     2070   2216   2198     68     69    -78       C  
ATOM    591  CG  GLN A  79      -8.217 -47.769 117.032  1.00 21.38           C  
ANISOU  591  CG  GLN A  79     2617   2773   2732     58     68    -83       C  
ATOM    592  CD  GLN A  79      -7.235 -47.357 118.120  1.00 18.44           C  
ANISOU  592  CD  GLN A  79     2260   2394   2354     60     76   -103       C  
ATOM    593  OE1 GLN A  79      -6.668 -46.261 118.082  1.00 22.90           O  
ANISOU  593  OE1 GLN A  79     2832   2944   2925     68     82   -115       O  
ATOM    594  NE2 GLN A  79      -7.012 -48.246 119.084  1.00 17.22           N  
ANISOU  594  NE2 GLN A  79     2107   2249   2185     53     75   -107       N  
ATOM    595  N   GLU A  80      -8.146 -45.939 112.809  1.00 11.95           N  
ANISOU  595  N   GLU A  80     1424   1553   1561     68     51    -55       N  
ATOM    596  CA  GLU A  80      -7.957 -44.788 111.932  1.00 16.00           C  
ANISOU  596  CA  GLU A  80     1941   2054   2085     78     54    -48       C  
ATOM    597  C   GLU A  80      -8.257 -45.060 110.451  1.00 15.26           C  
ANISOU  597  C   GLU A  80     1845   1967   1985     75     40    -31       C  
ATOM    598  O   GLU A  80      -8.734 -44.173 109.745  1.00 14.37           O  
ANISOU  598  O   GLU A  80     1727   1851   1880     86     41    -16       O  
ATOM    599  CB  GLU A  80      -6.524 -44.276 112.059  1.00 23.20           C  
ANISOU  599  CB  GLU A  80     2869   2947   2999     76     60    -63       C  
ATOM    600  CG  GLU A  80      -6.097 -43.993 113.483  1.00 33.20           C  
ANISOU  600  CG  GLU A  80     4140   4208   4268     78     71    -82       C  
ATOM    601  CD  GLU A  80      -7.020 -43.013 114.179  1.00 38.59           C  
ANISOU  601  CD  GLU A  80     4815   4887   4962     94     84    -83       C  
ATOM    602  N   ILE A  81      -7.948 -46.262 109.971  1.00 11.25           N  
ANISOU  602  N   ILE A  81     1342   1468   1463     60     27    -33       N  
ATOM    603  CA  ILE A  81      -8.088 -46.554 108.543  1.00  9.23           C  
ANISOU  603  CA  ILE A  81     1089   1219   1198     56     13    -20       C  
ATOM    604  C   ILE A  81      -8.742 -47.916 108.296  1.00  6.76           C  
ANISOU  604  C   ILE A  81      770    922    875     42     -4    -18       C  
ATOM    605  O   ILE A  81      -8.864 -48.729 109.216  1.00 11.40           O  
ANISOU  605  O   ILE A  81     1354   1514   1463     35     -4    -26       O  
ATOM    606  CB  ILE A  81      -6.710 -46.520 107.814  1.00  8.18           C  
ANISOU  606  CB  ILE A  81      974   1075   1058     51     15    -27       C  
ATOM    607  CG1 ILE A  81      -5.771 -47.606 108.346  1.00  9.78           C  
ANISOU  607  CG1 ILE A  81     1187   1276   1254     38     14    -44       C  
ATOM    608  CG2 ILE A  81      -6.054 -45.125 107.905  1.00  9.06           C  
ANISOU  608  CG2 ILE A  81     1090   1168   1183     63     31    -26       C  
ATOM    609  CD1 ILE A  81      -4.462 -47.729 107.531  1.00  9.89           C  
ANISOU  609  CD1 ILE A  81     1216   1281   1260     34     16    -49       C  
ATOM    610  N   ALA A  82      -9.182 -48.143 107.060  1.00  7.68           N  
ANISOU  610  N   ALA A  82      887   1049    983     39    -19     -7       N  
ATOM    611  CA  ALA A  82      -9.704 -49.440 106.657  1.00  6.87           C  
ANISOU  611  CA  ALA A  82      781    958    870     24    -38     -7       C  
ATOM    612  C   ALA A  82      -8.607 -50.269 105.999  1.00  8.87           C  
ANISOU  612  C   ALA A  82     1055   1208   1109     14    -43    -20       C  
ATOM    613  O   ALA A  82      -7.547 -49.747 105.618  1.00  7.50           O  
ANISOU  613  O   ALA A  82      896   1024    931     19    -33    -25       O  
ATOM    614  CB  ALA A  82     -10.892 -49.274 105.710  1.00 10.56           C  
ANISOU  614  CB  ALA A  82     1235   1441   1336     27    -54     11       C  
ATOM    615  N   PHE A  83      -8.872 -51.563 105.873  1.00  9.20           N  
ANISOU  615  N   PHE A  83     1097   1255   1144     -1    -57    -26       N  
ATOM    616  CA  PHE A  83      -7.972 -52.470 105.182  1.00  6.28           C  
ANISOU  616  CA  PHE A  83      746    881    759    -11    -63    -40       C  
ATOM    617  C   PHE A  83      -8.747 -53.389 104.261  1.00  9.86           C  
ANISOU  617  C   PHE A  83     1199   1346   1202    -23    -86    -39       C  
ATOM    618  O   PHE A  83      -9.876 -53.772 104.562  1.00 10.93           O  
ANISOU  618  O   PHE A  83     1318   1490   1345    -30    -98    -32       O  
ATOM    619  CB  PHE A  83      -7.196 -53.339 106.167  1.00  7.09           C  
ANISOU  619  CB  PHE A  83      855    973    867    -19    -56    -55       C  
ATOM    620  CG  PHE A  83      -6.143 -52.611 106.946  1.00  7.90           C  
ANISOU  620  CG  PHE A  83      962   1063    977    -10    -37    -60       C  
ATOM    621  CD1 PHE A  83      -4.807 -52.722 106.594  1.00  9.03           C  
ANISOU  621  CD1 PHE A  83     1121   1196   1114     -9    -30    -71       C  
ATOM    622  CD2 PHE A  83      -6.477 -51.870 108.063  1.00  9.51           C  
ANISOU  622  CD2 PHE A  83     1155   1266   1193     -2    -26    -56       C  
ATOM    623  CE1 PHE A  83      -3.826 -52.084 107.332  1.00  6.60           C  
ANISOU  623  CE1 PHE A  83      815    877    814     -3    -14    -76       C  
ATOM    624  CE2 PHE A  83      -5.516 -51.235 108.794  1.00  8.05           C  
ANISOU  624  CE2 PHE A  83      975   1070   1014      4    -11    -64       C  
ATOM    625  CZ  PHE A  83      -4.183 -51.339 108.437  1.00  5.04           C  
ANISOU  625  CZ  PHE A  83      608    679    629      3     -6    -74       C  
ATOM    626  N   SER A  84      -8.119 -53.778 103.160  1.00  7.34           N  
ANISOU  626  N   SER A  84      898   1026    864    -27    -93    -47       N  
ATOM    627  CA  SER A  84      -8.605 -54.915 102.384  1.00  8.83           C  
ANISOU  627  CA  SER A  84     1092   1222   1041    -41   -115    -54       C  
ATOM    628  C   SER A  84      -8.554 -56.171 103.246  1.00 10.36           C  
ANISOU  628  C   SER A  84     1284   1406   1246    -55   -117    -67       C  
ATOM    629  O   SER A  84      -7.961 -56.169 104.335  1.00 10.14           O  
ANISOU  629  O   SER A  84     1254   1367   1230    -52   -101    -70       O  
ATOM    630  CB  SER A  84      -7.761 -55.126 101.121  1.00  8.23           C  
ANISOU  630  CB  SER A  84     1040   1146    941    -40   -116    -65       C  
ATOM    631  OG  SER A  84      -6.497 -55.686 101.453  1.00  9.38           O  
ANISOU  631  OG  SER A  84     1201   1277   1088    -41   -102    -81       O  
ATOM    632  N   ASP A  85      -9.163 -57.242 102.755  1.00 10.29           N  
ANISOU  632  N   ASP A  85     1276   1400   1232    -70   -138    -73       N  
ATOM    633  CA  ASP A  85      -8.898 -58.572 103.292  1.00  8.46           C  
ANISOU  633  CA  ASP A  85     1049   1156   1010    -84   -141    -87       C  
ATOM    634  C   ASP A  85      -7.401 -58.853 103.283  1.00 10.03           C  
ANISOU  634  C   ASP A  85     1269   1339   1202    -79   -125   -103       C  
ATOM    635  O   ASP A  85      -6.642 -58.226 102.523  1.00  9.86           O  
ANISOU  635  O   ASP A  85     1261   1319   1165    -68   -117   -106       O  
ATOM    636  CB  ASP A  85      -9.619 -59.653 102.480  1.00 11.31           C  
ANISOU  636  CB  ASP A  85     1413   1519   1364   -102   -167    -96       C  
ATOM    637  CG  ASP A  85     -11.126 -59.573 102.600  1.00 14.91           C  
ANISOU  637  CG  ASP A  85     1844   1990   1831   -111   -185    -80       C  
ATOM    638  OD1 ASP A  85     -11.625 -59.265 103.703  1.00 16.65           O  
ANISOU  638  OD1 ASP A  85     2043   2212   2071   -108   -175    -66       O  
ATOM    639  OD2 ASP A  85     -11.802 -59.848 101.591  1.00 16.54           O  
ANISOU  639  OD2 ASP A  85     2050   2206   2027   -120   -209    -82       O  
ATOM    640  N   LYS A  86      -6.984 -59.801 104.117  1.00  6.47           N  
ANISOU  640  N   LYS A  86      820    874    764    -86   -121   -111       N  
ATOM    641  CA  LYS A  86      -5.554 -60.106 104.277  1.00 10.98           C  
ANISOU  641  CA  LYS A  86     1408   1431   1335    -80   -106   -124       C  
ATOM    642  C   LYS A  86      -4.857 -60.466 102.967  1.00 12.32           C  
ANISOU  642  C   LYS A  86     1600   1597   1485    -78   -108   -140       C  
ATOM    643  O   LYS A  86      -5.333 -61.316 102.210  1.00  9.94           O  
ANISOU  643  O   LYS A  86     1307   1296   1176    -90   -125   -150       O  
ATOM    644  CB  LYS A  86      -5.346 -61.259 105.259  1.00 10.93           C  
ANISOU  644  CB  LYS A  86     1399   1409   1344    -89   -105   -129       C  
ATOM    645  CG  LYS A  86      -3.883 -61.723 105.303  1.00 11.43           C  
ANISOU  645  CG  LYS A  86     1479   1456   1408    -83    -92   -142       C  
ATOM    646  CD  LYS A  86      -3.589 -62.788 106.366  1.00 17.62           C  
ANISOU  646  CD  LYS A  86     2260   2225   2209    -89    -91   -143       C  
ATOM    647  CE  LYS A  86      -4.183 -64.143 106.025  1.00 16.01           C  
ANISOU  647  CE  LYS A  86     2060   2010   2011   -105   -107   -151       C  
ATOM    648  NZ  LYS A  86      -3.671 -65.204 106.960  1.00 15.22           N  
ANISOU  648  NZ  LYS A  86     1962   1893   1929   -109   -104   -152       N  
ATOM    649  N   LEU A  87      -3.719 -59.816 102.727  1.00 10.05           N  
ANISOU  649  N   LEU A  87     1322   1307   1191    -65    -90   -142       N  
ATOM    650  CA  LEU A  87      -2.845 -60.128 101.599  1.00  8.01           C  
ANISOU  650  CA  LEU A  87     1085   1045    914    -61    -85   -157       C  
ATOM    651  C   LEU A  87      -1.876 -61.276 101.887  1.00  6.46           C  
ANISOU  651  C   LEU A  87      899    830    726    -62    -78   -173       C  
ATOM    652  O   LEU A  87      -1.650 -62.127 101.029  1.00  9.82           O  
ANISOU  652  O   LEU A  87     1342   1250   1140    -66    -83   -190       O  
ATOM    653  CB  LEU A  87      -2.055 -58.884 101.194  1.00  7.89           C  
ANISOU  653  CB  LEU A  87     1073   1036    890    -45    -67   -149       C  
ATOM    654  CG  LEU A  87      -2.903 -57.770 100.569  1.00  8.13           C  
ANISOU  654  CG  LEU A  87     1097   1083    908    -41    -73   -133       C  
ATOM    655  CD1 LEU A  87      -2.055 -56.512 100.375  1.00  9.49           C  
ANISOU  655  CD1 LEU A  87     1271   1257   1079    -27    -53   -123       C  
ATOM    656  CD2 LEU A  87      -3.511 -58.231  99.243  1.00 10.53           C  
ANISOU  656  CD2 LEU A  87     1414   1400   1188    -47    -92   -139       C  
ATOM    657  N   TYR A  88      -1.283 -61.265 103.080  1.00  6.86           N  
ANISOU  657  N   TYR A  88      940    870    796    -59    -67   -169       N  
ATOM    658  CA  TYR A  88      -0.412 -62.339 103.575  1.00  9.37           C  
ANISOU  658  CA  TYR A  88     1264   1170   1127    -60    -61   -180       C  
ATOM    659  C   TYR A  88      -0.127 -62.027 105.040  1.00 10.72           C  
ANISOU  659  C   TYR A  88     1420   1337   1317    -57    -53   -168       C  
ATOM    660  O   TYR A  88      -0.369 -60.900 105.482  1.00  9.25           O  
ANISOU  660  O   TYR A  88     1222   1162   1131    -53    -48   -156       O  
ATOM    661  CB  TYR A  88       0.901 -62.440 102.779  1.00 10.47           C  
ANISOU  661  CB  TYR A  88     1420   1303   1257    -49    -46   -193       C  
ATOM    662  CG  TYR A  88       1.637 -61.122 102.635  1.00  7.05           C  
ANISOU  662  CG  TYR A  88      982    878    819    -36    -28   -184       C  
ATOM    663  CD1 TYR A  88       2.475 -60.658 103.646  1.00  7.08           C  
ANISOU  663  CD1 TYR A  88      976    877    840    -30    -15   -177       C  
ATOM    664  CD2 TYR A  88       1.494 -60.348 101.487  1.00 11.63           C  
ANISOU  664  CD2 TYR A  88     1570   1471   1378    -31    -26   -181       C  
ATOM    665  CE1 TYR A  88       3.142 -59.453 103.531  1.00  7.84           C  
ANISOU  665  CE1 TYR A  88     1067    978    935    -20      0   -169       C  
ATOM    666  CE2 TYR A  88       2.155 -59.132 101.357  1.00  7.31           C  
ANISOU  666  CE2 TYR A  88     1018    929    828    -20     -9   -170       C  
ATOM    667  CZ  TYR A  88       2.987 -58.700 102.384  1.00  8.86           C  
ANISOU  667  CZ  TYR A  88     1203   1117   1045    -16      4   -165       C  
ATOM    668  OH  TYR A  88       3.655 -57.501 102.281  1.00  7.66           O  
ANISOU  668  OH  TYR A  88     1047    968    895     -7     19   -155       O  
ATOM    669  N   ALA A  89       0.394 -63.000 105.784  1.00  8.25           N  
ANISOU  669  N   ALA A  89     1107   1009   1018    -60    -52   -172       N  
ATOM    670  CA  ALA A  89       0.746 -62.763 107.180  1.00  6.85           C  
ANISOU  670  CA  ALA A  89      917    830    856    -57    -45   -161       C  
ATOM    671  C   ALA A  89       2.092 -62.044 107.327  1.00 11.30           C  
ANISOU  671  C   ALA A  89     1480   1393   1421    -44    -29   -162       C  
ATOM    672  O   ALA A  89       3.003 -62.237 106.526  1.00  9.72           O  
ANISOU  672  O   ALA A  89     1291   1186   1217    -37    -20   -172       O  
ATOM    673  CB  ALA A  89       0.774 -64.084 107.953  1.00  9.77           C  
ANISOU  673  CB  ALA A  89     1286   1186   1241    -64    -51   -161       C  
ATOM    674  N   ALA A  90       2.188 -61.202 108.352  1.00  8.83           N  
ANISOU  674  N   ALA A  90     1155   1086   1114    -40    -24   -152       N  
ATOM    675  CA  ALA A  90       3.445 -60.577 108.755  1.00  8.84           C  
ANISOU  675  CA  ALA A  90     1152   1084   1121    -31    -12   -152       C  
ATOM    676  C   ALA A  90       3.642 -60.821 110.235  1.00  7.46           C  
ANISOU  676  C   ALA A  90      968    908    957    -32    -14   -146       C  
ATOM    677  O   ALA A  90       3.733 -59.885 111.036  1.00 10.37           O  
ANISOU  677  O   ALA A  90     1328   1284   1327    -29    -11   -141       O  
ATOM    678  CB  ALA A  90       3.452 -59.074 108.452  1.00  9.95           C  
ANISOU  678  CB  ALA A  90     1290   1235   1256    -25     -4   -148       C  
ATOM    679  N   ASP A  91       3.691 -62.096 110.593  1.00  8.85           N  
ANISOU  679  N   ASP A  91     1147   1075   1142    -36    -20   -146       N  
ATOM    680  CA  ASP A  91       3.850 -62.486 111.977  1.00  7.11           C  
ANISOU  680  CA  ASP A  91      919    854    930    -37    -23   -138       C  
ATOM    681  C   ASP A  91       5.312 -62.620 112.335  1.00  8.66           C  
ANISOU  681  C   ASP A  91     1112   1042   1135    -29    -18   -140       C  
ATOM    682  O   ASP A  91       6.184 -62.665 111.472  1.00  9.23           O  
ANISOU  682  O   ASP A  91     1190   1107   1210    -23    -10   -149       O  
ATOM    683  CB  ASP A  91       3.098 -63.793 112.235  1.00  8.58           C  
ANISOU  683  CB  ASP A  91     1106   1031   1121    -47    -33   -133       C  
ATOM    684  CG  ASP A  91       1.592 -63.631 112.054  1.00  7.51           C  
ANISOU  684  CG  ASP A  91      968    906    980    -56    -40   -128       C  
ATOM    685  OD1 ASP A  91       1.070 -62.553 112.418  1.00 11.42           O  
ANISOU  685  OD1 ASP A  91     1455   1415   1467    -55    -37   -122       O  
ATOM    686  OD2 ASP A  91       0.941 -64.561 111.542  1.00 11.01           O  
ANISOU  686  OD2 ASP A  91     1417   1342   1427    -66    -48   -130       O  
ATOM    687  N   SER A  92       5.587 -62.652 113.624  1.00  8.30           N  
ANISOU  687  N   SER A  92     1059    999   1094    -28    -21   -131       N  
ATOM    688  CA  SER A  92       6.961 -62.808 114.052  1.00  8.23           C  
ANISOU  688  CA  SER A  92     1046    985   1095    -21    -19   -132       C  
ATOM    689  C   SER A  92       7.204 -64.254 114.420  1.00  9.53           C  
ANISOU  689  C   SER A  92     1212   1137   1271    -21    -24   -126       C  
ATOM    690  O   SER A  92       6.271 -65.052 114.452  1.00 10.82           O  
ANISOU  690  O   SER A  92     1380   1296   1435    -28    -30   -122       O  
ATOM    691  CB  SER A  92       7.265 -61.875 115.214  1.00  9.74           C  
ANISOU  691  CB  SER A  92     1228   1189   1284    -19    -21   -127       C  
ATOM    692  OG  SER A  92       7.289 -60.544 114.735  1.00 14.11           O  
ANISOU  692  OG  SER A  92     1780   1748   1832    -18    -14   -134       O  
ATOM    693  N   ARG A  93       8.459 -64.599 114.691  1.00  7.13           N  
ANISOU  693  N   ARG A  93      904    826    980    -13    -23   -125       N  
ATOM    694  CA  ARG A  93       8.792 -65.998 114.942  1.00  9.05           C  
ANISOU  694  CA  ARG A  93     1148   1053   1236    -10    -27   -119       C  
ATOM    695  C   ARG A  93      10.145 -66.095 115.640  1.00  5.86           C  
ANISOU  695  C   ARG A  93      734    648    844     -1    -28   -113       C  
ATOM    696  O   ARG A  93      10.997 -65.229 115.461  1.00  8.17           O  
ANISOU  696  O   ARG A  93     1019    946   1137      5    -23   -119       O  
ATOM    697  CB  ARG A  93       8.791 -66.788 113.624  1.00  8.52           C  
ANISOU  697  CB  ARG A  93     1093    969   1174     -9    -21   -132       C  
ATOM    698  CG  ARG A  93       8.569 -68.292 113.785  1.00  9.34           C  
ANISOU  698  CG  ARG A  93     1203   1054   1293    -11    -26   -127       C  
ATOM    699  CD  ARG A  93       8.131 -68.925 112.474  1.00 10.33           C  
ANISOU  699  CD  ARG A  93     1343   1165   1418    -14    -23   -143       C  
ATOM    700  NE  ARG A  93       8.158 -70.381 112.583  1.00  6.66           N  
ANISOU  700  NE  ARG A  93      884    676    971    -14    -27   -140       N  
ATOM    701  CZ  ARG A  93       8.110 -71.211 111.546  1.00  9.01           C  
ANISOU  701  CZ  ARG A  93     1196    954   1275    -14    -24   -156       C  
ATOM    702  NH1 ARG A  93       7.982 -70.736 110.310  1.00  7.10           N  
ANISOU  702  NH1 ARG A  93      963    716   1017    -13    -18   -175       N  
ATOM    703  NH2 ARG A  93       8.186 -72.518 111.751  1.00  5.74           N  
ANISOU  703  NH2 ARG A  93      786    515    880    -13    -28   -153       N  
ATOM    704  N   LEU A  94      10.314 -67.122 116.467  1.00  7.03           N  
ANISOU  704  N   LEU A  94      880    790   1003      1    -36   -100       N  
ATOM    705  CA  LEU A  94      11.589 -67.351 117.136  1.00  6.55           C  
ANISOU  705  CA  LEU A  94      807    727    954     11    -39    -92       C  
ATOM    706  C   LEU A  94      12.590 -68.033 116.225  1.00  5.01           C  
ANISOU  706  C   LEU A  94      613    513    779     22    -30   -100       C  
ATOM    707  O   LEU A  94      12.239 -68.934 115.463  1.00  9.27           O  
ANISOU  707  O   LEU A  94     1164   1034   1325     23    -25   -105       O  
ATOM    708  CB  LEU A  94      11.388 -68.197 118.399  1.00  8.61           C  
ANISOU  708  CB  LEU A  94     1066    988   1218     10    -51    -72       C  
ATOM    709  CG  LEU A  94      10.578 -67.535 119.519  1.00  9.64           C  
ANISOU  709  CG  LEU A  94     1195   1141   1328      2    -59    -63       C  
ATOM    710  CD1 LEU A  94      10.271 -68.567 120.594  1.00 12.64           C  
ANISOU  710  CD1 LEU A  94     1574   1519   1710      0    -68    -40       C  
ATOM    711  CD2 LEU A  94      11.313 -66.343 120.113  1.00 12.82           C  
ANISOU  711  CD2 LEU A  94     1588   1562   1722      4    -63    -66       C  
ATOM    712  N   ILE A  95      13.835 -67.575 116.290  1.00  7.29           N  
ANISOU  712  N   ILE A  95      888    805   1076     31    -27   -100       N  
ATOM    713  CA  ILE A  95      14.941 -68.274 115.656  1.00  8.14           C  
ANISOU  713  CA  ILE A  95      992    896   1206     45    -18   -103       C  
ATOM    714  C   ILE A  95      15.864 -68.802 116.742  1.00  7.46           C  
ANISOU  714  C   ILE A  95      890    809   1135     53    -29    -86       C  
ATOM    715  O   ILE A  95      16.089 -68.130 117.735  1.00  8.77           O  
ANISOU  715  O   ILE A  95     1045    992   1294     50    -41    -77       O  
ATOM    716  CB  ILE A  95      15.720 -67.369 114.706  1.00 12.19           C  
ANISOU  716  CB  ILE A  95     1499   1413   1720     50     -3   -116       C  
ATOM    717  CG1 ILE A  95      14.870 -67.031 113.487  1.00 18.31           C  
ANISOU  717  CG1 ILE A  95     2291   2187   2480     44      8   -132       C  
ATOM    718  CG2 ILE A  95      17.003 -68.032 114.243  1.00 19.62           C  
ANISOU  718  CG2 ILE A  95     2431   2339   2684     66      7   -117       C  
ATOM    719  CD1 ILE A  95      15.697 -66.477 112.374  1.00 30.53           C  
ANISOU  719  CD1 ILE A  95     3836   3734   4031     52     26   -143       C  
ATOM    720  N   ALA A  96      16.371 -70.017 116.561  1.00  9.47           N  
ANISOU  720  N   ALA A  96     1146   1043   1411     65    -26    -81       N  
ATOM    721  CA  ALA A  96      17.272 -70.606 117.541  1.00  9.95           C  
ANISOU  721  CA  ALA A  96     1191   1102   1489     75    -37    -62       C  
ATOM    722  C   ALA A  96      18.153 -71.615 116.822  1.00  8.45           C  
ANISOU  722  C   ALA A  96      998    887   1326     92    -24    -65       C  
ATOM    723  O   ALA A  96      18.006 -71.810 115.614  1.00  8.23           O  
ANISOU  723  O   ALA A  96      982    845   1300     95     -8    -83       O  
ATOM    724  CB  ALA A  96      16.478 -71.266 118.681  1.00  9.12           C  
ANISOU  724  CB  ALA A  96     1090    997   1376     68    -52    -43       C  
ATOM    725  N   ALA A  97      19.081 -72.239 117.543  1.00  9.61           N  
ANISOU  725  N   ALA A  97     1129   1029   1493    104    -32    -47       N  
ATOM    726  CA  ALA A  97      19.889 -73.294 116.961  1.00 11.48           C  
ANISOU  726  CA  ALA A  97     1363   1240   1759    123    -20    -47       C  
ATOM    727  C   ALA A  97      19.016 -74.381 116.362  1.00 10.72           C  
ANISOU  727  C   ALA A  97     1289   1116   1666    121    -13    -55       C  
ATOM    728  O   ALA A  97      17.962 -74.709 116.908  1.00  9.58           O  
ANISOU  728  O   ALA A  97     1157    972   1511    109    -24    -47       O  
ATOM    729  CB  ALA A  97      20.818 -73.891 118.003  1.00 14.05           C  
ANISOU  729  CB  ALA A  97     1668   1564   2106    136    -34    -22       C  
ATOM    730  N   LYS A  98      19.461 -74.935 115.239  1.00 11.27           N  
ANISOU  730  N   LYS A  98     1366   1165   1752    134      6    -71       N  
ATOM    731  CA  LYS A  98      18.778 -76.083 114.639  1.00 11.55           C  
ANISOU  731  CA  LYS A  98     1423   1171   1795    135     12    -81       C  
ATOM    732  C   LYS A  98      18.693 -77.217 115.658  1.00 14.95           C  
ANISOU  732  C   LYS A  98     1852   1584   2246    138     -2    -57       C  
ATOM    733  O   LYS A  98      19.683 -77.551 116.304  1.00 19.09           O  
ANISOU  733  O   LYS A  98     2357   2105   2791    153     -6    -38       O  
ATOM    734  CB  LYS A  98      19.511 -76.538 113.375  1.00 16.06           C  
ANISOU  734  CB  LYS A  98     1999   1721   2381    152     36   -103       C  
ATOM    735  CG  LYS A  98      18.933 -77.773 112.721  1.00 18.86           C  
ANISOU  735  CG  LYS A  98     2379   2053   2734    150     40   -113       C  
ATOM    736  CD  LYS A  98      19.633 -78.044 111.395  1.00 22.87           C  
ANISOU  736  CD  LYS A  98     2897   2558   3234    162     62   -132       C  
ATOM    737  CE  LYS A  98      19.116 -79.315 110.742  1.00 34.08           C  
ANISOU  737  CE  LYS A  98     4342   3954   4654    161     65   -144       C  
ATOM    738  NZ  LYS A  98      19.701 -79.503 109.383  1.00 37.19           N  
ANISOU  738  NZ  LYS A  98     4748   4346   5035    173     85   -166       N  
ATOM    739  N   GLY A  99      17.499 -77.780 115.821  1.00 11.53           N  
ANISOU  739  N   GLY A  99     1436   1139   1807    123    -10    -55       N  
ATOM    740  CA  GLY A  99      17.283 -78.841 116.786  1.00 15.95           C  
ANISOU  740  CA  GLY A  99     1995   1682   2384    124    -22    -29       C  
ATOM    741  C   GLY A  99      16.818 -78.347 118.146  1.00 16.06           C  
ANISOU  741  C   GLY A  99     1999   1723   2380    112    -41     -2       C  
ATOM    742  O   GLY A  99      16.504 -79.151 119.021  1.00 15.51           O  
ANISOU  742  O   GLY A  99     1929   1643   2320    110    -52     23       O  
ATOM    743  N   SER A 100      16.794 -77.028 118.336  1.00 12.46           N  
ANISOU  743  N   SER A 100     1535   1301   1897    104    -45     -7       N  
ATOM    744  CA  SER A 100      16.334 -76.454 119.606  1.00 12.88           C  
ANISOU  744  CA  SER A 100     1582   1383   1930     92    -62     14       C  
ATOM    745  C   SER A 100      14.916 -76.891 119.930  1.00 15.17           C  
ANISOU  745  C   SER A 100     1887   1668   2209     75    -67     22       C  
ATOM    746  O   SER A 100      14.075 -76.954 119.041  1.00 14.57           O  
ANISOU  746  O   SER A 100     1825   1581   2128     65    -59      3       O  
ATOM    747  CB  SER A 100      16.390 -74.929 119.581  1.00 13.15           C  
ANISOU  747  CB  SER A 100     1610   1449   1938     85    -62      1       C  
ATOM    748  OG  SER A 100      15.790 -74.386 120.753  1.00 13.73           O  
ANISOU  748  OG  SER A 100     1681   1549   1988     74    -77     17       O  
ATOM    749  N   PRO A 101      14.651 -77.200 121.210  1.00 17.18           N  
ANISOU  749  N   PRO A 101     2137   1932   2459     72    -80     52       N  
ATOM    750  CA  PRO A 101      13.312 -77.595 121.652  1.00 18.88           C  
ANISOU  750  CA  PRO A 101     2363   2146   2666     55    -84     64       C  
ATOM    751  C   PRO A 101      12.435 -76.397 121.993  1.00 15.47           C  
ANISOU  751  C   PRO A 101     1931   1747   2199     40    -87     59       C  
ATOM    752  O   PRO A 101      11.267 -76.581 122.328  1.00 11.75           O  
ANISOU  752  O   PRO A 101     1467   1278   1718     25    -88     68       O  
ATOM    753  CB  PRO A 101      13.597 -78.428 122.900  1.00 19.70           C  
ANISOU  753  CB  PRO A 101     2459   2246   2779     62    -96    101       C  
ATOM    754  CG  PRO A 101      14.825 -77.811 123.464  1.00 20.31           C  
ANISOU  754  CG  PRO A 101     2520   2346   2852     76   -104    108       C  
ATOM    755  CD  PRO A 101      15.638 -77.301 122.301  1.00 19.07           C  
ANISOU  755  CD  PRO A 101     2359   2182   2703     85    -93     77       C  
ATOM    756  N   ILE A 102      13.000 -75.195 121.889  1.00 11.53           N  
ANISOU  756  N   ILE A 102     1425   1272   1683     43    -87     44       N  
ATOM    757  CA  ILE A 102      12.290 -73.961 122.223  1.00  8.58           C  
ANISOU  757  CA  ILE A 102     1052    929   1279     31    -88     37       C  
ATOM    758  C   ILE A 102      10.983 -73.789 121.449  1.00 10.36           C  
ANISOU  758  C   ILE A 102     1289   1150   1495     16    -80     22       C  
ATOM    759  O   ILE A 102      10.885 -74.114 120.262  1.00 11.72           O  
ANISOU  759  O   ILE A 102     1470   1302   1680     16    -72      3       O  
ATOM    760  CB  ILE A 102      13.213 -72.746 121.990  1.00 12.67           C  
ANISOU  760  CB  ILE A 102     1560   1465   1788     37    -88     20       C  
ATOM    761  CG1 ILE A 102      14.253 -72.696 123.112  1.00 17.88           C  
ANISOU  761  CG1 ILE A 102     2205   2139   2448     47   -101     39       C  
ATOM    762  CG2 ILE A 102      12.430 -71.432 121.964  1.00 19.13           C  
ANISOU  762  CG2 ILE A 102     2382   2307   2579     25    -86      6       C  
ATOM    763  CD1 ILE A 102      15.167 -71.496 123.050  1.00 22.27           C  
ANISOU  763  CD1 ILE A 102     2750   2714   2998     51   -104     24       C  
ATOM    764  N   GLN A 103       9.976 -73.303 122.167  1.00 12.88           N  
ANISOU  764  N   GLN A 103     1610   1491   1793      5    -83     31       N  
ATOM    765  CA  GLN A 103       8.659 -73.006 121.627  1.00 13.98           C  
ANISOU  765  CA  GLN A 103     1758   1633   1922    -10    -78     20       C  
ATOM    766  C   GLN A 103       8.225 -71.623 122.095  1.00 13.51           C  
ANISOU  766  C   GLN A 103     1694   1605   1834    -15    -78     15       C  
ATOM    767  O   GLN A 103       8.625 -71.185 123.174  1.00  9.10           O  
ANISOU  767  O   GLN A 103     1129   1066   1261    -10    -84     26       O  
ATOM    768  CB  GLN A 103       7.649 -74.060 122.085  1.00 15.74           C  
ANISOU  768  CB  GLN A 103     1984   1844   2153    -21    -80     42       C  
ATOM    769  CG  GLN A 103       7.858 -75.416 121.457  1.00 13.49           C  
ANISOU  769  CG  GLN A 103     1704   1521   1898    -19    -79     43       C  
ATOM    770  CD  GLN A 103       7.331 -75.473 120.036  1.00 21.85           C  
ANISOU  770  CD  GLN A 103     2774   2564   2964    -27    -73     15       C  
ATOM    771  OE1 GLN A 103       6.426 -74.723 119.669  1.00 24.38           O  
ANISOU  771  OE1 GLN A 103     3096   2900   3269    -38    -71      4       O  
ATOM    772  NE2 GLN A 103       7.891 -76.366 119.231  1.00 25.33           N  
ANISOU  772  NE2 GLN A 103     3221   2974   3428    -20    -71      5       N  
ATOM    773  N   PRO A 104       7.392 -70.936 121.297  1.00  9.50           N  
ANISOU  773  N   PRO A 104     1191   1102   1317    -23    -71     -3       N  
ATOM    774  CA  PRO A 104       6.889 -69.618 121.694  1.00 12.75           C  
ANISOU  774  CA  PRO A 104     1599   1541   1704    -27    -70     -8       C  
ATOM    775  C   PRO A 104       5.795 -69.727 122.753  1.00 13.88           C  
ANISOU  775  C   PRO A 104     1741   1700   1834    -35    -71     11       C  
ATOM    776  O   PRO A 104       4.686 -69.235 122.558  1.00 11.86           O  
ANISOU  776  O   PRO A 104     1485   1453   1568    -43    -65      7       O  
ATOM    777  CB  PRO A 104       6.340 -69.048 120.382  1.00 11.74           C  
ANISOU  777  CB  PRO A 104     1477   1409   1576    -32    -63    -30       C  
ATOM    778  CG  PRO A 104       5.918 -70.274 119.597  1.00  9.30           C  
ANISOU  778  CG  PRO A 104     1174   1074   1285    -38    -62    -30       C  
ATOM    779  CD  PRO A 104       6.981 -71.296 119.924  1.00  8.76           C  
ANISOU  779  CD  PRO A 104     1105    988   1235    -28    -66    -20       C  
ATOM    780  N   THR A 105       6.115 -70.382 123.866  1.00 11.00           N  
ANISOU  780  N   THR A 105     1373   1338   1468    -31    -76     34       N  
ATOM    781  CA  THR A 105       5.189 -70.502 124.985  1.00 14.09           C  
ANISOU  781  CA  THR A 105     1763   1746   1844    -37    -76     56       C  
ATOM    782  C   THR A 105       5.855 -70.021 126.269  1.00 14.03           C  
ANISOU  782  C   THR A 105     1753   1763   1816    -28    -82     67       C  
