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***  MEMBRANE PROTEIN 19-MAY-21 7OL3  ***

elNémo ID: 21072722395841047

Job options:

ID        	=	 21072722395841047
JOBID     	=	 MEMBRANE PROTEIN 19-MAY-21 7OL3
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 0

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER    MEMBRANE PROTEIN                        19-MAY-21   7OL3              
TITLE     HUMAN ATL1 N417INS (CATALYTIC CORE)                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATLASTIN-1;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BRAIN-SPECIFIC GTP-BINDING PROTEIN,GTP-BINDING PROTEIN 3,   
COMPND   5 GBP-3,HGBP3,GUANINE NUCLEOTIDE-BINDING PROTEIN 3,SPASTIC PARAPLEGIA 3
COMPND   6 PROTEIN A;                                                           
COMPND   7 EC: 3.6.5.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ATL1, GBP3, SPG3A;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    DYNAMIN-RELATED PROTEIN, MEMBRANE FUSION, ENDOPLASMIC RETICULUM,      
KEYWDS   2 MEMBRANE PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.KELLY,H.SONDERMANN                                                
REVDAT   1   21-JUL-21 7OL3    0                                                
JRNL        AUTH   C.M.KELLY,P.J.ZEIGER,V.NARAYANAN,K.RAMSEY,H.SONDERMANN       
JRNL        TITL   HUMAN ATL1 N417INS (CATALYTIC CORE)                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19_4080                                     
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 82910                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.410                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 47.4300 -  4.5800    1.00     6148   153  0.1711 0.2126        
REMARK   3     2  4.5800 -  3.6300    1.00     5927   145  0.1280 0.1803        
REMARK   3     3  3.6300 -  3.1800    1.00     5822   145  0.1382 0.1636        
REMARK   3     4  3.1800 -  2.8800    1.00     5788   142  0.1573 0.2144        
REMARK   3     5  2.8800 -  2.6800    1.00     5791   144  0.1608 0.2277        
REMARK   3     6  2.6800 -  2.5200    1.00     5795   143  0.1651 0.2222        
REMARK   3     7  2.5200 -  2.3900    1.00     5753   142  0.1758 0.2256        
REMARK   3     8  2.3900 -  2.2900    1.00     5761   142  0.1982 0.2345        
REMARK   3     9  2.2900 -  2.2000    1.00     5721   142  0.2012 0.2587        
REMARK   3    10  2.2000 -  2.1300    1.00     5713   141  0.2053 0.2747        
REMARK   3    11  2.1300 -  2.0600    1.00     5728   142  0.2173 0.2674        
REMARK   3    12  2.0600 -  2.0000    1.00     5760   141  0.2345 0.2641        
REMARK   3    13  2.0000 -  1.9500    1.00     5661   140  0.2625 0.2679        
REMARK   3    14  1.9500 -  1.9000    0.97     5542   138  0.3186 0.3545        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.216           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.65                          
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      :  0.007           7066                                  
REMARK   3   ANGLE     :  0.864           9561                                  
REMARK   3   CHIRALITY :  0.052           1037                                  
REMARK   3   PLANARITY :  0.007           1229                                  
REMARK   3   DIHEDRAL  : 14.782           2655                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 7OL3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292115930.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96860                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82941                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.7900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4IDQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.1, 2% TACSIMATE PH   
REMARK 280  8, 18% PEG 3,350, 25% GLYCEROL (CRYO-PROTECTION), VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       24.54500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.00400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.50150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.00400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.54500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.50150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     TRP A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     PHE A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     LYS A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     TYR A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     TRP A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     VAL A    29                                                      
REMARK 465     GLU A   452                                                      
REMARK 465     HIS A   453                                                      
REMARK 465     HIS A   454                                                      
REMARK 465     HIS A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     HIS A   457                                                      
REMARK 465     HIS A   458                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ASN B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     TRP B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     PHE B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     THR B    18                                                      
REMARK 465     TYR B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     TRP B    21                                                      
REMARK 465     SER B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     VAL B    29                                                      
REMARK 465     HIS B   455                                                      
REMARK 465     HIS B   456                                                      
REMARK 465     HIS B   457                                                      
REMARK 465     HIS B   458                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A 451    CG   CD1  CD2                                       
REMARK 470     ARG B 416    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   769     O    HOH B   952              1.97            
REMARK 500   O3B  GDP B   501    AL    ALF B   502              2.00            
REMARK 500   O3B  GDP A   501    AL    ALF A   502              2.02            
REMARK 500   O    HOH A   761     O    HOH B   871              2.04            
REMARK 500   O    HOH A   627     O    HOH A   632              2.05            
REMARK 500   O    HOH A   851     O    HOH A  1007              2.07            
REMARK 500   O    HOH B   838     O    HOH B  1004              2.08            
REMARK 500   O    HOH B   602     O    HOH B   620              2.08            
REMARK 500  AL    ALF B   502     O    HOH B   693              2.10            
REMARK 500   O    HOH B   811     O    HOH B   979              2.13            
REMARK 500   O    HOH B   969     O    HOH B   993              2.13            
REMARK 500   OG   SER B   346     O    HOH B   601              2.14            
REMARK 500  AL    ALF A   502     O    HOH A   618              2.14            
REMARK 500   O    HOH A   610     O    HOH A   876              2.14            
REMARK 500   O    HOH A   909     O    HOH A   981              2.15            
REMARK 500   O    HOH A   759     O    HOH B   675              2.17            
REMARK 500   O    HOH A   698     O    HOH B  1038              2.17            
REMARK 500   O    HOH B   962     O    HOH B   973              2.17            
REMARK 500   O    GLY A   137     O    HOH A   601              2.17            
REMARK 500   O    HOH A   946     O    HOH A  1084              2.17            
REMARK 500   O    HOH A   670     O    HOH A   808              2.17            
REMARK 500   O    HOH A   951     O    HOH A  1017              2.18            
REMARK 500   O    HOH B   613     O    HOH B   642              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   688     O    HOH B   642     3454     2.10            
REMARK 500   O    HOH A   658     O    HOH B   950     3454     2.14            
REMARK 500   O    HOH B   946     O    HOH B   987     4455     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  98       37.71    -98.98                                   
REMARK 500    GLU A 119      -70.52   -112.42                                   
REMARK 500    GLN A 180      -41.73     74.13                                   
REMARK 500    GLN A 210     -100.58   -111.45                                   
REMARK 500    CYS A 375       27.81   -141.09                                   
REMARK 500    ARG B  77       31.87     70.19                                   
REMARK 500    ASP B  98       75.94   -116.38                                   
REMARK 500    GLN B 180      -37.44     72.20                                   
REMARK 500    GLN B 210      -90.43   -102.30                                   
REMARK 500    ASN B 441       72.26   -159.55                                   
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 A1091        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A1092        DISTANCE =  6.08 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  81   OG                                                     
REMARK 620 2 THR A 120   OG1  85.8                                              
REMARK 620 3 GDP A 501   O1B  95.3 169.6                                        
REMARK 620 4 HOH A 685   O    83.6  97.7  92.6                                  
REMARK 620 5 HOH A 741   O    83.8  87.7  82.2 165.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  81   OG                                                     
REMARK 620 2 THR B 120   OG1  87.0                                              
REMARK 620 3 GDP B 501   O2B  96.1 173.1                                        
REMARK 620 4 HOH B 690   O    87.0  92.3  94.0                                  
REMARK 620 5 HOH B 719   O    85.0  90.6  83.6 171.3                            
REMARK 620 N                    1     2     3     4                             
DBREF  7OL3 A    1   450  UNP    Q8WXF7   ATLA1_HUMAN      1    449             
DBREF  7OL3 B    1   450  UNP    Q8WXF7   ATLA1_HUMAN      1    449             
SEQADV 7OL3 ASN A  417  UNP  Q8WXF7              INSERTION                      
SEQADV 7OL3 ALA A  448  UNP  Q8WXF7    THR   447 CONFLICT                       
SEQADV 7OL3 ALA A  449  UNP  Q8WXF7    PRO   448 CONFLICT                       
SEQADV 7OL3 LEU A  451  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 GLU A  452  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS A  453  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS A  454  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS A  455  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS A  456  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS A  457  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS A  458  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 ASN B  417  UNP  Q8WXF7              INSERTION                      
SEQADV 7OL3 ALA B  448  UNP  Q8WXF7    THR   447 CONFLICT                       
SEQADV 7OL3 ALA B  449  UNP  Q8WXF7    PRO   448 CONFLICT                       
SEQADV 7OL3 LEU B  451  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 GLU B  452  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS B  453  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS B  454  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS B  455  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS B  456  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS B  457  UNP  Q8WXF7              EXPRESSION TAG                 
SEQADV 7OL3 HIS B  458  UNP  Q8WXF7              EXPRESSION TAG                 
SEQRES   1 A  458  MET ALA LYS ASN ARG ARG ASP ARG ASN SER TRP GLY GLY          
SEQRES   2 A  458  PHE SER GLU LYS THR TYR GLU TRP SER SER GLU GLU GLU          
SEQRES   3 A  458  GLU PRO VAL LYS LYS ALA GLY PRO VAL GLN VAL LEU ILE          
SEQRES   4 A  458  VAL LYS ASP ASP HIS SER PHE GLU LEU ASP GLU THR ALA          
SEQRES   5 A  458  LEU ASN ARG ILE LEU LEU SER GLU ALA VAL ARG ASP LYS          
SEQRES   6 A  458  GLU VAL VAL ALA VAL SER VAL ALA GLY ALA PHE ARG LYS          
SEQRES   7 A  458  GLY LYS SER PHE LEU MET ASP PHE MET LEU ARG TYR MET          
SEQRES   8 A  458  TYR ASN GLN GLU SER VAL ASP TRP VAL GLY ASP TYR ASN          
SEQRES   9 A  458  GLU PRO LEU THR GLY PHE SER TRP ARG GLY GLY SER GLU          
SEQRES  10 A  458  ARG GLU THR THR GLY ILE GLN ILE TRP SER GLU ILE PHE          
SEQRES  11 A  458  LEU ILE ASN LYS PRO ASP GLY LYS LYS VAL ALA VAL LEU          
SEQRES  12 A  458  LEU MET ASP THR GLN GLY THR PHE ASP SER GLN SER THR          
SEQRES  13 A  458  LEU ARG ASP SER ALA THR VAL PHE ALA LEU SER THR MET          
SEQRES  14 A  458  ILE SER SER ILE GLN VAL TYR ASN LEU SER GLN ASN VAL          
SEQRES  15 A  458  GLN GLU ASP ASP LEU GLN HIS LEU GLN LEU PHE THR GLU          
SEQRES  16 A  458  TYR GLY ARG LEU ALA MET GLU GLU THR PHE LEU LYS PRO          
SEQRES  17 A  458  PHE GLN SER LEU ILE PHE LEU VAL ARG ASP TRP SER PHE          
SEQRES  18 A  458  PRO TYR GLU PHE SER TYR GLY ALA ASP GLY GLY ALA LYS          
SEQRES  19 A  458  PHE LEU GLU LYS ARG LEU LYS VAL SER GLY ASN GLN HIS          
SEQRES  20 A  458  GLU GLU LEU GLN ASN VAL ARG LYS HIS ILE HIS SER CYS          
SEQRES  21 A  458  PHE THR ASN ILE SER CYS PHE LEU LEU PRO HIS PRO GLY          
SEQRES  22 A  458  LEU LYS VAL ALA THR ASN PRO ASN PHE ASP GLY LYS LEU          
SEQRES  23 A  458  LYS GLU ILE ASP ASP GLU PHE ILE LYS ASN LEU LYS ILE          
SEQRES  24 A  458  LEU ILE PRO TRP LEU LEU SER PRO GLU SER LEU ASP ILE          
SEQRES  25 A  458  LYS GLU ILE ASN GLY ASN LYS ILE THR CYS ARG GLY LEU          
SEQRES  26 A  458  VAL GLU TYR PHE LYS ALA TYR ILE LYS ILE TYR GLN GLY          
SEQRES  27 A  458  GLU GLU LEU PRO HIS PRO LYS SER MET LEU GLN ALA THR          
SEQRES  28 A  458  ALA GLU ALA ASN ASN LEU ALA ALA VAL ALA THR ALA LYS          
SEQRES  29 A  458  ASP THR TYR ASN LYS LYS MET GLU GLU ILE CYS GLY GLY          
SEQRES  30 A  458  ASP LYS PRO PHE LEU ALA PRO ASN ASP LEU GLN THR LYS          
SEQRES  31 A  458  HIS LEU GLN LEU LYS GLU GLU SER VAL LYS LEU PHE ARG          
SEQRES  32 A  458  GLY VAL LYS LYS MET GLY GLY GLU GLU PHE SER ARG ARG          
SEQRES  33 A  458  ASN TYR LEU GLN GLN LEU GLU SER GLU ILE ASP GLU LEU          
SEQRES  34 A  458  TYR ILE GLN TYR ILE LYS HIS ASN ASP SER LYS ASN ILE          
SEQRES  35 A  458  PHE HIS ALA ALA ARG ALA ALA ALA LEU GLU HIS HIS HIS          
SEQRES  36 A  458  HIS HIS HIS                                                  
SEQRES   1 B  458  MET ALA LYS ASN ARG ARG ASP ARG ASN SER TRP GLY GLY          
SEQRES   2 B  458  PHE SER GLU LYS THR TYR GLU TRP SER SER GLU GLU GLU          
SEQRES   3 B  458  GLU PRO VAL LYS LYS ALA GLY PRO VAL GLN VAL LEU ILE          
SEQRES   4 B  458  VAL LYS ASP ASP HIS SER PHE GLU LEU ASP GLU THR ALA          
SEQRES   5 B  458  LEU ASN ARG ILE LEU LEU SER GLU ALA VAL ARG ASP LYS          
SEQRES   6 B  458  GLU VAL VAL ALA VAL SER VAL ALA GLY ALA PHE ARG LYS          
SEQRES   7 B  458  GLY LYS SER PHE LEU MET ASP PHE MET LEU ARG TYR MET          
SEQRES   8 B  458  TYR ASN GLN GLU SER VAL ASP TRP VAL GLY ASP TYR ASN          
SEQRES   9 B  458  GLU PRO LEU THR GLY PHE SER TRP ARG GLY GLY SER GLU          
SEQRES  10 B  458  ARG GLU THR THR GLY ILE GLN ILE TRP SER GLU ILE PHE          
SEQRES  11 B  458  LEU ILE ASN LYS PRO ASP GLY LYS LYS VAL ALA VAL LEU          
SEQRES  12 B  458  LEU MET ASP THR GLN GLY THR PHE ASP SER GLN SER THR          
SEQRES  13 B  458  LEU ARG ASP SER ALA THR VAL PHE ALA LEU SER THR MET          
SEQRES  14 B  458  ILE SER SER ILE GLN VAL TYR ASN LEU SER GLN ASN VAL          
SEQRES  15 B  458  GLN GLU ASP ASP LEU GLN HIS LEU GLN LEU PHE THR GLU          
SEQRES  16 B  458  TYR GLY ARG LEU ALA MET GLU GLU THR PHE LEU LYS PRO          
SEQRES  17 B  458  PHE GLN SER LEU ILE PHE LEU VAL ARG ASP TRP SER PHE          
SEQRES  18 B  458  PRO TYR GLU PHE SER TYR GLY ALA ASP GLY GLY ALA LYS          
SEQRES  19 B  458  PHE LEU GLU LYS ARG LEU LYS VAL SER GLY ASN GLN HIS          
SEQRES  20 B  458  GLU GLU LEU GLN ASN VAL ARG LYS HIS ILE HIS SER CYS          
SEQRES  21 B  458  PHE THR ASN ILE SER CYS PHE LEU LEU PRO HIS PRO GLY          
SEQRES  22 B  458  LEU LYS VAL ALA THR ASN PRO ASN PHE ASP GLY LYS LEU          
SEQRES  23 B  458  LYS GLU ILE ASP ASP GLU PHE ILE LYS ASN LEU LYS ILE          
SEQRES  24 B  458  LEU ILE PRO TRP LEU LEU SER PRO GLU SER LEU ASP ILE          
SEQRES  25 B  458  LYS GLU ILE ASN GLY ASN LYS ILE THR CYS ARG GLY LEU          
SEQRES  26 B  458  VAL GLU TYR PHE LYS ALA TYR ILE LYS ILE TYR GLN GLY          
SEQRES  27 B  458  GLU GLU LEU PRO HIS PRO LYS SER MET LEU GLN ALA THR          
SEQRES  28 B  458  ALA GLU ALA ASN ASN LEU ALA ALA VAL ALA THR ALA LYS          
SEQRES  29 B  458  ASP THR TYR ASN LYS LYS MET GLU GLU ILE CYS GLY GLY          
SEQRES  30 B  458  ASP LYS PRO PHE LEU ALA PRO ASN ASP LEU GLN THR LYS          
SEQRES  31 B  458  HIS LEU GLN LEU LYS GLU GLU SER VAL LYS LEU PHE ARG          
SEQRES  32 B  458  GLY VAL LYS LYS MET GLY GLY GLU GLU PHE SER ARG ARG          
SEQRES  33 B  458  ASN TYR LEU GLN GLN LEU GLU SER GLU ILE ASP GLU LEU          
SEQRES  34 B  458  TYR ILE GLN TYR ILE LYS HIS ASN ASP SER LYS ASN ILE          
SEQRES  35 B  458  PHE HIS ALA ALA ARG ALA ALA ALA LEU GLU HIS HIS HIS          
SEQRES  36 B  458  HIS HIS HIS                                                  
HET    GDP  A 501      28                                                       
HET    ALF  A 502       5                                                       
HET     MG  A 503       1                                                       
HET    GDP  B 501      28                                                       
HET    ALF  B 502       5                                                       
HET     MG  B 503       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   4  ALF    2(AL F4 1-)                                                  
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   9  HOH   *946(H2 O)                                                    
HELIX    1 AA1 ASP A   49  LEU A   58  1                                  10    
HELIX    2 AA2 GLY A   79  GLN A   94  1                                  16    
HELIX    3 AA3 THR A  156  SER A  171  1                                  16    
HELIX    4 AA4 GLN A  183  MET A  201  1                                  19    
HELIX    5 AA5 GLY A  228  LYS A  241  1                                  14    
HELIX    6 AA6 HIS A  247  CYS A  260  1                                  14    
HELIX    7 AA7 GLY A  273  ASN A  279  1                                   7    
HELIX    8 AA8 LYS A  285  ILE A  289  5                                   5    
HELIX    9 AA9 ASP A  290  SER A  306  1                                  17    
HELIX   10 AB1 PRO A  307  LEU A  310  5                                   4    
HELIX   11 AB2 THR A  321  GLY A  338  1                                  18    
HELIX   12 AB3 SER A  346  GLY A  376  1                                  31    
HELIX   13 AB4 ALA A  383  VAL A  405  1                                  23    
HELIX   14 AB5 GLY A  409  TYR A  418  1                                  10    
HELIX   15 AB6 TYR A  418  SER A  439  1                                  22    
HELIX   16 AB7 HIS A  444  LEU A  451  1                                   8    
HELIX   17 AB8 ASP B   49  LEU B   58  1                                  10    
HELIX   18 AB9 GLY B   79  GLN B   94  1                                  16    
HELIX   19 AC1 THR B  156  SER B  171  1                                  16    
HELIX   20 AC2 GLN B  183  LEU B  199  1                                  17    
HELIX   21 AC3 GLY B  228  LYS B  241  1                                  14    
HELIX   22 AC4 HIS B  247  CYS B  260  1                                  14    
HELIX   23 AC5 GLY B  273  ASN B  279  1                                   7    
HELIX   24 AC6 LYS B  285  ILE B  289  5                                   5    
HELIX   25 AC7 ASP B  290  SER B  306  1                                  17    
HELIX   26 AC8 PRO B  307  LEU B  310  5                                   4    
HELIX   27 AC9 THR B  321  GLY B  338  1                                  18    
HELIX   28 AD1 SER B  346  GLY B  376  1                                  31    
HELIX   29 AD2 ALA B  383  VAL B  405  1                                  23    
HELIX   30 AD3 GLY B  409  TYR B  418  1                                  10    
HELIX   31 AD4 TYR B  418  LYS B  440  1                                  23    
HELIX   32 AD5 PHE B  443  HIS B  454  1                                  12    
SHEET    1 AA1 5 PHE A  46  LEU A  48  0                                        
SHEET    2 AA1 5 PRO A  34  VAL A  40 -1  N  ILE A  39   O  GLU A  47           
SHEET    3 AA1 5 ILE A 123  TRP A 126 -1  O  ILE A 125   N  VAL A  35           
SHEET    4 AA1 5 LYS A 139  THR A 147 -1  O  ASP A 146   N  GLN A 124           
SHEET    5 AA1 5 PHE A 130  ASN A 133 -1  N  ILE A 132   O  VAL A 140           
SHEET    1 AA2 8 PHE A  46  LEU A  48  0                                        
SHEET    2 AA2 8 PRO A  34  VAL A  40 -1  N  ILE A  39   O  GLU A  47           
SHEET    3 AA2 8 ILE A 123  TRP A 126 -1  O  ILE A 125   N  VAL A  35           
SHEET    4 AA2 8 LYS A 139  THR A 147 -1  O  ASP A 146   N  GLN A 124           
SHEET    5 AA2 8 VAL A  67  GLY A  74  1  N  VAL A  68   O  ALA A 141           
SHEET    6 AA2 8 ILE A 173  SER A 179  1  O  ASN A 177   N  ALA A  73           
SHEET    7 AA2 8 PHE A 209  TRP A 219  1  O  ARG A 217   N  LEU A 178           
SHEET    8 AA2 8 PHE A 261  PRO A 270  1  O  SER A 265   N  PHE A 214           
SHEET    1 AA3 2 GLU A 314  ILE A 315  0                                        
SHEET    2 AA3 2 ASN A 318  LYS A 319 -1  O  ASN A 318   N  ILE A 315           
SHEET    1 AA4 5 PHE B  46  LEU B  48  0                                        
SHEET    2 AA4 5 PRO B  34  VAL B  40 -1  N  ILE B  39   O  GLU B  47           
SHEET    3 AA4 5 ILE B 123  TRP B 126 -1  O  ILE B 125   N  VAL B  35           
SHEET    4 AA4 5 LYS B 139  THR B 147 -1  O  ASP B 146   N  GLN B 124           
SHEET    5 AA4 5 PHE B 130  ASN B 133 -1  N  ILE B 132   O  VAL B 140           
SHEET    1 AA5 8 PHE B  46  LEU B  48  0                                        
SHEET    2 AA5 8 PRO B  34  VAL B  40 -1  N  ILE B  39   O  GLU B  47           
SHEET    3 AA5 8 ILE B 123  TRP B 126 -1  O  ILE B 125   N  VAL B  35           
SHEET    4 AA5 8 LYS B 139  THR B 147 -1  O  ASP B 146   N  GLN B 124           
SHEET    5 AA5 8 VAL B  67  GLY B  74  1  N  VAL B  68   O  ALA B 141           
SHEET    6 AA5 8 ILE B 173  SER B 179  1  O  ASN B 177   N  ALA B  73           
SHEET    7 AA5 8 PHE B 209  ARG B 217  1  O  ARG B 217   N  LEU B 178           
SHEET    8 AA5 8 PHE B 261  LEU B 268  1  O  SER B 265   N  PHE B 214           
SHEET    1 AA6 2 GLU B 314  ILE B 315  0                                        
SHEET    2 AA6 2 ASN B 318  LYS B 319 -1  O  ASN B 318   N  ILE B 315           
LINK         OG  SER A  81                MG    MG A 503     1555   1555  2.12  
LINK         OG1 THR A 120                MG    MG A 503     1555   1555  2.06  
LINK         O1B GDP A 501                MG    MG A 503     1555   1555  1.98  
LINK        MG    MG A 503                 O   HOH A 685     1555   1555  2.10  
LINK        MG    MG A 503                 O   HOH A 741     1555   1555  2.15  
LINK         OG  SER B  81                MG    MG B 503     1555   1555  1.98  
LINK         OG1 THR B 120                MG    MG B 503     1555   1555  2.14  
LINK         O2B GDP B 501                MG    MG B 503     1555   1555  2.00  
LINK        MG    MG B 503                 O   HOH B 690     1555   1555  2.11  
LINK        MG    MG B 503                 O   HOH B 719     1555   1555  2.16  
CRYST1   49.090  115.003  184.008  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020371  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008695  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005435        0.00000                         
ATOM      1  N   LYS A  30     -15.087   7.717 -75.633  1.00 66.30           N  
ANISOU    1  N   LYS A  30     8900   8550   7740   -682    787    -72       N  
ATOM      2  CA  LYS A  30     -15.004   8.831 -74.690  1.00 77.43           C  
ANISOU    2  CA  LYS A  30    10299   9977   9142   -684    772    -42       C  
ATOM      3  C   LYS A  30     -16.166   8.793 -73.692  1.00 69.14           C  
ANISOU    3  C   LYS A  30     9268   8917   8085   -644    698     36       C  
ATOM      4  O   LYS A  30     -17.006   9.695 -73.664  1.00 65.11           O  
ANISOU    4  O   LYS A  30     8815   8406   7519   -664    687     89       O  
ATOM      5  CB  LYS A  30     -14.996  10.164 -75.444  1.00 79.14           C  
ANISOU    5  CB  LYS A  30    10570  10204   9295   -747    825    -43       C  
ATOM      6  CG  LYS A  30     -13.829  10.336 -76.397  1.00 83.19           C  
ANISOU    6  CG  LYS A  30    11066  10729   9812   -789    901   -120       C  
ATOM      7  CD  LYS A  30     -14.128  11.416 -77.427  1.00 91.23           C  
ANISOU    7  CD  LYS A  30    12157  11750  10758   -852    950   -115       C  
ATOM      8  CE  LYS A  30     -12.858  12.120 -77.889  1.00 95.38           C  
ANISOU    8  CE  LYS A  30    12656  12296  11287   -895   1020   -179       C  
ATOM      9  NZ  LYS A  30     -11.840  11.169 -78.413  1.00 92.46           N  
ANISOU    9  NZ  LYS A  30    12237  11928  10967   -890   1055   -252       N  
ATOM     10  N   LYS A  31     -16.205   7.753 -72.862  1.00 52.97           N  
ANISOU   10  N   LYS A  31     7172   6862   6093   -588    647     44       N  
ATOM     11  CA  LYS A  31     -17.385   7.465 -72.061  1.00 47.77           C  
ANISOU   11  CA  LYS A  31     6533   6189   5428   -547    575    117       C  
ATOM     12  C   LYS A  31     -17.316   8.181 -70.718  1.00 39.96           C  
ANISOU   12  C   LYS A  31     5513   5214   4455   -524    538    150       C  
ATOM     13  O   LYS A  31     -16.278   8.164 -70.048  1.00 40.94           O  
ANISOU   13  O   LYS A  31     5569   5355   4632   -508    543    113       O  
ATOM     14  CB  LYS A  31     -17.539   5.956 -71.859  1.00 45.78           C  
ANISOU   14  CB  LYS A  31     6248   5919   5226   -496    536    111       C  
ATOM     15  CG  LYS A  31     -18.811   5.557 -71.124  1.00 50.60           C  
ANISOU   15  CG  LYS A  31     6882   6513   5829   -454    463    185       C  
ATOM     16  CD  LYS A  31     -19.240   4.136 -71.474  1.00 53.54           C  
ANISOU   16  CD  LYS A  31     7254   6864   6225   -422    438    183       C  
ATOM     17  CE  LYS A  31     -20.363   3.644 -70.563  1.00 55.20           C  
ANISOU   17  CE  LYS A  31     7474   7059   6441   -373    361    252       C  
ATOM     18  NZ  LYS A  31     -19.857   3.182 -69.233  1.00 57.29           N  
ANISOU   18  NZ  LYS A  31     7663   7331   6774   -320    318    251       N  
ATOM     19  N   ALA A  32     -18.424   8.821 -70.346  1.00 30.94           N  
ANISOU   19  N   ALA A  32     4422   4067   3267   -524    501    221       N  
ATOM     20  CA  ALA A  32     -18.561   9.427 -69.031  1.00 30.18           C  
ANISOU   20  CA  ALA A  32     4303   3982   3183   -499    457    263       C  
ATOM     21  C   ALA A  32     -18.363   8.385 -67.935  1.00 29.61           C  
ANISOU   21  C   ALA A  32     4163   3906   3182   -435    403    265       C  
ATOM     22  O   ALA A  32     -18.656   7.198 -68.107  1.00 25.93           O  
ANISOU   22  O   ALA A  32     3689   3422   2740   -405    381    262       O  
ATOM     23  CB  ALA A  32     -19.942  10.074 -68.890  1.00 23.84           C  
ANISOU   23  CB  ALA A  32     3570   3169   2318   -504    421    342       C  
ATOM     24  N   GLY A  33     -17.850   8.834 -66.796  1.00 23.22           N  
ANISOU   24  N   GLY A  33     3303   3113   2406   -413    383    269       N  
ATOM     25  CA  GLY A  33     -17.634   7.934 -65.693  1.00 21.79           C  
ANISOU   25  CA  GLY A  33     3058   2931   2292   -353    331    272       C  
ATOM     26  C   GLY A  33     -17.400   8.681 -64.407  1.00 19.75           C  
ANISOU   26  C   GLY A  33     2763   2689   2052   -334    302    297       C  
ATOM     27  O   GLY A  33     -17.301   9.912 -64.387  1.00 19.52           O  
ANISOU   27  O   GLY A  33     2757   2674   1987   -369    325    306       O  
ATOM     28  N   PRO A  34     -17.325   7.953 -63.298  1.00 18.73           N  
ANISOU   28  N   PRO A  34     2579   2557   1979   -278    249    309       N  
ATOM     29  CA  PRO A  34     -17.056   8.611 -62.016  1.00 18.15           C  
ANISOU   29  CA  PRO A  34     2468   2501   1929   -256    219    331       C  
ATOM     30  C   PRO A  34     -15.596   9.013 -61.925  1.00 20.49           C  
ANISOU   30  C   PRO A  34     2705   2820   2262   -273    266    264       C  
ATOM     31  O   PRO A  34     -14.709   8.312 -62.417  1.00 19.95           O  
ANISOU   31  O   PRO A  34     2597   2753   2231   -274    299    201       O  
ATOM     32  CB  PRO A  34     -17.424   7.542 -60.981  1.00 20.10           C  
ANISOU   32  CB  PRO A  34     2674   2736   2226   -190    150    359       C  
ATOM     33  CG  PRO A  34     -17.273   6.255 -61.687  1.00 22.69           C  
ANISOU   33  CG  PRO A  34     2991   3049   2582   -177    160    321       C  
ATOM     34  CD  PRO A  34     -17.551   6.504 -63.147  1.00 20.54           C  
ANISOU   34  CD  PRO A  34     2782   2769   2252   -230    212    307       C  
ATOM     35  N   VAL A  35     -15.348  10.157 -61.291  1.00 19.49           N  
ANISOU   35  N   VAL A  35     2572   2712   2123   -286    269    279       N  
ATOM     36  CA  VAL A  35     -14.000  10.681 -61.136  1.00 19.34           C  
ANISOU   36  CA  VAL A  35     2499   2716   2135   -304    312    221       C  
ATOM     37  C   VAL A  35     -13.775  10.999 -59.665  1.00 19.05           C  
ANISOU   37  C   VAL A  35     2412   2692   2136   -266    267    245       C  
ATOM     38  O   VAL A  35     -14.533  11.772 -59.067  1.00 17.62           O  
ANISOU   38  O   VAL A  35     2262   2511   1921   -264    235    305       O  
ATOM     39  CB  VAL A  35     -13.760  11.923 -62.007  1.00 21.20           C  
ANISOU   39  CB  VAL A  35     2778   2963   2314   -369    374    204       C  
ATOM     40  CG1 VAL A  35     -12.395  12.518 -61.719  1.00 21.66           C  
ANISOU   40  CG1 VAL A  35     2779   3046   2405   -385    414    149       C  
ATOM     41  CG2 VAL A  35     -13.883  11.555 -63.477  1.00 25.02           C  
ANISOU   41  CG2 VAL A  35     3307   3435   2766   -406    421    175       C  
ATOM     42  N   GLN A  36     -12.743  10.394 -59.086  1.00 18.80           N  
ANISOU   42  N   GLN A  36     2303   2669   2173   -235    265    199       N  
ATOM     43  CA  GLN A  36     -12.336  10.657 -57.712  1.00 18.04           C  
ANISOU   43  CA  GLN A  36     2150   2587   2119   -199    228    211       C  
ATOM     44  C   GLN A  36     -11.695  12.040 -57.642  1.00 19.54           C  
ANISOU   44  C   GLN A  36     2338   2799   2287   -240    268    196       C  
ATOM     45  O   GLN A  36     -10.637  12.260 -58.225  1.00 23.11           O  
ANISOU   45  O   GLN A  36     2766   3265   2751   -272    326    133       O  
ATOM     46  CB  GLN A  36     -11.353   9.576 -57.262  1.00 21.01           C  
ANISOU   46  CB  GLN A  36     2444   2965   2574   -159    221    159       C  
ATOM     47  CG  GLN A  36     -11.112   9.544 -55.758  1.00 20.12           C  
ANISOU   47  CG  GLN A  36     2272   2862   2511   -109    169    178       C  
ATOM     48  CD  GLN A  36     -12.300   8.977 -55.020  1.00 20.74           C  
ANISOU   48  CD  GLN A  36     2369   2922   2589    -62     96    248       C  
ATOM     49  OE1 GLN A  36     -12.872   7.969 -55.435  1.00 18.40           O  
ANISOU   49  OE1 GLN A  36     2089   2606   2295    -44     78    256       O  
ATOM     50  NE2 GLN A  36     -12.701   9.636 -53.942  1.00 16.65           N  
ANISOU   50  NE2 GLN A  36     1849   2411   2067    -43     54    298       N  
ATOM     51  N   VAL A  37     -12.310  12.993 -56.950  1.00 17.41           N  
ANISOU   51  N   VAL A  37     2095   2535   1986   -241    239    253       N  
ATOM     52  CA  VAL A  37     -11.753  14.331 -56.855  1.00 20.24           C  
ANISOU   52  CA  VAL A  37     2454   2914   2321   -280    275    242       C  
ATOM     53  C   VAL A  37     -11.233  14.630 -55.454  1.00 21.31           C  
ANISOU   53  C   VAL A  37     2529   3066   2503   -245    241    249       C  
ATOM     54  O   VAL A  37     -10.146  15.195 -55.308  1.00 18.24           O  
ANISOU   54  O   VAL A  37     2098   2697   2135   -262    277    204       O  
ATOM     55  CB  VAL A  37     -12.756  15.406 -57.332  1.00 18.20           C  
ANISOU   55  CB  VAL A  37     2280   2653   1982   -321    282    294       C  
ATOM     56  CG1 VAL A  37     -13.076  15.192 -58.814  1.00 22.48           C  
ANISOU   56  CG1 VAL A  37     2879   3182   2480   -362    326    276       C  
ATOM     57  CG2 VAL A  37     -14.012  15.407 -56.507  1.00 21.50           C  
ANISOU   57  CG2 VAL A  37     2728   3060   2382   -286    213    375       C  
ATOM     58  N   LEU A  38     -11.965  14.235 -54.414  1.00 17.67           N  
ANISOU   58  N   LEU A  38     2059   2596   2058   -195    172    304       N  
ATOM     59  CA  LEU A  38     -11.446  14.256 -53.050  1.00 18.37           C  
ANISOU   59  CA  LEU A  38     2082   2698   2201   -153    135    307       C  
ATOM     60  C   LEU A  38     -10.962  12.853 -52.721  1.00 19.74           C  
ANISOU   60  C   LEU A  38     2193   2864   2444   -104    112    274       C  
ATOM     61  O   LEU A  38     -11.755  11.910 -52.628  1.00 15.24           O  
ANISOU   61  O   LEU A  38     1635   2274   1881    -70     69    305       O  
ATOM     62  CB  LEU A  38     -12.480  14.725 -52.029  1.00 18.83           C  
ANISOU   62  CB  LEU A  38     2165   2753   2238   -127     73    386       C  
ATOM     63  CG  LEU A  38     -11.934  14.741 -50.582  1.00 16.62           C  
ANISOU   63  CG  LEU A  38     1815   2486   2014    -82     33    390       C  
ATOM     64  CD1 LEU A  38     -10.806  15.760 -50.416  1.00 21.23           C  
ANISOU   64  CD1 LEU A  38     2365   3095   2607   -112     76    349       C  
ATOM     65  CD2 LEU A  38     -13.044  15.007 -49.567  1.00 17.49           C  
ANISOU   65  CD2 LEU A  38     1949   2589   2107    -49    -35    471       C  
ATOM     66  N   ILE A  39      -9.659  12.725 -52.561  1.00 18.94           N  
ANISOU   66  N   ILE A  39     2025   2778   2394   -102    142    210       N  
ATOM     67  CA  ILE A  39      -9.006  11.466 -52.262  1.00 20.37           C  
ANISOU   67  CA  ILE A  39     2140   2955   2645    -60    128    169       C  
ATOM     68  C   ILE A  39      -8.733  11.433 -50.770  1.00 20.82           C  
ANISOU   68  C   ILE A  39     2137   3021   2752    -10     77    187       C  
ATOM     69  O   ILE A  39      -8.159  12.380 -50.221  1.00 18.16           O  
ANISOU   69  O   ILE A  39     1778   2704   2418    -22     89    180       O  
ATOM     70  CB  ILE A  39      -7.695  11.341 -53.058  1.00 23.73           C  
ANISOU   70  CB  ILE A  39     2528   3392   3096    -90    195     84       C  
ATOM     71  CG1 ILE A  39      -7.987  11.265 -54.560  1.00 22.50           C  
ANISOU   71  CG1 ILE A  39     2431   3225   2892   -136    244     66       C  
ATOM     72  CG2 ILE A  39      -6.874  10.185 -52.536  1.00 23.09           C  
ANISOU   72  CG2 ILE A  39     2369   3311   3092    -43    179     41       C  
ATOM     73  CD1 ILE A  39      -6.805  11.644 -55.420  1.00 27.59           C  
ANISOU   73  CD1 ILE A  39     3058   3886   3540   -182    319     -8       C  
ATOM     74  N   VAL A  40      -9.141  10.360 -50.101  1.00 23.23           N  
ANISOU   74  N   VAL A  40     2418   3313   3097     45     21    209       N  
ATOM     75  CA  VAL A  40      -8.802  10.172 -48.693  1.00 21.73           C  
ANISOU   75  CA  VAL A  40     2164   3130   2961     96    -27    220       C  
ATOM     76  C   VAL A  40      -7.766   9.061 -48.625  1.00 27.87           C  
ANISOU   76  C   VAL A  40     2870   3909   3810    125    -19    156       C  
ATOM     77  O   VAL A  40      -7.905   8.025 -49.286  1.00 31.96           O  
ANISOU   77  O   VAL A  40     3393   4411   4339    134    -15    137       O  
ATOM     78  CB  VAL A  40     -10.037   9.875 -47.821  1.00 22.66           C  
ANISOU   78  CB  VAL A  40     2305   3234   3072    140   -102    298       C  
ATOM     79  CG1 VAL A  40      -9.644   9.843 -46.340  1.00 27.05           C  
ANISOU   79  CG1 VAL A  40     2797   3800   3682    189   -149    309       C  
ATOM     80  CG2 VAL A  40     -11.083  10.963 -48.003  1.00 22.49           C  
ANISOU   80  CG2 VAL A  40     2359   3209   2976    109   -107    359       C  
ATOM     81  N   LYS A  41      -6.702   9.304 -47.883  1.00 24.90           N  
ANISOU   81  N   LYS A  41     2428   3552   3481    138    -13    121       N  
ATOM     82  CA  LYS A  41      -5.584   8.383 -47.811  1.00 25.82           C  
ANISOU   82  CA  LYS A  41     2473   3673   3666    161      0     55       C  
ATOM     83  C   LYS A  41      -5.705   7.531 -46.555  1.00 23.84           C  
ANISOU   83  C   LYS A  41     2170   3416   3471    229    -67     78       C  
ATOM     84  O   LYS A  41      -6.425   7.873 -45.610  1.00 20.72           O  
ANISOU   84  O   LYS A  41     1786   3019   3067    255   -119    139       O  
ATOM     85  CB  LYS A  41      -4.255   9.151 -47.815  1.00 23.52           C  
ANISOU   85  CB  LYS A  41     2136   3406   3393    132     52     -4       C  
ATOM     86  CG  LYS A  41      -4.131  10.154 -48.952  1.00 29.17           C  
ANISOU   86  CG  LYS A  41     2902   4130   4051     64    118    -23       C  
ATOM     87  CD  LYS A  41      -3.611   9.494 -50.202  1.00 28.96           C  
ANISOU   87  CD  LYS A  41     2877   4097   4028     39    170    -84       C  
ATOM     88  CE  LYS A  41      -2.121   9.263 -50.091  1.00 32.07           C  
ANISOU   88  CE  LYS A  41     3195   4509   4482     41    205   -160       C  
ATOM     89  NZ  LYS A  41      -1.593   8.431 -51.207  1.00 38.10           N  
ANISOU   89  NZ  LYS A  41     3951   5265   5259     25    250   -220       N  
ATOM     90  N   ASP A  42      -4.979   6.407 -46.558  1.00 25.13           N  
ANISOU   90  N   ASP A  42     2278   3577   3695    258    -65     28       N  
ATOM     91  CA  ASP A  42      -4.934   5.533 -45.389  1.00 24.86           C  
ANISOU   91  CA  ASP A  42     2187   3537   3720    323   -125     41       C  
ATOM     92  C   ASP A  42      -4.449   6.244 -44.136  1.00 22.71           C  
ANISOU   92  C   ASP A  42     1871   3284   3475    342   -148     51       C  
ATOM     93  O   ASP A  42      -4.778   5.801 -43.029  1.00 26.79           O  
ANISOU   93  O   ASP A  42     2359   3795   4024    394   -208     86       O  
ATOM     94  CB  ASP A  42      -4.027   4.336 -45.661  1.00 25.33           C  
ANISOU   94  CB  ASP A  42     2190   3594   3840    344   -109    -25       C  
ATOM     95  CG  ASP A  42      -4.562   3.452 -46.760  1.00 29.80           C  
ANISOU   95  CG  ASP A  42     2795   4139   4387    335    -97    -31       C  
ATOM     96  OD1 ASP A  42      -5.774   3.561 -47.072  1.00 30.30           O  
ANISOU   96  OD1 ASP A  42     2926   4188   4400    327   -117     25       O  
ATOM     97  OD2 ASP A  42      -3.774   2.663 -47.311  1.00 29.82           O  
ANISOU   97  OD2 ASP A  42     2763   4141   4426    336    -66    -92       O  
ATOM     98  N   ASP A  43      -3.678   7.325 -44.272  1.00 18.29           N  
ANISOU   98  N   ASP A  43     1302   2746   2903    303   -102     21       N  
ATOM     99  CA  ASP A  43      -3.215   8.073 -43.110  1.00 19.27           C  
ANISOU   99  CA  ASP A  43     1385   2888   3050    318   -121     31       C  
ATOM    100  C   ASP A  43      -4.192   9.161 -42.692  1.00 21.44           C  
ANISOU  100  C   ASP A  43     1714   3164   3269    306   -147    102       C  
ATOM    101  O   ASP A  43      -3.809  10.062 -41.934  1.00 18.87           O  
ANISOU  101  O   ASP A  43     1366   2855   2947    303   -150    109       O  
ATOM    102  CB  ASP A  43      -1.829   8.683 -43.372  1.00 17.48           C  
ANISOU  102  CB  ASP A  43     1115   2684   2842    285    -61    -39       C  
ATOM    103  CG  ASP A  43      -1.834   9.743 -44.481  1.00 21.69           C  
ANISOU  103  CG  ASP A  43     1704   3224   3312    216      1    -50       C  
ATOM    104  OD1 ASP A  43      -2.870   9.941 -45.139  1.00 18.66           O  
ANISOU  104  OD1 ASP A  43     1392   2827   2870    193      0     -9       O  
ATOM    105  OD2 ASP A  43      -0.780  10.382 -44.696  1.00 18.84           O  
ANISOU  105  OD2 ASP A  43     1315   2883   2960    185     50   -101       O  
ATOM    106  N   HIS A  44      -5.429   9.110 -43.200  1.00 17.69           N  
ANISOU  106  N   HIS A  44     1309   2670   2741    296   -163    154       N  
ATOM    107  CA  HIS A  44      -6.501  10.055 -42.894  1.00 20.78           C  
ANISOU  107  CA  HIS A  44     1759   3060   3075    284   -190    226       C  
ATOM    108  C   HIS A  44      -6.200  11.463 -43.382  1.00 20.57           C  
ANISOU  108  C   HIS A  44     1763   3051   3001    225   -138    216       C  
ATOM    109  O   HIS A  44      -6.757  12.435 -42.859  1.00 24.45           O  
ANISOU  109  O   HIS A  44     2285   3548   3457    218   -158    267       O  
ATOM    110  CB  HIS A  44      -6.825  10.069 -41.393  1.00 19.32           C  
ANISOU  110  CB  HIS A  44     1544   2877   2919    336   -257    274       C  
ATOM    111  CG  HIS A  44      -7.063   8.706 -40.829  1.00 21.92           C  
ANISOU  111  CG  HIS A  44     1839   3191   3299    396   -309    283       C  
ATOM    112  ND1 HIS A  44      -8.294   8.085 -40.869  1.00 21.84           N  
ANISOU  112  ND1 HIS A  44     1873   3159   3268    418   -353    338       N  
ATOM    113  CD2 HIS A  44      -6.212   7.825 -40.251  1.00 23.36           C  
ANISOU  113  CD2 HIS A  44     1947   3376   3552    437   -323    242       C  
ATOM    114  CE1 HIS A  44      -8.191   6.882 -40.329  1.00 22.06           C  
ANISOU  114  CE1 HIS A  44     1902   3162   3319    455   -377    299       C  
ATOM    115  NE2 HIS A  44      -6.941   6.703 -39.942  1.00 21.45           N  
ANISOU  115  NE2 HIS A  44     1758   3102   3289    467   -360    241       N  
ATOM    116  N   SER A  45      -5.327  11.601 -44.370  1.00 20.17           N  
ANISOU  116  N   SER A  45     1707   3009   2949    183    -72    152       N  
ATOM    117  CA  SER A  45      -5.145  12.891 -45.009  1.00 20.65           C  
ANISOU  117  CA  SER A  45     1805   3083   2957    123    -20    144       C  
ATOM    118  C   SER A  45      -6.060  12.980 -46.227  1.00 21.22           C  
ANISOU  118  C   SER A  45     1958   3140   2963     84      3    166       C  
ATOM    119  O   SER A  45      -6.591  11.978 -46.712  1.00 19.10           O  
ANISOU  119  O   SER A  45     1708   2852   2697    100    -10    171       O  
ATOM    120  CB  SER A  45      -3.677  13.113 -45.405  1.00 21.59           C  
ANISOU  120  CB  SER A  45     1875   3222   3108     96     42     63       C  
ATOM    121  OG  SER A  45      -3.279  12.269 -46.473  1.00 20.11           O  
ANISOU  121  OG  SER A  45     1684   3025   2931     82     81     10       O  
ATOM    122  N   PHE A  46      -6.258  14.203 -46.701  1.00 22.82           N  
ANISOU  122  N   PHE A  46     2211   3352   3108     34     37    180       N  
ATOM    123  CA  PHE A  46      -7.133  14.479 -47.829  1.00 24.58           C  
ANISOU  123  CA  PHE A  46     2515   3562   3264     -8     61    203       C  
ATOM    124  C   PHE A  46      -6.311  15.101 -48.943  1.00 23.29           C  
ANISOU  124  C   PHE A  46     2362   3411   3077    -68    139    145       C  
ATOM    125  O   PHE A  46      -5.472  15.966 -48.692  1.00 24.81           O  
ANISOU  125  O   PHE A  46     2527   3624   3276    -89    168    117       O  
ATOM    126  CB  PHE A  46      -8.281  15.441 -47.453  1.00 27.85           C  
ANISOU  126  CB  PHE A  46     2990   3974   3619    -16     29    280       C  
ATOM    127  CG  PHE A  46      -8.874  15.190 -46.089  1.00 21.52           C  
ANISOU  127  CG  PHE A  46     2167   3168   2842     40    -46    337       C  
ATOM    128  CD1 PHE A  46      -9.854  14.233 -45.915  1.00 21.97           C  
ANISOU  128  CD1 PHE A  46     2242   3202   2902     79    -97    379       C  
ATOM    129  CD2 PHE A  46      -8.453  15.934 -44.987  1.00 24.94           C  
ANISOU  129  CD2 PHE A  46     2563   3618   3295     54    -64    347       C  
ATOM    130  CE1 PHE A  46     -10.410  14.003 -44.665  1.00 22.64           C  
ANISOU  130  CE1 PHE A  46     2310   3284   3010    130   -166    431       C  
ATOM    131  CE2 PHE A  46      -8.992  15.715 -43.733  1.00 27.50           C  
ANISOU  131  CE2 PHE A  46     2868   3938   3642    105   -133    399       C  
ATOM    132  CZ  PHE A  46      -9.972  14.740 -43.565  1.00 25.32           C  
ANISOU  132  CZ  PHE A  46     2611   3641   3369    144   -184    441       C  
ATOM    133  N   GLU A  47      -6.561  14.661 -50.171  1.00 24.38           N  
ANISOU  133  N   GLU A  47     2540   3536   3188    -95    172    126       N  
ATOM    134  CA  GLU A  47      -5.939  15.226 -51.360  1.00 24.38           C  
ANISOU  134  CA  GLU A  47     2561   3545   3158   -155    247     76       C  
ATOM    135  C   GLU A  47      -7.016  15.578 -52.367  1.00 25.21           C  
ANISOU  135  C   GLU A  47     2755   3636   3189   -193    261    113       C  
ATOM    136  O   GLU A  47      -7.950  14.804 -52.592  1.00 23.94           O  
ANISOU  136  O   GLU A  47     2627   3455   3016   -173    229    147       O  
ATOM    137  CB  GLU A  47      -4.964  14.254 -52.031  1.00 24.66           C  
ANISOU  137  CB  GLU A  47     2553   3579   3238   -154    285      1       C  
ATOM    138  CG  GLU A  47      -3.706  13.973 -51.251  1.00 37.52           C  
ANISOU  138  CG  GLU A  47     4093   5224   4938   -127    286    -50       C  
ATOM    139  CD  GLU A  47      -2.640  13.318 -52.112  1.00 47.17           C  
ANISOU  139  CD  GLU A  47     5280   6450   6194   -142    340   -130       C  
ATOM    140  OE1 GLU A  47      -2.976  12.838 -53.221  1.00 40.18           O  
ANISOU  140  OE1 GLU A  47     4434   5550   5282   -164    366   -142       O  
ATOM    141  OE2 GLU A  47      -1.464  13.298 -51.683  1.00 54.72           O  
ANISOU  141  OE2 GLU A  47     6168   7422   7201   -134    357   -181       O  
ATOM    142  N   LEU A  48      -6.868  16.727 -52.996  1.00 20.03           N  
ANISOU  142  N   LEU A  48     2136   2991   2483   -248    309    106       N  
ATOM    143  CA  LEU A  48      -7.721  17.098 -54.108  1.00 21.12           C  
ANISOU  143  CA  LEU A  48     2357   3118   2551   -291    334    129       C  
ATOM    144  C   LEU A  48      -6.983  16.749 -55.391  1.00 21.69           C  
ANISOU  144  C   LEU A  48     2429   3190   2624   -328    400     61       C  
ATOM    145  O   LEU A  48      -5.845  17.179 -55.584  1.00 23.47           O  
ANISOU  145  O   LEU A  48     2617   3432   2867   -354    449      4       O  
ATOM    146  CB  LEU A  48      -8.050  18.584 -54.051  1.00 24.99           C  
ANISOU  146  CB  LEU A  48     2892   3619   2984   -330    347    164       C  
ATOM    147  CG  LEU A  48      -8.955  19.094 -55.150  1.00 26.24           C  
ANISOU  147  CG  LEU A  48     3138   3767   3066   -376    372    192       C  
ATOM    148  CD1 LEU A  48     -10.297  18.372 -55.068  1.00 25.99           C  
ANISOU  148  CD1 LEU A  48     3149   3711   3016   -345    317    253       C  
ATOM    149  CD2 LEU A  48      -9.115  20.598 -54.956  1.00 24.73           C  
ANISOU  149  CD2 LEU A  48     2981   3590   2826   -412    386    222       C  
ATOM    150  N   ASP A  49      -7.602  15.941 -56.243  1.00 19.24           N  
ANISOU  150  N   ASP A  49     2156   2860   2296   -330    401     65       N  
ATOM    151  CA  ASP A  49      -7.041  15.714 -57.574  1.00 21.94           C  
ANISOU  151  CA  ASP A  49     2509   3200   2627   -371    466      5       C  
ATOM    152  C   ASP A  49      -7.424  16.931 -58.399  1.00 20.13           C  
ANISOU  152  C   ASP A  49     2351   2975   2323   -431    508     21       C  
ATOM    153  O   ASP A  49      -8.495  16.989 -59.004  1.00 19.95           O  
ANISOU  153  O   ASP A  49     2397   2937   2247   -447    501     63       O  
ATOM    154  CB  ASP A  49      -7.560  14.420 -58.193  1.00 19.90           C  
ANISOU  154  CB  ASP A  49     2266   2919   2376   -351    453      3       C  
ATOM    155  CG  ASP A  49      -6.924  14.113 -59.557  1.00 22.56           C  
ANISOU  155  CG  ASP A  49     2610   3254   2706   -391    520    -61       C  
ATOM    156  OD1 ASP A  49      -6.309  15.007 -60.184  1.00 22.42           O  
ANISOU  156  OD1 ASP A  49     2605   3252   2663   -441    578    -95       O  
ATOM    157  OD2 ASP A  49      -7.052  12.965 -60.015  1.00 23.74           O  
ANISOU  157  OD2 ASP A  49     2755   3389   2876   -372    514    -78       O  
ATOM    158  N   GLU A  50      -6.537  17.928 -58.411  1.00 20.58           N  
ANISOU  158  N   GLU A  50     2389   3053   2376   -466    552    -12       N  
ATOM    159  CA  GLU A  50      -6.884  19.193 -59.056  1.00 24.30           C  
ANISOU  159  CA  GLU A  50     2925   3530   2778   -522    589      6       C  
ATOM    160  C   GLU A  50      -6.949  19.044 -60.567  1.00 24.03           C  
ANISOU  160  C   GLU A  50     2940   3487   2705   -567    644    -24       C  
ATOM    161  O   GLU A  50      -7.816  19.639 -61.214  1.00 20.81           O  
ANISOU  161  O   GLU A  50     2605   3071   2231   -601    653     12       O  
ATOM    162  CB  GLU A  50      -5.887  20.282 -58.667  1.00 22.54           C  
ANISOU  162  CB  GLU A  50     2668   3332   2563   -546    622    -23       C  
ATOM    163  CG  GLU A  50      -5.911  20.601 -57.192  1.00 23.87           C  
ANISOU  163  CG  GLU A  50     2797   3510   2761   -506    569     13       C  
ATOM    164  CD  GLU A  50      -5.108  21.835 -56.845  1.00 28.04           C  
ANISOU  164  CD  GLU A  50     3305   4063   3286   -536    600     -6       C  
ATOM    165  OE1 GLU A  50      -4.665  22.535 -57.773  1.00 23.87           O  
ANISOU  165  OE1 GLU A  50     2803   3543   2725   -590    662    -40       O  
ATOM    166  OE2 GLU A  50      -4.919  22.102 -55.642  1.00 32.07           O  
ANISOU  166  OE2 GLU A  50     3774   4583   3827   -504    563     13       O  
ATOM    167  N   THR A  51      -6.044  18.250 -61.144  1.00 26.20           N  
ANISOU  167  N   THR A  51     3173   3762   3019   -569    680    -91       N  
ATOM    168  CA  THR A  51      -6.082  17.999 -62.581  1.00 26.57           C  
ANISOU  168  CA  THR A  51     3263   3799   3032   -609    731   -123       C  
ATOM    169  C   THR A  51      -7.435  17.446 -63.001  1.00 26.33           C  
ANISOU  169  C   THR A  51     3296   3745   2964   -598    697    -70       C  
ATOM    170  O   THR A  51      -8.060  17.946 -63.944  1.00 25.17           O  
ANISOU  170  O   THR A  51     3219   3590   2754   -640    724    -53       O  
ATOM    171  CB  THR A  51      -4.969  17.032 -62.972  1.00 28.11           C  
ANISOU  171  CB  THR A  51     3398   3997   3285   -600    763   -199       C  
ATOM    172  OG1 THR A  51      -3.718  17.540 -62.499  1.00 31.33           O  
ANISOU  172  OG1 THR A  51     3745   4428   3731   -607    791   -246       O  
ATOM    173  CG2 THR A  51      -4.916  16.866 -64.491  1.00 30.96           C  
ANISOU  173  CG2 THR A  51     3802   4350   3610   -646    822   -235       C  
ATOM    174  N   ALA A  52      -7.911  16.416 -62.301  1.00 26.42           N  
ANISOU  174  N   ALA A  52     3283   3742   3012   -543    638    -43       N  
ATOM    175  CA  ALA A  52      -9.195  15.821 -62.657  1.00 27.12           C  
ANISOU  175  CA  ALA A  52     3428   3807   3068   -529    603      7       C  
ATOM    176  C   ALA A  52     -10.327  16.823 -62.477  1.00 27.67           C  
ANISOU  176  C   ALA A  52     3566   3874   3073   -546    579     79       C  
ATOM    177  O   ALA A  52     -11.184  16.976 -63.357  1.00 26.52           O  
ANISOU  177  O   ALA A  52     3491   3715   2870   -574    590    105       O  
ATOM    178  CB  ALA A  52      -9.441  14.561 -61.831  1.00 27.92           C  
ANISOU  178  CB  ALA A  52     3487   3897   3225   -464    542     22       C  
ATOM    179  N   LEU A  53     -10.328  17.540 -61.353  1.00 23.81           N  
ANISOU  179  N   LEU A  53     3057   3398   2592   -529    548    111       N  
ATOM    180  CA  LEU A  53     -11.385  18.512 -61.105  1.00 23.45           C  
ANISOU  180  CA  LEU A  53     3072   3350   2487   -543    523    181       C  
ATOM    181  C   LEU A  53     -11.377  19.621 -62.154  1.00 25.67           C  
ANISOU  181  C   LEU A  53     3413   3638   2704   -609    583    171       C  
ATOM    182  O   LEU A  53     -12.436  20.016 -62.659  1.00 24.57           O  
ANISOU  182  O   LEU A  53     3346   3487   2503   -631    577    218       O  
ATOM    183  CB  LEU A  53     -11.237  19.083 -59.694  1.00 24.85           C  
ANISOU  183  CB  LEU A  53     3210   3541   2689   -514    482    210       C  
ATOM    184  CG  LEU A  53     -12.295  20.055 -59.178  1.00 27.04           C  
ANISOU  184  CG  LEU A  53     3540   3818   2915   -518    447    285       C  
ATOM    185  CD1 LEU A  53     -13.631  19.346 -58.922  1.00 24.25           C  
ANISOU  185  CD1 LEU A  53     3223   3442   2548   -481    385    349       C  
ATOM    186  CD2 LEU A  53     -11.786  20.727 -57.905  1.00 24.25           C  
ANISOU  186  CD2 LEU A  53     3138   3483   2591   -498    424    295       C  
ATOM    187  N   ASN A  54     -10.190  20.133 -62.501  1.00 26.98           N  
ANISOU  187  N   ASN A  54     3547   3822   2882   -643    641    110       N  
ATOM    188  CA  ASN A  54     -10.096  21.154 -63.544  1.00 28.50           C  
ANISOU  188  CA  ASN A  54     3792   4021   3016   -707    702     95       C  
ATOM    189  C   ASN A  54     -10.592  20.629 -64.889  1.00 28.12           C  
ANISOU  189  C   ASN A  54     3799   3955   2931   -733    731     85       C  
ATOM    190  O   ASN A  54     -11.268  21.346 -65.633  1.00 26.06           O  
ANISOU  190  O   ASN A  54     3609   3690   2604   -774    752    111       O  
ATOM    191  CB  ASN A  54      -8.653  21.636 -63.683  1.00 24.22           C  
ANISOU  191  CB  ASN A  54     3200   3501   2501   -735    759     25       C  
ATOM    192  CG  ASN A  54      -8.176  22.408 -62.480  1.00 28.02           C  
ANISOU  192  CG  ASN A  54     3638   4002   3007   -721    740     36       C  
ATOM    193  OD1 ASN A  54      -8.971  22.854 -61.654  1.00 27.78           O  
ANISOU  193  OD1 ASN A  54     3627   3970   2959   -701    691     98       O  
ATOM    194  ND2 ASN A  54      -6.866  22.581 -62.380  1.00 29.54           N  
ANISOU  194  ND2 ASN A  54     3772   4213   3240   -731    778    -26       N  
ATOM    195  N   ARG A  55     -10.232  19.390 -65.230  1.00 28.50           N  
ANISOU  195  N   ARG A  55     3814   3994   3022   -711    734     45       N  
ATOM    196  CA  ARG A  55     -10.636  18.821 -66.511  1.00 31.38           C  
ANISOU  196  CA  ARG A  55     4226   4341   3355   -734    762     32       C  
ATOM    197  C   ARG A  55     -12.155  18.822 -66.650  1.00 30.18           C  
ANISOU  197  C   ARG A  55     4147   4170   3150   -729    721    104       C  
ATOM    198  O   ARG A  55     -12.690  19.083 -67.734  1.00 28.80           O  
ANISOU  198  O   ARG A  55     4038   3986   2919   -769    751    111       O  
ATOM    199  CB  ARG A  55     -10.060  17.406 -66.638  1.00 31.75           C  
ANISOU  199  CB  ARG A  55     4219   4381   3464   -701    760    -16       C  
ATOM    200  CG  ARG A  55     -10.372  16.661 -67.926  1.00 44.71           C  
ANISOU  200  CG  ARG A  55     5900   6005   5084   -720    788    -37       C  
ATOM    201  CD  ARG A  55      -9.375  15.502 -68.170  1.00 49.86           C  
ANISOU  201  CD  ARG A  55     6489   6657   5799   -700    807   -105       C  
ATOM    202  NE  ARG A  55      -9.054  14.764 -66.950  1.00 54.24           N  
ANISOU  202  NE  ARG A  55     6973   7214   6423   -641    757   -104       N  
ATOM    203  CZ  ARG A  55      -7.825  14.556 -66.483  1.00 52.11           C  
ANISOU  203  CZ  ARG A  55     6627   6959   6212   -627    772   -158       C  
ATOM    204  NH1 ARG A  55      -6.751  14.967 -67.146  1.00 46.67           N  
ANISOU  204  NH1 ARG A  55     5920   6285   5527   -667    837   -222       N  
ATOM    205  NH2 ARG A  55      -7.670  13.920 -65.320  1.00 39.89           N  
ANISOU  205  NH2 ARG A  55     5021   5413   4724   -571    720   -149       N  
ATOM    206  N   ILE A  56     -12.865  18.577 -65.551  1.00 24.94           N  
ANISOU  206  N   ILE A  56     3312   3224   2940   -395    239    189       N  
ATOM    207  CA  ILE A  56     -14.315  18.443 -65.607  1.00 24.33           C  
ANISOU  207  CA  ILE A  56     3274   3135   2834   -379    179    205       C  
ATOM    208  C   ILE A  56     -14.988  19.810 -65.579  1.00 25.84           C  
ANISOU  208  C   ILE A  56     3490   3300   3028   -393    135    251       C  
ATOM    209  O   ILE A  56     -15.851  20.117 -66.408  1.00 25.66           O  
ANISOU  209  O   ILE A  56     3521   3272   2957   -407    108    283       O  
ATOM    210  CB  ILE A  56     -14.797  17.544 -64.455  1.00 23.76           C  
ANISOU  210  CB  ILE A  56     3165   3063   2801   -333    146    175       C  
ATOM    211  CG1 ILE A  56     -14.203  16.144 -64.619  1.00 22.40           C  
ANISOU  211  CG1 ILE A  56     2978   2911   2623   -319    189    133       C  
ATOM    212  CG2 ILE A  56     -16.326  17.514 -64.391  1.00 23.28           C  
ANISOU  212  CG2 ILE A  56     3135   2990   2721   -318     83    192       C  
ATOM    213  CD1 ILE A  56     -14.433  15.238 -63.436  1.00 22.95           C  
ANISOU  213  CD1 ILE A  56     3007   2977   2735   -275    165    105       C  
ATOM    214  N   LEU A  57     -14.592  20.666 -64.650  1.00 22.66           N  
ANISOU  214  N   LEU A  57     3049   2878   2682   -390    126    257       N  
ATOM    215  CA  LEU A  57     -15.365  21.871 -64.404  1.00 23.79           C  
ANISOU  215  CA  LEU A  57     3211   2989   2839   -392     79    295       C  
ATOM    216  C   LEU A  57     -14.773  23.115 -65.047  1.00 24.78           C  
ANISOU  216  C   LEU A  57     3361   3096   2957   -435    103    331       C  
ATOM    217  O   LEU A  57     -15.424  24.166 -65.029  1.00 25.65           O  
ANISOU  217  O   LEU A  57     3496   3174   3075   -439     66    368       O  
ATOM    218  CB  LEU A  57     -15.525  22.095 -62.894  1.00 21.25           C  
ANISOU  218  CB  LEU A  57     2841   2650   2582   -361     46    277       C  
ATOM    219  CG  LEU A  57     -16.505  21.185 -62.139  1.00 23.18           C  
ANISOU  219  CG  LEU A  57     3071   2899   2836   -317      6    255       C  
ATOM    220  CD1 LEU A  57     -16.443  21.439 -60.640  1.00 18.33           C  
ANISOU  220  CD1 LEU A  57     2412   2271   2281   -293    -15    236       C  
ATOM    221  CD2 LEU A  57     -17.907  21.394 -62.642  1.00 24.02           C  
ANISOU  221  CD2 LEU A  57     3219   2993   2913   -310    -40    285       C  
ATOM    222  N   LEU A  58     -13.571  23.037 -65.615  1.00 24.15           N  
ANISOU  222  N   LEU A  58     3274   3035   2866   -468    165    322       N  
ATOM    223  CA  LEU A  58     -12.998  24.190 -66.295  1.00 24.82           C  
ANISOU  223  CA  LEU A  58     3386   3103   2940   -515    194    359       C  
ATOM    224  C   LEU A  58     -13.077  24.087 -67.815  1.00 27.20           C  
ANISOU  224  C   LEU A  58     3753   3420   3162   -548    222    385       C  
ATOM    225  O   LEU A  58     -12.503  24.934 -68.508  1.00 29.22           O  
ANISOU  225  O   LEU A  58     4036   3666   3400   -592    257    416       O  
ATOM    226  CB  LEU A  58     -11.547  24.407 -65.864  1.00 23.41           C  
ANISOU  226  CB  LEU A  58     3153   2933   2810   -537    247    336       C  
ATOM    227  CG  LEU A  58     -11.344  24.708 -64.370  1.00 31.22           C  
ANISOU  227  CG  LEU A  58     4082   3906   3874   -514    218    313       C  
ATOM    228  CD1 LEU A  58      -9.946  25.251 -64.097  1.00 27.86           C  
ANISOU  228  CD1 LEU A  58     3609   3483   3493   -549    263    302       C  
ATOM    229  CD2 LEU A  58     -12.398  25.663 -63.831  1.00 23.92           C  
ANISOU  229  CD2 LEU A  58     3181   2939   2968   -500    156    340       C  
ATOM    230  N   SER A  59     -13.753  23.073 -68.353  1.00 25.87           N  
ANISOU  230  N   SER A  59     3613   3274   2943   -532    210    374       N  
ATOM    231  CA  SER A  59     -13.858  22.989 -69.802  1.00 27.85           C  
ANISOU  231  CA  SER A  59     3932   3540   3109   -567    234    398       C  
ATOM    232  C   SER A  59     -14.651  24.182 -70.331  1.00 31.36           C  
ANISOU  232  C   SER A  59     4435   3954   3528   -586    188    462       C  
ATOM    233  O   SER A  59     -15.424  24.823 -69.606  1.00 28.22           O  
ANISOU  233  O   SER A  59     4026   3525   3172   -560    128    482       O  
ATOM    234  CB  SER A  59     -14.496  21.666 -70.231  1.00 30.32           C  
ANISOU  234  CB  SER A  59     4267   3881   3373   -548    223    369       C  
ATOM    235  OG  SER A  59     -15.866  21.611 -69.889  1.00 30.04           O  
ANISOU  235  OG  SER A  59     4242   3833   3340   -517    145    384       O  
ATOM    236  N   GLU A  60     -14.428  24.497 -71.611  1.00 32.41           N  
ANISOU  236  N   GLU A  60     4630   4095   3589   -630    218    495       N  
ATOM    237  CA  GLU A  60     -14.977  25.726 -72.176  1.00 28.96           C  
ANISOU  237  CA  GLU A  60     4250   3625   3127   -653    182    562       C  
ATOM    238  C   GLU A  60     -16.492  25.752 -72.089  1.00 26.85           C  
ANISOU  238  C   GLU A  60     4006   3344   2852   -618     92    588       C  
ATOM    239  O   GLU A  60     -17.082  26.811 -71.854  1.00 32.32           O  
ANISOU  239  O   GLU A  60     4711   3998   3573   -610     44    633       O  
ATOM    240  CB  GLU A  60     -14.524  25.890 -73.630  1.00 34.90           C  
ANISOU  240  CB  GLU A  60     5074   4395   3792   -708    230    593       C  
ATOM    241  CG  GLU A  60     -15.055  27.140 -74.302  1.00 38.23           C  
ANISOU  241  CG  GLU A  60     5563   4782   4181   -734    193    669       C  
ATOM    242  CD  GLU A  60     -14.528  27.322 -75.715  1.00 47.03           C  
ANISOU  242  CD  GLU A  60     6752   5914   5204   -793    246    701       C  
ATOM    243  OE1 GLU A  60     -13.792  26.433 -76.199  1.00 46.76           O  
ANISOU  243  OE1 GLU A  60     6718   5921   5129   -814    314    659       O  
ATOM    244  OE2 GLU A  60     -14.848  28.361 -76.338  1.00 54.95           O  
ANISOU  244  OE2 GLU A  60     7816   6888   6175   -820    221    769       O  
ATOM    245  N   ALA A  61     -17.135  24.594 -72.239  1.00 30.22           N  
ANISOU  245  N   ALA A  61     4436   3802   3246   -596     70    558       N  
ATOM    246  CA  ALA A  61     -18.591  24.548 -72.296  1.00 32.07           C  
ANISOU  246  CA  ALA A  61     4690   4029   3465   -568    -14    583       C  
ATOM    247  C   ALA A  61     -19.235  24.879 -70.955  1.00 31.35           C  
ANISOU  247  C   ALA A  61     4541   3908   3462   -520    -64    576       C  
ATOM    248  O   ALA A  61     -20.381  25.344 -70.925  1.00 30.38           O  
ANISOU  248  O   ALA A  61     4431   3765   3347   -498   -133    612       O  
ATOM    249  CB  ALA A  61     -19.046  23.170 -72.776  1.00 33.07           C  
ANISOU  249  CB  ALA A  61     4831   4196   3537   -563    -20    547       C  
ATOM    250  N   VAL A  62     -18.532  24.663 -69.843  1.00 27.69           N  
ANISOU  250  N   VAL A  62     4014   3441   3065   -502    -31    532       N  
ATOM    251  CA  VAL A  62     -19.153  24.778 -68.531  1.00 24.57           C  
ANISOU  251  CA  VAL A  62     3567   3025   2745   -456    -74    516       C  
ATOM    252  C   VAL A  62     -18.467  25.789 -67.617  1.00 23.28           C  
ANISOU  252  C   VAL A  62     3369   2826   2650   -457    -56    517       C  
ATOM    253  O   VAL A  62     -19.098  26.244 -66.651  1.00 26.74           O  
ANISOU  253  O   VAL A  62     3779   3236   3145   -424    -96    517       O  
ATOM    254  CB  VAL A  62     -19.236  23.399 -67.835  1.00 28.14           C  
ANISOU  254  CB  VAL A  62     3974   3506   3212   -426    -69    457       C  
ATOM    255  CG1 VAL A  62     -19.824  22.368 -68.776  1.00 26.12           C  
ANISOU  255  CG1 VAL A  62     3756   3283   2886   -432    -81    451       C  
ATOM    256  CG2 VAL A  62     -17.863  22.940 -67.330  1.00 23.36           C  
ANISOU  256  CG2 VAL A  62     3326   2915   2633   -433     -3    412       C  
ATOM    257  N   ARG A  63     -17.225  26.186 -67.888  1.00 24.64           N  
ANISOU  257  N   ARG A  63     3542   2998   2821   -495      3    517       N  
ATOM    258  CA  ARG A  63     -16.436  26.920 -66.895  1.00 24.68           C  
ANISOU  258  CA  ARG A  63     3504   2978   2896   -498     23    503       C  
ATOM    259  C   ARG A  63     -17.152  28.186 -66.414  1.00 27.27           C  
ANISOU  259  C   ARG A  63     3842   3252   3267   -485    -24    540       C  
ATOM    260  O   ARG A  63     -17.088  28.533 -65.226  1.00 23.96           O  
ANISOU  260  O   ARG A  63     3381   2811   2913   -464    -35    516       O  
ATOM    261  CB  ARG A  63     -15.055  27.241 -67.480  1.00 29.29           C  
ANISOU  261  CB  ARG A  63     4093   3570   3466   -549     93    506       C  
ATOM    262  CG  ARG A  63     -14.793  28.703 -67.815  1.00 34.44           C  
ANISOU  262  CG  ARG A  63     4779   4179   4128   -585     99    556       C  
ATOM    263  CD  ARG A  63     -14.138  28.911 -69.176  1.00 35.40           C  
ANISOU  263  CD  ARG A  63     4952   4313   4185   -640    150    588       C  
ATOM    264  NE  ARG A  63     -13.097  27.943 -69.501  1.00 38.81           N  
ANISOU  264  NE  ARG A  63     5359   4793   4594   -659    218    546       N  
ATOM    265  CZ  ARG A  63     -12.304  28.027 -70.565  1.00 41.64           C  
ANISOU  265  CZ  ARG A  63     5750   5168   4903   -708    280    562       C  
ATOM    266  NH1 ARG A  63     -12.346  29.075 -71.381  1.00 35.13           N  
ANISOU  266  NH1 ARG A  63     4987   4315   4044   -749    284    620       N  
ATOM    267  NH2 ARG A  63     -11.450  27.036 -70.818  1.00 32.56           N  
ANISOU  267  NH2 ARG A  63     4573   4062   3736   -717    342    518       N  
ATOM    268  N   ASP A  64     -17.879  28.857 -67.306  1.00 26.01           N  
ANISOU  268  N   ASP A  64     3739   3070   3072   -494    -56    596       N  
ATOM    269  CA  ASP A  64     -18.527  30.124 -67.001  1.00 28.59           C  
ANISOU  269  CA  ASP A  64     4082   3339   3440   -481    -97    637       C  
ATOM    270  C   ASP A  64     -20.006  29.975 -66.726  1.00 26.18           C  
ANISOU  270  C   ASP A  64     3775   3025   3147   -431   -166    647       C  
ATOM    271  O   ASP A  64     -20.678  30.984 -66.492  1.00 25.23           O  
ANISOU  271  O   ASP A  64     3666   2855   3064   -413   -203    681       O  
ATOM    272  CB  ASP A  64     -18.336  31.116 -68.151  1.00 30.30           C  
ANISOU  272  CB  ASP A  64     4364   3529   3618   -523    -89    701       C  
ATOM    273  CG  ASP A  64     -16.887  31.430 -68.412  1.00 35.44           C  
ANISOU  273  CG  ASP A  64     5016   4184   4264   -577    -18    695       C  
ATOM    274  OD1 ASP A  64     -16.216  31.973 -67.501  1.00 35.26           O  
ANISOU  274  OD1 ASP A  64     4955   4136   4305   -583      4    672       O  
ATOM    275  OD2 ASP A  64     -16.421  31.128 -69.534  1.00 39.32           O  
ANISOU  275  OD2 ASP A  64     5547   4704   4687   -615     18    712       O  
ATOM    276  N   LYS A  65     -20.538  28.756 -66.777  1.00 21.65           N  
ANISOU  276  N   LYS A  65     3186   2495   2545   -410   -182    619       N  
ATOM    277  CA  LYS A  65     -21.943  28.543 -66.468  1.00 23.86           C  
ANISOU  277  CA  LYS A  65     3455   2770   2841   -365   -244    625       C  
ATOM    278  C   LYS A  65     -22.145  28.574 -64.963  1.00 23.66           C  
ANISOU  278  C   LYS A  65     3372   2726   2890   -327   -251    584       C  
ATOM    279  O   LYS A  65     -21.294  28.110 -64.205  1.00 23.38           O  
ANISOU  279  O   LYS A  65     3300   2707   2876   -331   -212    537       O  
ATOM    280  CB  LYS A  65     -22.427  27.202 -67.017  1.00 24.88           C  
ANISOU  280  CB  LYS A  65     3588   2950   2914   -360   -257    607       C  
ATOM    281  CG  LYS A  65     -22.345  27.079 -68.523  1.00 31.65           C  
ANISOU  281  CG  LYS A  65     4509   3830   3688   -398   -255    644       C  
ATOM    282  CD  LYS A  65     -23.569  27.662 -69.168  1.00 35.61           C  
ANISOU  282  CD  LYS A  65     5045   4313   4172   -386   -325    702       C  
ATOM    283  CE  LYS A  65     -23.345  27.865 -70.654  1.00 42.37           C  
ANISOU  283  CE  LYS A  65     5974   5182   4943   -431   -322    749       C  
ATOM    284  NZ  LYS A  65     -22.661  26.704 -71.282  1.00 41.59           N  
ANISOU  284  NZ  LYS A  65     5892   5135   4776   -463   -274    712       N  
ATOM    285  N   GLU A  66     -23.275  29.127 -64.532  1.00 23.13           N  
ANISOU  285  N   GLU A  66     3297   2627   2864   -289   -300    603       N  
ATOM    286  CA  GLU A  66     -23.668  28.963 -63.143  1.00 23.22           C  
ANISOU  286  CA  GLU A  66     3257   2629   2937   -251   -307    560       C  
ATOM    287  C   GLU A  66     -23.897  27.480 -62.866  1.00 19.80           C  
ANISOU  287  C   GLU A  66     2794   2247   2483   -237   -305    517       C  
ATOM    288  O   GLU A  66     -24.383  26.742 -63.722  1.00 22.02           O  
ANISOU  288  O   GLU A  66     3092   2559   2714   -241   -324    528       O  
ATOM    289  CB  GLU A  66     -24.910  29.800 -62.859  1.00 20.64           C  
ANISOU  289  CB  GLU A  66     2928   2258   2656   -212   -356    590       C  
ATOM    290  CG  GLU A  66     -24.617  31.294 -63.115  1.00 26.91           C  
ANISOU  290  CG  GLU A  66     3757   2993   3475   -226   -355    633       C  
ATOM    291  CD  GLU A  66     -25.795  32.213 -62.877  1.00 29.40           C  
ANISOU  291  CD  GLU A  66     4071   3257   3842   -184   -400    665       C  
ATOM    292  OE1 GLU A  66     -26.910  31.722 -62.640  1.00 31.94           O  
ANISOU  292  OE1 GLU A  66     4366   3593   4178   -146   -437    659       O  
ATOM    293  OE2 GLU A  66     -25.602  33.441 -62.927  1.00 30.92           O  
ANISOU  293  OE2 GLU A  66     4289   3393   4065   -190   -398    696       O  
ATOM    294  N   VAL A  67     -23.510  27.031 -61.686  1.00 19.04           N  
ANISOU  294  N   VAL A  67     2655   2159   2421   -223   -283    467       N  
ATOM    295  CA  VAL A  67     -23.459  25.603 -61.394  1.00 20.17           C  
ANISOU  295  CA  VAL A  67     2773   2347   2545   -215   -272    424       C  
ATOM    296  C   VAL A  67     -24.527  25.241 -60.372  1.00 21.16           C  
ANISOU  296  C   VAL A  67     2862   2469   2708   -174   -300    402       C  
ATOM    297  O   VAL A  67     -24.803  25.998 -59.432  1.00 18.20           O  
ANISOU  297  O   VAL A  67     2470   2062   2385   -153   -306    396       O  
ATOM    298  CB  VAL A  67     -22.055  25.162 -60.922  1.00 19.00           C  
ANISOU  298  CB  VAL A  67     2603   2217   2398   -235   -221    386       C  
ATOM    299  CG1 VAL A  67     -21.705  25.765 -59.541  1.00 19.60           C  
ANISOU  299  CG1 VAL A  67     2647   2268   2533   -221   -213    360       C  
ATOM    300  CG2 VAL A  67     -21.940  23.628 -60.933  1.00 16.88           C  
ANISOU  300  CG2 VAL A  67     2320   1994   2101   -229   -207    351       C  
ATOM    301  N   VAL A  68     -25.156  24.091 -60.599  1.00 19.11           N  
ANISOU  301  N   VAL A  68     2596   2243   2422   -165   -314    390       N  
ATOM    302  CA  VAL A  68     -25.975  23.394 -59.620  1.00 18.85           C  
ANISOU  302  CA  VAL A  68     2526   2218   2417   -133   -328    360       C  
ATOM    303  C   VAL A  68     -25.166  22.194 -59.168  1.00 19.43           C  
ANISOU  303  C   VAL A  68     2583   2323   2475   -139   -294    317       C  
ATOM    304  O   VAL A  68     -24.675  21.426 -60.005  1.00 19.75           O  
ANISOU  304  O   VAL A  68     2643   2391   2471   -161   -278    313       O  
ATOM    305  CB  VAL A  68     -27.322  22.948 -60.217  1.00 20.46           C  
ANISOU  305  CB  VAL A  68     2732   2435   2607   -121   -373    379       C  
ATOM    306  CG1 VAL A  68     -28.129  22.154 -59.191  1.00 19.84           C  
ANISOU  306  CG1 VAL A  68     2614   2366   2558    -93   -380    347       C  
ATOM    307  CG2 VAL A  68     -28.104  24.160 -60.720  1.00 23.91           C  
ANISOU  307  CG2 VAL A  68     3183   2839   3062   -111   -412    428       C  
ATOM    308  N   ALA A  69     -24.994  22.048 -57.860  1.00 17.10           N  
ANISOU  308  N   ALA A  69     2256   2023   2217   -121   -281    284       N  
ATOM    309  CA  ALA A  69     -24.197  20.956 -57.324  1.00 19.65           C  
ANISOU  309  CA  ALA A  69     2562   2373   2531   -122   -252    246       C  
ATOM    310  C   ALA A  69     -25.084  20.107 -56.429  1.00 17.36           C  
ANISOU  310  C   ALA A  69     2248   2091   2257    -96   -264    223       C  
ATOM    311  O   ALA A  69     -25.575  20.583 -55.392  1.00 16.57           O  
ANISOU  311  O   ALA A  69     2129   1973   2194    -76   -272    215       O  
ATOM    312  CB  ALA A  69     -22.977  21.479 -56.569  1.00 16.92           C  
ANISOU  312  CB  ALA A  69     2202   2018   2209   -130   -224    229       C  
ATOM    313  N   VAL A  70     -25.284  18.854 -56.828  1.00 16.76           N  
ANISOU  313  N   VAL A  70     2175   2041   2152    -98   -263    212       N  
ATOM    314  CA  VAL A  70     -26.144  17.928 -56.110  1.00 17.84           C  
ANISOU  314  CA  VAL A  70     2292   2186   2299    -79   -273    192       C  
ATOM    315  C   VAL A  70     -25.263  16.893 -55.441  1.00 18.68           C  
ANISOU  315  C   VAL A  70     2388   2307   2402    -76   -244    160       C  
ATOM    316  O   VAL A  70     -24.443  16.241 -56.101  1.00 18.30           O  
ANISOU  316  O   VAL A  70     2353   2275   2327    -91   -223    153       O  
ATOM    317  CB  VAL A  70     -27.164  17.246 -57.034  1.00 18.24           C  
ANISOU  317  CB  VAL A  70     2356   2251   2324    -85   -298    203       C  
ATOM    318  CG1 VAL A  70     -28.129  16.402 -56.193  1.00 13.07           C  
ANISOU  318  CG1 VAL A  70     1676   1601   1688    -68   -306    184       C  
ATOM    319  CG2 VAL A  70     -27.917  18.283 -57.860  1.00 20.02           C  
ANISOU  319  CG2 VAL A  70     2593   2463   2549    -89   -332    241       C  
ATOM    320  N   SER A  71     -25.441  16.733 -54.139  1.00 17.33           N  
ANISOU  320  N   SER A  71     2195   2132   2258    -57   -241    142       N  
ATOM    321  CA  SER A  71     -24.683  15.767 -53.375  1.00 14.26           C  
ANISOU  321  CA  SER A  71     1795   1754   1868    -51   -220    116       C  
ATOM    322  C   SER A  71     -25.632  14.854 -52.618  1.00 14.63           C  
ANISOU  322  C   SER A  71     1832   1804   1921    -35   -227    103       C  
ATOM    323  O   SER A  71     -26.779  15.208 -52.321  1.00 13.44           O  
ANISOU  323  O   SER A  71     1675   1645   1787    -27   -244    110       O  
ATOM    324  CB  SER A  71     -23.736  16.460 -52.388  1.00 17.15           C  
ANISOU  324  CB  SER A  71     2147   2114   2257    -47   -210    106       C  
ATOM    325  OG  SER A  71     -23.286  15.552 -51.393  1.00 15.41           O  
ANISOU  325  OG  SER A  71     1914   1903   2039    -34   -200     84       O  
ATOM    326  N   VAL A  72     -25.132  13.670 -52.311  1.00 13.50           N  
ANISOU  326  N   VAL A  72     1689   1672   1768    -31   -212     86       N  
ATOM    327  CA  VAL A  72     -25.797  12.748 -51.402  1.00 12.53           C  
ANISOU  327  CA  VAL A  72     1559   1550   1652    -19   -212     74       C  
ATOM    328  C   VAL A  72     -24.788  12.380 -50.329  1.00 13.36           C  
ANISOU  328  C   VAL A  72     1656   1657   1764     -7   -198     60       C  
ATOM    329  O   VAL A  72     -23.619  12.123 -50.633  1.00 12.78           O  
ANISOU  329  O   VAL A  72     1582   1590   1684     -9   -185     55       O  
ATOM    330  CB  VAL A  72     -26.311  11.488 -52.121  1.00 14.94           C  
ANISOU  330  CB  VAL A  72     1878   1862   1938    -26   -211     70       C  
ATOM    331  CG1 VAL A  72     -27.053  10.595 -51.124  1.00 12.54           C  
ANISOU  331  CG1 VAL A  72     1567   1554   1644    -17   -210     60       C  
ATOM    332  CG2 VAL A  72     -27.226  11.885 -53.279  1.00 18.82           C  
ANISOU  332  CG2 VAL A  72     2378   2355   2419    -42   -232     86       C  
ATOM    333  N   ALA A  73     -25.226  12.382 -49.076  1.00 13.90           N  
ANISOU  333  N   ALA A  73     1716   1721   1844      5   -200     53       N  
ATOM    334  CA  ALA A  73     -24.296  12.131 -47.981  1.00 14.38           C  
ANISOU  334  CA  ALA A  73     1771   1785   1907     16   -194     43       C  
ATOM    335  C   ALA A  73     -25.070  11.549 -46.806  1.00 11.46           C  
ANISOU  335  C   ALA A  73     1405   1413   1538     26   -194     37       C  
ATOM    336  O   ALA A  73     -26.281  11.728 -46.691  1.00 10.64           O  
ANISOU  336  O   ALA A  73     1300   1303   1440     25   -196     39       O  
ATOM    337  CB  ALA A  73     -23.565  13.420 -47.595  1.00 12.13           C  
ANISOU  337  CB  ALA A  73     1477   1497   1633     12   -199     41       C  
ATOM    338  N   GLY A  74     -24.364  10.844 -45.937  1.00 11.88           N  
ANISOU  338  N   GLY A  74     1459   1471   1585     36   -191     31       N  
ATOM    339  CA  GLY A  74     -25.009  10.193 -44.814  1.00 11.59           C  
ANISOU  339  CA  GLY A  74     1430   1431   1542     43   -187     29       C  
ATOM    340  C   GLY A  74     -24.279   8.910 -44.471  1.00 13.25           C  
ANISOU  340  C   GLY A  74     1649   1643   1743     53   -184     31       C  
ATOM    341  O   GLY A  74     -23.180   8.654 -44.953  1.00 12.98           O  
ANISOU  341  O   GLY A  74     1607   1612   1711     59   -185     31       O  
ATOM    342  N   ALA A  75     -24.903   8.119 -43.597  1.00 12.47           N  
ANISOU  342  N   ALA A  75     1563   1539   1636     57   -179     33       N  
ATOM    343  CA  ALA A  75     -24.253   6.916 -43.095  1.00 10.18           C  
ANISOU  343  CA  ALA A  75     1284   1245   1338     70   -179     40       C  
ATOM    344  C   ALA A  75     -23.849   5.991 -44.242  1.00 12.51           C  
ANISOU  344  C   ALA A  75     1581   1533   1640     74   -171     40       C  
ATOM    345  O   ALA A  75     -24.489   5.955 -45.294  1.00 10.89           O  
ANISOU  345  O   ALA A  75     1376   1324   1436     61   -164     36       O  
ATOM    346  CB  ALA A  75     -25.177   6.187 -42.111  1.00 13.85           C  
ANISOU  346  CB  ALA A  75     1769   1703   1792     69   -171     45       C  
ATOM    347  N   PHE A  76     -22.772   5.233 -44.025  1.00  9.07           N  
ANISOU  347  N   PHE A  76     1146   1095   1207     92   -173     44       N  
ATOM    348  CA  PHE A  76     -22.246   4.364 -45.063  1.00 14.02           C  
ANISOU  348  CA  PHE A  76     1773   1712   1843     98   -160     41       C  
ATOM    349  C   PHE A  76     -23.142   3.146 -45.258  1.00 11.62           C  
ANISOU  349  C   PHE A  76     1494   1386   1534     93   -147     41       C  
ATOM    350  O   PHE A  76     -23.963   2.795 -44.403  1.00 10.00           O  
ANISOU  350  O   PHE A  76     1304   1174   1322     89   -148     49       O  
ATOM    351  CB  PHE A  76     -20.784   3.967 -44.750  1.00 12.85           C  
ANISOU  351  CB  PHE A  76     1611   1566   1707    123   -166     45       C  
ATOM    352  CG  PHE A  76     -20.615   2.809 -43.783  1.00 11.85           C  
ANISOU  352  CG  PHE A  76     1500   1424   1580    144   -171     59       C  
ATOM    353  CD1 PHE A  76     -20.979   2.920 -42.449  1.00 16.65           C  
ANISOU  353  CD1 PHE A  76     2120   2035   2172    144   -187     71       C  
ATOM    354  CD2 PHE A  76     -20.009   1.632 -44.208  1.00 15.02           C  
ANISOU  354  CD2 PHE A  76     1905   1805   1996    165   -159     60       C  
ATOM    355  CE1 PHE A  76     -20.786   1.860 -41.563  1.00 17.22           C  
ANISOU  355  CE1 PHE A  76     2210   2091   2240    163   -194     89       C  
ATOM    356  CE2 PHE A  76     -19.806   0.565 -43.322  1.00 17.15           C  
ANISOU  356  CE2 PHE A  76     2191   2056   2269    187   -167     77       C  
ATOM    357  CZ  PHE A  76     -20.197   0.689 -41.999  1.00 15.26           C  
ANISOU  357  CZ  PHE A  76     1967   1822   2011    185   -186     94       C  
ATOM    358  N   ARG A  77     -23.042   2.559 -46.454  1.00 15.65           N  
ANISOU  358  N   ARG A  77     2011   1887   2048     89   -133     31       N  
ATOM    359  CA  ARG A  77     -23.757   1.334 -46.795  1.00 13.22           C  
ANISOU  359  CA  ARG A  77     1729   1555   1739     82   -120     27       C  
ATOM    360  C   ARG A  77     -25.277   1.539 -46.842  1.00 14.06           C  
ANISOU  360  C   ARG A  77     1842   1663   1836     54   -123     26       C  
ATOM    361  O   ARG A  77     -26.034   0.602 -46.606  1.00 15.99           O  
ANISOU  361  O   ARG A  77     2105   1889   2081     45   -116     28       O  
ATOM    362  CB  ARG A  77     -23.401   0.210 -45.805  1.00 13.62           C  
ANISOU  362  CB  ARG A  77     1796   1584   1796    103   -117     39       C  
ATOM    363  CG  ARG A  77     -22.681  -1.003 -46.356  1.00 15.05           C  
ANISOU  363  CG  ARG A  77     1989   1738   1990    121   -101     33       C  
ATOM    364  CD  ARG A  77     -21.252  -0.730 -46.833  1.00 14.90           C  
ANISOU  364  CD  ARG A  77     1946   1729   1986    145    -96     26       C  
ATOM    365  NE  ARG A  77     -21.227   0.008 -48.088  1.00 13.98           N  
ANISOU  365  NE  ARG A  77     1820   1630   1862    126    -86      8       N  
ATOM    366  CZ  ARG A  77     -21.538  -0.507 -49.270  1.00 14.59           C  
ANISOU  366  CZ  ARG A  77     1916   1695   1932    111    -66    -11       C  
ATOM    367  NH1 ARG A  77     -21.892  -1.778 -49.402  1.00 15.44           N  
ANISOU  367  NH1 ARG A  77     2052   1770   2043    112    -52    -18       N  
ATOM    368  NH2 ARG A  77     -21.498   0.272 -50.346  1.00 14.80           N  
ANISOU  368  NH2 ARG A  77     1937   1742   1946     92    -60    -22       N  
ATOM    369  N   LYS A  78     -25.755   2.744 -47.164  1.00 13.54           N  
ANISOU  369  N   LYS A  78     1759   1617   1767     40   -133     25       N  
ATOM    370  CA  LYS A  78     -27.190   3.033 -47.161  1.00 14.12           C  
ANISOU  370  CA  LYS A  78     1830   1694   1840     18   -139     26       C  
ATOM    371  C   LYS A  78     -27.767   3.287 -48.555  1.00 14.06           C  
ANISOU  371  C   LYS A  78     1821   1693   1828     -4   -145     18       C  
ATOM    372  O   LYS A  78     -28.854   3.865 -48.670  1.00 16.48           O  
ANISOU  372  O   LYS A  78     2115   2008   2139    -19   -157     21       O  
ATOM    373  CB  LYS A  78     -27.491   4.235 -46.267  1.00 11.85           C  
ANISOU  373  CB  LYS A  78     1525   1422   1557     22   -148     33       C  
ATOM    374  CG  LYS A  78     -27.101   4.053 -44.803  1.00 13.29           C  
ANISOU  374  CG  LYS A  78     1713   1601   1736     38   -144     41       C  
ATOM    375  CD  LYS A  78     -27.712   2.784 -44.187  1.00 15.72           C  
ANISOU  375  CD  LYS A  78     2041   1890   2040     33   -132     46       C  
ATOM    376  CE  LYS A  78     -27.467   2.758 -42.651  1.00 19.78           C  
ANISOU  376  CE  LYS A  78     2566   2406   2544     45   -130     58       C  
ATOM    377  NZ  LYS A  78     -27.595   1.375 -42.087  1.00 22.84           N  
ANISOU  377  NZ  LYS A  78     2981   2771   2926     46   -119     69       N  
ATOM    378  N   GLY A  79     -27.065   2.906 -49.617  1.00 14.10           N  
ANISOU  378  N   GLY A  79     1839   1695   1824     -5   -139      8       N  
ATOM    379  CA  GLY A  79     -27.638   3.061 -50.943  1.00 14.09           C  
ANISOU  379  CA  GLY A  79     1844   1701   1810    -30   -147      1       C  
ATOM    380  C   GLY A  79     -27.463   4.429 -51.564  1.00 14.32           C  
ANISOU  380  C   GLY A  79     1859   1750   1832    -33   -161      9       C  
ATOM    381  O   GLY A  79     -28.243   4.809 -52.443  1.00 13.61           O  
ANISOU  381  O   GLY A  79     1771   1669   1733    -53   -177     11       O  
ATOM    382  N   LYS A  80     -26.448   5.180 -51.143  1.00 13.46           N  
ANISOU  382  N   LYS A  80     1737   1647   1730    -15   -156     14       N  
ATOM    383  CA  LYS A  80     -26.238   6.505 -51.714  1.00 13.13           C  
ANISOU  383  CA  LYS A  80     1685   1619   1684    -20   -167     23       C  
ATOM    384  C   LYS A  80     -25.796   6.430 -53.176  1.00 13.42           C  
ANISOU  384  C   LYS A  80     1740   1661   1697    -36   -160     18       C  
ATOM    385  O   LYS A  80     -26.354   7.124 -54.033  1.00 12.71           O  
ANISOU  385  O   LYS A  80     1655   1581   1595    -53   -177     27       O  
ATOM    386  CB  LYS A  80     -25.226   7.273 -50.871  1.00 12.70           C  
ANISOU  386  CB  LYS A  80     1614   1569   1644     -2   -163     27       C  
ATOM    387  CG  LYS A  80     -25.706   7.519 -49.434  1.00 11.56           C  
ANISOU  387  CG  LYS A  80     1457   1420   1514     10   -170     32       C  
ATOM    388  CD  LYS A  80     -24.773   8.470 -48.691  1.00 13.05           C  
ANISOU  388  CD  LYS A  80     1631   1616   1713     21   -173     34       C  
ATOM    389  CE  LYS A  80     -23.372   7.864 -48.589  1.00 12.73           C  
ANISOU  389  CE  LYS A  80     1588   1577   1673     34   -161     29       C  
ATOM    390  NZ  LYS A  80     -23.427   6.489 -47.981  1.00 10.17           N  
ANISOU  390  NZ  LYS A  80     1274   1242   1347     47   -154     26       N  
ATOM    391  N   SER A  81     -24.778   5.619 -53.481  1.00 12.91           N  
ANISOU  391  N   SER A  81     1686   1592   1627    -29   -135      4       N  
ATOM    392  CA  SER A  81     -24.295   5.543 -54.861  1.00 11.99           C  
ANISOU  392  CA  SER A  81     1590   1482   1485    -44   -120     -5       C  
ATOM    393  C   SER A  81     -25.351   4.942 -55.784  1.00 13.79           C  
ANISOU  393  C   SER A  81     1845   1708   1687    -71   -132    -13       C  
ATOM    394  O   SER A  81     -25.513   5.374 -56.933  1.00 12.76           O  
ANISOU  394  O   SER A  81     1732   1589   1528    -93   -138    -10       O  
ATOM    395  CB  SER A  81     -23.006   4.721 -54.920  1.00 14.15           C  
ANISOU  395  CB  SER A  81     1865   1747   1763    -28    -86    -22       C  
ATOM    396  OG  SER A  81     -21.976   5.329 -54.156  1.00 10.19           O  
ANISOU  396  OG  SER A  81     1335   1251   1285     -7    -80    -15       O  
ATOM    397  N   PHE A  82     -26.058   3.929 -55.293  1.00 13.04           N  
ANISOU  397  N   PHE A  82     1755   1598   1601    -71   -135    -22       N  
ATOM    398  CA  PHE A  82     -27.193   3.344 -55.997  1.00 13.46           C  
ANISOU  398  CA  PHE A  82     1829   1650   1636    -99   -151    -30       C  
ATOM    399  C   PHE A  82     -28.204   4.422 -56.399  1.00 14.87           C  
ANISOU  399  C   PHE A  82     1996   1847   1808   -117   -188    -10       C  
ATOM    400  O   PHE A  82     -28.632   4.501 -57.561  1.00 14.57           O  
ANISOU  400  O   PHE A  82     1977   1819   1739   -143   -204    -11       O  
ATOM    401  CB  PHE A  82     -27.789   2.276 -55.062  1.00 11.47           C  
ANISOU  401  CB  PHE A  82     1575   1377   1405    -95   -148    -36       C  
ATOM    402  CG  PHE A  82     -29.008   1.592 -55.577  1.00 15.83           C  
ANISOU  402  CG  PHE A  82     2142   1925   1947   -127   -165    -46       C  
ATOM    403  CD1 PHE A  82     -30.268   2.111 -55.308  1.00 13.89           C  
ANISOU  403  CD1 PHE A  82     1873   1692   1714   -140   -196    -31       C  
ATOM    404  CD2 PHE A  82     -28.908   0.376 -56.238  1.00 15.90           C  
ANISOU  404  CD2 PHE A  82     2185   1916   1939   -143   -148    -72       C  
ATOM    405  CE1 PHE A  82     -31.401   1.459 -55.748  1.00 15.87           C  
ANISOU  405  CE1 PHE A  82     2130   1941   1959   -172   -214    -40       C  
ATOM    406  CE2 PHE A  82     -30.044  -0.280 -56.684  1.00 14.79           C  
ANISOU  406  CE2 PHE A  82     2057   1771   1790   -177   -167    -83       C  
ATOM    407  CZ  PHE A  82     -31.280   0.256 -56.443  1.00 14.28           C  
ANISOU  407  CZ  PHE A  82     1966   1723   1738   -193   -201    -66       C  
ATOM    408  N   LEU A  83     -28.570   5.282 -55.448  1.00 12.51           N  
ANISOU  408  N   LEU A  83     1666   1551   1536   -101   -202      9       N  
ATOM    409  CA  LEU A  83     -29.494   6.379 -55.722  1.00 11.74           C  
ANISOU  409  CA  LEU A  83     1551   1466   1442   -110   -236     30       C  
ATOM    410  C   LEU A  83     -28.940   7.325 -56.785  1.00 16.75           C  
ANISOU  410  C   LEU A  83     2201   2113   2052   -118   -243     43       C  
ATOM    411  O   LEU A  83     -29.638   7.684 -57.744  1.00 15.41           O  
ANISOU  411  O   LEU A  83     2040   1953   1861   -139   -271     54       O  
ATOM    412  CB  LEU A  83     -29.778   7.140 -54.430  1.00 12.39           C  
ANISOU  412  CB  LEU A  83     1602   1546   1561    -87   -240     43       C  
ATOM    413  CG  LEU A  83     -30.629   8.399 -54.614  1.00 15.65           C  
ANISOU  413  CG  LEU A  83     1994   1966   1987    -88   -270     65       C  
ATOM    414  CD1 LEU A  83     -32.066   8.012 -54.959  1.00 17.46           C  
ANISOU  414  CD1 LEU A  83     2213   2201   2221   -106   -298     67       C  
ATOM    415  CD2 LEU A  83     -30.552   9.304 -53.364  1.00 13.70           C  
ANISOU  415  CD2 LEU A  83     1721   1711   1772    -63   -263     72       C  
ATOM    416  N   MET A  84     -27.682   7.746 -56.622  1.00 15.14           N  
ANISOU  416  N   MET A  84     1997   1908   1849   -104   -217     42       N  
ATOM    417  CA  MET A  84     -27.071   8.663 -57.581  1.00 15.76           C  
ANISOU  417  CA  MET A  84     2089   1995   1903   -115   -217     56       C  
ATOM    418  C   MET A  84     -27.011   8.072 -58.982  1.00 17.77           C  
ANISOU  418  C   MET A  84     2381   2258   2111   -142   -212     46       C  
ATOM    419  O   MET A  84     -27.071   8.814 -59.975  1.00 15.75           O  
ANISOU  419  O   MET A  84     2144   2013   1827   -160   -227     63       O  
ATOM    420  CB  MET A  84     -25.671   9.043 -57.112  1.00 15.00           C  
ANISOU  420  CB  MET A  84     1983   1897   1821    -98   -185     52       C  
ATOM    421  CG  MET A  84     -25.653   9.680 -55.750  1.00 19.76           C  
ANISOU  421  CG  MET A  84     2554   2492   2463    -75   -191     60       C  
ATOM    422  SD  MET A  84     -24.720  11.217 -55.764  1.00 37.47           S  
ANISOU  422  SD  MET A  84     4787   4736   4715    -74   -186     77       S  
ATOM    423  CE  MET A  84     -25.570  12.046 -57.121  1.00 19.87           C  
ANISOU  423  CE  MET A  84     2580   2511   2458    -98   -214    103       C  
ATOM    424  N   ASP A  85     -26.894   6.747 -59.097  1.00 15.40           N  
ANISOU  424  N   ASP A  85     2098   1952   1801   -146   -193     18       N  
ATOM    425  CA  ASP A  85     -26.909   6.153 -60.428  1.00 15.41           C  
ANISOU  425  CA  ASP A  85     2141   1960   1755   -176   -188      3       C  
ATOM    426  C   ASP A  85     -28.293   6.225 -61.052  1.00 15.50           C  
ANISOU  426  C   ASP A  85     2162   1982   1746   -202   -235     14       C  
ATOM    427  O   ASP A  85     -28.414   6.323 -62.276  1.00 16.26           O  
ANISOU  427  O   ASP A  85     2292   2092   1795   -230   -247     16       O  
ATOM    428  CB  ASP A  85     -26.410   4.715 -60.375  1.00 14.69           C  
ANISOU  428  CB  ASP A  85     2066   1853   1661   -172   -151    -32       C  
ATOM    429  CG  ASP A  85     -24.936   4.641 -60.089  1.00 16.43           C  
ANISOU  429  CG  ASP A  85     2279   2068   1895   -148   -105    -43       C  
ATOM    430  OD1 ASP A  85     -24.277   5.689 -60.171  1.00 15.70           O  
ANISOU  430  OD1 ASP A  85     2175   1987   1805   -144    -99    -26       O  
ATOM    431  OD2 ASP A  85     -24.444   3.544 -59.789  1.00 17.28           O  
ANISOU  431  OD2 ASP A  85     2392   2159   2016   -134    -75    -68       O  
ATOM    432  N   PHE A  86     -29.349   6.189 -60.241  1.00 14.69           N  
ANISOU  432  N   PHE A  86     2029   1875   1677   -195   -264     22       N  
ATOM    433  CA  PHE A  86     -30.663   6.493 -60.797  1.00 14.89           C  
ANISOU  433  CA  PHE A  86     2051   1913   1693   -217   -315     39       C  
ATOM    434  C   PHE A  86     -30.797   7.978 -61.118  1.00 17.78           C  
ANISOU  434  C   PHE A  86     2407   2289   2058   -212   -343     76       C  
ATOM    435  O   PHE A  86     -31.459   8.338 -62.097  1.00 14.20           O  
ANISOU  435  O   PHE A  86     1968   1851   1576   -234   -383     93       O  
ATOM    436  CB  PHE A  86     -31.758   6.021 -59.847  1.00 13.58           C  
ANISOU  436  CB  PHE A  86     1851   1740   1568   -212   -332     36       C  