ATOM    783  O   THR A 105       7.083 -70.038 126.374  1.00 11.63           O  
ANISOU  783  O   THR A 105     1446   1456   1517    -19    -90     64       O  
ATOM    784  CB  THR A 105       4.730 -71.943 125.172  1.00 14.82           C  
ANISOU  784  CB  THR A 105     1856   1819   1955    -43    -76     81       C  
ATOM    785  OG1 THR A 105       5.833 -72.741 125.612  1.00 13.59           O  
ANISOU  785  OG1 THR A 105     1700   1652   1812    -33    -84     95       O  
ATOM    786  CG2 THR A 105       4.175 -72.504 123.862  1.00 17.24           C  
ANISOU  786  CG2 THR A 105     2167   2100   2284    -52    -73     68       C  
ATOM    787  N   LEU A 106       5.057 -69.597 127.245  1.00  9.54           N  
ANISOU  787  N   LEU A 106     1184   1219   1223    -31    -78     78       N  
ATOM    788  CA  LEU A 106       5.615 -69.161 128.525  1.00 15.45           C  
ANISOU  788  CA  LEU A 106     1931   1993   1947    -24    -85     86       C  
ATOM    789  C   LEU A 106       6.346 -70.300 129.235  1.00 17.36           C  
ANISOU  789  C   LEU A 106     2172   2228   2197    -18    -96    113       C  
ATOM    790  O   LEU A 106       7.396 -70.086 129.853  1.00 18.11           O  
ANISOU  790  O   LEU A 106     2264   2334   2282     -9   -108    115       O  
ATOM    791  CB  LEU A 106       4.521 -68.594 129.433  1.00 13.62           C  
ANISOU  791  CB  LEU A 106     1701   1788   1687    -27    -77     94       C  
ATOM    792  CG  LEU A 106       3.869 -67.273 129.019  1.00 18.63           C  
ANISOU  792  CG  LEU A 106     2337   2434   2309    -30    -67     68       C  
ATOM    793  CD1 LEU A 106       2.709 -66.948 129.956  1.00 24.02           C  
ANISOU  793  CD1 LEU A 106     3020   3142   2966    -32    -55     80       C  
ATOM    794  CD2 LEU A 106       4.883 -66.136 128.996  1.00 24.35           C  
ANISOU  794  CD2 LEU A 106     3062   3166   3023    -22    -74     43       C  
ATOM    795  N   GLU A 107       5.810 -71.513 129.128  1.00 17.13           N  
ANISOU  795  N   GLU A 107     2143   2180   2186    -24    -92    135       N  
ATOM    796  CA  GLU A 107       6.431 -72.681 129.746  1.00 19.29           C  
ANISOU  796  CA  GLU A 107     2415   2443   2471    -18   -101    165       C  
ATOM    797  C   GLU A 107       7.818 -72.970 129.164  1.00 18.00           C  
ANISOU  797  C   GLU A 107     2248   2259   2330     -7   -111    155       C  
ATOM    798  O   GLU A 107       8.739 -73.346 129.890  1.00 15.62           O  
ANISOU  798  O   GLU A 107     1943   1963   2028      3   -123    172       O  
ATOM    799  CB  GLU A 107       5.528 -73.907 129.589  1.00 22.93           C  
ANISOU  799  CB  GLU A 107     2877   2882   2954    -27    -94    188       C  
ATOM    800  N   SER A 108       7.969 -72.781 127.857  1.00 15.17           N  
ANISOU  800  N   SER A 108     1891   1882   1992     -9   -106    128       N  
ATOM    801  CA  SER A 108       9.241 -73.033 127.200  1.00 12.87           C  
ANISOU  801  CA  SER A 108     1595   1571   1723      2   -111    118       C  
ATOM    802  C   SER A 108      10.221 -71.871 127.409  1.00  9.54           C  
ANISOU  802  C   SER A 108     1167   1170   1286     10   -119    101       C  
ATOM    803  O   SER A 108      11.412 -72.089 127.624  1.00 12.69           O  
ANISOU  803  O   SER A 108     1559   1567   1696     21   -129    106       O  
ATOM    804  CB  SER A 108       9.028 -73.284 125.703  1.00 12.48           C  
ANISOU  804  CB  SER A 108     1551   1493   1697     -2   -102     95       C  
ATOM    805  OG  SER A 108      10.260 -73.498 125.041  1.00 16.75           O  
ANISOU  805  OG  SER A 108     2087   2017   2259     10   -103     84       O  
ATOM    806  N   LEU A 109       9.711 -70.643 127.382  1.00 12.93           N  
ANISOU  806  N   LEU A 109     1599   1620   1693      3   -114     82       N  
ATOM    807  CA  LEU A 109      10.584 -69.468 127.399  1.00  8.54           C  
ANISOU  807  CA  LEU A 109     1037   1079   1127      8   -120     61       C  
ATOM    808  C   LEU A 109      10.934 -68.999 128.803  1.00 12.36           C  
ANISOU  808  C   LEU A 109     1519   1593   1584     11   -133     72       C  
ATOM    809  O   LEU A 109      11.744 -68.091 128.968  1.00 11.09           O  
ANISOU  809  O   LEU A 109     1353   1445   1417     14   -142     57       O  
ATOM    810  CB  LEU A 109       9.940 -68.319 126.622  1.00  7.43           C  
ANISOU  810  CB  LEU A 109      901    943    978      1   -109     34       C  
ATOM    811  CG  LEU A 109       9.796 -68.590 125.119  1.00 10.90           C  
ANISOU  811  CG  LEU A 109     1344   1357   1441     -1    -98     19       C  
ATOM    812  CD1 LEU A 109       9.019 -67.480 124.424  1.00  9.69           C  
ANISOU  812  CD1 LEU A 109     1195   1210   1276     -8    -88     -3       C  
ATOM    813  CD2 LEU A 109      11.172 -68.805 124.453  1.00  6.96           C  
ANISOU  813  CD2 LEU A 109      838    842    965      8   -101     11       C  
ATOM    814  N   LYS A 110      10.310 -69.590 129.816  1.00 13.80           N  
ANISOU  814  N   LYS A 110     1705   1786   1750     10   -135     97       N  
ATOM    815  CA  LYS A 110      10.627 -69.224 131.193  1.00 14.78           C  
ANISOU  815  CA  LYS A 110     1829   1941   1845     13   -149    109       C  
ATOM    816  C   LYS A 110      12.115 -69.376 131.466  1.00 13.22           C  
ANISOU  816  C   LYS A 110     1621   1744   1658     23   -168    113       C  
ATOM    817  O   LYS A 110      12.688 -70.451 131.267  1.00 14.36           O  
ANISOU  817  O   LYS A 110     1760   1869   1827     30   -172    131       O  
ATOM    818  CB  LYS A 110       9.834 -70.077 132.188  1.00 19.37           C  
ANISOU  818  CB  LYS A 110     2416   2532   2411     12   -147    142       C  
ATOM    819  CG  LYS A 110      10.002 -69.622 133.634  1.00 24.81           C  
ANISOU  819  CG  LYS A 110     3108   3257   3062     16   -159    152       C  
ATOM    820  N   GLY A 111      12.742 -68.285 131.899  1.00  8.90           N  
ANISOU  820  N   GLY A 111     1072   1218   1093     24   -179     95       N  
ATOM    821  CA  GLY A 111      14.156 -68.299 132.236  1.00 11.02           C  
ANISOU  821  CA  GLY A 111     1327   1491   1369     32   -200     98       C  
ATOM    822  C   GLY A 111      15.089 -68.251 131.043  1.00  9.99           C  
ANISOU  822  C   GLY A 111     1184   1336   1275     35   -197     83       C  
ATOM    823  O   GLY A 111      16.309 -68.336 131.213  1.00 16.04           O  
ANISOU  823  O   GLY A 111     1937   2104   2055     42   -213     87       O  
ATOM    824  N   LYS A 112      14.539 -68.096 129.839  1.00 10.38           N  
ANISOU  824  N   LYS A 112     1238   1365   1340     31   -178     65       N  
ATOM    825  CA  LYS A 112      15.369 -68.023 128.634  1.00  9.63           C  
ANISOU  825  CA  LYS A 112     1134   1249   1277     34   -172     49       C  
ATOM    826  C   LYS A 112      15.686 -66.581 128.231  1.00 10.32           C  
ANISOU  826  C   LYS A 112     1217   1345   1359     29   -170     20       C  
ATOM    827  O   LYS A 112      14.928 -65.661 128.544  1.00 11.08           O  
ANISOU  827  O   LYS A 112     1322   1456   1431     21   -168      7       O  
ATOM    828  CB  LYS A 112      14.685 -68.729 127.456  1.00 10.47           C  
ANISOU  828  CB  LYS A 112     1248   1327   1403     33   -152     47       C  
ATOM    829  CG  LYS A 112      14.365 -70.201 127.669  1.00 18.56           C  
ANISOU  829  CG  LYS A 112     2276   2336   2440     38   -151     74       C  
ATOM    830  CD  LYS A 112      15.607 -71.024 127.907  1.00 21.89           C  
ANISOU  830  CD  LYS A 112     2685   2748   2884     51   -163     92       C  
ATOM    831  CE  LYS A 112      15.360 -72.492 127.582  1.00 28.62           C  
ANISOU  831  CE  LYS A 112     3541   3571   3761     57   -156    111       C  
ATOM    832  NZ  LYS A 112      14.219 -73.054 128.360  1.00 28.38           N  
ANISOU  832  NZ  LYS A 112     3522   3546   3715     49   -156    133       N  
ATOM    833  N   HIS A 113      16.814 -66.396 127.546  1.00  9.04           N  
ANISOU  833  N   HIS A 113     1041   1171   1222     33   -171     11       N  
ATOM    834  CA  HIS A 113      17.184 -65.091 127.004  1.00  8.36           C  
ANISOU  834  CA  HIS A 113      951   1089   1139     27   -168    -15       C  
ATOM    835  C   HIS A 113      16.756 -64.981 125.547  1.00 10.39           C  
ANISOU  835  C   HIS A 113     1213   1324   1410     26   -145    -30       C  
ATOM    836  O   HIS A 113      17.248 -65.713 124.681  1.00  9.99           O  
ANISOU  836  O   HIS A 113     1157   1254   1384     34   -136    -26       O  
ATOM    837  CB  HIS A 113      18.693 -64.834 127.126  1.00 11.17           C  
ANISOU  837  CB  HIS A 113     1285   1448   1513     32   -182    -16       C  
ATOM    838  CG  HIS A 113      19.128 -64.494 128.515  1.00 13.14           C  
ANISOU  838  CG  HIS A 113     1528   1722   1742     30   -208    -10       C  
ATOM    839  ND1 HIS A 113      19.142 -65.421 129.532  1.00 18.33           N  
ANISOU  839  ND1 HIS A 113     2187   2390   2389     36   -223     16       N  
ATOM    840  CD2 HIS A 113      19.525 -63.324 129.065  1.00 17.94           C  
ANISOU  840  CD2 HIS A 113     2131   2347   2337     22   -222    -26       C  
ATOM    841  CE1 HIS A 113      19.546 -64.842 130.648  1.00 20.17           C  
ANISOU  841  CE1 HIS A 113     2416   2648   2600     33   -246     15       C  
ATOM    842  NE2 HIS A 113      19.779 -63.569 130.394  1.00 19.33           N  
ANISOU  842  NE2 HIS A 113     2307   2546   2493     23   -247    -12       N  
ATOM    843  N   VAL A 114      15.827 -64.061 125.303  1.00  6.89           N  
ANISOU  843  N   VAL A 114      781    887    951     17   -135    -46       N  
ATOM    844  CA  VAL A 114      15.268 -63.827 123.974  1.00  8.00           C  
ANISOU  844  CA  VAL A 114      928   1012   1099     15   -115    -59       C  
ATOM    845  C   VAL A 114      15.628 -62.433 123.495  1.00  7.20           C  
ANISOU  845  C   VAL A 114      823    914   1000     10   -111    -80       C  
ATOM    846  O   VAL A 114      15.276 -61.442 124.136  1.00  8.88           O  
ANISOU  846  O   VAL A 114     1039   1141   1194      3   -116    -89       O  
ATOM    847  CB  VAL A 114      13.727 -63.969 123.965  1.00  7.71           C  
ANISOU  847  CB  VAL A 114      908    977   1044      9   -106    -58       C  
ATOM    848  CG1 VAL A 114      13.176 -63.720 122.559  1.00  8.96           C  
ANISOU  848  CG1 VAL A 114     1074   1121   1211      6    -88    -71       C  
ATOM    849  CG2 VAL A 114      13.310 -65.331 124.505  1.00 12.77           C  
ANISOU  849  CG2 VAL A 114     1554   1614   1685     12   -110    -35       C  
ATOM    850  N   GLY A 115      16.334 -62.357 122.372  1.00  6.58           N  
ANISOU  850  N   GLY A 115      737    821    943     13   -100    -86       N  
ATOM    851  CA  GLY A 115      16.774 -61.084 121.833  1.00  7.03           C  
ANISOU  851  CA  GLY A 115      787    877   1006      8    -94   -103       C  
ATOM    852  C   GLY A 115      15.714 -60.467 120.937  1.00  6.10           C  
ANISOU  852  C   GLY A 115      684    755    879      4    -77   -114       C  
ATOM    853  O   GLY A 115      15.013 -61.181 120.200  1.00  8.68           O  
ANISOU  853  O   GLY A 115     1021   1072   1205      6    -66   -111       O  
ATOM    854  N   VAL A 116      15.590 -59.145 121.035  1.00  6.03           N  
ANISOU  854  N   VAL A 116      674    752    863     -3    -77   -126       N  
ATOM    855  CA  VAL A 116      14.698 -58.355 120.191  1.00  6.78           C  
ANISOU  855  CA  VAL A 116      780    843    952     -7    -62   -136       C  
ATOM    856  C   VAL A 116      15.394 -57.063 119.772  1.00  6.43           C  
ANISOU  856  C   VAL A 116      728    796    921    -11    -57   -147       C  
ATOM    857  O   VAL A 116      16.244 -56.550 120.488  1.00  9.17           O  
ANISOU  857  O   VAL A 116     1063   1147   1274    -15    -70   -151       O  
ATOM    858  CB  VAL A 116      13.359 -57.996 120.909  1.00  6.26           C  
ANISOU  858  CB  VAL A 116      728    789    863    -11    -65   -138       C  
ATOM    859  CG1 VAL A 116      12.536 -59.240 121.155  1.00  5.77           C  
ANISOU  859  CG1 VAL A 116      673    728    790     -9    -66   -125       C  
ATOM    860  CG2 VAL A 116      13.614 -57.268 122.214  1.00  9.46           C  
ANISOU  860  CG2 VAL A 116     1130   1207   1257    -15    -79   -144       C  
ATOM    861  N   LEU A 117      15.008 -56.512 118.627  1.00  5.93           N  
ANISOU  861  N   LEU A 117      670    724    860    -12    -41   -152       N  
ATOM    862  CA  LEU A 117      15.590 -55.244 118.188  1.00  8.31           C  
ANISOU  862  CA  LEU A 117      963   1020   1174    -16    -35   -160       C  
ATOM    863  C   LEU A 117      14.906 -54.029 118.837  1.00 10.21           C  
ANISOU  863  C   LEU A 117     1210   1265   1403    -23    -39   -170       C  
ATOM    864  O   LEU A 117      13.670 -53.927 118.838  1.00  8.19           O  
ANISOU  864  O   LEU A 117      967   1012   1130    -22    -35   -171       O  
ATOM    865  CB  LEU A 117      15.509 -55.145 116.663  1.00 10.08           C  
ANISOU  865  CB  LEU A 117     1191   1234   1405    -13    -14   -158       C  
ATOM    866  CG  LEU A 117      16.080 -53.875 116.029  1.00  8.36           C  
ANISOU  866  CG  LEU A 117      965   1009   1202    -17     -4   -162       C  
ATOM    867  CD1 LEU A 117      17.615 -53.886 116.083  1.00 11.64           C  
ANISOU  867  CD1 LEU A 117     1361   1421   1642    -18     -5   -160       C  
ATOM    868  CD2 LEU A 117      15.581 -53.736 114.604  1.00  9.23           C  
ANISOU  868  CD2 LEU A 117     1085   1112   1308    -13     16   -159       C  
ATOM    869  N   GLN A 118      15.709 -53.119 119.400  1.00  7.55           N  
ANISOU  869  N   GLN A 118      863    928   1077    -29    -48   -179       N  
ATOM    870  CA  GLN A 118      15.168 -51.885 119.982  1.00  9.83           C  
ANISOU  870  CA  GLN A 118     1159   1218   1358    -35    -51   -192       C  
ATOM    871  C   GLN A 118      14.270 -51.130 119.022  1.00 10.17           C  
ANISOU  871  C   GLN A 118     1212   1252   1401    -34    -34   -193       C  
ATOM    872  O   GLN A 118      14.644 -50.899 117.872  1.00 12.24           O  
ANISOU  872  O   GLN A 118     1469   1503   1677    -34    -20   -188       O  
ATOM    873  CB  GLN A 118      16.295 -50.942 120.387  1.00 13.64           C  
ANISOU  873  CB  GLN A 118     1627   1695   1859    -44    -61   -202       C  
ATOM    874  CG  GLN A 118      16.696 -50.968 121.822  1.00 29.39           C  
ANISOU  874  CG  GLN A 118     3619   3702   3845    -49    -85   -210       C  
ATOM    875  CD  GLN A 118      17.567 -49.778 122.143  1.00 33.33           C  
ANISOU  875  CD  GLN A 118     4108   4194   4362    -60    -94   -224       C  
ATOM    876  OE1 GLN A 118      18.522 -49.492 121.422  1.00 31.00           O  
ANISOU  876  OE1 GLN A 118     3797   3888   4095    -64    -89   -220       O  
ATOM    877  NE2 GLN A 118      17.224 -49.056 123.204  1.00 37.56           N  
ANISOU  877  NE2 GLN A 118     4654   4736   4881    -63   -105   -236       N  
ATOM    878  N   GLY A 119      13.093 -50.739 119.498  1.00 10.43           N  
ANISOU  878  N   GLY A 119     1258   1291   1416    -33    -33   -199       N  
ATOM    879  CA  GLY A 119      12.176 -49.932 118.727  1.00 11.90           C  
ANISOU  879  CA  GLY A 119     1452   1469   1601    -31    -19   -199       C  
ATOM    880  C   GLY A 119      11.279 -50.713 117.795  1.00 17.47           C  
ANISOU  880  C   GLY A 119     2164   2176   2297    -25     -8   -187       C  
ATOM    881  O   GLY A 119      10.472 -50.123 117.081  1.00 16.00           O  
ANISOU  881  O   GLY A 119     1984   1986   2109    -22      3   -185       O  
ATOM    882  N   SER A 120      11.421 -52.037 117.794  1.00  9.04           N  
ANISOU  882  N   SER A 120     1095   1115   1224    -22    -12   -179       N  
ATOM    883  CA  SER A 120      10.652 -52.893 116.897  1.00  8.75           C  
ANISOU  883  CA  SER A 120     1066   1079   1180    -18     -5   -170       C  
ATOM    884  C   SER A 120       9.310 -53.313 117.486  1.00  8.91           C  
ANISOU  884  C   SER A 120     1094   1109   1181    -17     -8   -167       C  
ATOM    885  O   SER A 120       9.080 -53.236 118.699  1.00  7.92           O  
ANISOU  885  O   SER A 120      969    993   1047    -18    -17   -170       O  
ATOM    886  CB  SER A 120      11.442 -54.154 116.546  1.00  8.15           C  
ANISOU  886  CB  SER A 120      985   1000   1110    -16     -6   -163       C  
ATOM    887  OG  SER A 120      11.602 -54.959 117.700  1.00  8.19           O  
ANISOU  887  OG  SER A 120      989   1014   1110    -16    -20   -161       O  
ATOM    888  N   THR A 121       8.429 -53.792 116.617  1.00  9.57           N  
ANISOU  888  N   THR A 121     1184   1193   1259    -15     -2   -160       N  
ATOM    889  CA  THR A 121       7.176 -54.361 117.084  1.00  8.86           C  
ANISOU  889  CA  THR A 121     1099   1112   1155    -15     -5   -155       C  
ATOM    890  C   THR A 121       7.454 -55.657 117.843  1.00  6.63           C  
ANISOU  890  C   THR A 121      815    834    869    -17    -15   -149       C  
ATOM    891  O   THR A 121       6.700 -56.029 118.750  1.00  9.56           O  
ANISOU  891  O   THR A 121     1187   1214   1229    -18    -19   -144       O  
ATOM    892  CB  THR A 121       6.209 -54.612 115.918  1.00 15.61           C  
ANISOU  892  CB  THR A 121     1958   1965   2006    -15      1   -149       C  
ATOM    893  OG1 THR A 121       6.752 -55.617 115.056  1.00 20.62           O  
ANISOU  893  OG1 THR A 121     2595   2593   2646    -15      1   -146       O  
ATOM    894  CG2 THR A 121       6.029 -53.327 115.132  1.00 13.34           C  
ANISOU  894  CG2 THR A 121     1672   1674   1724    -12     10   -151       C  
ATOM    895  N   GLN A 122       8.541 -56.339 117.487  1.00  8.62           N  
ANISOU  895  N   GLN A 122     1065   1079   1133    -16    -16   -148       N  
ATOM    896  CA  GLN A 122       8.927 -57.558 118.211  1.00  7.69           C  
ANISOU  896  CA  GLN A 122      944    963   1015    -16    -26   -141       C  
ATOM    897  C   GLN A 122       9.269 -57.223 119.658  1.00  6.93           C  
ANISOU  897  C   GLN A 122      843    876    912    -16    -36   -142       C  
ATOM    898  O   GLN A 122       8.878 -57.944 120.586  1.00  8.27           O  
ANISOU  898  O   GLN A 122     1015   1055   1072    -17    -43   -133       O  
ATOM    899  CB  GLN A 122      10.117 -58.265 117.545  1.00  7.98           C  
ANISOU  899  CB  GLN A 122      976    988   1067    -12    -24   -140       C  
ATOM    900  CG  GLN A 122       9.768 -58.932 116.218  1.00 11.48           C  
ANISOU  900  CG  GLN A 122     1427   1422   1514    -11    -16   -139       C  
ATOM    901  CD  GLN A 122       9.577 -57.912 115.105  1.00 15.22           C  
ANISOU  901  CD  GLN A 122     1903   1893   1986    -11     -4   -145       C  
ATOM    902  OE1 GLN A 122      10.186 -56.844 115.128  1.00 13.88           O  
ANISOU  902  OE1 GLN A 122     1728   1724   1822    -10     -1   -150       O  
ATOM    903  NE2 GLN A 122       8.740 -58.240 114.129  1.00 12.81           N  
ANISOU  903  NE2 GLN A 122     1606   1585   1674    -11      0   -145       N  
ATOM    904  N   GLU A 123      10.016 -56.139 119.848  1.00  6.62           N  
ANISOU  904  N   GLU A 123      799    837    878    -17    -37   -152       N  
ATOM    905  CA  GLU A 123      10.345 -55.693 121.201  1.00  6.66           C  
ANISOU  905  CA  GLU A 123      802    853    875    -19    -49   -157       C  
ATOM    906  C   GLU A 123       9.078 -55.366 121.998  1.00  7.89           C  
ANISOU  906  C   GLU A 123      966   1021   1010    -18    -48   -158       C  
ATOM    907  O   GLU A 123       8.951 -55.749 123.154  1.00  8.36           O  
ANISOU  907  O   GLU A 123     1028   1094   1055    -18    -56   -154       O  
ATOM    908  CB  GLU A 123      11.260 -54.472 121.165  1.00  8.23           C  
ANISOU  908  CB  GLU A 123      994   1047   1085    -21    -50   -170       C  
ATOM    909  CG  GLU A 123      11.536 -53.877 122.547  1.00 12.59           C  
ANISOU  909  CG  GLU A 123     1546   1610   1626    -24    -64   -180       C  
ATOM    910  CD  GLU A 123      12.295 -52.566 122.476  1.00 12.76           C  
ANISOU  910  CD  GLU A 123     1563   1624   1662    -29    -66   -195       C  
ATOM    911  OE1 GLU A 123      11.861 -51.665 121.730  1.00 13.59           O  
ANISOU  911  OE1 GLU A 123     1672   1719   1774    -30    -53   -201       O  
ATOM    912  OE2 GLU A 123      13.333 -52.442 123.164  1.00 16.81           O  
ANISOU  912  OE2 GLU A 123     2068   2140   2180    -33    -81   -200       O  
ATOM    913  N   ALA A 124       8.158 -54.654 121.358  1.00  8.34           N  
ANISOU  913  N   ALA A 124     1027   1075   1066    -18    -36   -162       N  
ATOM    914  CA  ALA A 124       6.910 -54.254 122.000  1.00  9.76           C  
ANISOU  914  CA  ALA A 124     1214   1266   1230    -16    -31   -163       C  
ATOM    915  C   ALA A 124       6.143 -55.494 122.434  1.00 10.74           C  
ANISOU  915  C   ALA A 124     1339   1400   1342    -16    -33   -147       C  
ATOM    916  O   ALA A 124       5.696 -55.592 123.583  1.00 10.20           O  
ANISOU  916  O   ALA A 124     1273   1345   1257    -15    -35   -145       O  
ATOM    917  CB  ALA A 124       6.065 -53.389 121.060  1.00  9.65           C  
ANISOU  917  CB  ALA A 124     1201   1245   1220    -14    -19   -166       C  
ATOM    918  N   TYR A 125       6.007 -56.455 121.521  1.00  7.09           N  
ANISOU  918  N   TYR A 125      875    928    889    -18    -31   -137       N  
ATOM    919  CA  TYR A 125       5.295 -57.686 121.838  1.00  9.46           C  
ANISOU  919  CA  TYR A 125     1177   1234   1183    -20    -33   -122       C  
ATOM    920  C   TYR A 125       5.952 -58.446 122.992  1.00 11.03           C  
ANISOU  920  C   TYR A 125     1375   1441   1376    -19    -43   -113       C  
ATOM    921  O   TYR A 125       5.284 -58.863 123.942  1.00  9.15           O  
ANISOU  921  O   TYR A 125     1139   1215   1124    -19    -44   -103       O  
ATOM    922  CB  TYR A 125       5.202 -58.605 120.616  1.00  7.77           C  
ANISOU  922  CB  TYR A 125      963   1006    983    -22    -31   -116       C  
ATOM    923  CG  TYR A 125       4.552 -59.916 120.986  1.00  6.10           C  
ANISOU  923  CG  TYR A 125      753    797    770    -26    -34   -100       C  
ATOM    924  CD1 TYR A 125       3.170 -60.051 120.964  1.00 11.06           C  
ANISOU  924  CD1 TYR A 125     1379   1430   1391    -30    -29    -92       C  
ATOM    925  CD2 TYR A 125       5.314 -61.014 121.391  1.00  9.88           C  
ANISOU  925  CD2 TYR A 125     1230   1270   1254    -26    -42    -91       C  
ATOM    926  CE1 TYR A 125       2.567 -61.226 121.321  1.00 10.31           C  
ANISOU  926  CE1 TYR A 125     1284   1336   1297    -35    -32    -76       C  
ATOM    927  CE2 TYR A 125       4.712 -62.201 121.747  1.00 10.64           C  
ANISOU  927  CE2 TYR A 125     1327   1365   1351    -30    -44    -74       C  
ATOM    928  CZ  TYR A 125       3.331 -62.302 121.712  1.00 11.50           C  
ANISOU  928  CZ  TYR A 125     1436   1480   1455    -35    -39    -67       C  
ATOM    929  OH  TYR A 125       2.711 -63.480 122.066  1.00 15.50           O  
ANISOU  929  OH  TYR A 125     1941   1984   1964    -41    -41    -50       O  
ATOM    930  N   ALA A 126       7.259 -58.647 122.902  1.00  8.34           N  
ANISOU  930  N   ALA A 126     1030   1092   1046    -18    -51   -116       N  
ATOM    931  CA  ALA A 126       7.961 -59.423 123.920  1.00  8.52           C  
ANISOU  931  CA  ALA A 126     1051   1122   1065    -17    -64   -106       C  
ATOM    932  C   ALA A 126       7.943 -58.701 125.259  1.00  7.81           C  
ANISOU  932  C   ALA A 126      963   1051    954    -16    -70   -111       C  
ATOM    933  O   ALA A 126       7.779 -59.332 126.298  1.00  8.19           O  
ANISOU  933  O   ALA A 126     1013   1112    987    -15    -76    -98       O  
ATOM    934  CB  ALA A 126       9.390 -59.715 123.493  1.00  9.34           C  
ANISOU  934  CB  ALA A 126     1147   1214   1187    -14    -71   -108       C  
ATOM    935  N   ASN A 127       8.092 -57.384 125.244  1.00  9.15           N  
ANISOU  935  N   ASN A 127     1134   1222   1121    -16    -68   -130       N  
ATOM    936  CA  ASN A 127       8.026 -56.650 126.509  1.00 12.59           C  
ANISOU  936  CA  ASN A 127     1573   1674   1535    -15    -73   -139       C  
ATOM    937  C   ASN A 127       6.641 -56.706 127.148  1.00 12.22           C  
ANISOU  937  C   ASN A 127     1533   1642   1467    -13    -63   -132       C  
ATOM    938  O   ASN A 127       6.524 -56.771 128.368  1.00 13.21           O  
ANISOU  938  O   ASN A 127     1664   1786   1570    -11    -68   -129       O  
ATOM    939  CB  ASN A 127       8.442 -55.191 126.321  1.00  8.52           C  
ANISOU  939  CB  ASN A 127     1058   1153   1025    -16    -73   -162       C  
ATOM    940  CG  ASN A 127       9.959 -55.009 126.357  1.00 10.89           C  
ANISOU  940  CG  ASN A 127     1351   1449   1339    -19    -88   -169       C  
ATOM    941  OD1 ASN A 127      10.690 -55.892 126.790  1.00 13.29           O  
ANISOU  941  OD1 ASN A 127     1650   1758   1643    -19   -100   -157       O  
ATOM    942  ND2 ASN A 127      10.426 -53.855 125.909  1.00 13.12           N  
ANISOU  942  ND2 ASN A 127     1630   1720   1634    -23    -86   -186       N  
ATOM    943  N   ASP A 128       5.600 -56.687 126.325  1.00  8.24           N  
ANISOU  943  N   ASP A 128     1029   1131    969    -13    -49   -129       N  
ATOM    944  CA  ASP A 128       4.233 -56.631 126.842  1.00 10.17           C  
ANISOU  944  CA  ASP A 128     1277   1389   1197    -11    -37   -122       C  
ATOM    945  C   ASP A 128       3.675 -58.003 127.186  1.00 16.83           C  
ANISOU  945  C   ASP A 128     2119   2238   2036    -13    -37    -98       C  
ATOM    946  O   ASP A 128       2.705 -58.103 127.935  1.00 24.19           O  
ANISOU  946  O   ASP A 128     3053   3186   2952    -11    -29    -89       O  
ATOM    947  CB  ASP A 128       3.299 -55.954 125.841  1.00 13.92           C  
ANISOU  947  CB  ASP A 128     1751   1855   1683    -10    -24   -128       C  
ATOM    948  CG  ASP A 128       3.538 -54.462 125.727  1.00 12.46           C  
ANISOU  948  CG  ASP A 128     1569   1666   1500     -6    -20   -150       C  
ATOM    949  OD1 ASP A 128       2.952 -53.840 124.820  1.00 13.23           O  
ANISOU  949  OD1 ASP A 128     1664   1754   1609     -5    -11   -154       O  
ATOM    950  OD2 ASP A 128       4.321 -53.916 126.521  1.00 12.31           O  
ANISOU  950  OD2 ASP A 128     1553   1651   1472     -6    -28   -164       O  
ATOM    951  N   ASN A 129       4.274 -59.057 126.642  1.00 10.46           N  
ANISOU  951  N   ASN A 129     1309   1420   1246    -16    -45    -86       N  
ATOM    952  CA  ASN A 129       3.704 -60.395 126.794  1.00  8.58           C  
ANISOU  952  CA  ASN A 129     1069   1181   1009    -19    -44    -62       C  
ATOM    953  C   ASN A 129       4.613 -61.398 127.497  1.00 10.06           C  
ANISOU  953  C   ASN A 129     1257   1371   1196    -19    -57    -48       C  
ATOM    954  O   ASN A 129       4.121 -62.301 128.183  1.00 12.06           O  
ANISOU  954  O   ASN A 129     1509   1631   1441    -20    -56    -26       O  
ATOM    955  CB  ASN A 129       3.309 -60.957 125.421  1.00  9.42           C  
ANISOU  955  CB  ASN A 129     1173   1269   1139    -25    -40    -60       C  
ATOM    956  CG  ASN A 129       2.111 -60.235 124.823  1.00 13.51           C  
ANISOU  956  CG  ASN A 129     1689   1789   1657    -26    -28    -66       C  
ATOM    957  OD1 ASN A 129       2.255 -59.310 124.023  1.00 15.56           O  
ANISOU  957  OD1 ASN A 129     1949   2041   1922    -24    -25    -82       O  
ATOM    958  ND2 ASN A 129       0.922 -60.659 125.215  1.00 10.07           N  
ANISOU  958  ND2 ASN A 129     1250   1362   1215    -29    -21    -51       N  
ATOM    959  N   TRP A 130       5.923 -61.253 127.317  1.00 10.08           N  
ANISOU  959  N   TRP A 130     1257   1365   1207    -16    -68    -57       N  
ATOM    960  CA  TRP A 130       6.875 -62.240 127.821  1.00  9.90           C  
ANISOU  960  CA  TRP A 130     1231   1341   1189    -14    -82    -42       C  
ATOM    961  C   TRP A 130       7.732 -61.729 128.968  1.00  6.99           C  
ANISOU  961  C   TRP A 130      864    991    802    -10    -95    -46       C  
ATOM    962  O   TRP A 130       7.952 -62.442 129.949  1.00  8.94           O  
ANISOU  962  O   TRP A 130     1111   1250   1036     -8   -104    -28       O  
ATOM    963  CB  TRP A 130       7.797 -62.729 126.691  1.00  5.12           C  
ANISOU  963  CB  TRP A 130      620    712    611    -14    -85    -45       C  
ATOM    964  CG  TRP A 130       7.091 -63.599 125.667  1.00  8.52           C  
ANISOU  964  CG  TRP A 130     1052   1125   1060    -18    -76    -37       C  
ATOM    965  CD1 TRP A 130       5.857 -64.182 125.792  1.00  9.41           C  
ANISOU  965  CD1 TRP A 130     1167   1239   1168    -23    -69    -24       C  
ATOM    966  CD2 TRP A 130       7.583 -63.976 124.377  1.00  8.67           C  
ANISOU  966  CD2 TRP A 130     1070   1122   1103    -17    -74    -45       C  
ATOM    967  NE1 TRP A 130       5.553 -64.903 124.655  1.00 10.24           N  
ANISOU  967  NE1 TRP A 130     1274   1324   1294    -27    -65    -23       N  
ATOM    968  CE2 TRP A 130       6.601 -64.794 123.774  1.00 11.19           C  
ANISOU  968  CE2 TRP A 130     1392   1429   1430    -23    -67    -36       C  
ATOM    969  CE3 TRP A 130       8.758 -63.701 123.670  1.00 10.36           C  
ANISOU  969  CE3 TRP A 130     1280   1325   1332    -13    -76    -57       C  
ATOM    970  CZ2 TRP A 130       6.762 -65.334 122.499  1.00 10.52           C  
ANISOU  970  CZ2 TRP A 130     1309   1323   1365    -24    -64    -43       C  
ATOM    971  CZ3 TRP A 130       8.918 -64.243 122.413  1.00  9.28           C  
ANISOU  971  CZ3 TRP A 130     1144   1167   1214    -13    -70    -61       C  
ATOM    972  CH2 TRP A 130       7.924 -65.046 121.834  1.00  7.70           C  
ANISOU  972  CH2 TRP A 130      950    956   1019    -18    -64    -56       C  
ATOM    973  N   ARG A 131       8.237 -60.508 128.840  1.00 12.92           N  
ANISOU  973  N   ARG A 131     1614   1743   1551    -10    -98    -70       N  
ATOM    974  CA  ARG A 131       9.106 -59.937 129.872  1.00  7.95           C  
ANISOU  974  CA  ARG A 131      986   1131    906     -9   -114    -79       C  
ATOM    975  C   ARG A 131       8.436 -59.965 131.245  1.00 10.06           C  
ANISOU  975  C   ARG A 131     1261   1423   1138     -6   -114    -70       C  