ATOM    437  CG  PHE A  86     -32.089   4.578 -60.013  1.00 16.61           C  
ANISOU  437  CG  PHE A  86     2254   2116   1941   -234   -323      5       C  
ATOM    438  CD1 PHE A  86     -32.753   4.141 -61.153  1.00 15.43           C  
ANISOU  438  CD1 PHE A  86     2131   1978   1753   -272   -353     -3       C  
ATOM    439  CD2 PHE A  86     -31.714   3.650 -59.059  1.00 15.12           C  
ANISOU  439  CD2 PHE A  86     2062   1906   1777   -219   -288    -15       C  
ATOM    440  CE1 PHE A  86     -33.042   2.799 -61.333  1.00 21.16           C  
ANISOU  440  CE1 PHE A  86     2878   2692   2468   -297   -345    -35       C  
ATOM    441  CE2 PHE A  86     -31.996   2.320 -59.231  1.00 16.94           C  
ANISOU  441  CE2 PHE A  86     2314   2122   1999   -240   -278    -43       C  
ATOM    442  CZ  PHE A  86     -32.665   1.887 -60.372  1.00 19.46           C  
ANISOU  442  CZ  PHE A  86     2660   2452   2283   -281   -305    -55       C  
ATOM    443  N   MET A  87     -30.155   8.854 -60.337  1.00 14.81           N  
ANISOU  443  N   MET A  87     2009   1905   1713   -184   -325     89       N  
ATOM    444  CA  MET A  87     -30.144  10.266 -60.719  1.00 16.33           C  
ANISOU  444  CA  MET A  87     2199   2101   1904   -181   -347    124       C  
ATOM    445  C   MET A  87     -29.484  10.448 -62.074  1.00 18.59           C  
ANISOU  445  C   MET A  87     2532   2399   2134   -207   -341    130       C  
ATOM    446  O   MET A  87     -29.959  11.234 -62.901  1.00 18.80           O  
ANISOU  446  O   MET A  87     2572   2434   2138   -220   -377    161       O  
ATOM    447  CB  MET A  87     -29.437  11.116 -59.666  1.00 16.09           C  
ANISOU  447  CB  MET A  87     2143   2056   1913   -152   -324    131       C  
ATOM    448  CG  MET A  87     -30.143  11.111 -58.316  1.00 21.04           C  
ANISOU  448  CG  MET A  87     2729   2673   2591   -128   -330    127       C  
ATOM    449  SD  MET A  87     -29.259  12.169 -57.159  1.00 28.62           S  
ANISOU  449  SD  MET A  87     3668   3618   3589   -100   -305    131       S  
ATOM    450  CE  MET A  87     -30.212  11.926 -55.683  1.00 18.15           C  
ANISOU  450  CE  MET A  87     2304   2284   2309    -78   -309    121       C  
ATOM    451  N   LEU A  88     -28.392   9.714 -62.321  1.00 17.54           N  
ANISOU  451  N   LEU A  88     2422   2266   1977   -213   -294    103       N  
ATOM    452  CA  LEU A  88     -27.735   9.772 -63.621  1.00 20.00           C  
ANISOU  452  CA  LEU A  88     2780   2589   2230   -240   -279    103       C  
ATOM    453  C   LEU A  88     -28.697   9.413 -64.741  1.00 19.72           C  
ANISOU  453  C   LEU A  88     2778   2570   2145   -273   -319    107       C  
ATOM    454  O   LEU A  88     -28.747  10.101 -65.768  1.00 21.22           O  
ANISOU  454  O   LEU A  88     2999   2771   2291   -295   -339    133       O  
ATOM    455  CB  LEU A  88     -26.531   8.842 -63.649  1.00 16.64           C  
ANISOU  455  CB  LEU A  88     2368   2160   1793   -239   -219     66       C  
ATOM    456  CG  LEU A  88     -25.330   9.336 -62.874  1.00 18.99           C  
ANISOU  456  CG  LEU A  88     2639   2449   2127   -213   -179     67       C  
ATOM    457  CD1 LEU A  88     -24.275   8.238 -62.815  1.00 18.18           C  
ANISOU  457  CD1 LEU A  88     2542   2342   2023   -206   -125     29       C  
ATOM    458  CD2 LEU A  88     -24.810  10.607 -63.539  1.00 17.85           C  
ANISOU  458  CD2 LEU A  88     2508   2311   1962   -227   -177     97       C  
ATOM    459  N   ARG A  89     -29.461   8.329 -64.568  1.00 18.72           N  
ANISOU  459  N   ARG A  89     2648   2442   2023   -281   -333     82       N  
ATOM    460  CA  ARG A  89     -30.417   7.936 -65.601  1.00 21.23           C  
ANISOU  460  CA  ARG A  89     2995   2776   2295   -316   -377     82       C  
ATOM    461  C   ARG A  89     -31.380   9.070 -65.910  1.00 22.29           C  
ANISOU  461  C   ARG A  89     3115   2922   2432   -319   -441    129       C  
ATOM    462  O   ARG A  89     -31.682   9.343 -67.081  1.00 23.13           O  
ANISOU  462  O   ARG A  89     3259   3046   2483   -348   -474    147       O  
ATOM    463  CB  ARG A  89     -31.198   6.696 -65.174  1.00 21.42           C  
ANISOU  463  CB  ARG A  89     3006   2794   2337   -324   -386     51       C  
ATOM    464  CG  ARG A  89     -30.411   5.411 -65.306  1.00 21.88           C  
ANISOU  464  CG  ARG A  89     3098   2841   2376   -332   -333      4       C  
ATOM    465  CD  ARG A  89     -31.316   4.201 -65.177  1.00 23.47           C  
ANISOU  465  CD  ARG A  89     3299   3035   2584   -351   -350    -24       C  
ATOM    466  NE  ARG A  89     -30.522   2.985 -65.207  1.00 21.79           N  
ANISOU  466  NE  ARG A  89     3117   2803   2361   -354   -295    -69       N  
ATOM    467  CZ  ARG A  89     -31.007   1.768 -65.021  1.00 23.34           C  
ANISOU  467  CZ  ARG A  89     3320   2982   2565   -368   -292   -101       C  
ATOM    468  NH1 ARG A  89     -32.295   1.569 -64.786  1.00 22.38           N  
ANISOU  468  NH1 ARG A  89     3176   2865   2463   -386   -340    -94       N  
ATOM    469  NH2 ARG A  89     -30.179   0.727 -65.076  1.00 18.38           N  
ANISOU  469  NH2 ARG A  89     2722   2331   1930   -365   -239   -140       N  
ATOM    470  N   TYR A  90     -31.871   9.745 -64.873  1.00 17.64           N  
ANISOU  470  N   TYR A  90     2474   2322   1906   -287   -457    150       N  
ATOM    471  CA  TYR A  90     -32.739  10.889 -65.105  1.00 22.62           C  
ANISOU  471  CA  TYR A  90     3087   2958   2550   -281   -514    195       C  
ATOM    472  C   TYR A  90     -31.996  11.997 -65.839  1.00 21.32           C  
ANISOU  472  C   TYR A  90     2955   2793   2352   -285   -510    228       C  
ATOM    473  O   TYR A  90     -32.518  12.582 -66.797  1.00 21.57           O  
ANISOU  473  O   TYR A  90     3009   2837   2349   -302   -558    263       O  
ATOM    474  CB  TYR A  90     -33.299  11.404 -63.784  1.00 20.85           C  
ANISOU  474  CB  TYR A  90     2802   2718   2403   -243   -520    205       C  
ATOM    475  CG  TYR A  90     -34.135  12.640 -63.963  1.00 21.66           C  
ANISOU  475  CG  TYR A  90     2882   2819   2528   -230   -573    252       C  
ATOM    476  CD1 TYR A  90     -35.429  12.554 -64.447  1.00 20.62           C  
ANISOU  476  CD1 TYR A  90     2734   2702   2398   -242   -635    268       C  
ATOM    477  CD2 TYR A  90     -33.627  13.900 -63.666  1.00 25.48           C  
ANISOU  477  CD2 TYR A  90     3361   3284   3036   -206   -563    279       C  
ATOM    478  CE1 TYR A  90     -36.202  13.687 -64.623  1.00 24.33           C  
ANISOU  478  CE1 TYR A  90     3180   3169   2895   -225   -686    313       C  
ATOM    479  CE2 TYR A  90     -34.395  15.046 -63.848  1.00 25.84           C  
ANISOU  479  CE2 TYR A  90     3388   3322   3107   -191   -611    324       C  
ATOM    480  CZ  TYR A  90     -35.679  14.929 -64.325  1.00 24.75           C  
ANISOU  480  CZ  TYR A  90     3232   3199   2972   -198   -672    341       C  
ATOM    481  OH  TYR A  90     -36.444  16.054 -64.510  1.00 25.95           O  
ANISOU  481  OH  TYR A  90     3363   3343   3155   -178   -722    387       O  
ATOM    482  N   MET A  91     -30.781  12.319 -65.385  1.00 21.30           N  
ANISOU  482  N   MET A  91     2955   2777   2361   -270   -455    221       N  
ATOM    483  CA  MET A  91     -30.054  13.436 -65.975  1.00 22.90           C  
ANISOU  483  CA  MET A  91     3185   2976   2541   -275   -446    253       C  
ATOM    484  C   MET A  91     -29.781  13.201 -67.454  1.00 23.27           C  
ANISOU  484  C   MET A  91     3294   3043   2504   -316   -448    258       C  
ATOM    485  O   MET A  91     -29.756  14.156 -68.237  1.00 26.06           O  
ANISOU  485  O   MET A  91     3676   3398   2826   -329   -470    299       O  
ATOM    486  CB  MET A  91     -28.746  13.685 -65.217  1.00 20.09           C  
ANISOU  486  CB  MET A  91     2816   2606   2213   -257   -385    238       C  
ATOM    487  CG  MET A  91     -28.940  14.295 -63.828  1.00 19.94           C  
ANISOU  487  CG  MET A  91     2744   2565   2268   -220   -387    243       C  
ATOM    488  SD  MET A  91     -30.041  15.747 -63.809  1.00 22.31           S  
ANISOU  488  SD  MET A  91     3025   2850   2601   -204   -447    296       S  
ATOM    489  CE  MET A  91     -29.101  16.912 -64.790  1.00 21.76           C  
ANISOU  489  CE  MET A  91     3001   2774   2493   -223   -435    333       C  
ATOM    490  N   TYR A  92     -29.605  11.948 -67.860  1.00 23.38           N  
ANISOU  490  N   TYR A  92     3334   3070   2480   -338   -426    216       N  
ATOM    491  CA  TYR A  92     -29.359  11.666 -69.269  1.00 27.30           C  
ANISOU  491  CA  TYR A  92     3895   3586   2890   -380   -424    214       C  
ATOM    492  C   TYR A  92     -30.650  11.569 -70.066  1.00 29.46           C  
ANISOU  492  C   TYR A  92     4187   3880   3127   -405   -499    234       C  
ATOM    493  O   TYR A  92     -30.693  11.979 -71.229  1.00 35.94           O  
ANISOU  493  O   TYR A  92     5059   4717   3881   -436   -523    260       O  
ATOM    494  CB  TYR A  92     -28.569  10.373 -69.422  1.00 25.02           C  
ANISOU  494  CB  TYR A  92     3631   3301   2576   -393   -363    158       C  
ATOM    495  CG  TYR A  92     -27.087  10.556 -69.263  1.00 23.04           C  
ANISOU  495  CG  TYR A  92     3384   3042   2330   -383   -289    145       C  
ATOM    496  CD1 TYR A  92     -26.344  11.229 -70.226  1.00 23.00           C  
ANISOU  496  CD1 TYR A  92     3422   3046   2271   -407   -265    165       C  
ATOM    497  CD2 TYR A  92     -26.431  10.065 -68.149  1.00 19.87           C  
ANISOU  497  CD2 TYR A  92     2940   2624   1987   -351   -244    115       C  
ATOM    498  CE1 TYR A  92     -24.973  11.410 -70.079  1.00 23.19           C  
ANISOU  498  CE1 TYR A  92     3442   3064   2305   -400   -194    153       C  
ATOM    499  CE2 TYR A  92     -25.071  10.234 -67.990  1.00 21.50           C  
ANISOU  499  CE2 TYR A  92     3142   2824   2203   -342   -180    104       C  
ATOM    500  CZ  TYR A  92     -24.342  10.897 -68.956  1.00 22.16           C  
ANISOU  500  CZ  TYR A  92     3264   2919   2238   -367   -154    121       C  
ATOM    501  OH  TYR A  92     -22.984  11.054 -68.776  1.00 18.14           O  
ANISOU  501  OH  TYR A  92     2742   2406   1745   -360    -88    109       O  
ATOM    502  N   ASN A  93     -31.705  11.032 -69.468  1.00 29.12           N  
ANISOU  502  N   ASN A  93     4103   3836   3125   -395   -538    222       N  
ATOM    503  CA  ASN A  93     -32.893  10.623 -70.206  1.00 30.11           C  
ANISOU  503  CA  ASN A  93     4241   3982   3216   -425   -605    228       C  
ATOM    504  C   ASN A  93     -34.102  11.437 -69.767  1.00 27.67           C  
ANISOU  504  C   ASN A  93     3879   3672   2964   -402   -675    271       C  
ATOM    505  O   ASN A  93     -35.251  11.008 -69.874  1.00 36.96           O  
ANISOU  505  O   ASN A  93     5034   4862   4148   -414   -731    270       O  
ATOM    506  CB  ASN A  93     -33.096   9.122 -70.035  1.00 30.34           C  
ANISOU  506  CB  ASN A  93     4273   4014   3242   -442   -587    171       C  
ATOM    507  CG  ASN A  93     -31.825   8.337 -70.364  1.00 37.78           C  
ANISOU  507  CG  ASN A  93     5262   4950   4141   -456   -511    126       C  
ATOM    508  OD1 ASN A  93     -31.247   7.655 -69.505  1.00 33.85           O  
ANISOU  508  OD1 ASN A  93     4743   4434   3685   -434   -457     91       O  
ATOM    509  ND2 ASN A  93     -31.362   8.466 -71.602  1.00 36.26           N  
ANISOU  509  ND2 ASN A  93     5136   4775   3868   -490   -504    130       N  
ATOM    510  N   GLN A  94     -33.812  12.651 -69.317  1.00 31.89           N  
ANISOU  510  N   GLN A  94     4391   4188   3536   -369   -670    309       N  
ATOM    511  CA  GLN A  94     -34.789  13.556 -68.733  1.00 34.34           C  
ANISOU  511  CA  GLN A  94     4646   4488   3912   -337   -721    348       C  
ATOM    512  C   GLN A  94     -36.002  13.772 -69.627  1.00 42.29           C  
ANISOU  512  C   GLN A  94     5656   5517   4895   -355   -808    384       C  
ATOM    513  O   GLN A  94     -37.138  13.827 -69.144  1.00 39.87           O  
ANISOU  513  O   GLN A  94     5293   5211   4644   -337   -855    394       O  
ATOM    514  CB  GLN A  94     -34.076  14.873 -68.482  1.00 35.15           C  
ANISOU  514  CB  GLN A  94     4750   4567   4037   -311   -699    384       C  
ATOM    515  CG  GLN A  94     -34.773  15.841 -67.638  1.00 38.60           C  
ANISOU  515  CG  GLN A  94     5130   4982   4553   -269   -727    414       C  
ATOM    516  CD  GLN A  94     -33.783  16.837 -67.147  1.00 38.00           C  
ANISOU  516  CD  GLN A  94     5058   4877   4502   -247   -681    427       C  
ATOM    517  OE1 GLN A  94     -32.584  16.554 -67.125  1.00 39.33           O  
ANISOU  517  OE1 GLN A  94     5255   5045   4644   -259   -621    402       O  
ATOM    518  NE2 GLN A  94     -34.252  18.010 -66.757  1.00 34.72           N  
ANISOU  518  NE2 GLN A  94     4615   4438   4140   -215   -709    466       N  
ATOM    519  N   GLU A  95     -35.778  13.933 -70.931  1.00 46.93           N  
ANISOU  519  N   GLU A  95     6309   6123   5399   -391   -832    406       N  
ATOM    520  CA  GLU A  95     -36.877  14.257 -71.830  1.00 49.41           C  
ANISOU  520  CA  GLU A  95     6629   6458   5685   -408   -923    448       C  
ATOM    521  C   GLU A  95     -37.854  13.102 -71.988  1.00 47.02           C  
ANISOU  521  C   GLU A  95     6309   6182   5375   -436   -965    415       C  
ATOM    522  O   GLU A  95     -38.999  13.331 -72.392  1.00 46.29           O  
ANISOU  522  O   GLU A  95     6193   6106   5289   -441  -1048    447       O  
ATOM    523  CB  GLU A  95     -36.332  14.674 -73.198  1.00 57.26           C  
ANISOU  523  CB  GLU A  95     7707   7468   6582   -444   -936    479       C  
ATOM    524  CG  GLU A  95     -35.116  15.609 -73.146  1.00 64.06           C  
ANISOU  524  CG  GLU A  95     8599   8304   7437   -430   -877    501       C  
ATOM    525  CD  GLU A  95     -35.413  16.972 -72.528  1.00 69.18           C  
ANISOU  525  CD  GLU A  95     9203   8922   8160   -384   -900    553       C  
ATOM    526  OE1 GLU A  95     -36.583  17.253 -72.186  1.00 68.20           O  
ANISOU  526  OE1 GLU A  95     9025   8796   8092   -358   -963    577       O  
ATOM    527  OE2 GLU A  95     -34.463  17.773 -72.384  1.00 76.03           O  
ANISOU  527  OE2 GLU A  95    10090   9766   9033   -373   -853    570       O  
ATOM    528  N   SER A  96     -37.436  11.883 -71.656  1.00 38.99           N  
ANISOU  528  N   SER A  96     5300   5165   4350   -453   -911    354       N  
ATOM    529  CA  SER A  96     -38.242  10.693 -71.871  1.00 37.94           C  
ANISOU  529  CA  SER A  96     5161   5053   4203   -487   -942    317       C  
ATOM    530  C   SER A  96     -39.118  10.382 -70.666  1.00 36.47           C  
ANISOU  530  C   SER A  96     4889   4856   4112   -460   -949    303       C  
ATOM    531  O   SER A  96     -38.679  10.477 -69.517  1.00 37.15           O  
ANISOU  531  O   SER A  96     4940   4917   4260   -422   -892    289       O  
ATOM    532  CB  SER A  96     -37.348   9.493 -72.171  1.00 36.00           C  
ANISOU  532  CB  SER A  96     4972   4807   3899   -521   -877    256       C  
ATOM    533  OG  SER A  96     -38.040   8.280 -71.908  1.00 41.69           O  
ANISOU  533  OG  SER A  96     5671   5532   4636   -543   -887    212       O  
ATOM    534  N   VAL A  97     -40.361   9.978 -70.944  1.00 39.37           N  
ANISOU  534  N   VAL A  97     5226   5245   4488   -482  -1019    305       N  
ATOM    535  CA  VAL A  97     -41.270   9.513 -69.898  1.00 35.81           C  
ANISOU  535  CA  VAL A  97     4697   4789   4122   -467  -1024    287       C  
ATOM    536  C   VAL A  97     -40.708   8.278 -69.201  1.00 34.35           C  
ANISOU  536  C   VAL A  97     4521   4587   3944   -477   -949    226       C  
ATOM    537  O   VAL A  97     -40.954   8.059 -68.008  1.00 31.87           O  
ANISOU  537  O   VAL A  97     4150   4256   3703   -450   -917    211       O  
ATOM    538  CB  VAL A  97     -42.663   9.234 -70.504  1.00 40.10           C  
ANISOU  538  CB  VAL A  97     5209   5364   4664   -499  -1116    299       C  
ATOM    539  CG1 VAL A  97     -43.565   8.532 -69.497  1.00 40.96           C  
ANISOU  539  CG1 VAL A  97     5241   5468   4853   -495  -1112    272       C  
ATOM    540  CG2 VAL A  97     -43.314  10.530 -71.002  1.00 41.66           C  
ANISOU  540  CG2 VAL A  97     5381   5567   4881   -469  -1173    361       C  
ATOM    541  N   ASP A  98     -39.951   7.453 -69.922  1.00 32.48           N  
ANISOU  541  N   ASP A  98     4356   4354   3632   -514   -918    189       N  
ATOM    542  CA  ASP A  98     -39.375   6.231 -69.363  1.00 35.40           C  
ANISOU  542  CA  ASP A  98     4741   4704   4007   -523   -849    132       C  
ATOM    543  C   ASP A  98     -37.918   6.411 -68.955  1.00 31.06           C  
ANISOU  543  C   ASP A  98     4221   4129   3451   -493   -766    120       C  
ATOM    544  O   ASP A  98     -37.111   5.490 -69.127  1.00 28.96           O  
ANISOU  544  O   ASP A  98     4001   3853   3149   -510   -712     77       O  
ATOM    545  CB  ASP A  98     -39.506   5.081 -70.359  1.00 38.21           C  
ANISOU  545  CB  ASP A  98     5154   5073   4291   -583   -863     91       C  
ATOM    546  CG  ASP A  98     -40.948   4.671 -70.595  1.00 47.56           C  
ANISOU  546  CG  ASP A  98     6301   6279   5490   -618   -940     91       C  
ATOM    547  OD1 ASP A  98     -41.803   4.975 -69.733  1.00 49.79           O  
ANISOU  547  OD1 ASP A  98     6505   6560   5853   -593   -963    111       O  
ATOM    548  OD2 ASP A  98     -41.224   4.036 -71.639  1.00 53.13           O  
ANISOU  548  OD2 ASP A  98     7054   7004   6128   -672   -977     70       O  
ATOM    549  N   TRP A  99     -37.546   7.575 -68.408  1.00 30.87           N  
ANISOU  549  N   TRP A  99     4170   4095   3464   -449   -753    157       N  
ATOM    550  CA  TRP A  99     -36.146   7.798 -68.055  1.00 27.66           C  
ANISOU  550  CA  TRP A  99     3788   3669   3053   -424   -680    148       C  
ATOM    551  C   TRP A  99     -35.623   6.756 -67.072  1.00 25.04           C  
ANISOU  551  C   TRP A  99     3445   3314   2755   -412   -615    101       C  
ATOM    552  O   TRP A  99     -34.412   6.519 -67.027  1.00 25.81           O  
ANISOU  552  O   TRP A  99     3574   3399   2834   -404   -554     80       O  
ATOM    553  CB  TRP A  99     -35.948   9.200 -67.465  1.00 21.96           C  
ANISOU  553  CB  TRP A  99     3031   2936   2377   -381   -680    192       C  
ATOM    554  CG  TRP A  99     -36.737   9.437 -66.217  1.00 25.47           C  
ANISOU  554  CG  TRP A  99     3403   3369   2907   -346   -689    200       C  
ATOM    555  CD1 TRP A  99     -37.952  10.054 -66.122  1.00 22.90           C  
ANISOU  555  CD1 TRP A  99     3029   3051   2622   -336   -750    233       C  
ATOM    556  CD2 TRP A  99     -36.370   9.060 -64.880  1.00 24.29           C  
ANISOU  556  CD2 TRP A  99     3220   3197   2813   -317   -635    174       C  
ATOM    557  NE1 TRP A  99     -38.365  10.078 -64.816  1.00 23.39           N  
ANISOU  557  NE1 TRP A  99     3030   3098   2760   -304   -731    225       N  
ATOM    558  CE2 TRP A  99     -37.417   9.475 -64.032  1.00 21.51           C  
ANISOU  558  CE2 TRP A  99     2803   2841   2528   -293   -661    191       C  
ATOM    559  CE3 TRP A  99     -35.256   8.412 -64.318  1.00 20.00           C  
ANISOU  559  CE3 TRP A  99     2695   2637   2267   -309   -566    140       C  
ATOM    560  CZ2 TRP A  99     -37.385   9.273 -62.656  1.00 22.93           C  
ANISOU  560  CZ2 TRP A  99     2943   3003   2767   -265   -620    174       C  
ATOM    561  CZ3 TRP A  99     -35.231   8.197 -62.947  1.00 22.81           C  
ANISOU  561  CZ3 TRP A  99     3009   2974   2682   -279   -533    126       C  
ATOM    562  CH2 TRP A  99     -36.286   8.635 -62.131  1.00 21.55           C  
ANISOU  562  CH2 TRP A  99     2792   2813   2582   -260   -559    143       C  
ATOM    563  N   VAL A 100     -36.502   6.127 -66.287  1.00 23.96           N  
ANISOU  563  N   VAL A 100     3263   3172   2670   -410   -627     87       N  
ATOM    564  CA  VAL A 100     -36.033   5.238 -65.231  1.00 24.59           C  
ANISOU  564  CA  VAL A 100     3330   3226   2786   -394   -568     52       C  
ATOM    565  C   VAL A 100     -35.291   4.047 -65.806  1.00 27.27           C  
ANISOU  565  C   VAL A 100     3729   3557   3077   -422   -527      6       C  
ATOM    566  O   VAL A 100     -34.485   3.423 -65.108  1.00 29.23           O  
ANISOU  566  O   VAL A 100     3980   3781   3344   -402   -469    -20       O  
ATOM    567  CB  VAL A 100     -37.199   4.792 -64.326  1.00 26.38           C  
ANISOU  567  CB  VAL A 100     3501   3449   3074   -393   -588     47       C  
ATOM    568  CG1 VAL A 100     -37.992   3.657 -64.966  1.00 24.95           C  
ANISOU  568  CG1 VAL A 100     3337   3276   2868   -443   -617     19       C  
ATOM    569  CG2 VAL A 100     -36.671   4.388 -62.955  1.00 28.10           C  
ANISOU  569  CG2 VAL A 100     3696   3640   3341   -360   -528     31       C  
ATOM    570  N   GLY A 101     -35.523   3.730 -67.069  1.00 25.92           N  
ANISOU  570  N   GLY A 101     3605   3404   2841   -465   -557     -4       N  
ATOM    571  CA  GLY A 101     -34.702   2.777 -67.784  1.00 27.93           C  
ANISOU  571  CA  GLY A 101     3923   3649   3039   -490   -514    -47       C  
ATOM    572  C   GLY A 101     -35.452   1.496 -68.102  1.00 29.02           C  
ANISOU  572  C   GLY A 101     4081   3783   3162   -534   -531    -87       C  
ATOM    573  O   GLY A 101     -36.535   1.214 -67.584  1.00 29.14           O  
ANISOU  573  O   GLY A 101     4052   3799   3220   -542   -567    -84       O  
ATOM    574  N   ASP A 102     -34.851   0.732 -69.008  1.00 30.02           N  
ANISOU  574  N   ASP A 102     4274   3905   3227   -564   -502   -127       N  
ATOM    575  CA  ASP A 102     -35.333  -0.611 -69.277  1.00 25.54           C  
ANISOU  575  CA  ASP A 102     3735   3324   2645   -605   -503   -174       C  
ATOM    576  C   ASP A 102     -35.254  -1.444 -68.007  1.00 24.89           C  
ANISOU  576  C   ASP A 102     3620   3204   2634   -579   -459   -194       C  
ATOM    577  O   ASP A 102     -34.271  -1.376 -67.266  1.00 23.40           O  
ANISOU  577  O   ASP A 102     3421   2994   2476   -535   -402   -193       O  
ATOM    578  CB  ASP A 102     -34.502  -1.262 -70.377  1.00 25.56           C  
ANISOU  578  CB  ASP A 102     3819   3321   2571   -634   -463   -218       C  
ATOM    579  CG  ASP A 102     -35.089  -2.585 -70.825  1.00 31.85           C  
ANISOU  579  CG  ASP A 102     4653   4104   3344   -685   -472   -269       C  
ATOM    580  OD1 ASP A 102     -36.025  -2.565 -71.651  1.00 45.34           O  
ANISOU  580  OD1 ASP A 102     6378   5840   5009   -735   -538   -268       O  
ATOM    581  OD2 ASP A 102     -34.646  -3.640 -70.336  1.00 26.92           O  
ANISOU  581  OD2 ASP A 102     4042   3439   2747   -677   -416   -310       O  
ATOM    582  N   TYR A 103     -36.294  -2.240 -67.754  1.00 22.91           N  
ANISOU  582  N   TYR A 103     3352   2945   2408   -609   -488   -210       N  
ATOM    583  CA  TYR A 103     -36.356  -2.991 -66.507  1.00 22.98           C  
ANISOU  583  CA  TYR A 103     3329   2919   2485   -588   -452   -222       C  
ATOM    584  C   TYR A 103     -35.352  -4.131 -66.453  1.00 25.73           C  
ANISOU  584  C   TYR A 103     3727   3224   2825   -582   -382   -268       C  
ATOM    585  O   TYR A 103     -35.220  -4.763 -65.395  1.00 24.48           O  
ANISOU  585  O   TYR A 103     3550   3032   2721   -559   -346   -274       O  
ATOM    586  CB  TYR A 103     -37.776  -3.518 -66.270  1.00 20.64           C  
ANISOU  586  CB  TYR A 103     2999   2625   2219   -627   -500   -226       C  
ATOM    587  CG  TYR A 103     -38.648  -2.518 -65.530  1.00 23.03           C  
ANISOU  587  CG  TYR A 103     3224   2952   2575   -605   -542   -178       C  
ATOM    588  CD1 TYR A 103     -38.628  -1.170 -65.871  1.00 25.01           C  
ANISOU  588  CD1 TYR A 103     3455   3236   2812   -584   -576   -136       C  
ATOM    589  CD2 TYR A 103     -39.487  -2.922 -64.489  1.00 26.33           C  
ANISOU  589  CD2 TYR A 103     3589   3357   3057   -606   -543   -174       C  
ATOM    590  CE1 TYR A 103     -39.415  -0.245 -65.198  1.00 27.66           C  
ANISOU  590  CE1 TYR A 103     3720   3588   3200   -560   -611    -95       C  
ATOM    591  CE2 TYR A 103     -40.279  -2.000 -63.811  1.00 25.21           C  
ANISOU  591  CE2 TYR A 103     3376   3237   2967   -584   -575   -134       C  
ATOM    592  CZ  TYR A 103     -40.238  -0.665 -64.171  1.00 27.72           C  
ANISOU  592  CZ  TYR A 103     3675   3585   3273   -560   -609    -96       C  
ATOM    593  OH  TYR A 103     -41.021   0.256 -63.510  1.00 30.81           O  
ANISOU  593  OH  TYR A 103     3996   3993   3719   -535   -637    -58       O  
ATOM    594  N   ASN A 104     -34.629  -4.391 -67.543  1.00 20.35           N  
ANISOU  594  N   ASN A 104     3110   2543   2080   -600   -359   -298       N  
ATOM    595  CA  ASN A 104     -33.594  -5.414 -67.560  1.00 22.59           C  
ANISOU  595  CA  ASN A 104     3441   2785   2359   -588   -287   -343       C  
ATOM    596  C   ASN A 104     -32.192  -4.824 -67.600  1.00 25.85           C  
ANISOU  596  C   ASN A 104     3861   3198   2761   -543   -234   -335       C  
ATOM    597  O   ASN A 104     -31.215  -5.577 -67.688  1.00 25.95           O  
ANISOU  597  O   ASN A 104     3909   3179   2772   -527   -172   -371       O  
ATOM    598  CB  ASN A 104     -33.803  -6.358 -68.748  1.00 28.36           C  
ANISOU  598  CB  ASN A 104     4242   3507   3027   -646   -289   -396       C  
ATOM    599  CG  ASN A 104     -33.079  -7.672 -68.569  1.00 35.00           C  
ANISOU  599  CG  ASN A 104     5124   4292   3884   -638   -220   -446       C  
ATOM    600  OD1 ASN A 104     -33.165  -8.303 -67.515  1.00 35.26           O  
ANISOU  600  OD1 ASN A 104     5130   4287   3979   -616   -200   -446       O  
ATOM    601  ND2 ASN A 104     -32.323  -8.071 -69.581  1.00 31.55           N  
ANISOU  601  ND2 ASN A 104     4752   3846   3388   -652   -180   -489       N  
ATOM    602  N   GLU A 105     -32.066  -3.503 -67.526  1.00 22.48           N  
ANISOU  602  N   GLU A 105     3401   2806   2334   -521   -257   -289       N  
ATOM    603  CA  GLU A 105     -30.781  -2.825 -67.613  1.00 21.62           C  
ANISOU  603  CA  GLU A 105     3296   2702   2215   -484   -211   -279       C  
ATOM    604  C   GLU A 105     -30.114  -2.786 -66.242  1.00 22.73           C  
ANISOU  604  C   GLU A 105     3389   2819   2428   -427   -174   -263       C  
ATOM    605  O   GLU A 105     -30.730  -2.328 -65.269  1.00 21.25           O  
ANISOU  605  O   GLU A 105     3149   2637   2289   -410   -204   -230       O  
ATOM    606  CB  GLU A 105     -30.952  -1.407 -68.138  1.00 26.39           C  
ANISOU  606  CB  GLU A 105     3889   3350   2789   -489   -253   -234       C  
ATOM    607  CG  GLU A 105     -29.702  -0.831 -68.780  1.00 32.74           C  
ANISOU  607  CG  GLU A 105     4721   4164   3553   -477   -207   -234       C  
ATOM    608  CD  GLU A 105     -29.264  -1.617 -70.010  1.00 42.41           C  
ANISOU  608  CD  GLU A 105     6020   5386   4708   -513   -172   -282       C  
ATOM    609  OE1 GLU A 105     -30.135  -1.978 -70.835  1.00 44.96           O  
ANISOU  609  OE1 GLU A 105     6382   5721   4981   -563   -214   -298       O  
ATOM    610  OE2 GLU A 105     -28.048  -1.882 -70.154  1.00 42.93           O  
ANISOU  610  OE2 GLU A 105     6106   5437   4769   -493   -102   -307       O  
ATOM    611  N   PRO A 106     -28.869  -3.240 -66.129  1.00 22.52           N  
ANISOU  611  N   PRO A 106     3377   2768   2410   -398   -109   -286       N  
ATOM    612  CA  PRO A 106     -28.142  -3.087 -64.861  1.00 20.22           C  
ANISOU  612  CA  PRO A 106     3040   2461   2183   -343    -80   -267       C  
ATOM    613  C   PRO A 106     -27.931  -1.616 -64.534  1.00 19.62           C  
ANISOU  613  C   PRO A 106     2921   2416   2117   -321   -100   -221       C  
ATOM    614  O   PRO A 106     -27.891  -0.762 -65.416  1.00 19.84           O  
ANISOU  614  O   PRO A 106     2964   2474   2100   -340   -115   -208       O  
ATOM    615  CB  PRO A 106     -26.807  -3.798 -65.122  1.00 23.51           C  
ANISOU  615  CB  PRO A 106     3484   2851   2598   -320     -9   -303       C  
ATOM    616  CG  PRO A 106     -27.064  -4.690 -66.328  1.00 26.50           C  
ANISOU  616  CG  PRO A 106     3927   3219   2921   -365      2   -350       C  
ATOM    617  CD  PRO A 106     -28.082  -3.953 -67.151  1.00 26.25           C  
ANISOU  617  CD  PRO A 106     3909   3228   2837   -412    -59   -333       C  
ATOM    618  N   LEU A 107     -27.793  -1.329 -63.245  1.00 18.14           N  
ANISOU  618  N   LEU A 107     2685   2220   1986   -283   -100   -197       N  
ATOM    619  CA  LEU A 107     -27.569   0.030 -62.769  1.00 17.38           C  
ANISOU  619  CA  LEU A 107     2549   2148   1908   -260   -116   -156       C  
ATOM    620  C   LEU A 107     -26.071   0.314 -62.713  1.00 17.21           C  
ANISOU  620  C   LEU A 107     2521   2124   1893   -229    -66   -159       C  
ATOM    621  O   LEU A 107     -25.338  -0.343 -61.963  1.00 16.04           O  
ANISOU  621  O   LEU A 107     2360   1952   1782   -197    -31   -172       O  
ATOM    622  CB  LEU A 107     -28.202   0.205 -61.392  1.00 13.97           C  
ANISOU  622  CB  LEU A 107     2069   1709   1529   -238   -140   -133       C  
ATOM    623  CG  LEU A 107     -28.111   1.618 -60.839  1.00 16.64           C  
ANISOU  623  CG  LEU A 107     2367   2067   1887   -217   -159    -94       C  
ATOM    624  CD1 LEU A 107     -28.957   2.552 -61.677  1.00 18.22           C  
ANISOU  624  CD1 LEU A 107     2570   2294   2057   -245   -205    -72       C  
ATOM    625  CD2 LEU A 107     -28.552   1.636 -59.385  1.00 16.41           C  
ANISOU  625  CD2 LEU A 107     2298   2028   1910   -192   -169    -79       C  
ATOM    626  N   THR A 108     -25.612   1.304 -63.477  1.00 16.50           N  
ANISOU  626  N   THR A 108     2439   2059   1770   -238    -64   -145       N  
ATOM    627  CA  THR A 108     -24.184   1.589 -63.555  1.00 18.90           C  
ANISOU  627  CA  THR A 108     2737   2365   2081   -216    -13   -150       C  
ATOM    628  C   THR A 108     -23.914   3.065 -63.279  1.00 17.27           C  
ANISOU  628  C   THR A 108     2498   2179   1885   -207    -30   -110       C  
ATOM    629  O   THR A 108     -24.829   3.882 -63.176  1.00 17.37           O  
ANISOU  629  O   THR A 108     2500   2205   1896   -218    -78    -81       O  
ATOM    630  CB  THR A 108     -23.605   1.219 -64.927  1.00 20.80           C  
ANISOU  630  CB  THR A 108     3028   2611   2265   -241     27   -180       C  
ATOM    631  OG1 THR A 108     -24.258   1.998 -65.938  1.00 24.94           O  
ANISOU  631  OG1 THR A 108     3581   3162   2733   -281     -8   -162       O  
ATOM    632  CG2 THR A 108     -23.785  -0.266 -65.216  1.00 22.62           C  
ANISOU  632  CG2 THR A 108     3294   2813   2486   -250     49   -225       C  
ATOM    633  N   GLY A 109     -22.627   3.394 -63.175  1.00 17.71           N  
ANISOU  633  N   GLY A 109     2537   2237   1956   -186     13   -112       N  
ATOM    634  CA  GLY A 109     -22.187   4.753 -62.908  1.00 17.81           C  
ANISOU  634  CA  GLY A 109     2520   2266   1982   -180      5    -79       C  
ATOM    635  C   GLY A 109     -21.233   4.791 -61.734  1.00 17.43           C  
ANISOU  635  C   GLY A 109     2425   2208   1991   -141     26    -78       C  
ATOM    636  O   GLY A 109     -20.208   4.099 -61.742  1.00 18.98           O  
ANISOU  636  O   GLY A 109     2616   2396   2201   -123     72   -102       O  
ATOM    637  N   PHE A 110     -21.557   5.579 -60.710  1.00 15.43           N  
ANISOU  637  N   PHE A 110     2137   1956   1771   -126     -7    -51       N  
ATOM    638  CA  PHE A 110     -20.828   5.480 -59.452  1.00 16.23           C  
ANISOU  638  CA  PHE A 110     2195   2048   1923    -91      2    -51       C  
ATOM    639  C   PHE A 110     -20.903   4.044 -58.945  1.00 13.84           C  
ANISOU  639  C   PHE A 110     1897   1724   1639    -71     14    -74       C  
ATOM    640  O   PHE A 110     -21.946   3.392 -59.043  1.00 15.69           O  
ANISOU  640  O   PHE A 110     2154   1948   1859    -83     -5    -81       O  
ATOM    641  CB  PHE A 110     -21.415   6.429 -58.405  1.00 13.59           C  
ANISOU  641  CB  PHE A 110     1832   1716   1615    -83    -39    -23       C  
ATOM    642  CG  PHE A 110     -21.405   7.871 -58.809  1.00 13.74           C  
ANISOU  642  CG  PHE A 110     1848   1748   1623   -100    -52      2       C  
ATOM    643  CD1 PHE A 110     -20.219   8.576 -58.878  1.00 15.54           C  
ANISOU  643  CD1 PHE A 110     2059   1984   1862    -99    -27      6       C  
ATOM    644  CD2 PHE A 110     -22.586   8.536 -59.083  1.00 16.69           C  
ANISOU  644  CD2 PHE A 110     2235   2126   1982   -116    -92     23       C  
ATOM    645  CE1 PHE A 110     -20.212   9.902 -59.216  1.00 14.59           C  
ANISOU  645  CE1 PHE A 110     1939   1871   1734   -116    -38     31       C  
ATOM    646  CE2 PHE A 110     -22.577   9.885 -59.436  1.00 13.55           C  
ANISOU  646  CE2 PHE A 110     1837   1734   1578   -129   -105     49       C  
ATOM    647  CZ  PHE A 110     -21.394  10.558 -59.497  1.00 13.73           C  
ANISOU  647  CZ  PHE A 110     1847   1760   1608   -130    -78     54       C  
ATOM    648  N   SER A 111     -19.797   3.545 -58.412  1.00 13.60           N  
ANISOU  648  N   SER A 111     1842   1684   1640    -41     44    -85       N  
ATOM    649  CA  SER A 111     -19.760   2.150 -57.987  1.00 15.29           C  
ANISOU  649  CA  SER A 111     2063   1872   1873    -19     58   -106       C  
ATOM    650  C   SER A 111     -20.633   1.943 -56.752  1.00 15.09           C  
ANISOU  650  C   SER A 111     2028   1835   1870     -8     20    -90       C  
ATOM    651  O   SER A 111     -20.464   2.619 -55.733  1.00 16.77           O  
ANISOU  651  O   SER A 111     2209   2056   2108      8      0    -69       O  
ATOM    652  CB  SER A 111     -18.321   1.721 -57.701  1.00 16.87           C  
ANISOU  652  CB  SER A 111     2236   2066   2109     15     96   -117       C  
ATOM    653  OG  SER A 111     -18.299   0.407 -57.194  1.00 17.63           O  
ANISOU  653  OG  SER A 111     2339   2131   2228     41    105   -131       O  
ATOM    654  N   TRP A 112     -21.558   0.993 -56.840  1.00 14.67           N  
ANISOU  654  N   TRP A 112     2003   1763   1807    -18     13   -101       N  
ATOM    655  CA  TRP A 112     -22.391   0.604 -55.716  1.00 16.38           C  
ANISOU  655  CA  TRP A 112     2215   1966   2044    -10    -13    -89       C  
ATOM    656  C   TRP A 112     -22.364  -0.916 -55.612  1.00 14.83           C  
ANISOU  656  C   TRP A 112     2042   1734   1859      1      8   -109       C  
ATOM    657  O   TRP A 112     -22.142  -1.607 -56.600  1.00 14.98           O  
ANISOU  657  O   TRP A 112     2090   1741   1861     -9     35   -136       O  
ATOM    658  CB  TRP A 112     -23.830   1.106 -55.892  1.00 12.20           C  
ANISOU  658  CB  TRP A 112     1694   1448   1495    -42    -49    -78       C  
ATOM    659  CG  TRP A 112     -24.492   0.410 -57.033  1.00 14.79           C  
ANISOU  659  CG  TRP A 112     2060   1769   1791    -74    -46    -99       C  
ATOM    660  CD1 TRP A 112     -24.413   0.742 -58.355  1.00 15.27           C  
ANISOU  660  CD1 TRP A 112     2144   1845   1813    -99    -41   -110       C  
ATOM    661  CD2 TRP A 112     -25.283  -0.781 -56.961  1.00 13.40           C  
ANISOU  661  CD2 TRP A 112     1907   1568   1616    -86    -48   -115       C  
ATOM    662  NE1 TRP A 112     -25.128  -0.161 -59.108  1.00 15.70           N  
ANISOU  662  NE1 TRP A 112     2235   1887   1842   -128    -42   -132       N  
ATOM    663  CE2 TRP A 112     -25.666  -1.109 -58.277  1.00 14.82           C  
ANISOU  663  CE2 TRP A 112     2123   1751   1758   -121    -46   -137       C  
ATOM    664  CE3 TRP A 112     -25.721  -1.592 -55.910  1.00 13.54           C  
ANISOU  664  CE3 TRP A 112     1921   1561   1662    -76    -50   -111       C  
ATOM    665  CZ2 TRP A 112     -26.463  -2.221 -58.571  1.00 14.49           C  
ANISOU  665  CZ2 TRP A 112     2112   1687   1708   -146    -48   -159       C  
ATOM    666  CZ3 TRP A 112     -26.503  -2.707 -56.204  1.00 16.32           C  
ANISOU  666  CZ3 TRP A 112     2304   1889   2008   -100    -49   -130       C  
ATOM    667  CH2 TRP A 112     -26.862  -3.007 -57.528  1.00 14.72           C  
ANISOU  667  CH2 TRP A 112     2134   1689   1769   -135    -49   -155       C  
ATOM    668  N   ARG A 113     -22.602  -1.431 -54.413  1.00 14.33           N  
ANISOU  668  N   ARG A 113     1970   1652   1822     20     -3    -96       N  
ATOM    669  CA  ARG A 113     -22.606  -2.873 -54.197  1.00 15.77           C  
ANISOU  669  CA  ARG A 113     2177   1795   2019     31     15   -110       C  
ATOM    670  C   ARG A 113     -23.060  -3.134 -52.774  1.00 15.16           C  
ANISOU  670  C   ARG A 113     2090   1705   1964     45     -5    -86       C  
ATOM    671  O   ARG A 113     -23.044  -2.238 -51.923  1.00 12.93           O  
ANISOU  671  O   ARG A 113     1780   1445   1688     54    -27    -62       O  
ATOM    672  CB  ARG A 113     -21.221  -3.502 -54.414  1.00 16.22           C  
ANISOU  672  CB  ARG A 113     2231   1834   2097     66     52   -125       C  
ATOM    673  CG  ARG A 113     -20.136  -2.917 -53.492  1.00 17.10           C  
ANISOU  673  CG  ARG A 113     2298   1960   2238    103     46   -103       C  
ATOM    674  CD  ARG A 113     -18.941  -3.870 -53.274  1.00 17.39           C  
ANISOU  674  CD  ARG A 113     2327   1969   2311    147     74   -111       C  
ATOM    675  NE  ARG A 113     -17.851  -3.202 -52.562  1.00 18.00           N  
ANISOU  675  NE  ARG A 113     2357   2068   2415    178     65    -92       N  
ATOM    676  CZ  ARG A 113     -17.797  -3.027 -51.248  1.00 18.82           C  
ANISOU  676  CZ  ARG A 113     2440   2175   2535    197     33    -63       C  
ATOM    677  NH1 ARG A 113     -18.723  -3.520 -50.443  1.00 17.05           N  
ANISOU  677  NH1 ARG A 113     2240   1932   2305    192     13    -48       N  
ATOM    678  NH2 ARG A 113     -16.792  -2.324 -50.725  1.00 19.69           N  
ANISOU  678  NH2 ARG A 113     2506   2309   2665    218     22    -49       N  
ATOM    679  N   GLY A 114     -23.453  -4.375 -52.528  1.00 16.87           N  
ANISOU  679  N   GLY A 114     2334   1884   2190     45      4    -92       N  
ATOM    680  CA  GLY A 114     -23.714  -4.842 -51.188  1.00 14.58           C  
ANISOU  680  CA  GLY A 114     2044   1576   1921     60     -7    -68       C  
ATOM    681  C   GLY A 114     -22.406  -5.120 -50.479  1.00 15.99           C  
ANISOU  681  C   GLY A 114     2206   1742   2126    108      1    -56       C  
ATOM    682  O   GLY A 114     -21.323  -4.703 -50.908  1.00 16.12           O  
ANISOU  682  O   GLY A 114     2202   1774   2150    129     12    -63       O  
ATOM    683  N   GLY A 115     -22.510  -5.865 -49.399  1.00 16.73           N  
ANISOU  683  N   GLY A 115     2311   1809   2235    125     -5    -36       N  
ATOM    684  CA  GLY A 115     -21.354  -6.099 -48.542  1.00 16.34           C  
ANISOU  684  CA  GLY A 115     2245   1751   2213    172     -8    -16       C  
ATOM    685  C   GLY A 115     -21.298  -5.104 -47.407  1.00 16.25           C  
ANISOU  685  C   GLY A 115     2207   1774   2195    178    -39     12       C  
ATOM    686  O   GLY A 115     -21.799  -3.983 -47.494  1.00 18.03           O  
ANISOU  686  O   GLY A 115     2415   2035   2401    154    -52     11       O  
ATOM    687  N   SER A 116     -20.702  -5.537 -46.299  1.00 19.64           N  
ANISOU  687  N   SER A 116     2634   2190   2640    211    -52     38       N  
ATOM    688  CA  SER A 116     -20.712  -4.697 -45.111  1.00 21.53           C  
ANISOU  688  CA  SER A 116     2855   2459   2867    213    -82     64       C  
ATOM    689  C   SER A 116     -19.599  -3.653 -45.105  1.00 18.93           C  
ANISOU  689  C   SER A 116     2482   2166   2545    231    -97     63       C  
ATOM    690  O   SER A 116     -19.622  -2.764 -44.245  1.00 18.01           O  
ANISOU  690  O   SER A 116     2351   2078   2414    226   -122     78       O  
ATOM    691  CB  SER A 116     -20.598  -5.566 -43.861  1.00 21.17           C  
ANISOU  691  CB  SER A 116     2831   2386   2826    236    -96     95       C  
ATOM    692  OG  SER A 116     -19.402  -6.315 -43.928  1.00 18.96           O  
ANISOU  692  OG  SER A 116     2543   2083   2578    279    -93    101       O  
ATOM    693  N   GLU A 117     -18.644  -3.737 -46.026  1.00 16.88           N  
ANISOU  693  N   GLU A 117     2201   1905   2306    248    -79     46       N  
ATOM    694  CA  GLU A 117     -17.490  -2.843 -46.060  1.00 19.82           C  
ANISOU  694  CA  GLU A 117     2528   2310   2691    263    -88     45       C  
ATOM    695  C   GLU A 117     -17.733  -1.709 -47.042  1.00 18.76           C  
ANISOU  695  C   GLU A 117     2381   2206   2540    231    -78     24       C  
ATOM    696  O   GLU A 117     -18.217  -1.935 -48.155  1.00 17.62           O  
ANISOU  696  O   GLU A 117     2256   2052   2386    211    -52      3       O  
ATOM    697  CB  GLU A 117     -16.214  -3.585 -46.470  1.00 19.66           C  
ANISOU  697  CB  GLU A 117     2487   2273   2710    303    -70     39       C  
ATOM    698  CG  GLU A 117     -15.812  -4.720 -45.518  1.00 29.88           C  
ANISOU  698  CG  GLU A 117     3791   3534   4028    343    -84     64       C  
ATOM    699  CD  GLU A 117     -14.964  -4.232 -44.355  1.00 43.59           C  
ANISOU  699  CD  GLU A 117     5493   5296   5774    367   -126     92       C  
ATOM    700  OE1 GLU A 117     -13.721  -4.174 -44.522  1.00 50.15           O  
ANISOU  700  OE1 GLU A 117     6279   6137   6640    397   -127     90       O  
ATOM    701  OE2 GLU A 117     -15.532  -3.890 -43.285  1.00 38.57           O  
ANISOU  701  OE2 GLU A 117     4872   4671   5110    353   -158    114       O  
ATOM    702  N   ARG A 118     -17.363  -0.498 -46.631  1.00 17.04           N  
ANISOU  702  N   ARG A 118     2133   2023   2319    225    -99     31       N  
ATOM    703  CA  ARG A 118     -17.585   0.687 -47.452  1.00 16.67           C  
ANISOU  703  CA  ARG A 118     2075   2002   2257    194    -93     18       C  
ATOM    704  C   ARG A 118     -16.984   0.519 -48.840  1.00 16.71           C  
ANISOU  704  C   ARG A 118     2073   2005   2270    193    -58     -4       C  
ATOM    705  O   ARG A 118     -15.995  -0.194 -49.039  1.00 15.84           O  
ANISOU  705  O   ARG A 118     1948   1883   2186    222    -39    -10       O  
ATOM    706  CB  ARG A 118     -16.982   1.911 -46.771  1.00 13.91           C  
ANISOU  706  CB  ARG A 118     1692   1684   1911    192   -118     27       C  
ATOM    707  CG  ARG A 118     -15.490   1.803 -46.532  1.00 17.32           C  
ANISOU  707  CG  ARG A 118     2083   2123   2373    221   -122     30       C  
ATOM    708  CD  ARG A 118     -14.737   2.749 -47.433  1.00 18.87           C  
ANISOU  708  CD  ARG A 118     2248   2343   2580    207   -105     17       C  
ATOM    709  NE  ARG A 118     -13.281   2.648 -47.305  1.00 16.88           N  
ANISOU  709  NE  ARG A 118     1948   2101   2364    233   -105     18       N  
ATOM    710  CZ  ARG A 118     -12.525   3.420 -46.530  1.00 21.76           C  
ANISOU  710  CZ  ARG A 118     2529   2743   2995    234   -134     27       C  
ATOM    711  NH1 ARG A 118     -13.053   4.314 -45.711  1.00 16.31           N  
ANISOU  711  NH1 ARG A 118     1848   2066   2283    213   -166     35       N  
ATOM    712  NH2 ARG A 118     -11.201   3.296 -46.583  1.00 20.28           N  
ANISOU  712  NH2 ARG A 118     2291   2567   2846    255   -131     26       N  
ATOM    713  N   GLU A 119     -17.612   1.170 -49.815  1.00 14.73           N  
ANISOU  713  N   GLU A 119     1836   1766   1996    160    -47    -16       N  
ATOM    714  CA  GLU A 119     -17.126   1.190 -51.187  1.00 15.24           C  
ANISOU  714  CA  GLU A 119     1901   1834   2057    151    -13    -37       C  
ATOM    715  C   GLU A 119     -16.669   2.601 -51.543  1.00 15.19           C  
ANISOU  715  C   GLU A 119     1868   1858   2045    132    -15    -34       C  
ATOM    716  O   GLU A 119     -15.470   2.840 -51.649  1.00 17.26           O  
ANISOU  716  O   GLU A 119     2096   2132   2329    145     -1    -37       O  
ATOM    717  CB  GLU A 119     -18.207   0.690 -52.151  1.00 16.41           C  
ANISOU  717  CB  GLU A 119     2092   1967   2175    125      1    -52       C  
ATOM    718  CG  GLU A 119     -17.903   0.939 -53.619  1.00 17.67           C  
ANISOU  718  CG  GLU A 119     2261   2136   2315    105     33    -72       C  
ATOM    719  CD  GLU A 119     -16.739   0.100 -54.142  1.00 20.48           C  
ANISOU  719  CD  GLU A 119     2609   2479   2693    130     75    -93       C  
ATOM    720  OE1 GLU A 119     -16.405  -0.937 -53.526  1.00 18.05           O  
ANISOU  720  OE1 GLU A 119     2300   2146   2414    163     79    -94       O  
ATOM    721  OE2 GLU A 119     -16.152   0.488 -55.169  1.00 29.49           O  
ANISOU  721  OE2 GLU A 119     3748   3635   3823    118    106   -108       O  
ATOM    722  N   THR A 120     -17.597   3.552 -51.690  1.00 13.57           N  
ANISOU  722  N   THR A 120     1676   1666   1815    102    -33    -27       N  
ATOM    723  CA  THR A 120     -17.206   4.926 -51.975  1.00 12.45           C  
ANISOU  723  CA  THR A 120     1514   1547   1671     84    -37    -21       C  
ATOM    724  C   THR A 120     -16.316   5.477 -50.875  1.00 16.52           C  
ANISOU  724  C   THR A 120     1989   2074   2212    100    -55    -11       C  
ATOM    725  O   THR A 120     -16.592   5.299 -49.686  1.00 16.53           O  
ANISOU  725  O   THR A 120     1989   2071   2220    113    -82     -1       O  
ATOM    726  CB  THR A 120     -18.434   5.832 -52.107  1.00 14.44           C  
ANISOU  726  CB  THR A 120     1785   1804   1898     56    -59    -11       C  
ATOM    727  OG1 THR A 120     -19.405   5.202 -52.946  1.00 15.54           O  
ANISOU  727  OG1 THR A 120     1959   1932   2012     41    -52    -19       O  
ATOM    728  CG2 THR A 120     -18.034   7.200 -52.727  1.00 13.25           C  
ANISOU  728  CG2 THR A 120     1623   1670   1742     34    -56     -5       C  
ATOM    729  N   THR A 121     -15.237   6.152 -51.278  1.00 14.81           N  
ANISOU  729  N   THR A 121     1742   1874   2010     94    -41    -14       N  
ATOM    730  CA  THR A 121     -14.418   6.925 -50.361  1.00 16.57           C  
ANISOU  730  CA  THR A 121     1926   2112   2256     98    -62     -5       C  
ATOM    731  C   THR A 121     -14.291   8.346 -50.889  1.00 14.81           C  
ANISOU  731  C   THR A 121     1696   1903   2027     66    -59     -2       C  
ATOM    732  O   THR A 121     -14.504   8.618 -52.078  1.00 16.41           O  
ANISOU  732  O   THR A 121     1918   2107   2211     44    -34     -6       O  
ATOM    733  CB  THR A 121     -13.021   6.317 -50.172  1.00 14.21           C  
ANISOU  733  CB  THR A 121     1585   1819   1994    126    -50    -11       C  
ATOM    734  OG1 THR A 121     -12.309   6.411 -51.405  1.00 16.88           O  
ANISOU  734  OG1 THR A 121     1911   2165   2337    116     -7    -23       O  
ATOM    735  CG2 THR A 121     -13.129   4.846 -49.787  1.00 18.08           C  
ANISOU  735  CG2 THR A 121     2088   2289   2493    161    -49    -11       C  
ATOM    736  N   GLY A 122     -13.938   9.250 -49.983  1.00 17.77           N  
ANISOU  736  N   GLY A 122     2048   2288   2416     60    -86      4       N  
ATOM    737  CA  GLY A 122     -13.746  10.637 -50.352  1.00 14.70           C  
ANISOU  737  CA  GLY A 122     1652   1907   2026     28    -85      8       C  
ATOM    738  C   GLY A 122     -14.972  11.214 -51.020  1.00 16.06           C  
ANISOU  738  C   GLY A 122     1865   2068   2169      7    -85     15       C  
ATOM    739  O   GLY A 122     -16.115  10.995 -50.595  1.00 14.03           O  
ANISOU  739  O   GLY A 122     1634   1800   1897     13   -104     18       O  
ATOM    740  N   ILE A 123     -14.743  11.963 -52.093  1.00 13.93           N  
ANISOU  740  N   ILE A 123     1601   1802   1891    -19    -64     19       N  
ATOM    741  CA  ILE A 123     -15.821  12.510 -52.897  1.00 13.49           C  
ANISOU  741  CA  ILE A 123     1583   1736   1808    -39    -66     30       C  
ATOM    742  C   ILE A 123     -15.484  12.255 -54.352  1.00 17.47           C  
ANISOU  742  C   ILE A 123     2101   2245   2290    -55    -29     28       C  
ATOM    743  O   ILE A 123     -14.381  12.583 -54.812  1.00 16.83           O  
ANISOU  743  O   ILE A 123     1999   2175   2221    -67     -1     26       O  
ATOM    744  CB  ILE A 123     -16.043  14.018 -52.661  1.00 14.31           C  
ANISOU  744  CB  ILE A 123     1688   1832   1917    -61    -84     43       C  
ATOM    745  CG1 ILE A 123     -16.431  14.296 -51.201  1.00 16.25           C  
ANISOU  745  CG1 ILE A 123     1925   2071   2178    -47   -117     39       C  
ATOM    746  CG2 ILE A 123     -17.127  14.523 -53.597  1.00 12.70           C  
ANISOU  746  CG2 ILE A 123     1522   1617   1686    -77    -88     59       C  
ATOM    747  CD1 ILE A 123     -16.523  15.757 -50.865  1.00 14.20           C  
ANISOU  747  CD1 ILE A 123     1666   1800   1929    -67   -132     46       C  
ATOM    748  N   GLN A 124     -16.421  11.662 -55.065  1.00 14.26           N  
ANISOU  748  N   GLN A 124     1731   1834   1854    -56    -27     28       N  
ATOM    749  CA  GLN A 124     -16.296  11.480 -56.495  1.00 17.66           C  
ANISOU  749  CA  GLN A 124     2187   2269   2253    -76      5     27       C  
ATOM    750  C   GLN A 124     -17.383  12.292 -57.185  1.00 14.97           C  
ANISOU  750  C   GLN A 124     1883   1923   1881   -100    -16     48       C  
ATOM    751  O   GLN A 124     -18.425  12.611 -56.599  1.00 15.94           O  
ANISOU  751  O   GLN A 124     2012   2037   2008    -94    -53     58       O  
ATOM    752  CB  GLN A 124     -16.375   9.997 -56.873  1.00 17.29           C  
ANISOU  752  CB  GLN A 124     2155   2221   2194    -60     25      6       C  
ATOM    753  CG  GLN A 124     -17.702   9.335 -56.596  1.00 18.97           C  
ANISOU  753  CG  GLN A 124     2394   2422   2393    -52     -4      5       C  
ATOM    754  CD  GLN A 124     -17.667   7.822 -56.816  1.00 25.46           C  
ANISOU  754  CD  GLN A 124     3229   3236   3210    -36     17    -18       C  
ATOM    755  OE1 GLN A 124     -18.569   7.083 -56.368  1.00 21.72           O  
ANISOU  755  OE1 GLN A 124     2768   2750   2734    -26     -3    -21       O  
ATOM    756  NE2 GLN A 124     -16.616   7.352 -57.505  1.00 12.50           N  
ANISOU  756  NE2 GLN A 124     1583   1600   1568    -34     61    -35       N  
ATOM    757  N   ILE A 125     -17.125  12.655 -58.438  1.00 13.64           N  
ANISOU  757  N   ILE A 125     1739   1762   1683   -127      8     55       N  
ATOM    758  CA  ILE A 125     -18.111  13.378 -59.225  1.00 14.74           C  
ANISOU  758  CA  ILE A 125     1915   1896   1788   -149    -15     79       C  
ATOM    759  C   ILE A 125     -18.271  12.672 -60.565  1.00 16.72           C  
ANISOU  759  C   ILE A 125     2207   2157   1989   -167      7     73       C  
ATOM    760  O   ILE A 125     -17.416  11.894 -60.996  1.00 18.47           O  
ANISOU  760  O   ILE A 125     2427   2387   2203   -167     50     50       O  
ATOM    761  CB  ILE A 125     -17.747  14.874 -59.425  1.00 16.63           C  
ANISOU  761  CB  ILE A 125     2155   2130   2034   -172    -16    106       C  
ATOM    762  CG1 ILE A 125     -16.435  15.022 -60.203  1.00 17.18           C  
ANISOU  762  CG1 ILE A 125     2220   2212   2094   -194     34    101       C  
ATOM    763  CG2 ILE A 125     -17.712  15.637 -58.067  1.00 13.48           C  
ANISOU  763  CG2 ILE A 125     1721   1718   1681   -157    -42    109       C  
ATOM    764  CD1 ILE A 125     -16.102  16.482 -60.577  1.00 15.89           C  
ANISOU  764  CD1 ILE A 125     2065   2041   1932   -224     37    130       C  
ATOM    765  N   TRP A 126     -19.395  12.933 -61.218  1.00 16.05           N  
ANISOU  765  N   TRP A 126     2158   2070   1870   -182    -25     91       N  
ATOM    766  CA  TRP A 126     -19.589  12.439 -62.572  1.00 15.13           C  
ANISOU  766  CA  TRP A 126     2087   1964   1696   -207    -10     88       C  
ATOM    767  C   TRP A 126     -18.791  13.296 -63.547  1.00 16.78           C  
ANISOU  767  C   TRP A 126     2317   2181   1877   -238     21    105       C  
ATOM    768  O   TRP A 126     -18.762  14.528 -63.439  1.00 15.35           O  
ANISOU  768  O   TRP A 126     2131   1992   1708   -247      6    135       O  
ATOM    769  CB  TRP A 126     -21.072  12.452 -62.939  1.00 16.65           C  
ANISOU  769  CB  TRP A 126     2310   2155   1862   -215    -61    104       C  
ATOM    770  CG  TRP A 126     -21.392  11.608 -64.125  1.00 17.61           C  
ANISOU  770  CG  TRP A 126     2477   2288   1925   -237    -53     91       C  
ATOM    771  CD1 TRP A 126     -21.865  12.038 -65.329  1.00 17.24           C  
ANISOU  771  CD1 TRP A 126     2477   2252   1823   -269    -70    113       C  
ATOM    772  CD2 TRP A 126     -21.255  10.184 -64.231  1.00 18.07           C  
ANISOU  772  CD2 TRP A 126     2544   2348   1973   -232    -27     51       C  
ATOM    773  NE1 TRP A 126     -22.039  10.971 -66.177  1.00 21.22           N  
ANISOU  773  NE1 TRP A 126     3018   2765   2278   -287    -57     86       N  
ATOM    774  CE2 TRP A 126     -21.675   9.821 -65.528  1.00 19.94           C  
ANISOU  774  CE2 TRP A 126     2834   2596   2145   -264    -29     47       C  
ATOM    775  CE3 TRP A 126     -20.828   9.181 -63.350  1.00 18.75           C  
ANISOU  775  CE3 TRP A 126     2601   2425   2099   -203     -5     20       C  
ATOM    776  CZ2 TRP A 126     -21.681   8.497 -65.973  1.00 19.09           C  
ANISOU  776  CZ2 TRP A 126     2753   2490   2012   -269     -5      8       C  
ATOM    777  CZ3 TRP A 126     -20.829   7.867 -63.792  1.00 18.20           C  
ANISOU  777  CZ3 TRP A 126     2555   2352   2007   -205     18    -15       C  
ATOM    778  CH2 TRP A 126     -21.261   7.536 -65.094  1.00 18.83           C  
ANISOU  778  CH2 TRP A 126     2689   2442   2023   -239     20    -23       C  
ATOM    779  N   SER A 127     -18.120  12.635 -64.494  1.00 17.16           N  
ANISOU  779  N   SER A 127     2389   2243   1889   -254     70     84       N  
ATOM    780  CA  SER A 127     -17.247  13.357 -65.414  1.00 19.01           C  
ANISOU  780  CA  SER A 127     2641   2486   2095   -286    111     98       C  
ATOM    781  C   SER A 127     -18.024  14.211 -66.409  1.00 20.62           C  
ANISOU  781  C   SER A 127     2898   2692   2245   -318     80    137       C  
ATOM    782  O   SER A 127     -17.458  15.144 -66.992  1.00 22.25           O  
ANISOU  782  O   SER A 127     3120   2900   2434   -346    102    162       O  
ATOM    783  CB  SER A 127     -16.355  12.373 -66.173  1.00 19.84           C  
ANISOU  783  CB  SER A 127     2760   2606   2174   -294    176     62       C  
ATOM    784  OG  SER A 127     -17.127  11.647 -67.112  1.00 26.41           O  
ANISOU  784  OG  SER A 127     3647   3444   2944   -310    169     51       O  
ATOM    785  N   GLU A 128     -19.293  13.924 -66.635  1.00 19.75           N  
ANISOU  785  N   GLU A 128     2816   2580   2108   -318     30    145       N  
ATOM    786  CA  GLU A 128     -20.068  14.710 -67.582  1.00 22.28           C  
ANISOU  786  CA  GLU A 128     3185   2903   2378   -346     -7    186       C  
ATOM    787  C   GLU A 128     -20.921  15.706 -66.816  1.00 20.03           C  
ANISOU  787  C   GLU A 128     2876   2598   2135   -328    -67    222       C  
ATOM    788  O   GLU A 128     -21.749  15.311 -65.994  1.00 21.17           O  
ANISOU  788  O   GLU A 128     2994   2735   2313   -301   -104    212       O  
ATOM    789  CB  GLU A 128     -20.942  13.831 -68.471  1.00 20.33           C  
ANISOU  789  CB  GLU A 128     2985   2670   2069   -362    -30    175       C  
ATOM    790  CG  GLU A 128     -21.735  14.672 -69.465  1.00 23.14           C  
ANISOU  790  CG  GLU A 128     3391   3031   2371   -391    -76    222       C  
ATOM    791  CD  GLU A 128     -22.258  13.845 -70.594  1.00 23.26           C  
ANISOU  791  CD  GLU A 128     3463   3066   2310   -419    -86    209       C  
ATOM    792  OE1 GLU A 128     -22.063  12.614 -70.539  1.00 24.33           O  
ANISOU  792  OE1 GLU A 128     3596   3207   2440   -414    -56    160       O  
ATOM    793  OE2 GLU A 128     -22.864  14.412 -71.517  1.00 29.46           O  
ANISOU  793  OE2 GLU A 128     4295   3860   3040   -446   -124    246       O  
ATOM    794  N   ILE A 129     -20.702  16.987 -67.078  1.00 19.42           N  
ANISOU  794  N   ILE A 129     2811   2510   2059   -343    -71    262       N  
ATOM    795  CA  ILE A 129     -21.494  18.057 -66.489  1.00 20.24           C  
ANISOU  795  CA  ILE A 129     2899   2590   2201   -327   -124    298       C  
ATOM    796  C   ILE A 129     -22.709  18.266 -67.380  1.00 23.53           C  
ANISOU  796  C   ILE A 129     3359   3009   2572   -339   -180    333       C  
ATOM    797  O   ILE A 129     -22.573  18.548 -68.576  1.00 24.36           O  
ANISOU  797  O   ILE A 129     3516   3124   2615   -372   -175    358       O  
ATOM    798  CB  ILE A 129     -20.667  19.348 -66.352  1.00 21.04           C  
ANISOU  798  CB  ILE A 129     2995   2672   2327   -339   -102    324       C  
ATOM    799  CG1 ILE A 129     -19.440  19.110 -65.462  1.00 19.66           C  
ANISOU  799  CG1 ILE A 129     2773   2498   2200   -330    -52    288       C  
ATOM    800  CG2 ILE A 129     -21.511  20.474 -65.840  1.00 19.15           C  
ANISOU  800  CG2 ILE A 129     2748   2402   2127   -323   -154    361       C  
ATOM    801  CD1 ILE A 129     -19.772  18.622 -64.046  1.00 17.63           C  
ANISOU  801  CD1 ILE A 129     2465   2235   2000   -290    -72    259       C  
ATOM    802  N   PHE A 130     -23.897  18.093 -66.815  1.00 17.83           N  
ANISOU  802  N   PHE A 130     2615   2282   1878   -313   -234    335       N  
ATOM    803  CA  PHE A 130     -25.113  18.248 -67.592  1.00 20.82           C  
ANISOU  803  CA  PHE A 130     3024   2666   2222   -321   -295    368       C  
ATOM    804  C   PHE A 130     -25.486  19.714 -67.747  1.00 21.37           C  
ANISOU  804  C   PHE A 130     3103   2710   2307   -319   -331    425       C  
ATOM    805  O   PHE A 130     -25.435  20.491 -66.790  1.00 25.07           O  
ANISOU  805  O   PHE A 130     3537   3151   2839   -294   -332    432       O  
ATOM    806  CB  PHE A 130     -26.250  17.477 -66.938  1.00 17.39           C  
ANISOU  806  CB  PHE A 130     2556   2236   1817   -296   -335    348       C  
ATOM    807  CG  PHE A 130     -25.926  16.034 -66.714  1.00 22.58           C  
ANISOU  807  CG  PHE A 130     3206   2910   2465   -296   -301    295       C  
ATOM    808  CD1 PHE A 130     -26.049  15.109 -67.751  1.00 23.58           C  
ANISOU  808  CD1 PHE A 130     3374   3060   2525   -325   -299    278       C  
ATOM    809  CD2 PHE A 130     -25.462  15.606 -65.484  1.00 18.39           C  
ANISOU  809  CD2 PHE A 130     2628   2370   1988   -269   -271    261       C  
ATOM    810  CE1 PHE A 130     -25.732  13.777 -67.549  1.00 23.00           C  
ANISOU  810  CE1 PHE A 130     3296   2996   2447   -324   -265    228       C  
ATOM    811  CE2 PHE A 130     -25.148  14.276 -65.271  1.00 18.94           C  
ANISOU  811  CE2 PHE A 130     2693   2451   2052   -267   -240    215       C  
ATOM    812  CZ  PHE A 130     -25.276  13.360 -66.297  1.00 20.84           C  
ANISOU  812  CZ  PHE A 130     2975   2711   2234   -293   -235    198       C  
ATOM    813  N   LEU A 131     -25.870  20.085 -68.963  1.00 25.73           N  
ANISOU  813  N   LEU A 131     3708   3270   2800   -345   -361    465       N  
ATOM    814  CA  LEU A 131     -26.314  21.435 -69.279  1.00 27.50           C  
ANISOU  814  CA  LEU A 131     3949   3467   3032   -343   -402    526       C  
ATOM    815  C   LEU A 131     -27.834  21.445 -69.334  1.00 27.58           C  
ANISOU  815  C   LEU A 131     3948   3478   3054   -322   -482    551       C  
ATOM    816  O   LEU A 131     -28.423  20.757 -70.167  1.00 27.77           O  
ANISOU  816  O   LEU A 131     3999   3531   3022   -341   -514    552       O  
ATOM    817  CB  LEU A 131     -25.721  21.900 -70.608  1.00 27.25           C  
ANISOU  817  CB  LEU A 131     3986   3443   2925   -387   -386    563       C  
ATOM    818  CG  LEU A 131     -24.193  21.944 -70.641  1.00 28.42           C  
ANISOU  818  CG  LEU A 131     4143   3592   3063   -412   -304    541       C  
ATOM    819  CD1 LEU A 131     -23.685  22.623 -71.900  1.00 34.75           C  
ANISOU  819  CD1 LEU A 131     5013   4395   3794   -456   -287    586       C  
ATOM    820  CD2 LEU A 131     -23.695  22.674 -69.416  1.00 29.73           C  
ANISOU  820  CD2 LEU A 131     4258   3725   3313   -386   -282    534       C  
ATOM    821  N   ILE A 132     -28.465  22.222 -68.453  1.00 26.36           N  
ANISOU  821  N   ILE A 132     3751   3292   2974   -284   -512    568       N  
ATOM    822  CA  ILE A 132     -29.918  22.228 -68.308  1.00 31.01           C  
ANISOU  822  CA  ILE A 132     4311   3879   3591   -257   -582    586       C  
ATOM    823  C   ILE A 132     -30.436  23.651 -68.465  1.00 32.87           C  
ANISOU  823  C   ILE A 132     4553   4077   3858   -238   -626    648       C  
ATOM    824  O   ILE A 132     -29.871  24.594 -67.900  1.00 30.51           O  
ANISOU  824  O   ILE A 132     4248   3742   3604   -226   -597    657       O  
ATOM    825  CB  ILE A 132     -30.364  21.657 -66.943  1.00 30.73           C  
ANISOU  825  CB  ILE A 132     4209   3841   3626   -221   -574    540       C  
ATOM    826  CG1 ILE A 132     -29.946  20.187 -66.788  1.00 29.23           C  
ANISOU  826  CG1 ILE A 132     4014   3683   3408   -237   -536    483       C  
ATOM    827  CG2 ILE A 132     -31.860  21.811 -66.765  1.00 30.18           C  
ANISOU  827  CG2 ILE A 132     4104   3767   3596   -192   -642    562       C  
ATOM    828  CD1 ILE A 132     -30.417  19.278 -67.915  1.00 28.76           C  
ANISOU  828  CD1 ILE A 132     3991   3660   3277   -268   -566    481       C  
ATOM    829  N   ASN A 133     -31.522  23.801 -69.216  1.00 35.80           N  
ANISOU  829  N   ASN A 133     4936   4457   4210   -236   -697    690       N  
ATOM    830  CA  ASN A 133     -32.238  25.068 -69.318  1.00 39.09           C  
ANISOU  830  CA  ASN A 133     5349   4835   4667   -209   -750    751       C  
ATOM    831  C   ASN A 133     -33.255  25.160 -68.188  1.00 42.02           C  
ANISOU  831  C   ASN A 133     5647   5189   5130   -158   -775    736       C  
ATOM    832  O   ASN A 133     -34.209  24.375 -68.140  1.00 41.65           O  
ANISOU  832  O   ASN A 133     5567   5170   5089   -149   -813    721       O  
ATOM    833  CB  ASN A 133     -32.954  25.184 -70.662  1.00 38.91           C  
ANISOU  833  CB  ASN A 133     5371   4831   4581   -228   -821    807       C  
ATOM    834  CG  ASN A 133     -32.015  25.093 -71.838  1.00 38.93           C  
ANISOU  834  CG  ASN A 133     5453   4854   4485   -282   -795    823       C  
ATOM    835  OD1 ASN A 133     -30.995  25.773 -71.888  1.00 40.54           O  
ANISOU  835  OD1 ASN A 133     5687   5033   4682   -296   -745    835       O  
ATOM    836  ND2 ASN A 133     -32.360  24.248 -72.803  1.00 47.01           N  
ANISOU  836  ND2 ASN A 133     6510   5922   5430   -314   -827    822       N  
ATOM    837  N   LYS A 134     -33.066  26.121 -67.291  1.00 43.00           N  
ANISOU  837  N   LYS A 134     5747   5266   5325   -127   -752    739       N  
ATOM    838  CA  LYS A 134     -34.061  26.366 -66.264  1.00 46.39           C  
ANISOU  838  CA  LYS A 134     6111   5673   5841    -77   -773    729       C  
ATOM    839  C   LYS A 134     -35.309  26.981 -66.902  1.00 53.03           C  
ANISOU  839  C   LYS A 134     6944   6504   6702    -53   -853    789       C  
ATOM    840  O   LYS A 134     -35.270  27.412 -68.059  1.00 51.11           O  
ANISOU  840  O   LYS A 134     6752   6261   6406    -73   -891    844       O  
ATOM    841  CB  LYS A 134     -33.480  27.268 -65.176  1.00 47.75           C  
ANISOU  841  CB  LYS A 134     6267   5796   6078    -53   -725    714       C  
ATOM    842  CG  LYS A 134     -32.350  26.595 -64.392  1.00 42.24           C  
ANISOU  842  CG  LYS A 134     5565   5113   5371    -72   -653    652       C  
ATOM    843  CD  LYS A 134     -32.265  27.094 -62.960  1.00 38.74           C  
ANISOU  843  CD  LYS A 134     5081   4634   5005    -39   -618    619       C  
ATOM    844  CE  LYS A 134     -33.500  26.706 -62.167  1.00 42.18           C  
ANISOU  844  CE  LYS A 134     5457   5075   5494      0   -641    598       C  
ATOM    845  NZ  LYS A 134     -33.483  27.258 -60.780  1.00 44.99           N  
ANISOU  845  NZ  LYS A 134     5779   5395   5921     32   -607    566       N  
ATOM    846  N   PRO A 135     -36.443  26.990 -66.187  1.00 58.97           N  
ANISOU  846  N   PRO A 135     7631   7248   7526     -9   -882    782       N  
ATOM    847  CA  PRO A 135     -37.675  27.533 -66.791  1.00 60.49           C  
ANISOU  847  CA  PRO A 135     7806   7433   7745     18   -964    839       C  
ATOM    848  C   PRO A 135     -37.545  28.965 -67.286  1.00 58.50           C  
ANISOU  848  C   PRO A 135     7590   7129   7507     33   -981    900       C  
ATOM    849  O   PRO A 135     -38.182  29.319 -68.285  1.00 66.17           O  
ANISOU  849  O   PRO A 135     8576   8111   8455     33  -1025    936       O  
ATOM    850  CB  PRO A 135     -38.697  27.422 -65.652  1.00 62.63           C  
ANISOU  850  CB  PRO A 135     7993   7696   8108     66   -966    809       C  
ATOM    851  CG  PRO A 135     -38.215  26.273 -64.839  1.00 59.81           C  
ANISOU  851  CG  PRO A 135     7618   7370   7738     46   -906    736       C  
ATOM    852  CD  PRO A 135     -36.712  26.337 -64.891  1.00 53.50           C  
ANISOU  852  CD  PRO A 135     6876   6563   6888     13   -845    720       C  
ATOM    853  N   ASP A 136     -36.740  29.797 -66.627  1.00 59.29           N  
ANISOU  853  N   ASP A 136     7705   7179   7643     43   -932    897       N  
ATOM    854  CA  ASP A 136     -36.529  31.178 -67.046  1.00 57.12           C  
ANISOU  854  CA  ASP A 136     7469   6849   7384     54   -938    949       C  
ATOM    855  C   ASP A 136     -35.566  31.307 -68.222  1.00 57.27           C  
ANISOU  855  C   ASP A 136     7570   6879   7311      0   -931    983       C  
ATOM    856  O   ASP A 136     -35.223  32.431 -68.601  1.00 57.12           O  
ANISOU  856  O   ASP A 136     7590   6816   7296      1   -923   1022       O  
ATOM    857  CB  ASP A 136     -36.022  32.017 -65.868  1.00 61.79           C  
ANISOU  857  CB  ASP A 136     8047   7378   8051     80   -888    929       C  
ATOM    858  CG  ASP A 136     -34.717  31.492 -65.281  1.00 66.74           C  
ANISOU  858  CG  ASP A 136     8690   8022   8647     42   -808    868       C  
ATOM    859  OD1 ASP A 136     -34.160  30.504 -65.807  1.00 59.49           O  
ANISOU  859  OD1 ASP A 136     7794   7156   7652     -1   -794    849       O  
ATOM    860  OD2 ASP A 136     -34.250  32.066 -64.273  1.00 76.22           O  
ANISOU  860  OD2 ASP A 136     9878   9182   9901     57   -760    837       O  
ATOM    861  N   GLY A 137     -35.116  30.193 -68.799  1.00 55.41           N  
ANISOU  861  N   GLY A 137     7363   6700   6991    -46   -928    968       N  
ATOM    862  CA  GLY A 137     -34.210  30.225 -69.922  1.00 57.94           C  
ANISOU  862  CA  GLY A 137     7760   7035   7218   -100   -913    994       C  
ATOM    863  C   GLY A 137     -32.739  30.228 -69.567  1.00 56.09           C  
ANISOU  863  C   GLY A 137     7555   6792   6964   -134   -830    961       C  
ATOM    864  O   GLY A 137     -31.904  30.050 -70.465  1.00 58.71           O  
ANISOU  864  O   GLY A 137     7947   7145   7214   -183   -807    974       O  
ATOM    865  N   LYS A 138     -32.387  30.436 -68.300  1.00 52.67           N  
ANISOU  865  N   LYS A 138     7079   6331   6603   -110   -780    915       N  
ATOM    866  CA  LYS A 138     -30.987  30.357 -67.906  1.00 50.19           C  
ANISOU  866  CA  LYS A 138     6781   6015   6274   -142   -701    875       C  
ATOM    867  C   LYS A 138     -30.486  28.930 -68.080  1.00 43.85           C  
ANISOU  867  C   LYS A 138     5977   5275   5408   -175   -670    823       C  
ATOM    868  O   LYS A 138     -31.163  27.973 -67.692  1.00 42.47           O  
ANISOU  868  O   LYS A 138     5760   5133   5242   -158   -686    787       O  
ATOM    869  CB  LYS A 138     -30.815  30.817 -66.459  1.00 47.77           C  
ANISOU  869  CB  LYS A 138     6426   5668   6055   -110   -664    833       C  
ATOM    870  CG  LYS A 138     -29.396  30.679 -65.940  1.00 46.13           C  
ANISOU  870  CG  LYS A 138     6226   5464   5839   -142   -588    788       C  
ATOM    871  CD  LYS A 138     -28.944  31.927 -65.189  1.00 47.13           C  
ANISOU  871  CD  LYS A 138     6351   5525   6031   -131   -561    791       C  
ATOM    872  CE  LYS A 138     -29.808  32.218 -63.963  1.00 48.97           C  
ANISOU  872  CE  LYS A 138     6530   5728   6350    -77   -574    765       C  
ATOM    873  NZ  LYS A 138     -29.150  33.183 -63.021  1.00 40.54           N  
ANISOU  873  NZ  LYS A 138     5459   4605   5339    -73   -533    744       N  
ATOM    874  N   LYS A 139     -29.316  28.784 -68.699  1.00 37.95           N  
ANISOU  874  N   LYS A 139     5277   4544   4598   -223   -622    821       N  
ATOM    875  CA  LYS A 139     -28.686  27.483 -68.872  1.00 42.40           C  
ANISOU  875  CA  LYS A 139     5843   5162   5106   -253   -582    770       C  
ATOM    876  C   LYS A 139     -27.649  27.292 -67.768  1.00 36.64           C  
ANISOU  876  C   LYS A 139     5078   4425   4417   -252   -512    712       C  
ATOM    877  O   LYS A 139     -26.734  28.109 -67.624  1.00 35.40           O  
ANISOU  877  O   LYS A 139     4936   4238   4275   -268   -473    721       O  
ATOM    878  CB  LYS A 139     -28.048  27.350 -70.257  1.00 44.58           C  
ANISOU  878  CB  LYS A 139     6189   5462   5286   -305   -569    798       C  
ATOM    879  CG  LYS A 139     -27.329  26.016 -70.469  1.00 43.46           C  
ANISOU  879  CG  LYS A 139     6052   5371   5088   -336   -519    741       C  
ATOM    880  CD  LYS A 139     -26.990  25.751 -71.933  1.00 46.76           C  
ANISOU  880  CD  LYS A 139     6543   5821   5404   -385   -515    767       C  
ATOM    881  CE  LYS A 139     -26.113  26.851 -72.508  1.00 55.27           C  
ANISOU  881  CE  LYS A 139     7671   6871   6459   -416   -482    813       C  
ATOM    882  NZ  LYS A 139     -25.160  26.361 -73.551  1.00 58.39           N  
ANISOU  882  NZ  LYS A 139     8123   7300   6762   -471   -429    805       N  
ATOM    883  N   VAL A 140     -27.802  26.221 -66.990  1.00 30.98           N  
ANISOU  883  N   VAL A 140     4316   3737   3719   -236   -500    655       N  
ATOM    884  CA  VAL A 140     -26.941  25.950 -65.846  1.00 27.77           C  
ANISOU  884  CA  VAL A 140     3871   3327   3352   -230   -444    601       C  
ATOM    885  C   VAL A 140     -26.179  24.655 -66.083  1.00 27.12           C  
ANISOU  885  C   VAL A 140     3793   3292   3221   -256   -402    557       C  
ATOM    886  O   VAL A 140     -26.555  23.812 -66.900  1.00 24.41           O  
ANISOU  886  O   VAL A 140     3471   2982   2822   -270   -419    556       O  
ATOM    887  CB  VAL A 140     -27.729  25.858 -64.524  1.00 26.67           C  
ANISOU  887  CB  VAL A 140     3674   3174   3286   -185   -460    572       C  
ATOM    888  CG1 VAL A 140     -28.491  27.156 -64.259  1.00 32.07           C  
ANISOU  888  CG1 VAL A 140     4352   3808   4026   -155   -497    612       C  
ATOM    889  CG2 VAL A 140     -28.678  24.667 -64.559  1.00 28.94           C  
ANISOU  889  CG2 VAL A 140     3939   3498   3557   -172   -491    551       C  
ATOM    890  N   ALA A 141     -25.090  24.515 -65.345  1.00 23.27           N  
ANISOU  890  N   ALA A 141     3283   2803   2756   -261   -347    519       N  
ATOM    891  CA  ALA A 141     -24.293  23.305 -65.316  1.00 22.71           C  
ANISOU  891  CA  ALA A 141     3203   2770   2657   -275   -302    471       C  
ATOM    892  C   ALA A 141     -24.639  22.527 -64.055  1.00 24.33           C  
ANISOU  892  C   ALA A 141     3355   2980   2908   -241   -304    425       C  
ATOM    893  O   ALA A 141     -24.749  23.112 -62.972  1.00 24.12           O  
ANISOU  893  O   ALA A 141     3296   2928   2941   -217   -307    418       O  
ATOM    894  CB  ALA A 141     -22.809  23.653 -65.336  1.00 17.64           C  
ANISOU  894  CB  ALA A 141     2565   2124   2013   -303   -242    462       C  
ATOM    895  N   VAL A 142     -24.817  21.213 -64.193  1.00 18.15           N  
ANISOU  895  N   VAL A 142     2568   2230   2097   -241   -300    394       N  
ATOM    896  CA  VAL A 142     -25.207  20.364 -63.075  1.00 18.55           C  
ANISOU  896  CA  VAL A 142     2576   2288   2186   -212   -302    354       C  
ATOM    897  C   VAL A 142     -24.074  19.390 -62.781  1.00 19.96           C  
ANISOU  897  C   VAL A 142     2741   2486   2355   -220   -249    311       C  
ATOM    898  O   VAL A 142     -23.702  18.572 -63.630  1.00 18.19           O  
ANISOU  898  O   VAL A 142     2543   2286   2082   -241   -228    299       O  
ATOM    899  CB  VAL A 142     -26.521  19.618 -63.344  1.00 22.95           C  
ANISOU  899  CB  VAL A 142     3132   2861   2728   -203   -346    355       C  
ATOM    900  CG1 VAL A 142     -26.881  18.739 -62.133  1.00 19.03           C  
ANISOU  900  CG1 VAL A 142     2591   2368   2271   -176   -342    314       C  
ATOM    901  CG2 VAL A 142     -27.641  20.607 -63.651  1.00 19.80           C  
ANISOU  901  CG2 VAL A 142     2737   2442   2344   -192   -402    401       C  
ATOM    902  N   LEU A 143     -23.529  19.498 -61.578  1.00 17.84           N  
ANISOU  902  N   LEU A 143     2436   2207   2135   -202   -229    287       N  
ATOM    903  CA  LEU A 143     -22.513  18.604 -61.049  1.00 20.48           C  
ANISOU  903  CA  LEU A 143     2748   2557   2475   -199   -187    247       C  
ATOM    904  C   LEU A 143     -23.183  17.617 -60.102  1.00 17.63           C  
ANISOU  904  C   LEU A 143     2360   2202   2137   -171   -201    219       C  
ATOM    905  O   LEU A 143     -24.035  18.006 -59.297  1.00 20.14           O  
ANISOU  905  O   LEU A 143     2659   2505   2488   -150   -230    224       O  
ATOM    906  CB  LEU A 143     -21.445  19.412 -60.306  1.00 17.66           C  
ANISOU  906  CB  LEU A 143     2368   2186   2156   -201   -162    242       C  
ATOM    907  CG  LEU A 143     -20.388  18.699 -59.460  1.00 16.95           C  
ANISOU  907  CG  LEU A 143     2243   2109   2089   -192   -128    204       C  
ATOM    908  CD1 LEU A 143     -19.396  17.987 -60.348  1.00 24.97           C  
ANISOU  908  CD1 LEU A 143     3268   3147   3071   -212    -85    192       C  
ATOM    909  CD2 LEU A 143     -19.670  19.719 -58.603  1.00 21.02           C  
ANISOU  909  CD2 LEU A 143     2733   2606   2646   -194   -121    204       C  
ATOM    910  N   LEU A 144     -22.812  16.342 -60.212  1.00 17.80           N  
ANISOU  910  N   LEU A 144     2381   2243   2139   -171   -178    190       N  
ATOM    911  CA  LEU A 144     -23.306  15.294 -59.325  1.00 16.28           C  
ANISOU  911  CA  LEU A 144     2166   2054   1965   -148   -185    163       C  
ATOM    912  C   LEU A 144     -22.155  14.787 -58.468  1.00 17.81           C  
ANISOU  912  C   LEU A 144     2333   2251   2183   -136   -150    135       C  
ATOM    913  O   LEU A 144     -21.109  14.398 -58.994  1.00 18.76           O  
ANISOU  913  O   LEU A 144     2458   2382   2287   -147   -114    123       O  
ATOM    914  CB  LEU A 144     -23.931  14.133 -60.108  1.00 20.52           C  
ANISOU  914  CB  LEU A 144     2727   2605   2464   -157   -191    152       C  
ATOM    915  CG  LEU A 144     -25.199  14.379 -60.921  1.00 21.45           C  
ANISOU  915  CG  LEU A 144     2868   2726   2557   -170   -235    177       C  
ATOM    916  CD1 LEU A 144     -25.937  13.069 -61.210  1.00 24.30           C  
ANISOU  916  CD1 LEU A 144     3239   3098   2896   -175   -245    156       C  
ATOM    917  CD2 LEU A 144     -26.111  15.344 -60.199  1.00 22.02           C  
ANISOU  917  CD2 LEU A 144     2916   2781   2670   -151   -271    199       C  
ATOM    918  N   MET A 145     -22.353  14.790 -57.157  1.00 16.05           N  
ANISOU  918  N   MET A 145     2081   2019   1997   -113   -161    125       N  
ATOM    919  CA  MET A 145     -21.324  14.461 -56.185  1.00 17.68           C  
ANISOU  919  CA  MET A 145     2261   2229   2229    -99   -139    104       C  
ATOM    920  C   MET A 145     -21.766  13.254 -55.375  1.00 16.33           C  
ANISOU  920  C   MET A 145     2079   2059   2066    -77   -144     84       C  
ATOM    921  O   MET A 145     -22.849  13.265 -54.787  1.00 16.52           O  
ANISOU  921  O   MET A 145     2101   2076   2101    -67   -168     88       O  
ATOM    922  CB  MET A 145     -21.066  15.633 -55.237  1.00 21.80           C  
ANISOU  922  CB  MET A 145     2761   2737   2784    -95   -149    110       C  
ATOM    923  CG  MET A 145     -20.815  16.968 -55.913  1.00 27.93           C  
ANISOU  923  CG  MET A 145     3550   3503   3559   -117   -149    134       C  
ATOM    924  SD  MET A 145     -20.678  18.290 -54.676  1.00 35.53           S  
ANISOU  924  SD  MET A 145     4493   4443   4564   -111   -163    135       S  
ATOM    925  CE  MET A 145     -19.498  17.518 -53.613  1.00 12.40           C  
ANISOU  925  CE  MET A 145     1530   1531   1652   -101   -146    104       C  
ATOM    926  N   ASP A 146     -20.923  12.235 -55.324  1.00 14.35           N  
ANISOU  926  N   ASP A 146     1822   1816   1814    -69   -119     65       N  
ATOM    927  CA  ASP A 146     -21.182  11.032 -54.545  1.00 15.88           C  
ANISOU  927  CA  ASP A 146     2010   2008   2017    -48   -120     49       C  
ATOM    928  C   ASP A 146     -20.116  10.963 -53.462  1.00 15.31           C  
ANISOU  928  C   ASP A 146     1907   1937   1972    -30   -111     39       C  
ATOM    929  O   ASP A 146     -18.945  11.260 -53.727  1.00 15.53           O  
ANISOU  929  O   ASP A 146     1921   1973   2008    -35    -91     37       O  
ATOM    930  CB  ASP A 146     -21.155   9.796 -55.448  1.00 14.31           C  
ANISOU  930  CB  ASP A 146     1832   1811   1793    -53    -99     34       C  
ATOM    931  CG  ASP A 146     -21.646   8.526 -54.755  1.00 14.19           C  
ANISOU  931  CG  ASP A 146     1819   1788   1786    -35   -103     20       C  
ATOM    932  OD1 ASP A 146     -22.424   8.609 -53.775  1.00 13.04           O  
ANISOU  932  OD1 ASP A 146     1664   1635   1655    -26   -125     26       O  
ATOM    933  OD2 ASP A 146     -21.236   7.432 -55.204  1.00 12.05           O  
ANISOU  933  OD2 ASP A 146     1559   1513   1506    -31    -79      3       O  
ATOM    934  N   THR A 147     -20.520  10.622 -52.233  1.00 13.89           N  
ANISOU  934  N   THR A 147     1719   1752   1808    -12   -127     36       N  
ATOM    935  CA  THR A 147     -19.635  10.783 -51.088  1.00 13.55           C  
ANISOU  935  CA  THR A 147     1649   1712   1787      2   -131     32       C  
ATOM    936  C   THR A 147     -19.458   9.487 -50.309  1.00 12.92           C  
ANISOU  936  C   THR A 147     1565   1630   1714     26   -129     23       C  
ATOM    937  O   THR A 147     -20.335   8.613 -50.273  1.00 13.17           O  
ANISOU  937  O   THR A 147     1616   1653   1736     31   -131     22       O  
ATOM    938  CB  THR A 147     -20.141  11.873 -50.117  1.00 13.51           C  
ANISOU  938  CB  THR A 147     1638   1702   1793      0   -154     38       C  
ATOM    939  OG1 THR A 147     -21.361  11.435 -49.500  1.00 14.15           O  
ANISOU  939  OG1 THR A 147     1732   1776   1870      9   -167     38       O  
ATOM    940  CG2 THR A 147     -20.412  13.190 -50.856  1.00 13.83           C  
ANISOU  940  CG2 THR A 147     1685   1737   1831    -20   -158     50       C  
ATOM    941  N   GLN A 148     -18.301   9.396 -49.667  1.00 12.09           N  
ANISOU  941  N   GLN A 148     1435   1532   1627     39   -129     20       N  
ATOM    942  CA  GLN A 148     -18.046   8.380 -48.662  1.00 12.53           C  
ANISOU  942  CA  GLN A 148     1484   1584   1691     65   -136     18       C  
ATOM    943  C   GLN A 148     -19.076   8.467 -47.548  1.00 12.99           C  
ANISOU  943  C   GLN A 148     1558   1637   1742     67   -158     23       C  
ATOM    944  O   GLN A 148     -19.190   9.499 -46.876  1.00 13.05           O  
ANISOU  944  O   GLN A 148     1559   1648   1750     59   -175     25       O  
ATOM    945  CB  GLN A 148     -16.646   8.583 -48.084  1.00 14.05           C  
ANISOU  945  CB  GLN A 148     1642   1790   1907     76   -142     17       C  
ATOM    946  CG  GLN A 148     -16.251   7.545 -47.036  1.00 12.46           C  
ANISOU  946  CG  GLN A 148     1433   1585   1715    105   -155     20       C  
ATOM    947  CD  GLN A 148     -14.820   7.749 -46.569  1.00 18.74           C  
ANISOU  947  CD  GLN A 148     2187   2397   2537    116   -166     21       C  
ATOM    948  OE1 GLN A 148     -13.994   8.327 -47.293  1.00 16.23           O  
ANISOU  948  OE1 GLN A 148     1843   2090   2233    104   -150     15       O  
ATOM    949  NE2 GLN A 148     -14.522   7.293 -45.355  1.00 16.83           N  
ANISOU  949  NE2 GLN A 148     1938   2158   2299    136   -193     29       N  
ATOM    950  N   GLY A 149     -19.797   7.373 -47.316  1.00 12.13           N  
ANISOU  950  N   GLY A 149     1468   1515   1625     77   -156     24       N  
ATOM    951  CA  GLY A 149     -20.700   7.342 -46.179  1.00 10.86           C  
ANISOU  951  CA  GLY A 149     1321   1350   1457     79   -171     30       C  
ATOM    952  C   GLY A 149     -19.959   7.547 -44.871  1.00 10.87           C  
ANISOU  952  C   GLY A 149     1310   1359   1461     91   -190     33       C  
ATOM    953  O   GLY A 149     -18.826   7.089 -44.688  1.00 14.58           O  
ANISOU  953  O   GLY A 149     1763   1834   1942    107   -194     35       O  
ATOM    954  N   THR A 150     -20.619   8.234 -43.945  1.00 12.38           N  
ANISOU  954  N   THR A 150     1509   1553   1643     84   -202     33       N  
ATOM    955  CA  THR A 150     -20.042   8.491 -42.635  1.00 12.63           C  
ANISOU  955  CA  THR A 150     1536   1593   1668     90   -222     35       C  
ATOM    956  C   THR A 150     -20.041   7.228 -41.773  1.00 16.85           C  
ANISOU  956  C   THR A 150     2088   2123   2193    108   -228     46       C  
ATOM    957  O   THR A 150     -20.794   6.269 -42.013  1.00 11.56           O  
ANISOU  957  O   THR A 150     1437   1437   1519    112   -213     51       O  
ATOM    958  CB  THR A 150     -20.830   9.583 -41.917  1.00 14.75           C  
ANISOU  958  CB  THR A 150     1815   1862   1926     76   -227     27       C  
ATOM    959  OG1 THR A 150     -22.180   9.147 -41.774  1.00 11.32           O  
ANISOU  959  OG1 THR A 150     1402   1417   1482     74   -214     29       O  
ATOM    960  CG2 THR A 150     -20.810  10.884 -42.713  1.00 13.62           C  
ANISOU  960  CG2 THR A 150     1659   1719   1797     59   -224     19       C  
ATOM    961  N   PHE A 151     -19.157   7.237 -40.767  1.00 14.18           N  
ANISOU  961  N   PHE A 151     1743   1796   1850    118   -252     52       N  
ATOM    962  CA  PHE A 151     -19.091   6.228 -39.708  1.00 16.35           C  
ANISOU  962  CA  PHE A 151     2037   2067   2110    135   -265     68       C  
ATOM    963  C   PHE A 151     -18.695   4.841 -40.213  1.00 17.69           C  
ANISOU  963  C   PHE A 151     2206   2220   2295    158   -257     80       C  
ATOM    964  O   PHE A 151     -19.024   3.834 -39.582  1.00 17.46           O  
ANISOU  964  O   PHE A 151     2203   2177   2254    170   -259     96       O  
ATOM    965  CB  PHE A 151     -20.414   6.162 -38.936  1.00 16.75           C  
ANISOU  965  CB  PHE A 151     2123   2110   2133    123   -256     69       C  
ATOM    966  CG  PHE A 151     -20.848   7.501 -38.416  1.00 15.86           C  
ANISOU  966  CG  PHE A 151     2011   2007   2007    103   -258     53       C  
ATOM    967  CD1 PHE A 151     -20.040   8.198 -37.543  1.00 19.91           C  
ANISOU  967  CD1 PHE A 151     2520   2537   2508    100   -285     49       C  
ATOM    968  CD2 PHE A 151     -22.037   8.072 -38.825  1.00 21.27           C  
ANISOU  968  CD2 PHE A 151     2703   2685   2695     88   -235     42       C  
ATOM    969  CE1 PHE A 151     -20.428   9.443 -37.066  1.00 25.63           C  
ANISOU  969  CE1 PHE A 151     3250   3267   3221     80   -285     30       C  
ATOM    970  CE2 PHE A 151     -22.422   9.322 -38.358  1.00 20.20           C  
ANISOU  970  CE2 PHE A 151     2568   2554   2552     74   -235     26       C  
ATOM    971  CZ  PHE A 151     -21.619  10.000 -37.484  1.00 19.32           C  
ANISOU  971  CZ  PHE A 151     2458   2456   2428     69   -257     18       C  
ATOM    972  N   ASP A 152     -17.949   4.753 -41.311  1.00 14.66           N  
ANISOU  972  N   ASP A 152     1795   1836   1938    166   -246     73       N  
ATOM    973  CA  ASP A 152     -17.486   3.428 -41.679  1.00 14.24           C  
ANISOU  973  CA  ASP A 152     1743   1764   1902    192   -237     82       C  
ATOM    974  C   ASP A 152     -16.370   2.991 -40.726  1.00 18.94           C  
ANISOU  974  C   ASP A 152     2323   2367   2507    219   -268    100       C  
ATOM    975  O   ASP A 152     -15.929   3.745 -39.855  1.00 20.75           O  
ANISOU  975  O   ASP A 152     2540   2618   2726    214   -298    103       O  
ATOM    976  CB  ASP A 152     -17.089   3.368 -43.162  1.00 13.65           C  
ANISOU  976  CB  ASP A 152     1649   1686   1850    192   -209     67       C  
ATOM    977  CG  ASP A 152     -15.826   4.158 -43.513  1.00 16.26           C  
ANISOU  977  CG  ASP A 152     1935   2039   2204    194   -214     59       C  
ATOM    978  OD1 ASP A 152     -14.848   4.201 -42.731  1.00 16.34           O  
ANISOU  978  OD1 ASP A 152     1920   2062   2226    210   -241     69       O  
ATOM    979  OD2 ASP A 152     -15.795   4.680 -44.648  1.00 15.25           O  
ANISOU  979  OD2 ASP A 152     1798   1916   2082    178   -191     45       O  
ATOM    980  N   SER A 153     -15.936   1.741 -40.869  1.00 19.68           N  
ANISOU  980  N   SER A 153     2419   2439   2621    249   -263    112       N  
ATOM    981  CA  SER A 153     -15.079   1.145 -39.852  1.00 24.28           C  
ANISOU  981  CA  SER A 153     2994   3023   3210    279   -297    136       C  
ATOM    982  C   SER A 153     -13.639   1.641 -39.916  1.00 19.82           C  
ANISOU  982  C   SER A 153     2373   2482   2675    294   -319    134       C  
ATOM    983  O   SER A 153     -12.873   1.371 -38.987  1.00 20.29           O  
ANISOU  983  O   SER A 153     2420   2550   2739    315   -358    155       O  
ATOM    984  CB  SER A 153     -15.107  -0.386 -39.977  1.00 29.41           C  
ANISOU  984  CB  SER A 153     3666   3634   3876    310   -284    152       C  
ATOM    985  OG  SER A 153     -14.483  -0.821 -41.182  1.00 29.74           O  
ANISOU  985  OG  SER A 153     3681   3663   3956    328   -254    136       O  
ATOM    986  N   GLN A 154     -13.258   2.373 -40.963  1.00 17.44           N  
ANISOU  986  N   GLN A 154     2039   2194   2394    280   -296    111       N  
ATOM    987  CA  GLN A 154     -11.882   2.839 -41.119  1.00 21.64           C  
ANISOU  987  CA  GLN A 154     2513   2750   2961    290   -310    107       C  
ATOM    988  C   GLN A 154     -11.695   4.315 -40.814  1.00 20.98           C  
ANISOU  988  C   GLN A 154     2410   2697   2864    256   -330     95       C  
ATOM    989  O   GLN A 154     -10.552   4.779 -40.815  1.00 22.72           O  
ANISOU  989  O   GLN A 154     2579   2940   3112    258   -347     93       O  
ATOM    990  CB  GLN A 154     -11.375   2.599 -42.549  1.00 20.59           C  
ANISOU  990  CB  GLN A 154     2352   2609   2862    298   -265     89       C  
ATOM    991  CG  GLN A 154     -10.810   1.219 -42.795  1.00 28.05           C  
ANISOU  991  CG  GLN A 154     3288   3528   3841    343   -252     97       C  
ATOM    992  CD  GLN A 154     -11.890   0.187 -42.818  1.00 35.57           C  
ANISOU  992  CD  GLN A 154     4298   4444   4774    349   -235    103       C  
ATOM    993  OE1 GLN A 154     -12.887   0.344 -43.528  1.00 41.19           O  
ANISOU  993  OE1 GLN A 154     5043   5146   5463    322   -205     87       O  
ATOM    994  NE2 GLN A 154     -11.729  -0.869 -42.018  1.00 35.84           N  
ANISOU  994  NE2 GLN A 154     4345   4456   4817    383   -256    128       N  
ATOM    995  N   SER A 155     -12.766   5.064 -40.570  1.00 15.78           N  
ANISOU  995  N   SER A 155     1787   2039   2169    224   -328     88       N  
ATOM    996  CA  SER A 155     -12.706   6.516 -40.588  1.00 14.82           C  
ANISOU  996  CA  SER A 155     1653   1938   2041    190   -334     71       C  
ATOM    997  C   SER A 155     -12.733   7.106 -39.186  1.00 18.98           C  
ANISOU  997  C   SER A 155     2192   2481   2539    177   -378     75       C  
ATOM    998  O   SER A 155     -13.491   6.656 -38.325  1.00 16.67           O  
ANISOU  998  O   SER A 155     1940   2180   2214    181   -388     86       O  
ATOM    999  CB  SER A 155     -13.869   7.091 -41.403  1.00 15.39           C  
ANISOU  999  CB  SER A 155     1754   1998   2097    164   -300     57       C  
ATOM   1000  OG  SER A 155     -13.815   6.639 -42.747  1.00 16.50           O  
ANISOU 1000  OG  SER A 155     1886   2127   2256    170   -262     51       O  
ATOM   1001  N   THR A 156     -11.917   8.138 -38.974  1.00 16.92           N  
ANISOU 1001  N   THR A 156     1897   2242   2288    157   -400     65       N  
ATOM   1002  CA  THR A 156     -12.093   8.975 -37.805  1.00 18.07           C  
ANISOU 1002  CA  THR A 156     2062   2402   2402    134   -434     59       C  
ATOM   1003  C   THR A 156     -13.341   9.829 -37.974  1.00 15.97           C  
ANISOU 1003  C   THR A 156     1835   2122   2112    107   -407     42       C  
ATOM   1004  O   THR A 156     -13.895   9.965 -39.071  1.00 15.24           O  
ANISOU 1004  O   THR A 156     1745   2015   2031    102   -369     35       O  
ATOM   1005  CB  THR A 156     -10.879   9.878 -37.583  1.00 20.27           C  
ANISOU 1005  CB  THR A 156     2294   2706   2701    115   -465     48       C  
ATOM   1006  OG1 THR A 156     -10.691  10.717 -38.739  1.00 19.04           O  
ANISOU 1006  OG1 THR A 156     2113   2548   2574     94   -432     32       O  
ATOM   1007  CG2 THR A 156      -9.625   9.038 -37.327  1.00 19.37           C  
ANISOU 1007  CG2 THR A 156     2134   2609   2616    145   -498     67       C  
ATOM   1008  N   LEU A 157     -13.793  10.406 -36.863  1.00 16.97           N  
ANISOU 1008  N   LEU A 157     1991   2253   2202     90   -427     34       N  
ATOM   1009  CA  LEU A 157     -14.871  11.384 -36.956  1.00 15.63           C  
ANISOU 1009  CA  LEU A 157     1851   2070   2017     65   -403     15       C  
ATOM   1010  C   LEU A 157     -14.458  12.550 -37.847  1.00 14.75           C  
ANISOU 1010  C   LEU A 157     1712   1958   1935     42   -391     -2       C  
ATOM   1011  O   LEU A 157     -15.257  13.044 -38.652  1.00 15.13           O  
ANISOU 1011  O   LEU A 157     1771   1989   1990     33   -359     -8       O  
ATOM   1012  CB  LEU A 157     -15.263  11.866 -35.558  1.00 16.82           C  
ANISOU 1012  CB  LEU A 157     2037   2227   2125     50   -424      5       C  
ATOM   1013  CG  LEU A 157     -16.496  12.770 -35.528  1.00 21.09           C  
ANISOU 1013  CG  LEU A 157     2611   2750   2652     31   -394    -15       C  
ATOM   1014  CD1 LEU A 157     -17.695  12.087 -36.188  1.00 16.73           C  
ANISOU 1014  CD1 LEU A 157     2075   2178   2102     46   -356     -5       C  
ATOM   1015  CD2 LEU A 157     -16.823  13.170 -34.095  1.00 26.19           C  
ANISOU 1015  CD2 LEU A 157     3295   3404   3253     16   -411    -29       C  
ATOM   1016  N   ARG A 158     -13.193  12.970 -37.754  1.00 15.62           N  
ANISOU 1016  N   ARG A 158     1783   2086   2065     32   -417     -6       N  
ATOM   1017  CA  ARG A 158     -12.713  14.036 -38.626  1.00 17.16           C  
ANISOU 1017  CA  ARG A 158     1950   2279   2290      6   -402    -19       C  
ATOM   1018  C   ARG A 158     -12.847  13.656 -40.098  1.00 14.88           C  
ANISOU 1018  C   ARG A 158     1648   1979   2026     17   -362    -10       C  
ATOM   1019  O   ARG A 158     -13.265  14.487 -40.917  1.00 15.70           O  
ANISOU 1019  O   ARG A 158     1760   2069   2138     -2   -336    -17       O  
ATOM   1020  CB  ARG A 158     -11.266  14.393 -38.291  1.00 18.45           C  
ANISOU 1020  CB  ARG A 158     2067   2467   2475     -8   -437    -24       C  
ATOM   1021  CG  ARG A 158     -10.770  15.590 -39.091  1.00 17.36           C  
ANISOU 1021  CG  ARG A 158     1904   2325   2368    -41   -421    -38       C  
ATOM   1022  CD  ARG A 158      -9.324  15.941 -38.765  1.00 20.91           C  
ANISOU 1022  CD  ARG A 158     2301   2801   2844    -59   -454    -43       C  
ATOM   1023  NE  ARG A 158      -8.846  17.012 -39.630  1.00 21.80           N  
ANISOU 1023  NE  ARG A 158     2389   2907   2988    -94   -432    -54       N  
ATOM   1024  CZ  ARG A 158      -7.763  17.737 -39.390  1.00 28.02           C  