ATOM    976  O   ARG A 131       9.084 -60.208 132.263  1.00  9.57           O  
ANISOU  976  O   ARG A 131     1200   1377   1059     -4   -130    -63       O  
ATOM    977  CB  ARG A 131       9.498 -58.499 129.502  1.00  5.65           C  
ANISOU  977  CB  ARG A 131      693    834    618    -11   -114   -108       C  
ATOM    978  CG  ARG A 131      10.339 -57.808 130.588  1.00  7.59           C  
ANISOU  978  CG  ARG A 131      941   1097    848    -11   -132   -121       C  
ATOM    979  CD  ARG A 131      10.636 -56.330 130.280  1.00 11.55           C  
ANISOU  979  CD  ARG A 131     1442   1591   1355    -15   -131   -150       C  
ATOM    980  NE  ARG A 131      11.148 -55.695 131.487  1.00 12.42           N  
ANISOU  980  NE  ARG A 131     1558   1720   1443    -17   -148   -164       N  
ATOM    981  CZ  ARG A 131      10.377 -55.148 132.424  1.00 14.88           C  
ANISOU  981  CZ  ARG A 131     1883   2049   1724    -14   -144   -174       C  
ATOM    982  NH1 ARG A 131       9.065 -55.124 132.255  1.00 13.61           N  
ANISOU  982  NH1 ARG A 131     1729   1888   1554    -10   -123   -170       N  
ATOM    983  NH2 ARG A 131      10.916 -54.618 133.520  1.00 17.29           N  
ANISOU  983  NH2 ARG A 131     2192   2370   2006    -16   -162   -189       N  
ATOM    984  N   THR A 132       7.124 -59.731 131.268  1.00  8.65           N  
ANISOU  984  N   THR A 132     1089   1250    948     -6    -97    -70       N  
ATOM    985  CA  THR A 132       6.413 -59.612 132.535  1.00 12.37           C  
ANISOU  985  CA  THR A 132     1568   1747   1384     -3    -93    -64       C  
ATOM    986  C   THR A 132       5.970 -60.966 133.088  1.00 12.01           C  
ANISOU  986  C   THR A 132     1522   1709   1331     -2    -91    -31       C  
ATOM    987  O   THR A 132       5.288 -61.027 134.110  1.00 13.32           O  
ANISOU  987  O   THR A 132     1696   1898   1469      1    -85    -20       O  
ATOM    988  CB  THR A 132       5.178 -58.706 132.372  1.00 11.01           C  
ANISOU  988  CB  THR A 132     1401   1578   1203     -2    -72    -78       C  
ATOM    989  OG1 THR A 132       4.327 -59.274 131.376  1.00 14.20           O  
ANISOU  989  OG1 THR A 132     1800   1967   1630     -5    -58    -65       O  
ATOM    990  CG2 THR A 132       5.603 -57.316 131.906  1.00 11.83           C  
ANISOU  990  CG2 THR A 132     1507   1673   1316     -2    -73   -110       C  
ATOM    991  N   LYS A 133       6.355 -62.042 132.405  1.00  8.87           N  
ANISOU  991  N   LYS A 133     1118   1293    961     -5    -96    -13       N  
ATOM    992  CA  LYS A 133       5.978 -63.395 132.805  1.00  8.60           C  
ANISOU  992  CA  LYS A 133     1082   1259    926     -5    -94     20       C  
ATOM    993  C   LYS A 133       7.175 -64.343 132.795  1.00 10.63           C  
ANISOU  993  C   LYS A 133     1333   1505   1199     -3   -112     35       C  
ATOM    994  O   LYS A 133       7.062 -65.510 132.397  1.00 14.50           O  
ANISOU  994  O   LYS A 133     1820   1980   1711     -4   -110     57       O  
ATOM    995  CB  LYS A 133       4.869 -63.924 131.902  1.00  8.45           C  
ANISOU  995  CB  LYS A 133     1060   1224    928    -11    -77     29       C  
ATOM    996  CG  LYS A 133       3.582 -63.120 132.038  1.00 13.36           C  
ANISOU  996  CG  LYS A 133     1685   1859   1534    -11    -59     21       C  
ATOM    997  CD  LYS A 133       2.533 -63.536 131.016  1.00 17.93           C  
ANISOU  997  CD  LYS A 133     2257   2420   2134    -18    -46     27       C  
ATOM    998  CE  LYS A 133       1.255 -62.755 131.245  1.00 29.03           C  
ANISOU  998  CE  LYS A 133     3663   3842   3526    -17    -27     22       C  
ATOM    999  NZ  LYS A 133       0.090 -63.363 130.553  1.00 37.69           N  
ANISOU  999  NZ  LYS A 133     4751   4928   4641    -25    -16     36       N  
ATOM   1000  N   GLY A 134       8.329 -63.827 133.205  1.00 10.65           N  
ANISOU 1000  N   GLY A 134     1335   1517   1196      1   -130     23       N  
ATOM   1001  CA  GLY A 134       9.473 -64.676 133.509  1.00 12.90           C  
ANISOU 1001  CA  GLY A 134     1613   1799   1491      5   -149     41       C  
ATOM   1002  C   GLY A 134      10.434 -64.973 132.373  1.00 10.73           C  
ANISOU 1002  C   GLY A 134     1328   1497   1254      6   -154     34       C  
ATOM   1003  O   GLY A 134      11.299 -65.836 132.513  1.00 14.55           O  
ANISOU 1003  O   GLY A 134     1804   1974   1751     11   -167     52       O  
ATOM   1004  N   VAL A 135      10.281 -64.266 131.260  1.00  8.58           N  
ANISOU 1004  N   VAL A 135     1054   1208    997      2   -143     10       N  
ATOM   1005  CA  VAL A 135      11.194 -64.390 130.127  1.00  6.25           C  
ANISOU 1005  CA  VAL A 135      750    890    736      3   -145      1       C  
ATOM   1006  C   VAL A 135      12.201 -63.240 130.169  1.00 10.59           C  
ANISOU 1006  C   VAL A 135     1293   1446   1285      3   -156    -22       C  
ATOM   1007  O   VAL A 135      11.832 -62.086 130.366  1.00  7.68           O  
ANISOU 1007  O   VAL A 135      930   1088    900     -1   -153    -42       O  
ATOM   1008  CB  VAL A 135      10.431 -64.379 128.787  1.00  5.28           C  
ANISOU 1008  CB  VAL A 135      629    746    632     -1   -126     -9       C  
ATOM   1009  CG1 VAL A 135      11.398 -64.615 127.621  1.00  8.28           C  
ANISOU 1009  CG1 VAL A 135     1001   1103   1044      2   -125    -16       C  
ATOM   1010  CG2 VAL A 135       9.287 -65.431 128.796  1.00  7.06           C  
ANISOU 1010  CG2 VAL A 135      860    965    857     -4   -115     13       C  
ATOM   1011  N   ASP A 136      13.476 -63.561 130.008  1.00  7.20           N  
ANISOU 1011  N   ASP A 136      851   1009    876      7   -169    -18       N  
ATOM   1012  CA  ASP A 136      14.499 -62.531 129.957  1.00 10.03           C  
ANISOU 1012  CA  ASP A 136     1200   1371   1240      5   -180    -39       C  
ATOM   1013  C   ASP A 136      14.621 -61.964 128.557  1.00 12.64           C  
ANISOU 1013  C   ASP A 136     1526   1680   1595      2   -165    -58       C  
ATOM   1014  O   ASP A 136      15.263 -62.554 127.691  1.00 11.87           O  
ANISOU 1014  O   ASP A 136     1420   1565   1525      7   -161    -53       O  
ATOM   1015  CB  ASP A 136      15.834 -63.098 130.432  1.00 12.59           C  
ANISOU 1015  CB  ASP A 136     1510   1699   1576     11   -201    -25       C  
ATOM   1016  CG  ASP A 136      15.780 -63.522 131.876  1.00 16.64           C  
ANISOU 1016  CG  ASP A 136     2027   2236   2059     14   -219     -7       C  
ATOM   1017  OD1 ASP A 136      16.081 -64.698 132.167  1.00 20.38           O  
ANISOU 1017  OD1 ASP A 136     2496   2707   2541     21   -226     21       O  
ATOM   1018  OD2 ASP A 136      15.416 -62.671 132.717  1.00 15.44           O  
ANISOU 1018  OD2 ASP A 136     1884   2106   1877      9   -225    -19       O  
ATOM   1019  N   VAL A 137      14.002 -60.808 128.359  1.00 10.59           N  
ANISOU 1019  N   VAL A 137     1275   1424   1325     -4   -156    -78       N  
ATOM   1020  CA  VAL A 137      13.961 -60.154 127.062  1.00  8.55           C  
ANISOU 1020  CA  VAL A 137     1015   1148   1086     -7   -140    -95       C  
ATOM   1021  C   VAL A 137      15.071 -59.111 126.968  1.00  9.82           C  
ANISOU 1021  C   VAL A 137     1165   1308   1260    -10   -149   -112       C  
ATOM   1022  O   VAL A 137      15.106 -58.139 127.720  1.00 15.24           O  
ANISOU 1022  O   VAL A 137     1853   2007   1930    -15   -158   -126       O  
ATOM   1023  CB  VAL A 137      12.579 -59.490 126.811  1.00  9.13           C  
ANISOU 1023  CB  VAL A 137     1102   1223   1145    -10   -124   -105       C  
ATOM   1024  CG1 VAL A 137      12.573 -58.700 125.507  1.00  9.53           C  
ANISOU 1024  CG1 VAL A 137     1151   1257   1213    -13   -110   -120       C  
ATOM   1025  CG2 VAL A 137      11.461 -60.543 126.828  1.00  8.25           C  
ANISOU 1025  CG2 VAL A 137      998   1111   1025     -9   -115    -87       C  
ATOM   1026  N   VAL A 138      15.975 -59.324 126.022  1.00  8.06           N  
ANISOU 1026  N   VAL A 138      929   1069   1065     -8   -145   -111       N  
ATOM   1027  CA  VAL A 138      17.150 -58.472 125.858  1.00  7.60           C  
ANISOU 1027  CA  VAL A 138      856   1009   1025    -12   -153   -123       C  
ATOM   1028  C   VAL A 138      17.030 -57.653 124.584  1.00  9.87           C  
ANISOU 1028  C   VAL A 138     1143   1279   1327    -15   -133   -136       C  
ATOM   1029  O   VAL A 138      16.903 -58.219 123.499  1.00  8.12           O  
ANISOU 1029  O   VAL A 138      922   1044   1119    -11   -117   -130       O  
ATOM   1030  CB  VAL A 138      18.431 -59.334 125.815  1.00 13.14           C  
ANISOU 1030  CB  VAL A 138     1538   1706   1748     -6   -163   -108       C  
ATOM   1031  CG1 VAL A 138      19.665 -58.471 125.685  1.00 11.97           C  
ANISOU 1031  CG1 VAL A 138     1371   1556   1622    -11   -172   -119       C  
ATOM   1032  CG2 VAL A 138      18.494 -60.239 127.046  1.00 12.43           C  
ANISOU 1032  CG2 VAL A 138     1449   1632   1643     -1   -183    -91       C  
ATOM   1033  N   ALA A 139      17.074 -56.326 124.716  1.00  6.68           N  
ANISOU 1033  N   ALA A 139      740    877    922    -24   -135   -154       N  
ATOM   1034  CA  ALA A 139      16.886 -55.433 123.571  1.00  8.36           C  
ANISOU 1034  CA  ALA A 139      954   1075   1148    -27   -116   -165       C  
ATOM   1035  C   ALA A 139      18.226 -54.988 123.000  1.00  8.89           C  
ANISOU 1035  C   ALA A 139     1000   1132   1244    -30   -117   -167       C  
ATOM   1036  O   ALA A 139      19.149 -54.642 123.751  1.00  9.82           O  
ANISOU 1036  O   ALA A 139     1106   1257   1369    -36   -136   -172       O  
ATOM   1037  CB  ALA A 139      16.056 -54.223 123.969  1.00  8.94           C  
ANISOU 1037  CB  ALA A 139     1040   1153   1206    -33   -115   -181       C  
ATOM   1038  N   TYR A 140      18.301 -54.963 121.672  1.00  7.63           N  
ANISOU 1038  N   TYR A 140      839    958   1101    -27    -96   -165       N  
ATOM   1039  CA  TYR A 140      19.539 -54.674 120.950  1.00  7.92           C  
ANISOU 1039  CA  TYR A 140      855    985   1168    -29    -91   -164       C  
ATOM   1040  C   TYR A 140      19.429 -53.418 120.095  1.00 10.12           C  
ANISOU 1040  C   TYR A 140     1135   1252   1456    -35    -75   -173       C  
ATOM   1041  O   TYR A 140      18.405 -53.170 119.468  1.00 10.28           O  
ANISOU 1041  O   TYR A 140     1172   1269   1466    -34    -60   -175       O  
ATOM   1042  CB  TYR A 140      19.914 -55.838 120.037  1.00  8.23           C  
ANISOU 1042  CB  TYR A 140      890   1017   1220    -18    -77   -150       C  
ATOM   1043  CG  TYR A 140      20.460 -57.057 120.732  1.00 11.11           C  
ANISOU 1043  CG  TYR A 140     1246   1389   1587    -10    -92   -138       C  
ATOM   1044  CD1 TYR A 140      19.645 -57.883 121.508  1.00  9.17           C  
ANISOU 1044  CD1 TYR A 140     1014   1151   1319     -6   -101   -131       C  
ATOM   1045  CD2 TYR A 140      21.793 -57.404 120.581  1.00 10.86           C  
ANISOU 1045  CD2 TYR A 140     1191   1354   1582     -6    -94   -130       C  
ATOM   1046  CE1 TYR A 140      20.164 -59.021 122.123  1.00  5.37           C  
ANISOU 1046  CE1 TYR A 140      525    674    842      1   -114   -117       C  
ATOM   1047  CE2 TYR A 140      22.317 -58.520 121.181  1.00 10.30           C  
ANISOU 1047  CE2 TYR A 140     1110   1286   1515      3   -108   -117       C  
ATOM   1048  CZ  TYR A 140      21.510 -59.324 121.958  1.00  9.27           C  
ANISOU 1048  CZ  TYR A 140      996   1164   1363      7   -118   -110       C  
ATOM   1049  OH  TYR A 140      22.055 -60.429 122.552  1.00 11.62           O  
ANISOU 1049  OH  TYR A 140     1283   1464   1666     16   -131    -94       O  
ATOM   1050  N   ALA A 141      20.501 -52.643 120.029  1.00  8.54           N  
ANISOU 1050  N   ALA A 141      918   1048   1281    -43    -78   -177       N  
ATOM   1051  CA  ALA A 141      20.539 -51.516 119.103  1.00  8.87           C  
ANISOU 1051  CA  ALA A 141      957   1075   1337    -49    -61   -181       C  
ATOM   1052  C   ALA A 141      20.683 -51.998 117.646  1.00 11.04           C  
ANISOU 1052  C   ALA A 141     1231   1342   1622    -40    -35   -169       C  
ATOM   1053  O   ALA A 141      20.131 -51.398 116.723  1.00 15.42           O  
ANISOU 1053  O   ALA A 141     1795   1889   2175    -40    -17   -169       O  
ATOM   1054  CB  ALA A 141      21.671 -50.566 119.478  1.00  9.66           C  
ANISOU 1054  CB  ALA A 141     1037   1171   1462    -61    -73   -188       C  
ATOM   1055  N   ASN A 142      21.383 -53.114 117.462  1.00  8.05           N  
ANISOU 1055  N   ASN A 142      841    966   1252    -31    -34   -159       N  
ATOM   1056  CA  ASN A 142      21.818 -53.587 116.148  1.00  9.24           C  
ANISOU 1056  CA  ASN A 142      986   1108   1415    -22    -10   -149       C  
ATOM   1057  C   ASN A 142      21.323 -55.006 115.866  1.00  7.04           C  
ANISOU 1057  C   ASN A 142      721    832   1122     -9     -5   -144       C  
ATOM   1058  O   ASN A 142      21.647 -55.938 116.602  1.00  9.22           O  
ANISOU 1058  O   ASN A 142      991   1113   1399     -4    -19   -139       O  
ATOM   1059  CB  ASN A 142      23.352 -53.514 116.093  1.00 12.97           C  
ANISOU 1059  CB  ASN A 142     1429   1579   1920    -23    -10   -143       C  
ATOM   1060  CG  ASN A 142      23.950 -54.122 114.835  1.00 12.60           C  
ANISOU 1060  CG  ASN A 142     1375   1526   1887    -11     16   -133       C  
ATOM   1061  OD1 ASN A 142      23.280 -54.292 113.809  1.00 14.03           O  
ANISOU 1061  OD1 ASN A 142     1573   1703   2054     -5     37   -132       O  
ATOM   1062  ND2 ASN A 142      25.247 -54.422 114.905  1.00 14.56           N  
ANISOU 1062  ND2 ASN A 142     1595   1774   2161     -8     15   -125       N  
ATOM   1063  N   GLN A 143      20.520 -55.169 114.812  1.00  9.35           N  
ANISOU 1063  N   GLN A 143     1030   1120   1401     -4     14   -144       N  
ATOM   1064  CA  GLN A 143      20.010 -56.487 114.429  1.00 10.07           C  
ANISOU 1064  CA  GLN A 143     1135   1210   1480      7     20   -141       C  
ATOM   1065  C   GLN A 143      21.118 -57.521 114.256  1.00  9.50           C  
ANISOU 1065  C   GLN A 143     1048   1134   1428     18     24   -133       C  
ATOM   1066  O   GLN A 143      20.974 -58.681 114.643  1.00 10.44           O  
ANISOU 1066  O   GLN A 143     1171   1253   1543     26     16   -130       O  
ATOM   1067  CB  GLN A 143      19.204 -56.405 113.128  1.00 14.73           C  
ANISOU 1067  CB  GLN A 143     1743   1796   2057     11     40   -143       C  
ATOM   1068  CG  GLN A 143      18.655 -57.753 112.665  1.00 15.00           C  
ANISOU 1068  CG  GLN A 143     1793   1827   2079     20     45   -142       C  
ATOM   1069  CD  GLN A 143      17.674 -58.355 113.656  1.00 16.58           C  
ANISOU 1069  CD  GLN A 143     2004   2032   2264     17     26   -143       C  
ATOM   1070  OE1 GLN A 143      16.668 -57.737 114.006  1.00 19.63           O  
ANISOU 1070  OE1 GLN A 143     2400   2423   2634     10     19   -146       O  
ATOM   1071  NE2 GLN A 143      17.967 -59.565 114.123  1.00 11.80           N  
ANISOU 1071  NE2 GLN A 143     1397   1424   1664     24     18   -138       N  
ATOM   1072  N   ASP A 144      22.229 -57.112 113.664  1.00  8.44           N  
ANISOU 1072  N   ASP A 144      895    996   1316     20     37   -130       N  
ATOM   1073  CA  ASP A 144      23.280 -58.077 113.400  1.00 11.52           C  
ANISOU 1073  CA  ASP A 144     1269   1382   1725     33     45   -123       C  
ATOM   1074  C   ASP A 144      23.973 -58.565 114.677  1.00  8.35           C  
ANISOU 1074  C   ASP A 144      849    986   1338     34     20   -117       C  
ATOM   1075  O   ASP A 144      24.530 -59.664 114.684  1.00 11.80           O  
ANISOU 1075  O   ASP A 144     1278   1418   1786     47     22   -110       O  
ATOM   1076  CB  ASP A 144      24.294 -57.485 112.420  1.00 15.23           C  
ANISOU 1076  CB  ASP A 144     1721   1848   2216     35     68   -119       C  
ATOM   1077  CG  ASP A 144      23.713 -57.322 111.023  1.00 25.20           C  
ANISOU 1077  CG  ASP A 144     3004   3108   3465     40     95   -122       C  
ATOM   1078  OD1 ASP A 144      23.961 -56.283 110.378  1.00 28.39           O  
ANISOU 1078  OD1 ASP A 144     3402   3511   3874     34    110   -120       O  
ATOM   1079  OD2 ASP A 144      22.995 -58.239 110.574  1.00 18.27           O  
ANISOU 1079  OD2 ASP A 144     2146   2226   2568     48    101   -126       O  
ATOM   1080  N   LEU A 145      23.961 -57.775 115.750  1.00  9.46           N  
ANISOU 1080  N   LEU A 145      984   1135   1477     21     -2   -119       N  
ATOM   1081  CA  LEU A 145      24.527 -58.260 117.007  1.00  7.27           C  
ANISOU 1081  CA  LEU A 145      692    865   1207     21    -29   -113       C  
ATOM   1082  C   LEU A 145      23.592 -59.305 117.621  1.00  9.19           C  
ANISOU 1082  C   LEU A 145      954   1111   1427     27    -40   -110       C  
ATOM   1083  O   LEU A 145      24.040 -60.220 118.317  1.00  7.15           O  
ANISOU 1083  O   LEU A 145      687    854   1175     34    -54   -100       O  
ATOM   1084  CB  LEU A 145      24.796 -57.116 117.995  1.00  7.05           C  
ANISOU 1084  CB  LEU A 145      652    846   1180      5    -51   -119       C  
ATOM   1085  CG  LEU A 145      25.464 -57.512 119.323  1.00  9.97           C  
ANISOU 1085  CG  LEU A 145     1005   1227   1555      4    -81   -112       C  
ATOM   1086  CD1 LEU A 145      26.852 -58.146 119.100  1.00 11.60           C  
ANISOU 1086  CD1 LEU A 145     1182   1431   1795     15    -79    -99       C  
ATOM   1087  CD2 LEU A 145      25.580 -56.308 120.241  1.00  8.07           C  
ANISOU 1087  CD2 LEU A 145      759    995   1311    -13   -104   -123       C  
ATOM   1088  N   ILE A 146      22.297 -59.192 117.343  1.00  6.75           N  
ANISOU 1088  N   ILE A 146      671    800   1093     23    -33   -117       N  
ATOM   1089  CA  ILE A 146      21.364 -60.244 117.758  1.00  8.68           C  
ANISOU 1089  CA  ILE A 146      933   1045   1319     28    -40   -113       C  
ATOM   1090  C   ILE A 146      21.780 -61.587 117.160  1.00  9.11           C  
ANISOU 1090  C   ILE A 146      986   1087   1388     43    -29   -106       C  
ATOM   1091  O   ILE A 146      21.909 -62.573 117.869  1.00  8.31           O  
ANISOU 1091  O   ILE A 146      882    986   1289     50    -42    -95       O  
ATOM   1092  CB  ILE A 146      19.913 -59.934 117.340  1.00  9.17           C  
ANISOU 1092  CB  ILE A 146     1022   1107   1357     22    -32   -122       C  
ATOM   1093  CG1 ILE A 146      19.406 -58.671 118.036  1.00 10.32           C  
ANISOU 1093  CG1 ILE A 146     1171   1263   1489      9    -43   -130       C  
ATOM   1094  CG2 ILE A 146      18.998 -61.131 117.615  1.00 11.52           C  
ANISOU 1094  CG2 ILE A 146     1335   1402   1641     26    -36   -116       C  
ATOM   1095  CD1 ILE A 146      17.972 -58.288 117.678  1.00  8.59           C  
ANISOU 1095  CD1 ILE A 146      973   1044   1247      4    -35   -136       C  
ATOM   1096  N   TYR A 147      22.000 -61.611 115.852  1.00  8.73           N  
ANISOU 1096  N   TYR A 147      940   1030   1349     49     -4   -110       N  
ATOM   1097  CA  TYR A 147      22.363 -62.854 115.181  1.00  9.81           C  
ANISOU 1097  CA  TYR A 147     1078   1152   1497     65      9   -107       C  
ATOM   1098  C   TYR A 147      23.704 -63.373 115.676  1.00  8.82           C  
ANISOU 1098  C   TYR A 147      925   1026   1399     76      3    -95       C  
ATOM   1099  O   TYR A 147      23.860 -64.571 115.919  1.00  9.50           O  
ANISOU 1099  O   TYR A 147     1012   1104   1495     87     -1    -87       O  
ATOM   1100  CB  TYR A 147      22.386 -62.650 113.663  1.00  9.68           C  
ANISOU 1100  CB  TYR A 147     1069   1129   1481     70     38   -116       C  
ATOM   1101  CG  TYR A 147      20.995 -62.504 113.087  1.00 12.04           C  
ANISOU 1101  CG  TYR A 147     1395   1426   1752     63     43   -126       C  
ATOM   1102  CD1 TYR A 147      19.967 -63.318 113.530  1.00 12.51           C  
ANISOU 1102  CD1 TYR A 147     1473   1484   1798     61     31   -126       C  
ATOM   1103  CD2 TYR A 147      20.710 -61.548 112.124  1.00 17.90           C  
ANISOU 1103  CD2 TYR A 147     2145   2172   2484     58     59   -133       C  
ATOM   1104  CE1 TYR A 147      18.693 -63.196 113.020  1.00 18.74           C  
ANISOU 1104  CE1 TYR A 147     2284   2272   2564     54     35   -134       C  
ATOM   1105  CE2 TYR A 147      19.426 -61.415 111.609  1.00 17.05           C  
ANISOU 1105  CE2 TYR A 147     2062   2065   2353     52     62   -140       C  
ATOM   1106  CZ  TYR A 147      18.427 -62.242 112.066  1.00 19.04           C  
ANISOU 1106  CZ  TYR A 147     2329   2314   2591     50     49   -141       C  
ATOM   1107  OH  TYR A 147      17.141 -62.134 111.569  1.00 27.71           O  
ANISOU 1107  OH  TYR A 147     3448   3414   3668     44     50   -148       O  
ATOM   1108  N   SER A 148      24.664 -62.465 115.850  1.00 12.34           N  
ANISOU 1108  N   SER A 148     1348   1480   1862     71      0    -93       N  
ATOM   1109  CA  SER A 148      25.993 -62.847 116.311  1.00  9.68           C  
ANISOU 1109  CA  SER A 148      981   1143   1553     80     -8    -81       C  
ATOM   1110  C   SER A 148      25.939 -63.431 117.715  1.00  8.11           C  
ANISOU 1110  C   SER A 148      779    952   1351     80    -38    -70       C  
ATOM   1111  O   SER A 148      26.593 -64.436 118.006  1.00  9.45           O  
ANISOU 1111  O   SER A 148      935   1116   1538     94    -43    -57       O  
ATOM   1112  CB  SER A 148      26.944 -61.649 116.278  1.00 11.58           C  
ANISOU 1112  CB  SER A 148     1196   1393   1813     71     -8    -81       C  
ATOM   1113  OG  SER A 148      27.187 -61.216 114.942  1.00 14.16           O  
ANISOU 1113  OG  SER A 148     1521   1711   2146     74     23    -87       O  
ATOM   1114  N   ASP A 149      25.128 -62.823 118.577  1.00  9.46           N  
ANISOU 1114  N   ASP A 149      962   1135   1497     65    -58    -74       N  
ATOM   1115  CA  ASP A 149      24.966 -63.332 119.932  1.00  6.51           C  
ANISOU 1115  CA  ASP A 149      589    772   1113     64    -86    -63       C  
ATOM   1116  C   ASP A 149      24.249 -64.675 119.941  1.00  9.11           C  
ANISOU 1116  C   ASP A 149      936   1090   1435     75    -82    -54       C  
ATOM   1117  O   ASP A 149      24.543 -65.520 120.773  1.00 11.05           O  
ANISOU 1117  O   ASP A 149     1175   1337   1686     82    -99    -38       O  
ATOM   1118  CB  ASP A 149      24.212 -62.334 120.803  1.00  6.89           C  
ANISOU 1118  CB  ASP A 149      647    835   1134     47   -103    -71       C  
ATOM   1119  CG  ASP A 149      25.129 -61.289 121.410  1.00 10.10           C  
ANISOU 1119  CG  ASP A 149     1032   1255   1551     37   -121    -74       C  
ATOM   1120  OD1 ASP A 149      26.354 -61.324 121.124  1.00 10.49           O  
ANISOU 1120  OD1 ASP A 149     1055   1301   1630     42   -119    -68       O  
ATOM   1121  OD2 ASP A 149      24.628 -60.429 122.167  1.00 13.96           O  
ANISOU 1121  OD2 ASP A 149     1529   1756   2019     23   -136    -84       O  
ATOM   1122  N   LEU A 150      23.319 -64.869 119.014  1.00  7.87           N  
ANISOU 1122  N   LEU A 150      802    922   1267     74    -62    -64       N  
ATOM   1123  CA  LEU A 150      22.651 -66.159 118.907  1.00  7.94           C  
ANISOU 1123  CA  LEU A 150      828    917   1273     83    -58    -58       C  
ATOM   1124  C   LEU A 150      23.663 -67.245 118.539  1.00 11.11           C  
ANISOU 1124  C   LEU A 150     1216   1302   1704    102    -50    -49       C  
ATOM   1125  O   LEU A 150      23.717 -68.315 119.163  1.00 12.77           O  
ANISOU 1125  O   LEU A 150     1424   1505   1921    111    -60    -33       O  
ATOM   1126  CB  LEU A 150      21.515 -66.108 117.879  1.00  9.14           C  
ANISOU 1126  CB  LEU A 150     1005   1059   1407     78    -39    -73       C  
ATOM   1127  CG  LEU A 150      20.674 -67.385 117.750  1.00 11.92           C  
ANISOU 1127  CG  LEU A 150     1377   1396   1756     83    -37    -69       C  
ATOM   1128  CD1 LEU A 150      19.981 -67.721 119.073  1.00 14.33           C  
ANISOU 1128  CD1 LEU A 150     1687   1710   2046     76    -59    -55       C  
ATOM   1129  CD2 LEU A 150      19.663 -67.229 116.623  1.00 13.04           C  
ANISOU 1129  CD2 LEU A 150     1541   1531   1884     77    -20    -86       C  
ATOM   1130  N   THR A 151      24.477 -66.965 117.530  1.00 10.50           N  
ANISOU 1130  N   THR A 151     1126   1219   1645    109    -30    -56       N  
ATOM   1131  CA  THR A 151      25.457 -67.944 117.089  1.00 15.91           C  
ANISOU 1131  CA  THR A 151     1797   1888   2361    130    -17    -49       C  
ATOM   1132  C   THR A 151      26.519 -68.173 118.165  1.00 15.18           C  
ANISOU 1132  C   THR A 151     1676   1804   2289    136    -39    -29       C  
ATOM   1133  O   THR A 151      27.085 -69.258 118.251  1.00 21.17           O  
ANISOU 1133  O   THR A 151     2425   2549   3069    154    -38    -16       O  
ATOM   1134  CB  THR A 151      26.113 -67.530 115.755  1.00 16.23           C  
ANISOU 1134  CB  THR A 151     1830   1922   2414    137     12    -61       C  
ATOM   1135  OG1 THR A 151      26.862 -66.322 115.925  1.00 23.86           O  
ANISOU 1135  OG1 THR A 151     2772   2905   3387    128      8    -60       O  
ATOM   1136  CG2 THR A 151      25.039 -67.300 114.714  1.00 10.01           C  
ANISOU 1136  CG2 THR A 151     1072   1129   1602    130     30    -79       C  
ATOM   1137  N   ALA A 152      26.746 -67.167 119.008  1.00 17.67           N  
ANISOU 1137  N   ALA A 152     1978   2140   2596    123    -60    -26       N  
ATOM   1138  CA  ALA A 152      27.731 -67.260 120.087  1.00 16.60           C  
ANISOU 1138  CA  ALA A 152     1814   2017   2477    126    -86     -8       C  
ATOM   1139  C   ALA A 152      27.186 -67.934 121.348  1.00 21.00           C  
ANISOU 1139  C   ALA A 152     2381   2581   3018    126   -112      7       C  
ATOM   1140  O   ALA A 152      27.942 -68.204 122.292  1.00 19.73           O  
ANISOU 1140  O   ALA A 152     2199   2429   2867    131   -135     26       O  
ATOM   1141  CB  ALA A 152      28.253 -65.869 120.432  1.00 17.06           C  
ANISOU 1141  CB  ALA A 152     1855   2095   2534    111    -98    -15       C  
ATOM   1142  N   GLY A 153      25.880 -68.188 121.375  1.00 16.86           N  
ANISOU 1142  N   GLY A 153     1887   2052   2467    119   -109      2       N  
ATOM   1143  CA  GLY A 153      25.244 -68.806 122.529  1.00 11.57           C  
ANISOU 1143  CA  GLY A 153     1229   1389   1779    117   -130     19       C  
ATOM   1144  C   GLY A 153      24.934 -67.864 123.680  1.00 16.82           C  
ANISOU 1144  C   GLY A 153     1894   2080   2415    101   -155     18       C  
ATOM   1145  O   GLY A 153      24.686 -68.300 124.803  1.00 23.97           O  
ANISOU 1145  O   GLY A 153     2804   2998   3307    100   -176     35       O  
ATOM   1146  N   ARG A 154      24.954 -66.564 123.411  1.00 13.97           N  
ANISOU 1146  N   ARG A 154     1531   1731   2047     87   -153     -1       N  
ATOM   1147  CA  ARG A 154      24.607 -65.585 124.431  1.00 12.93           C  
ANISOU 1147  CA  ARG A 154     1403   1622   1888     72   -174     -7       C  
ATOM   1148  C   ARG A 154      23.106 -65.324 124.468  1.00 14.84           C  
ANISOU 1148  C   ARG A 154     1675   1866   2097     61   -167    -17       C  
ATOM   1149  O   ARG A 154      22.622 -64.654 125.376  1.00 19.00           O  
ANISOU 1149  O   ARG A 154     2210   2413   2598     50   -182    -21       O  
ATOM   1150  CB  ARG A 154      25.345 -64.273 124.197  1.00 15.18           C  
ANISOU 1150  CB  ARG A 154     1671   1916   2182     61   -176    -22       C  
ATOM   1151  CG  ARG A 154      26.847 -64.420 124.174  1.00 17.19           C  
ANISOU 1151  CG  ARG A 154     1891   2170   2470     70   -184    -12       C  
ATOM   1152  CD  ARG A 154      27.476 -63.078 123.943  1.00 20.30           C  
ANISOU 1152  CD  ARG A 154     2269   2571   2874     57   -186    -28       C  
ATOM   1153  NE  ARG A 154      27.502 -62.302 125.172  1.00 33.86           N  
ANISOU 1153  NE  ARG A 154     3984   4310   4572     42   -217    -32       N  
ATOM   1154  CZ  ARG A 154      28.604 -62.083 125.880  1.00 38.77           C  
ANISOU 1154  CZ  ARG A 154     4579   4945   5208     40   -243    -25       C  
ATOM   1155  NH1 ARG A 154      29.763 -62.576 125.466  1.00 43.52           N  
ANISOU 1155  NH1 ARG A 154     5150   5539   5846     52   -240    -12       N  
ATOM   1156  NH2 ARG A 154      28.549 -61.368 126.992  1.00 39.28           N  
ANISOU 1156  NH2 ARG A 154     4646   5030   5251     26   -272    -32       N  
ATOM   1157  N   LEU A 155      22.386 -65.828 123.463  1.00 12.83           N  
ANISOU 1157  N   LEU A 155     1437   1593   1846     65   -143    -22       N  
ATOM   1158  CA  LEU A 155      20.918 -65.829 123.457  1.00 10.67           C  
ANISOU 1158  CA  LEU A 155     1189   1320   1545     56   -136    -27       C  
ATOM   1159  C   LEU A 155      20.413 -67.254 123.282  1.00 10.68           C  
ANISOU 1159  C   LEU A 155     1202   1304   1553     65   -129    -13       C  
ATOM   1160  O   LEU A 155      21.070 -68.068 122.631  1.00 10.03           O  
ANISOU 1160  O   LEU A 155     1112   1203   1497     78   -120     -8       O  
ATOM   1161  CB  LEU A 155      20.357 -64.950 122.335  1.00 10.09           C  
ANISOU 1161  CB  LEU A 155     1126   1240   1467     49   -115    -49       C  
ATOM   1162  CG  LEU A 155      20.538 -63.434 122.439  1.00  7.77           C  
ANISOU 1162  CG  LEU A 155      826    959   1165     37   -119    -65       C  
ATOM   1163  CD1 LEU A 155      20.182 -62.794 121.113  1.00 10.08           C  
ANISOU 1163  CD1 LEU A 155     1127   1242   1461     34    -96    -81       C  
ATOM   1164  CD2 LEU A 155      19.705 -62.846 123.571  1.00 11.25           C  
ANISOU 1164  CD2 LEU A 155     1279   1420   1576     27   -135    -67       C  
ATOM   1165  N   ASP A 156      19.270 -67.570 123.883  1.00  9.50           N  
ANISOU 1165  N   ASP A 156     1069   1159   1380     59   -133     -6       N  
ATOM   1166  CA  ASP A 156      18.595 -68.842 123.616  1.00  8.52           C  
ANISOU 1166  CA  ASP A 156      958   1016   1263     64   -125      6       C  
ATOM   1167  C   ASP A 156      17.831 -68.767 122.309  1.00 10.21           C  
ANISOU 1167  C   ASP A 156     1187   1214   1478     60   -103    -13       C  
ATOM   1168  O   ASP A 156      17.749 -69.736 121.562  1.00  9.66           O  