ANISOU 1024  CZ  ARG A 158     3137   3711   3800   -125   -456    -66       C  
ATOM   1025  NH1 ARG A 158      -6.991  17.500 -38.341  1.00 27.72           N  
ANISOU 1025  NH1 ARG A 158     3073   3699   3759   -126   -507    -68       N  
ATOM   1026  NH2 ARG A 158      -7.455  18.735 -40.213  1.00 25.80           N  
ANISOU 1026  NH2 ARG A 158     2840   3417   3544   -160   -429    -73       N  
ATOM   1027  N   ASP A 159     -12.498  12.413 -40.454  1.00 16.42           N  
ANISOU 1027  N   ASP A 159     1827   2178   2232     47   -356      5       N  
ATOM   1028  CA  ASP A 159     -12.706  11.918 -41.818  1.00 16.23           C  
ANISOU 1028  CA  ASP A 159     1800   2144   2224     57   -316     11       C  
ATOM   1029  C   ASP A 159     -14.156  12.092 -42.254  1.00 12.95           C  
ANISOU 1029  C   ASP A 159     1427   1706   1786     51   -291      9       C  
ATOM   1030  O   ASP A 159     -14.442  12.687 -43.295  1.00 13.41           O  
ANISOU 1030  O   ASP A 159     1489   1756   1852     35   -266      6       O  
ATOM   1031  CB  ASP A 159     -12.341  10.433 -41.927  1.00 16.58           C  
ANISOU 1031  CB  ASP A 159     1833   2188   2278     93   -312     24       C  
ATOM   1032  CG  ASP A 159     -10.848  10.158 -41.780  1.00 20.73           C  
ANISOU 1032  CG  ASP A 159     2305   2735   2838    106   -331     28       C  
ATOM   1033  OD1 ASP A 159     -10.025  11.067 -42.029  1.00 16.38           O  
ANISOU 1033  OD1 ASP A 159     1717   2198   2308     82   -333     18       O  
ATOM   1034  OD2 ASP A 159     -10.515   9.003 -41.428  1.00 21.79           O  
ANISOU 1034  OD2 ASP A 159     2431   2869   2979    140   -342     41       O  
ATOM   1035  N   SER A 160     -15.083  11.535 -41.471  1.00 14.00           N  
ANISOU 1035  N   SER A 160     1594   1831   1893     63   -299     14       N  
ATOM   1036  CA  SER A 160     -16.492  11.575 -41.845  1.00 14.65           C  
ANISOU 1036  CA  SER A 160     1711   1896   1961     60   -277     13       C  
ATOM   1037  C   SER A 160     -16.992  13.005 -41.909  1.00 13.38           C  
ANISOU 1037  C   SER A 160     1559   1726   1799     34   -274      1       C  
ATOM   1038  O   SER A 160     -17.679  13.380 -42.863  1.00 13.58           O  
ANISOU 1038  O   SER A 160     1593   1739   1829     27   -253      3       O  
ATOM   1039  CB  SER A 160     -17.329  10.746 -40.861  1.00 12.89           C  
ANISOU 1039  CB  SER A 160     1519   1668   1712     74   -283     20       C  
ATOM   1040  OG  SER A 160     -16.955   9.374 -40.901  1.00 14.97           O  
ANISOU 1040  OG  SER A 160     1779   1930   1979     99   -284     34       O  
ATOM   1041  N   ALA A 161     -16.602  13.836 -40.931  1.00 12.69           N  
ANISOU 1041  N   ALA A 161     1469   1645   1706     20   -296    -10       N  
ATOM   1042  CA  ALA A 161     -17.060  15.223 -40.895  1.00 15.48           C  
ANISOU 1042  CA  ALA A 161     1835   1984   2062     -2   -292    -24       C  
ATOM   1043  C   ALA A 161     -16.497  16.025 -42.056  1.00 16.07           C  
ANISOU 1043  C   ALA A 161     1889   2054   2163    -21   -280    -23       C  
ATOM   1044  O   ALA A 161     -17.192  16.877 -42.614  1.00 16.17           O  
ANISOU 1044  O   ALA A 161     1915   2046   2181    -32   -265    -24       O  
ATOM   1045  CB  ALA A 161     -16.673  15.881 -39.568  1.00 15.24           C  
ANISOU 1045  CB  ALA A 161     1811   1961   2019    -16   -318    -41       C  
ATOM   1046  N   THR A 162     -15.245  15.770 -42.440  1.00 12.44           N  
ANISOU 1046  N   THR A 162     1396   1611   1721    -23   -284    -19       N  
ATOM   1047  CA  THR A 162     -14.667  16.508 -43.555  1.00 15.44           C  
ANISOU 1047  CA  THR A 162     1756   1987   2123    -44   -266    -17       C  
ATOM   1048  C   THR A 162     -15.415  16.209 -44.840  1.00 13.79           C  
ANISOU 1048  C   THR A 162     1563   1767   1911    -38   -237     -4       C  
ATOM   1049  O   THR A 162     -15.753  17.122 -45.600  1.00 13.40           O  
ANISOU 1049  O   THR A 162     1524   1700   1866    -56   -224      0       O  
ATOM   1050  CB  THR A 162     -13.185  16.177 -43.710  1.00 16.25           C  
ANISOU 1050  CB  THR A 162     1814   2113   2248    -47   -271    -16       C  
ATOM   1051  OG1 THR A 162     -12.500  16.533 -42.507  1.00 14.20           O  
ANISOU 1051  OG1 THR A 162     1539   1866   1990    -57   -306    -28       O  
ATOM   1052  CG2 THR A 162     -12.581  16.953 -44.881  1.00 13.82           C  
ANISOU 1052  CG2 THR A 162     1488   1802   1962    -73   -246    -14       C  
ATOM   1053  N   VAL A 163     -15.683  14.929 -45.100  1.00 12.59           N  
ANISOU 1053  N   VAL A 163     1414   1620   1749    -14   -228      4       N  
ATOM   1054  CA  VAL A 163     -16.425  14.565 -46.299  1.00 14.19           C  
ANISOU 1054  CA  VAL A 163     1635   1814   1944    -11   -205     13       C  
ATOM   1055  C   VAL A 163     -17.811  15.192 -46.262  1.00 13.07           C  
ANISOU 1055  C   VAL A 163     1523   1652   1791    -15   -207     16       C  
ATOM   1056  O   VAL A 163     -18.227  15.866 -47.209  1.00 12.27           O  
ANISOU 1056  O   VAL A 163     1431   1539   1691    -29   -197     24       O  
ATOM   1057  CB  VAL A 163     -16.502  13.033 -46.451  1.00 13.17           C  
ANISOU 1057  CB  VAL A 163     1507   1690   1807     14   -196     16       C  
ATOM   1058  CG1 VAL A 163     -17.483  12.678 -47.558  1.00 12.68           C  
ANISOU 1058  CG1 VAL A 163     1470   1617   1730     13   -177     23       C  
ATOM   1059  CG2 VAL A 163     -15.109  12.456 -46.797  1.00 14.54           C  
ANISOU 1059  CG2 VAL A 163     1647   1879   1999     22   -186     15       C  
ATOM   1060  N   PHE A 164     -18.544  14.987 -45.161  1.00 14.20           N  
ANISOU 1060  N   PHE A 164     1679   1791   1924     -3   -220     10       N  
ATOM   1061  CA  PHE A 164     -19.908  15.508 -45.092  1.00 13.62           C  
ANISOU 1061  CA  PHE A 164     1628   1700   1847     -4   -219     11       C  
ATOM   1062  C   PHE A 164     -19.913  17.024 -45.226  1.00 12.00           C  
ANISOU 1062  C   PHE A 164     1425   1479   1656    -22   -221      8       C  
ATOM   1063  O   PHE A 164     -20.681  17.584 -46.017  1.00 12.29           O  
ANISOU 1063  O   PHE A 164     1472   1499   1698    -26   -215     18       O  
ATOM   1064  CB  PHE A 164     -20.595  15.084 -43.791  1.00 12.80           C  
ANISOU 1064  CB  PHE A 164     1537   1597   1730      9   -227      2       C  
ATOM   1065  CG  PHE A 164     -22.110  15.211 -43.843  1.00 14.10           C  
ANISOU 1065  CG  PHE A 164     1717   1746   1893     15   -218      4       C  
ATOM   1066  CD1 PHE A 164     -22.722  16.462 -43.770  1.00 13.16           C  
ANISOU 1066  CD1 PHE A 164     1604   1609   1787      8   -217     -1       C  
ATOM   1067  CD2 PHE A 164     -22.911  14.086 -43.979  1.00 16.32           C  
ANISOU 1067  CD2 PHE A 164     2005   2030   2164     26   -211     11       C  
ATOM   1068  CE1 PHE A 164     -24.116  16.586 -43.821  1.00 13.20           C  
ANISOU 1068  CE1 PHE A 164     1615   1601   1798     16   -210      1       C  
ATOM   1069  CE2 PHE A 164     -24.321  14.201 -44.047  1.00 14.49           C  
ANISOU 1069  CE2 PHE A 164     1780   1787   1937     29   -204     13       C  
ATOM   1070  CZ  PHE A 164     -24.916  15.452 -43.961  1.00 12.04           C  
ANISOU 1070  CZ  PHE A 164     1470   1462   1643     26   -204      8       C  
ATOM   1071  N   ALA A 165     -19.050  17.703 -44.467  1.00 12.79           N  
ANISOU 1071  N   ALA A 165     1516   1580   1763    -34   -232     -5       N  
ATOM   1072  CA  ALA A 165     -19.005  19.162 -44.506  1.00 12.45           C  
ANISOU 1072  CA  ALA A 165     1478   1516   1736    -54   -233    -10       C  
ATOM   1073  C   ALA A 165     -18.622  19.677 -45.888  1.00 13.82           C  
ANISOU 1073  C   ALA A 165     1647   1682   1922    -71   -220      7       C  
ATOM   1074  O   ALA A 165     -19.239  20.620 -46.398  1.00 12.93           O  
ANISOU 1074  O   ALA A 165     1549   1544   1819    -78   -216     16       O  
ATOM   1075  CB  ALA A 165     -18.037  19.695 -43.449  1.00 11.41           C  
ANISOU 1075  CB  ALA A 165     1337   1390   1608    -70   -249    -30       C  
ATOM   1076  N   LEU A 166     -17.582  19.100 -46.503  1.00 11.71           N  
ANISOU 1076  N   LEU A 166     1360   1436   1655    -77   -213     13       N  
ATOM   1077  CA  LEU A 166     -17.172  19.588 -47.817  1.00 12.08           C  
ANISOU 1077  CA  LEU A 166     1405   1477   1708    -97   -196     29       C  
ATOM   1078  C   LEU A 166     -18.284  19.408 -48.839  1.00 15.54           C  
ANISOU 1078  C   LEU A 166     1867   1905   2132    -89   -188     48       C  
ATOM   1079  O   LEU A 166     -18.543  20.299 -49.662  1.00 14.68           O  
ANISOU 1079  O   LEU A 166     1774   1777   2027   -104   -183     64       O  
ATOM   1080  CB  LEU A 166     -15.919  18.863 -48.291  1.00 16.49           C  
ANISOU 1080  CB  LEU A 166     1936   2062   2269   -102   -182     29       C  
ATOM   1081  CG  LEU A 166     -14.570  19.384 -47.841  1.00 20.42           C  
ANISOU 1081  CG  LEU A 166     2400   2569   2788   -123   -185     17       C  
ATOM   1082  CD1 LEU A 166     -13.504  18.392 -48.252  1.00 22.06           C  
ANISOU 1082  CD1 LEU A 166     2574   2805   3001   -116   -170     17       C  
ATOM   1083  CD2 LEU A 166     -14.314  20.761 -48.448  1.00 19.46           C  
ANISOU 1083  CD2 LEU A 166     2287   2427   2681   -158   -175     25       C  
ATOM   1084  N   SER A 167     -18.956  18.259 -48.807  1.00 11.95           N  
ANISOU 1084  N   SER A 167     1417   1461   1662    -66   -189     47       N  
ATOM   1085  CA  SER A 167     -20.000  18.041 -49.790  1.00 14.94           C  
ANISOU 1085  CA  SER A 167     1816   1834   2027    -62   -187     64       C  
ATOM   1086  C   SER A 167     -21.152  19.000 -49.548  1.00 15.36           C  
ANISOU 1086  C   SER A 167     1884   1861   2091    -58   -200     71       C  
ATOM   1087  O   SER A 167     -21.735  19.524 -50.499  1.00 13.42           O  
ANISOU 1087  O   SER A 167     1653   1603   1844    -64   -203     91       O  
ATOM   1088  CB  SER A 167     -20.470  16.583 -49.758  1.00 11.98           C  
ANISOU 1088  CB  SER A 167     1443   1474   1636    -43   -185     59       C  
ATOM   1089  OG  SER A 167     -21.308  16.352 -48.642  1.00 15.63           O  
ANISOU 1089  OG  SER A 167     1907   1932   2101    -26   -197     50       O  
ATOM   1090  N   THR A 168     -21.465  19.280 -48.280  1.00 15.11           N  
ANISOU 1090  N   THR A 168     1849   1822   2072    -48   -209     54       N  
ATOM   1091  CA  THR A 168     -22.481  20.292 -47.995  1.00 13.71           C  
ANISOU 1091  CA  THR A 168     1682   1616   1911    -42   -216     56       C  
ATOM   1092  C   THR A 168     -22.024  21.683 -48.439  1.00 16.49           C  
ANISOU 1092  C   THR A 168     2042   1943   2281    -61   -215     66       C  
ATOM   1093  O   THR A 168     -22.810  22.451 -49.016  1.00 17.30           O  
ANISOU 1093  O   THR A 168     2157   2020   2396    -58   -221     84       O  
ATOM   1094  CB  THR A 168     -22.820  20.288 -46.505  1.00 11.60           C  
ANISOU 1094  CB  THR A 168     1413   1346   1649    -29   -218     32       C  
ATOM   1095  OG1 THR A 168     -23.188  18.959 -46.108  1.00 14.11           O  
ANISOU 1095  OG1 THR A 168     1727   1686   1949    -14   -216     27       O  
ATOM   1096  CG2 THR A 168     -23.975  21.226 -46.206  1.00 12.83           C  
ANISOU 1096  CG2 THR A 168     1578   1472   1826    -18   -219     30       C  
ATOM   1097  N   MET A 169     -20.765  22.037 -48.168  1.00 13.27           N  
ANISOU 1097  N   MET A 169     1626   1539   1878    -82   -211     55       N  
ATOM   1098  CA  MET A 169     -20.294  23.374 -48.514  1.00 15.65           C  
ANISOU 1098  CA  MET A 169     1935   1812   2198   -105   -208     63       C  
ATOM   1099  C   MET A 169     -20.243  23.589 -50.017  1.00 18.07           C  
ANISOU 1099  C   MET A 169     2253   2114   2497   -119   -201     96       C  
ATOM   1100  O   MET A 169     -20.426  24.719 -50.481  1.00 19.60           O  
ANISOU 1100  O   MET A 169     2465   2276   2707   -130   -202    113       O  
ATOM   1101  CB  MET A 169     -18.908  23.623 -47.934  1.00 16.43           C  
ANISOU 1101  CB  MET A 169     2017   1920   2304   -129   -205     44       C  
ATOM   1102  CG  MET A 169     -18.829  23.584 -46.437  1.00 18.68           C  
ANISOU 1102  CG  MET A 169     2297   2209   2591   -123   -217     12       C  
ATOM   1103  SD  MET A 169     -17.192  22.953 -46.047  1.00 19.84           S  
ANISOU 1103  SD  MET A 169     2411   2395   2734   -141   -220     -2       S  
ATOM   1104  CE  MET A 169     -16.249  24.469 -46.075  1.00 16.87           C  
ANISOU 1104  CE  MET A 169     2033   1993   2385   -183   -219     -8       C  
ATOM   1105  N   ILE A 170     -19.986  22.530 -50.783  1.00 15.94           N  
ANISOU 1105  N   ILE A 170     1978   1874   2203   -118   -193    104       N  
ATOM   1106  CA  ILE A 170     -19.890  22.642 -52.234  1.00 18.47           C  
ANISOU 1106  CA  ILE A 170     2315   2196   2507   -134   -184    133       C  
ATOM   1107  C   ILE A 170     -21.264  22.532 -52.883  1.00 15.45           C  
ANISOU 1107  C   ILE A 170     1953   1805   2114   -117   -200    155       C  
ATOM   1108  O   ILE A 170     -21.580  23.269 -53.819  1.00 16.18           O  
ANISOU 1108  O   ILE A 170     2067   1879   2202   -128   -205    185       O  
ATOM   1109  CB  ILE A 170     -18.921  21.574 -52.779  1.00 16.27           C  
ANISOU 1109  CB  ILE A 170     2022   1952   2206   -143   -163    127       C  
ATOM   1110  CG1 ILE A 170     -17.482  21.882 -52.333  1.00 21.79           C  
ANISOU 1110  CG1 ILE A 170     2696   2659   2923   -164   -148    111       C  
ATOM   1111  CG2 ILE A 170     -19.018  21.504 -54.303  1.00 20.12           C  
ANISOU 1111  CG2 ILE A 170     2534   2444   2666   -159   -151    154       C  
ATOM   1112  CD1 ILE A 170     -16.992  23.294 -52.749  1.00 21.33           C  
ANISOU 1112  CD1 ILE A 170     2648   2574   2881   -197   -140    127       C  
ATOM   1113  N   SER A 171     -22.097  21.621 -52.392  1.00 15.75           N  
ANISOU 1113  N   SER A 171     1982   1856   2146    -93   -210    143       N  
ATOM   1114  CA  SER A 171     -23.386  21.370 -53.024  1.00 15.16           C  
ANISOU 1114  CA  SER A 171     1919   1780   2062    -79   -228    162       C  
ATOM   1115  C   SER A 171     -24.352  22.531 -52.792  1.00 14.84           C  
ANISOU 1115  C   SER A 171     1884   1703   2052    -66   -246    176       C  
ATOM   1116  O   SER A 171     -24.271  23.250 -51.796  1.00 14.91           O  
ANISOU 1116  O   SER A 171     1886   1690   2088    -60   -243    159       O  
ATOM   1117  CB  SER A 171     -24.005  20.085 -52.472  1.00 16.17           C  
ANISOU 1117  CB  SER A 171     2034   1928   2181    -59   -231    143       C  
ATOM   1118  OG  SER A 171     -24.539  20.324 -51.175  1.00 17.35           O  
ANISOU 1118  OG  SER A 171     2171   2066   2357    -41   -235    125       O  
ATOM   1119  N   SER A 172     -25.265  22.722 -53.741  1.00 16.23           N  
ANISOU 1119  N   SER A 172     2072   1872   2221    -62   -266    206       N  
ATOM   1120  CA  SER A 172     -26.440  23.551 -53.498  1.00 15.75           C  
ANISOU 1120  CA  SER A 172     2009   1781   2195    -39   -286    219       C  
ATOM   1121  C   SER A 172     -27.657  22.720 -53.107  1.00 17.78           C  
ANISOU 1121  C   SER A 172     2246   2053   2458    -15   -299    209       C  
ATOM   1122  O   SER A 172     -28.609  23.266 -52.532  1.00 15.38           O  
ANISOU 1122  O   SER A 172     1927   1726   2189      9   -308    208       O  
ATOM   1123  CB  SER A 172     -26.771  24.387 -54.741  1.00 16.46           C  
ANISOU 1123  CB  SER A 172     2122   1850   2281    -47   -307    263       C  
ATOM   1124  OG  SER A 172     -26.840  23.563 -55.892  1.00 18.38           O  
ANISOU 1124  OG  SER A 172     2379   2124   2481    -61   -317    281       O  
ATOM   1125  N   ILE A 173     -27.647  21.422 -53.419  1.00 16.10           N  
ANISOU 1125  N   ILE A 173     2029   1874   2213    -22   -298    201       N  
ATOM   1126  CA  ILE A 173     -28.680  20.483 -53.000  1.00 14.74           C  
ANISOU 1126  CA  ILE A 173     1838   1719   2045     -6   -305    188       C  
ATOM   1127  C   ILE A 173     -27.972  19.320 -52.318  1.00 14.02           C  
ANISOU 1127  C   ILE A 173     1741   1651   1934    -11   -282    158       C  
ATOM   1128  O   ILE A 173     -27.221  18.580 -52.968  1.00 14.71           O  
ANISOU 1128  O   ILE A 173     1841   1758   1989    -27   -274    157       O  
ATOM   1129  CB  ILE A 173     -29.515  19.975 -54.182  1.00 17.92           C  
ANISOU 1129  CB  ILE A 173     2245   2137   2428    -11   -333    212       C  
ATOM   1130  CG1 ILE A 173     -30.250  21.125 -54.875  1.00 18.26           C  
ANISOU 1130  CG1 ILE A 173     2292   2156   2491     -3   -363    249       C  
ATOM   1131  CG2 ILE A 173     -30.486  18.895 -53.698  1.00 16.53           C  
ANISOU 1131  CG2 ILE A 173     2045   1978   2256     -1   -336    195       C  
ATOM   1132  CD1 ILE A 173     -30.756  20.725 -56.275  1.00 23.99           C  
ANISOU 1132  CD1 ILE A 173     3032   2900   3183    -18   -395    278       C  
ATOM   1133  N   GLN A 174     -28.209  19.149 -51.024  1.00 13.70           N  
ANISOU 1133  N   GLN A 174     1686   1608   1913      4   -270    134       N  
ATOM   1134  CA  GLN A 174     -27.624  18.058 -50.255  1.00 15.53           C  
ANISOU 1134  CA  GLN A 174     1913   1859   2127      3   -252    109       C  
ATOM   1135  C   GLN A 174     -28.738  17.092 -49.899  1.00 13.35           C  
ANISOU 1135  C   GLN A 174     1625   1593   1853     13   -254    102       C  
ATOM   1136  O   GLN A 174     -29.690  17.464 -49.199  1.00 15.17           O  
ANISOU 1136  O   GLN A 174     1841   1814   2109     28   -254     97       O  
ATOM   1137  CB  GLN A 174     -26.934  18.563 -48.984  1.00 12.63           C  
ANISOU 1137  CB  GLN A 174     1544   1483   1773      8   -238     87       C  
ATOM   1138  CG  GLN A 174     -26.369  17.451 -48.091  1.00 14.10           C  
ANISOU 1138  CG  GLN A 174     1728   1689   1942      9   -225     66       C  
ATOM   1139  CD  GLN A 174     -25.171  16.740 -48.700  1.00 14.53           C  
ANISOU 1139  CD  GLN A 174     1786   1762   1974     -3   -220     68       C  
ATOM   1140  OE1 GLN A 174     -25.316  15.867 -49.578  1.00 14.97           O  
ANISOU 1140  OE1 GLN A 174     1847   1829   2013     -7   -220     75       O  
ATOM   1141  NE2 GLN A 174     -23.969  17.095 -48.227  1.00 14.34           N  
ANISOU 1141  NE2 GLN A 174     1759   1739   1952     -9   -214     58       N  
ATOM   1142  N   VAL A 175     -28.617  15.861 -50.382  1.00 11.67           N  
ANISOU 1142  N   VAL A 175     1418   1400   1615      4   -253    100       N  
ATOM   1143  CA  VAL A 175     -29.538  14.795 -50.025  1.00 13.00           C  
ANISOU 1143  CA  VAL A 175     1578   1578   1784      8   -252     92       C  
ATOM   1144  C   VAL A 175     -28.908  14.062 -48.850  1.00 13.90           C  
ANISOU 1144  C   VAL A 175     1694   1698   1891     13   -230     71       C  
ATOM   1145  O   VAL A 175     -27.949  13.313 -49.011  1.00 15.80           O  
ANISOU 1145  O   VAL A 175     1946   1947   2111      8   -222     66       O  
ATOM   1146  CB  VAL A 175     -29.806  13.851 -51.195  1.00 12.55           C  
ANISOU 1146  CB  VAL A 175     1530   1535   1704     -8   -263     99       C  
ATOM   1147  CG1 VAL A 175     -30.790  12.749 -50.764  1.00 14.32           C  
ANISOU 1147  CG1 VAL A 175     1744   1766   1932     -8   -261     89       C  
ATOM   1148  CG2 VAL A 175     -30.330  14.632 -52.393  1.00 13.75           C  
ANISOU 1148  CG2 VAL A 175     1685   1685   1856    -15   -290    124       C  
ATOM   1149  N   TYR A 176     -29.427  14.320 -47.664  1.00 14.10           N  
ANISOU 1149  N   TYR A 176     1709   1716   1932     25   -221     60       N  
ATOM   1150  CA  TYR A 176     -28.987  13.655 -46.447  1.00 12.16           C  
ANISOU 1150  CA  TYR A 176     1469   1475   1675     29   -204     44       C  
ATOM   1151  C   TYR A 176     -29.710  12.320 -46.397  1.00 13.27           C  
ANISOU 1151  C   TYR A 176     1610   1624   1809     26   -198     44       C  
ATOM   1152  O   TYR A 176     -30.926  12.268 -46.178  1.00 11.66           O  
ANISOU 1152  O   TYR A 176     1393   1418   1621     26   -196     44       O  
ATOM   1153  CB  TYR A 176     -29.332  14.533 -45.253  1.00 10.89           C  
ANISOU 1153  CB  TYR A 176     1303   1303   1530     39   -194     32       C  
ATOM   1154  CG  TYR A 176     -28.890  14.068 -43.904  1.00 10.27           C  
ANISOU 1154  CG  TYR A 176     1236   1231   1435     42   -180     17       C  
ATOM   1155  CD1 TYR A 176     -27.830  13.176 -43.745  1.00 11.19           C  
ANISOU 1155  CD1 TYR A 176     1364   1358   1528     40   -182     17       C  
ATOM   1156  CD2 TYR A 176     -29.547  14.529 -42.767  1.00 11.41           C  
ANISOU 1156  CD2 TYR A 176     1380   1368   1587     49   -164      2       C  
ATOM   1157  CE1 TYR A 176     -27.430  12.779 -42.463  1.00 13.58           C  
ANISOU 1157  CE1 TYR A 176     1679   1667   1814     43   -175      7       C  
ATOM   1158  CE2 TYR A 176     -29.168  14.147 -41.522  1.00 11.58           C  
ANISOU 1158  CE2 TYR A 176     1417   1397   1586     49   -153    -10       C  
ATOM   1159  CZ  TYR A 176     -28.106  13.275 -41.367  1.00 13.59           C  
ANISOU 1159  CZ  TYR A 176     1685   1664   1816     46   -162     -6       C  
ATOM   1160  OH  TYR A 176     -27.735  12.919 -40.103  1.00 12.22           O  
ANISOU 1160  OH  TYR A 176     1529   1497   1618     46   -157    -14       O  
ATOM   1161  N   ASN A 177     -28.987  11.248 -46.663  1.00 11.11           N  
ANISOU 1161  N   ASN A 177     1350   1357   1516     21   -196     43       N  
ATOM   1162  CA  ASN A 177     -29.601   9.943 -46.847  1.00 13.40           C  
ANISOU 1162  CA  ASN A 177     1645   1649   1799     13   -191     42       C  
ATOM   1163  C   ASN A 177     -29.609   9.192 -45.512  1.00 12.46           C  
ANISOU 1163  C   ASN A 177     1534   1528   1674     19   -174     36       C  
ATOM   1164  O   ASN A 177     -28.552   8.904 -44.939  1.00 13.61           O  
ANISOU 1164  O   ASN A 177     1691   1674   1807     27   -170     33       O  
ATOM   1165  CB  ASN A 177     -28.838   9.191 -47.938  1.00 13.28           C  
ANISOU 1165  CB  ASN A 177     1644   1636   1766      5   -194     44       C  
ATOM   1166  CG  ASN A 177     -29.480   7.870 -48.307  1.00 12.07           C  
ANISOU 1166  CG  ASN A 177     1499   1480   1606     -7   -190     41       C  
ATOM   1167  OD1 ASN A 177     -30.493   7.836 -48.990  1.00 14.65           O  
ANISOU 1167  OD1 ASN A 177     1819   1809   1937    -21   -202     44       O  
ATOM   1168  ND2 ASN A 177     -28.859   6.777 -47.893  1.00 10.58           N  
ANISOU 1168  ND2 ASN A 177     1327   1286   1408     -2   -177     35       N  
ATOM   1169  N   LEU A 178     -30.795   8.915 -45.001  1.00 11.65           N  
ANISOU 1169  N   LEU A 178     1423   1423   1581     14   -164     34       N  
ATOM   1170  CA  LEU A 178     -30.958   8.286 -43.705  1.00 14.80           C  
ANISOU 1170  CA  LEU A 178     1832   1820   1971     16   -145     31       C  
ATOM   1171  C   LEU A 178     -31.713   6.979 -43.889  1.00 14.20           C  
ANISOU 1171  C   LEU A 178     1761   1739   1895      2   -136     34       C  
ATOM   1172  O   LEU A 178     -32.409   6.786 -44.887  1.00 16.18           O  
ANISOU 1172  O   LEU A 178     2000   1991   2157    -11   -146     35       O  
ATOM   1173  CB  LEU A 178     -31.722   9.198 -42.738  1.00 14.61           C  
ANISOU 1173  CB  LEU A 178     1795   1796   1959     21   -131     24       C  
ATOM   1174  CG  LEU A 178     -31.133  10.579 -42.480  1.00 18.02           C  
ANISOU 1174  CG  LEU A 178     2225   2227   2395     33   -138     17       C  
ATOM   1175  CD1 LEU A 178     -31.942  11.629 -43.251  1.00 16.83           C  
ANISOU 1175  CD1 LEU A 178     2048   2071   2274     35   -146     19       C  
ATOM   1176  CD2 LEU A 178     -31.196  10.849 -41.007  1.00 18.20           C  
ANISOU 1176  CD2 LEU A 178     2259   2250   2406     37   -118      5       C  
ATOM   1177  N   SER A 179     -31.597   6.100 -42.903  1.00 12.91           N  
ANISOU 1177  N   SER A 179     1618   1570   1718      1   -120     36       N  
ATOM   1178  CA  SER A 179     -32.232   4.789 -42.939  1.00 15.51           C  
ANISOU 1178  CA  SER A 179     1957   1890   2047    -15   -108     39       C  
ATOM   1179  C   SER A 179     -33.357   4.717 -41.908  1.00 14.93           C  
ANISOU 1179  C   SER A 179     1877   1817   1980    -25    -83     39       C  
ATOM   1180  O   SER A 179     -33.119   4.939 -40.717  1.00 14.75           O  
ANISOU 1180  O   SER A 179     1868   1796   1941    -17    -69     40       O  
ATOM   1181  CB  SER A 179     -31.199   3.695 -42.688  1.00 16.13           C  
ANISOU 1181  CB  SER A 179     2067   1955   2106     -7   -106     46       C  
ATOM   1182  OG  SER A 179     -31.833   2.452 -42.569  1.00 19.32           O  
ANISOU 1182  OG  SER A 179     2486   2344   2511    -24    -92     50       O  
ATOM   1183  N   GLN A 180     -34.579   4.433 -42.386  1.00 11.58           N  
ANISOU 1183  N   GLN A 180     1430   1392   1576    -45    -78     37       N  
ATOM   1184  CA  GLN A 180     -35.767   4.072 -41.606  1.00 13.91           C  
ANISOU 1184  CA  GLN A 180     1715   1688   1884    -62    -49     37       C  
ATOM   1185  C   GLN A 180     -36.433   5.220 -40.850  1.00 14.81           C  
ANISOU 1185  C   GLN A 180     1803   1812   2011    -53    -31     29       C  
ATOM   1186  O   GLN A 180     -37.664   5.294 -40.802  1.00 15.33           O  
ANISOU 1186  O   GLN A 180     1837   1883   2105    -66    -16     26       O  
ATOM   1187  CB  GLN A 180     -35.442   2.946 -40.612  1.00 14.63           C  
ANISOU 1187  CB  GLN A 180     1845   1765   1950    -68    -27     46       C  
ATOM   1188  CG  GLN A 180     -35.136   1.624 -41.317  1.00 16.10           C  
ANISOU 1188  CG  GLN A 180     2054   1933   2132    -81    -35     52       C  
ATOM   1189  CD  GLN A 180     -34.780   0.513 -40.353  1.00 19.05           C  
ANISOU 1189  CD  GLN A 180     2469   2287   2484    -84    -16     66       C  
ATOM   1190  OE1 GLN A 180     -34.293   0.760 -39.259  1.00 26.74           O  
ANISOU 1190  OE1 GLN A 180     3462   3264   3435    -70     -7     74       O  
ATOM   1191  NE2 GLN A 180     -35.027  -0.717 -40.756  1.00 20.02           N  
ANISOU 1191  NE2 GLN A 180     2608   2388   2612   -104    -11     70       N  
ATOM   1192  N   ASN A 181     -35.652   6.095 -40.231  1.00 15.40           N  
ANISOU 1192  N   ASN A 181     1891   1891   2071    -32    -32     25       N  
ATOM   1193  CA  ASN A 181     -36.217   7.094 -39.330  1.00 15.25           C  
ANISOU 1193  CA  ASN A 181     1857   1877   2060    -24     -7     13       C  
ATOM   1194  C   ASN A 181     -35.238   8.256 -39.251  1.00 15.58           C  
ANISOU 1194  C   ASN A 181     1908   1920   2093     -2    -25      6       C  
ATOM   1195  O   ASN A 181     -34.089   8.156 -39.677  1.00 15.88           O  
ANISOU 1195  O   ASN A 181     1964   1957   2113      4    -50     12       O  
ATOM   1196  CB  ASN A 181     -36.468   6.495 -37.939  1.00 13.59           C  
ANISOU 1196  CB  ASN A 181     1672   1666   1824    -34     31     13       C  
ATOM   1197  CG  ASN A 181     -37.502   7.265 -37.119  1.00 16.04           C  
ANISOU 1197  CG  ASN A 181     1961   1983   2152    -34     70     -3       C  
ATOM   1198  OD1 ASN A 181     -37.975   8.332 -37.504  1.00 17.63           O  
ANISOU 1198  OD1 ASN A 181     2127   2186   2387    -21     67    -14       O  
ATOM   1199  ND2 ASN A 181     -37.854   6.706 -35.966  1.00 19.53           N  
ANISOU 1199  ND2 ASN A 181     2425   2425   2569    -48    109     -2       N  
ATOM   1200  N   VAL A 182     -35.710   9.366 -38.716  1.00 14.84           N  
ANISOU 1200  N   VAL A 182     1798   1827   2013      8     -8     -9       N  
ATOM   1201  CA  VAL A 182     -34.854  10.493 -38.377  1.00 18.68           C  
ANISOU 1201  CA  VAL A 182     2297   2310   2489     24    -17    -20       C  
ATOM   1202  C   VAL A 182     -34.743  10.493 -36.863  1.00 18.77           C  
ANISOU 1202  C   VAL A 182     2339   2325   2468     21     14    -32       C  
ATOM   1203  O   VAL A 182     -35.711  10.807 -36.156  1.00 20.08           O  
ANISOU 1203  O   VAL A 182     2495   2490   2643     20     51    -46       O  
ATOM   1204  CB  VAL A 182     -35.407  11.822 -38.903  1.00 15.80           C  
ANISOU 1204  CB  VAL A 182     1899   1938   2165     38    -21    -28       C  
ATOM   1205  CG1 VAL A 182     -34.588  12.987 -38.347  1.00 17.99           C  
ANISOU 1205  CG1 VAL A 182     2195   2208   2431     50    -23    -44       C  
ATOM   1206  CG2 VAL A 182     -35.382  11.837 -40.417  1.00 17.45           C  
ANISOU 1206  CG2 VAL A 182     2087   2146   2397     39    -57    -12       C  
ATOM   1207  N   GLN A 183     -33.581  10.106 -36.360  1.00 15.58           N  
ANISOU 1207  N   GLN A 183     1972   1925   2023     20     -1    -27       N  
ATOM   1208  CA  GLN A 183     -33.365   9.986 -34.930  1.00 13.60           C  
ANISOU 1208  CA  GLN A 183     1757   1679   1730     15     20    -34       C  
ATOM   1209  C   GLN A 183     -32.602  11.198 -34.437  1.00 15.03           C  
ANISOU 1209  C   GLN A 183     1952   1861   1898     23     10    -54       C  
ATOM   1210  O   GLN A 183     -31.988  11.936 -35.213  1.00 13.76           O  
ANISOU 1210  O   GLN A 183     1776   1695   1756     32    -18    -56       O  
ATOM   1211  CB  GLN A 183     -32.584   8.715 -34.597  1.00 13.94           C  
ANISOU 1211  CB  GLN A 183     1835   1727   1736      8      6    -12       C  
ATOM   1212  CG  GLN A 183     -33.171   7.432 -35.165  1.00 18.48           C  
ANISOU 1212  CG  GLN A 183     2402   2295   2324     -2     13      7       C  
ATOM   1213  CD  GLN A 183     -32.267   6.243 -34.907  1.00 19.27           C  
ANISOU 1213  CD  GLN A 183     2537   2392   2393     -3     -5     30       C  
ATOM   1214  OE1 GLN A 183     -31.170   6.383 -34.336  1.00 20.58           O  
ANISOU 1214  OE1 GLN A 183     2727   2563   2528      7    -26     33       O  
ATOM   1215  NE2 GLN A 183     -32.736   5.057 -35.288  1.00 18.14           N  
ANISOU 1215  NE2 GLN A 183     2396   2238   2259    -14      4     46       N  
ATOM   1216  N   GLU A 184     -32.601  11.370 -33.119  1.00 15.52           N  
ANISOU 1216  N   GLU A 184     2046   1928   1922     16     32    -68       N  
ATOM   1217  CA  GLU A 184     -31.943  12.542 -32.552  1.00 15.15           C  
ANISOU 1217  CA  GLU A 184     2016   1881   1860     19     24    -93       C  
ATOM   1218  C   GLU A 184     -30.435  12.530 -32.801  1.00 17.62           C  
ANISOU 1218  C   GLU A 184     2340   2200   2156     21    -25    -83       C  
ATOM   1219  O   GLU A 184     -29.837  13.604 -32.973  1.00 19.10           O  
ANISOU 1219  O   GLU A 184     2522   2381   2353     24    -43    -99       O  
ATOM   1220  CB  GLU A 184     -32.247  12.643 -31.058  1.00 15.04           C  
ANISOU 1220  CB  GLU A 184     2040   1873   1800      8     59   -112       C  
ATOM   1221  CG  GLU A 184     -32.034  14.028 -30.490  1.00 20.84           C  
ANISOU 1221  CG  GLU A 184     2788   2601   2529      9     66   -148       C  
ATOM   1222  CD  GLU A 184     -32.942  15.091 -31.117  1.00 18.57           C  
ANISOU 1222  CD  GLU A 184     2461   2293   2301     23     90   -168       C  
ATOM   1223  OE1 GLU A 184     -34.023  14.755 -31.665  1.00 17.89           O  
ANISOU 1223  OE1 GLU A 184     2341   2203   2255     30    114   -158       O  
ATOM   1224  OE2 GLU A 184     -32.564  16.271 -31.043  1.00 20.99           O  
ANISOU 1224  OE2 GLU A 184     2772   2586   2617     27     84   -193       O  
ATOM   1225  N   ASP A 185     -29.794  11.349 -32.817  1.00 14.45           N  
ANISOU 1225  N   ASP A 185     1952   1808   1732     19    -47    -56       N  
ATOM   1226  CA  ASP A 185     -28.372  11.321 -33.163  1.00 15.60           C  
ANISOU 1226  CA  ASP A 185     2097   1959   1871     24    -93    -46       C  
ATOM   1227  C   ASP A 185     -28.151  11.721 -34.616  1.00 17.72           C  
ANISOU 1227  C   ASP A 185     2329   2219   2186     33   -109    -43       C  
ATOM   1228  O   ASP A 185     -27.135  12.348 -34.936  1.00 17.05           O  
ANISOU 1228  O   ASP A 185     2235   2136   2106     34   -136    -47       O  
ATOM   1229  CB  ASP A 185     -27.741   9.947 -32.878  1.00 17.80           C  
ANISOU 1229  CB  ASP A 185     2397   2246   2122     26   -111    -18       C  
ATOM   1230  CG  ASP A 185     -28.441   8.804 -33.606  1.00 19.34           C  
ANISOU 1230  CG  ASP A 185     2580   2431   2337     28    -96      3       C  
ATOM   1231  OD1 ASP A 185     -29.679   8.813 -33.689  1.00 18.45           O  
ANISOU 1231  OD1 ASP A 185     2459   2312   2241     22    -62     -3       O  
ATOM   1232  OD2 ASP A 185     -27.754   7.893 -34.101  1.00 20.04           O  
ANISOU 1232  OD2 ASP A 185     2668   2517   2429     37   -118     24       O  
ATOM   1233  N   ASP A 186     -29.097  11.409 -35.504  1.00 14.84           N  
ANISOU 1233  N   ASP A 186     1940   1845   1852     35    -93    -35       N  
ATOM   1234  CA  ASP A 186     -29.006  11.934 -36.862  1.00 15.74           C  
ANISOU 1234  CA  ASP A 186     2024   1952   2004     41   -107    -32       C  
ATOM   1235  C   ASP A 186     -28.985  13.455 -36.866  1.00 16.53           C  
ANISOU 1235  C   ASP A 186     2115   2042   2122     42   -107    -53       C  
ATOM   1236  O   ASP A 186     -28.213  14.065 -37.610  1.00 14.48           O  
ANISOU 1236  O   ASP A 186     1845   1779   1877     43   -130    -51       O  
ATOM   1237  CB  ASP A 186     -30.165  11.437 -37.719  1.00 16.82           C  
ANISOU 1237  CB  ASP A 186     2139   2083   2169     41    -93    -23       C  
ATOM   1238  CG  ASP A 186     -30.193   9.938 -37.832  1.00 15.21           C  
ANISOU 1238  CG  ASP A 186     1945   1883   1953     36    -92     -4       C  
ATOM   1239  OD1 ASP A 186     -29.125   9.336 -38.059  1.00 16.82           O  
ANISOU 1239  OD1 ASP A 186     2159   2089   2143     40   -114      7       O  
ATOM   1240  OD2 ASP A 186     -31.276   9.361 -37.676  1.00 16.79           O  
ANISOU 1240  OD2 ASP A 186     2141   2080   2158     29    -69     -2       O  
ATOM   1241  N   LEU A 187     -29.841  14.085 -36.065  1.00 13.07           N  
ANISOU 1241  N   LEU A 187     1683   1598   1685     42    -79    -73       N  
ATOM   1242  CA  LEU A 187     -29.838  15.543 -36.013  1.00 12.36           C  
ANISOU 1242  CA  LEU A 187     1590   1493   1615     45    -76    -95       C  
ATOM   1243  C   LEU A 187     -28.540  16.060 -35.412  1.00 13.02           C  
ANISOU 1243  C   LEU A 187     1696   1581   1671     36    -99   -107       C  
ATOM   1244  O   LEU A 187     -27.985  17.056 -35.890  1.00 15.98           O  
ANISOU 1244  O   LEU A 187     2063   1942   2065     34   -114   -114       O  
ATOM   1245  CB  LEU A 187     -31.044  16.049 -35.223  1.00 12.84           C  
ANISOU 1245  CB  LEU A 187     1652   1543   1684     49    -35   -117       C  
ATOM   1246  CG  LEU A 187     -32.412  15.632 -35.756  1.00 15.22           C  
ANISOU 1246  CG  LEU A 187     1922   1841   2019     57    -12   -107       C  
ATOM   1247  CD1 LEU A 187     -33.546  16.337 -34.998  1.00 15.08           C  
ANISOU 1247  CD1 LEU A 187     1899   1811   2019     64     32   -132       C  
ATOM   1248  CD2 LEU A 187     -32.502  15.877 -37.284  1.00 11.90           C  
ANISOU 1248  CD2 LEU A 187     1469   1412   1641     65    -39    -87       C  
ATOM   1249  N   GLN A 188     -28.012  15.370 -34.400  1.00 14.86           N  
ANISOU 1249  N   GLN A 188     1956   1831   1859     28   -104   -108       N  
ATOM   1250  CA  GLN A 188     -26.763  15.819 -33.788  1.00 16.99           C  
ANISOU 1250  CA  GLN A 188     2244   2109   2102     17   -132   -119       C  
ATOM   1251  C   GLN A 188     -25.592  15.696 -34.750  1.00 15.93           C  
ANISOU 1251  C   GLN A 188     2088   1980   1984     17   -169   -101       C  
ATOM   1252  O   GLN A 188     -24.721  16.575 -34.781  1.00 16.42           O  
ANISOU 1252  O   GLN A 188     2148   2040   2052      7   -188   -114       O  
ATOM   1253  CB  GLN A 188     -26.486  15.038 -32.505  1.00 18.29           C  
ANISOU 1253  CB  GLN A 188     2444   2294   2212      9   -136   -118       C  
ATOM   1254  CG  GLN A 188     -27.524  15.283 -31.405  1.00 21.59           C  
ANISOU 1254  CG  GLN A 188     2890   2708   2605      3    -94   -141       C  
ATOM   1255  CD  GLN A 188     -27.333  14.373 -30.183  1.00 32.46           C  
ANISOU 1255  CD  GLN A 188     4307   4105   3920     -7    -96   -133       C  
ATOM   1256  OE1 GLN A 188     -27.716  14.734 -29.070  1.00 37.53           O  
ANISOU 1256  OE1 GLN A 188     4984   4750   4525    -18    -72   -156       O  
ATOM   1257  NE2 GLN A 188     -26.759  13.184 -30.393  1.00 30.51           N  
ANISOU 1257  NE2 GLN A 188     4060   3871   3663     -2   -122    -99       N  
ATOM   1258  N   HIS A 189     -25.531  14.596 -35.514  1.00 16.10           N  
ANISOU 1258  N   HIS A 189     2095   2010   2014     26   -175    -74       N  
ATOM   1259  CA  HIS A 189     -24.492  14.440 -36.532  1.00 14.49           C  
ANISOU 1259  CA  HIS A 189     1868   1810   1828     28   -201    -59       C  
ATOM   1260  C   HIS A 189     -24.592  15.544 -37.578  1.00 16.13           C  
ANISOU 1260  C   HIS A 189     2056   2001   2073     25   -198    -64       C  
ATOM   1261  O   HIS A 189     -23.584  16.141 -37.968  1.00 14.04           O  
ANISOU 1261  O   HIS A 189     1780   1736   1818     17   -216    -66       O  
ATOM   1262  CB  HIS A 189     -24.609  13.071 -37.227  1.00 15.68           C  
ANISOU 1262  CB  HIS A 189     2010   1965   1981     39   -200    -33       C  
ATOM   1263  CG  HIS A 189     -24.442  11.889 -36.317  1.00 23.17           C  
ANISOU 1263  CG  HIS A 189     2980   2925   2898     43   -204    -22       C  
ATOM   1264  ND1 HIS A 189     -23.587  11.887 -35.240  1.00 24.54           N  
ANISOU 1264  ND1 HIS A 189     3171   3113   3041     40   -226    -24       N  
ATOM   1265  CD2 HIS A 189     -25.004  10.656 -36.350  1.00 22.84           C  
ANISOU 1265  CD2 HIS A 189     2948   2882   2850     50   -191     -4       C  
ATOM   1266  CE1 HIS A 189     -23.630  10.709 -34.643  1.00 23.04           C  
ANISOU 1266  CE1 HIS A 189     3000   2927   2826     47   -228     -6       C  
ATOM   1267  NE2 HIS A 189     -24.486   9.945 -35.296  1.00 26.16           N  
ANISOU 1267  NE2 HIS A 189     3391   3311   3236     52   -205      5       N  
ATOM   1268  N   LEU A 190     -25.807  15.789 -38.084  1.00 13.94           N  
ANISOU 1268  N   LEU A 190     1771   1708   1817     31   -176    -63       N  
ATOM   1269  CA  LEU A 190     -25.997  16.853 -39.060  1.00 14.02           C  
ANISOU 1269  CA  LEU A 190     1766   1699   1861     31   -176    -63       C  
ATOM   1270  C   LEU A 190     -25.514  18.180 -38.501  1.00 13.39           C  
ANISOU 1270  C   LEU A 190     1697   1606   1786     21   -180    -85       C  
ATOM   1271  O   LEU A 190     -24.849  18.953 -39.199  1.00 12.84           O  
ANISOU 1271  O   LEU A 190     1618   1526   1736     12   -192    -83       O  
ATOM   1272  CB  LEU A 190     -27.472  16.954 -39.467  1.00 13.78           C  
ANISOU 1272  CB  LEU A 190     1725   1655   1854     42   -156    -59       C  
ATOM   1273  CG  LEU A 190     -27.803  18.050 -40.485  1.00 14.90           C  
ANISOU 1273  CG  LEU A 190     1854   1775   2034     45   -160    -53       C  
ATOM   1274  CD1 LEU A 190     -27.161  17.708 -41.852  1.00 17.39           C  
ANISOU 1274  CD1 LEU A 190     2158   2097   2352     40   -179    -28       C  
ATOM   1275  CD2 LEU A 190     -29.307  18.262 -40.632  1.00 13.58           C  
ANISOU 1275  CD2 LEU A 190     1671   1594   1893     59   -142    -52       C  
ATOM   1276  N   GLN A 191     -25.812  18.442 -37.227  1.00 15.10           N  
ANISOU 1276  N   GLN A 191     1934   1821   1983     18   -167   -109       N  
ATOM   1277  CA  GLN A 191     -25.384  19.687 -36.603  1.00 14.99           C  
ANISOU 1277  CA  GLN A 191     1935   1791   1970      5   -169   -137       C  
ATOM   1278  C   GLN A 191     -23.866  19.761 -36.540  1.00 15.97           C  
ANISOU 1278  C   GLN A 191     2057   1929   2080    -13   -201   -137       C  
ATOM   1279  O   GLN A 191     -23.269  20.786 -36.883  1.00 15.67           O  
ANISOU 1279  O   GLN A 191     2016   1876   2063    -27   -211   -146       O  
ATOM   1280  CB  GLN A 191     -25.980  19.807 -35.198  1.00 14.48           C  
ANISOU 1280  CB  GLN A 191     1899   1726   1877      4   -147   -166       C  
ATOM   1281  CG  GLN A 191     -25.545  21.064 -34.468  1.00 16.67           C  
ANISOU 1281  CG  GLN A 191     2197   1985   2150    -12   -147   -201       C  
ATOM   1282  CD  GLN A 191     -26.021  21.097 -33.019  1.00 20.86           C  
ANISOU 1282  CD  GLN A 191     2764   2520   2643    -17   -124   -232       C  
ATOM   1283  OE1 GLN A 191     -26.017  20.082 -32.318  1.00 22.47           O  
ANISOU 1283  OE1 GLN A 191     2982   2751   2804    -19   -126   -225       O  
ATOM   1284  NE2 GLN A 191     -26.435  22.258 -32.573  1.00 23.51           N  
ANISOU 1284  NE2 GLN A 191     3116   2826   2990    -20   -101   -266       N  
ATOM   1285  N   LEU A 192     -23.227  18.678 -36.096  1.00 15.71           N  
ANISOU 1285  N   LEU A 192     2026   1926   2016    -13   -219   -127       N  
ATOM   1286  CA  LEU A 192     -21.773  18.647 -36.016  1.00 14.06           C  
ANISOU 1286  CA  LEU A 192     1808   1735   1800    -28   -252   -125       C  
ATOM   1287  C   LEU A 192     -21.139  18.869 -37.382  1.00 13.38           C  
ANISOU 1287  C   LEU A 192     1692   1644   1749    -31   -259   -108       C  
ATOM   1288  O   LEU A 192     -20.235  19.696 -37.529  1.00 13.29           O  
ANISOU 1288  O   LEU A 192     1671   1629   1751    -50   -274   -117       O  
ATOM   1289  CB  LEU A 192     -21.309  17.312 -35.438  1.00 14.48           C  
ANISOU 1289  CB  LEU A 192     1864   1817   1820    -20   -270   -110       C  
ATOM   1290  CG  LEU A 192     -19.785  17.215 -35.378  1.00 20.13           C  
ANISOU 1290  CG  LEU A 192     2560   2553   2534    -31   -307   -105       C  
ATOM   1291  CD1 LEU A 192     -19.259  18.130 -34.251  1.00 19.13           C  
ANISOU 1291  CD1 LEU A 192     2452   2430   2385    -55   -328   -134       C  
ATOM   1292  CD2 LEU A 192     -19.348  15.775 -35.199  1.00 24.80           C  
ANISOU 1292  CD2 LEU A 192     3147   3168   3109    -14   -324    -80       C  
ATOM   1293  N   PHE A 193     -21.587  18.118 -38.390  1.00 12.94           N  
ANISOU 1293  N   PHE A 193     1622   1589   1706    -15   -248    -84       N  
ATOM   1294  CA  PHE A 193     -20.979  18.206 -39.714  1.00 12.25           C  
ANISOU 1294  CA  PHE A 193     1511   1501   1644    -19   -251    -67       C  
ATOM   1295  C   PHE A 193     -21.209  19.570 -40.344  1.00 13.43           C  
ANISOU 1295  C   PHE A 193     1660   1622   1820    -31   -243    -71       C  
ATOM   1296  O   PHE A 193     -20.311  20.111 -40.994  1.00 14.60           O  
ANISOU 1296  O   PHE A 193     1795   1768   1985    -47   -250    -67       O  
ATOM   1297  CB  PHE A 193     -21.537  17.126 -40.646  1.00 15.60           C  
ANISOU 1297  CB  PHE A 193     1927   1930   2070     -2   -240    -44       C  
ATOM   1298  CG  PHE A 193     -21.330  15.719 -40.158  1.00 15.75           C  
ANISOU 1298  CG  PHE A 193     1948   1970   2067     11   -246    -35       C  
ATOM   1299  CD1 PHE A 193     -20.252  15.394 -39.360  1.00 14.60           C  
ANISOU 1299  CD1 PHE A 193     1798   1842   1906      9   -267    -39       C  
ATOM   1300  CD2 PHE A 193     -22.224  14.720 -40.515  1.00 15.97           C  
ANISOU 1300  CD2 PHE A 193     1981   1997   2091     25   -232    -23       C  
ATOM   1301  CE1 PHE A 193     -20.069  14.075 -38.912  1.00 17.60           C  
ANISOU 1301  CE1 PHE A 193     2182   2237   2269     25   -274    -27       C  
ATOM   1302  CE2 PHE A 193     -22.052  13.418 -40.070  1.00 19.10           C  
ANISOU 1302  CE2 PHE A 193     2383   2405   2469     37   -235    -14       C  
ATOM   1303  CZ  PHE A 193     -20.969  13.097 -39.272  1.00 16.68           C  
ANISOU 1303  CZ  PHE A 193     2074   2114   2148     39   -257    -14       C  
ATOM   1304  N   THR A 194     -22.420  20.122 -40.213  1.00 12.96           N  
ANISOU 1304  N   THR A 194     1615   1539   1770    -22   -226    -78       N  
ATOM   1305  CA  THR A 194     -22.650  21.447 -40.784  1.00 14.51           C  
ANISOU 1305  CA  THR A 194     1815   1703   1997    -29   -220    -80       C  
ATOM   1306  C   THR A 194     -21.883  22.506 -40.006  1.00 16.09           C  
ANISOU 1306  C   THR A 194     2025   1890   2198    -52   -228   -106       C  
ATOM   1307  O   THR A 194     -21.351  23.451 -40.599  1.00 13.79           O  
ANISOU 1307  O   THR A 194     1731   1579   1930    -69   -231   -104       O  
ATOM   1308  CB  THR A 194     -24.146  21.786 -40.827  1.00 16.86           C  
ANISOU 1308  CB  THR A 194     2119   1977   2310    -10   -201    -80       C  
ATOM   1309  OG1 THR A 194     -24.704  21.714 -39.507  1.00 16.46           O  
ANISOU 1309  OG1 THR A 194     2084   1927   2243     -3   -189   -106       O  
ATOM   1310  CG2 THR A 194     -24.901  20.817 -41.776  1.00 13.90           C  
ANISOU 1310  CG2 THR A 194     1730   1614   1937      6   -198    -52       C  
ATOM   1311  N   GLU A 195     -21.792  22.357 -38.682  1.00 13.78           N  
ANISOU 1311  N   GLU A 195     1747   1608   1879    -55   -232   -132       N  
ATOM   1312  CA  GLU A 195     -20.970  23.289 -37.910  1.00 14.13           C  
ANISOU 1312  CA  GLU A 195     1804   1644   1920    -82   -244   -160       C  
ATOM   1313  C   GLU A 195     -19.519  23.236 -38.365  1.00 17.32           C  
ANISOU 1313  C   GLU A 195     2184   2067   2330   -105   -268   -150       C  
ATOM   1314  O   GLU A 195     -18.862  24.273 -38.520  1.00 17.36           O  
ANISOU 1314  O   GLU A 195     2188   2054   2355   -131   -274   -161       O  
ATOM   1315  CB  GLU A 195     -21.072  22.974 -36.418  1.00 17.57           C  
ANISOU 1315  CB  GLU A 195     2264   2096   2316    -84   -248   -187       C  
ATOM   1316  CG  GLU A 195     -20.152  23.806 -35.518  1.00 20.79           C  
ANISOU 1316  CG  GLU A 195     2687   2502   2712   -116   -268   -219       C  
ATOM   1317  CD  GLU A 195     -20.495  25.286 -35.531  1.00 24.43           C  
ANISOU 1317  CD  GLU A 195     3166   2916   3201   -129   -251   -245       C  