ANISOU 1168  O   ASP A 156     1123   1121   1425     66    -92    -13       O  
ATOM   1169  CB  ASP A 156      17.634 -69.199 124.750  1.00 10.40           C  
ANISOU 1169  CB  ASP A 156     1208   1267   1478     58   -137     23       C  
ATOM   1170  CG  ASP A 156      18.364 -69.531 126.023  1.00 21.91           C  
ANISOU 1170  CG  ASP A 156     2652   2738   2933     64   -159     45       C  
ATOM   1171  OD1 ASP A 156      18.996 -70.609 126.076  1.00 21.77           O  
ANISOU 1171  OD1 ASP A 156     2627   2706   2938     77   -162     64       O  
ATOM   1172  OD2 ASP A 156      18.328 -68.708 126.956  1.00 13.47           O  
ANISOU 1172  OD2 ASP A 156     1582   1695   1839     57   -173     44       O  
ATOM   1173  N   ALA A 157      17.265 -67.600 122.044  1.00  6.98           N  
ANISOU 1173  N   ALA A 157      783    817   1051     49    -99    -30       N  
ATOM   1174  CA  ALA A 157      16.485 -67.392 120.836  1.00  6.58           C  
ANISOU 1174  CA  ALA A 157      747    756    997     44    -81    -47       C  
ATOM   1175  C   ALA A 157      16.385 -65.909 120.539  1.00  9.84           C  
ANISOU 1175  C   ALA A 157     1158   1182   1397     35    -76    -64       C  
ATOM   1176  O   ALA A 157      16.669 -65.074 121.395  1.00  9.93           O  
ANISOU 1176  O   ALA A 157     1162   1212   1399     31    -88    -64       O  
ATOM   1177  CB  ALA A 157      15.070 -68.012 120.973  1.00  6.45           C  
ANISOU 1177  CB  ALA A 157      748    736    968     36    -79    -41       C  
ATOM   1178  N   ALA A 158      15.965 -65.600 119.317  1.00  9.07           N  
ANISOU 1178  N   ALA A 158     1070   1076   1300     33    -60    -79       N  
ATOM   1179  CA  ALA A 158      15.709 -64.239 118.882  1.00  8.58           C  
ANISOU 1179  CA  ALA A 158     1009   1023   1226     26    -53    -94       C  
ATOM   1180  C   ALA A 158      14.307 -64.169 118.302  1.00  9.55           C  
ANISOU 1180  C   ALA A 158     1149   1144   1334     19    -45   -100       C  
ATOM   1181  O   ALA A 158      13.903 -65.060 117.552  1.00  7.60           O  
ANISOU 1181  O   ALA A 158      912    884   1092     21    -38   -101       O  
ATOM   1182  CB  ALA A 158      16.733 -63.806 117.848  1.00 14.62           C  
ANISOU 1182  CB  ALA A 158     1765   1781   2008     32    -40   -103       C  
ATOM   1183  N   LEU A 159      13.567 -63.120 118.645  1.00  8.54           N  
ANISOU 1183  N   LEU A 159     1025   1030   1188     10    -48   -105       N  
ATOM   1184  CA  LEU A 159      12.232 -62.926 118.088  1.00  6.93           C  
ANISOU 1184  CA  LEU A 159      835    827    971      4    -41   -110       C  
ATOM   1185  C   LEU A 159      12.291 -61.920 116.952  1.00  6.72           C  
ANISOU 1185  C   LEU A 159      811    799    945      3    -28   -123       C  
ATOM   1186  O   LEU A 159      12.586 -60.741 117.171  1.00  8.94           O  
ANISOU 1186  O   LEU A 159     1085   1088   1224      1    -28   -129       O  
ATOM   1187  CB  LEU A 159      11.244 -62.454 119.156  1.00  8.92           C  
ANISOU 1187  CB  LEU A 159     1091   1095   1205     -3    -49   -106       C  
ATOM   1188  CG  LEU A 159       9.827 -62.204 118.627  1.00  7.05           C  
ANISOU 1188  CG  LEU A 159      863    859    955    -10    -42   -109       C  
ATOM   1189  CD1 LEU A 159       9.155 -63.504 118.162  1.00 10.03           C  
ANISOU 1189  CD1 LEU A 159     1249   1226   1337    -11    -41   -103       C  
ATOM   1190  CD2 LEU A 159       8.964 -61.498 119.660  1.00  9.01           C  
ANISOU 1190  CD2 LEU A 159     1112   1125   1186    -14    -46   -107       C  
ATOM   1191  N   GLN A 160      11.992 -62.392 115.746  1.00  7.32           N  
ANISOU 1191  N   GLN A 160      894    864   1022      5    -18   -128       N  
ATOM   1192  CA  GLN A 160      12.142 -61.588 114.540  1.00  8.20           C  
ANISOU 1192  CA  GLN A 160     1009    974   1133      6     -4   -138       C  
ATOM   1193  C   GLN A 160      10.890 -61.637 113.700  1.00  8.28           C  
ANISOU 1193  C   GLN A 160     1033    984   1130      1      0   -142       C  
ATOM   1194  O   GLN A 160      10.095 -62.562 113.829  1.00  9.77           O  
ANISOU 1194  O   GLN A 160     1229   1169   1315     -2     -6   -139       O  
ATOM   1195  CB  GLN A 160      13.309 -62.093 113.682  1.00 11.12           C  
ANISOU 1195  CB  GLN A 160     1375   1332   1518     15      7   -142       C  
ATOM   1196  CG  GLN A 160      14.624 -62.265 114.407  1.00 11.73           C  
ANISOU 1196  CG  GLN A 160     1435   1407   1613     21      2   -136       C  
ATOM   1197  CD  GLN A 160      15.247 -60.944 114.788  1.00 17.67           C  
ANISOU 1197  CD  GLN A 160     2175   2170   2369     18      1   -137       C  
ATOM   1198  OE1 GLN A 160      15.993 -60.857 115.757  1.00 25.06           O  
ANISOU 1198  OE1 GLN A 160     3098   3110   3314     18    -10   -132       O  
ATOM   1199  NE2 GLN A 160      14.934 -59.900 114.029  1.00 19.10           N  
ANISOU 1199  NE2 GLN A 160     2360   2353   2543     14     12   -143       N  
ATOM   1200  N   ASP A 161      10.748 -60.676 112.790  1.00  9.05           N  
ANISOU 1200  N   ASP A 161     1133   1084   1221      1      9   -148       N  
ATOM   1201  CA  ASP A 161       9.760 -60.832 111.742  1.00  8.71           C  
ANISOU 1201  CA  ASP A 161     1103   1040   1166     -2     13   -152       C  
ATOM   1202  C   ASP A 161      10.072 -62.107 110.962  1.00  8.87           C  
ANISOU 1202  C   ASP A 161     1132   1048   1191      3     17   -158       C  
ATOM   1203  O   ASP A 161      11.225 -62.361 110.616  1.00 10.17           O  
ANISOU 1203  O   ASP A 161     1292   1205   1366     11     26   -161       O  
ATOM   1204  CB  ASP A 161       9.739 -59.624 110.807  1.00  9.12           C  
ANISOU 1204  CB  ASP A 161     1157   1098   1211     -1     24   -156       C  
ATOM   1205  CG  ASP A 161       8.787 -59.827 109.639  1.00 11.57           C  
ANISOU 1205  CG  ASP A 161     1480   1408   1506     -3     26   -159       C  
ATOM   1206  OD1 ASP A 161       7.561 -59.690 109.849  1.00 12.05           O  
ANISOU 1206  OD1 ASP A 161     1544   1477   1559     -9     17   -156       O  
ATOM   1207  OD2 ASP A 161       9.266 -60.156 108.532  1.00 10.99           O  
ANISOU 1207  OD2 ASP A 161     1414   1330   1431      3     35   -165       O  
ATOM   1208  N   GLU A 162       9.042 -62.911 110.686  1.00  7.04           N  
ANISOU 1208  N   GLU A 162      910    812    951     -3     10   -160       N  
ATOM   1209  CA  GLU A 162       9.264 -64.227 110.115  1.00  7.46           C  
ANISOU 1209  CA  GLU A 162      973    850   1011      0     11   -166       C  
ATOM   1210  C   GLU A 162       9.953 -64.156 108.752  1.00 10.54           C  
ANISOU 1210  C   GLU A 162     1371   1236   1398      9     27   -178       C  
ATOM   1211  O   GLU A 162      11.004 -64.777 108.547  1.00  8.22           O  
ANISOU 1211  O   GLU A 162     1076    931   1116     18     35   -182       O  
ATOM   1212  CB  GLU A 162       7.945 -64.994 110.009  1.00  8.89           C  
ANISOU 1212  CB  GLU A 162     1164   1028   1186    -10      0   -167       C  
ATOM   1213  CG  GLU A 162       8.115 -66.408 109.483  1.00 12.21           C  
ANISOU 1213  CG  GLU A 162     1596   1429   1615     -9      0   -176       C  
ATOM   1214  CD  GLU A 162       6.807 -67.159 109.392  1.00  9.84           C  
ANISOU 1214  CD  GLU A 162     1304   1124   1312    -21    -13   -177       C  
ATOM   1215  OE1 GLU A 162       5.739 -66.521 109.469  1.00 10.11           O  
ANISOU 1215  OE1 GLU A 162     1335   1172   1334    -31    -20   -172       O  
ATOM   1216  OE2 GLU A 162       6.844 -68.395 109.243  1.00 10.78           O  
ANISOU 1216  OE2 GLU A 162     1430   1224   1442    -22    -16   -183       O  
ATOM   1217  N   VAL A 163       9.374 -63.424 107.809  1.00  8.48           N  
ANISOU 1217  N   VAL A 163     1118    985   1120      6     30   -182       N  
ATOM   1218  CA  VAL A 163       9.956 -63.426 106.474  1.00 11.23           C  
ANISOU 1218  CA  VAL A 163     1477   1331   1461     14     46   -193       C  
ATOM   1219  C   VAL A 163      11.313 -62.713 106.470  1.00  7.21           C  
ANISOU 1219  C   VAL A 163      955    823    962     24     62   -189       C  
ATOM   1220  O   VAL A 163      12.239 -63.149 105.788  1.00 11.77           O  
ANISOU 1220  O   VAL A 163     1535   1394   1544     34     76   -195       O  
ATOM   1221  CB  VAL A 163       9.005 -62.801 105.447  1.00 10.69           C  
ANISOU 1221  CB  VAL A 163     1419   1274   1369     10     45   -196       C  
ATOM   1222  CG1 VAL A 163       9.744 -62.563 104.130  1.00 12.79           C  
ANISOU 1222  CG1 VAL A 163     1694   1542   1623     20     63   -202       C  
ATOM   1223  CG2 VAL A 163       7.819 -63.723 105.239  1.00 15.19           C  
ANISOU 1223  CG2 VAL A 163     2001   1840   1930      0     29   -203       C  
ATOM   1224  N   ALA A 164      11.450 -61.632 107.244  1.00  9.56           N  
ANISOU 1224  N   ALA A 164     1238   1129   1265     21     59   -178       N  
ATOM   1225  CA  ALA A 164      12.733 -60.929 107.279  1.00 10.81           C  
ANISOU 1225  CA  ALA A 164     1383   1289   1436     28     73   -174       C  
ATOM   1226  C   ALA A 164      13.848 -61.864 107.746  1.00 14.33           C  
ANISOU 1226  C   ALA A 164     1819   1723   1902     36     75   -175       C  
ATOM   1227  O   ALA A 164      14.943 -61.857 107.192  1.00 18.39           O  
ANISOU 1227  O   ALA A 164     2327   2233   2425     45     92   -176       O  
ATOM   1228  CB  ALA A 164      12.658 -59.703 108.175  1.00 12.56           C  
ANISOU 1228  CB  ALA A 164     1592   1519   1663     21     66   -165       C  
ATOM   1229  N   ALA A 165      13.562 -62.685 108.752  1.00 12.47           N  
ANISOU 1229  N   ALA A 165     1581   1482   1674     33     60   -172       N  
ATOM   1230  CA  ALA A 165      14.551 -63.639 109.251  1.00 14.32           C  
ANISOU 1230  CA  ALA A 165     1806   1705   1928     41     60   -170       C  
ATOM   1231  C   ALA A 165      14.825 -64.751 108.235  1.00 16.44           C  
ANISOU 1231  C   ALA A 165     2088   1959   2198     51     72   -181       C  
ATOM   1232  O   ALA A 165      15.971 -65.180 108.052  1.00 15.09           O  
ANISOU 1232  O   ALA A 165     1908   1780   2044     64     84   -182       O  
ATOM   1233  CB  ALA A 165      14.084 -64.223 110.548  1.00 10.29           C  
ANISOU 1233  CB  ALA A 165     1294   1194   1424     36     41   -162       C  
ATOM   1234  N   SER A 166      13.755 -65.224 107.605  1.00 10.37           N  
ANISOU 1234  N   SER A 166     1338   1187   1413     46     69   -190       N  
ATOM   1235  CA  SER A 166      13.831 -66.247 106.567  1.00 14.38           C  
ANISOU 1235  CA  SER A 166     1863   1685   1916     53     77   -200       C  
ATOM   1236  C   SER A 166      14.728 -65.794 105.421  1.00 20.54           C  
ANISOU 1236  C   SER A 166     2644   2471   2688     64     98   -203       C  
ATOM   1237  O   SER A 166      15.521 -66.573 104.910  1.00 25.01           O  
ANISOU 1237  O   SER A 166     3213   3028   3261     76    108   -207       O  
ATOM   1238  CB  SER A 166      12.432 -66.575 106.045  1.00 18.66           C  
ANISOU 1238  CB  SER A 166     2425   2229   2437     42     65   -207       C  
ATOM   1239  OG  SER A 166      12.487 -67.486 104.965  1.00 23.60           O  
ANISOU 1239  OG  SER A 166     3069   2846   3054     48     70   -217       O  
ATOM   1240  N   GLU A 167      14.604 -64.532 105.029  1.00 16.17           N  
ANISOU 1240  N   GLU A 167     2088   1933   2123     61    104   -200       N  
ATOM   1241  CA  GLU A 167      15.348 -64.019 103.875  1.00 15.76           C  
ANISOU 1241  CA  GLU A 167     2037   1888   2062     70    125   -200       C  
ATOM   1242  C   GLU A 167      16.725 -63.481 104.248  1.00 21.05           C  
ANISOU 1242  C   GLU A 167     2684   2558   2755     78    139   -192       C  
ATOM   1243  O   GLU A 167      17.630 -63.443 103.411  1.00 25.14           O  
ANISOU 1243  O   GLU A 167     3200   3078   3273     88    159   -191       O  
ATOM   1244  CB  GLU A 167      14.545 -62.916 103.173  1.00 13.91           C  
ANISOU 1244  CB  GLU A 167     1812   1668   1805     63    126   -200       C  
ATOM   1245  CG  GLU A 167      13.217 -63.375 102.601  1.00 17.25           C  
ANISOU 1245  CG  GLU A 167     2257   2094   2204     56    113   -208       C  
ATOM   1246  CD  GLU A 167      13.387 -64.141 101.302  1.00 23.27           C  
ANISOU 1246  CD  GLU A 167     3037   2855   2949     66    121   -219       C  
ATOM   1247  OE1 GLU A 167      12.953 -65.306 101.233  1.00 24.56           O  
ANISOU 1247  OE1 GLU A 167     3214   3008   3111     65    109   -229       O  
ATOM   1248  OE2 GLU A 167      13.959 -63.572 100.350  1.00 23.67           O  
ANISOU 1248  OE2 GLU A 167     3090   2915   2989     74    139   -218       O  
ATOM   1249  N   GLY A 168      16.889 -63.070 105.500  1.00 17.20           N  
ANISOU 1249  N   GLY A 168     2178   2070   2288     72    129   -185       N  
ATOM   1250  CA  GLY A 168      18.055 -62.297 105.894  1.00 12.75           C  
ANISOU 1250  CA  GLY A 168     1591   1509   1747     76    139   -177       C  
ATOM   1251  C   GLY A 168      19.086 -62.947 106.801  1.00 21.54           C  
ANISOU 1251  C   GLY A 168     2683   2613   2887     83    135   -171       C  
ATOM   1252  O   GLY A 168      20.183 -62.412 106.972  1.00 25.73           O  
ANISOU 1252  O   GLY A 168     3192   3146   3437     86    144   -163       O  
ATOM   1253  N   PHE A 169      18.744 -64.077 107.403  1.00 17.09           N  
ANISOU 1253  N   PHE A 169     2125   2039   2328     84    121   -174       N  
ATOM   1254  CA  PHE A 169      19.708 -64.831 108.205  1.00 16.29           C  
ANISOU 1254  CA  PHE A 169     2007   1929   2254     94    117   -167       C  
ATOM   1255  C   PHE A 169      19.646 -66.315 107.855  1.00 14.43           C  
ANISOU 1255  C   PHE A 169     1785   1676   2021    104    120   -174       C  
ATOM   1256  O   PHE A 169      20.667 -66.937 107.575  1.00 13.39           O  
ANISOU 1256  O   PHE A 169     1646   1539   1904    118    131   -171       O  
ATOM   1257  CB  PHE A 169      19.444 -64.611 109.698  1.00 12.24           C  
ANISOU 1257  CB  PHE A 169     1482   1422   1746     83     91   -155       C  
ATOM   1258  CG  PHE A 169      20.325 -65.431 110.617  1.00  9.14           C  
ANISOU 1258  CG  PHE A 169     1073   1022   1379     92     82   -145       C  
ATOM   1259  CD1 PHE A 169      21.698 -65.244 110.637  1.00 11.10           C  
ANISOU 1259  CD1 PHE A 169     1296   1271   1650    102     91   -138       C  
ATOM   1260  CD2 PHE A 169      19.764 -66.353 111.494  1.00 10.15           C  
ANISOU 1260  CD2 PHE A 169     1206   1143   1507     90     63   -140       C  
ATOM   1261  CE1 PHE A 169      22.499 -65.979 111.488  1.00 13.23           C  
ANISOU 1261  CE1 PHE A 169     1549   1536   1944    111     81   -127       C  
ATOM   1262  CE2 PHE A 169      20.555 -67.091 112.348  1.00 11.64           C  
ANISOU 1262  CE2 PHE A 169     1380   1326   1718     99     54   -128       C  
ATOM   1263  CZ  PHE A 169      21.931 -66.898 112.351  1.00 13.85           C  
ANISOU 1263  CZ  PHE A 169     1635   1607   2021    110     62   -121       C  
ATOM   1264  N   LEU A 170      18.437 -66.872 107.838  1.00 11.43           N  
ANISOU 1264  N   LEU A 170     1427   1292   1625     96    108   -181       N  
ATOM   1265  CA  LEU A 170      18.267 -68.309 107.647  1.00  9.16           C  
ANISOU 1265  CA  LEU A 170     1153    986   1339    102    106   -185       C  
ATOM   1266  C   LEU A 170      18.667 -68.748 106.238  1.00 12.08           C  
ANISOU 1266  C   LEU A 170     1537   1355   1696    113    124   -194       C  
ATOM   1267  O   LEU A 170      19.035 -69.897 106.037  1.00 14.88           O  
ANISOU 1267  O   LEU A 170     1899   1695   2060    123    128   -198       O  
ATOM   1268  CB  LEU A 170      16.822 -68.733 107.946  1.00 10.58           C  
ANISOU 1268  CB  LEU A 170     1351   1163   1508     89     88   -190       C  
ATOM   1269  CG  LEU A 170      16.376 -68.584 109.410  1.00  9.83           C  
ANISOU 1269  CG  LEU A 170     1245   1071   1421     79     66   -176       C  
ATOM   1270  CD1 LEU A 170      14.905 -68.955 109.599  1.00 13.25           C  
ANISOU 1270  CD1 LEU A 170     1694   1502   1839     64     51   -178       C  
ATOM   1271  CD2 LEU A 170      17.254 -69.364 110.394  1.00 12.28           C  
ANISOU 1271  CD2 LEU A 170     1538   1369   1757     89     60   -163       C  
ATOM   1272  N   LYS A 171      18.623 -67.822 105.283  1.00 18.55           N  
ANISOU 1272  N   LYS A 171     2363   2190   2496    111    136   -198       N  
ATOM   1273  CA  LYS A 171      19.023 -68.111 103.907  1.00 23.87           C  
ANISOU 1273  CA  LYS A 171     3050   2865   3154    122    154   -207       C  
ATOM   1274  C   LYS A 171      20.486 -67.776 103.634  1.00 25.50           C  
ANISOU 1274  C   LYS A 171     3237   3077   3376    136    175   -200       C  
ATOM   1275  O   LYS A 171      21.025 -68.101 102.572  1.00 26.67           O  
ANISOU 1275  O   LYS A 171     3392   3226   3515    148    192   -206       O  
ATOM   1276  CB  LYS A 171      18.131 -67.352 102.925  1.00 28.83           C  
ANISOU 1276  CB  LYS A 171     3696   3508   3751    114    155   -214       C  
ATOM   1277  CG  LYS A 171      16.822 -68.059 102.624  1.00 27.25           C  
ANISOU 1277  CG  LYS A 171     3520   3301   3531    106    139   -225       C  
ATOM   1278  N   GLN A 172      21.135 -67.120 104.585  1.00 20.86           N  
ANISOU 1278  N   GLN A 172     2623   2492   2811    134    173   -186       N  
ATOM   1279  CA  GLN A 172      22.556 -66.855 104.461  1.00 21.01           C  
ANISOU 1279  CA  GLN A 172     2618   2514   2849    145    190   -177       C  
ATOM   1280  C   GLN A 172      23.338 -68.038 105.028  1.00 16.25           C  
ANISOU 1280  C   GLN A 172     2005   1897   2272    158    188   -174       C  
ATOM   1281  O   GLN A 172      22.832 -68.771 105.881  1.00 12.35           O  
ANISOU 1281  O   GLN A 172     1514   1391   1787    156    170   -174       O  
ATOM   1282  CB  GLN A 172      22.924 -65.554 105.170  1.00 28.53           C  
ANISOU 1282  CB  GLN A 172     3546   3478   3817    136    188   -165       C  
ATOM   1283  CG  GLN A 172      21.972 -64.412 104.846  1.00 33.92           C  
ANISOU 1283  CG  GLN A 172     4239   4172   4476    121    185   -168       C  
ATOM   1284  CD  GLN A 172      21.908 -64.089 103.361  1.00 36.55           C  
ANISOU 1284  CD  GLN A 172     4589   4514   4784    125    205   -172       C  
ATOM   1285  OE1 GLN A 172      22.936 -64.022 102.675  1.00 27.41           O  
ANISOU 1285  OE1 GLN A 172     3422   3360   3632    136    226   -168       O  
ATOM   1286  NE2 GLN A 172      20.691 -63.880 102.857  1.00 38.33           N  
ANISOU 1286  NE2 GLN A 172     4837   4744   4981    117    199   -180       N  
ATOM   1287  N   PRO A 173      24.559 -68.260 104.525  1.00 16.40           N  
ANISOU 1287  N   PRO A 173     2012   1917   2304    173    207   -170       N  
ATOM   1288  CA  PRO A 173      25.390 -69.326 105.088  1.00 14.58           C  
ANISOU 1288  CA  PRO A 173     1767   1672   2100    187    205   -164       C  
ATOM   1289  C   PRO A 173      25.498 -69.254 106.617  1.00 15.18           C  
ANISOU 1289  C   PRO A 173     1822   1745   2202    181    184   -150       C  
ATOM   1290  O   PRO A 173      25.478 -70.291 107.275  1.00 16.67           O  
ANISOU 1290  O   PRO A 173     2011   1920   2406    188    172   -147       O  
ATOM   1291  CB  PRO A 173      26.738 -69.094 104.404  1.00 16.17           C  
ANISOU 1291  CB  PRO A 173     1951   1881   2311    200    229   -158       C  
ATOM   1292  CG  PRO A 173      26.338 -68.560 103.055  1.00 11.98           C  
ANISOU 1292  CG  PRO A 173     1440   1361   1749    198    245   -170       C  
ATOM   1293  CD  PRO A 173      25.180 -67.648 103.336  1.00 18.25           C  
ANISOU 1293  CD  PRO A 173     2245   2163   2526    179    231   -171       C  
ATOM   1294  N   ALA A 174      25.567 -68.047 107.174  1.00 15.56           N  
ANISOU 1294  N   ALA A 174     1851   1806   2255    169    177   -142       N  
ATOM   1295  CA  ALA A 174      25.685 -67.883 108.621  1.00 18.91           C  
ANISOU 1295  CA  ALA A 174     2252   2230   2702    164    154   -130       C  
ATOM   1296  C   ALA A 174      24.498 -68.489 109.376  1.00 12.30           C  
ANISOU 1296  C   ALA A 174     1432   1383   1859    158    133   -134       C  
ATOM   1297  O   ALA A 174      24.618 -68.859 110.550  1.00 14.69           O  
ANISOU 1297  O   ALA A 174     1720   1681   2181    160    114   -123       O  
ATOM   1298  CB  ALA A 174      25.829 -66.407 108.969  1.00 21.41           C  
ANISOU 1298  CB  ALA A 174     2550   2562   3021    151    150   -125       C  
ATOM   1299  N   GLY A 175      23.357 -68.593 108.702  1.00 12.75           N  
ANISOU 1299  N   GLY A 175     1519   1438   1889    151    135   -148       N  
ATOM   1300  CA  GLY A 175      22.153 -69.079 109.358  1.00 11.70           C  
ANISOU 1300  CA  GLY A 175     1401   1295   1748    142    116   -151       C  
ATOM   1301  C   GLY A 175      21.875 -70.554 109.123  1.00 13.37           C  
ANISOU 1301  C   GLY A 175     1632   1488   1962    149    116   -156       C  
ATOM   1302  O   GLY A 175      20.826 -71.077 109.537  1.00 12.73           O  
ANISOU 1302  O   GLY A 175     1566   1397   1875    141    101   -158       O  
ATOM   1303  N   LYS A 176      22.815 -71.238 108.472  1.00 11.19           N  
ANISOU 1303  N   LYS A 176     1354   1204   1693    165    132   -156       N  
ATOM   1304  CA  LYS A 176      22.576 -72.617 108.051  1.00 16.15           C  
ANISOU 1304  CA  LYS A 176     2002   1813   2321    173    134   -164       C  
ATOM   1305  C   LYS A 176      22.262 -73.556 109.213  1.00 15.08           C  
ANISOU 1305  C   LYS A 176     1864   1659   2205    173    115   -153       C  
ATOM   1306  O   LYS A 176      21.415 -74.442 109.073  1.00 20.06           O  
ANISOU 1306  O   LYS A 176     2517   2275   2831    169    109   -161       O  
ATOM   1307  CB  LYS A 176      23.776 -73.150 107.270  1.00 21.16           C  
ANISOU 1307  CB  LYS A 176     2632   2443   2964    193    154   -166       C  
ATOM   1308  CG  LYS A 176      23.533 -74.505 106.617  1.00 28.24           C  
ANISOU 1308  CG  LYS A 176     3553   3319   3858    202    159   -179       C  
ATOM   1309  N   GLU A 177      22.904 -73.358 110.364  1.00 13.53           N  
ANISOU 1309  N   GLU A 177     1641   1466   2034    177    103   -134       N  
ATOM   1310  CA  GLU A 177      22.662 -74.259 111.493  1.00 17.01           C  
ANISOU 1310  CA  GLU A 177     2078   1890   2494    179     84   -120       C  
ATOM   1311  C   GLU A 177      21.691 -73.659 112.504  1.00 11.86           C  
ANISOU 1311  C   GLU A 177     1424   1245   1837    164     62   -113       C  
ATOM   1312  O   GLU A 177      21.774 -73.937 113.707  1.00  9.92           O  
ANISOU 1312  O   GLU A 177     1166   1002   1601    162     42    -92       O  
ATOM   1313  CB  GLU A 177      23.974 -74.643 112.175  1.00 25.65           C  
ANISOU 1313  CB  GLU A 177     3145   2983   3618    196     82   -100       C  
ATOM   1314  CG  GLU A 177      24.837 -75.548 111.314  1.00 30.50           C  
ANISOU 1314  CG  GLU A 177     3763   3585   4240    213    102   -105       C  
ATOM   1315  CD  GLU A 177      24.031 -76.658 110.640  1.00 39.02           C  
ANISOU 1315  CD  GLU A 177     4874   4643   5309    213    107   -120       C  
ATOM   1316  OE1 GLU A 177      23.360 -77.442 111.350  1.00 40.93           O  
ANISOU 1316  OE1 GLU A 177     5124   4867   5559    208     91   -112       O  
ATOM   1317  OE2 GLU A 177      24.069 -76.746 109.393  1.00 42.28           O  
ANISOU 1317  OE2 GLU A 177     5304   5055   5706    216    125   -139       O  
ATOM   1318  N   TYR A 178      20.786 -72.834 111.983  1.00 12.73           N  
ANISOU 1318  N   TYR A 178     1549   1368   1918    147     64   -127       N  
ATOM   1319  CA  TYR A 178      19.736 -72.176 112.752  1.00  8.58           C  
ANISOU 1319  CA  TYR A 178     1029    861   1371    126     44   -120       C  
ATOM   1320  C   TYR A 178      18.418 -72.414 112.041  1.00  8.81           C  
ANISOU 1320  C   TYR A 178     1085    882   1379    114     45   -136       C  
ATOM   1321  O   TYR A 178      18.395 -72.737 110.849  1.00 12.58           O  
ANISOU 1321  O   TYR A 178     1577   1348   1854    120     62   -156       O  
ATOM   1322  CB  TYR A 178      20.051 -70.678 112.931  1.00  8.57           C  
ANISOU 1322  CB  TYR A 178     1012    887   1356    118     42   -118       C  
ATOM   1323  CG  TYR A 178      21.318 -70.608 113.723  1.00 10.11           C  
ANISOU 1323  CG  TYR A 178     1179   1087   1574    129     36   -102       C  
ATOM   1324  CD1 TYR A 178      21.280 -70.589 115.112  1.00 13.56           C  
ANISOU 1324  CD1 TYR A 178     1605   1535   2012    123     12    -83       C  
ATOM   1325  CD2 TYR A 178      22.549 -70.692 113.096  1.00 12.35           C  
ANISOU 1325  CD2 TYR A 178     1447   1365   1879    146     55   -104       C  
ATOM   1326  CE1 TYR A 178      22.436 -70.609 115.849  1.00 12.96           C  
ANISOU 1326  CE1 TYR A 178     1504   1464   1957    133      4    -67       C  
ATOM   1327  CE2 TYR A 178      23.713 -70.715 113.831  1.00 13.74           C  
ANISOU 1327  CE2 TYR A 178     1596   1546   2080    156     47    -87       C  
ATOM   1328  CZ  TYR A 178      23.646 -70.668 115.204  1.00 12.15           C  
ANISOU 1328  CZ  TYR A 178     1383   1355   1878    149     20    -69       C  
ATOM   1329  OH  TYR A 178      24.810 -70.696 115.935  1.00 15.98           O  
ANISOU 1329  OH  TYR A 178     1839   1846   2385    158     10    -52       O  
ATOM   1330  N   ALA A 179      17.322 -72.273 112.782  1.00  9.92           N  
ANISOU 1330  N   ALA A 179     1232   1032   1505     97     28   -128       N  
ATOM   1331  CA  ALA A 179      16.003 -72.585 112.255  1.00 11.20           C  
ANISOU 1331  CA  ALA A 179     1418   1188   1652     84     25   -140       C  
ATOM   1332  C   ALA A 179      14.947 -71.923 113.102  1.00  8.75           C  
ANISOU 1332  C   ALA A 179     1106    896   1322     66      9   -129       C  
ATOM   1333  O   ALA A 179      15.202 -71.529 114.248  1.00  8.89           O  
ANISOU 1333  O   ALA A 179     1109    928   1341     65     -3   -111       O  
ATOM   1334  CB  ALA A 179      15.780 -74.103 112.221  1.00 11.17           C  
ANISOU 1334  CB  ALA A 179     1425   1153   1667     89     23   -140       C  
ATOM   1335  N   PHE A 180      13.745 -71.808 112.558  1.00  7.76           N  
ANISOU 1335  N   PHE A 180      997    773   1180     53      7   -140       N  
ATOM   1336  CA  PHE A 180      12.648 -71.341 113.378  1.00  6.58           C  
ANISOU 1336  CA  PHE A 180      847    639   1015     37     -7   -129       C  
ATOM   1337  C   PHE A 180      12.373 -72.332 114.495  1.00  7.69           C  
ANISOU 1337  C   PHE A 180      985    769   1169     34    -20   -109       C  
ATOM   1338  O   PHE A 180      12.379 -73.544 114.273  1.00 11.16           O  
ANISOU 1338  O   PHE A 180     1432   1183   1626     37    -19   -109       O  
ATOM   1339  CB  PHE A 180      11.397 -71.146 112.544  1.00  7.43           C  
ANISOU 1339  CB  PHE A 180      970    749   1105     23     -8   -142       C  
ATOM   1340  CG  PHE A 180      11.486 -69.999 111.589  1.00  7.47           C  
ANISOU 1340  CG  PHE A 180      977    768   1092     24      3   -157       C  
ATOM   1341  CD1 PHE A 180      11.707 -68.707 112.051  1.00 10.19           C  
ANISOU 1341  CD1 PHE A 180     1310   1136   1427     23      3   -150       C  
ATOM   1342  CD2 PHE A 180      11.315 -70.207 110.223  1.00  9.60           C  
ANISOU 1342  CD2 PHE A 180     1262   1030   1355     25     12   -176       C  
ATOM   1343  CE1 PHE A 180      11.774 -67.642 111.168  1.00 10.06           C  
ANISOU 1343  CE1 PHE A 180     1295   1131   1396     23     13   -161       C  
ATOM   1344  CE2 PHE A 180      11.378 -69.145 109.336  1.00 13.84           C  
ANISOU 1344  CE2 PHE A 180     1802   1582   1874     26     22   -186       C  
ATOM   1345  CZ  PHE A 180      11.608 -67.860 109.805  1.00 11.39           C  
ANISOU 1345  CZ  PHE A 180     1478   1292   1557     26     23   -177       C  
ATOM   1346  N   ALA A 181      12.124 -71.795 115.687  1.00  9.37           N  
ANISOU 1346  N   ALA A 181     1187   1001   1371     28    -31    -91       N  
ATOM   1347  CA  ALA A 181      11.763 -72.592 116.845  1.00  7.83           C  
ANISOU 1347  CA  ALA A 181      989    802   1183     24    -43    -68       C  
ATOM   1348  C   ALA A 181      10.274 -72.447 117.103  1.00  6.27           C  
ANISOU 1348  C   ALA A 181      799    614    971      7    -49    -64       C  
ATOM   1349  O   ALA A 181       9.821 -71.429 117.649  1.00  8.72           O  
ANISOU 1349  O   ALA A 181     1103    948   1260      1    -52    -61       O  
ATOM   1350  CB  ALA A 181      12.568 -72.159 118.061  1.00  9.79           C  
ANISOU 1350  CB  ALA A 181     1222   1068   1431     31    -51    -51       C  
ATOM   1351  N   GLY A 182       9.517 -73.453 116.684  1.00  9.56           N  
ANISOU 1351  N   GLY A 182     1226   1009   1397     -1    -50    -66       N  
ATOM   1352  CA  GLY A 182       8.077 -73.425 116.836  1.00  7.42           C  
ANISOU 1352  CA  GLY A 182      959    745   1116    -18    -55    -61       C  
ATOM   1353  C   GLY A 182       7.439 -72.649 115.706  1.00 10.27           C  
ANISOU 1353  C   GLY A 182     1327   1113   1460    -25    -51    -84       C  
ATOM   1354  O   GLY A 182       8.119 -72.242 114.762  1.00 11.36           O  
ANISOU 1354  O   GLY A 182     1469   1250   1596    -17    -42   -102       O  
ATOM   1355  N   PRO A 183       6.119 -72.433 115.802  1.00  8.30           N  
ANISOU 1355  N   PRO A 183     1079    875   1201    -40    -56    -80       N  
ATOM   1356  CA  PRO A 183       5.341 -71.721 114.794  1.00 10.04           C  
ANISOU 1356  CA  PRO A 183     1304   1104   1406    -48    -54    -97       C  
ATOM   1357  C   PRO A 183       5.442 -70.210 114.934  1.00  8.85           C  
ANISOU 1357  C   PRO A 183     1146    980   1235    -44    -50    -99       C  
ATOM   1358  O   PRO A 183       5.942 -69.712 115.942  1.00  8.77           O  
ANISOU 1358  O   PRO A 183     1127    983   1221    -38    -50    -88       O  
ATOM   1359  CB  PRO A 183       3.913 -72.179 115.081  1.00  7.37           C  
ANISOU 1359  CB  PRO A 183      965    766   1070    -66    -63    -86       C  
ATOM   1360  CG  PRO A 183       3.909 -72.331 116.581  1.00  8.10           C  
ANISOU 1360  CG  PRO A 183     1047    866   1164    -65    -65    -60       C  
ATOM   1361  CD  PRO A 183       5.265 -72.954 116.883  1.00  9.65           C  
ANISOU 1361  CD  PRO A 183     1244   1047   1376    -51    -63    -56       C  
ATOM   1362  N   SER A 184       4.931 -69.491 113.939  1.00  8.94           N  
ANISOU 1362  N   SER A 184     1163   1000   1234    -48    -48   -114       N  
ATOM   1363  CA  SER A 184       4.889 -68.037 114.011  1.00  8.34           C  
ANISOU 1363  CA  SER A 184     1080    947   1141    -45    -43   -116       C  
ATOM   1364  C   SER A 184       4.092 -67.583 115.228  1.00  9.59           C  
ANISOU 1364  C   SER A 184     1229   1124   1293    -51    -47    -99       C  
ATOM   1365  O   SER A 184       3.193 -68.289 115.708  1.00 12.80           O  
ANISOU 1365  O   SER A 184     1633   1527   1703    -61    -53    -87       O  
ATOM   1366  CB  SER A 184       4.277 -67.455 112.741  1.00  8.57           C  
ANISOU 1366  CB  SER A 184     1117    982   1159    -49    -42   -131       C  
ATOM   1367  OG  SER A 184       2.947 -67.924 112.586  1.00 12.08           O  
ANISOU 1367  OG  SER A 184     1563   1426   1603    -63    -51   -128       O  
ATOM   1368  N   VAL A 185       4.456 -66.410 115.731  1.00  9.90           N  
ANISOU 1368  N   VAL A 185     1261   1179   1320    -45    -43    -98       N  
ATOM   1369  CA  VAL A 185       3.796 -65.804 116.870  1.00  7.99           C  
ANISOU 1369  CA  VAL A 185     1011    956   1068    -48    -45    -86       C  
ATOM   1370  C   VAL A 185       2.751 -64.842 116.333  1.00  9.86           C  
ANISOU 1370  C   VAL A 185     1247   1205   1294    -52    -42    -92       C  
ATOM   1371  O   VAL A 185       3.077 -63.944 115.565  1.00 12.61           O  
ANISOU 1371  O   VAL A 185     1598   1557   1638    -47    -37   -104       O  
ATOM   1372  CB  VAL A 185       4.794 -65.049 117.772  1.00 11.35           C  
ANISOU 1372  CB  VAL A 185     1431   1393   1489    -38    -43    -85       C  
ATOM   1373  CG1 VAL A 185       4.056 -64.330 118.888  1.00 20.32           C  
ANISOU 1373  CG1 VAL A 185     2562   2549   2610    -40    -43    -76       C  
ATOM   1374  CG2 VAL A 185       5.842 -66.007 118.341  1.00 15.42           C  
ANISOU 1374  CG2 VAL A 185     1945   1897   2015    -33    -47    -77       C  
ATOM   1375  N   LYS A 186       1.501 -65.042 116.729  1.00 10.51           N  
ANISOU 1375  N   LYS A 186     1325   1295   1374    -61    -45    -81       N  
ATOM   1376  CA  LYS A 186       0.404 -64.252 116.196  1.00 10.21           C  
ANISOU 1376  CA  LYS A 186     1283   1268   1328    -65    -43    -83       C  
ATOM   1377  C   LYS A 186      -0.226 -63.379 117.273  1.00 12.23           C  
ANISOU 1377  C   LYS A 186     1530   1543   1573    -62    -38    -74       C  
ATOM   1378  O   LYS A 186      -0.476 -63.829 118.391  1.00 12.39           O  
ANISOU 1378  O   LYS A 186     1546   1570   1593    -64    -38    -60       O  
ATOM   1379  CB  LYS A 186      -0.641 -65.179 115.564  1.00 17.99           C  
ANISOU 1379  CB  LYS A 186     2268   2245   2320    -77    -51    -80       C  
ATOM   1380  CG  LYS A 186      -0.022 -66.117 114.528  1.00 15.63           C  
ANISOU 1380  CG  LYS A 186     1982   1925   2031    -79    -56    -92       C  
ATOM   1381  CD  LYS A 186      -0.912 -67.302 114.185  1.00 22.21           C  
ANISOU 1381  CD  LYS A 186     2815   2746   2876    -94    -65    -89       C  
ATOM   1382  CE  LYS A 186      -0.191 -68.296 113.263  1.00 16.67           C  
ANISOU 1382  CE  LYS A 186     2128   2021   2184    -94    -69   -104       C  
ATOM   1383  NZ  LYS A 186       0.806 -69.228 113.942  1.00 15.18           N  
ANISOU 1383  NZ  LYS A 186     1943   1816   2010    -89    -67    -98       N  
ATOM   1384  N   ASP A 187      -0.469 -62.120 116.931  1.00  9.50           N  
ANISOU 1384  N   ASP A 187     1183   1208   1220    -57    -33    -82       N  
ATOM   1385  CA  ASP A 187      -1.195 -61.235 117.834  1.00  7.23           C  
ANISOU 1385  CA  ASP A 187      886    937    923    -54    -26    -75       C  
ATOM   1386  C   ASP A 187      -1.781 -60.062 117.072  1.00  9.14           C  
ANISOU 1386  C   ASP A 187     1125   1185   1161    -50    -22    -82       C  
ATOM   1387  O   ASP A 187      -1.052 -59.265 116.500  1.00  8.45           O  
ANISOU 1387  O   ASP A 187     1044   1094   1073    -43    -20    -93       O  
ATOM   1388  CB  ASP A 187      -0.300 -60.720 118.952  1.00 10.74           C  
ANISOU 1388  CB  ASP A 187     1333   1388   1360    -46    -23    -78       C  
ATOM   1389  CG  ASP A 187      -1.108 -60.130 120.096  1.00 12.48           C  
ANISOU 1389  CG  ASP A 187     1547   1627   1569    -43    -15    -70       C  
ATOM   1390  OD1 ASP A 187      -1.823 -59.125 119.887  1.00 13.77           O  
ANISOU 1390  OD1 ASP A 187     1706   1798   1729    -39     -9    -74       O  
ATOM   1391  OD2 ASP A 187      -1.047 -60.687 121.201  1.00 13.48           O  
ANISOU 1391  OD2 ASP A 187     1672   1760   1690    -43    -16    -60       O  
ATOM   1392  N   LYS A 188      -3.105 -59.962 117.085  1.00  8.56           N  
ANISOU 1392  N   LYS A 188     1042   1121   1087    -54    -22    -73       N  
ATOM   1393  CA  LYS A 188      -3.803 -58.915 116.337  1.00  7.91           C  
ANISOU 1393  CA  LYS A 188      956   1045   1004    -49    -19    -76       C  
ATOM   1394  C   LYS A 188      -3.335 -57.499 116.694  1.00  8.52           C  
ANISOU 1394  C   LYS A 188     1035   1126   1076    -37     -9    -84       C  
ATOM   1395  O   LYS A 188      -3.289 -56.615 115.835  1.00  8.30           O  
ANISOU 1395  O   LYS A 188     1009   1096   1048    -32     -7    -90       O  
ATOM   1396  CB  LYS A 188      -5.315 -59.053 116.569  1.00  6.28           C  
ANISOU 1396  CB  LYS A 188      736    851    801    -54    -19    -62       C  
ATOM   1397  CG  LYS A 188      -6.156 -58.009 115.868  1.00  8.92           C  
ANISOU 1397  CG  LYS A 188     1062   1192   1135    -49    -17    -61       C  
ATOM   1398  CD  LYS A 188      -5.998 -58.097 114.353  1.00 13.05           C  
ANISOU 1398  CD  LYS A 188     1592   1708   1660    -52    -27    -67       C  
ATOM   1399  CE  LYS A 188      -7.003 -57.207 113.634  1.00 15.13           C  
ANISOU 1399  CE  LYS A 188     1846   1980   1924    -48    -29    -62       C  
ATOM   1400  NZ  LYS A 188      -6.810 -57.175 112.145  1.00  8.24           N  
ANISOU 1400  NZ  LYS A 188      981   1102   1048    -50    -39    -68       N  
ATOM   1401  N   LYS A 189      -2.986 -57.268 117.955  1.00  7.68           N  
ANISOU 1401  N   LYS A 189      929   1025    963    -32     -3    -85       N  
ATOM   1402  CA  LYS A 189      -2.579 -55.925 118.354  1.00 10.32           C  
ANISOU 1402  CA  LYS A 189     1266   1363   1294    -22      5    -95       C  
ATOM   1403  C   LYS A 189      -1.177 -55.539 117.894  1.00 10.63           C  
ANISOU 1403  C   LYS A 189     1313   1389   1335    -19      3   -108       C  
ATOM   1404  O   LYS A 189      -0.896 -54.351 117.685  1.00 11.62           O  
ANISOU 1404  O   LYS A 189     1441   1511   1463    -13      9   -116       O  
ATOM   1405  CB  LYS A 189      -2.668 -55.771 119.871  1.00  7.60           C  
ANISOU 1405  CB  LYS A 189      920   1030    939    -17     12    -94       C  
ATOM   1406  CG  LYS A 189      -4.093 -55.641 120.373  1.00  9.24           C  
ANISOU 1406  CG  LYS A 189     1116   1251   1143    -15     20    -83       C  
ATOM   1407  CD  LYS A 189      -4.090 -55.050 121.757  1.00 13.14           C  
ANISOU 1407  CD  LYS A 189     1612   1757   1623     -7     30    -88       C  
ATOM   1408  CE  LYS A 189      -5.496 -54.725 122.217  1.00 14.81           C  
ANISOU 1408  CE  LYS A 189     1812   1982   1832     -1     43    -78       C  
ATOM   1409  NZ  LYS A 189      -5.463 -53.952 123.485  1.00  9.23           N  
ANISOU 1409  NZ  LYS A 189     1110   1286   1110     10     55    -87       N  
ATOM   1410  N   TYR A 190      -0.301 -56.530 117.735  1.00  9.08           N  
ANISOU 1410  N   TYR A 190     1122   1185   1142    -25     -4   -108       N  
ATOM   1411  CA  TYR A 190       1.103 -56.261 117.432  1.00 11.62           C  
ANISOU 1411  CA  TYR A 190     1449   1496   1468    -22     -5   -118       C  
ATOM   1412  C   TYR A 190       1.483 -56.542 115.983  1.00  8.50           C  
ANISOU 1412  C   TYR A 190     1059   1091   1080    -24     -7   -121       C  
ATOM   1413  O   TYR A 190       2.208 -55.746 115.360  1.00 12.00           O  
ANISOU 1413  O   TYR A 190     1505   1528   1527    -20     -2   -128       O  
ATOM   1414  CB  TYR A 190       2.007 -57.066 118.386  1.00 11.94           C  
ANISOU 1414  CB  TYR A 190     1491   1536   1508    -24    -11   -117       C  
ATOM   1415  CG  TYR A 190       1.838 -56.600 119.806  1.00 11.63           C  
ANISOU 1415  CG  TYR A 190     1451   1510   1458    -21     -9   -118       C  
ATOM   1416  CD1 TYR A 190       0.788 -57.068 120.585  1.00 10.99           C  
ANISOU 1416  CD1 TYR A 190     1366   1441   1368    -22     -7   -107       C  
ATOM   1417  CD2 TYR A 190       2.691 -55.647 120.358  1.00 13.39           C  
ANISOU 1417  CD2 TYR A 190     1675   1733   1679    -17     -9   -130       C  
ATOM   1418  CE1 TYR A 190       0.599 -56.626 121.873  1.00 10.37           C  
ANISOU 1418  CE1 TYR A 190     1287   1376   1276    -18     -4   -107       C  
ATOM   1419  CE2 TYR A 190       2.512 -55.202 121.660  1.00 15.82           C  
ANISOU 1419  CE2 TYR A 190     1984   2054   1974    -13     -8   -133       C  
ATOM   1420  CZ  TYR A 190       1.454 -55.693 122.408  1.00 13.79           C  
ANISOU 1420  CZ  TYR A 190     1724   1809   1705    -13     -4   -122       C  
ATOM   1421  OH  TYR A 190       1.236 -55.263 123.698  1.00 13.65           O  
ANISOU 1421  OH  TYR A 190     1709   1807   1671     -9     -1   -125       O  
ATOM   1422  N   PHE A 191       0.990 -57.654 115.443  1.00  8.12           N  
ANISOU 1422  N   PHE A 191     1012   1040   1032    -30    -12   -115       N  
ATOM   1423  CA  PHE A 191       1.372 -58.105 114.102  1.00  7.51           C  
ANISOU 1423  CA  PHE A 191      941    953    958    -32    -14   -120       C  
ATOM   1424  C   PHE A 191       0.193 -58.085 113.116  1.00  6.27           C  
ANISOU 1424  C   PHE A 191      784    800    797    -36    -17   -116       C  
ATOM   1425  O   PHE A 191       0.371 -58.237 111.909  1.00  9.44           O  
ANISOU 1425  O   PHE A 191     1192   1196   1197    -36    -19   -121       O  
ATOM   1426  CB  PHE A 191       1.991 -59.504 114.188  1.00  6.37           C  
ANISOU 1426  CB  PHE A 191      801    799    819    -36    -20   -120       C  
ATOM   1427  CG  PHE A 191       3.067 -59.603 115.235  1.00  7.78           C  
ANISOU 1427  CG  PHE A 191      978    976   1002    -32    -19   -120       C  
ATOM   1428  CD1 PHE A 191       4.159 -58.744 115.198  1.00 12.86           C  
ANISOU 1428  CD1 PHE A 191     1620   1617   1648    -26    -14   -127       C  
ATOM   1429  CD2 PHE A 191       2.978 -60.519 116.269  1.00 10.19           C  
ANISOU 1429  CD2 PHE A 191     1281   1282   1309    -36    -24   -111       C  
ATOM   1430  CE1 PHE A 191       5.143 -58.804 116.179  1.00  7.33           C  
ANISOU 1430  CE1 PHE A 191      916    917    952    -24    -16   -128       C  
ATOM   1431  CE2 PHE A 191       3.957 -60.588 117.245  1.00 14.03           C  
ANISOU 1431  CE2 PHE A 191     1765   1769   1796    -32    -26   -110       C  
ATOM   1432  CZ  PHE A 191       5.044 -59.731 117.199  1.00 12.45           C  
ANISOU 1432  CZ  PHE A 191     1564   1568   1599    -26    -23   -119       C  
ATOM   1433  N   GLY A 192      -1.011 -57.899 113.640  1.00  5.13           N  
ANISOU 1433  N   GLY A 192      632    667    652    -38    -19   -107       N  
ATOM   1434  CA  GLY A 192      -2.191 -57.644 112.820  1.00  7.39           C  
ANISOU 1434  CA  GLY A 192      914    960    936    -40    -23   -102       C  
ATOM   1435  C   GLY A 192      -3.015 -58.794 112.245  1.00  7.69           C  
ANISOU 1435  C   GLY A 192      951    997    975    -52    -35    -98       C  
ATOM   1436  O   GLY A 192      -4.044 -58.549 111.606  1.00  8.70           O  
ANISOU 1436  O   GLY A 192     1073   1132   1101    -54    -40    -93       O  
ATOM   1437  N   ASP A 193      -2.597 -60.040 112.472  1.00  8.72           N  
ANISOU 1437  N   ASP A 193     1086   1117   1110    -59    -40   -100       N  
ATOM   1438  CA  ASP A 193      -3.211 -61.197 111.809  1.00  8.38           C  
ANISOU 1438  CA  ASP A 193     1045   1069   1071    -71    -52   -100       C  
ATOM   1439  C   ASP A 193      -3.390 -60.917 110.320  1.00 10.70           C  
ANISOU 1439  C   ASP A 193     1346   1363   1356    -71    -58   -108       C  
ATOM   1440  O   ASP A 193      -4.477 -61.074 109.752  1.00 14.41           O  
ANISOU 1440  O   ASP A 193     1811   1840   1825    -79    -69   -104       O  
ATOM   1441  CB  ASP A 193      -4.540 -61.579 112.466  1.00 11.19           C  
ANISOU 1441  CB  ASP A 193     1386   1432   1432    -81    -57    -86       C  
ATOM   1442  CG  ASP A 193      -4.337 -62.374 113.745  1.00 13.84           C  
ANISOU 1442  CG  ASP A 193     1719   1764   1775    -84    -54    -78       C  
ATOM   1443  OD1 ASP A 193      -3.238 -62.950 113.915  1.00 16.38           O  
ANISOU 1443  OD1 ASP A 193     2050   2073   2099    -82    -53    -84       O  
ATOM   1444  OD2 ASP A 193      -5.275 -62.438 114.572  1.00 18.22           O  
ANISOU 1444  OD2 ASP A 193     2261   2329   2334    -88    -52    -64       O  
ATOM   1445  N   GLY A 194      -2.294 -60.491 109.701  1.00  9.01           N  
ANISOU 1445  N   GLY A 194     1143   1144   1136    -63    -51   -118       N  
ATOM   1446  CA  GLY A 194      -2.271 -60.202 108.282  1.00  8.94           C  
ANISOU 1446  CA  GLY A 194     1144   1138   1116    -61    -54   -125       C  
ATOM   1447  C   GLY A 194      -1.804 -58.797 107.967  1.00 11.96           C  
ANISOU 1447  C   GLY A 194     1527   1526   1492    -48    -43   -123       C  
ATOM   1448  O   GLY A 194      -1.834 -57.907 108.832  1.00  8.74           O  
ANISOU 1448  O   GLY A 194     1109   1122   1089    -43    -35   -116       O  
ATOM   1449  N   THR A 195      -1.335 -58.622 106.730  1.00  7.87           N  
ANISOU 1449  N   THR A 195     1020   1007    962    -45    -41   -130       N  
ATOM   1450  CA  THR A 195      -1.193 -57.301 106.120  1.00  5.98           C  
ANISOU 1450  CA  THR A 195      782    775    716    -35    -33   -124       C  
ATOM   1451  C   THR A 195      -2.352 -57.097 105.141  1.00  8.85           C  
ANISOU 1451  C   THR A 195     1145   1151   1068    -38    -45   -118       C  
ATOM   1452  O   THR A 195      -2.965 -58.058 104.680  1.00 10.05           O  
ANISOU 1452  O   THR A 195     1300   1304   1214    -48    -60   -123       O  
ATOM   1453  CB  THR A 195       0.137 -57.144 105.359  1.00  9.00           C  
ANISOU 1453  CB  THR A 195     1177   1151   1093    -28    -20   -132       C  
ATOM   1454  OG1 THR A 195       0.141 -57.995 104.205  1.00  8.03           O  
ANISOU 1454  OG1 THR A 195     1068   1028    956    -31    -27   -141       O  
ATOM   1455  CG2 THR A 195       1.292 -57.513 106.247  1.00  9.16           C  
ANISOU 1455  CG2 THR A 195     1196   1159   1126    -26    -11   -138       C  
ATOM   1456  N   GLY A 196      -2.656 -55.848 104.826  1.00  7.75           N  
ANISOU 1456  N   GLY A 196     1000   1019    925    -29    -41   -107       N  
ATOM   1457  CA  GLY A 196      -3.709 -55.556 103.874  1.00  7.96           C  
ANISOU 1457  CA  GLY A 196     1026   1059    940    -30    -54    -98       C  
ATOM   1458  C   GLY A 196      -3.456 -54.249 103.144  1.00  4.22           C  
ANISOU 1458  C   GLY A 196      555    590    460    -18    -44    -88       C  
ATOM   1459  O   GLY A 196      -2.552 -53.492 103.497  1.00  8.77           O  
ANISOU 1459  O   GLY A 196     1131   1158   1043    -10    -27    -87       O  
ATOM   1460  N   VAL A 197      -4.253 -53.997 102.106  1.00  4.64           N  
ANISOU 1460  N   VAL A 197      609    656    498    -18    -56    -79       N  
ATOM   1461  CA  VAL A 197      -4.232 -52.689 101.472  1.00  6.58           C  
ANISOU 1461  CA  VAL A 197      855    907    739     -5    -49    -63       C  
ATOM   1462  C   VAL A 197      -4.795 -51.679 102.459  1.00  9.55           C  
ANISOU 1462  C   VAL A 197     1213   1281   1135      2    -42    -51       C  
ATOM   1463  O   VAL A 197      -5.936 -51.817 102.895  1.00  8.16           O  
ANISOU 1463  O   VAL A 197     1022   1111    966     -2    -54    -45       O  
ATOM   1464  CB  VAL A 197      -5.059 -52.656 100.175  1.00  8.15           C  
ANISOU 1464  CB  VAL A 197     1057   1123    917     -6    -66    -54       C  
ATOM   1465  CG1 VAL A 197      -4.945 -51.277  99.502  1.00  8.49           C  
ANISOU 1465  CG1 VAL A 197     1101   1169    955      8    -56    -35       C  
ATOM   1466  CG2 VAL A 197      -4.637 -53.780  99.230  1.00  9.58           C  
ANISOU 1466  CG2 VAL A 197     1258   1307   1076    -14    -74    -71       C  
ATOM   1467  N   GLY A 198      -4.004 -50.674 102.826  1.00  7.02           N  
ANISOU 1467  N   GLY A 198      892    949    826     11    -24    -48       N  
ATOM   1468  CA  GLY A 198      -4.489 -49.647 103.728  1.00 10.38           C  
ANISOU 1468  CA  GLY A 198     1303   1370   1270     19    -17    -39       C  
ATOM   1469  C   GLY A 198      -5.318 -48.662 102.935  1.00  8.20           C  
ANISOU 1469  C   GLY A 198     1022   1103    992     29    -21    -18       C  
ATOM   1470  O   GLY A 198      -4.905 -48.233 101.859  1.00  7.61           O  
ANISOU 1470  O   GLY A 198      957   1030    905     33    -18    -10       O  
ATOM   1471  N   LEU A 199      -6.487 -48.314 103.464  1.00  5.73           N  
ANISOU 1471  N   LEU A 199      692    795    689     33    -26     -9       N  
ATOM   1472  CA  LEU A 199      -7.462 -47.499 102.740  1.00  7.26           C  
ANISOU 1472  CA  LEU A 199      877    999    883     43    -33     12       C  
ATOM   1473  C   LEU A 199      -8.192 -46.531 103.671  1.00  7.82           C  
ANISOU 1473  C   LEU A 199      930   1064    976     54    -25     21       C  
ATOM   1474  O   LEU A 199      -8.322 -46.790 104.864  1.00  8.59           O  
ANISOU 1474  O   LEU A 199     1021   1158   1086     52    -19     10       O  
ATOM   1475  CB  LEU A 199      -8.491 -48.404 102.042  1.00  6.20           C  
ANISOU 1475  CB  LEU A 199      738    884    734     34    -58     17       C  
ATOM   1476  CG  LEU A 199      -7.965 -49.395 100.993  1.00  5.86           C  
ANISOU 1476  CG  LEU A 199      713    848    666     23    -69      6       C  
ATOM   1477  CD1 LEU A 199      -8.979 -50.499 100.770  1.00 11.43           C  
ANISOU 1477  CD1 LEU A 199     1411   1568   1363      9    -94      3       C  
ATOM   1478  CD2 LEU A 199      -7.644 -48.689  99.672  1.00  7.68           C  
ANISOU 1478  CD2 LEU A 199      956   1084    878     31    -69     20       C  
ATOM   1479  N   ARG A 200      -8.694 -45.423 103.131  1.00  7.22           N  
ANISOU 1479  N   ARG A 200      848    988    906     68    -23     41       N  
ATOM   1480  CA  ARG A 200      -9.534 -44.547 103.949  1.00  6.21           C  
ANISOU 1480  CA  ARG A 200      703    855    801     81    -15     50       C  
ATOM   1481  C   ARG A 200     -10.861 -45.244 104.255  1.00  9.26           C  
ANISOU 1481  C   ARG A 200     1070   1260   1189     77    -30     54       C  
ATOM   1482  O   ARG A 200     -11.414 -45.929 103.394  1.00 10.18           O  
ANISOU 1482  O   ARG A 200     1184   1393   1291     69    -50     61       O  
ATOM   1483  CB  ARG A 200      -9.765 -43.217 103.239  1.00  9.45           C  
ANISOU 1483  CB  ARG A 200     1111   1261   1220     98    -10     73       C  
ATOM   1484  CG  ARG A 200      -8.519 -42.346 103.179  1.00  6.52           C  
ANISOU 1484  CG  ARG A 200      755    868    856    103      9     70       C  
ATOM   1485  CD  ARG A 200      -8.823 -41.025 102.479  1.00  7.48           C  
ANISOU 1485  CD  ARG A 200      873    982    988    120     14     95       C  
ATOM   1486  NE  ARG A 200      -9.118 -41.222 101.058  1.00 10.54           N  
ANISOU 1486  NE  ARG A 200     1264   1387   1353    119     -2    116       N  
ATOM   1487  CZ  ARG A 200      -8.178 -41.312 100.120  1.00  8.40           C  
ANISOU 1487  CZ  ARG A 200     1011   1117   1065    115      0    119       C  
ATOM   1488  NH1 ARG A 200      -6.900 -41.216 100.459  1.00  6.79           N  
ANISOU 1488  NH1 ARG A 200      819    895    865    109     17    104       N  
ATOM   1489  NH2 ARG A 200      -8.507 -41.499  98.847  1.00  8.50           N  
ANISOU 1489  NH2 ARG A 200     1028   1148   1053    115    -16    136       N  
ATOM   1490  N   LYS A 201     -11.357 -45.091 105.481  1.00  8.32           N  
ANISOU 1490  N   LYS A 201      938   1138   1087     82    -20     49       N  
ATOM   1491  CA  LYS A 201     -12.590 -45.771 105.882  1.00  9.85           C  
ANISOU 1491  CA  LYS A 201     1110   1347   1284     77    -30     54       C  
ATOM   1492  C   LYS A 201     -13.793 -45.452 104.985  1.00 10.23           C  
ANISOU 1492  C   LYS A 201     1140   1411   1335     84    -47     79       C  
ATOM   1493  O   LYS A 201     -14.639 -46.317 104.755  1.00 12.17           O  
ANISOU 1493  O   LYS A 201     1373   1674   1577     73    -65     84       O  
ATOM   1494  CB  LYS A 201     -12.933 -45.442 107.334  1.00  8.89           C  
ANISOU 1494  CB  LYS A 201      977   1220   1181     85    -12     48       C  
ATOM   1495  CG  LYS A 201     -11.961 -46.063 108.346  1.00 14.27           C  
ANISOU 1495  CG  LYS A 201     1672   1893   1857     75     -2     24       C  
ATOM   1496  CD  LYS A 201     -12.534 -46.038 109.760  1.00 20.59           C  
ANISOU 1496  CD  LYS A 201     2459   2694   2668     80     12     19       C  
ATOM   1497  CE  LYS A 201     -11.651 -46.801 110.733  1.00 20.11           C  
ANISOU 1497  CE  LYS A 201     2411   2629   2599     69     19     -1       C  
ATOM   1498  NZ  LYS A 201     -12.260 -46.906 112.092  1.00 24.99           N  
ANISOU 1498  NZ  LYS A 201     3018   3254   3225     73     32     -4       N  
ATOM   1499  N   ASP A 202     -13.883 -44.226 104.473  1.00  9.49           N  
ANISOU 1499  N   ASP A 202     1045   1311   1249    102    -41     95       N  
ATOM   1500  CA  ASP A 202     -15.034 -43.886 103.635  1.00 14.62           C  
ANISOU 1500  CA  ASP A 202     1677   1977   1902    110    -57    121       C  
ATOM   1501  C   ASP A 202     -14.934 -44.388 102.196  1.00 15.68           C  
ANISOU 1501  C   ASP A 202     1821   2125   2010    100    -82    129       C  
ATOM   1502  O   ASP A 202     -15.910 -44.328 101.456  1.00 13.93           O  
ANISOU 1502  O   ASP A 202     1584   1922   1788    103   -101    149       O  
ATOM   1503  CB  ASP A 202     -15.261 -42.377 103.620  1.00 17.38           C  
ANISOU 1503  CB  ASP A 202     2020   2314   2271    135    -43    139       C  
ATOM   1504  CG  ASP A 202     -15.953 -41.883 104.868  1.00 21.83           C  
ANISOU 1504  CG  ASP A 202     2564   2871   2861    148    -25    137       C  
ATOM   1505  OD1 ASP A 202     -16.079 -40.654 105.026  1.00 25.86           O  
ANISOU 1505  OD1 ASP A 202     3070   3366   3390    169     -9    147       O  
ATOM   1506  OD2 ASP A 202     -16.375 -42.721 105.697  1.00 25.00           O  
ANISOU 1506  OD2 ASP A 202     2954   3281   3263    138    -25    126       O  
ATOM   1507  N   ASP A 203     -13.768 -44.882 101.789  1.00 10.98           N  
ANISOU 1507  N   ASP A 203     1251   1525   1396     89    -81    113       N  
ATOM   1508  CA  ASP A 203     -13.611 -45.345 100.415  1.00 11.43           C  
ANISOU 1508  CA  ASP A 203     1321   1596   1425     80   -101    119       C  
ATOM   1509  C   ASP A 203     -14.043 -46.802 100.285  1.00 15.31           C  
ANISOU 1509  C   ASP A 203     1811   2104   1904     59   -124    106       C  
ATOM   1510  O   ASP A 203     -13.220 -47.698 100.094  1.00 11.10           O  
ANISOU 1510  O   ASP A 203     1297   1567   1353     45   -126     86       O  
ATOM   1511  CB  ASP A 203     -12.169 -45.159  99.949  1.00 10.29           C  
ANISOU 1511  CB  ASP A 203     1205   1438   1266     80    -88    109       C  
ATOM   1512  CG  ASP A 203     -11.842 -43.708  99.634  1.00 13.30           C  
ANISOU 1512  CG  ASP A 203     1589   1807   1657     99    -72    129       C  
ATOM   1513  OD1 ASP A 203     -12.760 -42.855  99.659  1.00 15.71           O  
ANISOU 1513  OD1 ASP A 203     1877   2114   1979    114    -73    150       O  
ATOM   1514  OD2 ASP A 203     -10.670 -43.418  99.328  1.00 13.46           O  
ANISOU 1514  OD2 ASP A 203     1629   1815   1670     99    -58    124       O  
ATOM   1515  N   THR A 204     -15.350 -47.029 100.393  1.00 13.07           N  
ANISOU 1515  N   THR A 204     1501   1834   1629     57   -141    117       N  
ATOM   1516  CA  THR A 204     -15.891 -48.379 100.445  1.00 10.78           C  
ANISOU 1516  CA  THR A 204     1204   1557   1334     36   -162    106       C  
ATOM   1517  C   THR A 204     -15.862 -49.063  99.083  1.00 12.27           C  
ANISOU 1517  C   THR A 204     1407   1761   1494     23   -190    103       C  
ATOM   1518  O   THR A 204     -15.633 -50.280  99.005  1.00 13.40           O  
ANISOU 1518  O   THR A 204     1561   1905   1626      4   -201     83       O  
ATOM   1519  CB  THR A 204     -17.336 -48.366 100.988  1.00  9.26           C  
ANISOU 1519  CB  THR A 204      977   1377   1165     38   -171    122       C  
ATOM   1520  OG1 THR A 204     -18.112 -47.401 100.256  1.00 10.82           O  
ANISOU 1520  OG1 THR A 204     1159   1586   1366     54   -181    149       O  
ATOM   1521  CG2 THR A 204     -17.309 -47.983 102.454  1.00 11.07           C  
ANISOU 1521  CG2 THR A 204     1195   1592   1420     47   -142    117       C  
ATOM   1522  N   GLU A 205     -16.078 -48.285  98.021  1.00 11.22           N  
ANISOU 1522  N   GLU A 205     1277   1639   1348     35   -200    123       N  
ATOM   1523  CA  GLU A 205     -16.009 -48.815  96.655  1.00 12.17           C  
ANISOU 1523  CA  GLU A 205     1414   1777   1435     25   -225    121       C  
ATOM   1524  C   GLU A 205     -14.608 -49.335  96.339  1.00 11.15           C  
ANISOU 1524  C   GLU A 205     1318   1636   1283     19   -213     97       C  
ATOM   1525  O   GLU A 205     -14.447 -50.424  95.781  1.00 12.48           O  
ANISOU 1525  O   GLU A 205     1501   1810   1429      2   -230     79       O  
ATOM   1526  CB  GLU A 205     -16.396 -47.757  95.622  1.00 12.56           C  
ANISOU 1526  CB  GLU A 205     1460   1839   1473     42   -235    150       C  
ATOM   1527  CG  GLU A 205     -17.862 -47.379  95.594  1.00 14.91           C  
ANISOU 1527  CG  GLU A 205     1724   2155   1788     48   -255    176       C  
ATOM   1528  CD  GLU A 205     -18.113 -46.224  94.658  1.00 16.28           C  
ANISOU 1528  CD  GLU A 205     1895   2338   1952     68   -261    207       C  
ATOM   1529  OE1 GLU A 205     -17.860 -45.072  95.071  1.00 24.18           O  
ANISOU 1529  OE1 GLU A 205     2892   3322   2972     89   -236    222       O  
ATOM   1530  OE2 GLU A 205     -18.546 -46.466  93.510  1.00 28.87           O  
ANISOU 1530  OE2 GLU A 205     3493   3957   3521     63   -291    217       O  
ATOM   1531  N   LEU A 206     -13.601 -48.545  96.694  1.00  8.05           N  
ANISOU 1531  N   LEU A 206      938   1225    897     32   -184     98       N  
ATOM   1532  CA  LEU A 206     -12.228 -48.956  96.450  1.00  9.07           C  
ANISOU 1532  CA  LEU A 206     1096   1343   1008     27   -169     78       C  
ATOM   1533  C   LEU A 206     -11.883 -50.242  97.225  1.00  8.44           C  
ANISOU 1533  C   LEU A 206     1020   1253    933      9   -168     49       C  
ATOM   1534  O   LEU A 206     -11.309 -51.159  96.655  1.00 11.63           O  
ANISOU 1534  O   LEU A 206     1445   1659   1316     -2   -175     30       O  
ATOM   1535  CB  LEU A 206     -11.259 -47.826  96.798  1.00 12.27           C  
ANISOU 1535  CB  LEU A 206     1508   1729   1424     43   -138     85       C  
ATOM   1536  CG  LEU A 206      -9.796 -48.046  96.401  1.00  8.89           C  
ANISOU 1536  CG  LEU A 206     1107   1291    979     41   -121     70       C  
ATOM   1537  CD1 LEU A 206      -9.655 -48.359  94.902  1.00 10.68           C  
ANISOU 1537  CD1 LEU A 206     1353   1536   1167     39   -136     72       C  
ATOM   1538  CD2 LEU A 206      -8.965 -46.820  96.778  1.00 11.51           C  
ANISOU 1538  CD2 LEU A 206     1441   1604   1328     56    -92     80       C  
ATOM   1539  N   LYS A 207     -12.259 -50.326  98.499  1.00  8.49           N  
ANISOU 1539  N   LYS A 207     1008   1250    967      8   -160     46       N  
ATOM   1540  CA  LYS A 207     -12.012 -51.548  99.268  1.00  9.44           C  
ANISOU 1540  CA  LYS A 207     1132   1362   1095     -9   -160     24       C  
ATOM   1541  C   LYS A 207     -12.729 -52.760  98.672  1.00 10.24           C  
ANISOU 1541  C   LYS A 207     1231   1475   1183    -28   -190     15       C  
ATOM   1542  O   LYS A 207     -12.138 -53.836  98.553  1.00 12.54           O  
ANISOU 1542  O   LYS A 207     1539   1760   1464    -41   -193     -7       O  
ATOM   1543  CB  LYS A 207     -12.431 -51.375 100.733  1.00 13.56           C  
ANISOU 1543  CB  LYS A 207     1631   1874   1645     -6   -146     26       C  
ATOM   1544  CG  LYS A 207     -12.382 -52.687 101.524  1.00 12.75           C  
ANISOU 1544  CG  LYS A 207     1528   1765   1550    -24   -149      8       C  
ATOM   1545  CD  LYS A 207     -12.711 -52.476 103.004  1.00 15.86           C  
ANISOU 1545  CD  LYS A 207     1904   2153   1971    -20   -133     12       C  
ATOM   1546  CE  LYS A 207     -13.188 -53.773 103.669  1.00 15.11           C  
ANISOU 1546  CE  LYS A 207     1799   2058   1884    -39   -142      3       C  
ATOM   1547  NZ  LYS A 207     -12.240 -54.933 103.547  1.00 14.13           N  
ANISOU 1547  NZ  LYS A 207     1697   1922   1750    -53   -145    -18       N  
ATOM   1548  N   ALA A 208     -13.991 -52.588  98.285  1.00 10.07           N  
ANISOU 1548  N   ALA A 208     1189   1472   1164    -29   -212     32       N  
ATOM   1549  CA  ALA A 208     -14.741 -53.700  97.717  1.00 11.02           C  
ANISOU 1549  CA  ALA A 208     1307   1605   1276    -49   -244     23       C  
ATOM   1550  C   ALA A 208     -14.067 -54.215  96.448  1.00 14.98           C  
ANISOU 1550  C   ALA A 208     1839   2111   1742    -55   -256      7       C  
ATOM   1551  O   ALA A 208     -14.002 -55.425  96.219  1.00 13.15           O  
ANISOU 1551  O   ALA A 208     1618   1876   1502    -73   -271    -15       O  
ATOM   1552  CB  ALA A 208     -16.190 -53.291  97.424  1.00 14.70           C  
ANISOU 1552  CB  ALA A 208     1744   2091   1750    -48   -267     47       C  
ATOM   1553  N   ALA A 209     -13.561 -53.290  95.636  1.00 11.33           N  