ATOM   1318  OE1 GLU A 195     -21.601  25.643 -35.987  1.00 18.15           O  
ANISOU 1318  OE1 GLU A 195     2375   2090   2430   -107   -222   -240       O  
ATOM   1319  OE2 GLU A 195     -19.654  26.094 -35.079  1.00 28.06           O  
ANISOU 1319  OE2 GLU A 195     3635   3368   3660   -161   -268   -270       O  
ATOM   1320  N   TYR A 196     -18.999  22.029 -38.578  1.00 15.05           N  
ANISOU 1320  N   TYR A 196     1876   1815   2029    -95   -281   -131       N  
ATOM   1321  CA  TYR A 196     -17.634  21.892 -39.073  1.00 17.07           C  
ANISOU 1321  CA  TYR A 196     2100   2089   2295   -112   -299   -121       C  
ATOM   1322  C   TYR A 196     -17.479  22.564 -40.425  1.00 15.41           C  
ANISOU 1322  C   TYR A 196     1877   1859   2118   -123   -284   -104       C  
ATOM   1323  O   TYR A 196     -16.424  23.142 -40.720  1.00 16.69           O  
ANISOU 1323  O   TYR A 196     2022   2023   2298   -150   -292   -106       O  
ATOM   1324  CB  TYR A 196     -17.278  20.411 -39.156  1.00 13.89           C  
ANISOU 1324  CB  TYR A 196     1678   1722   1877    -92   -308   -101       C  
ATOM   1325  CG  TYR A 196     -15.806  20.110 -39.277  1.00 17.78           C  
ANISOU 1325  CG  TYR A 196     2135   2242   2379   -104   -330    -96       C  
ATOM   1326  CD1 TYR A 196     -14.869  20.718 -38.430  1.00 17.61           C  
ANISOU 1326  CD1 TYR A 196     2106   2230   2356   -131   -358   -116       C  
ATOM   1327  CD2 TYR A 196     -15.354  19.195 -40.209  1.00 16.56           C  
ANISOU 1327  CD2 TYR A 196     1953   2103   2236    -90   -323    -73       C  
ATOM   1328  CE1 TYR A 196     -13.508  20.431 -38.533  1.00 17.66           C  
ANISOU 1328  CE1 TYR A 196     2071   2263   2377   -142   -380   -111       C  
ATOM   1329  CE2 TYR A 196     -13.999  18.888 -40.311  1.00 16.55           C  
ANISOU 1329  CE2 TYR A 196     1912   2126   2249    -98   -339    -69       C  
ATOM   1330  CZ  TYR A 196     -13.087  19.508 -39.470  1.00 18.04           C  
ANISOU 1330  CZ  TYR A 196     2087   2326   2441   -123   -369    -87       C  
ATOM   1331  OH  TYR A 196     -11.762  19.185 -39.591  1.00 19.07           O  
ANISOU 1331  OH  TYR A 196     2170   2484   2592   -129   -387    -82       O  
ATOM   1332  N   GLY A 197     -18.519  22.489 -41.267  1.00 12.44           N  
ANISOU 1332  N   GLY A 197     1511   1466   1750   -104   -263    -86       N  
ATOM   1333  CA  GLY A 197     -18.497  23.227 -42.521  1.00 13.80           C  
ANISOU 1333  CA  GLY A 197     1681   1616   1948   -115   -250    -67       C  
ATOM   1334  C   GLY A 197     -18.481  24.728 -42.297  1.00 16.82           C  
ANISOU 1334  C   GLY A 197     2079   1959   2352   -137   -248    -83       C  
ATOM   1335  O   GLY A 197     -17.627  25.442 -42.837  1.00 14.22           O  
ANISOU 1335  O   GLY A 197     1741   1620   2041   -166   -249    -78       O  
ATOM   1336  N   ARG A 198     -19.395  25.222 -41.457  1.00 14.70           N  
ANISOU 1336  N   ARG A 198     1836   1668   2083   -126   -244   -104       N  
ATOM   1337  CA  ARG A 198     -19.423  26.655 -41.161  1.00 17.82           C  
ANISOU 1337  CA  ARG A 198     2251   2019   2500   -145   -239   -123       C  
ATOM   1338  C   ARG A 198     -18.093  27.157 -40.619  1.00 19.47           C  
ANISOU 1338  C   ARG A 198     2454   2234   2709   -185   -256   -146       C  
ATOM   1339  O   ARG A 198     -17.691  28.286 -40.918  1.00 17.52           O  
ANISOU 1339  O   ARG A 198     2214   1954   2488   -212   -253   -150       O  
ATOM   1340  CB  ARG A 198     -20.547  26.965 -40.174  1.00 19.32           C  
ANISOU 1340  CB  ARG A 198     2467   2187   2686   -126   -228   -150       C  
ATOM   1341  CG  ARG A 198     -21.894  26.655 -40.751  1.00 19.72           C  
ANISOU 1341  CG  ARG A 198     2518   2227   2747    -90   -212   -128       C  
ATOM   1342  CD  ARG A 198     -22.995  26.872 -39.732  1.00 23.44           C  
ANISOU 1342  CD  ARG A 198     3008   2681   3217    -70   -194   -156       C  
ATOM   1343  NE  ARG A 198     -23.164  28.268 -39.349  1.00 26.96           N  
ANISOU 1343  NE  ARG A 198     3478   3077   3690    -78   -183   -182       N  
ATOM   1344  CZ  ARG A 198     -24.311  28.769 -38.906  1.00 33.58           C  
ANISOU 1344  CZ  ARG A 198     4330   3883   4546    -54   -159   -199       C  
ATOM   1345  NH1 ARG A 198     -25.408  28.029 -38.840  1.00 31.20           N  
ANISOU 1345  NH1 ARG A 198     4017   3596   4240    -22   -145   -191       N  
ATOM   1346  NH2 ARG A 198     -24.360  30.039 -38.512  1.00 28.99           N  
ANISOU 1346  NH2 ARG A 198     3772   3252   3990    -62   -147   -226       N  
ATOM   1347  N   LEU A 199     -17.378  26.331 -39.861  1.00 17.26           N  
ANISOU 1347  N   LEU A 199     2159   1997   2403   -189   -276   -157       N  
ATOM   1348  CA  LEU A 199     -16.109  26.779 -39.300  1.00 21.29           C  
ANISOU 1348  CA  LEU A 199     2658   2518   2915   -228   -299   -179       C  
ATOM   1349  C   LEU A 199     -15.088  27.102 -40.378  1.00 21.11           C  
ANISOU 1349  C   LEU A 199     2605   2496   2920   -255   -297   -158       C  
ATOM   1350  O   LEU A 199     -14.215  27.949 -40.164  1.00 21.45           O  
ANISOU 1350  O   LEU A 199     2642   2529   2980   -294   -307   -175       O  
ATOM   1351  CB  LEU A 199     -15.549  25.720 -38.355  1.00 22.17           C  
ANISOU 1351  CB  LEU A 199     2754   2677   2992   -223   -326   -188       C  
ATOM   1352  CG  LEU A 199     -16.229  25.807 -36.998  1.00 24.28           C  
ANISOU 1352  CG  LEU A 199     3059   2940   3227   -217   -331   -219       C  
ATOM   1353  CD1 LEU A 199     -15.854  24.615 -36.152  1.00 26.80           C  
ANISOU 1353  CD1 LEU A 199     3369   3306   3508   -206   -357   -218       C  
ATOM   1354  CD2 LEU A 199     -15.828  27.117 -36.329  1.00 24.01           C  
ANISOU 1354  CD2 LEU A 199     3045   2878   3199   -256   -339   -257       C  
ATOM   1355  N   ALA A 200     -15.171  26.438 -41.527  1.00 18.69           N  
ANISOU 1355  N   ALA A 200     2281   2202   2620   -237   -283   -124       N  
ATOM   1356  CA  ALA A 200     -14.238  26.642 -42.620  1.00 18.20           C  
ANISOU 1356  CA  ALA A 200     2192   2144   2580   -262   -273   -103       C  
ATOM   1357  C   ALA A 200     -14.683  27.730 -43.590  1.00 21.05           C  
ANISOU 1357  C   ALA A 200     2575   2458   2964   -274   -251    -86       C  
ATOM   1358  O   ALA A 200     -13.944  28.038 -44.528  1.00 22.59           O  
ANISOU 1358  O   ALA A 200     2756   2652   3176   -300   -239    -67       O  
ATOM   1359  CB  ALA A 200     -14.030  25.327 -43.374  1.00 18.53           C  
ANISOU 1359  CB  ALA A 200     2206   2224   2610   -238   -266    -78       C  
ATOM   1360  N   MET A 201     -15.862  28.311 -43.396  1.00 20.82           N  
ANISOU 1360  N   MET A 201     2583   2390   2939   -256   -244    -89       N  
ATOM   1361  CA  MET A 201     -16.416  29.271 -44.335  1.00 18.35           C  
ANISOU 1361  CA  MET A 201     2294   2030   2649   -259   -227    -66       C  
ATOM   1362  C   MET A 201     -16.199  30.682 -43.831  1.00 21.11           C  
ANISOU 1362  C   MET A 201     2666   2331   3025   -290   -227    -89       C  
ATOM   1363  O   MET A 201     -15.942  30.910 -42.648  1.00 23.05           O  
ANISOU 1363  O   MET A 201     2916   2577   3265   -303   -240   -128       O  
ATOM   1364  CB  MET A 201     -17.909  29.030 -44.559  1.00 17.31           C  
ANISOU 1364  CB  MET A 201     2182   1882   2512   -216   -221    -52       C  
ATOM   1365  CG  MET A 201     -18.192  27.660 -45.113  1.00 21.26           C  
ANISOU 1365  CG  MET A 201     2665   2426   2988   -189   -220    -30       C  
ATOM   1366  SD  MET A 201     -19.922  27.204 -44.999  1.00 21.97           S  
ANISOU 1366  SD  MET A 201     2769   2507   3071   -141   -218    -24       S  
ATOM   1367  CE  MET A 201     -20.671  28.492 -46.000  1.00 15.67           C  
ANISOU 1367  CE  MET A 201     1996   1652   2305   -139   -211      5       C  
ATOM   1368  N   GLU A 202     -16.298  31.630 -44.754  1.00 22.28           N  
ANISOU 1368  N   GLU A 202     2832   2435   3198   -305   -213    -64       N  
ATOM   1369  CA  GLU A 202     -16.191  33.029 -44.385  1.00 27.39           C  
ANISOU 1369  CA  GLU A 202     3506   3025   3876   -333   -210    -83       C  
ATOM   1370  C   GLU A 202     -17.449  33.462 -43.648  1.00 25.01           C  
ANISOU 1370  C   GLU A 202     3237   2685   3582   -298   -207   -104       C  
ATOM   1371  O   GLU A 202     -18.537  32.922 -43.856  1.00 24.18           O  
ANISOU 1371  O   GLU A 202     3134   2585   3469   -254   -204    -88       O  
ATOM   1372  CB  GLU A 202     -15.981  33.902 -45.623  1.00 27.43           C  
ANISOU 1372  CB  GLU A 202     3525   2990   3906   -356   -195    -45       C  
ATOM   1373  CG  GLU A 202     -14.641  33.683 -46.331  1.00 36.24           C  
ANISOU 1373  CG  GLU A 202     4610   4138   5020   -399   -189    -28       C  
ATOM   1374  CD  GLU A 202     -13.423  33.984 -45.447  1.00 43.83           C  
ANISOU 1374  CD  GLU A 202     5550   5113   5992   -446   -200    -68       C  
ATOM   1375  OE1 GLU A 202     -13.531  34.817 -44.513  1.00 47.69           O  
ANISOU 1375  OE1 GLU A 202     6062   5564   6495   -460   -208   -103       O  
ATOM   1376  OE2 GLU A 202     -12.352  33.383 -45.696  1.00 41.50           O  
ANISOU 1376  OE2 GLU A 202     5214   4865   5691   -469   -200    -64       O  
ATOM   1377  N   GLU A 203     -17.285  34.437 -42.770  1.00 23.98           N  
ANISOU 1377  N   GLU A 203     3129   2515   3468   -321   -207   -143       N  
ATOM   1378  CA  GLU A 203     -18.425  34.985 -42.053  1.00 32.22           C  
ANISOU 1378  CA  GLU A 203     4205   3514   4523   -291   -197   -168       C  
ATOM   1379  C   GLU A 203     -19.444  35.546 -43.039  1.00 27.98           C  
ANISOU 1379  C   GLU A 203     3685   2928   4019   -259   -183   -128       C  
ATOM   1380  O   GLU A 203     -19.096  36.096 -44.092  1.00 24.33           O  
ANISOU 1380  O   GLU A 203     3228   2440   3577   -278   -180    -91       O  
ATOM   1381  CB  GLU A 203     -17.955  36.064 -41.072  1.00 34.19           C  
ANISOU 1381  CB  GLU A 203     4481   3723   4788   -327   -197   -217       C  
ATOM   1382  CG  GLU A 203     -16.975  35.524 -40.019  1.00 39.23           C  
ANISOU 1382  CG  GLU A 203     5102   4412   5390   -360   -218   -257       C  
ATOM   1383  CD  GLU A 203     -16.370  36.612 -39.144  1.00 59.52           C  
ANISOU 1383  CD  GLU A 203     7699   6944   7972   -407   -223   -307       C  
ATOM   1384  OE1 GLU A 203     -17.021  37.662 -38.951  1.00 66.81           O  
ANISOU 1384  OE1 GLU A 203     8662   7799   8923   -401   -204   -325       O  
ATOM   1385  OE2 GLU A 203     -15.236  36.418 -38.652  1.00 64.93           O  
ANISOU 1385  OE2 GLU A 203     8365   7667   8640   -449   -247   -328       O  
ATOM   1386  N   THR A 204     -20.716  35.376 -42.703  1.00 23.74           N  
ANISOU 1386  N   THR A 204     3156   2380   3486   -211   -175   -134       N  
ATOM   1387  CA  THR A 204     -21.795  35.727 -43.607  1.00 23.67           C  
ANISOU 1387  CA  THR A 204     3154   2333   3506   -173   -169    -93       C  
ATOM   1388  C   THR A 204     -22.978  36.173 -42.765  1.00 21.48           C  
ANISOU 1388  C   THR A 204     2893   2016   3252   -134   -152   -124       C  
ATOM   1389  O   THR A 204     -23.152  35.712 -41.634  1.00 26.29           O  
ANISOU 1389  O   THR A 204     3500   2650   3838   -127   -146   -168       O  
ATOM   1390  CB  THR A 204     -22.169  34.532 -44.496  1.00 23.92           C  
ANISOU 1390  CB  THR A 204     3158   2417   3512   -148   -179    -51       C  
ATOM   1391  OG1 THR A 204     -23.282  34.865 -45.332  1.00 28.12           O  
ANISOU 1391  OG1 THR A 204     3696   2916   4072   -111   -179    -12       O  
ATOM   1392  CG2 THR A 204     -22.533  33.302 -43.634  1.00 23.23           C  
ANISOU 1392  CG2 THR A 204     3049   2386   3390   -126   -180    -77       C  
ATOM   1393  N   PHE A 205     -23.782  37.085 -43.316  1.00 16.84           N  
ANISOU 1393  N   PHE A 205     2322   1365   2711   -107   -145   -101       N  
ATOM   1394  CA  PHE A 205     -25.062  37.448 -42.718  1.00 18.57           C  
ANISOU 1394  CA  PHE A 205     2547   1546   2961    -60   -126   -122       C  
ATOM   1395  C   PHE A 205     -26.215  36.590 -43.224  1.00 21.61           C  
ANISOU 1395  C   PHE A 205     2902   1964   3346    -11   -132    -89       C  
ATOM   1396  O   PHE A 205     -27.324  36.686 -42.688  1.00 25.75           O  
ANISOU 1396  O   PHE A 205     3420   2469   3894     31   -115   -107       O  
ATOM   1397  CB  PHE A 205     -25.376  38.931 -42.991  1.00 17.66           C  
ANISOU 1397  CB  PHE A 205     2464   1340   2906    -52   -116   -115       C  
ATOM   1398  CG  PHE A 205     -24.380  39.889 -42.375  1.00 19.04           C  
ANISOU 1398  CG  PHE A 205     2673   1473   3089   -101   -106   -156       C  
ATOM   1399  CD1 PHE A 205     -24.288  40.024 -40.996  1.00 20.98           C  
ANISOU 1399  CD1 PHE A 205     2934   1716   3322   -111    -89   -224       C  
ATOM   1400  CD2 PHE A 205     -23.541  40.650 -43.174  1.00 16.28           C  
ANISOU 1400  CD2 PHE A 205     2343   1087   2757   -140   -115   -126       C  
ATOM   1401  CE1 PHE A 205     -23.382  40.902 -40.421  1.00 20.84           C  
ANISOU 1401  CE1 PHE A 205     2950   1660   3310   -161    -84   -265       C  
ATOM   1402  CE2 PHE A 205     -22.622  41.533 -42.607  1.00 20.19           C  
ANISOU 1402  CE2 PHE A 205     2868   1543   3262   -190   -107   -165       C  
ATOM   1403  CZ  PHE A 205     -22.547  41.666 -41.231  1.00 18.98           C  
ANISOU 1403  CZ  PHE A 205     2729   1387   3097   -201    -93   -236       C  
ATOM   1404  N   LEU A 206     -25.989  35.774 -44.247  1.00 18.30           N  
ANISOU 1404  N   LEU A 206     2463   1591   2901    -16   -154    -43       N  
ATOM   1405  CA  LEU A 206     -27.006  34.881 -44.781  1.00 21.74           C  
ANISOU 1405  CA  LEU A 206     2868   2061   3331     23   -164    -12       C  
ATOM   1406  C   LEU A 206     -26.812  33.480 -44.220  1.00 19.80           C  
ANISOU 1406  C   LEU A 206     2600   1889   3035     17   -164    -33       C  
ATOM   1407  O   LEU A 206     -25.790  33.166 -43.615  1.00 17.49           O  
ANISOU 1407  O   LEU A 206     2312   1623   2709    -17   -163    -61       O  
ATOM   1408  CB  LEU A 206     -26.935  34.856 -46.307  1.00 19.59           C  
ANISOU 1408  CB  LEU A 206     2595   1791   3058     19   -189     52       C  
ATOM   1409  CG  LEU A 206     -26.889  36.256 -46.933  1.00 24.25           C  
ANISOU 1409  CG  LEU A 206     3214   2306   3692     16   -191     80       C  
ATOM   1410  CD1 LEU A 206     -26.546  36.180 -48.407  1.00 26.57           C  
ANISOU 1410  CD1 LEU A 206     3515   2611   3970     -1   -214    143       C  
ATOM   1411  CD2 LEU A 206     -28.215  36.971 -46.733  1.00 24.67           C  
ANISOU 1411  CD2 LEU A 206     3266   2306   3802     68   -186     82       C  
ATOM   1412  N   LYS A 207     -27.806  32.631 -44.431  1.00 18.14           N  
ANISOU 1412  N   LYS A 207     2363   1708   2820     50   -168    -17       N  
ATOM   1413  CA  LYS A 207     -27.637  31.236 -44.065  1.00 16.99           C  
ANISOU 1413  CA  LYS A 207     2198   1629   2627     44   -170    -29       C  
ATOM   1414  C   LYS A 207     -26.498  30.632 -44.885  1.00 16.88           C  
ANISOU 1414  C   LYS A 207     2183   1653   2578     10   -188     -3       C  
ATOM   1415  O   LYS A 207     -26.317  30.992 -46.055  1.00 17.16           O  
ANISOU 1415  O   LYS A 207     2224   1675   2622      2   -202     37       O  
ATOM   1416  CB  LYS A 207     -28.940  30.465 -44.286  1.00 16.59           C  
ANISOU 1416  CB  LYS A 207     2119   1600   2584     81   -171    -13       C  
ATOM   1417  CG  LYS A 207     -30.081  30.924 -43.354  1.00 18.14           C  
ANISOU 1417  CG  LYS A 207     2310   1766   2817    116   -145    -43       C  
ATOM   1418  CD  LYS A 207     -31.291  30.011 -43.502  1.00 20.42           C  
ANISOU 1418  CD  LYS A 207     2563   2085   3110    146   -145    -30       C  
ATOM   1419  CE  LYS A 207     -32.401  30.337 -42.509  1.00 17.53           C  
ANISOU 1419  CE  LYS A 207     2185   1697   2778    179   -111    -64       C  
ATOM   1420  NZ  LYS A 207     -33.474  29.290 -42.628  1.00 22.92           N  
ANISOU 1420  NZ  LYS A 207     2828   2417   3462    200   -111    -52       N  
ATOM   1421  N   PRO A 208     -25.686  29.753 -44.294  1.00 16.83           N  
ANISOU 1421  N   PRO A 208     2171   1692   2531    -11   -188    -26       N  
ATOM   1422  CA  PRO A 208     -24.521  29.225 -45.024  1.00 18.82           C  
ANISOU 1422  CA  PRO A 208     2417   1977   2755    -42   -200     -6       C  
ATOM   1423  C   PRO A 208     -24.869  28.323 -46.197  1.00 19.17           C  
ANISOU 1423  C   PRO A 208     2448   2053   2784    -31   -212     34       C  
ATOM   1424  O   PRO A 208     -24.129  28.321 -47.191  1.00 18.25           O  
ANISOU 1424  O   PRO A 208     2334   1944   2657    -53   -218     60       O  
ATOM   1425  CB  PRO A 208     -23.757  28.451 -43.936  1.00 18.53           C  
ANISOU 1425  CB  PRO A 208     2374   1981   2686    -56   -198    -42       C  
ATOM   1426  CG  PRO A 208     -24.821  28.112 -42.906  1.00 17.57           C  
ANISOU 1426  CG  PRO A 208     2252   1861   2562    -28   -186    -68       C  
ATOM   1427  CD  PRO A 208     -25.694  29.329 -42.886  1.00 16.15           C  
ANISOU 1427  CD  PRO A 208     2085   1625   2425     -9   -175    -71       C  
ATOM   1428  N   PHE A 209     -25.953  27.548 -46.121  1.00 19.43           N  
ANISOU 1428  N   PHE A 209     2465   2103   2813     -2   -213     37       N  
ATOM   1429  CA  PHE A 209     -26.232  26.530 -47.131  1.00 15.46           C  
ANISOU 1429  CA  PHE A 209     1951   1635   2289      3   -225     67       C  
ATOM   1430  C   PHE A 209     -27.632  26.732 -47.690  1.00 16.66           C  
ANISOU 1430  C   PHE A 209     2095   1769   2466     32   -236     92       C  
ATOM   1431  O   PHE A 209     -28.412  27.553 -47.208  1.00 15.85           O  
ANISOU 1431  O   PHE A 209     1992   1630   2400     54   -230     83       O  
ATOM   1432  CB  PHE A 209     -26.069  25.115 -46.558  1.00 15.83           C  
ANISOU 1432  CB  PHE A 209     1984   1729   2302      4   -221     49       C  
ATOM   1433  CG  PHE A 209     -24.789  24.926 -45.818  1.00 15.86           C  
ANISOU 1433  CG  PHE A 209     1990   1750   2286    -19   -215     23       C  
ATOM   1434  CD1 PHE A 209     -23.573  25.036 -46.481  1.00 16.87           C  
ANISOU 1434  CD1 PHE A 209     2118   1886   2404    -46   -218     35       C  
ATOM   1435  CD2 PHE A 209     -24.791  24.690 -44.461  1.00 15.13           C  
ANISOU 1435  CD2 PHE A 209     1898   1666   2186    -15   -207    -11       C  
ATOM   1436  CE1 PHE A 209     -22.368  24.890 -45.795  1.00 17.10           C  
ANISOU 1436  CE1 PHE A 209     2143   1933   2422    -67   -217     12       C  
ATOM   1437  CE2 PHE A 209     -23.602  24.544 -43.765  1.00 15.68           C  
ANISOU 1437  CE2 PHE A 209     1968   1752   2236    -36   -210    -32       C  
ATOM   1438  CZ  PHE A 209     -22.385  24.642 -44.436  1.00 17.77           C  
ANISOU 1438  CZ  PHE A 209     2228   2027   2498    -62   -216    -20       C  
ATOM   1439  N   GLN A 210     -27.958  25.934 -48.707  1.00 17.53           N  
ANISOU 1439  N   GLN A 210     2198   1907   2557     33   -251    121       N  
ATOM   1440  CA  GLN A 210     -29.138  26.162 -49.514  1.00 19.00           C  
ANISOU 1440  CA  GLN A 210     2376   2080   2764     55   -271    153       C  
ATOM   1441  C   GLN A 210     -30.141  25.050 -49.248  1.00 17.85           C  
ANISOU 1441  C   GLN A 210     2205   1965   2613     73   -274    144       C  
ATOM   1442  O   GLN A 210     -30.855  25.105 -48.233  1.00 19.41           O  
ANISOU 1442  O   GLN A 210     2386   2154   2835     93   -258    119       O  
ATOM   1443  CB  GLN A 210     -28.722  26.296 -50.976  1.00 19.01           C  
ANISOU 1443  CB  GLN A 210     2395   2084   2745     36   -291    194       C  
ATOM   1444  CG  GLN A 210     -28.122  27.658 -51.248  1.00 22.11           C  
ANISOU 1444  CG  GLN A 210     2812   2432   3157     24   -290    210       C  
ATOM   1445  CD  GLN A 210     -27.546  27.729 -52.625  1.00 18.74           C  
ANISOU 1445  CD  GLN A 210     2408   2012   2702     -2   -302    249       C  
ATOM   1446  OE1 GLN A 210     -26.402  27.357 -52.837  1.00 18.33           O  
ANISOU 1446  OE1 GLN A 210     2364   1982   2618    -32   -288    243       O  
ATOM   1447  NE2 GLN A 210     -28.338  28.194 -53.577  1.00 23.45           N  
ANISOU 1447  NE2 GLN A 210     3013   2590   3307     10   -329    292       N  
ATOM   1448  N   SER A 211     -30.252  24.042 -50.116  1.00 15.18           N  
ANISOU 1448  N   SER A 211     1862   1661   2244     63   -289    163       N  
ATOM   1449  CA  SER A 211     -31.295  23.032 -50.005  1.00 15.75           C  
ANISOU 1449  CA  SER A 211     1909   1758   2316     76   -295    158       C  
ATOM   1450  C   SER A 211     -30.773  21.779 -49.308  1.00 18.08           C  
ANISOU 1450  C   SER A 211     2203   2087   2578     64   -275    130       C  
ATOM   1451  O   SER A 211     -29.711  21.244 -49.670  1.00 13.03           O  
ANISOU 1451  O   SER A 211     1579   1466   1905     43   -272    129       O  
ATOM   1452  CB  SER A 211     -31.849  22.668 -51.384  1.00 19.74           C  
ANISOU 1452  CB  SER A 211     2413   2278   2808     71   -328    194       C  
ATOM   1453  OG  SER A 211     -32.337  23.823 -52.041  1.00 23.49           O  
ANISOU 1453  OG  SER A 211     2891   2723   3313     84   -351    227       O  
ATOM   1454  N   LEU A 212     -31.541  21.296 -48.331  1.00 16.61           N  
ANISOU 1454  N   LEU A 212     1998   1907   2405     78   -260    108       N  
ATOM   1455  CA  LEU A 212     -31.287  20.021 -47.675  1.00 17.07           C  
ANISOU 1455  CA  LEU A 212     2056   1995   2435     70   -245     87       C  
ATOM   1456  C   LEU A 212     -32.522  19.139 -47.816  1.00 16.44           C  
ANISOU 1456  C   LEU A 212     1953   1932   2363     76   -250     91       C  
ATOM   1457  O   LEU A 212     -33.644  19.588 -47.550  1.00 15.52           O  
ANISOU 1457  O   LEU A 212     1811   1802   2282     95   -249     92       O  
ATOM   1458  CB  LEU A 212     -30.950  20.223 -46.199  1.00 17.02           C  
ANISOU 1458  CB  LEU A 212     2055   1982   2430     75   -218     54       C  
ATOM   1459  CG  LEU A 212     -30.776  18.972 -45.337  1.00 16.03           C  
ANISOU 1459  CG  LEU A 212     1931   1882   2276     69   -202     35       C  
ATOM   1460  CD1 LEU A 212     -29.565  18.179 -45.786  1.00 16.54           C  
ANISOU 1460  CD1 LEU A 212     2010   1967   2306     51   -209     40       C  
ATOM   1461  CD2 LEU A 212     -30.653  19.375 -43.891  1.00 18.29           C  
ANISOU 1461  CD2 LEU A 212     2226   2160   2564     74   -178      6       C  
ATOM   1462  N   ILE A 213     -32.321  17.889 -48.227  1.00 13.04           N  
ANISOU 1462  N   ILE A 213     1527   1528   1901     61   -254     93       N  
ATOM   1463  CA  ILE A 213     -33.404  16.908 -48.310  1.00 13.32           C  
ANISOU 1463  CA  ILE A 213     1542   1579   1940     59   -257     93       C  
ATOM   1464  C   ILE A 213     -33.091  15.795 -47.331  1.00 14.65           C  
ANISOU 1464  C   ILE A 213     1718   1762   2087     53   -232     71       C  
ATOM   1465  O   ILE A 213     -32.087  15.090 -47.497  1.00 14.55           O  
ANISOU 1465  O   ILE A 213     1726   1759   2042     40   -230     68       O  
ATOM   1466  CB  ILE A 213     -33.564  16.301 -49.710  1.00 13.58           C  
ANISOU 1466  CB  ILE A 213     1578   1627   1953     43   -286    114       C  
ATOM   1467  CG1 ILE A 213     -33.391  17.338 -50.819  1.00 21.96           C  
ANISOU 1467  CG1 ILE A 213     2649   2678   3018     43   -314    141       C  
ATOM   1468  CG2 ILE A 213     -34.851  15.430 -49.765  1.00 14.02           C  
ANISOU 1468  CG2 ILE A 213     1608   1697   2022     39   -294    114       C  
ATOM   1469  CD1 ILE A 213     -34.307  18.429 -50.782  1.00 22.19           C  
ANISOU 1469  CD1 ILE A 213     2656   2686   3091     64   -327    155       C  
ATOM   1470  N   PHE A 214     -33.940  15.624 -46.325  1.00 14.98           N  
ANISOU 1470  N   PHE A 214     1742   1802   2147     61   -211     57       N  
ATOM   1471  CA  PHE A 214     -33.937  14.382 -45.555  1.00 13.69           C  
ANISOU 1471  CA  PHE A 214     1586   1653   1963     52   -190     44       C  
ATOM   1472  C   PHE A 214     -34.587  13.291 -46.405  1.00 13.02           C  
ANISOU 1472  C   PHE A 214     1492   1582   1874     37   -204     54       C  
ATOM   1473  O   PHE A 214     -35.804  13.286 -46.603  1.00 14.34           O  
ANISOU 1473  O   PHE A 214     1628   1751   2068     37   -210     59       O  
ATOM   1474  CB  PHE A 214     -34.680  14.555 -44.236  1.00 12.48           C  
ANISOU 1474  CB  PHE A 214     1420   1494   1826     62   -159     26       C  
ATOM   1475  CG  PHE A 214     -33.954  15.400 -43.212  1.00 13.14           C  
ANISOU 1475  CG  PHE A 214     1524   1567   1903     71   -141      8       C  
ATOM   1476  CD1 PHE A 214     -33.848  16.772 -43.373  1.00 15.06           C  
ANISOU 1476  CD1 PHE A 214     1763   1789   2169     84   -148      7       C  
ATOM   1477  CD2 PHE A 214     -33.421  14.820 -42.071  1.00 12.61           C  
ANISOU 1477  CD2 PHE A 214     1479   1507   1805     66   -120     -7       C  
ATOM   1478  CE1 PHE A 214     -33.196  17.552 -42.427  1.00 15.22           C  
ANISOU 1478  CE1 PHE A 214     1803   1798   2183     89   -132    -13       C  
ATOM   1479  CE2 PHE A 214     -32.784  15.602 -41.105  1.00 13.91           C  
ANISOU 1479  CE2 PHE A 214     1663   1664   1960     71   -108    -25       C  
ATOM   1480  CZ  PHE A 214     -32.661  16.966 -41.292  1.00 11.36           C  
ANISOU 1480  CZ  PHE A 214     1336   1320   1660     80   -114    -31       C  
ATOM   1481  N   LEU A 215     -33.782  12.396 -46.943  1.00 13.86           N  
ANISOU 1481  N   LEU A 215     1621   1697   1949     22   -211     57       N  
ATOM   1482  CA  LEU A 215     -34.286  11.233 -47.667  1.00 15.45           C  
ANISOU 1482  CA  LEU A 215     1822   1908   2141      4   -221     61       C  
ATOM   1483  C   LEU A 215     -34.287  10.057 -46.704  1.00 13.85           C  
ANISOU 1483  C   LEU A 215     1629   1707   1926     -3   -195     48       C  
ATOM   1484  O   LEU A 215     -33.224   9.566 -46.322  1.00 12.03           O  
ANISOU 1484  O   LEU A 215     1425   1474   1671     -1   -184     43       O  
ATOM   1485  CB  LEU A 215     -33.437  10.928 -48.896  1.00 13.07           C  
ANISOU 1485  CB  LEU A 215     1543   1611   1811     -8   -240     68       C  
ATOM   1486  CG  LEU A 215     -33.857   9.686 -49.700  1.00 11.79           C  
ANISOU 1486  CG  LEU A 215     1388   1457   1634    -31   -249     67       C  
ATOM   1487  CD1 LEU A 215     -35.298   9.791 -50.198  1.00 13.68           C  
ANISOU 1487  CD1 LEU A 215     1597   1703   1896    -41   -272     75       C  
ATOM   1488  CD2 LEU A 215     -32.911   9.474 -50.859  1.00 13.34           C  
ANISOU 1488  CD2 LEU A 215     1612   1657   1799    -41   -260     70       C  
ATOM   1489  N   VAL A 216     -35.473   9.603 -46.313  1.00 12.68           N  
ANISOU 1489  N   VAL A 216     1459   1561   1797    -11   -184     46       N  
ATOM   1490  CA  VAL A 216     -35.591   8.464 -45.413  1.00 13.70           C  
ANISOU 1490  CA  VAL A 216     1601   1689   1916    -21   -157     38       C  
ATOM   1491  C   VAL A 216     -35.759   7.204 -46.257  1.00 14.19           C  
ANISOU 1491  C   VAL A 216     1674   1752   1967    -45   -168     40       C  
ATOM   1492  O   VAL A 216     -36.811   6.980 -46.865  1.00 16.88           O  
ANISOU 1492  O   VAL A 216     1990   2098   2326    -61   -181     42       O  
ATOM   1493  CB  VAL A 216     -36.751   8.630 -44.432  1.00 18.53           C  
ANISOU 1493  CB  VAL A 216     2186   2301   2553    -20   -132     32       C  
ATOM   1494  CG1 VAL A 216     -36.790   7.433 -43.488  1.00 12.75           C  
ANISOU 1494  CG1 VAL A 216     1475   1566   1804    -34   -102     28       C  
ATOM   1495  CG2 VAL A 216     -36.591   9.931 -43.673  1.00 15.25           C  
ANISOU 1495  CG2 VAL A 216     1764   1882   2148      3   -119     26       C  
ATOM   1496  N   ARG A 217     -34.695   6.414 -46.335  1.00 10.45           N  
ANISOU 1496  N   ARG A 217     1234   1271   1465    -46   -164     38       N  
ATOM   1497  CA  ARG A 217     -34.749   5.115 -46.982  1.00 14.66           C  
ANISOU 1497  CA  ARG A 217     1785   1799   1986    -67   -167     35       C  
ATOM   1498  C   ARG A 217     -35.488   4.120 -46.093  1.00 11.77           C  
ANISOU 1498  C   ARG A 217     1420   1424   1627    -82   -142     32       C  
ATOM   1499  O   ARG A 217     -35.446   4.204 -44.861  1.00 13.31           O  
ANISOU 1499  O   ARG A 217     1619   1617   1823    -72   -118     34       O  
ATOM   1500  CB  ARG A 217     -33.334   4.608 -47.271  1.00 13.80           C  
ANISOU 1500  CB  ARG A 217     1710   1681   1851    -58   -165     32       C  
ATOM   1501  CG  ARG A 217     -32.475   5.599 -48.065  1.00 12.69           C  
ANISOU 1501  CG  ARG A 217     1570   1549   1701    -46   -183     35       C  
ATOM   1502  CD  ARG A 217     -33.008   5.776 -49.483  1.00 12.96           C  
ANISOU 1502  CD  ARG A 217     1598   1592   1734    -64   -208     36       C  
ATOM   1503  NE  ARG A 217     -32.470   4.787 -50.415  1.00 13.11           N  
ANISOU 1503  NE  ARG A 217     1646   1606   1730    -78   -208     27       N  
ATOM   1504  CZ  ARG A 217     -31.386   4.982 -51.153  1.00 14.08           C  
ANISOU 1504  CZ  ARG A 217     1787   1730   1832    -73   -208     25       C  
ATOM   1505  NH1 ARG A 217     -30.684   6.102 -51.063  1.00 12.28           N  
ANISOU 1505  NH1 ARG A 217     1551   1509   1605    -56   -210     34       N  
ATOM   1506  NH2 ARG A 217     -31.010   4.042 -52.019  1.00 14.49           N  
ANISOU 1506  NH2 ARG A 217     1865   1775   1864    -86   -203     13       N  
ATOM   1507  N   ASP A 218     -36.167   3.171 -46.729  1.00 12.74           N  
ANISOU 1507  N   ASP A 218     1543   1543   1755   -110   -148     29       N  
ATOM   1508  CA  ASP A 218     -36.861   2.101 -46.010  1.00 13.74           C  
ANISOU 1508  CA  ASP A 218     1674   1657   1889   -131   -123     27       C  
ATOM   1509  C   ASP A 218     -37.866   2.657 -45.004  1.00 13.18           C  
ANISOU 1509  C   ASP A 218     1569   1596   1842   -130   -102     30       C  
ATOM   1510  O   ASP A 218     -38.056   2.096 -43.922  1.00 12.32           O  
ANISOU 1510  O   ASP A 218     1473   1478   1731   -136    -70     33       O  
ATOM   1511  CB  ASP A 218     -35.864   1.166 -45.310  1.00 11.40           C  
ANISOU 1511  CB  ASP A 218     1423   1340   1570   -122   -102     30       C  
ATOM   1512  CG  ASP A 218     -34.872   0.541 -46.280  1.00 14.54           C  
ANISOU 1512  CG  ASP A 218     1850   1724   1949   -120   -115     24       C  
ATOM   1513  OD1 ASP A 218     -35.056   0.693 -47.510  1.00 15.07           O  
ANISOU 1513  OD1 ASP A 218     1910   1800   2016   -132   -138     16       O  
ATOM   1514  OD2 ASP A 218     -33.899  -0.090 -45.817  1.00 13.71           O  
ANISOU 1514  OD2 ASP A 218     1777   1602   1830   -104   -102     28       O  
ATOM   1515  N   TRP A 219     -38.481   3.797 -45.323  1.00 15.34           N  
ANISOU 1515  N   TRP A 219     1802   1886   2139   -122   -118     31       N  
ATOM   1516  CA  TRP A 219     -39.601   4.261 -44.520  1.00 14.79           C  
ANISOU 1516  CA  TRP A 219     1694   1825   2101   -123    -95     30       C  
ATOM   1517  C   TRP A 219     -40.609   3.131 -44.415  1.00 14.70           C  
ANISOU 1517  C   TRP A 219     1671   1811   2105   -159    -80     28       C  
ATOM   1518  O   TRP A 219     -40.977   2.526 -45.421  1.00 12.61           O  
ANISOU 1518  O   TRP A 219     1400   1547   1846   -185   -105     26       O  
ATOM   1519  CB  TRP A 219     -40.250   5.492 -45.153  1.00 12.81           C  
ANISOU 1519  CB  TRP A 219     1397   1589   1882   -110   -121     32       C  
ATOM   1520  CG  TRP A 219     -41.417   5.993 -44.346  1.00 12.37           C  
ANISOU 1520  CG  TRP A 219     1294   1540   1865   -107    -94     28       C  
ATOM   1521  CD1 TRP A 219     -42.735   5.975 -44.702  1.00 14.99           C  
ANISOU 1521  CD1 TRP A 219     1572   1884   2240   -123   -101     29       C  
ATOM   1522  CD2 TRP A 219     -41.363   6.544 -43.032  1.00 14.98           C  
ANISOU 1522  CD2 TRP A 219     1628   1868   2196    -88    -52     22       C  
ATOM   1523  NE1 TRP A 219     -43.507   6.508 -43.694  1.00 14.81           N  
ANISOU 1523  NE1 TRP A 219     1515   1864   2249   -112    -63     23       N  
ATOM   1524  CE2 TRP A 219     -42.684   6.875 -42.661  1.00 14.15           C  
ANISOU 1524  CE2 TRP A 219     1469   1772   2137    -91    -31     17       C  
ATOM   1525  CE3 TRP A 219     -40.321   6.816 -42.136  1.00 16.80           C  
ANISOU 1525  CE3 TRP A 219     1900   2090   2393    -69    -33     18       C  
ATOM   1526  CZ2 TRP A 219     -42.986   7.456 -41.440  1.00 13.68           C  
ANISOU 1526  CZ2 TRP A 219     1401   1711   2087    -76     16      6       C  
ATOM   1527  CZ3 TRP A 219     -40.627   7.383 -40.920  1.00 12.84           C  
ANISOU 1527  CZ3 TRP A 219     1394   1589   1896    -57      8      8       C  
ATOM   1528  CH2 TRP A 219     -41.949   7.707 -40.586  1.00 14.82           C  
ANISOU 1528  CH2 TRP A 219     1595   1847   2190    -60     34      1       C  
ATOM   1529  N   SER A 220     -41.015   2.805 -43.196  1.00 15.13           N  
ANISOU 1529  N   SER A 220     1725   1860   2162   -166    -37     27       N  
ATOM   1530  CA  SER A 220     -41.822   1.612 -43.006  1.00 16.11           C  
ANISOU 1530  CA  SER A 220     1847   1976   2297   -204    -16     27       C  
ATOM   1531  C   SER A 220     -43.242   1.895 -42.547  1.00 16.13           C  
ANISOU 1531  C   SER A 220     1793   1993   2343   -219      9     24       C  
ATOM   1532  O   SER A 220     -43.990   0.941 -42.293  1.00 15.13           O  
ANISOU 1532  O   SER A 220     1659   1860   2228   -256     32     24       O  
ATOM   1533  CB  SER A 220     -41.127   0.671 -42.019  1.00 18.12           C  
ANISOU 1533  CB  SER A 220     2157   2209   2517   -208     17     34       C  
ATOM   1534  OG  SER A 220     -39.810   0.405 -42.464  1.00 16.30           O  
ANISOU 1534  OG  SER A 220     1973   1966   2255   -190     -6     37       O  
ATOM   1535  N   PHE A 221     -43.649   3.163 -42.463  1.00 15.43           N  
ANISOU 1535  N   PHE A 221     1662   1921   2281   -193      7     20       N  
ATOM   1536  CA  PHE A 221     -44.921   3.543 -41.846  1.00 15.67           C  
ANISOU 1536  CA  PHE A 221     1635   1964   2355   -199     41     15       C  
ATOM   1537  C   PHE A 221     -45.744   4.455 -42.762  1.00 15.69           C  
ANISOU 1537  C   PHE A 221     1570   1984   2407   -188      4     15       C  
ATOM   1538  O   PHE A 221     -46.142   5.558 -42.370  1.00 15.67           O  
ANISOU 1538  O   PHE A 221     1530   1988   2434   -159     18     10       O  
ATOM   1539  CB  PHE A 221     -44.657   4.204 -40.492  1.00 14.81           C  
ANISOU 1539  CB  PHE A 221     1542   1853   2231   -174     89      9       C  
ATOM   1540  CG  PHE A 221     -43.576   3.534 -39.686  1.00 16.27           C  
ANISOU 1540  CG  PHE A 221     1800   2023   2360   -175    109     15       C  
ATOM   1541  CD1 PHE A 221     -43.684   2.196 -39.322  1.00 18.55           C  
ANISOU 1541  CD1 PHE A 221     2118   2299   2632   -210    131     22       C  
ATOM   1542  CD2 PHE A 221     -42.459   4.249 -39.273  1.00 18.12           C  
ANISOU 1542  CD2 PHE A 221     2071   2253   2559   -143    103     13       C  
ATOM   1543  CE1 PHE A 221     -42.696   1.573 -38.571  1.00 16.32           C  
ANISOU 1543  CE1 PHE A 221     1901   2000   2299   -207    146     32       C  
ATOM   1544  CE2 PHE A 221     -41.455   3.633 -38.523  1.00 17.57           C  
ANISOU 1544  CE2 PHE A 221     2065   2172   2440   -142    115     21       C  
ATOM   1545  CZ  PHE A 221     -41.578   2.289 -38.172  1.00 17.53           C  
ANISOU 1545  CZ  PHE A 221     2089   2154   2419   -172    135     32       C  
ATOM   1546  N   PRO A 222     -46.045   4.009 -43.990  1.00 15.14           N  
ANISOU 1546  N   PRO A 222     1484   1920   2348   -211    -45     19       N  
ATOM   1547  CA  PRO A 222     -46.883   4.834 -44.876  1.00 17.10           C  
ANISOU 1547  CA  PRO A 222     1668   2187   2643   -202    -87     24       C  
ATOM   1548  C   PRO A 222     -48.276   5.072 -44.320  1.00 16.40           C  
ANISOU 1548  C   PRO A 222     1504   2112   2615   -207    -57     19       C  
ATOM   1549  O   PRO A 222     -48.924   6.043 -44.723  1.00 17.49           O  
ANISOU 1549  O   PRO A 222     1584   2262   2799   -184    -81     24       O  
ATOM   1550  CB  PRO A 222     -46.930   4.023 -46.178  1.00 16.32           C  
ANISOU 1550  CB  PRO A 222     1577   2093   2532   -237   -140     27       C  
ATOM   1551  CG  PRO A 222     -46.752   2.600 -45.714  1.00 16.67           C  
ANISOU 1551  CG  PRO A 222     1663   2121   2551   -275   -107     20       C  
ATOM   1552  CD  PRO A 222     -45.767   2.686 -44.585  1.00 17.57           C  
ANISOU 1552  CD  PRO A 222     1830   2218   2629   -250    -61     19       C  
ATOM   1553  N   TYR A 223     -48.753   4.216 -43.408  1.00 16.97           N  
ANISOU 1553  N   TYR A 223     1575   2181   2692   -237     -3     12       N  
ATOM   1554  CA  TYR A 223     -50.026   4.447 -42.741  1.00 15.97           C  
ANISOU 1554  CA  TYR A 223     1377   2067   2623   -243     39      5       C  
ATOM   1555  C   TYR A 223     -49.945   5.555 -41.706  1.00 18.19           C  
ANISOU 1555  C   TYR A 223     1652   2345   2913   -199     86     -3       C  
ATOM   1556  O   TYR A 223     -50.980   5.951 -41.163  1.00 21.54           O  
ANISOU 1556  O   TYR A 223     2013   2780   3391   -194    125    -12       O  
ATOM   1557  CB  TYR A 223     -50.502   3.156 -42.070  1.00 18.58           C  
ANISOU 1557  CB  TYR A 223     1716   2394   2951   -293     87      1       C  
ATOM   1558  CG  TYR A 223     -49.453   2.522 -41.164  1.00 18.57           C  
ANISOU 1558  CG  TYR A 223     1802   2370   2885   -297    127      1       C  
ATOM   1559  CD1 TYR A 223     -49.312   2.919 -39.843  1.00 14.31           C  
ANISOU 1559  CD1 TYR A 223     1281   1827   2331   -278    189     -4       C  
ATOM   1560  CD2 TYR A 223     -48.602   1.534 -41.643  1.00 17.48           C  
ANISOU 1560  CD2 TYR A 223     1728   2214   2701   -318    101      8       C  
ATOM   1561  CE1 TYR A 223     -48.352   2.331 -39.011  1.00 17.57           C  
ANISOU 1561  CE1 TYR A 223     1774   2221   2681   -282    219      0       C  
ATOM   1562  CE2 TYR A 223     -47.638   0.952 -40.830  1.00 16.65           C  
ANISOU 1562  CE2 TYR A 223     1698   2087   2540   -317    132     12       C  
ATOM   1563  CZ  TYR A 223     -47.520   1.344 -39.519  1.00 18.09           C  
ANISOU 1563  CZ  TYR A 223     1898   2269   2707   -299    187     11       C  
ATOM   1564  OH  TYR A 223     -46.563   0.742 -38.718  1.00 19.19           O  
ANISOU 1564  OH  TYR A 223     2113   2388   2790   -299    211     19       O  
ATOM   1565  N   GLU A 224     -48.740   6.016 -41.373  1.00 18.28           N  
ANISOU 1565  N   GLU A 224     1728   2343   2876   -169     88     -4       N  
ATOM   1566  CA  GLU A 224     -48.551   7.145 -40.471  1.00 17.84           C  
ANISOU 1566  CA  GLU A 224     1674   2281   2822   -128    127    -15       C  
ATOM   1567  C   GLU A 224     -48.174   8.416 -41.211  1.00 16.74           C  
ANISOU 1567  C   GLU A 224     1524   2138   2698    -85     79    -10       C  
ATOM   1568  O   GLU A 224     -48.727   9.484 -40.931  1.00 18.93           O  
ANISOU 1568  O   GLU A 224     1757   2415   3021    -53     96    -18       O  
ATOM   1569  CB  GLU A 224     -47.474   6.830 -39.426  1.00 14.44           C  
ANISOU 1569  CB  GLU A 224     1325   1837   2325   -128    164    -20       C  
ATOM   1570  CG  GLU A 224     -47.347   7.920 -38.394  1.00 23.29           C  
ANISOU 1570  CG  GLU A 224     2452   2954   3445    -94    208    -37       C  
ATOM   1571  CD  GLU A 224     -46.237   7.667 -37.409  1.00 21.06           C  
ANISOU 1571  CD  GLU A 224     2249   2661   3092    -95    235    -40       C  
ATOM   1572  OE1 GLU A 224     -45.117   7.314 -37.836  1.00 20.31           O  
ANISOU 1572  OE1 GLU A 224     2205   2558   2953    -95    195    -29       O  
ATOM   1573  OE2 GLU A 224     -46.486   7.816 -36.199  1.00 28.74           O  
ANISOU 1573  OE2 GLU A 224     3233   3634   4052    -95    296    -55       O  
ATOM   1574  N   PHE A 225     -47.241   8.312 -42.154  1.00 16.55           N  
ANISOU 1574  N   PHE A 225     1541   2110   2638    -85     24      3       N  
ATOM   1575  CA  PHE A 225     -46.891   9.393 -43.063  1.00 18.22           C  
ANISOU 1575  CA  PHE A 225     1744   2317   2860    -52    -28     13       C  
ATOM   1576  C   PHE A 225     -46.702   8.750 -44.424  1.00 16.83           C  
ANISOU 1576  C   PHE A 225     1576   2149   2668    -76    -91     29       C  
ATOM   1577  O   PHE A 225     -45.908   7.813 -44.556  1.00 15.90           O  
ANISOU 1577  O   PHE A 225     1513   2027   2501   -100    -95     29       O  
ATOM   1578  CB  PHE A 225     -45.618  10.125 -42.614  1.00 17.48           C  
ANISOU 1578  CB  PHE A 225     1710   2207   2725    -23    -19      8       C  
ATOM   1579  CG  PHE A 225     -45.765  10.861 -41.297  1.00 19.07           C  
ANISOU 1579  CG  PHE A 225     1909   2399   2938      0     40    -12       C  
ATOM   1580  CD1 PHE A 225     -46.381  12.107 -41.249  1.00 16.60           C  
ANISOU 1580  CD1 PHE A 225     1550   2080   2678     36     46    -17       C  
ATOM   1581  CD2 PHE A 225     -45.273  10.315 -40.114  1.00 17.28           C  
ANISOU 1581  CD2 PHE A 225     1730   2170   2666    -13     89    -25       C  
ATOM   1582  CE1 PHE A 225     -46.522  12.780 -40.046  1.00 19.76           C  
ANISOU 1582  CE1 PHE A 225     1952   2469   3087     56    105    -41       C  
ATOM   1583  CE2 PHE A 225     -45.416  10.982 -38.910  1.00 20.80           C  
ANISOU 1583  CE2 PHE A 225     2180   2609   3114      5    145    -46       C  
ATOM   1584  CZ  PHE A 225     -46.042  12.223 -38.875  1.00 18.05           C  
ANISOU 1584  CZ  PHE A 225     1786   2253   2820     39    155    -56       C  
ATOM   1585  N   SER A 226     -47.472   9.210 -45.410  1.00 17.14           N  
ANISOU 1585  N   SER A 226     1563   2200   2751    -71   -139     42       N  
ATOM   1586  CA  SER A 226     -47.420   8.630 -46.746  1.00 20.90           C  
ANISOU 1586  CA  SER A 226     2045   2687   3209    -98   -201     56       C  
ATOM   1587  C   SER A 226     -46.003   8.664 -47.291  1.00 17.83           C  
ANISOU 1587  C   SER A 226     1729   2286   2758    -93   -224     61       C  
ATOM   1588  O   SER A 226     -45.213   9.561 -46.975  1.00 15.58           O  
ANISOU 1588  O   SER A 226     1470   1988   2460    -60   -214     62       O  
ATOM   1589  CB  SER A 226     -48.336   9.399 -47.708  1.00 16.71           C  
ANISOU 1589  CB  SER A 226     1450   2169   2730    -85   -256     73       C  
ATOM   1590  OG  SER A 226     -49.688   9.287 -47.302  1.00 25.48           O  
ANISOU 1590  OG  SER A 226     2483   3293   3904    -92   -237     69       O  
ATOM   1591  N   TYR A 227     -45.691   7.683 -48.135  1.00 18.64           N  
ANISOU 1591  N   TYR A 227     1862   2394   2825   -127   -254     62       N  
ATOM   1592  CA  TYR A 227     -44.461   7.754 -48.908  1.00 17.10           C  
ANISOU 1592  CA  TYR A 227     1727   2193   2578   -123   -282     68       C  
ATOM   1593  C   TYR A 227     -44.413   9.062 -49.693  1.00 17.18           C  
ANISOU 1593  C   TYR A 227     1723   2205   2601    -93   -325     88       C  
ATOM   1594  O   TYR A 227     -45.441   9.611 -50.101  1.00 17.87           O  
ANISOU 1594  O   TYR A 227     1753   2302   2733    -86   -356    100       O  
ATOM   1595  CB  TYR A 227     -44.363   6.574 -49.878  1.00 14.38           C  
ANISOU 1595  CB  TYR A 227     1409   1854   2200   -165   -312     65       C  
ATOM   1596  CG  TYR A 227     -44.215   5.231 -49.221  1.00 15.91           C  
ANISOU 1596  CG  TYR A 227     1632   2038   2376   -195   -272     48       C  
ATOM   1597  CD1 TYR A 227     -43.208   4.997 -48.294  1.00 16.27           C  
ANISOU 1597  CD1 TYR A 227     1724   2065   2393   -180   -228     42       C  
ATOM   1598  CD2 TYR A 227     -45.087   4.189 -49.528  1.00 20.22           C  
ANISOU 1598  CD2 TYR A 227     2157   2589   2935   -238   -281     41       C  
ATOM   1599  CE1 TYR A 227     -43.070   3.767 -47.689  1.00 16.16           C  
ANISOU 1599  CE1 TYR A 227     1739   2038   2363   -205   -194     31       C  
ATOM   1600  CE2 TYR A 227     -44.955   2.951 -48.931  1.00 19.72           C  
ANISOU 1600  CE2 TYR A 227     2124   2511   2857   -266   -243     28       C  
ATOM   1601  CZ  TYR A 227     -43.946   2.750 -48.012  1.00 17.93           C  
ANISOU 1601  CZ  TYR A 227     1946   2264   2602   -247   -200     25       C  
ATOM   1602  OH  TYR A 227     -43.809   1.531 -47.403  1.00 16.66           O  
ANISOU 1602  OH  TYR A 227     1818   2085   2427   -272   -165     18       O  
ATOM   1603  N   GLY A 228     -43.213   9.572 -49.898  1.00 16.27           N  
ANISOU 1603  N   GLY A 228     1655   2078   2447    -76   -328     92       N  
ATOM   1604  CA  GLY A 228     -43.040  10.700 -50.781  1.00 16.62           C  
ANISOU 1604  CA  GLY A 228     1698   2122   2495    -54   -370    114       C  
ATOM   1605  C   GLY A 228     -42.802  11.999 -50.043  1.00 20.26           C  
ANISOU 1605  C   GLY A 228     2151   2564   2982    -13   -348    116       C  
ATOM   1606  O   GLY A 228     -42.484  12.030 -48.849  1.00 15.39           O  
ANISOU 1606  O   GLY A 228     1543   1936   2367     -1   -298     98       O  
ATOM   1607  N   ALA A 229     -42.984  13.104 -50.785  1.00 16.31           N  
ANISOU 1607  N   ALA A 229     1636   2059   2502      9   -387    140       N  
ATOM   1608  CA  ALA A 229     -42.607  14.432 -50.313  1.00 18.58           C  
ANISOU 1608  CA  ALA A 229     1926   2323   2810     47   -372    144       C  
ATOM   1609  C   ALA A 229     -43.613  15.038 -49.338  1.00 17.43           C  
ANISOU 1609  C   ALA A 229     1726   2169   2729     75   -342    135       C  
ATOM   1610  O   ALA A 229     -43.220  15.809 -48.462  1.00 15.25           O  
ANISOU 1610  O   ALA A 229     1461   1871   2464    101   -306    122       O  
ATOM   1611  CB  ALA A 229     -42.442  15.376 -51.502  1.00 16.35           C  