ANISOU 1553  N   ALA A 209     1391   1655   1260    -39   -248     18       N  
ATOM   1554  CA  ALA A 209     -12.904 -53.637  94.385  1.00 13.34           C  
ANISOU 1554  CA  ALA A 209     1675   1917   1477    -41   -256      6       C  
ATOM   1555  C   ALA A 209     -11.612 -54.420  94.646  1.00 12.26           C  
ANISOU 1555  C   ALA A 209     1562   1760   1335    -46   -236    -22       C  
ATOM   1556  O   ALA A 209     -11.352 -55.433  93.988  1.00 12.75           O  
ANISOU 1556  O   ALA A 209     1644   1823   1376    -58   -249    -45       O  
ATOM   1557  CB  ALA A 209     -12.618 -52.379  93.566  1.00 14.43           C  
ANISOU 1557  CB  ALA A 209     1820   2065   1596    -21   -247     28       C  
ATOM   1558  N   PHE A 210     -10.802 -53.941  95.591  1.00 12.60           N  
ANISOU 1558  N   PHE A 210     1604   1786   1399    -36   -206    -21       N  
ATOM   1559  CA  PHE A 210      -9.585 -54.648  95.986  1.00 10.95           C  
ANISOU 1559  CA  PHE A 210     1413   1557   1190    -40   -186    -45       C  
ATOM   1560  C   PHE A 210      -9.936 -56.031  96.526  1.00 14.10           C  
ANISOU 1560  C   PHE A 210     1809   1948   1601    -60   -200    -65       C  
ATOM   1561  O   PHE A 210      -9.324 -57.018  96.149  1.00 10.15           O  
ANISOU 1561  O   PHE A 210     1329   1440   1088    -68   -202    -88       O  
ATOM   1562  CB  PHE A 210      -8.794 -53.866  97.047  1.00  8.95           C  
ANISOU 1562  CB  PHE A 210     1153   1286    960    -28   -155    -38       C  
ATOM   1563  CG  PHE A 210      -7.810 -52.867  96.479  1.00  8.04           C  
ANISOU 1563  CG  PHE A 210     1053   1170    833    -12   -134    -29       C  
ATOM   1564  CD1 PHE A 210      -6.718 -53.290  95.742  1.00 12.30           C  
ANISOU 1564  CD1 PHE A 210     1616   1706   1351    -12   -125    -44       C  
ATOM   1565  CD2 PHE A 210      -7.949 -51.501  96.728  1.00 11.16           C  
ANISOU 1565  CD2 PHE A 210     1435   1564   1242      3   -122     -6       C  
ATOM   1566  CE1 PHE A 210      -5.811 -52.381  95.232  1.00 13.18           C  
ANISOU 1566  CE1 PHE A 210     1738   1816   1452      2   -103    -33       C  
ATOM   1567  CE2 PHE A 210      -7.034 -50.589  96.230  1.00  8.92           C  
ANISOU 1567  CE2 PHE A 210     1163   1277    951     16   -102      4       C  
ATOM   1568  CZ  PHE A 210      -5.968 -51.033  95.472  1.00 11.02           C  
ANISOU 1568  CZ  PHE A 210     1452   1541   1193     15    -93     -9       C  
ATOM   1569  N   ASP A 211     -10.926 -56.092  97.413  1.00 14.06           N  
ANISOU 1569  N   ASP A 211     1777   1943   1621    -66   -209    -55       N  
ATOM   1570  CA  ASP A 211     -11.337 -57.363  98.007  1.00 13.46           C  
ANISOU 1570  CA  ASP A 211     1696   1858   1560    -85   -221    -69       C  
ATOM   1571  C   ASP A 211     -11.797 -58.366  96.946  1.00 13.59           C  
ANISOU 1571  C   ASP A 211     1723   1883   1557   -102   -251    -85       C  
ATOM   1572  O   ASP A 211     -11.428 -59.544  96.985  1.00 11.04           O  
ANISOU 1572  O   ASP A 211     1414   1546   1235   -116   -255   -108       O  
ATOM   1573  CB  ASP A 211     -12.452 -57.144  99.029  1.00 14.61           C  
ANISOU 1573  CB  ASP A 211     1809   2007   1735    -89   -225    -52       C  
ATOM   1574  CG  ASP A 211     -11.952 -56.518 100.323  1.00 13.51           C  
ANISOU 1574  CG  ASP A 211     1661   1856   1617    -76   -195    -45       C  
ATOM   1575  OD1 ASP A 211     -10.725 -56.514 100.560  1.00 14.77           O  
ANISOU 1575  OD1 ASP A 211     1838   2001   1772    -70   -175    -56       O  
ATOM   1576  OD2 ASP A 211     -12.791 -56.037 101.117  1.00 15.64           O  
ANISOU 1576  OD2 ASP A 211     1905   2130   1906    -73   -192    -28       O  
ATOM   1577  N   LYS A 212     -12.594 -57.887  95.998  1.00 13.17           N  
ANISOU 1577  N   LYS A 212     1666   1852   1487   -101   -273    -73       N  
ATOM   1578  CA  LYS A 212     -13.109 -58.732  94.926  1.00 21.58           C  
ANISOU 1578  CA  LYS A 212     2742   2928   2531   -117   -305    -88       C  
ATOM   1579  C   LYS A 212     -11.964 -59.280  94.073  1.00 16.45           C  
ANISOU 1579  C   LYS A 212     2129   2271   1850   -116   -299   -114       C  
ATOM   1580  O   LYS A 212     -11.889 -60.486  93.805  1.00 15.28           O  
ANISOU 1580  O   LYS A 212     1991   2110   1704   -124   -303   -139       O  
ATOM   1581  CB  LYS A 212     -14.101 -57.937  94.066  1.00 17.97           C  
ANISOU 1581  CB  LYS A 212     2272   2499   2058   -113   -329    -66       C  
ATOM   1582  CG  LYS A 212     -14.950 -58.771  93.116  1.00 22.95           C  
ANISOU 1582  CG  LYS A 212     2904   3135   2681   -121   -356    -80       C  
ATOM   1583  CD  LYS A 212     -16.143 -57.953  92.646  1.00 27.38           C  
ANISOU 1583  CD  LYS A 212     3442   3719   3242   -115   -376    -54       C  
ATOM   1584  N   ALA A 213     -11.062 -58.399  93.655  1.00 15.36           N  
ANISOU 1584  N   ALA A 213     2006   2137   1694    -96   -276   -107       N  
ATOM   1585  CA  ALA A 213      -9.936 -58.830  92.835  1.00 16.68           C  
ANISOU 1585  CA  ALA A 213     2207   2300   1832    -92   -265   -129       C  
ATOM   1586  C   ALA A 213      -9.054 -59.818  93.590  1.00 14.32           C  
ANISOU 1586  C   ALA A 213     1917   1973   1551    -98   -248   -153       C  
ATOM   1587  O   ALA A 213      -8.546 -60.780  93.009  1.00 14.47           O  
ANISOU 1587  O   ALA A 213     1955   1984   1558   -100   -246   -178       O  
ATOM   1588  CB  ALA A 213      -9.112 -57.630  92.373  1.00 14.57           C  
ANISOU 1588  CB  ALA A 213     1950   2040   1548    -70   -240   -113       C  
ATOM   1589  N   LEU A 214      -8.885 -59.595  94.891  1.00 10.81           N  
ANISOU 1589  N   LEU A 214     1454   1514   1140    -95   -230   -143       N  
ATOM   1590  CA  LEU A 214      -8.009 -60.446  95.677  1.00 10.21           C  
ANISOU 1590  CA  LEU A 214     1386   1413   1082    -98   -213   -160       C  
ATOM   1591  C   LEU A 214      -8.584 -61.858  95.805  1.00 17.38           C  
ANISOU 1591  C   LEU A 214     2293   2310   2001   -119   -234   -179       C  
ATOM   1592  O   LEU A 214      -7.852 -62.830  95.625  1.00 16.22           O  
ANISOU 1592  O   LEU A 214     2161   2148   1856   -119   -223   -201       O  
ATOM   1593  CB  LEU A 214      -7.748 -59.837  97.065  1.00 10.38           C  
ANISOU 1593  CB  LEU A 214     1386   1423   1133    -90   -190   -144       C  
ATOM   1594  CG  LEU A 214      -6.953 -60.667  98.080  1.00 14.45           C  
ANISOU 1594  CG  LEU A 214     1905   1915   1671    -94   -175   -157       C  
ATOM   1595  CD1 LEU A 214      -5.533 -60.981  97.601  1.00 15.73           C  
ANISOU 1595  CD1 LEU A 214     2092   2066   1819    -85   -156   -175       C  
ATOM   1596  CD2 LEU A 214      -6.928 -59.990  99.450  1.00  9.68           C  
ANISOU 1596  CD2 LEU A 214     1279   1306   1093    -87   -158   -139       C  
ATOM   1597  N   THR A 215      -9.879 -61.984  96.101  1.00 16.36           N  
ANISOU 1597  N   THR A 215     2141   2189   1888   -131   -255   -168       N  
ATOM   1598  CA  THR A 215     -10.461 -63.329  96.222  1.00 14.00           C  
ANISOU 1598  CA  THR A 215     1834   1878   1609   -146   -266   -183       C  
ATOM   1599  C   THR A 215     -10.365 -64.075  94.899  1.00 14.38           C  
ANISOU 1599  C   THR A 215     1900   1930   1634   -148   -275   -207       C  
ATOM   1600  O   THR A 215     -10.094 -65.274  94.876  1.00 22.71           O  
ANISOU 1600  O   THR A 215     2962   2968   2698   -156   -271   -227       O  
ATOM   1601  CB  THR A 215     -11.945 -63.322  96.661  1.00 18.87           C  
ANISOU 1601  CB  THR A 215     2420   2503   2246   -159   -287   -166       C  
ATOM   1602  OG1 THR A 215     -12.683 -62.368  95.888  1.00 31.88           O  
ANISOU 1602  OG1 THR A 215     4060   4177   3876   -153   -304   -150       O  
ATOM   1603  CG2 THR A 215     -12.072 -62.986  98.118  1.00 16.53           C  
ANISOU 1603  CG2 THR A 215     2103   2200   1978   -161   -276   -147       C  
ATOM   1604  N   GLU A 216     -10.577 -63.355  93.805  1.00 15.14           N  
ANISOU 1604  N   GLU A 216     2004   2049   1701   -139   -285   -202       N  
ATOM   1605  CA  GLU A 216     -10.526 -63.959  92.476  1.00 19.54           C  
ANISOU 1605  CA  GLU A 216     2578   2615   2231   -140   -294   -224       C  
ATOM   1606  C   GLU A 216      -9.113 -64.415  92.078  1.00 22.63           C  
ANISOU 1606  C   GLU A 216     2997   2995   2608   -132   -269   -246       C  
ATOM   1607  O   GLU A 216      -8.943 -65.501  91.511  1.00 17.45           O  
ANISOU 1607  O   GLU A 216     2351   2331   1947   -139   -270   -271       O  
ATOM   1608  CB  GLU A 216     -11.099 -62.981  91.452  1.00 18.42           C  
ANISOU 1608  CB  GLU A 216     2437   2502   2059   -132   -311   -210       C  
ATOM   1609  CG  GLU A 216     -12.609 -62.802  91.619  1.00 22.11           C  
ANISOU 1609  CG  GLU A 216     2876   2982   2542   -142   -339   -193       C  
ATOM   1610  CD  GLU A 216     -13.179 -61.629  90.843  1.00 31.85           C  
ANISOU 1610  CD  GLU A 216     4106   4243   3752   -130   -354   -171       C  
ATOM   1611  OE1 GLU A 216     -12.404 -60.902  90.189  1.00 34.09           O  
ANISOU 1611  OE1 GLU A 216     4410   4537   4006   -115   -342   -166       O  
ATOM   1612  OE2 GLU A 216     -14.412 -61.434  90.899  1.00 36.28           O  
ANISOU 1612  OE2 GLU A 216     4644   4816   4326   -137   -376   -155       O  
ATOM   1613  N   LEU A 217      -8.094 -63.614  92.374  1.00 18.79           N  
ANISOU 1613  N   LEU A 217     2519   2505   2114   -117   -245   -236       N  
ATOM   1614  CA  LEU A 217      -6.739 -64.024  92.007  1.00 12.61           C  
ANISOU 1614  CA  LEU A 217     1759   1711   1321   -108   -219   -255       C  
ATOM   1615  C   LEU A 217      -6.244 -65.140  92.935  1.00 15.73           C  
ANISOU 1615  C   LEU A 217     2151   2077   1748   -115   -207   -269       C  
ATOM   1616  O   LEU A 217      -5.338 -65.899  92.588  1.00 17.02           O  
ANISOU 1616  O   LEU A 217     2330   2228   1909   -112   -191   -289       O  
ATOM   1617  CB  LEU A 217      -5.781 -62.822  92.008  1.00 14.47           C  
ANISOU 1617  CB  LEU A 217     2005   1953   1541    -90   -197   -239       C  
ATOM   1618  CG  LEU A 217      -5.324 -62.143  93.305  1.00 13.47           C  
ANISOU 1618  CG  LEU A 217     1870   1812   1437    -84   -181   -223       C  
ATOM   1619  CD1 LEU A 217      -4.088 -62.834  93.859  1.00 14.82           C  
ANISOU 1619  CD1 LEU A 217     2048   1958   1625    -79   -156   -238       C  
ATOM   1620  CD2 LEU A 217      -5.034 -60.668  93.036  1.00 13.39           C  
ANISOU 1620  CD2 LEU A 217     1866   1817   1406    -70   -172   -201       C  
ATOM   1621  N   ARG A 218      -6.839 -65.243  94.119  1.00 14.50           N  
ANISOU 1621  N   ARG A 218     1976   1911   1624   -124   -214   -256       N  
ATOM   1622  CA  ARG A 218      -6.510 -66.344  95.019  1.00 11.79           C  
ANISOU 1622  CA  ARG A 218     1628   1540   1310   -132   -205   -266       C  
ATOM   1623  C   ARG A 218      -7.187 -67.622  94.527  1.00 16.86           C  
ANISOU 1623  C   ARG A 218     2271   2177   1958   -149   -221   -285       C  
ATOM   1624  O   ARG A 218      -6.564 -68.674  94.459  1.00 19.65           O  
ANISOU 1624  O   ARG A 218     2636   2511   2320   -152   -210   -304       O  
ATOM   1625  CB  ARG A 218      -6.932 -66.025  96.460  1.00 18.44           C  
ANISOU 1625  CB  ARG A 218     2450   2375   2182   -137   -206   -245       C  
ATOM   1626  CG  ARG A 218      -5.947 -65.116  97.196  1.00 11.77           C  
ANISOU 1626  CG  ARG A 218     1607   1526   1339   -122   -184   -233       C  
ATOM   1627  CD  ARG A 218      -6.300 -64.972  98.672  1.00 15.13           C  
ANISOU 1627  CD  ARG A 218     2013   1942   1794   -128   -184   -216       C  
ATOM   1628  NE  ARG A 218      -6.491 -66.272  99.308  1.00 20.00           N  
ANISOU 1628  NE  ARG A 218     2623   2539   2436   -141   -186   -223       N  
ATOM   1629  CZ  ARG A 218      -5.503 -67.089  99.664  1.00 18.40           C  
ANISOU 1629  CZ  ARG A 218     2431   2316   2244   -138   -169   -234       C  
ATOM   1630  NH1 ARG A 218      -4.234 -66.753  99.451  1.00 19.48           N  
ANISOU 1630  NH1 ARG A 218     2583   2449   2371   -123   -149   -240       N  
ATOM   1631  NH2 ARG A 218      -5.784 -68.254 100.228  1.00 23.38           N  
ANISOU 1631  NH2 ARG A 218     3056   2928   2897   -151   -172   -236       N  
ATOM   1632  N   GLN A 219      -8.458 -67.506  94.164  1.00 20.70           N  
ANISOU 1632  N   GLN A 219     2744   2679   2440   -160   -247   -279       N  
ATOM   1633  CA  GLN A 219      -9.255 -68.661  93.759  1.00 21.41           C  
ANISOU 1633  CA  GLN A 219     2833   2765   2539   -179   -265   -296       C  
ATOM   1634  C   GLN A 219      -8.804 -69.309  92.452  1.00 24.95           C  
ANISOU 1634  C   GLN A 219     3303   3215   2960   -178   -265   -325       C  
ATOM   1635  O   GLN A 219      -8.941 -70.524  92.294  1.00 24.88           O  
ANISOU 1635  O   GLN A 219     3300   3191   2963   -192   -269   -345       O  
ATOM   1636  CB  GLN A 219     -10.730 -68.267  93.647  1.00 25.44           C  
ANISOU 1636  CB  GLN A 219     3321   3294   3051   -189   -293   -281       C  
ATOM   1637  CG  GLN A 219     -11.433 -68.151  94.991  1.00 35.60           C  
ANISOU 1637  CG  GLN A 219     4581   4572   4371   -197   -296   -259       C  
ATOM   1638  CD  GLN A 219     -12.825 -67.558  94.876  1.00 40.67           C  
ANISOU 1638  CD  GLN A 219     5200   5236   5016   -204   -321   -240       C  
ATOM   1639  OE1 GLN A 219     -13.428 -67.561  93.803  1.00 46.02           O  
ANISOU 1639  OE1 GLN A 219     5880   5931   5675   -207   -341   -248       O  
ATOM   1640  NE2 GLN A 219     -13.339 -67.036  95.984  1.00 40.35           N  
ANISOU 1640  NE2 GLN A 219     5136   5195   4999   -205   -319   -215       N  
ATOM   1641  N   ASP A 220      -8.274 -68.529  91.514  1.00 19.24           N  
ANISOU 1641  N   ASP A 220     2595   2512   2203   -163   -259   -326       N  
ATOM   1642  CA  ASP A 220      -7.887 -69.125  90.237  1.00 24.42           C  
ANISOU 1642  CA  ASP A 220     3274   3174   2832   -162   -258   -353       C  
ATOM   1643  C   ASP A 220      -6.410 -69.512  90.194  1.00 20.45           C  
ANISOU 1643  C   ASP A 220     2790   2652   2327   -149   -226   -366       C  
ATOM   1644  O   ASP A 220      -5.880 -69.834  89.128  1.00 22.27           O  
ANISOU 1644  O   ASP A 220     3041   2889   2534   -144   -219   -386       O  
ATOM   1645  CB  ASP A 220      -8.238 -68.198  89.057  1.00 21.36           C  
ANISOU 1645  CB  ASP A 220     2892   2820   2404   -154   -270   -347       C  
ATOM   1646  CG  ASP A 220      -7.349 -66.957  88.964  1.00 23.54           C  
ANISOU 1646  CG  ASP A 220     3177   3108   2661   -133   -249   -329       C  
ATOM   1647  OD1 ASP A 220      -6.389 -66.815  89.746  1.00 20.12           O  
ANISOU 1647  OD1 ASP A 220     2745   2656   2243   -124   -225   -324       O  
ATOM   1648  OD2 ASP A 220      -7.612 -66.127  88.063  1.00 18.68           O  
ANISOU 1648  OD2 ASP A 220     2566   2519   2012   -125   -258   -320       O  
ATOM   1649  N   GLY A 221      -5.750 -69.468  91.349  1.00 19.23           N  
ANISOU 1649  N   GLY A 221     2629   2477   2200   -144   -208   -355       N  
ATOM   1650  CA  GLY A 221      -4.393 -69.967  91.475  1.00 22.71           C  
ANISOU 1650  CA  GLY A 221     3083   2897   2647   -132   -179   -367       C  
ATOM   1651  C   GLY A 221      -3.291 -68.959  91.203  1.00 21.75           C  
ANISOU 1651  C   GLY A 221     2971   2786   2507   -110   -156   -358       C  
ATOM   1652  O   GLY A 221      -2.105 -69.269  91.353  1.00 20.91           O  
ANISOU 1652  O   GLY A 221     2873   2665   2409    -98   -131   -365       O  
ATOM   1653  N   THR A 222      -3.675 -67.748  90.810  1.00 21.93           N  
ANISOU 1653  N   THR A 222     2991   2835   2505   -105   -164   -342       N  
ATOM   1654  CA  THR A 222      -2.698 -66.705  90.511  1.00 17.99           C  
ANISOU 1654  CA  THR A 222     2502   2348   1987    -85   -141   -331       C  
ATOM   1655  C   THR A 222      -1.877 -66.331  91.745  1.00 15.36           C  
ANISOU 1655  C   THR A 222     2159   1996   1680    -76   -121   -317       C  
ATOM   1656  O   THR A 222      -0.678 -66.097  91.641  1.00 16.15           O  
ANISOU 1656  O   THR A 222     2268   2092   1777    -60    -96   -319       O  
ATOM   1657  CB  THR A 222      -3.377 -65.441  89.950  1.00 17.29           C  
ANISOU 1657  CB  THR A 222     2412   2289   1869    -83   -155   -311       C  
ATOM   1658  OG1 THR A 222      -4.069 -65.775  88.741  1.00 19.46           O  
ANISOU 1658  OG1 THR A 222     2696   2583   2117    -90   -173   -324       O  
ATOM   1659  CG2 THR A 222      -2.343 -64.360  89.640  1.00 15.69           C  
ANISOU 1659  CG2 THR A 222     2220   2096   1646    -64   -129   -298       C  
ATOM   1660  N   TYR A 223      -2.523 -66.290  92.910  1.00 14.02           N  
ANISOU 1660  N   TYR A 223     1972   1817   1538    -86   -132   -304       N  
ATOM   1661  CA  TYR A 223      -1.824 -65.923  94.146  1.00 13.39           C  
ANISOU 1661  CA  TYR A 223     1883   1722   1482    -78   -116   -291       C  
ATOM   1662  C   TYR A 223      -0.631 -66.843  94.398  1.00 15.44           C  
ANISOU 1662  C   TYR A 223     2148   1958   1760    -71    -94   -305       C  
ATOM   1663  O   TYR A 223       0.485 -66.381  94.641  1.00 14.50           O  
ANISOU 1663  O   TYR A 223     2030   1835   1644    -55    -72   -300       O  
ATOM   1664  CB  TYR A 223      -2.782 -65.962  95.344  1.00 15.53           C  
ANISOU 1664  CB  TYR A 223     2134   1986   1779    -92   -132   -277       C  
ATOM   1665  CG  TYR A 223      -2.157 -65.523  96.660  1.00 13.73           C  
ANISOU 1665  CG  TYR A 223     1897   1744   1574    -86   -117   -263       C  
ATOM   1666  CD1 TYR A 223      -1.359 -66.389  97.398  1.00 12.86           C  
ANISOU 1666  CD1 TYR A 223     1787   1612   1489    -85   -102   -268       C  
ATOM   1667  CD2 TYR A 223      -2.376 -64.243  97.166  1.00 12.70           C  
ANISOU 1667  CD2 TYR A 223     1759   1626   1442    -81   -118   -243       C  
ATOM   1668  CE1 TYR A 223      -0.788 -65.999  98.591  1.00 13.16           C  
ANISOU 1668  CE1 TYR A 223     1818   1639   1545    -80    -90   -254       C  
ATOM   1669  CE2 TYR A 223      -1.809 -63.844  98.367  1.00 10.03           C  
ANISOU 1669  CE2 TYR A 223     1412   1275   1123    -75   -105   -233       C  
ATOM   1670  CZ  TYR A 223      -1.015 -64.731  99.076  1.00 10.26           C  
ANISOU 1670  CZ  TYR A 223     1443   1281   1173    -75    -92   -237       C  
ATOM   1671  OH  TYR A 223      -0.421 -64.365 100.271  1.00  9.48           O  
ANISOU 1671  OH  TYR A 223     1331   1176   1096    -68    -80   -229       O  
ATOM   1672  N   ASP A 224      -0.870 -68.150  94.340  1.00 18.55           N  
ANISOU 1672  N   ASP A 224     2544   2336   2166    -82   -101   -321       N  
ATOM   1673  CA  ASP A 224       0.180 -69.120  94.636  1.00 16.40           C  
ANISOU 1673  CA  ASP A 224     2277   2041   1914    -76    -82   -332       C  
ATOM   1674  C   ASP A 224       1.302 -69.087  93.611  1.00 15.49           C  
ANISOU 1674  C   ASP A 224     2175   1930   1780    -57    -63   -346       C  
ATOM   1675  O   ASP A 224       2.482 -69.242  93.959  1.00 16.98           O  
ANISOU 1675  O   ASP A 224     2361   2106   1982    -41    -43   -347       O  
ATOM   1676  CB  ASP A 224      -0.413 -70.522  94.738  1.00 15.99           C  
ANISOU 1676  CB  ASP A 224     2227   1970   1879    -94    -94   -346       C  
ATOM   1677  CG  ASP A 224      -1.342 -70.662  95.928  1.00 25.35           C  
ANISOU 1677  CG  ASP A 224     3397   3147   3088   -110   -109   -330       C  
ATOM   1678  OD1 ASP A 224      -1.029 -70.085  96.992  1.00 30.25           O  
ANISOU 1678  OD1 ASP A 224     4007   3763   3722   -105   -101   -311       O  
ATOM   1679  OD2 ASP A 224      -2.386 -71.325  95.803  1.00 32.88           O  
ANISOU 1679  OD2 ASP A 224     4348   4099   4046   -128   -128   -336       O  
ATOM   1680  N   LYS A 225       0.944 -68.875  92.351  1.00 15.05           N  
ANISOU 1680  N   LYS A 225     2131   1895   1691    -58    -69   -357       N  
ATOM   1681  CA  LYS A 225       1.952 -68.749  91.310  1.00 18.75           C  
ANISOU 1681  CA  LYS A 225     2614   2373   2137    -40    -49   -368       C  
ATOM   1682  C   LYS A 225       2.830 -67.521  91.554  1.00 20.21           C  
ANISOU 1682  C   LYS A 225     2796   2567   2318    -23    -29   -349       C  
ATOM   1683  O   LYS A 225       4.044 -67.566  91.348  1.00 18.96           O  
ANISOU 1683  O   LYS A 225     2640   2404   2160     -5     -6   -354       O  
ATOM   1684  CB  LYS A 225       1.295 -68.673  89.931  1.00 21.51           C  
ANISOU 1684  CB  LYS A 225     2979   2746   2449    -46    -62   -380       C  
ATOM   1685  CG  LYS A 225       0.551 -69.940  89.531  1.00 24.82           C  
ANISOU 1685  CG  LYS A 225     3404   3156   2871    -63    -80   -403       C  
ATOM   1686  N   MET A 226       2.223 -66.429  92.010  1.00 14.71           N  
ANISOU 1686  N   MET A 226     2091   1882   1617    -27    -38   -328       N  
ATOM   1687  CA  MET A 226       2.991 -65.215  92.273  1.00 13.75           C  
ANISOU 1687  CA  MET A 226     1966   1768   1491    -12    -19   -310       C  
ATOM   1688  C   MET A 226       3.877 -65.383  93.512  1.00 14.26           C  
ANISOU 1688  C   MET A 226     2018   1810   1591     -4     -6   -303       C  
ATOM   1689  O   MET A 226       5.043 -64.970  93.518  1.00 13.56           O  
ANISOU 1689  O   MET A 226     1929   1719   1504     13     18   -299       O  
ATOM   1690  CB  MET A 226       2.057 -64.010  92.435  1.00 13.54           C  
ANISOU 1690  CB  MET A 226     1936   1758   1452    -18    -32   -288       C  
ATOM   1691  CG  MET A 226       1.442 -63.540  91.120  1.00 16.90           C  
ANISOU 1691  CG  MET A 226     2375   2209   1838    -20    -42   -286       C  
ATOM   1692  SD  MET A 226       0.569 -61.963  91.263  1.00 21.26           S  
ANISOU 1692  SD  MET A 226     2923   2781   2375    -21    -54   -256       S  
ATOM   1693  CE  MET A 226      -0.645 -62.359  92.524  1.00 16.91           C  
ANISOU 1693  CE  MET A 226     2352   2218   1855    -39    -83   -253       C  
ATOM   1694  N   ALA A 227       3.318 -65.991  94.554  1.00 12.09           N  
ANISOU 1694  N   ALA A 227     1732   1519   1344    -15    -21   -301       N  
ATOM   1695  CA  ALA A 227       4.031 -66.178  95.814  1.00 14.87           C  
ANISOU 1695  CA  ALA A 227     2074   1849   1727     -6    -15   -292       C  
ATOM   1696  C   ALA A 227       5.223 -67.124  95.661  1.00 13.67           C  
ANISOU 1696  C   ALA A 227     1929   1681   1587      8      0   -304       C  
ATOM   1697  O   ALA A 227       6.253 -66.942  96.312  1.00 13.47           O  
ANISOU 1697  O   ALA A 227     1900   1643   1575     21     15   -294       O  
ATOM   1698  CB  ALA A 227       3.081 -66.693  96.881  1.00 17.28           C  
ANISOU 1698  CB  ALA A 227     2370   2142   2055    -21    -36   -286       C  
ATOM   1699  N   LYS A 228       5.080 -68.122  94.792  1.00 14.21           N  
ANISOU 1699  N   LYS A 228     2005   1748   1648      5     -4   -326       N  
ATOM   1700  CA  LYS A 228       6.119 -69.139  94.605  1.00 15.10           C  
ANISOU 1700  CA  LYS A 228     2123   1842   1772     19      8   -339       C  
ATOM   1701  C   LYS A 228       7.421 -68.548  94.069  1.00 18.85           C  
ANISOU 1701  C   LYS A 228     2601   2325   2234     39     35   -338       C  
ATOM   1702  O   LYS A 228       8.491 -69.134  94.238  1.00 18.43           O  
ANISOU 1702  O   LYS A 228     2550   2257   2196     54     48   -341       O  
ATOM   1703  CB  LYS A 228       5.627 -70.241  93.663  1.00 19.64           C  
ANISOU 1703  CB  LYS A 228     2708   2416   2340      9      1   -366       C  
ATOM   1704  N   LYS A 229       7.336 -67.380  93.437  1.00 19.83           N  
ANISOU 1704  N   LYS A 229     2728   2474   2334     40     44   -330       N  
ATOM   1705  CA  LYS A 229       8.533 -66.703  92.957  1.00 19.96           C  
ANISOU 1705  CA  LYS A 229     2744   2500   2340     56     73   -325       C  
ATOM   1706  C   LYS A 229       9.433 -66.251  94.101  1.00 20.65           C  
ANISOU 1706  C   LYS A 229     2816   2574   2454     64     86   -306       C  
ATOM   1707  O   LYS A 229      10.641 -66.110  93.926  1.00 16.25           O  
ANISOU 1707  O   LYS A 229     2255   2017   1902     78    110   -302       O  
ATOM   1708  CB  LYS A 229       8.152 -65.512  92.075  1.00 18.55           C  
ANISOU 1708  CB  LYS A 229     2572   2348   2128     53     79   -315       C  
ATOM   1709  CG  LYS A 229       7.440 -65.934  90.795  1.00 24.51           C  
ANISOU 1709  CG  LYS A 229     3343   3119   2851     46     69   -334       C  
ATOM   1710  CD  LYS A 229       7.150 -64.753  89.886  1.00 33.83           C  
ANISOU 1710  CD  LYS A 229     4533   4326   3996     46     75   -320       C  
ATOM   1711  N   TYR A 230       8.854 -66.043  95.279  1.00 16.78           N  
ANISOU 1711  N   TYR A 230     2318   2075   1983     54     71   -293       N  
ATOM   1712  CA  TYR A 230       9.629 -65.540  96.405  1.00 13.70           C  
ANISOU 1712  CA  TYR A 230     1912   1676   1617     57     83   -275       C  
ATOM   1713  C   TYR A 230       9.770 -66.530  97.555  1.00 14.02           C  
ANISOU 1713  C   TYR A 230     1948   1693   1687     55     73   -274       C  
ATOM   1714  O   TYR A 230      10.784 -66.535  98.256  1.00 18.41           O  
ANISOU 1714  O   TYR A 230     2491   2239   2264     62     87   -266       O  
ATOM   1715  CB  TYR A 230       8.991 -64.264  96.956  1.00 13.38           C  
ANISOU 1715  CB  TYR A 230     1863   1647   1575     46     79   -258       C  
ATOM   1716  CG  TYR A 230       8.757 -63.188  95.930  1.00 11.69           C  
ANISOU 1716  CG  TYR A 230     1655   1454   1332     47     88   -254       C  
ATOM   1717  CD1 TYR A 230       7.531 -63.052  95.302  1.00 16.35           C  
ANISOU 1717  CD1 TYR A 230     2257   2058   1898     38     70   -258       C  
ATOM   1718  CD2 TYR A 230       9.761 -62.279  95.617  1.00 17.43           C  
ANISOU 1718  CD2 TYR A 230     2376   2189   2057     57    114   -243       C  
ATOM   1719  CE1 TYR A 230       7.310 -62.052  94.369  1.00 14.78           C  
ANISOU 1719  CE1 TYR A 230     2065   1879   1670     39     78   -250       C  
ATOM   1720  CE2 TYR A 230       9.553 -61.278  94.689  1.00 16.92           C  
ANISOU 1720  CE2 TYR A 230     2320   2143   1966     59    124   -235       C  
ATOM   1721  CZ  TYR A 230       8.329 -61.167  94.072  1.00 11.98           C  
ANISOU 1721  CZ  TYR A 230     1708   1531   1313     50    106   -238       C  
ATOM   1722  OH  TYR A 230       8.130 -60.172  93.155  1.00 13.35           O  
ANISOU 1722  OH  TYR A 230     1891   1724   1458     53    114   -226       O  
ATOM   1723  N   PHE A 231       8.742 -67.344  97.767  1.00 15.26           N  
ANISOU 1723  N   PHE A 231     2113   1839   1844     43     50   -281       N  
ATOM   1724  CA  PHE A 231       8.648 -68.109  99.004  1.00 13.56           C  
ANISOU 1724  CA  PHE A 231     1893   1603   1656     36     41   -275       C  
ATOM   1725  C   PHE A 231       8.468 -69.604  98.772  1.00 11.21           C  
ANISOU 1725  C   PHE A 231     1612   1285   1364     35     31   -289       C  
ATOM   1726  O   PHE A 231       7.815 -70.019  97.825  1.00 17.77           O  
ANISOU 1726  O   PHE A 231     2455   2119   2178     32     19   -302       O  
ATOM   1727  CB  PHE A 231       7.477 -67.604  99.856  1.00 13.43           C  
ANISOU 1727  CB  PHE A 231     1869   1592   1643     17     24   -263       C  
ATOM   1728  CG  PHE A 231       7.425 -66.107 100.007  1.00 15.06           C  
ANISOU 1728  CG  PHE A 231     2062   1818   1842     16     31   -251       C  
ATOM   1729  CD1 PHE A 231       8.357 -65.440 100.802  1.00 14.34           C  
ANISOU 1729  CD1 PHE A 231     1954   1728   1768     22     46   -239       C  
ATOM   1730  CD2 PHE A 231       6.438 -65.366  99.369  1.00 15.17           C  
ANISOU 1730  CD2 PHE A 231     2081   1849   1834      8     22   -251       C  
ATOM   1731  CE1 PHE A 231       8.303 -64.055 100.948  1.00 15.12           C  
ANISOU 1731  CE1 PHE A 231     2042   1842   1863     20     53   -229       C  
ATOM   1732  CE2 PHE A 231       6.381 -63.981  99.506  1.00 16.13           C  
ANISOU 1732  CE2 PHE A 231     2192   1987   1950      8     30   -240       C  
ATOM   1733  CZ  PHE A 231       7.317 -63.326 100.296  1.00 14.50           C  
ANISOU 1733  CZ  PHE A 231     1969   1778   1761     13     46   -229       C  
ATOM   1734  N   ASP A 232       9.026 -70.393  99.680  1.00 11.03           N  
ANISOU 1734  N   ASP A 232     1584   1242   1366     37     34   -284       N  
ATOM   1735  CA  ASP A 232       8.825 -71.839  99.681  1.00 14.50           C  
ANISOU 1735  CA  ASP A 232     2038   1657   1815     34     26   -295       C  
ATOM   1736  C   ASP A 232       7.991 -72.290 100.874  1.00 19.46           C  
ANISOU 1736  C   ASP A 232     2659   2272   2462     13     12   -284       C  
ATOM   1737  O   ASP A 232       8.040 -73.453 101.268  1.00 21.89           O  
ANISOU 1737  O   ASP A 232     2972   2558   2788     10      9   -286       O  
ATOM   1738  CB  ASP A 232      10.171 -72.563  99.682  1.00 21.45           C  
ANISOU 1738  CB  ASP A 232     2918   2522   2711     53     43   -300       C  
ATOM   1739  CG  ASP A 232      10.934 -72.373  98.383  1.00 37.77           C  
ANISOU 1739  CG  ASP A 232     4991   4601   4760     72     57   -315       C  
ATOM   1740  OD1 ASP A 232      10.298 -72.383  97.308  1.00 43.88           O  
ANISOU 1740  OD1 ASP A 232     5777   5386   5511     70     49   -329       O  
ATOM   1741  OD2 ASP A 232      12.171 -72.215  98.437  1.00 45.58           O  
ANISOU 1741  OD2 ASP A 232     5968   5591   5758     88     77   -311       O  
ATOM   1742  N   PHE A 233       7.232 -71.367 101.454  1.00 14.28           N  
ANISOU 1742  N   PHE A 233     1989   1633   1804      1      4   -271       N  
ATOM   1743  CA  PHE A 233       6.347 -71.704 102.562  1.00 10.57           C  
ANISOU 1743  CA  PHE A 233     1509   1157   1351    -18    -10   -261       C  
ATOM   1744  C   PHE A 233       5.010 -70.992 102.360  1.00 15.39           C  
ANISOU 1744  C   PHE A 233     2117   1785   1946    -35    -25   -258       C  
ATOM   1745  O   PHE A 233       4.839 -70.230 101.401  1.00 13.38           O  
ANISOU 1745  O   PHE A 233     1870   1547   1668    -31    -25   -263       O  
ATOM   1746  CB  PHE A 233       6.982 -71.327 103.911  1.00  7.63           C  
ANISOU 1746  CB  PHE A 233     1114    785   1002    -12     -4   -246       C  
ATOM   1747  CG  PHE A 233       6.873 -69.860 104.251  1.00 14.92           C  
ANISOU 1747  CG  PHE A 233     2021   1731   1916    -13     -2   -236       C  
ATOM   1748  CD1 PHE A 233       7.729 -68.929 103.681  1.00 21.03           C  
ANISOU 1748  CD1 PHE A 233     2794   2519   2680      1     13   -237       C  
ATOM   1749  CD2 PHE A 233       5.911 -69.416 105.156  1.00 14.44           C  
ANISOU 1749  CD2 PHE A 233     1947   1679   1860    -26    -15   -225       C  
ATOM   1750  CE1 PHE A 233       7.622 -67.570 103.996  1.00 13.30           C  
ANISOU 1750  CE1 PHE A 233     1801   1558   1694      0     16   -228       C  
ATOM   1751  CE2 PHE A 233       5.801 -68.066 105.481  1.00 13.59           C  
ANISOU 1751  CE2 PHE A 233     1826   1591   1745    -26    -13   -217       C  
ATOM   1752  CZ  PHE A 233       6.650 -67.143 104.893  1.00 15.25           C  
ANISOU 1752  CZ  PHE A 233     2036   1812   1945    -13      3   -219       C  
ATOM   1753  N   ASN A 234       4.057 -71.251 103.253  1.00 12.74           N  
ANISOU 1753  N   ASN A 234     1770   1447   1624    -51    -39   -249       N  
ATOM   1754  CA  ASN A 234       2.725 -70.661 103.138  1.00  8.25           C  
ANISOU 1754  CA  ASN A 234     1195    896   1044    -68    -54   -246       C  
ATOM   1755  C   ASN A 234       2.720 -69.221 103.665  1.00  9.12           C  
ANISOU 1755  C   ASN A 234     1288   1027   1150    -62    -51   -233       C  
ATOM   1756  O   ASN A 234       2.348 -68.972 104.811  1.00 12.05           O  
ANISOU 1756  O   ASN A 234     1642   1400   1535    -67    -56   -221       O  
ATOM   1757  CB  ASN A 234       1.706 -71.523 103.892  1.00 10.95           C  
ANISOU 1757  CB  ASN A 234     1529   1227   1405    -87    -69   -240       C  
ATOM   1758  CG  ASN A 234       0.325 -70.916 103.904  1.00 15.69           C  
ANISOU 1758  CG  ASN A 234     2117   1846   1998   -102    -85   -234       C  
ATOM   1759  OD1 ASN A 234      -0.042 -70.171 102.997  1.00 17.84           O  
ANISOU 1759  OD1 ASN A 234     2393   2136   2248   -103    -88   -239       O  
ATOM   1760  ND2 ASN A 234      -0.446 -71.211 104.954  1.00 16.33           N  
ANISOU 1760  ND2 ASN A 234     2182   1924   2099   -114    -95   -221       N  
ATOM   1761  N   VAL A 235       3.156 -68.277 102.829  1.00  9.12           N  
ANISOU 1761  N   VAL A 235     1294   1041   1130    -51    -42   -237       N  
ATOM   1762  CA  VAL A 235       3.295 -66.889 103.269  1.00 10.24           C  
ANISOU 1762  CA  VAL A 235     1420   1201   1270    -45    -36   -227       C  
ATOM   1763  C   VAL A 235       1.931 -66.270 103.636  1.00 11.40           C  
ANISOU 1763  C   VAL A 235     1555   1363   1413    -59    -51   -219       C  
ATOM   1764  O   VAL A 235       1.856 -65.386 104.505  1.00  9.98           O  
ANISOU 1764  O   VAL A 235     1358   1193   1239    -57    -48   -208       O  
ATOM   1765  CB  VAL A 235       4.005 -66.040 102.185  1.00 11.41           C  
ANISOU 1765  CB  VAL A 235     1577   1361   1397    -31    -21   -232       C  
ATOM   1766  CG1 VAL A 235       3.158 -65.949 100.916  1.00 11.73           C  
ANISOU 1766  CG1 VAL A 235     1632   1412   1412    -37    -32   -240       C  
ATOM   1767  CG2 VAL A 235       4.379 -64.641 102.722  1.00  8.10           C  
ANISOU 1767  CG2 VAL A 235     1142    956    980    -26    -10   -221       C  
ATOM   1768  N   TYR A 236       0.865 -66.756 103.001  1.00 11.79           N  
ANISOU 1768  N   TYR A 236     1611   1414   1454    -72    -68   -224       N  
ATOM   1769  CA  TYR A 236      -0.487 -66.282 103.309  1.00  8.33           C  
ANISOU 1769  CA  TYR A 236     1160    991   1016    -84    -85   -216       C  
ATOM   1770  C   TYR A 236      -0.843 -66.501 104.773  1.00 13.73           C  
ANISOU 1770  C   TYR A 236     1824   1669   1723    -91    -88   -202       C  
ATOM   1771  O   TYR A 236      -1.447 -65.635 105.409  1.00 11.50           O  
ANISOU 1771  O   TYR A 236     1526   1401   1441    -92    -88   -185       O  
ATOM   1772  CB  TYR A 236      -1.521 -66.965 102.421  1.00  8.63           C  
ANISOU 1772  CB  TYR A 236     1206   1029   1044   -100   -102   -223       C  
ATOM   1773  CG  TYR A 236      -2.936 -66.457 102.638  1.00 12.23           C  
ANISOU 1773  CG  TYR A 236     1645   1502   1501   -112   -122   -213       C  
ATOM   1774  CD1 TYR A 236      -3.344 -65.215 102.140  1.00 10.08           C  
ANISOU 1774  CD1 TYR A 236     1368   1252   1211   -106   -124   -206       C  
ATOM   1775  CD2 TYR A 236      -3.860 -67.217 103.341  1.00 12.47           C  
ANISOU 1775  CD2 TYR A 236     1662   1526   1551   -128   -134   -205       C  
ATOM   1776  CE1 TYR A 236      -4.640 -64.755 102.334  1.00  9.75           C  
ANISOU 1776  CE1 TYR A 236     1308   1225   1171   -115   -139   -191       C  
ATOM   1777  CE2 TYR A 236      -5.157 -66.770 103.533  1.00 12.90           C  
ANISOU 1777  CE2 TYR A 236     1699   1595   1607   -138   -151   -193       C  
ATOM   1778  CZ  TYR A 236      -5.544 -65.546 103.040  1.00 11.55           C  
ANISOU 1778  CZ  TYR A 236     1523   1447   1420   -131   -153   -185       C  
ATOM   1779  OH  TYR A 236      -6.842 -65.124 103.255  1.00 11.72           O  
ANISOU 1779  OH  TYR A 236     1524   1484   1445   -140   -166   -169       O  
ATOM   1780  N   GLY A 237      -0.458 -67.654 105.307  1.00  9.39           N  
ANISOU 1780  N   GLY A 237     1278   1099   1191    -94    -87   -204       N  
ATOM   1781  CA  GLY A 237      -0.741 -67.972 106.693  1.00 11.16           C  
ANISOU 1781  CA  GLY A 237     1487   1318   1436   -100    -89   -188       C  
ATOM   1782  C   GLY A 237      -2.083 -68.663 106.865  1.00 14.44           C  
ANISOU 1782  C   GLY A 237     1895   1730   1861   -120   -107   -183       C  
ATOM   1783  O   GLY A 237      -2.639 -69.205 105.911  1.00 18.68           O  
ANISOU 1783  O   GLY A 237     2441   2264   2391   -130   -118   -194       O  
ATOM   1784  N   ASP A 238      -2.598 -68.651 108.091  1.00 23.19           N  
ANISOU 1784  N   ASP A 238     2987   2843   2983   -125   -107   -162       N  
ATOM   1785  CA  ASP A 238      -3.863 -69.314 108.395  1.00 28.95           C  
ANISOU 1785  CA  ASP A 238     3704   3569   3725   -144   -122   -153       C  
TER    1786      ASP A 238                                                      
HETATM 1787  C   ACT A 301      12.338 -69.142  96.453  1.00 38.54           C  
ANISOU 1787  C   ACT A 301     5067   4767   4810     94    105   -307       C  
HETATM 1788  O   ACT A 301      12.991 -68.257  95.858  1.00 41.71           O  
ANISOU 1788  O   ACT A 301     5462   5186   5201    102    125   -302       O  
HETATM 1789  OXT ACT A 301      12.799 -69.529  97.550  1.00 43.95           O  
ANISOU 1789  OXT ACT A 301     5742   5435   5523     95    105   -297       O  
HETATM 1790  CH3 ACT A 301      11.074 -69.707  95.885  1.00 27.77           C  
ANISOU 1790  CH3 ACT A 301     3719   3403   3429     84     81   -323       C  
HETATM 1791  C   ACT A 302      -1.997 -58.767 124.573  1.00  2.98           C  
ANISOU 1791  C   ACT A 302      340    481    313    -24      8    -58       C  
HETATM 1792  O   ACT A 302      -1.152 -59.097 123.708  1.00 16.52           O  
ANISOU 1792  O   ACT A 302     2057   2179   2040    -28     -2    -64       O  
HETATM 1793  OXT ACT A 302      -1.758 -59.099 125.744  1.00 47.08           O  
ANISOU 1793  OXT ACT A 302     5927   6077   5882    -23      8    -51       O  
HETATM 1794  CH3 ACT A 302      -3.221 -58.004 124.201  1.00 12.01           C  
ANISOU 1794  CH3 ACT A 302     1476   1630   1459    -21     20    -59       C  
HETATM 1795  C   ACT A 303      18.094 -62.913 135.421  1.00 29.79           C  
ANISOU 1795  C   ACT A 303     3678   3976   3664     15   -303      4       C  
HETATM 1796  O   ACT A 303      17.069 -62.233 135.173  1.00 37.57           O  
ANISOU 1796  O   ACT A 303     4679   4960   4636     10   -283    -15       O  
HETATM 1797  OXT ACT A 303      17.908 -63.977 136.048  1.00 32.29           O  
ANISOU 1797  OXT ACT A 303     3998   4301   3969     23   -307     35       O  
HETATM 1798  CH3 ACT A 303      19.469 -62.489 135.005  1.00 29.52           C  
ANISOU 1798  CH3 ACT A 303     3622   3934   3660     13   -319     -7       C  
HETATM 1799  C   ACT A 304      22.344 -68.677 127.459  1.00 39.82           C  
ANISOU 1799  C   ACT A 304     4853   5041   5235     83   -212     61       C  
HETATM 1800  O   ACT A 304      22.129 -67.470 127.200  1.00 44.02           O  
ANISOU 1800  O   ACT A 304     5388   5583   5754     71   -208     37       O  
HETATM 1801  OXT ACT A 304      22.664 -68.932 128.641  1.00 44.61           O  
ANISOU 1801  OXT ACT A 304     5454   5666   5830     86   -236     81       O  
HETATM 1802  CH3 ACT A 304      22.227 -69.751 126.419  1.00 30.31           C  
ANISOU 1802  CH3 ACT A 304     3654   3806   4057     94   -190     65       C  
HETATM 1803  O   HOH A 401      21.094 -60.240 107.288  1.00 37.69           O  
ANISOU 1803  O   HOH A 401     4676   4676   4969     74    148   -148       O  
HETATM 1804  O   HOH A 402      11.230 -76.012 118.872  1.00 25.21           O  
ANISOU 1804  O   HOH A 402     3193   2954   3432     24    -63     -9       O  
HETATM 1805  O   HOH A 403       9.825 -44.111 108.441  1.00 27.76           O  
ANISOU 1805  O   HOH A 403     3484   3410   3652     -4    106   -108       O  
HETATM 1806  O   HOH A 404     -10.788 -60.539  99.486  1.00 18.22           O  
ANISOU 1806  O   HOH A 404     2313   2416   2192   -123   -224   -118       O  
HETATM 1807  O   HOH A 405     -17.059 -47.598  91.897  1.00 21.59           O  
ANISOU 1807  O   HOH A 405     2630   3045   2529     44   -304    185       O  
HETATM 1808  O   HOH A 406      23.802 -60.562 110.860  1.00 26.04           O  
ANISOU 1808  O   HOH A 406     3123   3201   3570     72     99   -123       O  
HETATM 1809  O   HOH A 407      10.386 -56.101 109.959  1.00 27.89           O  
ANISOU 1809  O   HOH A 407     3523   3484   3591      1     46   -152       O  
HETATM 1810  O   HOH A 408       9.651 -43.213  92.942  1.00 31.76           O  
ANISOU 1810  O   HOH A 408     4095   4035   3935     72    250    103       O  
HETATM 1811  O   HOH A 409     -10.736 -61.440  88.399  1.00 26.74           O  
ANISOU 1811  O   HOH A 409     3529   3614   3015   -101   -320   -202       O  
HETATM 1812  O   HOH A 410     -15.067 -41.973  99.236  1.00 23.02           O  
ANISOU 1812  O   HOH A 410     2760   3063   2925    136    -96    194       O  
HETATM 1813  O   HOH A 411      24.932 -63.221 103.984  1.00 25.54           O  
ANISOU 1813  O   HOH A 411     3129   3124   3452    137    229   -144       O  
HETATM 1814  O   HOH A 412      11.205 -48.669 106.597  1.00 30.68           O  
ANISOU 1814  O   HOH A 412     3864   3819   3974      3    110   -111       O  
HETATM 1815  O   HOH A 413     -14.409 -53.118  81.353  1.00 23.98           O  
ANISOU 1815  O   HOH A 413     3211   3432   2468     -2   -419     22       O  
HETATM 1816  O   HOH A 414      26.276 -76.095 108.331  1.00 29.98           O  
ANISOU 1816  O   HOH A 414     3716   3516   4157    241    159   -139       O  
HETATM 1817  O   HOH A 415     -15.784 -38.729 103.398  1.00 23.24           O  
ANISOU 1817  O   HOH A 415     2747   3015   3067    195     -8    185       O  
HETATM 1818  O   HOH A 416      19.678 -76.060 108.174  1.00 27.69           O  
ANISOU 1818  O   HOH A 416     3534   3212   3776    158    101   -184       O  
HETATM 1819  O   HOH A 417      -0.331 -62.992 121.992  1.00 24.30           O  
ANISOU 1819  O   HOH A 417     3046   3118   3070    -52    -27    -37       O  
HETATM 1820  O   HOH A 418      -3.783 -70.815 104.293  1.00 29.22           O  
ANISOU 1820  O   HOH A 418     3789   3589   3722   -153   -136   -214       O  
HETATM 1821  O   HOH A 419      11.874 -72.735 130.456  1.00 24.90           O  
ANISOU 1821  O   HOH A 419     3100   3154   3207     30   -155    164       O  
HETATM 1822  O   HOH A 420       3.821 -57.155 111.570  1.00 18.09           O  
ANISOU 1822  O   HOH A 420     2295   2274   2303    -21      1   -137       O  
HETATM 1823  O   HOH A 421      18.893 -71.903 128.304  1.00 37.44           O  
ANISOU 1823  O   HOH A 421     4612   4709   4906     84   -193    117       O  
HETATM 1824  O   HOH A 422       5.217 -75.238 125.414  1.00 26.30           O  
ANISOU 1824  O   HOH A 422     3314   3213   3468    -43    -85    128       O  
HETATM 1825  O   HOH A 423       4.014 -40.287 101.514  1.00 27.83           O  
ANISOU 1825  O   HOH A 423     3533   3444   3598     56    135     33       O  
HETATM 1826  O   HOH A 424      14.917 -71.750 131.359  1.00 28.44           O  
ANISOU 1826  O   HOH A 424     3521   3632   3653     52   -196    158       O  
HETATM 1827  O   HOH A 425       4.866 -70.038 109.014  1.00 12.50           O  
ANISOU 1827  O   HOH A 425     1661   1423   1665    -47    -39   -187       O  
HETATM 1828  O   HOH A 426       9.508 -51.252 120.708  1.00 19.34           O  
ANISOU 1828  O   HOH A 426     2416   2445   2489    -22    -28   -195       O  
HETATM 1829  O   HOH A 427       7.063 -76.970 116.842  1.00 22.61           O  
ANISOU 1829  O   HOH A 427     2900   2594   3097    -33    -65    -41       O  
HETATM 1830  O   HOH A 428       9.943 -77.251 124.464  1.00 26.78           O  
ANISOU 1830  O   HOH A 428     3369   3201   3605     11   -100    123       O  
HETATM 1831  O   HOH A 429      23.529 -74.531 115.537  1.00 20.26           O  
ANISOU 1831  O   HOH A 429     2431   2315   2954    184     20    -48       O  
HETATM 1832  O   HOH A 430       5.834 -51.914 125.818  1.00 29.04           O  
ANISOU 1832  O   HOH A 430     3672   3745   3615     -8    -34   -198       O  
HETATM 1833  O   HOH A 431      -4.024 -58.898 121.269  1.00 23.25           O  
ANISOU 1833  O   HOH A 431     2890   3026   2919    -38      6    -53       O  
HETATM 1834  O   HOH A 432      -7.601 -62.870 102.180  1.00 10.14           O  
ANISOU 1834  O   HOH A 432     1313   1323   1215   -124   -169   -150       O  
HETATM 1835  O   HOH A 433       1.665 -66.887 110.560  1.00 15.00           O  
ANISOU 1835  O   HOH A 433     1941   1810   1948    -71    -55   -147       O  
HETATM 1836  O   HOH A 434     -15.856 -57.024  97.150  1.00 22.90           O  
ANISOU 1836  O   HOH A 434     2813   3113   2774   -108   -306    -19       O  
HETATM 1837  O   HOH A 435      11.254 -66.638 102.814  1.00 24.01           O  
ANISOU 1837  O   HOH A 435     3147   2919   3055     43     71   -229       O  
HETATM 1838  O   HOH A 436       4.602 -44.058 111.941  1.00 34.15           O  
ANISOU 1838  O   HOH A 436     4307   4246   4421     15     70   -136       O  
HETATM 1839  O   HOH A 437      20.231 -47.592 122.016  1.00 33.41           O  
ANISOU 1839  O   HOH A 437     4083   4180   4431    -83   -105   -232       O  
HETATM 1840  O   HOH A 438       7.324 -51.641 102.849  1.00  9.60           O  
ANISOU 1840  O   HOH A 438     1252   1197   1197     18     92   -106       O  
HETATM 1841  O   HOH A 439      17.494 -61.476 109.051  1.00 30.60           O  
ANISOU 1841  O   HOH A 439     3825   3778   4024     52     89   -159       O  
HETATM 1842  O   HOH A 440      12.764 -57.116 114.670  1.00 18.83           O  
ANISOU 1842  O   HOH A 440     2337   2338   2479     -4      6   -151       O  
HETATM 1843  O   HOH A 441     -14.256 -57.985 102.114  1.00 27.12           O  
ANISOU 1843  O   HOH A 441     3331   3582   3391   -108   -217    -32       O  
HETATM 1844  O   HOH A 442      -0.204 -70.793 115.805  1.00 29.97           O  
ANISOU 1844  O   HOH A 442     3803   3679   3904   -105    -73    -60       O  
HETATM 1845  O   HOH A 443      -0.788 -61.656 114.058  1.00  9.40           O  
ANISOU 1845  O   HOH A 443     1180   1185   1207    -59    -37   -101       O  
HETATM 1846  O   HOH A 444       3.222 -41.885 111.037  1.00 33.04           O  
ANISOU 1846  O   HOH A 444     4168   4088   4300     31     85   -117       O  
HETATM 1847  O   HOH A 445      -2.817 -67.035  86.779  1.00 31.54           O  
ANISOU 1847  O   HOH A 445     4262   4115   3606    -83   -151   -368       O  
HETATM 1848  O   HOH A 446      -5.264 -51.289 119.914  1.00 18.66           O  
ANISOU 1848  O   HOH A 446     2304   2441   2345     21     50   -106       O  
HETATM 1849  O   HOH A 447     -15.781 -59.341  90.006  1.00 36.20           O  
ANISOU 1849  O   HOH A 447     4610   4848   4295   -118   -404   -103       O  
HETATM 1850  O   HOH A 448      -0.049 -50.215 114.757  1.00 15.61           O  
ANISOU 1850  O   HOH A 448     1952   1985   1993      7     28   -129       O  
HETATM 1851  O   HOH A 449      26.893 -71.260 114.385  1.00 25.93           O  
ANISOU 1851  O   HOH A 449     3072   3088   3692    193     52    -57       O  
HETATM 1852  O   HOH A 450     -13.788 -42.796  87.407  1.00 36.68           O  
ANISOU 1852  O   HOH A 450     4633   4968   4335    128   -238    305       O  
HETATM 1853  O   HOH A 451       0.452 -59.284 128.748  1.00 13.32           O  
ANISOU 1853  O   HOH A 451     1670   1831   1559    -13     -8    -51       O  
HETATM 1854  O   HOH A 452       3.347 -67.133 108.445  1.00 17.08           O  
ANISOU 1854  O   HOH A 452     2230   2057   2203    -54    -42   -179       O  
HETATM 1855  O   HOH A 453      12.265 -66.371 134.948  1.00 18.56           O  
ANISOU 1855  O   HOH A 453     2311   2525   2214     21   -202     87       O  
HETATM 1856  O   HOH A 454     -16.110 -52.069 100.939  1.00 16.23           O  
ANISOU 1856  O   HOH A 454     1900   2252   2015    -24   -198     60       O  
HETATM 1857  O   HOH A 455       5.310 -69.655  90.248  1.00 28.52           O  
ANISOU 1857  O   HOH A 455     3869   3594   3375      8     12   -398       O  
HETATM 1858  O   HOH A 456      -0.165 -58.461  87.275  1.00 27.55           O  
ANISOU 1858  O   HOH A 456     3758   3672   3037      6    -53   -194       O  
HETATM 1859  O   HOH A 457      -1.739 -64.511 111.686  1.00 17.67           O  
ANISOU 1859  O   HOH A 457     2244   2203   2268    -85    -63   -114       O  
HETATM 1860  O   HOH A 458      -4.310 -32.945 101.827  1.00  9.91           O  
ANISOU 1860  O   HOH A 458     1216   1108   1441    167    126    156       O  
HETATM 1861  O   HOH A 459     -11.314 -57.822  85.452  1.00 29.41           O  
ANISOU 1861  O   HOH A 459     3895   4025   3252    -49   -343   -123       O  
HETATM 1862  O   HOH A 460      -1.922 -53.449  86.763  1.00 19.61           O  
ANISOU 1862  O   HOH A 460     2719   2721   2010     38    -63    -62       O  
HETATM 1863  O   HOH A 461       7.529 -55.173  89.474  1.00 19.61           O  
ANISOU 1863  O   HOH A 461     2710   2598   2143     77    156   -130       O  
HETATM 1864  O   HOH A 462      14.567 -50.348 124.335  1.00 32.18           O  
ANISOU 1864  O   HOH A 462     4003   4081   4141    -48   -102   -230       O  
HETATM 1865  O   HOH A 463      -4.795 -63.881 116.801  1.00 31.95           O  
ANISOU 1865  O   HOH A 463     3996   4062   4080    -93    -45    -44       O  
HETATM 1866  O   HOH A 464      14.423 -60.927 100.074  1.00 28.90           O  
ANISOU 1866  O   HOH A 464     3733   3598   3648     71    164   -197       O  
HETATM 1867  O   HOH A 465      13.938 -58.422 116.878  1.00 15.07           O  
ANISOU 1867  O   HOH A 465     1845   1868   2012     -2    -21   -142       O  
HETATM 1868  O   HOH A 466      -8.626 -44.851 100.365  1.00  8.79           O  
ANISOU 1868  O   HOH A 466     1064   1205   1071     75    -39     74       O  
HETATM 1869  O   HOH A 467      19.075 -68.204 129.506  1.00 25.81           O  
ANISOU 1869  O   HOH A 467     3134   3309   3364     57   -218     67       O  
HETATM 1870  O   HOH A 468      -2.855 -52.544 118.153  1.00 11.84           O  
ANISOU 1870  O   HOH A 468     1457   1552   1489      2     25   -113       O  
HETATM 1871  O   HOH A 469      13.259 -53.055 125.802  1.00 20.24           O  
ANISOU 1871  O   HOH A 469     2510   2609   2573    -33   -111   -202       O  
HETATM 1872  O   HOH A 470       0.385 -60.677 110.584  1.00  9.06           O  
ANISOU 1872  O   HOH A 470     1160   1132   1151    -49    -33   -129       O  
HETATM 1873  O   HOH A 471       6.777 -57.787 108.081  1.00 18.85           O  
ANISOU 1873  O   HOH A 471     2412   2350   2399     -7     28   -154       O  
HETATM 1874  O   HOH A 472      -4.405 -62.048 118.235  1.00 20.21           O  
ANISOU 1874  O   HOH A 472     2506   2600   2573    -72    -27    -44       O  
HETATM 1875  O   HOH A 473      15.770 -55.049  95.752  1.00 27.07           O  
ANISOU 1875  O   HOH A 473     3501   3423   3362     86    270   -123       O  
HETATM 1876  O   HOH A 474       6.147 -56.448 112.537  1.00 26.17           O  
ANISOU 1876  O   HOH A 474     3310   3289   3344    -14      9   -144       O  
HETATM 1877  O   HOH A 475     -16.358 -46.236  89.812  1.00 26.53           O  
ANISOU 1877  O   HOH A 475     3288   3691   3101     69   -305    223       O  
HETATM 1878  O   HOH A 476       7.528 -68.146 131.900  1.00 27.00           O  
ANISOU 1878  O   HOH A 476     3395   3523   3340     -3   -117    105       O  
HETATM 1879  O   HOH A 477       7.452 -54.790 130.086  1.00 17.75           O  
ANISOU 1879  O   HOH A 477     2249   2380   2114     -9    -84   -169       O  
HETATM 1880  O   HOH A 478       2.392 -69.316 118.100  1.00 20.20           O  
ANISOU 1880  O   HOH A 478     2558   2471   2646    -69    -59    -46       O  
HETATM 1881  O   HOH A 479      12.032 -45.009  90.705  1.00 31.88           O  
ANISOU 1881  O   HOH A 479     4133   4086   3893     86    307     96       O  
HETATM 1882  O   HOH A 480      28.845 -62.055 120.255  1.00 26.48           O  
ANISOU 1882  O   HOH A 480     3022   3315   3723     64   -105    -48       O  
HETATM 1883  O   HOH A 481      11.351 -56.401  96.643  1.00 11.43           O  
ANISOU 1883  O   HOH A 481     1559   1449   1334     59    175   -155       O  
HETATM 1884  O   HOH A 482      12.292 -64.250  98.193  1.00 26.26           O  
ANISOU 1884  O   HOH A 482     3460   3256   3261     72    126   -242       O  
HETATM 1885  O   HOH A 483      16.000 -56.073 111.934  1.00 24.91           O  
ANISOU 1885  O   HOH A 483     3082   3089   3293      7     49   -150       O  
HETATM 1886  O   HOH A 484      14.687 -56.329  89.331  1.00 26.92           O  
ANISOU 1886  O   HOH A 484     3581   3485   3162    118    298   -139       O  
HETATM 1887  O   HOH A 485       8.365 -69.146 117.208  1.00  8.02           O  
ANISOU 1887  O   HOH A 485     1016    898   1132    -15    -48    -78       O  
HETATM 1888  O   HOH A 486      -9.169 -56.896 106.690  1.00 16.17           O  
ANISOU 1888  O   HOH A 486     1986   2130   2026    -63    -98    -59       O  
HETATM 1889  O   HOH A 487      -5.610 -67.139 107.155  1.00 19.86           O  
ANISOU 1889  O   HOH A 487     2538   2467   2542   -145   -135   -147       O  
HETATM 1890  O   HOH A 488     -11.719 -44.994 115.939  1.00 41.41           O  
ANISOU 1890  O   HOH A 488     5108   5315   5311    106     92    -46       O  
HETATM 1891  O   HOH A 489     -19.214 -45.062 101.188  1.00 22.40           O  
ANISOU 1891  O   HOH A 489     2586   3043   2881     99   -150    187       O  
HETATM 1892  O   HOH A 490      17.987 -73.695 122.253  1.00 25.60           O  
ANISOU 1892  O   HOH A 490     3147   3083   3498     93    -99     41       O  
HETATM 1893  O   HOH A 491     -12.122 -48.496 102.486  1.00 12.26           O  
ANISOU 1893  O   HOH A 491     1448   1686   1524     35    -93     49       O  
HETATM 1894  O   HOH A 492      16.879 -57.070 129.542  1.00 26.75           O  
ANISOU 1894  O   HOH A 492     3297   3491   3376    -23   -203   -143       O  
HETATM 1895  O   HOH A 493      15.740 -50.931  96.983  1.00 15.37           O  
ANISOU 1895  O   HOH A 493     1973   1929   1937     61    268    -62       O  
HETATM 1896  O   HOH A 494      15.502 -73.716 116.138  1.00 12.48           O  
ANISOU 1896  O   HOH A 494     1555   1355   1831     74    -24    -72       O  
HETATM 1897  O   HOH A 495     -13.210 -50.541  86.520  1.00 23.45           O  
ANISOU 1897  O   HOH A 495     3040   3327   2541     13   -326     95       O  
HETATM 1898  O   HOH A 496     -11.055 -59.758 106.364  1.00 31.07           O  
ANISOU 1898  O   HOH A 496     3858   4020   3929   -107   -142    -61       O  
HETATM 1899  O   HOH A 497       0.622 -68.806 100.684  1.00 14.70           O  
ANISOU 1899  O   HOH A 497     2019   1765   1799    -84    -75   -255       O  
HETATM 1900  O   HOH A 498      13.313 -55.815 127.669  1.00 20.92           O  
ANISOU 1900  O   HOH A 498     2596   2728   2623    -23   -137   -163       O  
HETATM 1901  O   HOH A 499       6.263 -59.407 112.277  1.00 12.36           O  
ANISOU 1901  O   HOH A 499     1571   1529   1598    -18     -1   -144       O  
HETATM 1902  O   HOH A 500      -2.270 -36.540 107.371  1.00 12.32           O  
ANISOU 1902  O   HOH A 500     1529   1429   1725    110    116     -5       O  
HETATM 1903  O   HOH A 501       4.196 -76.038 118.678  1.00 24.92           O  
ANISOU 1903  O   HOH A 501     3176   2937   3357    -69    -75      1       O  
HETATM 1904  O   HOH A 502      16.028 -60.082 131.936  1.00 17.71           O  
ANISOU 1904  O   HOH A 502     2167   2386   2175     -5   -225    -79       O  
HETATM 1905  O   HOH A 503      -6.868 -59.495 110.627  1.00 13.26           O  
ANISOU 1905  O   HOH A 503     1630   1726   1684    -76    -67    -76       O  
HETATM 1906  O   HOH A 504      21.434 -71.063 105.166  1.00 18.83           O  
ANISOU 1906  O   HOH A 504     2385   2183   2588    160    160   -197       O  
HETATM 1907  O   HOH A 505      28.175 -71.477 116.983  1.00 41.75           O  
ANISOU 1907  O   HOH A 505     5024   5110   5729    198     -1    -10       O  
HETATM 1908  O   HOH A 506      19.491 -71.506 120.310  1.00 15.55           O  
ANISOU 1908  O   HOH A 506     1856   1824   2230     97    -75     -8       O  
HETATM 1909  O   HOH A 507      22.484 -61.268 125.169  1.00 24.83           O  
ANISOU 1909  O   HOH A 507     2949   3169   3318     18   -183    -71       O  
HETATM 1910  O   HOH A 508       3.974 -65.299 106.312  1.00 12.32           O  
ANISOU 1910  O   HOH A 508     1639   1475   1566    -40    -24   -196       O  
HETATM 1911  O   HOH A 509      -3.824 -69.178  94.524  1.00 19.54           O  
ANISOU 1911  O   HOH A 509     2651   2468   2307   -126   -158   -322       O  
HETATM 1912  O   HOH A 510       7.938 -57.525  91.183  1.00 15.16           O  
ANISOU 1912  O   HOH A 510     2138   1995   1625     66    142   -182       O  
HETATM 1913  O   HOH A 511      12.012 -58.792 104.577  1.00 25.77           O  
ANISOU 1913  O   HOH A 511     3296   3203   3291     29     99   -171       O  
HETATM 1914  O   HOH A 512      15.237 -48.483  98.321  1.00 18.30           O  
ANISOU 1914  O   HOH A 512     2320   2281   2354     43    251    -38       O  
HETATM 1915  O   HOH A 513       8.505 -61.414 134.718  1.00  9.50           O  
ANISOU 1915  O   HOH A 513     1203   1414    992      3   -139    -22       O  
HETATM 1916  O   HOH A 514       7.898 -52.142  88.248  1.00 22.29           O  
ANISOU 1916  O   HOH A 514     3039   2962   2467     92    192    -54       O  
HETATM 1917  O   HOH A 515      21.846 -53.288 111.628  1.00 25.22           O  
ANISOU 1917  O   HOH A 515     3025   3113   3446     -3     78   -132       O  
HETATM 1918  O   HOH A 516      -7.788 -65.720 105.820  1.00 23.43           O  
ANISOU 1918  O   HOH A 516     2969   2958   2973   -154   -160   -137       O  
HETATM 1919  O   HOH A 517       8.482 -74.016 109.402  1.00 14.53           O  
ANISOU 1919  O   HOH A 517     1933   1591   1998     -7    -17   -194       O  
HETATM 1920  O   HOH A 518      -8.563 -46.329  84.931  1.00 28.28           O  
ANISOU 1920  O   HOH A 518     3716   3916   3113     90   -176    185       O  
HETATM 1921  O   HOH A 519      12.124 -41.972 103.410  1.00 30.30           O  
ANISOU 1921  O   HOH A 519     3803   3715   3994      3    182    -27       O  
HETATM 1922  O   HOH A 520      18.564 -51.761  93.998  1.00 13.04           O  
ANISOU 1922  O   HOH A 520     1683   1657   1615     94    356    -49       O  
HETATM 1923  O   HOH A 521       4.767 -63.932 108.758  1.00  8.39           O  
ANISOU 1923  O   HOH A 521     1111    990   1086    -32    -16   -169       O  
HETATM 1924  O   HOH A 522       2.992 -65.918 124.100  1.00 29.92           O  
ANISOU 1924  O   HOH A 522     3765   3809   3792    -43    -52     -4       O  
HETATM 1925  O   HOH A 523      -3.864 -51.621  85.868  1.00 24.75           O  
ANISOU 1925  O   HOH A 523     3353   3410   2640     47   -101     -1       O  
HETATM 1926  O   HOH A 524      15.644 -59.993 105.205  1.00 23.23           O  
ANISOU 1926  O   HOH A 524     2941   2861   3026     51    128   -173       O  
HETATM 1927  O   HOH A 525     -14.112 -49.027 104.205  1.00 14.14           O  
ANISOU 1927  O   HOH A 525     1641   1935   1795     31    -97     57       O  
HETATM 1928  O   HOH A 526      -1.780 -49.231  86.004  1.00 28.66           O  
ANISOU 1928  O   HOH A 526     3841   3883   3166     76    -24     54       O  
HETATM 1929  O   HOH A 527     -17.685 -43.352  99.498  1.00 22.00           O  
ANISOU 1929  O   HOH A 527     2578   2976   2805    123   -140    205       O  
HETATM 1930  O   HOH A 528       6.533 -54.083 101.825  1.00  8.93           O  
ANISOU 1930  O   HOH A 528     1191   1124   1077     16     76   -126       O  
HETATM 1931  O   HOH A 529       7.718 -42.436  93.811  1.00 20.06           O  
ANISOU 1931  O   HOH A 529     2609   2546   2466     72    214    107       O  
HETATM 1932  O   HOH A 530      15.123 -77.307 114.377  1.00 20.27           O  
ANISOU 1932  O   HOH A 530     2581   2248   2873     88     -6    -93       O  
HETATM 1933  O   HOH A 531      26.278 -60.948 112.282  1.00 17.80           O  
ANISOU 1933  O   HOH A 531     2019   2160   2585     81     81   -103       O  
HETATM 1934  O   HOH A 532      12.700 -62.933 133.448  1.00 11.43           O  
ANISOU 1934  O   HOH A 532     1407   1615   1320      7   -194     -6       O  
HETATM 1935  O   HOH A 533       5.567 -61.192 105.958  1.00  9.13           O  
ANISOU 1935  O   HOH A 533     1216   1106   1145    -15     12   -177       O  
HETATM 1936  O   HOH A 534       2.500 -44.509 108.260  1.00 11.20           O  
ANISOU 1936  O   HOH A 534     1408   1363   1484     30     74    -85       O  
HETATM 1937  O   HOH A 535       0.257 -72.877 107.128  1.00 20.02           O  
ANISOU 1937  O   HOH A 535     2637   2351   2617   -115    -92   -203       O  
HETATM 1938  O   HOH A 536      -9.073 -39.188 105.503  1.00 24.98           O  
ANISOU 1938  O   HOH A 536     3073   3152   3266    142     54     70       O  