ANISOU 1611  CB  ALA A 229     1652   2035   2526     59   -425    177       C  
ATOM   1612  N   ASP A 230     -44.907  14.761 -49.505  1.00 16.42           N  
ANISOU 1612  N   ASP A 230     1537   2055   2645     71   -358    140       N  
ATOM   1613  CA  ASP A 230     -45.912  15.362 -48.633  1.00 21.38           C  
ANISOU 1613  CA  ASP A 230     2107   2675   3342    101   -325    131       C  
ATOM   1614  C   ASP A 230     -45.925  14.691 -47.267  1.00 20.35           C  
ANISOU 1614  C   ASP A 230     1980   2546   3205     90   -256     97       C  
ATOM   1615  O   ASP A 230     -45.937  15.366 -46.232  1.00 19.56           O  
ANISOU 1615  O   ASP A 230     1877   2429   3127    116   -208     80       O  
ATOM   1616  CB  ASP A 230     -47.298  15.270 -49.276  1.00 22.19           C  
ANISOU 1616  CB  ASP A 230     2136   2797   3499     99   -366    148       C  
ATOM   1617  CG  ASP A 230     -47.387  16.014 -50.603  1.00 25.46           C  
ANISOU 1617  CG  ASP A 230     2544   3209   3920    113   -440    186       C  
ATOM   1618  OD1 ASP A 230     -46.703  17.039 -50.766  1.00 27.90           O  
ANISOU 1618  OD1 ASP A 230     2885   3492   4222    140   -446    199       O  
ATOM   1619  OD2 ASP A 230     -48.159  15.580 -51.479  1.00 35.82           O  
ANISOU 1619  OD2 ASP A 230     3820   4545   5245     94   -492    204       O  
ATOM   1620  N   GLY A 231     -45.939  13.358 -47.248  1.00 19.81           N  
ANISOU 1620  N   GLY A 231     1923   2497   3105     50   -249     89       N  
ATOM   1621  CA  GLY A 231     -45.756  12.654 -45.992  1.00 18.74           C  
ANISOU 1621  CA  GLY A 231     1808   2361   2951     36   -186     63       C  
ATOM   1622  C   GLY A 231     -44.440  13.025 -45.336  1.00 16.27           C  
ANISOU 1622  C   GLY A 231     1560   2031   2592     49   -159     52       C  
ATOM   1623  O   GLY A 231     -44.386  13.281 -44.127  1.00 16.78           O  
ANISOU 1623  O   GLY A 231     1631   2086   2658     61   -107     31       O  
ATOM   1624  N   GLY A 232     -43.367  13.085 -46.132  1.00 17.94           N  
ANISOU 1624  N   GLY A 232     1817   2238   2760     46   -195     64       N  
ATOM   1625  CA  GLY A 232     -42.078  13.495 -45.594  1.00 16.08           C  
ANISOU 1625  CA  GLY A 232     1636   1987   2485     57   -176     55       C  
ATOM   1626  C   GLY A 232     -42.121  14.885 -44.996  1.00 19.55           C  
ANISOU 1626  C   GLY A 232     2066   2406   2958     93   -157     47       C  
ATOM   1627  O   GLY A 232     -41.547  15.133 -43.930  1.00 17.54           O  
ANISOU 1627  O   GLY A 232     1840   2141   2685    100   -118     27       O  
ATOM   1628  N   ALA A 233     -42.799  15.818 -45.672  1.00 16.97           N  
ANISOU 1628  N   ALA A 233     1700   2070   2678    115   -186     64       N  
ATOM   1629  CA  ALA A 233     -42.851  17.189 -45.162  1.00 18.02           C  
ANISOU 1629  CA  ALA A 233     1825   2175   2847    152   -168     57       C  
ATOM   1630  C   ALA A 233     -43.531  17.238 -43.800  1.00 17.12           C  
ANISOU 1630  C   ALA A 233     1687   2057   2759    163   -106     26       C  
ATOM   1631  O   ALA A 233     -43.033  17.874 -42.861  1.00 17.64           O  
ANISOU 1631  O   ALA A 233     1781   2105   2817    177    -68      4       O  
ATOM   1632  CB  ALA A 233     -43.579  18.097 -46.158  1.00 19.14           C  
ANISOU 1632  CB  ALA A 233     1925   2306   3041    177   -212     84       C  
ATOM   1633  N   LYS A 234     -44.674  16.560 -43.670  1.00 18.93           N  
ANISOU 1633  N   LYS A 234     1867   2306   3021    153    -92     24       N  
ATOM   1634  CA  LYS A 234     -45.386  16.542 -42.395  1.00 19.95           C  
ANISOU 1634  CA  LYS A 234     1972   2434   3174    160    -27     -4       C  
ATOM   1635  C   LYS A 234     -44.559  15.858 -41.320  1.00 19.04           C  
ANISOU 1635  C   LYS A 234     1915   2324   2996    137     17    -26       C  
ATOM   1636  O   LYS A 234     -44.504  16.317 -40.171  1.00 16.40           O  
ANISOU 1636  O   LYS A 234     1596   1978   2659    148     69    -53       O  
ATOM   1637  CB  LYS A 234     -46.737  15.836 -42.555  1.00 22.55           C  
ANISOU 1637  CB  LYS A 234     2233   2785   3549    147    -22      1       C  
ATOM   1638  CG  LYS A 234     -47.715  16.579 -43.467  1.00 28.01           C  
ANISOU 1638  CG  LYS A 234     2856   3473   4312    175    -64     22       C  
ATOM   1639  CD  LYS A 234     -49.059  15.852 -43.608  1.00 38.41           C  
ANISOU 1639  CD  LYS A 234     4099   4817   5679    158    -62     26       C  
ATOM   1640  CE  LYS A 234     -49.935  16.023 -42.360  1.00 45.33           C  
ANISOU 1640  CE  LYS A 234     4932   5691   6600    171     15     -4       C  
ATOM   1641  NZ  LYS A 234     -51.294  15.390 -42.507  1.00 45.61           N  
ANISOU 1641  NZ  LYS A 234     4885   5752   6693    155     19      0       N  
ATOM   1642  N   PHE A 235     -43.923  14.744 -41.670  1.00 17.29           N  
ANISOU 1642  N   PHE A 235     1728   2118   2724    104     -5    -15       N  
ATOM   1643  CA  PHE A 235     -43.107  14.021 -40.702  1.00 14.74           C  
ANISOU 1643  CA  PHE A 235     1459   1799   2341     84     29    -30       C  
ATOM   1644  C   PHE A 235     -41.931  14.871 -40.240  1.00 17.33           C  
ANISOU 1644  C   PHE A 235     1837   2110   2637    100     31    -42       C  
ATOM   1645  O   PHE A 235     -41.643  14.957 -39.041  1.00 17.02           O  
ANISOU 1645  O   PHE A 235     1827   2067   2571    100     74    -64       O  
ATOM   1646  CB  PHE A 235     -42.621  12.718 -41.325  1.00 14.56           C  
ANISOU 1646  CB  PHE A 235     1462   1792   2279     52     -1    -14       C  
ATOM   1647  CG  PHE A 235     -41.506  12.067 -40.571  1.00 17.65           C  
ANISOU 1647  CG  PHE A 235     1916   2184   2608     38     17    -21       C  
ATOM   1648  CD1 PHE A 235     -41.776  11.300 -39.448  1.00 16.96           C  
ANISOU 1648  CD1 PHE A 235     1842   2102   2501     21     64    -32       C  
ATOM   1649  CD2 PHE A 235     -40.187  12.222 -40.982  1.00 17.32           C  
ANISOU 1649  CD2 PHE A 235     1916   2136   2529     41    -15    -14       C  
ATOM   1650  CE1 PHE A 235     -40.746  10.685 -38.752  1.00 17.48           C  
ANISOU 1650  CE1 PHE A 235     1965   2167   2509     10     74    -33       C  
ATOM   1651  CE2 PHE A 235     -39.153  11.605 -40.287  1.00 17.35           C  
ANISOU 1651  CE2 PHE A 235     1972   2141   2481     31     -3    -18       C  
ATOM   1652  CZ  PHE A 235     -39.440  10.835 -39.176  1.00 17.69           C  
ANISOU 1652  CZ  PHE A 235     2029   2189   2503     16     38    -26       C  
ATOM   1653  N   LEU A 236     -41.232  15.505 -41.186  1.00 14.16           N  
ANISOU 1653  N   LEU A 236     1448   1698   2234    111    -15    -26       N  
ATOM   1654  CA  LEU A 236     -40.036  16.255 -40.818  1.00 17.65           C  
ANISOU 1654  CA  LEU A 236     1936   2124   2646    120    -15    -36       C  
ATOM   1655  C   LEU A 236     -40.395  17.546 -40.101  1.00 18.13           C  
ANISOU 1655  C   LEU A 236     1987   2160   2740    147     16    -59       C  
ATOM   1656  O   LEU A 236     -39.684  17.966 -39.183  1.00 18.47           O  
ANISOU 1656  O   LEU A 236     2069   2193   2754    148     40    -81       O  
ATOM   1657  CB  LEU A 236     -39.188  16.552 -42.056  1.00 19.95           C  
ANISOU 1657  CB  LEU A 236     2242   2411   2927    120    -68    -13       C  
ATOM   1658  CG  LEU A 236     -37.834  17.197 -41.761  1.00 16.25           C  
ANISOU 1658  CG  LEU A 236     1820   1929   2426    121    -72    -22       C  
ATOM   1659  CD1 LEU A 236     -36.891  16.202 -41.089  1.00 15.90           C  
ANISOU 1659  CD1 LEU A 236     1815   1901   2325    100    -61    -30       C  
ATOM   1660  CD2 LEU A 236     -37.209  17.734 -43.038  1.00 20.97           C  
ANISOU 1660  CD2 LEU A 236     2423   2518   3026    123   -117      2       C  
ATOM   1661  N   GLU A 237     -41.484  18.198 -40.511  1.00 19.14           N  
ANISOU 1661  N   GLU A 237     2063   2277   2931    171     15    -53       N  
ATOM   1662  CA  GLU A 237     -41.933  19.379 -39.782  1.00 21.66           C  
ANISOU 1662  CA  GLU A 237     2371   2569   3290    200     52    -78       C  
ATOM   1663  C   GLU A 237     -42.113  19.055 -38.307  1.00 22.60           C  
ANISOU 1663  C   GLU A 237     2508   2695   3385    191    117   -113       C  
ATOM   1664  O   GLU A 237     -41.662  19.803 -37.434  1.00 24.86           O  
ANISOU 1664  O   GLU A 237     2828   2962   3656    199    147   -142       O  
ATOM   1665  CB  GLU A 237     -43.234  19.917 -40.382  1.00 24.72           C  
ANISOU 1665  CB  GLU A 237     2691   2946   3755    229     45    -66       C  
ATOM   1666  CG  GLU A 237     -43.825  21.087 -39.582  1.00 32.26           C  
ANISOU 1666  CG  GLU A 237     3628   3870   4760    264     92    -95       C  
ATOM   1667  CD  GLU A 237     -45.091  21.652 -40.202  1.00 48.62           C  
ANISOU 1667  CD  GLU A 237     5627   5930   6918    298     81    -79       C  
ATOM   1668  OE1 GLU A 237     -45.915  20.858 -40.718  1.00 54.50           O  
ANISOU 1668  OE1 GLU A 237     6322   6702   7684    288     64    -60       O  
ATOM   1669  OE2 GLU A 237     -45.265  22.891 -40.171  1.00 57.61           O  
ANISOU 1669  OE2 GLU A 237     6756   7029   8103    335     88    -86       O  
ATOM   1670  N   LYS A 238     -42.723  17.913 -38.011  1.00 24.91           N  
ANISOU 1670  N   LYS A 238     2783   3014   3667    170    138   -112       N  
ATOM   1671  CA  LYS A 238     -42.920  17.524 -36.622  1.00 24.56           C  
ANISOU 1671  CA  LYS A 238     2759   2978   3593    157    201   -141       C  
ATOM   1672  C   LYS A 238     -41.593  17.191 -35.949  1.00 21.17           C  
ANISOU 1672  C   LYS A 238     2403   2554   3087    136    199   -149       C  
ATOM   1673  O   LYS A 238     -41.392  17.516 -34.775  1.00 21.27           O  
ANISOU 1673  O   LYS A 238     2450   2562   3070    135    242   -179       O  
ATOM   1674  CB  LYS A 238     -43.885  16.343 -36.559  1.00 27.30           C  
ANISOU 1674  CB  LYS A 238     3070   3351   3950    136    222   -132       C  
ATOM   1675  CG  LYS A 238     -44.280  15.920 -35.167  1.00 36.13           C  
ANISOU 1675  CG  LYS A 238     4205   4479   5043    120    293   -158       C  
ATOM   1676  CD  LYS A 238     -45.315  14.801 -35.225  1.00 31.16           C  
ANISOU 1676  CD  LYS A 238     3533   3872   4433     97    314   -146       C  
ATOM   1677  CE  LYS A 238     -45.647  14.291 -33.831  1.00 42.25           C  
ANISOU 1677  CE  LYS A 238     4962   5287   5804     76    388   -168       C  
ATOM   1678  NZ  LYS A 238     -44.414  13.875 -33.093  1.00 44.10           N  
ANISOU 1678  NZ  LYS A 238     5280   5524   5952     57    386   -170       N  
ATOM   1679  N   ARG A 239     -40.658  16.583 -36.688  1.00 19.38           N  
ANISOU 1679  N   ARG A 239     2199   2337   2826    121    148   -124       N  
ATOM   1680  CA  ARG A 239     -39.375  16.205 -36.100  1.00 20.96           C  
ANISOU 1680  CA  ARG A 239     2461   2544   2959    103    140   -128       C  
ATOM   1681  C   ARG A 239     -38.512  17.413 -35.763  1.00 21.69           C  
ANISOU 1681  C   ARG A 239     2585   2616   3041    116    135   -148       C  
ATOM   1682  O   ARG A 239     -37.760  17.384 -34.781  1.00 20.14           O  
ANISOU 1682  O   ARG A 239     2436   2424   2794    104    148   -165       O  
ATOM   1683  CB  ARG A 239     -38.604  15.296 -37.053  1.00 20.48           C  
ANISOU 1683  CB  ARG A 239     2411   2496   2874     88     90    -97       C  
ATOM   1684  CG  ARG A 239     -38.931  13.859 -36.928  1.00 24.99           C  
ANISOU 1684  CG  ARG A 239     2983   3087   3424     65    100    -84       C  
ATOM   1685  CD  ARG A 239     -38.128  13.194 -35.819  1.00 24.44           C  
ANISOU 1685  CD  ARG A 239     2968   3026   3292     48    116    -90       C  
ATOM   1686  NE  ARG A 239     -38.301  11.743 -35.880  1.00 24.42           N  
ANISOU 1686  NE  ARG A 239     2971   3036   3270     26    118    -71       N  
ATOM   1687  CZ  ARG A 239     -39.342  11.105 -35.368  1.00 24.09           C  
ANISOU 1687  CZ  ARG A 239     2915   3001   3237     12    158    -72       C  
ATOM   1688  NH1 ARG A 239     -40.312  11.757 -34.748  1.00 27.16           N  
ANISOU 1688  NH1 ARG A 239     3279   3388   3653     19    203    -93       N  
ATOM   1689  NH2 ARG A 239     -39.417   9.785 -35.488  1.00 25.74           N  
ANISOU 1689  NH2 ARG A 239     3134   3216   3430    -11    156    -53       N  
ATOM   1690  N   LEU A 240     -38.555  18.458 -36.596  1.00 19.19           N  
ANISOU 1690  N   LEU A 240     2247   2277   2769    137    110   -143       N  
ATOM   1691  CA  LEU A 240     -37.649  19.595 -36.468  1.00 16.32           C  
ANISOU 1691  CA  LEU A 240     1913   1889   2399    145     99   -158       C  
ATOM   1692  C   LEU A 240     -38.283  20.797 -35.791  1.00 20.63           C  
ANISOU 1692  C   LEU A 240     2453   2405   2981    167    140   -191       C  
ATOM   1693  O   LEU A 240     -37.614  21.825 -35.631  1.00 19.17           O  
ANISOU 1693  O   LEU A 240     2294   2194   2795    172    134   -208       O  
ATOM   1694  CB  LEU A 240     -37.135  20.013 -37.844  1.00 16.67           C  
ANISOU 1694  CB  LEU A 240     1946   1922   2465    151     45   -129       C  
ATOM   1695  CG  LEU A 240     -36.271  18.982 -38.563  1.00 17.34           C  
ANISOU 1695  CG  LEU A 240     2044   2032   2512    130      6   -101       C  
ATOM   1696  CD1 LEU A 240     -35.741  19.617 -39.841  1.00 15.82           C  
ANISOU 1696  CD1 LEU A 240     1846   1825   2339    135    -38    -77       C  
ATOM   1697  CD2 LEU A 240     -35.138  18.522 -37.645  1.00 14.58           C  
ANISOU 1697  CD2 LEU A 240     1741   1696   2102    110     10   -115       C  
ATOM   1698  N   LYS A 241     -39.552  20.690 -35.408  1.00 22.56           N  
ANISOU 1698  N   LYS A 241     2661   2650   3259    179    183   -202       N  
ATOM   1699  CA  LYS A 241     -40.274  21.801 -34.812  1.00 25.00           C  
ANISOU 1699  CA  LYS A 241     2958   2929   3612    205    229   -235       C  
ATOM   1700  C   LYS A 241     -39.623  22.216 -33.502  1.00 24.20           C  
ANISOU 1700  C   LYS A 241     2915   2821   3460    193    265   -278       C  
ATOM   1701  O   LYS A 241     -39.271  21.371 -32.675  1.00 24.45           O  
ANISOU 1701  O   LYS A 241     2982   2880   3429    166    280   -286       O  
ATOM   1702  CB  LYS A 241     -41.729  21.396 -34.578  1.00 26.27           C  
ANISOU 1702  CB  LYS A 241     3065   3100   3815    217    274   -240       C  
ATOM   1703  CG  LYS A 241     -42.642  22.529 -34.101  1.00 31.99           C  
ANISOU 1703  CG  LYS A 241     3763   3792   4601    251    325   -273       C  
ATOM   1704  CD  LYS A 241     -42.588  23.716 -35.065  1.00 35.41           C  
ANISOU 1704  CD  LYS A 241     4176   4184   5093    284    287   -259       C  
ATOM   1705  CE  LYS A 241     -43.174  23.371 -36.449  1.00 46.66           C  
ANISOU 1705  CE  LYS A 241     5541   5619   6567    296    235   -210       C  
ATOM   1706  NZ  LYS A 241     -42.981  24.452 -37.477  1.00 42.96           N  
ANISOU 1706  NZ  LYS A 241     5063   5114   6145    324    188   -187       N  
ATOM   1707  N   VAL A 242     -39.448  23.518 -33.327  1.00 22.00           N  
ANISOU 1707  N   VAL A 242     2651   2502   3206    210    274   -304       N  
ATOM   1708  CA  VAL A 242     -38.959  24.091 -32.077  1.00 25.82           C  
ANISOU 1708  CA  VAL A 242     3190   2974   3647    199    311   -352       C  
ATOM   1709  C   VAL A 242     -40.167  24.542 -31.267  1.00 24.08           C  
ANISOU 1709  C   VAL A 242     2950   2736   3462    220    385   -390       C  
ATOM   1710  O   VAL A 242     -40.978  25.341 -31.749  1.00 25.30           O  
ANISOU 1710  O   VAL A 242     3061   2858   3693    256    398   -392       O  
ATOM   1711  CB  VAL A 242     -37.995  25.260 -32.336  1.00 24.75           C  
ANISOU 1711  CB  VAL A 242     3085   2801   3518    201    280   -363       C  
ATOM   1712  CG1 VAL A 242     -37.499  25.848 -31.019  1.00 27.52           C  
ANISOU 1712  CG1 VAL A 242     3495   3140   3822    184    316   -416       C  
ATOM   1713  CG2 VAL A 242     -36.822  24.808 -33.213  1.00 21.56           C  
ANISOU 1713  CG2 VAL A 242     2692   2415   3085    180    211   -323       C  
ATOM   1714  N   SER A 243     -40.305  24.020 -30.050  1.00 30.41           N  
ANISOU 1714  N   SER A 243     3784   3561   4208    199    435   -419       N  
ATOM   1715  CA  SER A 243     -41.388  24.389 -29.145  1.00 28.55           C  
ANISOU 1715  CA  SER A 243     3538   3314   3996    215    516   -462       C  
ATOM   1716  C   SER A 243     -40.823  24.953 -27.852  1.00 34.37           C  
ANISOU 1716  C   SER A 243     4348   4040   4671    196    554   -516       C  
ATOM   1717  O   SER A 243     -39.728  24.577 -27.421  1.00 33.56           O  
ANISOU 1717  O   SER A 243     4303   3959   4491    162    523   -515       O  
ATOM   1718  CB  SER A 243     -42.283  23.194 -28.807  1.00 33.43           C  
ANISOU 1718  CB  SER A 243     4128   3971   4604    203    555   -449       C  
ATOM   1719  OG  SER A 243     -42.885  22.658 -29.970  1.00 40.19           O  
ANISOU 1719  OG  SER A 243     4915   4837   5517    216    521   -404       O  
ATOM   1720  N   GLY A 244     -41.609  25.827 -27.210  1.00 33.88           N  
ANISOU 1720  N   GLY A 244     4282   3947   4644    219    624   -564       N  
ATOM   1721  CA  GLY A 244     -41.139  26.521 -26.021  1.00 34.15           C  
ANISOU 1721  CA  GLY A 244     4388   3964   4624    202    663   -622       C  
ATOM   1722  C   GLY A 244     -40.916  25.612 -24.829  1.00 35.52           C  
ANISOU 1722  C   GLY A 244     4617   4182   4698    161    694   -637       C  
ATOM   1723  O   GLY A 244     -40.012  25.852 -24.025  1.00 39.11           O  
ANISOU 1723  O   GLY A 244     5144   4639   5078    131    686   -667       O  
ATOM   1724  N   ASN A 245     -41.720  24.564 -24.700  1.00 30.98           N  
ANISOU 1724  N   ASN A 245     4010   3642   4119    155    726   -616       N  
ATOM   1725  CA  ASN A 245     -41.622  23.614 -23.600  1.00 40.05           C  
ANISOU 1725  CA  ASN A 245     5211   4832   5175    116    759   -622       C  
ATOM   1726  C   ASN A 245     -40.607  22.509 -23.865  1.00 39.72           C  
ANISOU 1726  C   ASN A 245     5194   4827   5069     85    684   -572       C  
ATOM   1727  O   ASN A 245     -40.417  21.627 -23.018  1.00 39.38           O  
ANISOU 1727  O   ASN A 245     5198   4818   4947     52    699   -567       O  
ATOM   1728  CB  ASN A 245     -42.998  23.000 -23.330  1.00 46.00           C  
ANISOU 1728  CB  ASN A 245     5917   5602   5959    123    834   -622       C  
ATOM   1729  CG  ASN A 245     -43.677  22.511 -24.601  1.00 52.48           C  
ANISOU 1729  CG  ASN A 245     6648   6426   6865    146    803   -572       C  
ATOM   1730  OD1 ASN A 245     -43.017  22.107 -25.566  1.00 48.77           O  
ANISOU 1730  OD1 ASN A 245     6166   5965   6400    144    723   -526       O  
ATOM   1731  ND2 ASN A 245     -45.006  22.554 -24.610  1.00 63.52           N  
ANISOU 1731  ND2 ASN A 245     7983   7821   8332    168    867   -583       N  
ATOM   1732  N   GLN A 246     -39.971  22.537 -25.028  1.00 34.47           N  
ANISOU 1732  N   GLN A 246     4501   4155   4440     95    608   -534       N  
ATOM   1733  CA  GLN A 246     -38.961  21.556 -25.392  1.00 31.76           C  
ANISOU 1733  CA  GLN A 246     4177   3842   4047     71    537   -488       C  
ATOM   1734  C   GLN A 246     -37.672  21.839 -24.628  1.00 28.49           C  
ANISOU 1734  C   GLN A 246     3838   3435   3553     43    505   -508       C  
ATOM   1735  O   GLN A 246     -37.257  22.994 -24.500  1.00 25.26           O  
ANISOU 1735  O   GLN A 246     3450   2995   3153     48    501   -545       O  
ATOM   1736  CB  GLN A 246     -38.736  21.660 -26.899  1.00 29.82           C  
ANISOU 1736  CB  GLN A 246     3877   3584   3868     93    473   -448       C  
ATOM   1737  CG  GLN A 246     -38.159  20.508 -27.629  1.00 32.54           C  
ANISOU 1737  CG  GLN A 246     4211   3957   4195     80    414   -395       C  
ATOM   1738  CD  GLN A 246     -38.064  20.827 -29.114  1.00 29.69           C  
ANISOU 1738  CD  GLN A 246     3799   3579   3903    102    362   -364       C  
ATOM   1739  OE1 GLN A 246     -38.052  22.002 -29.515  1.00 25.86           O  
ANISOU 1739  OE1 GLN A 246     3301   3059   3464    123    356   -381       O  
ATOM   1740  NE2 GLN A 246     -38.021  19.790 -29.938  1.00 26.62           N  
ANISOU 1740  NE2 GLN A 246     3384   3212   3520     97    325   -319       N  
ATOM   1741  N   HIS A 247     -37.037  20.788 -24.106  1.00 23.55           N  
ANISOU 1741  N   HIS A 247     3253   2845   2850     13    481   -485       N  
ATOM   1742  CA  HIS A 247     -35.728  20.971 -23.499  1.00 23.70           C  
ANISOU 1742  CA  HIS A 247     3335   2874   2796    -13    435   -496       C  
ATOM   1743  C   HIS A 247     -34.828  21.714 -24.483  1.00 22.01           C  
ANISOU 1743  C   HIS A 247     3100   2639   2625     -2    371   -488       C  
ATOM   1744  O   HIS A 247     -34.890  21.485 -25.692  1.00 23.42           O  
ANISOU 1744  O   HIS A 247     3225   2812   2863     17    338   -451       O  
ATOM   1745  CB  HIS A 247     -35.116  19.619 -23.120  1.00 24.37           C  
ANISOU 1745  CB  HIS A 247     3451   3000   2808    -39    401   -456       C  
ATOM   1746  CG  HIS A 247     -33.900  19.722 -22.247  1.00 18.98           C  
ANISOU 1746  CG  HIS A 247     2836   2333   2041    -68    360   -468       C  
ATOM   1747  ND1 HIS A 247     -32.659  20.075 -22.733  1.00 24.78           N  
ANISOU 1747  ND1 HIS A 247     3571   3066   2778    -71    287   -459       N  
ATOM   1748  CD2 HIS A 247     -33.729  19.479 -20.927  1.00 22.87           C  
ANISOU 1748  CD2 HIS A 247     3397   2848   2444    -97    379   -487       C  
ATOM   1749  CE1 HIS A 247     -31.778  20.055 -21.749  1.00 26.39           C  
ANISOU 1749  CE1 HIS A 247     3835   3290   2901   -101    259   -473       C  
ATOM   1750  NE2 HIS A 247     -32.403  19.699 -20.640  1.00 25.84           N  
ANISOU 1750  NE2 HIS A 247     3811   3235   2771   -117    313   -489       N  
ATOM   1751  N   GLU A 248     -34.022  22.645 -23.968  1.00 24.29           N  
ANISOU 1751  N   GLU A 248     3432   2913   2884    -17    354   -526       N  
ATOM   1752  CA  GLU A 248     -33.260  23.496 -24.877  1.00 25.23           C  
ANISOU 1752  CA  GLU A 248     3531   3005   3051     -9    304   -523       C  
ATOM   1753  C   GLU A 248     -32.236  22.703 -25.679  1.00 21.10           C  
ANISOU 1753  C   GLU A 248     2989   2507   2521    -16    229   -470       C  
ATOM   1754  O   GLU A 248     -31.888  23.101 -26.792  1.00 19.60           O  
ANISOU 1754  O   GLU A 248     2762   2299   2386     -3    193   -451       O  
ATOM   1755  CB  GLU A 248     -32.589  24.633 -24.116  1.00 32.12           C  
ANISOU 1755  CB  GLU A 248     4455   3857   3893    -29    302   -576       C  
ATOM   1756  CG  GLU A 248     -31.553  24.234 -23.107  1.00 37.51           C  
ANISOU 1756  CG  GLU A 248     5199   4574   4480    -69    267   -584       C  
ATOM   1757  CD  GLU A 248     -31.078  25.442 -22.315  1.00 54.74           C  
ANISOU 1757  CD  GLU A 248     7433   6732   6634    -92    274   -646       C  
ATOM   1758  OE1 GLU A 248     -31.944  26.186 -21.792  1.00 60.51           O  
ANISOU 1758  OE1 GLU A 248     8181   7432   7377    -83    342   -695       O  
ATOM   1759  OE2 GLU A 248     -29.850  25.665 -22.241  1.00 61.92           O  
ANISOU 1759  OE2 GLU A 248     8363   7650   7513   -119    213   -647       O  
ATOM   1760  N   GLU A 249     -31.762  21.577 -25.152  1.00 21.65           N  
ANISOU 1760  N   GLU A 249     3084   2616   2525    -36    207   -446       N  
ATOM   1761  CA  GLU A 249     -30.876  20.726 -25.935  1.00 22.19           C  
ANISOU 1761  CA  GLU A 249     3131   2707   2595    -37    143   -396       C  
ATOM   1762  C   GLU A 249     -31.572  20.218 -27.193  1.00 20.67           C  
ANISOU 1762  C   GLU A 249     2878   2508   2469    -11    146   -358       C  
ATOM   1763  O   GLU A 249     -30.955  20.118 -28.259  1.00 21.32           O  
ANISOU 1763  O   GLU A 249     2930   2589   2583     -4    100   -329       O  
ATOM   1764  CB  GLU A 249     -30.390  19.572 -25.064  1.00 20.84           C  
ANISOU 1764  CB  GLU A 249     2999   2575   2345    -58    125   -376       C  
ATOM   1765  CG  GLU A 249     -29.710  18.458 -25.811  1.00 25.87           C  
ANISOU 1765  CG  GLU A 249     3612   3233   2986    -54     72   -322       C  
ATOM   1766  CD  GLU A 249     -29.387  17.293 -24.896  1.00 27.94           C  
ANISOU 1766  CD  GLU A 249     3915   3528   3174    -70     60   -300       C  
ATOM   1767  OE1 GLU A 249     -28.901  17.531 -23.765  1.00 31.12           O  
ANISOU 1767  OE1 GLU A 249     4370   3944   3511    -93     52   -322       O  
ATOM   1768  OE2 GLU A 249     -29.647  16.144 -25.294  1.00 22.91           O  
ANISOU 1768  OE2 GLU A 249     3260   2900   2544    -61     58   -259       O  
ATOM   1769  N   LEU A 250     -32.861  19.895 -27.088  1.00 20.05           N  
ANISOU 1769  N   LEU A 250     2782   2427   2410      2    200   -359       N  
ATOM   1770  CA  LEU A 250     -33.634  19.515 -28.263  1.00 16.83           C  
ANISOU 1770  CA  LEU A 250     2315   2012   2067     24    203   -328       C  
ATOM   1771  C   LEU A 250     -33.925  20.725 -29.140  1.00 18.26           C  
ANISOU 1771  C   LEU A 250     2461   2157   2321     47    202   -340       C  
ATOM   1772  O   LEU A 250     -33.920  20.623 -30.373  1.00 18.22           O  
ANISOU 1772  O   LEU A 250     2414   2146   2362     61    171   -308       O  
ATOM   1773  CB  LEU A 250     -34.941  18.848 -27.823  1.00 19.77           C  
ANISOU 1773  CB  LEU A 250     2676   2394   2442     27    262   -328       C  
ATOM   1774  CG  LEU A 250     -34.756  17.518 -27.081  1.00 19.35           C  
ANISOU 1774  CG  LEU A 250     2657   2373   2321      4    264   -306       C  
ATOM   1775  CD1 LEU A 250     -35.971  17.210 -26.237  1.00 23.55           C  
ANISOU 1775  CD1 LEU A 250     3195   2911   2842     -1    337   -322       C  
ATOM   1776  CD2 LEU A 250     -34.554  16.454 -28.106  1.00 17.56           C  
ANISOU 1776  CD2 LEU A 250     2399   2158   2115      8    223   -258       C  
ATOM   1777  N   GLN A 251     -34.216  21.867 -28.516  1.00 19.08           N  
ANISOU 1777  N   GLN A 251     2583   2234   2434     52    238   -385       N  
ATOM   1778  CA  GLN A 251     -34.441  23.098 -29.268  1.00 20.57           C  
ANISOU 1778  CA  GLN A 251     2744   2381   2692     75    237   -397       C  
ATOM   1779  C   GLN A 251     -33.204  23.486 -30.055  1.00 17.87           C  
ANISOU 1779  C   GLN A 251     2404   2031   2355     66    174   -379       C  
ATOM   1780  O   GLN A 251     -33.292  23.844 -31.235  1.00 17.39           O  
ANISOU 1780  O   GLN A 251     2306   1951   2350     84    151   -354       O  
ATOM   1781  CB  GLN A 251     -34.819  24.242 -28.326  1.00 22.27           C  
ANISOU 1781  CB  GLN A 251     2989   2564   2909     78    288   -454       C  
ATOM   1782  CG  GLN A 251     -36.165  24.110 -27.667  1.00 23.04           C  
ANISOU 1782  CG  GLN A 251     3075   2661   3019     92    361   -477       C  
ATOM   1783  CD  GLN A 251     -36.604  25.404 -27.005  1.00 32.48           C  
ANISOU 1783  CD  GLN A 251     4290   3815   4237    105    414   -534       C  
ATOM   1784  OE1 GLN A 251     -35.969  25.889 -26.075  1.00 35.44           O  
ANISOU 1784  OE1 GLN A 251     4723   4185   4559     82    421   -574       O  
ATOM   1785  NE2 GLN A 251     -37.688  25.972 -27.495  1.00 37.11           N  
ANISOU 1785  NE2 GLN A 251     4827   4369   4903    142    449   -538       N  
ATOM   1786  N   ASN A 252     -32.040  23.432 -29.404  1.00 18.99           N  
ANISOU 1786  N   ASN A 252     2590   2189   2438     37    146   -391       N  
ATOM   1787  CA  ASN A 252     -30.832  24.016 -29.972  1.00 19.28           C  
ANISOU 1787  CA  ASN A 252     2630   2215   2481     25     95   -384       C  
ATOM   1788  C   ASN A 252     -30.354  23.269 -31.214  1.00 20.67           C  
ANISOU 1788  C   ASN A 252     2769   2409   2676     29     49   -333       C  
ATOM   1789  O   ASN A 252     -29.847  23.895 -32.153  1.00 21.98           O  
ANISOU 1789  O   ASN A 252     2918   2555   2879     31     21   -320       O  
ATOM   1790  CB  ASN A 252     -29.745  24.082 -28.902  1.00 20.28           C  
ANISOU 1790  CB  ASN A 252     2807   2360   2540     -9     74   -411       C  
ATOM   1791  CG  ASN A 252     -29.998  25.199 -27.890  1.00 25.49           C  
ANISOU 1791  CG  ASN A 252     3507   2990   3187    -17    113   -469       C  
ATOM   1792  OD1 ASN A 252     -30.858  26.053 -28.103  1.00 25.39           O  
ANISOU 1792  OD1 ASN A 252     3482   2937   3227      5    152   -490       O  
ATOM   1793  ND2 ASN A 252     -29.246  25.202 -26.798  1.00 24.06           N  
ANISOU 1793  ND2 ASN A 252     3376   2828   2938    -49    100   -497       N  
ATOM   1794  N   VAL A 253     -30.494  21.939 -31.252  1.00 17.84           N  
ANISOU 1794  N   VAL A 253     2401   2085   2292     29     44   -303       N  
ATOM   1795  CA  VAL A 253     -30.053  21.224 -32.453  1.00 17.38           C  
ANISOU 1795  CA  VAL A 253     2311   2040   2251     33      4   -259       C  
ATOM   1796  C   VAL A 253     -30.946  21.597 -33.631  1.00 16.68           C  
ANISOU 1796  C   VAL A 253     2181   1928   2228     57     12   -241       C  
ATOM   1797  O   VAL A 253     -30.471  21.779 -34.757  1.00 17.40           O  
ANISOU 1797  O   VAL A 253     2252   2014   2346     59    -19   -216       O  
ATOM   1798  CB  VAL A 253     -30.015  19.700 -32.215  1.00 19.53           C  
ANISOU 1798  CB  VAL A 253     2586   2349   2484     28     -2   -233       C  
ATOM   1799  CG1 VAL A 253     -31.394  19.163 -31.930  1.00 19.73           C  
ANISOU 1799  CG1 VAL A 253     2602   2377   2518     39     44   -232       C  
ATOM   1800  CG2 VAL A 253     -29.417  18.972 -33.434  1.00 15.97           C  
ANISOU 1800  CG2 VAL A 253     2108   1910   2048     31    -41   -193       C  
ATOM   1801  N   ARG A 254     -32.241  21.775 -33.369  1.00 15.85           N  
ANISOU 1801  N   ARG A 254     2062   1811   2149     75     55   -254       N  
ATOM   1802  CA  ARG A 254     -33.186  22.161 -34.407  1.00 16.99           C  
ANISOU 1802  CA  ARG A 254     2163   1933   2358    100     60   -237       C  
ATOM   1803  C   ARG A 254     -32.941  23.586 -34.868  1.00 18.28           C  
ANISOU 1803  C   ARG A 254     2328   2056   2563    109     51   -247       C  
ATOM   1804  O   ARG A 254     -32.934  23.860 -36.073  1.00 17.50           O  
ANISOU 1804  O   ARG A 254     2203   1944   2502    119     24   -217       O  
ATOM   1805  CB  ARG A 254     -34.612  22.005 -33.889  1.00 16.20           C  
ANISOU 1805  CB  ARG A 254     2044   1832   2280    116    111   -251       C  
ATOM   1806  CG  ARG A 254     -35.063  20.545 -33.860  1.00 16.48           C  
ANISOU 1806  CG  ARG A 254     2066   1902   2292    108    116   -228       C  
ATOM   1807  CD  ARG A 254     -36.049  20.268 -32.762  1.00 18.42           C  
ANISOU 1807  CD  ARG A 254     2315   2155   2527    109    174   -253       C  
ATOM   1808  NE  ARG A 254     -36.402  18.856 -32.793  1.00 19.14           N  
ANISOU 1808  NE  ARG A 254     2397   2277   2598     96    177   -227       N  
ATOM   1809  CZ  ARG A 254     -35.645  17.889 -32.296  1.00 19.86           C  
ANISOU 1809  CZ  ARG A 254     2524   2393   2629     74    163   -217       C  
ATOM   1810  NH1 ARG A 254     -34.563  18.158 -31.586  1.00 17.53           N  
ANISOU 1810  NH1 ARG A 254     2275   2101   2284     61    148   -232       N  
ATOM   1811  NH2 ARG A 254     -35.975  16.622 -32.528  1.00 20.08           N  
ANISOU 1811  NH2 ARG A 254     2540   2442   2648     65    161   -190       N  
ATOM   1812  N   LYS A 255     -32.758  24.511 -33.920  1.00 16.40           N  
ANISOU 1812  N   LYS A 255     2121   1794   2316    104     75   -289       N  
ATOM   1813  CA  LYS A 255     -32.462  25.893 -34.292  1.00 21.53           C  
ANISOU 1813  CA  LYS A 255     2777   2397   3005    110     67   -301       C  
ATOM   1814  C   LYS A 255     -31.211  25.965 -35.155  1.00 20.54           C  
ANISOU 1814  C   LYS A 255     2655   2276   2872     90     16   -274       C  
ATOM   1815  O   LYS A 255     -31.176  26.696 -36.150  1.00 20.20           O  
ANISOU 1815  O   LYS A 255     2598   2204   2874    100     -1   -254       O  
ATOM   1816  CB  LYS A 255     -32.291  26.754 -33.043  1.00 20.60           C  
ANISOU 1816  CB  LYS A 255     2701   2257   2868    100     99   -355       C  
ATOM   1817  CG  LYS A 255     -33.556  26.977 -32.238  1.00 20.79           C  
ANISOU 1817  CG  LYS A 255     2724   2267   2910    122    160   -388       C  
ATOM   1818  CD  LYS A 255     -33.253  27.936 -31.111  1.00 24.78           C  
ANISOU 1818  CD  LYS A 255     3277   2744   3394    108    189   -445       C  
ATOM   1819  CE  LYS A 255     -34.468  28.226 -30.273  1.00 27.69           C  
ANISOU 1819  CE  LYS A 255     3647   3096   3779    130    257   -484       C  
ATOM   1820  NZ  LYS A 255     -34.142  29.332 -29.341  1.00 26.35           N  
ANISOU 1820  NZ  LYS A 255     3527   2889   3595    118    284   -543       N  
ATOM   1821  N   HIS A 256     -30.184  25.190 -34.803  1.00 19.08           N  
ANISOU 1821  N   HIS A 256     2487   2128   2633     64     -7   -271       N  
ATOM   1822  CA  HIS A 256     -28.997  25.108 -35.644  1.00 18.81           C  
ANISOU 1822  CA  HIS A 256     2449   2104   2594     46    -51   -244       C  
ATOM   1823  C   HIS A 256     -29.355  24.668 -37.056  1.00 18.88           C  
ANISOU 1823  C   HIS A 256     2422   2117   2633     61    -69   -199       C  
ATOM   1824  O   HIS A 256     -29.005  25.338 -38.036  1.00 18.23           O  
ANISOU 1824  O   HIS A 256     2333   2014   2581     60    -88   -180       O  
ATOM   1825  CB  HIS A 256     -27.973  24.147 -35.040  1.00 17.72           C  
ANISOU 1825  CB  HIS A 256     2326   2009   2397     22    -73   -244       C  
ATOM   1826  CG  HIS A 256     -26.739  24.004 -35.871  1.00 19.20           C  
ANISOU 1826  CG  HIS A 256     2503   2209   2584      5   -114   -220       C  
ATOM   1827  ND1 HIS A 256     -25.587  24.720 -35.619  1.00 21.46           N  
ANISOU 1827  ND1 HIS A 256     2804   2488   2861    -21   -134   -236       N  
ATOM   1828  CD2 HIS A 256     -26.486  23.257 -36.970  1.00 18.15           C  
ANISOU 1828  CD2 HIS A 256     2344   2094   2457      9   -134   -181       C  
ATOM   1829  CE1 HIS A 256     -24.668  24.400 -36.513  1.00 19.36           C  
ANISOU 1829  CE1 HIS A 256     2519   2237   2600    -32   -163   -208       C  
ATOM   1830  NE2 HIS A 256     -25.189  23.516 -37.347  1.00 20.40           N  
ANISOU 1830  NE2 HIS A 256     2628   2384   2739    -13   -162   -176       N  
ATOM   1831  N   ILE A 257     -30.059  23.542 -37.182  1.00 17.56           N  
ANISOU 1831  N   ILE A 257     2237   1978   2458     72    -62   -181       N  
ATOM   1832  CA  ILE A 257     -30.376  23.010 -38.503  1.00 16.97           C  
ANISOU 1832  CA  ILE A 257     2131   1911   2404     82    -82   -141       C  
ATOM   1833  C   ILE A 257     -31.157  24.031 -39.325  1.00 17.54           C  
ANISOU 1833  C   ILE A 257     2186   1947   2532    103    -81   -129       C  
ATOM   1834  O   ILE A 257     -30.844  24.266 -40.498  1.00 16.04           O  
ANISOU 1834  O   ILE A 257     1987   1750   2359    101   -108    -99       O  
ATOM   1835  CB  ILE A 257     -31.122  21.670 -38.371  1.00 14.42           C  
ANISOU 1835  CB  ILE A 257     1794   1621   2065     88    -71   -130       C  
ATOM   1836  CG1 ILE A 257     -30.153  20.600 -37.834  1.00 12.23           C  
ANISOU 1836  CG1 ILE A 257     1535   1376   1734     68    -83   -129       C  
ATOM   1837  CG2 ILE A 257     -31.681  21.248 -39.701  1.00 13.34           C  
ANISOU 1837  CG2 ILE A 257     1627   1489   1954     98    -90    -94       C  
ATOM   1838  CD1 ILE A 257     -30.831  19.289 -37.377  1.00 16.84           C  
ANISOU 1838  CD1 ILE A 257     2116   1987   2296     70    -66   -124       C  
ATOM   1839  N   HIS A 258     -32.182  24.661 -38.726  1.00 19.09           N  
ANISOU 1839  N   HIS A 258     2376   2117   2759    124    -49   -151       N  
ATOM   1840  CA  HIS A 258     -32.953  25.673 -39.458  1.00 22.18           C  
ANISOU 1840  CA  HIS A 258     2748   2469   3211    149    -50   -138       C  
ATOM   1841  C   HIS A 258     -32.080  26.858 -39.865  1.00 18.58           C  
ANISOU 1841  C   HIS A 258     2315   1976   2770    140    -67   -136       C  
ATOM   1842  O   HIS A 258     -32.213  27.385 -40.970  1.00 18.39           O  
ANISOU 1842  O   HIS A 258     2279   1929   2778    150    -89   -104       O  
ATOM   1843  CB  HIS A 258     -34.136  26.169 -38.618  1.00 22.38           C  
ANISOU 1843  CB  HIS A 258     2763   2471   3271    176     -6   -168       C  
ATOM   1844  CG  HIS A 258     -35.175  25.123 -38.371  1.00 26.34           C  
ANISOU 1844  CG  HIS A 258     3234   3004   3771    186     13   -165       C  
ATOM   1845  ND1 HIS A 258     -35.948  24.593 -39.383  1.00 23.72           N  
ANISOU 1845  ND1 HIS A 258     2861   2686   3466    199     -7   -128       N  
ATOM   1846  CD2 HIS A 258     -35.568  24.506 -37.232  1.00 20.64           C  
ANISOU 1846  CD2 HIS A 258     2518   2303   3022    181     52   -193       C  
ATOM   1847  CE1 HIS A 258     -36.769  23.690 -38.877  1.00 23.34           C  
ANISOU 1847  CE1 HIS A 258     2792   2665   3413    201     18   -136       C  
ATOM   1848  NE2 HIS A 258     -36.560  23.619 -37.575  1.00 24.33           N  
ANISOU 1848  NE2 HIS A 258     2945   2794   3504    190     56   -173       N  
ATOM   1849  N   SER A 259     -31.185  27.291 -38.983  1.00 18.25           N  
ANISOU 1849  N   SER A 259     2307   1926   2702    118    -58   -170       N  
ATOM   1850  CA  SER A 259     -30.319  28.420 -39.302  1.00 22.08           C  
ANISOU 1850  CA  SER A 259     2814   2374   3202    103    -72   -172       C  
ATOM   1851  C   SER A 259     -29.350  28.114 -40.442  1.00 19.55           C  
ANISOU 1851  C   SER A 259     2489   2071   2867     82   -109   -133       C  
ATOM   1852  O   SER A 259     -28.810  29.048 -41.045  1.00 19.67           O  
ANISOU 1852  O   SER A 259     2516   2053   2904     71   -121   -121       O  
ATOM   1853  CB  SER A 259     -29.535  28.834 -38.057  1.00 20.24           C  
ANISOU 1853  CB  SER A 259     2616   2135   2939     78    -58   -219       C  
ATOM   1854  OG  SER A 259     -28.440  27.956 -37.859  1.00 20.84           O  
ANISOU 1854  OG  SER A 259     2699   2258   2963     48    -80   -217       O  
ATOM   1855  N   CYS A 260     -29.118  26.835 -40.753  1.00 19.05           N  
ANISOU 1855  N   CYS A 260     2411   2057   2769     74   -123   -114       N  
ATOM   1856  CA  CYS A 260     -28.107  26.452 -41.737  1.00 19.95           C  
ANISOU 1856  CA  CYS A 260     2523   2192   2865     53   -152    -83       C  
ATOM   1857  C   CYS A 260     -28.617  26.410 -43.170  1.00 19.24           C  
ANISOU 1857  C   CYS A 260     2417   2098   2797     65   -169    -39       C  
ATOM   1858  O   CYS A 260     -27.818  26.553 -44.103  1.00 17.69           O  
ANISOU 1858  O   CYS A 260     2225   1902   2594     46   -187    -14       O  
ATOM   1859  CB  CYS A 260     -27.524  25.073 -41.409  1.00 17.81           C  
ANISOU 1859  CB  CYS A 260     2247   1972   2547     40   -158    -85       C  
ATOM   1860  SG  CYS A 260     -26.312  25.043 -40.079  1.00 21.17           S  
ANISOU 1860  SG  CYS A 260     2695   2413   2934     13   -158   -123       S  
ATOM   1861  N   PHE A 261     -29.909  26.189 -43.388  1.00 17.93           N  
ANISOU 1861  N   PHE A 261     2229   1929   2653     93   -165    -28       N  
ATOM   1862  CA  PHE A 261     -30.391  25.913 -44.733  1.00 17.35           C  
ANISOU 1862  CA  PHE A 261     2141   1863   2590    101   -189     15       C  
ATOM   1863  C   PHE A 261     -31.571  26.798 -45.079  1.00 17.86           C  
ANISOU 1863  C   PHE A 261     2191   1889   2707    131   -191     30       C  
ATOM   1864  O   PHE A 261     -32.468  26.999 -44.259  1.00 17.70           O  
ANISOU 1864  O   PHE A 261     2156   1855   2713    155   -168      7       O  
ATOM   1865  CB  PHE A 261     -30.803  24.448 -44.888  1.00 16.34           C  
ANISOU 1865  CB  PHE A 261     1993   1780   2434    101   -193     23       C  
ATOM   1866  CG  PHE A 261     -29.666  23.491 -44.687  1.00 16.49           C  
ANISOU 1866  CG  PHE A 261     2023   1835   2406     76   -194     14       C  
ATOM   1867  CD1 PHE A 261     -28.856  23.124 -45.751  1.00 16.58           C  
ANISOU 1867  CD1 PHE A 261     2040   1862   2396     58   -213     39       C  
ATOM   1868  CD2 PHE A 261     -29.396  22.986 -43.433  1.00 15.32           C  
ANISOU 1868  CD2 PHE A 261     1882   1702   2236     72   -176    -17       C  
ATOM   1869  CE1 PHE A 261     -27.797  22.241 -45.558  1.00 15.71           C  
ANISOU 1869  CE1 PHE A 261     1936   1783   2251     39   -212     30       C  
ATOM   1870  CE2 PHE A 261     -28.334  22.115 -43.232  1.00 17.68           C  
ANISOU 1870  CE2 PHE A 261     2188   2032   2496     53   -181    -22       C  
ATOM   1871  CZ  PHE A 261     -27.545  21.747 -44.286  1.00 13.94           C  
ANISOU 1871  CZ  PHE A 261     1714   1572   2009     39   -198      1       C  
ATOM   1872  N   THR A 262     -31.577  27.289 -46.316  1.00 17.49           N  
ANISOU 1872  N   THR A 262     2146   1826   2674    132   -217     71       N  
ATOM   1873  CA  THR A 262     -32.686  28.098 -46.784  1.00 19.23           C  
ANISOU 1873  CA  THR A 262     2351   2010   2946    164   -228     94       C  
ATOM   1874  C   THR A 262     -33.898  27.257 -47.160  1.00 20.89           C  
ANISOU 1874  C   THR A 262     2524   2249   3166    184   -242    110       C  
ATOM   1875  O   THR A 262     -35.017  27.774 -47.148  1.00 21.91           O  
ANISOU 1875  O   THR A 262     2626   2353   3344    217   -243    117       O  
ATOM   1876  CB  THR A 262     -32.237  28.965 -47.963  1.00 21.00           C  
ANISOU 1876  CB  THR A 262     2597   2205   3178    156   -255    135       C  
ATOM   1877  OG1 THR A 262     -31.920  28.128 -49.076  1.00 26.44           O  
ANISOU 1877  OG1 THR A 262     3287   2932   3826    135   -282    168       O  
ATOM   1878  CG2 THR A 262     -30.989  29.749 -47.582  1.00 18.73           C  
ANISOU 1878  CG2 THR A 262     2344   1891   2883    129   -240    117       C  
ATOM   1879  N   ASN A 263     -33.718  25.972 -47.461  1.00 19.68           N  
ANISOU 1879  N   ASN A 263     2364   2144   2968    165   -251    114       N  
ATOM   1880  CA AASN A 263     -34.839  25.095 -47.786  0.49 20.78           C  
ANISOU 1880  CA AASN A 263     2468   2312   3115    177   -264    127       C  
ATOM   1881  CA BASN A 263     -34.849  25.102 -47.757  0.51 20.72           C  
ANISOU 1881  CA BASN A 263     2461   2304   3108    177   -263    126       C  
ATOM   1882  C   ASN A 263     -34.541  23.711 -47.239  1.00 20.78           C  
ANISOU 1882  C   ASN A 263     2468   2357   3072    156   -248    103       C  
ATOM   1883  O   ASN A 263     -33.502  23.134 -47.573  1.00 21.08           O  
ANISOU 1883  O   ASN A 263     2529   2415   3064    130   -253    106       O  
ATOM   1884  CB AASN A 263     -35.082  25.031 -49.298  0.49 21.24           C  
ANISOU 1884  CB AASN A 263     2524   2378   3167    172   -309    174       C  
ATOM   1885  CB BASN A 263     -35.156  25.049 -49.254  0.51 21.24           C  
ANISOU 1885  CB BASN A 263     2523   2378   3171    174   -309    174       C  
ATOM   1886  CG AASN A 263     -35.616  26.341 -49.867  0.49 22.51           C  
ANISOU 1886  CG AASN A 263     2681   2494   3376    198   -331    206       C  
ATOM   1887  CG BASN A 263     -36.552  24.515 -49.538  0.51 24.00           C  
ANISOU 1887  CG BASN A 263     2827   2745   3546    192   -327    186       C  
ATOM   1888  OD1AASN A 263     -36.649  26.858 -49.423  0.49 24.75           O  
ANISOU 1888  OD1AASN A 263     2934   2754   3714    232   -325    201       O  
ATOM   1889  OD1BASN A 263     -37.514  25.278 -49.647  0.51 27.15           O  
ANISOU 1889  OD1BASN A 263     3200   3118   3999    223   -339    201       O  
ATOM   1890  ND2AASN A 263     -34.910  26.884 -50.851  0.49 22.99           N  
ANISOU 1890  ND2AASN A 263     2774   2541   3419    182   -355    239       N  
ATOM   1891  ND2BASN A 263     -36.668  23.203 -49.653  0.51 23.41           N  
ANISOU 1891  ND2BASN A 263     2744   2713   3439    173   -330    180       N  
ATOM   1892  N   ILE A 264     -35.449  23.185 -46.418  1.00 17.26           N  
ANISOU 1892  N   ILE A 264     1995   1922   2641    169   -226     82       N  
ATOM   1893  CA  ILE A 264     -35.324  21.853 -45.838  1.00 16.98           C  
ANISOU 1893  CA  ILE A 264     1959   1923   2568    152   -209     63       C  
ATOM   1894  C   ILE A 264     -36.601  21.099 -46.169  1.00 19.80           C  
ANISOU 1894  C   ILE A 264     2277   2301   2945    159   -218     74       C  
ATOM   1895  O   ILE A 264     -37.701  21.555 -45.828  1.00 20.34           O  
ANISOU 1895  O   ILE A 264     2312   2356   3062    183   -207     70       O  
ATOM   1896  CB  ILE A 264     -35.103  21.898 -44.315  1.00 18.42           C  
ANISOU 1896  CB  ILE A 264     2153   2102   2744    154   -167     22       C  
ATOM   1897  CG1 ILE A 264     -33.840  22.692 -43.982  1.00 18.44           C  
ANISOU 1897  CG1 ILE A 264     2192   2085   2730    143   -163      9       C  
ATOM   1898  CG2 ILE A 264     -35.002  20.472 -43.735  1.00 16.08           C  
ANISOU 1898  CG2 ILE A 264     1860   1842   2408    136   -152      9       C  
ATOM   1899  CD1 ILE A 264     -33.702  23.054 -42.515  1.00 18.36           C  
ANISOU 1899  CD1 ILE A 264     2197   2063   2715    146   -126    -32       C  
ATOM   1900  N   SER A 265     -36.461  19.957 -46.830  1.00 17.02           N  
ANISOU 1900  N   SER A 265     1927   1979   2559    137   -236     87       N  
ATOM   1901  CA ASER A 265     -37.604  19.131 -47.183  0.50 17.13           C  
ANISOU 1901  CA ASER A 265     1906   2015   2588    135   -248     96       C  
ATOM   1902  CA BSER A 265     -37.572  19.123 -47.255  0.50 16.46           C  
ANISOU 1902  CA BSER A 265     1822   1931   2502    134   -250     97       C  
ATOM   1903  C   SER A 265     -37.277  17.678 -46.865  1.00 17.95           C  
ANISOU 1903  C   SER A 265     2023   2148   2650    109   -234     82       C  
ATOM   1904  O   SER A 265     -36.187  17.355 -46.374  1.00 14.13           O  
ANISOU 1904  O   SER A 265     1573   1667   2129     98   -218     68       O  
ATOM   1905  CB ASER A 265     -37.987  19.314 -48.657  0.50 19.47           C  