HETATM 1939  O   HOH A 537      18.333 -75.365 109.805  1.00 29.09           O  
ANISOU 1939  O   HOH A 537     3701   3396   3955    133     72   -167       O  
HETATM 1940  O   HOH A 538       1.565 -58.571  89.052  1.00 18.18           O  
ANISOU 1940  O   HOH A 538     2559   2445   1905     18    -11   -200       O  
HETATM 1941  O   HOH A 539      -9.746 -50.625 116.255  1.00 15.32           O  
ANISOU 1941  O   HOH A 539     1826   2033   1960     30     43    -51       O  
HETATM 1942  O   HOH A 540       4.648 -56.331  89.420  1.00 21.04           O  
ANISOU 1942  O   HOH A 540     2907   2794   2294     54     79   -155       O  
HETATM 1943  O   HOH A 541       2.751 -69.644 107.546  1.00 19.64           O  
ANISOU 1943  O   HOH A 541     2576   2343   2543    -69    -57   -200       O  
HETATM 1944  O   HOH A 542      -9.626 -43.491 107.130  1.00 14.27           O  
ANISOU 1944  O   HOH A 542     1708   1849   1864     96     22     25       O  
HETATM 1945  O   HOH A 543       0.248 -53.542 102.767  1.00  6.44           O  
ANISOU 1945  O   HOH A 543      858    845    743     -3      2   -102       O  
HETATM 1946  O   HOH A 544     -15.357 -54.811 100.895  1.00 16.39           O  
ANISOU 1946  O   HOH A 544     1948   2260   2021    -66   -218     16       O  
HETATM 1947  O   HOH A 545      -1.257 -66.826 109.829  1.00 29.63           O  
ANISOU 1947  O   HOH A 545     3786   3679   3792    -98    -79   -141       O  
HETATM 1948  O   HOH A 546      19.647 -53.001 113.171  1.00 17.79           O  
ANISOU 1948  O   HOH A 546     2114   2179   2465    -13     44   -147       O  
HETATM 1949  O   HOH A 547      -3.459 -64.175 109.617  1.00 25.96           O  
ANISOU 1949  O   HOH A 547     3295   3264   3304    -98    -82   -122       O  
HETATM 1950  O   HOH A 548      18.653 -72.083 107.838  1.00 13.14           O  
ANISOU 1950  O   HOH A 548     1678   1437   1879    125    101   -188       O  
HETATM 1951  O   HOH A 549      -3.374 -69.946  87.758  1.00 30.55           O  
ANISOU 1951  O   HOH A 549     4130   3935   3544   -112   -168   -412       O  
HETATM 1952  O   HOH A 550      25.630 -62.245 127.336  1.00 28.05           O  
ANISOU 1952  O   HOH A 550     3293   3605   3759     30   -251    -33       O  
HETATM 1953  O   HOH A 551      14.957 -59.480 102.321  1.00 25.64           O  
ANISOU 1953  O   HOH A 551     3280   3180   3282     59    157   -179       O  
HETATM 1954  O   HOH A 552       0.643 -67.266 118.315  1.00 21.12           O  
ANISOU 1954  O   HOH A 552     2662   2628   2733    -75    -52    -46       O  
HETATM 1955  O   HOH A 553     -11.177 -66.511  90.026  1.00 25.49           O  
ANISOU 1955  O   HOH A 553     3356   3376   2952   -166   -326   -289       O  
HETATM 1956  O   HOH A 554      -8.847 -60.739 106.087  1.00 19.14           O  
ANISOU 1956  O   HOH A 554     2387   2481   2405   -106   -131    -91       O  
HETATM 1957  O   HOH A 555      12.761 -51.167 105.938  1.00 32.33           O  
ANISOU 1957  O   HOH A 555     4074   4035   4176     10    119   -121       O  
HETATM 1958  O   HOH A 556     -10.499 -51.022 109.783  1.00 14.82           O  
ANISOU 1958  O   HOH A 556     1765   1971   1895     10    -26    -20       O  
HETATM 1959  O  AHOH A 557       2.887 -54.315 112.961  0.60 20.27           O  
ANISOU 1959  O  AHOH A 557     2558   2563   2580    -14      9   -133       O  
HETATM 1960  O  BHOH A 557       3.516 -53.000 112.216  0.40 11.82           O  
ANISOU 1960  O  BHOH A 557     1489   1486   1516     -9     19   -135       O  
HETATM 1961  O   HOH A 558      -6.306 -63.233 109.190  1.00 24.69           O  
ANISOU 1961  O   HOH A 558     3106   3135   3141   -111   -100   -102       O  
HETATM 1962  O   HOH A 559     -13.941 -45.730  97.232  1.00 12.44           O  
ANISOU 1962  O   HOH A 559     1469   1764   1492     74   -151    145       O  
HETATM 1963  O   HOH A 560       3.371 -52.755 109.303  1.00 18.08           O  
ANISOU 1963  O   HOH A 560     2294   2278   2299     -5     27   -126       O  
HETATM 1964  O   HOH A 561      12.777 -58.675 112.266  1.00 19.61           O  
ANISOU 1964  O   HOH A 561     2451   2423   2576      6     27   -152       O  
HETATM 1965  O   HOH A 562     -11.770 -56.894 105.628  1.00 31.87           O  
ANISOU 1965  O   HOH A 562     3942   4147   4019    -75   -133    -36       O  
HETATM 1966  O   HOH A 563      22.442 -76.694 116.047  1.00 26.99           O  
ANISOU 1966  O   HOH A 563     3310   3124   3821    187      9    -35       O  
HETATM 1967  O  AHOH A 564      -9.159 -67.362  99.634  0.59 16.38           O  
ANISOU 1967  O  AHOH A 564     2130   2087   2008   -177   -227   -211       O  
HETATM 1968  O  BHOH A 564      -8.959 -68.959  99.566  0.41 11.25           O  
ANISOU 1968  O  BHOH A 564     1489   1414   1373   -189   -225   -230       O  
HETATM 1969  O   HOH A 565       1.586 -70.946 111.735  1.00 16.60           O  
ANISOU 1969  O   HOH A 565     2152   1951   2205    -90    -72   -135       O  
HETATM 1970  O   HOH A 566      17.978 -72.864 124.556  1.00 28.86           O  
ANISOU 1970  O   HOH A 566     3547   3544   3873     85   -132     70       O  
HETATM 1971  O   HOH A 567     -12.783 -55.522  91.461  1.00 24.16           O  
ANISOU 1971  O   HOH A 567     3101   3319   2760    -66   -311    -36       O  
HETATM 1972  O   HOH A 568      10.468 -45.641 100.367  1.00 23.81           O  
ANISOU 1972  O   HOH A 568     3028   2964   3055     29    179    -26       O  
HETATM 1973  O   HOH A 569     -13.075 -37.577 103.197  1.00 21.59           O  
ANISOU 1973  O   HOH A 569     2588   2759   2857    192     23    166       O  
HETATM 1974  O   HOH A 570      25.290 -71.688 110.718  1.00 20.42           O  
ANISOU 1974  O   HOH A 570     2454   2370   2934    188    115   -114       O  
HETATM 1975  O   HOH A 571      10.327 -59.293  91.456  1.00 29.82           O  
ANISOU 1975  O   HOH A 571     3979   3827   3524     79    174   -210       O  
HETATM 1976  O   HOH A 572       3.807 -73.987 120.711  1.00 32.71           O  
ANISOU 1976  O   HOH A 572     4143   3992   4294    -66    -73     27       O  
HETATM 1977  O   HOH A 573       5.535 -44.936  89.547  1.00 30.99           O  
ANISOU 1977  O   HOH A 573     4067   4035   3674     94    180    111       O  
HETATM 1978  O   HOH A 574      10.861 -41.597 109.459  1.00 34.90           O  
ANISOU 1978  O   HOH A 574     4376   4275   4611    -16    111   -116       O  
HETATM 1979  O   HOH A 575       8.096 -40.453  95.697  1.00 28.20           O  
ANISOU 1979  O   HOH A 575     3610   3525   3579     62    219    114       O  
HETATM 1980  O   HOH A 576       9.493 -59.103 105.817  1.00 19.45           O  
ANISOU 1980  O   HOH A 576     2502   2409   2478     11     61   -170       O  
HETATM 1981  O   HOH A 577      13.527 -68.019 100.312  1.00 37.05           O  
ANISOU 1981  O   HOH A 577     4821   4560   4695     83    110   -254       O  
HETATM 1982  O   HOH A 578      17.407 -50.364 116.953  1.00 21.34           O  
ANISOU 1982  O   HOH A 578     2586   2640   2882    -41    -13   -183       O  
HETATM 1983  O   HOH A 579       1.008 -46.920 112.254  1.00 24.00           O  
ANISOU 1983  O   HOH A 579     3020   3013   3084     21     49   -122       O  
HETATM 1984  O   HOH A 580     -11.263 -52.329 107.389  1.00 18.61           O  
ANISOU 1984  O   HOH A 580     2247   2466   2358    -10    -67    -11       O  
HETATM 1985  O   HOH A 581      13.386 -72.983 109.893  1.00 19.22           O  
ANISOU 1985  O   HOH A 581     2486   2189   2628     58     29   -185       O  
HETATM 1986  O   HOH A 582      15.159 -54.377 100.973  1.00 14.20           O  
ANISOU 1986  O   HOH A 582     1811   1754   1829     48    193   -126       O  
HETATM 1987  O   HOH A 583      -2.254 -68.999  99.434  1.00 20.49           O  
ANISOU 1987  O   HOH A 583     2737   2531   2517   -118   -117   -268       O  
HETATM 1988  O   HOH A 584       9.232 -53.703 113.784  1.00 15.72           O  
ANISOU 1988  O   HOH A 584     1965   1955   2052    -11     19   -155       O  
HETATM 1989  O   HOH A 585      -2.190 -42.637  85.363  1.00 35.30           O  
ANISOU 1989  O   HOH A 585     4632   4706   4073    131     28    245       O  
HETATM 1990  O   HOH A 586       2.171 -69.359 126.676  1.00 22.76           O  
ANISOU 1990  O   HOH A 586     2855   2899   2894    -53    -57     80       O  
HETATM 1991  O   HOH A 587       8.514 -49.490  88.436  1.00 19.10           O  
ANISOU 1991  O   HOH A 587     2606   2549   2102     97    223     10       O  
HETATM 1992  O   HOH A 588       6.340 -60.689 136.853  1.00 13.60           O  
ANISOU 1992  O   HOH A 588     1748   1988   1432     10   -112    -19       O  
HETATM 1993  O   HOH A 589       8.976 -53.615  86.207  1.00 23.26           O  
ANISOU 1993  O   HOH A 589     3197   3109   2532    104    218    -84       O  
HETATM 1994  O   HOH A 590       2.998 -72.084 128.399  1.00 21.30           O  
ANISOU 1994  O   HOH A 590     2670   2696   2727    -50    -69    146       O  
HETATM 1995  O   HOH A 591       0.853 -56.072 102.069  1.00  8.19           O  
ANISOU 1995  O   HOH A 591     1101   1061    949    -13     -8   -130       O  
HETATM 1996  O   HOH A 592     -10.068 -43.327  96.424  1.00 27.74           O  
ANISOU 1996  O   HOH A 592     3469   3650   3422    101    -76    152       O  
HETATM 1997  O   HOH A 593      10.929 -45.888 105.711  1.00 31.16           O  
ANISOU 1997  O   HOH A 593     3922   3862   4054      4    129    -86       O  
HETATM 1998  O   HOH A 594      14.411 -56.197 103.650  1.00 29.83           O  
ANISOU 1998  O   HOH A 594     3784   3722   3830     38    144   -149       O  
HETATM 1999  O   HOH A 595       8.109 -39.471 107.353  1.00 33.32           O  
ANISOU 1999  O   HOH A 595     4193   4063   4403     10    133    -69       O  
HETATM 2000  O   HOH A 596      13.911 -75.928 116.255  1.00 17.74           O  
ANISOU 2000  O   HOH A 596     2247   1978   2515     62    -32    -62       O  
HETATM 2001  O   HOH A 597       2.208 -52.989 116.476  1.00 20.00           O  
ANISOU 2001  O   HOH A 597     2514   2544   2541     -9     10   -140       O  
HETATM 2002  O   HOH A 598      10.927 -69.104 101.571  1.00 18.16           O  
ANISOU 2002  O   HOH A 598     2442   2151   2306     49     62   -255       O  
HETATM 2003  O   HOH A 599      22.148 -70.305 120.728  1.00 27.23           O  
ANISOU 2003  O   HOH A 599     3284   3326   3735    111    -86     -4       O  
HETATM 2004  O   HOH A 600     -14.169 -39.219 101.348  1.00 24.30           O  
ANISOU 2004  O   HOH A 600     2921   3157   3155    175    -27    191       O  
HETATM 2005  O   HOH A 601       6.731 -62.062 108.239  1.00  9.83           O  
ANISOU 2005  O   HOH A 601     1288   1181   1267    -13     10   -170       O  
HETATM 2006  O   HOH A 602       8.518 -55.989 112.177  1.00 21.92           O  
ANISOU 2006  O   HOH A 602     2765   2739   2824     -9     21   -150       O  
HETATM 2007  O   HOH A 603     -12.029 -40.892 101.796  1.00 16.40           O  
ANISOU 2007  O   HOH A 603     1959   2150   2123    139    -20    140       O  
HETATM 2008  O   HOH A 604       5.064 -55.716 108.674  1.00 23.25           O  
ANISOU 2008  O   HOH A 604     2960   2922   2950    -10     23   -141       O  
HETATM 2009  O   HOH A 605      13.804 -59.113 130.828  1.00 10.78           O  
ANISOU 2009  O   HOH A 605     1312   1494   1288    -10   -181   -101       O  
HETATM 2010  O   HOH A 606       4.485 -51.966 128.799  1.00 33.46           O  
ANISOU 2010  O   HOH A 606     4249   4352   4112      2    -31   -202       O  
HETATM 2011  O   HOH A 607     -11.542 -40.125  98.919  1.00 19.95           O  
ANISOU 2011  O   HOH A 607     2430   2613   2536    147    -37    185       O  
HETATM 2012  O   HOH A 608       4.467 -73.220 105.498  1.00 12.63           O  
ANISOU 2012  O   HOH A 608     1739   1391   1668    -56    -43   -234       O  
HETATM 2013  O   HOH A 609      15.924 -59.998 109.824  1.00 32.36           O  
ANISOU 2013  O   HOH A 609     4054   4015   4225     33     70   -156       O  
HETATM 2014  O   HOH A 610     -12.236 -57.891  89.875  1.00 31.31           O  
ANISOU 2014  O   HOH A 610     4056   4217   3623    -84   -332   -101       O  
HETATM 2015  O   HOH A 611      10.395 -76.351 116.514  1.00 25.30           O  
ANISOU 2015  O   HOH A 611     3230   2936   3448     14    -49    -56       O  
HETATM 2016  O   HOH A 612       8.418 -51.821 124.892  1.00 23.08           O  
ANISOU 2016  O   HOH A 612     2904   2968   2897    -19    -54   -206       O  
HETATM 2017  O   HOH A 613     -16.712 -45.235  97.879  1.00 15.54           O  
ANISOU 2017  O   HOH A 613     1799   2179   1926     86   -175    180       O  
HETATM 2018  O   HOH A 614      13.760 -50.461 114.989  1.00 27.73           O  
ANISOU 2018  O   HOH A 614     3443   3451   3642    -25     19   -173       O  
HETATM 2019  O   HOH A 615       1.638 -69.635  98.432  1.00 35.18           O  
ANISOU 2019  O   HOH A 615     4642   4360   4367    -75    -54   -288       O  
HETATM 2020  O   HOH A 616       3.741 -46.893  88.824  1.00 19.92           O  
ANISOU 2020  O   HOH A 616     2691   2671   2208     90    129     75       O  
HETATM 2021  O   HOH A 617     -20.239 -41.824  93.202  1.00 34.92           O  
ANISOU 2021  O   HOH A 617     4199   4716   4354    153   -267    338       O  
HETATM 2022  O   HOH A 618      -9.233 -50.381 118.999  1.00 19.07           O  
ANISOU 2022  O   HOH A 618     2310   2516   2419     40     68    -69       O  
HETATM 2023  O   HOH A 619       8.724 -71.745 107.486  1.00 20.73           O  
ANISOU 2023  O   HOH A 619     2724   2421   2729      1      1   -213       O  
HETATM 2024  O   HOH A 620     -13.655 -54.918  87.237  1.00 39.88           O  
ANISOU 2024  O   HOH A 620     5139   5371   4644    -46   -366    -22       O  
HETATM 2025  O  AHOH A 621       4.798 -50.372 106.758  0.50 32.52           O  
ANISOU 2025  O  AHOH A 621     4129   4096   4133      7     57   -110       O  
HETATM 2026  O  BHOH A 621       6.956 -50.518 106.509  0.50 32.52           O  
ANISOU 2026  O  BHOH A 621     4129   4096   4133      7     57   -110       O  
HETATM 2027  O   HOH A 622      27.217 -68.890 112.268  1.00 31.39           O  
ANISOU 2027  O   HOH A 622     3765   3805   4357    176     95    -85       O  
HETATM 2028  O   HOH A 623      15.709 -54.345 103.215  1.00 26.75           O  
ANISOU 2028  O   HOH A 623     3372   3331   3460     38    170   -130       O  
HETATM 2029  O   HOH A 624      19.339 -74.451 106.716  1.00 27.40           O  
ANISOU 2029  O   HOH A 624     3507   3207   3695    149    115   -202       O  
HETATM 2030  O   HOH A 625      22.923 -62.000 108.485  1.00 34.80           O  
ANISOU 2030  O   HOH A 625     4276   4296   4649     94    141   -140       O  
HETATM 2031  O   HOH A 626      -4.631 -45.498 120.403  1.00 27.14           O  
ANISOU 2031  O   HOH A 626     3396   3469   3447     68     88   -161       O  
HETATM 2032  O   HOH A 627       4.983 -51.509  88.473  1.00 23.83           O  
ANISOU 2032  O   HOH A 627     3231   3174   2650     78    124    -37       O  
HETATM 2033  O   HOH A 628      -1.672 -40.182 110.628  1.00 26.86           O  
ANISOU 2033  O   HOH A 628     3372   3317   3518     76     92    -79       O  
HETATM 2034  O   HOH A 629       8.914 -69.303 106.986  1.00 17.97           O  
ANISOU 2034  O   HOH A 629     2365   2112   2351      4     12   -211       O  
HETATM 2035  O   HOH A 630     -12.035 -50.301 114.694  1.00 30.15           O  
ANISOU 2035  O   HOH A 630     3671   3927   3857     34     31    -20       O  
HETATM 2036  O   HOH A 631      14.497 -44.556  92.227  1.00 32.46           O  
ANISOU 2036  O   HOH A 631     4161   4120   4052     73    340     91       O  
HETATM 2037  O   HOH A 632       5.839 -58.475 105.671  1.00 13.62           O  
ANISOU 2037  O   HOH A 632     1774   1693   1708     -7     28   -161       O  
HETATM 2038  O   HOH A 633      -0.559 -40.329  90.062  1.00 30.94           O  
ANISOU 2038  O   HOH A 633     4013   4025   3720    123     91    230       O  
HETATM 2039  O   HOH A 634      24.426 -73.006 118.153  1.00 26.66           O  
ANISOU 2039  O   HOH A 634     3194   3180   3754    169    -31     -7       O  
HETATM 2040  O   HOH A 635      -1.688 -36.414  94.885  1.00 27.85           O  
ANISOU 2040  O   HOH A 635     3550   3509   3525    136    110    233       O  
HETATM 2041  O   HOH A 636      26.622 -78.155 110.946  1.00 30.34           O  
ANISOU 2041  O   HOH A 636     3739   3526   4263    255    121    -95       O  
HETATM 2042  O   HOH A 637     -12.302 -41.422 105.284  1.00 19.46           O  
ANISOU 2042  O   HOH A 637     2329   2520   2545    135     10     91       O  
HETATM 2043  O   HOH A 638     -10.962 -64.624  87.509  1.00 35.01           O  
ANISOU 2043  O   HOH A 638     4589   4644   4068   -135   -336   -276       O  
HETATM 2044  O   HOH A 639     -14.996 -48.703 112.735  1.00 43.84           O  
ANISOU 2044  O   HOH A 639     5354   5681   5621     58     20     25       O  
HETATM 2045  O   HOH A 640       6.345 -53.175 129.091  1.00 26.91           O  
ANISOU 2045  O   HOH A 640     3413   3524   3287     -7    -60   -191       O  
HETATM 2046  O   HOH A 641       0.146 -51.183 117.226  1.00 26.37           O  
ANISOU 2046  O   HOH A 641     3314   3362   3344      3     23   -139       O  
HETATM 2047  O   HOH A 642       8.937 -62.278  90.633  1.00 33.41           O  
ANISOU 2047  O   HOH A 642     4459   4278   3959     67    125   -269       O  
HETATM 2048  O   HOH A 643      30.513 -62.600 122.137  1.00 29.46           O  
ANISOU 2048  O   HOH A 643     3352   3714   4126     69   -158    -22       O  
HETATM 2049  O   HOH A 644      22.213 -51.310 112.516  1.00 30.77           O  
ANISOU 2049  O   HOH A 644     3711   3810   4170    -25     63   -137       O  
HETATM 2050  O   HOH A 645      -3.511 -70.504 101.565  1.00 31.50           O  
ANISOU 2050  O   HOH A 645     4107   3897   3964   -146   -136   -249       O  
HETATM 2051  O   HOH A 646      -3.036 -69.491 111.433  1.00 39.91           O  
ANISOU 2051  O   HOH A 646     5072   4955   5136   -133    -99   -113       O  
HETATM 2052  O   HOH A 647     -12.288 -44.027  95.706  1.00 28.26           O  
ANISOU 2052  O   HOH A 647     3509   3756   3473     97   -125    170       O  
HETATM 2053  O   HOH A 648     -11.477 -41.601  96.418  1.00 32.76           O  
ANISOU 2053  O   HOH A 648     4076   4284   4088    128    -78    196       O  
HETATM 2054  O   HOH A 649       0.127 -69.479 110.174  1.00 30.55           O  
ANISOU 2054  O   HOH A 649     3920   3747   3942    -99    -79   -150       O  
HETATM 2055  O   HOH A 650       5.105 -47.204 110.597  1.00 37.94           O  
ANISOU 2055  O   HOH A 650     4792   4754   4868      7     59   -127       O  
HETATM 2056  O   HOH A 651     -18.989 -44.326 103.888  1.00 30.55           O  
ANISOU 2056  O   HOH A 651     3608   4044   3955    118    -91    167       O  
HETATM 2057  O   HOH A 652      16.019 -72.910 108.153  1.00 24.08           O  
ANISOU 2057  O   HOH A 652     3097   2809   3244     95     70   -197       O  
HETATM 2058  O   HOH A 653      -0.188 -35.599  96.480  1.00 26.89           O  
ANISOU 2058  O   HOH A 653     3421   3336   3461    125    138    207       O  
HETATM 2059  O   HOH A 654     -11.217 -55.189 107.724  1.00 23.27           O  
ANISOU 2059  O   HOH A 654     2843   3053   2947    -47    -89    -27       O  
HETATM 2060  O   HOH A 655      15.846 -51.840  99.880  1.00 20.84           O  
ANISOU 2060  O   HOH A 655     2639   2599   2679     47    226    -91       O  
HETATM 2061  O   HOH A 656       2.585 -51.380 114.346  1.00 20.56           O  
ANISOU 2061  O   HOH A 656     2587   2599   2625     -3     21   -140       O  
HETATM 2062  O   HOH A 657      -6.491 -71.340  96.986  1.00 39.38           O  
ANISOU 2062  O   HOH A 657     5121   4943   4901   -180   -199   -305       O  
HETATM 2063  O   HOH A 658      -7.315 -65.125 113.114  1.00 32.65           O  
ANISOU 2063  O   HOH A 658     4079   4137   4188   -130    -87    -57       O  
HETATM 2064  O   HOH A 659       4.749 -48.593 108.112  1.00 35.00           O  
ANISOU 2064  O   HOH A 659     4432   4398   4470      9     61   -110       O  
HETATM 2065  O   HOH A 660      18.486 -59.424 108.416  1.00 38.13           O  
ANISOU 2065  O   HOH A 660     4760   4741   4987     49    109   -152       O  
HETATM 2066  O   HOH A 661       5.964 -72.324 107.551  1.00 15.37           O  
ANISOU 2066  O   HOH A 661     2055   1743   2043    -36    -30   -211       O  
HETATM 2067  O   HOH A 662     -10.710 -48.225 119.826  1.00 30.77           O  
ANISOU 2067  O   HOH A 662     3778   4003   3911     73    101    -71       O  
HETATM 2068  O   HOH A 663       6.127 -74.937 104.221  1.00 19.59           O  
ANISOU 2068  O   HOH A 663     2653   2237   2555    -33    -23   -258       O  
HETATM 2069  O   HOH A 664      18.390 -54.418  93.563  1.00 19.90           O  
ANISOU 2069  O   HOH A 664     2579   2532   2450    108    337    -94       O  
HETATM 2070  O   HOH A 665       0.143 -47.454 114.480  1.00 24.60           O  
ANISOU 2070  O   HOH A 665     3091   3104   3151     21     44   -135       O  
HETATM 2071  O   HOH A 666      13.876 -57.425 105.665  1.00 30.64           O  
ANISOU 2071  O   HOH A 666     3880   3816   3945     30    111   -158       O  
HETATM 2072  O   HOH A 667      12.170 -50.432 126.615  1.00 28.32           O  
ANISOU 2072  O   HOH A 667     3552   3629   3578    -37   -103   -241       O  
HETATM 2073  O   HOH A 668     -10.323 -65.451  99.503  1.00 31.18           O  
ANISOU 2073  O   HOH A 668     3981   3997   3868   -171   -243   -182       O  
HETATM 2074  O   HOH A 669       0.721 -71.115 108.740  1.00 20.62           O  
ANISOU 2074  O   HOH A 669     2688   2453   2694   -101    -84   -180       O  
HETATM 2075  O   HOH A 670      -9.130 -63.031  99.859  1.00 15.15           O  
ANISOU 2075  O   HOH A 670     1956   1983   1816   -140   -215   -160       O  
HETATM 2076  O   HOH A 671      12.274 -58.852  95.461  1.00 21.24           O  
ANISOU 2076  O   HOH A 671     2827   2686   2556     75    188   -192       O  
HETATM 2077  O   HOH A 672       4.458 -37.601 107.398  1.00 35.47           O  
ANISOU 2077  O   HOH A 672     4476   4327   4676     43    130    -49       O  
HETATM 2078  O   HOH A 673      15.177 -53.838 127.258  1.00 24.79           O  
ANISOU 2078  O   HOH A 673     3069   3203   3148    -36   -150   -196       O  
HETATM 2079  O   HOH A 674      -5.734 -65.232 110.475  1.00 26.85           O  
ANISOU 2079  O   HOH A 674     3383   3382   3437   -124   -100    -99       O  
HETATM 2080  O   HOH A 675      13.371 -62.872  96.344  1.00 33.67           O  
ANISOU 2080  O   HOH A 675     4401   4221   4170     88    166   -235       O  
HETATM 2081  O   HOH A 676       8.108 -50.485 122.977  1.00 33.02           O  
ANISOU 2081  O   HOH A 676     4161   4199   4185    -18    -33   -212       O  
HETATM 2082  O   HOH A 677      11.616 -42.209 100.142  1.00 43.17           O  
ANISOU 2082  O   HOH A 677     5458   5375   5569     23    212     18       O  
HETATM 2083  O   HOH A 678      10.589 -70.903 106.510  1.00 32.24           O  
ANISOU 2083  O   HOH A 678     4180   3891   4179     26     29   -219       O  
HETATM 2084  O   HOH A 679      19.668 -76.033 121.323  1.00 25.91           O  
ANISOU 2084  O   HOH A 679     3175   3062   3608    130    -84     54       O  
HETATM 2085  O   HOH A 680      13.421 -71.123 106.993  1.00 30.18           O  
ANISOU 2085  O   HOH A 680     3895   3617   3954     60     56   -212       O  
HETATM 2086  O   HOH A 681      14.278 -60.073  97.283  1.00 33.82           O  
ANISOU 2086  O   HOH A 681     4385   4249   4216     82    194   -196       O  
HETATM 2087  O   HOH A 682       5.237 -50.505 123.383  1.00 35.24           O  
ANISOU 2087  O   HOH A 682     4452   4498   4438     -6    -13   -202       O  
HETATM 2088  O   HOH A 683       6.465 -50.175 109.373  1.00 33.10           O  
ANISOU 2088  O   HOH A 683     4186   4153   4237      1     55   -129       O  
HETATM 2089  O   HOH A 684     -10.971 -60.398  86.126  1.00 33.25           O  
ANISOU 2089  O   HOH A 684     4376   4486   3771    -80   -336   -189       O  
HETATM 2090  O   HOH A 685      26.015 -63.466 111.384  1.00 33.30           O  
ANISOU 2090  O   HOH A 685     4006   4101   4545    113    102   -107       O  
HETATM 2091  O   HOH A 686      12.031 -52.870 113.534  1.00 25.88           O  
ANISOU 2091  O   HOH A 686     3232   3228   3374    -12     28   -159       O  
HETATM 2092  O   HOH A 687      22.094 -73.510 127.209  1.00 44.35           O  
ANISOU 2092  O   HOH A 687     5438   5538   5874    127   -194    137       O  
HETATM 2093  O   HOH A 688      -8.580 -58.907 108.486  1.00 22.92           O  
ANISOU 2093  O   HOH A 688     2843   2967   2899    -81    -92    -69       O  
HETATM 2094  O   HOH A 689      17.044 -57.777 101.741  1.00 30.79           O  
ANISOU 2094  O   HOH A 689     3903   3837   3958     67    198   -158       O  
HETATM 2095  O   HOH A 690     -17.891 -60.534  88.160  1.00 39.52           O  
ANISOU 2095  O   HOH A 690     5018   5300   4699   -135   -468   -125       O  
HETATM 2096  O   HOH A 691       4.029 -52.382 118.468  1.00 30.37           O  
ANISOU 2096  O   HOH A 691     3828   3857   3856     -9      5   -158       O  
HETATM 2097  O   HOH A 692      12.932 -57.035 110.426  1.00 39.06           O  
ANISOU 2097  O   HOH A 692     4918   4887   5036      8     52   -154       O  
HETATM 2098  O   HOH A 693     -19.916 -42.746  98.395  1.00 27.41           O  
ANISOU 2098  O   HOH A 693     3217   3697   3502    139   -179    257       O  
HETATM 2099  O   HOH A 694      -1.680 -37.298 109.895  1.00 21.75           O  
ANISOU 2099  O   HOH A 694     2726   2622   2918     96    114    -60       O  
HETATM 2100  O   HOH A 695      17.614 -54.033 111.358  1.00 28.45           O  
ANISOU 2100  O   HOH A 695     3506   3532   3772      1     67   -146       O  
HETATM 2101  O   HOH A 696       4.387 -63.314  88.772  1.00 34.00           O  
ANISOU 2101  O   HOH A 696     4570   4393   3957     19     29   -299       O  
HETATM 2102  O   HOH A 697       5.384 -49.027  88.188  1.00 36.79           O  
ANISOU 2102  O   HOH A 697     4854   4814   4311     89    153     25       O  
HETATM 2103  O   HOH A 698      -8.192 -63.229 107.328  1.00 20.94           O  
ANISOU 2103  O   HOH A 698     2622   2676   2657   -128   -132   -102       O  
HETATM 2104  O   HOH A 699      15.456 -58.185  94.742  1.00 34.81           O  
ANISOU 2104  O   HOH A 699     4516   4406   4304     99    250   -170       O  
HETATM 2105  O   HOH A 700      26.619 -74.602 114.035  1.00 38.95           O  
ANISOU 2105  O   HOH A 700     4758   4683   5358    220     63    -52       O  
HETATM 2106  O   HOH A 701       8.385 -56.063  87.099  1.00 25.60           O  
ANISOU 2106  O   HOH A 701     3498   3385   2844     89    179   -147       O  
HETATM 2107  O   HOH A 702     -16.133 -51.109 103.632  1.00 23.06           O  
ANISOU 2107  O   HOH A 702     2740   3098   2925     -3   -146     65       O  
HETATM 2108  O   HOH A 703       8.506 -49.260 109.387  1.00 34.41           O  
ANISOU 2108  O   HOH A 703     4342   4303   4428     -1     68   -131       O  
HETATM 2109  O   HOH A 704      14.016 -56.199 108.254  1.00 24.77           O  
ANISOU 2109  O   HOH A 704     3109   3073   3229     16     85   -151       O  
HETATM 2110  O   HOH A 705     -17.424 -56.010  99.860  1.00 20.46           O  
ANISOU 2110  O   HOH A 705     2433   2802   2538    -96   -276     24       O  
HETATM 2111  O   HOH A 706     -13.680 -51.228 106.433  1.00 24.98           O  
ANISOU 2111  O   HOH A 706     3015   3299   3178      2    -86     26       O  
HETATM 2112  O   HOH A 707       2.003 -45.012 111.046  1.00 32.54           O  
ANISOU 2112  O   HOH A 707     4104   4070   4188     26     64   -115       O  
HETATM 2113  O   HOH A 708     -15.684 -55.759  87.049  1.00 13.64           O  
ANISOU 2113  O   HOH A 708     1784   2057   1343    -62   -415    -29       O  
HETATM 2114  O   HOH A 709      -0.105 -43.567 112.123  1.00 36.59           O  
ANISOU 2114  O   HOH A 709     4611   4583   4711     44     70   -114       O  
HETATM 2115  O   HOH A 710      23.433 -76.612 104.314  1.00 50.69           O  
ANISOU 2115  O   HOH A 710     6448   6133   6678    225    182   -219       O  
HETATM 2116  O   HOH A 711      -2.176 -48.991 121.209  1.00 21.38           O  
ANISOU 2116  O   HOH A 711     2679   2759   2687     30     52   -158       O  
HETATM 2117  O   HOH A 712      11.648 -58.343  89.198  1.00 29.81           O  
ANISOU 2117  O   HOH A 712     3989   3857   3480     99    221   -191       O  
HETATM 2118  O   HOH A 713       0.854 -36.694 110.502  1.00 23.70           O  
ANISOU 2118  O   HOH A 713     2981   2835   3187     74    120    -87       O  
HETATM 2119  O   HOH A 714      -7.253 -72.054 108.064  1.00 35.40           O  
ANISOU 2119  O   HOH A 714     4500   4365   4585   -205   -166   -143       O  
HETATM 2120  O   HOH A 715       2.610 -47.281 116.579  1.00 43.03           O  
ANISOU 2120  O   HOH A 715     5432   5427   5491     11     39   -168       O  
HETATM 2121  O   HOH A 716      -0.768 -46.373 120.920  1.00 30.94           O  
ANISOU 2121  O   HOH A 716     3902   3935   3920     37     57   -191       O  
CONECT  283  338                                                                
CONECT  338  283                                                                
CONECT 1787 1788 1789 1790                                                      
CONECT 1788 1787                                                                
CONECT 1789 1787                                                                
CONECT 1790 1787                                                                
CONECT 1791 1792 1793 1794                                                      
CONECT 1792 1791                                                                
CONECT 1793 1791                                                                
CONECT 1794 1791                                                                
CONECT 1795 1796 1797 1798                                                      
CONECT 1796 1795                                                                
CONECT 1797 1795                                                                
CONECT 1798 1795                                                                
CONECT 1799 1800 1801 1802                                                      
CONECT 1800 1799                                                                
CONECT 1801 1799                                                                
CONECT 1802 1799                                                                
MASTER      307    0    4   12   13    0    4    6 2117    1   18   19          
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.