ANISOU 1905  CB ASER A 265     2191   2314   2891    133   -298    132       C  
ATOM   1906  CB BSER A 265     -37.804  19.257 -48.766  0.50 19.43           C  
ANISOU 1906  CB BSER A 265     2192   2311   2878    129   -300    134       C  
ATOM   1907  OG ASER A 265     -36.928  18.927 -49.503  0.50 19.61           O  
ANISOU 1907  OG ASER A 265     2248   2344   2860    109   -317    144       O  
ATOM   1908  OG BSER A 265     -37.825  20.621 -49.153  0.50 20.85           O  
ANISOU 1908  OG BSER A 265     2373   2460   3089    151   -317    153       O  
ATOM   1909  N   CYS A 266     -38.240  16.797 -47.117  1.00 15.09           N  
ANISOU 1909  N   CYS A 266     1632   1804   2296    100   -241     86       N  
ATOM   1910  CA  CYS A 266     -38.097  15.407 -46.689  1.00 15.60           C  
ANISOU 1910  CA  CYS A 266     1708   1890   2329     77   -223     72       C  
ATOM   1911  C   CYS A 266     -38.919  14.497 -47.581  1.00 14.89           C  
ANISOU 1911  C   CYS A 266     1595   1819   2242     58   -249     86       C  
ATOM   1912  O   CYS A 266     -40.080  14.795 -47.882  1.00 18.13           O  
ANISOU 1912  O   CYS A 266     1962   2231   2694     66   -265     95       O  
ATOM   1913  CB  CYS A 266     -38.532  15.231 -45.233  1.00 14.94           C  
ANISOU 1913  CB  CYS A 266     1615   1805   2257     83   -175     47       C  
ATOM   1914  SG  CYS A 266     -38.658  13.534 -44.652  1.00 14.86           S  
ANISOU 1914  SG  CYS A 266     1614   1815   2218     56   -151     36       S  
ATOM   1915  N   PHE A 267     -38.319  13.386 -47.987  1.00 14.98           N  
ANISOU 1915  N   PHE A 267     1635   1844   2213     33   -255     84       N  
ATOM   1916  CA  PHE A 267     -38.971  12.414 -48.850  1.00 13.48           C  
ANISOU 1916  CA  PHE A 267     1434   1671   2018      8   -280     92       C  
ATOM   1917  C   PHE A 267     -38.908  11.055 -48.172  1.00 14.84           C  
ANISOU 1917  C   PHE A 267     1619   1850   2170    -12   -250     74       C  
ATOM   1918  O   PHE A 267     -37.832  10.624 -47.741  1.00 13.61           O  
ANISOU 1918  O   PHE A 267     1502   1689   1981    -14   -231     65       O  
ATOM   1919  CB  PHE A 267     -38.296  12.371 -50.220  1.00 14.91           C  
ANISOU 1919  CB  PHE A 267     1644   1858   2165     -5   -317    108       C  
ATOM   1920  CG  PHE A 267     -39.122  11.710 -51.278  1.00 17.25           C  
ANISOU 1920  CG  PHE A 267     1925   2170   2459    -29   -354    117       C  
ATOM   1921  CD1 PHE A 267     -39.148  10.322 -51.395  1.00 15.07           C  
ANISOU 1921  CD1 PHE A 267     1663   1904   2159    -59   -347    104       C  
ATOM   1922  CD2 PHE A 267     -39.864  12.478 -52.174  1.00 16.74           C  
ANISOU 1922  CD2 PHE A 267     1835   2111   2416    -24   -398    141       C  
ATOM   1923  CE1 PHE A 267     -39.902   9.709 -52.387  1.00 17.02           C  
ANISOU 1923  CE1 PHE A 267     1900   2166   2402    -86   -384    109       C  
ATOM   1924  CE2 PHE A 267     -40.634  11.872 -53.162  1.00 17.94           C  
ANISOU 1924  CE2 PHE A 267     1974   2281   2563    -50   -439    150       C  
ATOM   1925  CZ  PHE A 267     -40.644  10.482 -53.273  1.00 17.17           C  
ANISOU 1925  CZ  PHE A 267     1891   2194   2438    -83   -431    132       C  
ATOM   1926  N   LEU A 268     -40.053  10.389 -48.050  1.00 13.91           N  
ANISOU 1926  N   LEU A 268     1469   1741   2076    -27   -247     71       N  
ATOM   1927  CA  LEU A 268     -40.098   9.071 -47.429  1.00 15.58           C  
ANISOU 1927  CA  LEU A 268     1694   1954   2272    -50   -218     58       C  
ATOM   1928  C   LEU A 268     -40.127   8.018 -48.534  1.00 14.44           C  
ANISOU 1928  C   LEU A 268     1564   1817   2105    -82   -247     60       C  
ATOM   1929  O   LEU A 268     -41.055   7.985 -49.345  1.00 13.82           O  
ANISOU 1929  O   LEU A 268     1454   1751   2047    -97   -279     68       O  
ATOM   1930  CB  LEU A 268     -41.302   8.942 -46.499  1.00 14.88           C  
ANISOU 1930  CB  LEU A 268     1564   1869   2222    -53   -188     50       C  
ATOM   1931  CG  LEU A 268     -41.416  10.050 -45.455  1.00 16.80           C  
ANISOU 1931  CG  LEU A 268     1791   2104   2489    -22   -156     43       C  
ATOM   1932  CD1 LEU A 268     -42.648   9.821 -44.562  1.00 12.28           C  
ANISOU 1932  CD1 LEU A 268     1176   1536   1954    -27   -118     33       C  
ATOM   1933  CD2 LEU A 268     -40.119  10.157 -44.597  1.00 14.71           C  
ANISOU 1933  CD2 LEU A 268     1577   1828   2183    -10   -131     34       C  
ATOM   1934  N   LEU A 269     -39.093   7.193 -48.588  1.00 13.60           N  
ANISOU 1934  N   LEU A 269     1505   1704   1959    -92   -237     54       N  
ATOM   1935  CA  LEU A 269     -38.954   6.236 -49.673  1.00 15.46           C  
ANISOU 1935  CA  LEU A 269     1763   1942   2169   -120   -260     51       C  
ATOM   1936  C   LEU A 269     -39.211   4.822 -49.168  1.00 15.54           C  
ANISOU 1936  C   LEU A 269     1786   1943   2175   -145   -234     39       C  
ATOM   1937  O   LEU A 269     -38.674   4.444 -48.116  1.00 15.56           O  
ANISOU 1937  O   LEU A 269     1809   1933   2169   -135   -199     34       O  
ATOM   1938  CB  LEU A 269     -37.549   6.336 -50.277  1.00 16.94           C  
ANISOU 1938  CB  LEU A 269     1995   2124   2317   -111   -265     51       C  
ATOM   1939  CG  LEU A 269     -37.301   5.647 -51.623  1.00 16.36           C  
ANISOU 1939  CG  LEU A 269     1949   2055   2213   -137   -290     48       C  
ATOM   1940  CD1 LEU A 269     -38.213   6.253 -52.710  1.00 17.08           C  
ANISOU 1940  CD1 LEU A 269     2014   2163   2313   -149   -337     61       C  
ATOM   1941  CD2 LEU A 269     -35.845   5.818 -51.990  1.00 16.03           C  
ANISOU 1941  CD2 LEU A 269     1946   2007   2137   -123   -283     46       C  
ATOM   1942  N   PRO A 270     -40.021   4.017 -49.857  1.00 15.64           N  
ANISOU 1942  N   PRO A 270     1789   1961   2194   -180   -253     34       N  
ATOM   1943  CA  PRO A 270     -40.243   2.643 -49.401  1.00 16.97           C  
ANISOU 1943  CA  PRO A 270     1974   2115   2359   -207   -227     23       C  
ATOM   1944  C   PRO A 270     -38.972   1.820 -49.514  1.00 13.96           C  
ANISOU 1944  C   PRO A 270     1651   1713   1939   -205   -212     15       C  
ATOM   1945  O   PRO A 270     -38.042   2.156 -50.244  1.00 14.28           O  
ANISOU 1945  O   PRO A 270     1717   1755   1954   -192   -227     14       O  
ATOM   1946  CB  PRO A 270     -41.318   2.100 -50.353  1.00 16.23           C  
ANISOU 1946  CB  PRO A 270     1857   2031   2278   -248   -259     18       C  
ATOM   1947  CG  PRO A 270     -41.833   3.300 -51.130  1.00 16.81           C  
ANISOU 1947  CG  PRO A 270     1892   2129   2367   -236   -303     31       C  
ATOM   1948  CD  PRO A 270     -40.680   4.274 -51.148  1.00 16.50           C  
ANISOU 1948  CD  PRO A 270     1878   2086   2306   -198   -301     40       C  
ATOM   1949  N   HIS A 271     -38.966   0.713 -48.787  1.00 15.97           N  
ANISOU 1949  N   HIS A 271     1927   1947   2193   -218   -181      9       N  
ATOM   1950  CA  HIS A 271     -37.929  -0.291 -48.951  1.00 13.96           C  
ANISOU 1950  CA  HIS A 271     1725   1669   1911   -219   -169      1       C  
ATOM   1951  C   HIS A 271     -37.934  -0.806 -50.391  1.00 17.00           C  
ANISOU 1951  C   HIS A 271     2128   2052   2278   -245   -196    -14       C  
ATOM   1952  O   HIS A 271     -39.004  -0.948 -50.996  1.00 15.24           O  
ANISOU 1952  O   HIS A 271     1882   1841   2069   -279   -219    -19       O  
ATOM   1953  CB  HIS A 271     -38.181  -1.432 -47.972  1.00 14.47           C  
ANISOU 1953  CB  HIS A 271     1807   1708   1983   -233   -134      1       C  
ATOM   1954  CG  HIS A 271     -37.015  -2.343 -47.773  1.00 14.90           C  
ANISOU 1954  CG  HIS A 271     1914   1733   2015   -220   -115     -1       C  
ATOM   1955  ND1 HIS A 271     -36.593  -3.240 -48.732  1.00 17.24           N  
ANISOU 1955  ND1 HIS A 271     2243   2009   2297   -235   -122    -17       N  
ATOM   1956  CD2 HIS A 271     -36.213  -2.534 -46.698  1.00 16.48           C  
ANISOU 1956  CD2 HIS A 271     2137   1918   2207   -193    -91     10       C  
ATOM   1957  CE1 HIS A 271     -35.566  -3.925 -48.266  1.00 18.12           C  
ANISOU 1957  CE1 HIS A 271     2394   2093   2399   -214   -100    -14       C  
ATOM   1958  NE2 HIS A 271     -35.324  -3.525 -47.030  1.00 16.56           N  
ANISOU 1958  NE2 HIS A 271     2189   1899   2203   -189    -84      4       N  
ATOM   1959  N   PRO A 272     -36.763  -1.063 -50.978  1.00 15.16           N  
ANISOU 1959  N   PRO A 272     1936   1809   2017   -233   -194    -22       N  
ATOM   1960  CA  PRO A 272     -36.697  -1.545 -52.365  1.00 15.38           C  
ANISOU 1960  CA  PRO A 272     1987   1835   2020   -259   -215    -39       C  
ATOM   1961  C   PRO A 272     -36.982  -3.030 -52.543  1.00 16.65           C  
ANISOU 1961  C   PRO A 272     2180   1967   2181   -293   -202    -59       C  
ATOM   1962  O   PRO A 272     -36.971  -3.506 -53.683  1.00 17.26           O  
ANISOU 1962  O   PRO A 272     2281   2041   2235   -319   -217    -79       O  
ATOM   1963  CB  PRO A 272     -35.247  -1.225 -52.761  1.00 14.50           C  
ANISOU 1963  CB  PRO A 272     1906   1722   1883   -228   -207    -42       C  
ATOM   1964  CG  PRO A 272     -34.493  -1.242 -51.478  1.00 16.85           C  
ANISOU 1964  CG  PRO A 272     2206   2004   2191   -193   -176    -31       C  
ATOM   1965  CD  PRO A 272     -35.436  -0.686 -50.451  1.00 14.12           C  
ANISOU 1965  CD  PRO A 272     1822   1671   1872   -192   -176    -15       C  
ATOM   1966  N   GLY A 273     -37.232  -3.766 -51.474  1.00 15.35           N  
ANISOU 1966  N   GLY A 273     2018   1779   2037   -296   -174    -55       N  
ATOM   1967  CA  GLY A 273     -37.386  -5.200 -51.539  1.00 16.03           C  
ANISOU 1967  CA  GLY A 273     2139   1829   2124   -326   -156    -71       C  
ATOM   1968  C   GLY A 273     -36.150  -5.906 -51.011  1.00 17.96           C  
ANISOU 1968  C   GLY A 273     2427   2036   2360   -294   -123    -70       C  
ATOM   1969  O   GLY A 273     -35.029  -5.384 -51.064  1.00 15.20           O  
ANISOU 1969  O   GLY A 273     2086   1693   1997   -255   -119    -66       O  
ATOM   1970  N   LEU A 274     -36.360  -7.107 -50.471  1.00 17.49           N  
ANISOU 1970  N   LEU A 274     2394   1937   2313   -312    -98    -73       N  
ATOM   1971  CA  LEU A 274     -35.271  -7.855 -49.844  1.00 20.73           C  
ANISOU 1971  CA  LEU A 274     2845   2309   2723   -279    -68    -66       C  
ATOM   1972  C   LEU A 274     -34.228  -8.306 -50.854  1.00 18.90           C  
ANISOU 1972  C   LEU A 274     2651   2058   2474   -266    -65    -90       C  
ATOM   1973  O   LEU A 274     -33.058  -8.466 -50.497  1.00 23.60           O  
ANISOU 1973  O   LEU A 274     3265   2635   3068   -223    -48    -83       O  
ATOM   1974  CB  LEU A 274     -35.823  -9.067 -49.087  1.00 19.67           C  
ANISOU 1974  CB  LEU A 274     2734   2132   2607   -304    -44    -60       C  
ATOM   1975  CG  LEU A 274     -36.648  -8.686 -47.856  1.00 24.28           C  
ANISOU 1975  CG  LEU A 274     3286   2732   3206   -311    -34    -34       C  
ATOM   1976  CD1 LEU A 274     -37.224  -9.913 -47.174  1.00 28.31           C  
ANISOU 1976  CD1 LEU A 274     3824   3200   3733   -342     -7    -27       C  
ATOM   1977  CD2 LEU A 274     -35.793  -7.868 -46.880  1.00 23.61           C  
ANISOU 1977  CD2 LEU A 274     3194   2665   3113   -260    -28     -9       C  
ATOM   1978  N   LYS A 275     -34.620  -8.524 -52.110  1.00 21.37           N  
ANISOU 1978  N   LYS A 275     2974   2374   2772   -301    -80   -118       N  
ATOM   1979  CA  LYS A 275     -33.626  -8.874 -53.122  1.00 21.36           C  
ANISOU 1979  CA  LYS A 275     3009   2356   2750   -289    -72   -145       C  
ATOM   1980  C   LYS A 275     -32.611  -7.748 -53.309  1.00 22.90           C  
ANISOU 1980  C   LYS A 275     3187   2585   2930   -246    -76   -135       C  
ATOM   1981  O   LYS A 275     -31.400  -7.998 -53.359  1.00 19.19           O  
ANISOU 1981  O   LYS A 275     2737   2096   2458   -211    -54   -140       O  
ATOM   1982  CB  LYS A 275     -34.318  -9.212 -54.440  1.00 25.58           C  
ANISOU 1982  CB  LYS A 275     3561   2895   3264   -340    -91   -178       C  
ATOM   1983  CG  LYS A 275     -33.368  -9.688 -55.507  1.00 28.15           C  
ANISOU 1983  CG  LYS A 275     3931   3200   3563   -334    -74   -211       C  
ATOM   1984  CD  LYS A 275     -34.111 -10.155 -56.762  1.00 36.61           C  
ANISOU 1984  CD  LYS A 275     5029   4272   4609   -392    -93   -247       C  
ATOM   1985  CE  LYS A 275     -34.915 -11.429 -56.534  1.00 34.88           C  
ANISOU 1985  CE  LYS A 275     4834   4008   4411   -434    -84   -264       C  
ATOM   1986  NZ  LYS A 275     -35.113 -12.161 -57.835  1.00 41.49           N  
ANISOU 1986  NZ  LYS A 275     5718   4829   5218   -481    -89   -311       N  
ATOM   1987  N   VAL A 276     -33.084  -6.499 -53.393  1.00 17.62           N  
ANISOU 1987  N   VAL A 276     2478   1963   2255   -249   -105   -120       N  
ATOM   1988  CA  VAL A 276     -32.170  -5.361 -53.476  1.00 16.29           C  
ANISOU 1988  CA  VAL A 276     2291   1823   2074   -212   -109   -108       C  
ATOM   1989  C   VAL A 276     -31.224  -5.356 -52.282  1.00 15.11           C  
ANISOU 1989  C   VAL A 276     2138   1661   1944   -166    -87    -88       C  
ATOM   1990  O   VAL A 276     -30.019  -5.135 -52.426  1.00 16.50           O  
ANISOU 1990  O   VAL A 276     2319   1837   2114   -133    -75    -90       O  
ATOM   1991  CB  VAL A 276     -32.967  -4.041 -53.577  1.00 14.48           C  
ANISOU 1991  CB  VAL A 276     2019   1638   1843   -222   -143    -92       C  
ATOM   1992  CG1 VAL A 276     -32.049  -2.825 -53.375  1.00 12.33           C  
ANISOU 1992  CG1 VAL A 276     1727   1391   1567   -184   -144    -75       C  
ATOM   1993  CG2 VAL A 276     -33.675  -3.961 -54.932  1.00 16.16           C  
ANISOU 1993  CG2 VAL A 276     2238   1869   2032   -263   -172   -109       C  
ATOM   1994  N   ALA A 277     -31.748  -5.650 -51.094  1.00 17.60           N  
ANISOU 1994  N   ALA A 277     2445   1964   2279   -165    -81    -70       N  
ATOM   1995  CA  ALA A 277     -30.960  -5.574 -49.867  1.00 19.75           C  
ANISOU 1995  CA  ALA A 277     2714   2228   2563   -125    -68    -47       C  
ATOM   1996  C   ALA A 277     -30.011  -6.758 -49.707  1.00 17.15           C  
ANISOU 1996  C   ALA A 277     2422   1855   2241   -102    -43    -51       C  
ATOM   1997  O   ALA A 277     -28.907  -6.602 -49.174  1.00 18.90           O  
ANISOU 1997  O   ALA A 277     2640   2074   2468    -60    -37    -38       O  
ATOM   1998  CB  ALA A 277     -31.900  -5.490 -48.660  1.00 16.63           C  
ANISOU 1998  CB  ALA A 277     2302   1836   2179   -136    -68    -25       C  
ATOM   1999  N   THR A 278     -30.411  -7.956 -50.133  1.00 16.09           N  
ANISOU 1999  N   THR A 278     2320   1681   2111   -127    -30    -69       N  
ATOM   2000  CA  THR A 278     -29.703  -9.148 -49.676  1.00 17.02           C  
ANISOU 2000  CA  THR A 278     2473   1748   2245   -103     -6    -66       C  
ATOM   2001  C   THR A 278     -29.174 -10.069 -50.759  1.00 17.31           C  
ANISOU 2001  C   THR A 278     2546   1749   2282   -105     13    -99       C  
ATOM   2002  O   THR A 278     -28.400 -10.971 -50.430  1.00 16.79           O  
ANISOU 2002  O   THR A 278     2507   1639   2235    -75     34    -96       O  
ATOM   2003  CB  THR A 278     -30.596 -10.005 -48.762  1.00 18.82           C  
ANISOU 2003  CB  THR A 278     2719   1944   2487   -127      3    -49       C  
ATOM   2004  OG1 THR A 278     -31.623 -10.615 -49.553  1.00 19.74           O  
ANISOU 2004  OG1 THR A 278     2851   2046   2603   -179      3    -75       O  
ATOM   2005  CG2 THR A 278     -31.221  -9.169 -47.639  1.00 16.30           C  
ANISOU 2005  CG2 THR A 278     2368   1659   2167   -129     -9    -19       C  
ATOM   2006  N   ASN A 279     -29.583  -9.924 -52.011  1.00 16.46           N  
ANISOU 2006  N   ASN A 279     2444   1656   2154   -139      7   -131       N  
ATOM   2007  CA  ASN A 279     -29.188 -10.897 -53.016  1.00 19.27           C  
ANISOU 2007  CA  ASN A 279     2842   1973   2506   -146     30   -168       C  
ATOM   2008  C   ASN A 279     -27.845 -10.485 -53.601  1.00 18.52           C  
ANISOU 2008  C   ASN A 279     2742   1889   2404   -106     45   -179       C  
ATOM   2009  O   ASN A 279     -27.741  -9.390 -54.171  1.00 18.21           O  
ANISOU 2009  O   ASN A 279     2679   1899   2342   -110     30   -181       O  
ATOM   2010  CB  ASN A 279     -30.242 -11.005 -54.109  1.00 16.37           C  
ANISOU 2010  CB  ASN A 279     2489   1616   2115   -206     15   -198       C  
ATOM   2011  CG  ASN A 279     -29.972 -12.161 -55.074  1.00 25.13           C  
ANISOU 2011  CG  ASN A 279     3651   2679   3219   -222     41   -242       C  
ATOM   2012  OD1 ASN A 279     -28.897 -12.256 -55.670  1.00 22.11           O  
ANISOU 2012  OD1 ASN A 279     3284   2286   2829   -193     66   -262       O  
ATOM   2013  ND2 ASN A 279     -30.953 -13.047 -55.222  1.00 25.07           N  
ANISOU 2013  ND2 ASN A 279     3671   2640   3215   -270     39   -259       N  
ATOM   2014  N   PRO A 280     -26.800 -11.305 -53.479  1.00 18.75           N  
ANISOU 2014  N   PRO A 280     2792   1876   2455    -67     75   -186       N  
ATOM   2015  CA  PRO A 280     -25.476 -10.877 -53.959  1.00 19.66           C  
ANISOU 2015  CA  PRO A 280     2894   2005   2570    -26     93   -196       C  
ATOM   2016  C   PRO A 280     -25.380 -10.770 -55.474  1.00 20.19           C  
ANISOU 2016  C   PRO A 280     2982   2085   2605    -52    108   -238       C  
ATOM   2017  O   PRO A 280     -24.424 -10.165 -55.977  1.00 20.44           O  
ANISOU 2017  O   PRO A 280     2996   2141   2629    -28    122   -245       O  
ATOM   2018  CB  PRO A 280     -24.546 -11.974 -53.426  1.00 19.39           C  
ANISOU 2018  CB  PRO A 280     2877   1914   2575     21    122   -193       C  
ATOM   2019  CG  PRO A 280     -25.406 -13.188 -53.453  1.00 19.22           C  
ANISOU 2019  CG  PRO A 280     2903   1840   2561    -11    132   -207       C  
ATOM   2020  CD  PRO A 280     -26.794 -12.707 -53.033  1.00 18.06           C  
ANISOU 2020  CD  PRO A 280     2744   1722   2396    -60     98   -188       C  
ATOM   2021  N   ASN A 281     -26.327 -11.327 -56.216  1.00 19.33           N  
ANISOU 2021  N   ASN A 281     2909   1962   2475   -102    105   -267       N  
ATOM   2022  CA  ASN A 281     -26.300 -11.202 -57.666  1.00 21.40           C  
ANISOU 2022  CA  ASN A 281     3196   2239   2697   -133    115   -307       C  
ATOM   2023  C   ASN A 281     -27.100 -10.020 -58.178  1.00 22.24           C  
ANISOU 2023  C   ASN A 281     3281   2406   2764   -171     75   -298       C  
ATOM   2024  O   ASN A 281     -27.045  -9.724 -59.382  1.00 21.12           O  
ANISOU 2024  O   ASN A 281     3158   2285   2580   -197     77   -324       O  
ATOM   2025  CB  ASN A 281     -26.815 -12.492 -58.295  1.00 23.35           C  
ANISOU 2025  CB  ASN A 281     3499   2435   2937   -169    133   -349       C  
ATOM   2026  CG  ASN A 281     -26.050 -13.694 -57.811  1.00 28.39           C  
ANISOU 2026  CG  ASN A 281     4162   3006   3618   -128    174   -358       C  
ATOM   2027  OD1 ASN A 281     -24.820 -13.699 -57.829  1.00 28.77           O  
ANISOU 2027  OD1 ASN A 281     4202   3046   3685    -78    205   -361       O  
ATOM   2028  ND2 ASN A 281     -26.767 -14.701 -57.326  1.00 31.37           N  
ANISOU 2028  ND2 ASN A 281     4567   3334   4018   -149    173   -358       N  
ATOM   2029  N   PHE A 282     -27.848  -9.350 -57.305  1.00 17.32           N  
ANISOU 2029  N   PHE A 282     2619   1808   2152   -176     39   -260       N  
ATOM   2030  CA  PHE A 282     -28.595  -8.173 -57.717  1.00 18.86           C  
ANISOU 2030  CA  PHE A 282     2789   2058   2319   -206     -1   -247       C  
ATOM   2031  C   PHE A 282     -27.655  -7.155 -58.353  1.00 16.77           C  
ANISOU 2031  C   PHE A 282     2513   1829   2031   -185      6   -245       C  
ATOM   2032  O   PHE A 282     -26.612  -6.828 -57.788  1.00 18.67           O  
ANISOU 2032  O   PHE A 282     2731   2070   2292   -140     25   -230       O  
ATOM   2033  CB  PHE A 282     -29.297  -7.566 -56.501  1.00 16.34           C  
ANISOU 2033  CB  PHE A 282     2427   1757   2025   -199    -30   -207       C  
ATOM   2034  CG  PHE A 282     -29.955  -6.257 -56.785  1.00 17.96           C  
ANISOU 2034  CG  PHE A 282     2599   2014   2211   -217    -68   -188       C  
ATOM   2035  CD1 PHE A 282     -31.058  -6.196 -57.627  1.00 16.18           C  
ANISOU 2035  CD1 PHE A 282     2381   1806   1962   -267    -99   -200       C  
ATOM   2036  CD2 PHE A 282     -29.473  -5.086 -56.219  1.00 17.07           C  
ANISOU 2036  CD2 PHE A 282     2448   1930   2106   -185    -76   -159       C  
ATOM   2037  CE1 PHE A 282     -31.669  -4.977 -57.904  1.00 17.53           C  
ANISOU 2037  CE1 PHE A 282     2519   2021   2119   -279   -138   -180       C  
ATOM   2038  CE2 PHE A 282     -30.072  -3.873 -56.483  1.00 14.71           C  
ANISOU 2038  CE2 PHE A 282     2121   1673   1794   -198   -110   -141       C  
ATOM   2039  CZ  PHE A 282     -31.177  -3.814 -57.325  1.00 16.15           C  
ANISOU 2039  CZ  PHE A 282     2309   1872   1956   -243   -142   -150       C  
ATOM   2040  N   ASP A 283     -28.005  -6.667 -59.545  1.00 17.29           N  
ANISOU 2040  N   ASP A 283     2593   1924   2051   -221    -10   -260       N  
ATOM   2041  CA  ASP A 283     -27.154  -5.661 -60.169  1.00 17.68           C  
ANISOU 2041  CA  ASP A 283     2634   2007   2076   -207     -2   -255       C  
ATOM   2042  C   ASP A 283     -27.955  -4.451 -60.637  1.00 17.30           C  
ANISOU 2042  C   ASP A 283     2569   2006   1998   -236    -49   -233       C  
ATOM   2043  O   ASP A 283     -27.551  -3.760 -61.574  1.00 19.11           O  
ANISOU 2043  O   ASP A 283     2809   2262   2190   -245    -47   -235       O  
ATOM   2044  CB  ASP A 283     -26.314  -6.247 -61.311  1.00 18.47           C  
ANISOU 2044  CB  ASP A 283     2779   2093   2146   -212     42   -297       C  
ATOM   2045  CG  ASP A 283     -27.147  -6.786 -62.470  1.00 27.30           C  
ANISOU 2045  CG  ASP A 283     3947   3210   3217   -268     29   -331       C  
ATOM   2046  OD1 ASP A 283     -28.401  -6.766 -62.420  1.00 23.53           O  
ANISOU 2046  OD1 ASP A 283     3466   2742   2734   -305    -17   -322       O  
ATOM   2047  OD2 ASP A 283     -26.519  -7.236 -63.456  1.00 31.05           O  
ANISOU 2047  OD2 ASP A 283     4464   3674   3659   -276     66   -369       O  
ATOM   2048  N   GLY A 284     -29.055  -4.143 -59.957  1.00 16.01           N  
ANISOU 2048  N   GLY A 284     2376   1853   1855   -248    -88   -208       N  
ATOM   2049  CA  GLY A 284     -29.750  -2.888 -60.181  1.00 14.25           C  
ANISOU 2049  CA  GLY A 284     2126   1671   1617   -262   -133   -180       C  
ATOM   2050  C   GLY A 284     -30.885  -2.927 -61.178  1.00 17.66           C  
ANISOU 2050  C   GLY A 284     2576   2120   2014   -313   -173   -189       C  
ATOM   2051  O   GLY A 284     -31.429  -1.863 -61.512  1.00 17.57           O  
ANISOU 2051  O   GLY A 284     2543   2143   1989   -324   -213   -164       O  
ATOM   2052  N   LYS A 285     -31.239  -4.100 -61.696  1.00 15.64           N  
ANISOU 2052  N   LYS A 285     2358   1841   1742   -346   -167   -224       N  
ATOM   2053  CA  LYS A 285     -32.334  -4.187 -62.654  1.00 18.64           C  
ANISOU 2053  CA  LYS A 285     2755   2240   2087   -400   -211   -235       C  
ATOM   2054  C   LYS A 285     -33.656  -3.866 -61.968  1.00 20.67           C  
ANISOU 2054  C   LYS A 285     2963   2511   2379   -413   -257   -208       C  
ATOM   2055  O   LYS A 285     -33.980  -4.432 -60.918  1.00 17.90           O  
ANISOU 2055  O   LYS A 285     2592   2136   2073   -403   -245   -206       O  
ATOM   2056  CB  LYS A 285     -32.389  -5.581 -63.277  1.00 18.15           C  
ANISOU 2056  CB  LYS A 285     2748   2146   2004   -434   -191   -283       C  
ATOM   2057  CG  LYS A 285     -31.153  -5.965 -64.084  1.00 21.57           C  
ANISOU 2057  CG  LYS A 285     3232   2564   2401   -425   -141   -317       C  
ATOM   2058  CD  LYS A 285     -31.384  -7.274 -64.824  1.00 24.62           C  
ANISOU 2058  CD  LYS A 285     3676   2919   2761   -466   -126   -369       C  
ATOM   2059  CE  LYS A 285     -30.181  -7.701 -65.662  1.00 28.70           C  
ANISOU 2059  CE  LYS A 285     4245   3418   3241   -456    -69   -408       C  
ATOM   2060  NZ  LYS A 285     -29.209  -8.509 -64.890  1.00 35.99           N  
ANISOU 2060  NZ  LYS A 285     5170   4292   4213   -409     -9   -421       N  
ATOM   2061  N   LEU A 286     -34.419  -2.951 -62.566  1.00 17.07           N  
ANISOU 2061  N   LEU A 286     2490   2094   1903   -433   -310   -187       N  
ATOM   2062  CA  LEU A 286     -35.701  -2.566 -61.992  1.00 19.32           C  
ANISOU 2062  CA  LEU A 286     2721   2395   2225   -444   -354   -162       C  
ATOM   2063  C   LEU A 286     -36.645  -3.755 -61.857  1.00 22.43           C  
ANISOU 2063  C   LEU A 286     3118   2769   2635   -485   -362   -187       C  
ATOM   2064  O   LEU A 286     -37.478  -3.777 -60.942  1.00 20.40           O  
ANISOU 2064  O   LEU A 286     2814   2510   2426   -484   -371   -171       O  
ATOM   2065  CB  LEU A 286     -36.338  -1.472 -62.846  1.00 18.11           C  
ANISOU 2065  CB  LEU A 286     2552   2283   2045   -460   -412   -137       C  
ATOM   2066  CG  LEU A 286     -35.637  -0.105 -62.765  1.00 19.37           C  
ANISOU 2066  CG  LEU A 286     2696   2462   2203   -419   -410   -103       C  
ATOM   2067  CD1 LEU A 286     -35.880   0.701 -64.016  1.00 18.93           C  
ANISOU 2067  CD1 LEU A 286     2657   2438   2096   -442   -457    -86       C  
ATOM   2068  CD2 LEU A 286     -36.117   0.653 -61.527  1.00 15.10           C  
ANISOU 2068  CD2 LEU A 286     2092   1924   1723   -386   -416    -71       C  
ATOM   2069  N   LYS A 287     -36.527  -4.756 -62.737  1.00 18.29           N  
ANISOU 2069  N   LYS A 287     2648   2228   2073   -522   -354   -227       N  
ATOM   2070  CA  LYS A 287     -37.411  -5.913 -62.638  1.00 20.03           C  
ANISOU 2070  CA  LYS A 287     2875   2426   2310   -567   -361   -253       C  
ATOM   2071  C   LYS A 287     -37.260  -6.633 -61.307  1.00 19.17           C  
ANISOU 2071  C   LYS A 287     2752   2275   2255   -543   -316   -251       C  
ATOM   2072  O   LYS A 287     -38.165  -7.369 -60.906  1.00 20.96           O  
ANISOU 2072  O   LYS A 287     2967   2486   2511   -575   -324   -259       O  
ATOM   2073  CB  LYS A 287     -37.161  -6.889 -63.787  1.00 21.64           C  
ANISOU 2073  CB  LYS A 287     3149   2612   2463   -609   -353   -301       C  
ATOM   2074  CG  LYS A 287     -35.924  -7.747 -63.667  1.00 21.97           C  
ANISOU 2074  CG  LYS A 287     3242   2606   2500   -583   -285   -332       C  
ATOM   2075  CD  LYS A 287     -35.736  -8.523 -64.957  1.00 26.53           C  
ANISOU 2075  CD  LYS A 287     3890   3172   3020   -627   -280   -382       C  
ATOM   2076  CE  LYS A 287     -34.643  -9.543 -64.832  1.00 27.48           C  
ANISOU 2076  CE  LYS A 287     4058   3238   3145   -604   -210   -418       C  
ATOM   2077  NZ  LYS A 287     -34.580 -10.412 -66.041  1.00 38.67           N  
ANISOU 2077  NZ  LYS A 287     5547   4637   4509   -651   -200   -474       N  
ATOM   2078  N   GLU A 288     -36.161  -6.408 -60.597  1.00 16.86           N  
ANISOU 2078  N   GLU A 288     2461   1967   1978   -488   -272   -239       N  
ATOM   2079  CA  GLU A 288     -35.942  -7.022 -59.298  1.00 20.05           C  
ANISOU 2079  CA  GLU A 288     2855   2334   2428   -461   -233   -231       C  
ATOM   2080  C   GLU A 288     -36.122  -6.034 -58.153  1.00 18.94           C  
ANISOU 2080  C   GLU A 288     2657   2215   2323   -425   -238   -189       C  
ATOM   2081  O   GLU A 288     -35.753  -6.340 -57.012  1.00 20.52           O  
ANISOU 2081  O   GLU A 288     2850   2390   2555   -395   -205   -177       O  
ATOM   2082  CB  GLU A 288     -34.551  -7.656 -59.261  1.00 22.84           C  
ANISOU 2082  CB  GLU A 288     3254   2651   2775   -427   -180   -250       C  
ATOM   2083  CG  GLU A 288     -34.471  -8.898 -60.136  1.00 27.22           C  
ANISOU 2083  CG  GLU A 288     3868   3168   3305   -463   -164   -297       C  
ATOM   2084  CD  GLU A 288     -33.048  -9.332 -60.450  1.00 31.54           C  
ANISOU 2084  CD  GLU A 288     4459   3687   3838   -428   -114   -320       C  
ATOM   2085  OE1 GLU A 288     -32.096  -8.870 -59.781  1.00 27.49           O  
ANISOU 2085  OE1 GLU A 288     3927   3174   3344   -374    -89   -297       O  
ATOM   2086  OE2 GLU A 288     -32.882 -10.138 -61.387  1.00 37.67           O  
ANISOU 2086  OE2 GLU A 288     5288   4440   4586   -456    -98   -362       O  
ATOM   2087  N   ILE A 289     -36.689  -4.862 -58.434  1.00 18.10           N  
ANISOU 2087  N   ILE A 289     2512   2152   2213   -427   -279   -167       N  
ATOM   2088  CA  ILE A 289     -36.902  -3.811 -57.450  1.00 17.59           C  
ANISOU 2088  CA  ILE A 289     2393   2108   2181   -393   -285   -131       C  
ATOM   2089  C   ILE A 289     -38.397  -3.704 -57.184  1.00 24.02           C  
ANISOU 2089  C   ILE A 289     3160   2939   3027   -424   -317   -120       C  
ATOM   2090  O   ILE A 289     -39.211  -3.784 -58.113  1.00 19.46           O  
ANISOU 2090  O   ILE A 289     2579   2380   2435   -465   -358   -130       O  
ATOM   2091  CB  ILE A 289     -36.314  -2.472 -57.940  1.00 14.86           C  
ANISOU 2091  CB  ILE A 289     2038   1793   1814   -365   -301   -112       C  
ATOM   2092  CG1 ILE A 289     -34.816  -2.641 -58.211  1.00 18.36           C  
ANISOU 2092  CG1 ILE A 289     2525   2221   2231   -338   -264   -125       C  
ATOM   2093  CG2 ILE A 289     -36.526  -1.366 -56.909  1.00 17.92           C  
ANISOU 2093  CG2 ILE A 289     2374   2197   2237   -330   -305    -79       C  
ATOM   2094  CD1 ILE A 289     -34.126  -1.378 -58.719  1.00 15.15           C  
ANISOU 2094  CD1 ILE A 289     2114   1841   1802   -315   -273   -107       C  
ATOM   2095  N   ASP A 290     -38.752  -3.539 -55.911  1.00 20.86           N  
ANISOU 2095  N   ASP A 290     2723   2535   2669   -404   -299   -101       N  
ATOM   2096  CA AASP A 290     -40.157  -3.453 -55.530  0.49 21.35           C  
ANISOU 2096  CA AASP A 290     2732   2612   2767   -431   -320    -92       C  
ATOM   2097  CA BASP A 290     -40.151  -3.439 -55.515  0.51 21.38           C  
ANISOU 2097  CA BASP A 290     2735   2616   2771   -430   -320    -92       C  
ATOM   2098  C   ASP A 290     -40.853  -2.326 -56.284  1.00 20.04           C  
ANISOU 2098  C   ASP A 290     2525   2488   2600   -436   -373    -76       C  
ATOM   2099  O   ASP A 290     -40.329  -1.216 -56.406  1.00 17.67           O  
ANISOU 2099  O   ASP A 290     2218   2205   2290   -400   -382    -58       O  
ATOM   2100  CB AASP A 290     -40.291  -3.244 -54.022  0.49 21.63           C  
ANISOU 2100  CB AASP A 290     2736   2640   2841   -403   -285    -73       C  
ATOM   2101  CB BASP A 290     -40.228  -3.192 -54.011  0.51 21.63           C  
ANISOU 2101  CB BASP A 290     2737   2640   2840   -400   -284    -72       C  
ATOM   2102  CG AASP A 290     -40.472  -4.550 -53.257  0.49 22.99           C  
ANISOU 2102  CG AASP A 290     2929   2775   3030   -425   -247    -83       C  
ATOM   2103  CG BASP A 290     -41.639  -3.024 -53.517  0.51 22.78           C  
ANISOU 2103  CG BASP A 290     2823   2803   3029   -423   -296    -62       C  
ATOM   2104  OD1AASP A 290     -40.090  -5.623 -53.771  0.49 23.10           O  
ANISOU 2104  OD1AASP A 290     2992   2760   3025   -447   -238   -106       O  
ATOM   2105  OD1BASP A 290     -42.185  -1.907 -53.634  0.51 24.25           O  
ANISOU 2105  OD1BASP A 290     2961   3021   3232   -409   -325    -45       O  
ATOM   2106  OD2AASP A 290     -41.013  -4.501 -52.131  0.49 25.00           O  
ANISOU 2106  OD2AASP A 290     3153   3029   3317   -420   -225    -69       O  
ATOM   2107  OD2BASP A 290     -42.201  -4.016 -53.013  0.51 23.44           O  
ANISOU 2107  OD2BASP A 290     2907   2866   3132   -454   -275    -71       O  
ATOM   2108  N   ASP A 291     -42.048  -2.625 -56.797  1.00 20.41           N  
ANISOU 2108  N   ASP A 291     2545   2549   2659   -481   -411    -83       N  
ATOM   2109  CA  ASP A 291     -42.744  -1.657 -57.640  1.00 23.37           C  
ANISOU 2109  CA  ASP A 291     2883   2964   3032   -488   -471    -66       C  
ATOM   2110  C   ASP A 291     -43.122  -0.391 -56.885  1.00 22.99           C  
ANISOU 2110  C   ASP A 291     2775   2935   3026   -446   -475    -34       C  
ATOM   2111  O   ASP A 291     -43.146   0.691 -57.479  1.00 24.07           O  
ANISOU 2111  O   ASP A 291     2895   3095   3154   -428   -512    -14       O  
ATOM   2112  CB  ASP A 291     -43.991  -2.291 -58.256  1.00 26.24           C  
ANISOU 2112  CB  ASP A 291     3223   3341   3406   -547   -515    -79       C  
ATOM   2113  CG  ASP A 291     -43.655  -3.355 -59.295  1.00 30.88           C  
ANISOU 2113  CG  ASP A 291     3876   3914   3943   -592   -524   -114       C  
ATOM   2114  OD1 ASP A 291     -42.616  -3.220 -59.996  1.00 28.16           O  
ANISOU 2114  OD1 ASP A 291     3587   3565   3546   -578   -519   -121       O  
ATOM   2115  OD2 ASP A 291     -44.438  -4.326 -59.400  1.00 33.65           O  
ANISOU 2115  OD2 ASP A 291     4223   4256   4306   -643   -533   -135       O  
ATOM   2116  N   GLU A 292     -43.442  -0.489 -55.592  1.00 21.98           N  
ANISOU 2116  N   GLU A 292     2614   2795   2942   -432   -435    -29       N  
ATOM   2117  CA  GLU A 292     -43.802   0.735 -54.880  1.00 22.38           C  
ANISOU 2117  CA  GLU A 292     2610   2862   3032   -392   -433     -4       C  
ATOM   2118  C   GLU A 292     -42.582   1.619 -54.662  1.00 19.45           C  
ANISOU 2118  C   GLU A 292     2268   2485   2639   -342   -414      8       C  
ATOM   2119  O   GLU A 292     -42.698   2.853 -54.684  1.00 17.13           O  
ANISOU 2119  O   GLU A 292     1943   2206   2359   -312   -434     29       O  
ATOM   2120  CB  GLU A 292     -44.476   0.422 -53.547  1.00 24.72           C  
ANISOU 2120  CB  GLU A 292     2867   3149   3376   -392   -391     -4       C  
ATOM   2121  CG  GLU A 292     -45.158   1.653 -52.954  1.00 30.21           C  
ANISOU 2121  CG  GLU A 292     3497   3864   4119   -359   -394     17       C  
ATOM   2122  CD  GLU A 292     -46.153   1.319 -51.855  1.00 40.33           C  
ANISOU 2122  CD  GLU A 292     4728   5144   5452   -370   -358     14       C  
ATOM   2123  OE1 GLU A 292     -46.083   0.198 -51.298  1.00 42.02           O  
ANISOU 2123  OE1 GLU A 292     4968   5337   5660   -397   -320      0       O  
ATOM   2124  OE2 GLU A 292     -47.007   2.188 -51.549  1.00 39.71           O  
ANISOU 2124  OE2 GLU A 292     4584   5083   5420   -353   -365     27       O  
ATOM   2125  N   PHE A 293     -41.412   1.004 -54.464  1.00 16.58           N  
ANISOU 2125  N   PHE A 293     1960   2097   2242   -334   -378     -6       N  
ATOM   2126  CA  PHE A 293     -40.160   1.755 -54.480  1.00 18.88           C  
ANISOU 2126  CA  PHE A 293     2281   2385   2508   -295   -366      3       C  
ATOM   2127  C   PHE A 293     -39.966   2.466 -55.815  1.00 19.15           C  
ANISOU 2127  C   PHE A 293     2327   2438   2510   -298   -411     11       C  
ATOM   2128  O   PHE A 293     -39.632   3.659 -55.860  1.00 17.07           O  
ANISOU 2128  O   PHE A 293     2053   2184   2248   -268   -420     32       O  
ATOM   2129  CB  PHE A 293     -38.989   0.816 -54.199  1.00 15.73           C  
ANISOU 2129  CB  PHE A 293     1937   1958   2082   -290   -325    -15       C  
ATOM   2130  CG  PHE A 293     -37.648   1.481 -54.247  1.00 13.63           C  
ANISOU 2130  CG  PHE A 293     1697   1690   1792   -254   -311     -9       C  
ATOM   2131  CD1 PHE A 293     -36.965   1.629 -55.449  1.00 13.89           C  
ANISOU 2131  CD1 PHE A 293     1763   1729   1785   -260   -327    -14       C  
ATOM   2132  CD2 PHE A 293     -37.063   1.962 -53.087  1.00 16.12           C  
ANISOU 2132  CD2 PHE A 293     2004   1997   2123   -217   -281      1       C  
ATOM   2133  CE1 PHE A 293     -35.717   2.228 -55.490  1.00 14.50           C  
ANISOU 2133  CE1 PHE A 293     1861   1805   1844   -230   -311     -9       C  
ATOM   2134  CE2 PHE A 293     -35.819   2.569 -53.111  1.00 14.24           C  
ANISOU 2134  CE2 PHE A 293     1786   1758   1866   -188   -270      6       C  
ATOM   2135  CZ  PHE A 293     -35.144   2.703 -54.314  1.00 15.81           C  
ANISOU 2135  CZ  PHE A 293     2014   1963   2031   -194   -283      1       C  
ATOM   2136  N   ILE A 294     -40.139   1.736 -56.919  1.00 18.80           N  
ANISOU 2136  N   ILE A 294     2311   2399   2434   -338   -437     -4       N  
ATOM   2137  CA  ILE A 294     -39.968   2.338 -58.238  1.00 19.52           C  
ANISOU 2137  CA  ILE A 294     2422   2509   2485   -346   -480      5       C  
ATOM   2138  C   ILE A 294     -40.932   3.506 -58.413  1.00 21.52           C  
ANISOU 2138  C   ILE A 294     2621   2788   2767   -336   -528     36       C  
ATOM   2139  O   ILE A 294     -40.554   4.587 -58.881  1.00 18.92           O  
ANISOU 2139  O   ILE A 294     2296   2468   2424   -314   -547     59       O  
ATOM   2140  CB  ILE A 294     -40.163   1.282 -59.339  1.00 19.64           C  
ANISOU 2140  CB  ILE A 294     2477   2527   2460   -397   -501    -20       C  
ATOM   2141  CG1 ILE A 294     -39.094   0.180 -59.220  1.00 17.25           C  
ANISOU 2141  CG1 ILE A 294     2231   2193   2131   -400   -449    -51       C  
ATOM   2142  CG2 ILE A 294     -40.154   1.951 -60.725  1.00 17.04           C  
ANISOU 2142  CG2 ILE A 294     2168   2223   2084   -411   -552     -8       C  
ATOM   2143  CD1 ILE A 294     -39.249  -0.976 -60.222  1.00 20.65           C  
ANISOU 2143  CD1 ILE A 294     2707   2617   2523   -450   -461    -85       C  
ATOM   2144  N   LYS A 295     -42.197   3.297 -58.048  1.00 20.66           N  
ANISOU 2144  N   LYS A 295     2459   2688   2703   -352   -546     38       N  
ATOM   2145  CA  LYS A 295     -43.191   4.354 -58.177  1.00 20.87           C  
ANISOU 2145  CA  LYS A 295     2426   2736   2767   -339   -592     67       C  
ATOM   2146  C   LYS A 295     -42.722   5.627 -57.476  1.00 20.37           C  
ANISOU 2146  C   LYS A 295     2346   2666   2728   -286   -571     89       C  
ATOM   2147  O   LYS A 295     -42.762   6.718 -58.051  1.00 19.38           O  
ANISOU 2147  O   LYS A 295     2212   2551   2601   -267   -607    116       O  
ATOM   2148  CB  LYS A 295     -44.527   3.877 -57.607  1.00 21.58           C  
ANISOU 2148  CB  LYS A 295     2453   2833   2912   -360   -598     61       C  
ATOM   2149  CG  LYS A 295     -45.670   4.886 -57.745  1.00 28.00           C  
ANISOU 2149  CG  LYS A 295     3194   3670   3775   -346   -647     90       C  
ATOM   2150  CD  LYS A 295     -46.999   4.277 -57.268  1.00 32.49           C  
ANISOU 2150  CD  LYS A 295     3697   4249   4399   -373   -650     81       C  
ATOM   2151  CE  LYS A 295     -47.422   4.855 -55.920  1.00 37.73           C  
ANISOU 2151  CE  LYS A 295     4304   4904   5127   -335   -605     88       C  
ATOM   2152  NZ  LYS A 295     -48.427   4.002 -55.214  1.00 51.36           N  
ANISOU 2152  NZ  LYS A 295     5982   6634   6900   -366   -581     72       N  
ATOM   2153  N   ASN A 296     -42.242   5.502 -56.239  1.00 19.25           N  
ANISOU 2153  N   ASN A 296     2204   2504   2606   -262   -513     79       N  
ATOM   2154  CA  ASN A 296     -41.804   6.692 -55.517  1.00 18.97           C  
ANISOU 2154  CA  ASN A 296     2155   2460   2593   -215   -492     95       C  
ATOM   2155  C   ASN A 296     -40.453   7.202 -55.998  1.00 19.01           C  
ANISOU 2155  C   ASN A 296     2213   2458   2553   -199   -486    101       C  
ATOM   2156  O   ASN A 296     -40.213   8.417 -55.972  1.00 16.41           O  
ANISOU 2156  O   ASN A 296     1875   2126   2234   -168   -493    122       O  
ATOM   2157  CB  ASN A 296     -41.771   6.400 -54.024  1.00 17.93           C  
ANISOU 2157  CB  ASN A 296     2009   2313   2492   -199   -436     81       C  
ATOM   2158  CG  ASN A 296     -43.157   6.397 -53.420  1.00 18.13           C  
ANISOU 2158  CG  ASN A 296     1969   2347   2573   -203   -436     83       C  
ATOM   2159  OD1 ASN A 296     -43.683   7.446 -53.043  1.00 17.06           O  
ANISOU 2159  OD1 ASN A 296     1789   2214   2479   -173   -441     98       O  
ATOM   2160  ND2 ASN A 296     -43.766   5.229 -53.357  1.00 16.89           N  
ANISOU 2160  ND2 ASN A 296     1804   2191   2421   -241   -431     67       N  
ATOM   2161  N   LEU A 297     -39.577   6.304 -56.453  1.00 16.36           N  
ANISOU 2161  N   LEU A 297     1930   2116   2169   -219   -470     82       N  
ATOM   2162  CA  LEU A 297     -38.314   6.735 -57.037  1.00 19.25           C  
ANISOU 2162  CA  LEU A 297     2343   2479   2493   -208   -463     86       C  
ATOM   2163  C   LEU A 297     -38.546   7.635 -58.246  1.00 17.36           C  
ANISOU 2163  C   LEU A 297     2107   2256   2233   -214   -514    112       C  
ATOM   2164  O   LEU A 297     -37.885   8.671 -58.397  1.00 19.52           O  
ANISOU 2164  O   LEU A 297     2392   2525   2499   -192   -513    131       O  
ATOM   2165  CB  LEU A 297     -37.478   5.515 -57.427  1.00 17.91           C  
ANISOU 2165  CB  LEU A 297     2225   2301   2280   -231   -437     58       C  
ATOM   2166  CG  LEU A 297     -36.137   5.768 -58.125  1.00 17.50           C  
ANISOU 2166  CG  LEU A 297     2220   2247   2183   -225   -423     57       C  
ATOM   2167  CD1 LEU A 297     -35.084   6.273 -57.138  1.00 16.92           C  
ANISOU 2167  CD1 LEU A 297     2145   2159   2125   -189   -381     59       C  
ATOM   2168  CD2 LEU A 297     -35.660   4.507 -58.859  1.00 17.97           C  
ANISOU 2168  CD2 LEU A 297     2327   2300   2199   -255   -408     28       C  
ATOM   2169  N   LYS A 298     -39.477   7.250 -59.124  1.00 18.97           N  
ANISOU 2169  N   LYS A 298     2304   2477   2425   -246   -560    114       N  
ATOM   2170  CA  LYS A 298     -39.774   8.053 -60.302  1.00 19.66           C  
ANISOU 2170  CA  LYS A 298     2398   2583   2490   -254   -616    143       C  
ATOM   2171  C   LYS A 298     -40.345   9.415 -59.938  1.00 19.87           C  
ANISOU 2171  C   LYS A 298     2377   2608   2566   -218   -640    178       C  
ATOM   2172  O   LYS A 298     -40.283  10.339 -60.752  1.00 21.12           O  
ANISOU 2172  O   LYS A 298     2547   2772   2706   -212   -677    209       O  
ATOM   2173  CB  LYS A 298     -40.748   7.298 -61.210  1.00 19.88           C  
ANISOU 2173  CB  LYS A 298     2424   2632   2498   -298   -667    137       C  
ATOM   2174  CG  LYS A 298     -40.124   6.041 -61.821  1.00 23.17           C  
ANISOU 2174  CG  LYS A 298     2900   3046   2857   -337   -647    102       C  
ATOM   2175  CD  LYS A 298     -41.185   5.138 -62.440  1.00 27.35           C  
ANISOU 2175  CD  LYS A 298     3421   3592   3377   -385   -691     87       C  
ATOM   2176  CE  LYS A 298     -41.713   5.741 -63.719  1.00 31.14           C  
ANISOU 2176  CE  LYS A 298     3909   4101   3823   -405   -764    114       C  
ATOM   2177  NZ  LYS A 298     -42.986   5.091 -64.135  1.00 38.74           N  
ANISOU 2177  NZ  LYS A 298     4841   5083   4794   -448   -819    106       N  
ATOM   2178  N   ILE A 299     -40.912   9.554 -58.744  1.00 19.69           N  
ANISOU 2178  N   ILE A 299     2303   2576   2604   -194   -617    174       N  
ATOM   2179  CA  ILE A 299     -41.339  10.862 -58.263  1.00 18.99           C  
ANISOU 2179  CA  ILE A 299     2170   2478   2566   -154   -627    201       C  
ATOM   2180  C   ILE A 299     -40.175  11.597 -57.624  1.00 20.71           C  
ANISOU 2180  C   ILE A 299     2414   2674   2782   -123   -582    201       C  
ATOM   2181  O   ILE A 299     -39.988  12.799 -57.847  1.00 20.22           O  
ANISOU 2181  O   ILE A 299     2353   2602   2729    -99   -597    228       O  
ATOM   2182  CB  ILE A 299     -42.503  10.688 -57.282  1.00 19.02           C  
ANISOU 2182  CB  ILE A 299     2107   2483   2635   -144   -618    193       C  
ATOM   2183  CG1 ILE A 299     -43.707  10.095 -58.023  1.00 23.80           C  
ANISOU 2183  CG1 ILE A 299     2680   3114   3249   -177   -672    197       C  
ATOM   2184  CG2 ILE A 299     -42.843  12.021 -56.606  1.00 19.91           C  
ANISOU 2184  CG2 ILE A 299     2178   2581   2806    -97   -613    213       C  
ATOM   2185  CD1 ILE A 299     -44.695   9.419 -57.115  1.00 30.18           C  
ANISOU 2185  CD1 ILE A 299     3432   3926   4110   -185   -651    178       C  
ATOM   2186  N   LEU A 300     -39.362  10.869 -56.854  1.00 17.23           N  
ANISOU 2186  N   LEU A 300     1996   2223   2328   -125   -529    171       N  
ATOM   2187  CA  LEU A 300     -38.265  11.469 -56.099  1.00 19.43           C  
ANISOU 2187  CA  LEU A 300     2293   2483   2607    -98   -486    167       C  
ATOM   2188  C   LEU A 300     -37.271  12.181 -57.005  1.00 16.59           C  
ANISOU 2188  C   LEU A 300     1975   2120   2208    -98   -497    185       C  
ATOM   2189  O   LEU A 300     -36.910  13.336 -56.760  1.00 16.94           O  
ANISOU 2189  O   LEU A 300     2017   2149   2269    -74   -492    202       O  
ATOM   2190  CB  LEU A 300     -37.552  10.386 -55.285  1.00 17.21           C  
ANISOU 2190  CB  LEU A 300     2032   2196   2312   -104   -437    136       C  
ATOM   2191  CG  LEU A 300     -36.219  10.761 -54.626  1.00 14.46           C  
ANISOU 2191  CG  LEU A 300     1709   1833   1953    -84   -398    128       C  
ATOM   2192  CD1 LEU A 300     -36.416  11.849 -53.570  1.00 12.38           C  
ANISOU 2192  CD1 LEU A 300     1415   1555   1733    -52   -384    134       C  
ATOM   2193  CD2 LEU A 300     -35.588   9.532 -53.994  1.00 14.03           C  
ANISOU 2193  CD2 LEU A 300     1674   1774   1882    -92   -360    102       C  
ATOM   2194  N   ILE A 301     -36.766  11.484 -58.020  1.00 14.81           N  
ANISOU 2194  N   ILE A 301     1791   1907   1929   -128   -505    179       N  
ATOM   2195  CA  ILE A 301     -35.654  12.029 -58.797  1.00 17.99           C  
ANISOU 2195  CA  ILE A 301     2239   2308   2290   -132   -500    191       C  
ATOM   2196  C   ILE A 301     -36.022  13.329 -59.505  1.00 16.95           C  
ANISOU 2196  C   ILE A 301     2104   2175   2163   -123   -542    232       C  
ATOM   2197  O   ILE A 301     -35.263  14.300 -59.391  1.00 20.60           O  
ANISOU 2197  O   ILE A 301     2578   2620   2628   -107   -527    246       O  
ATOM   2198  CB  ILE A 301     -35.109  10.955 -59.768  1.00 15.92           C  
ANISOU 2198  CB  ILE A 301     2022   2058   1967   -167   -495    173       C  
ATOM   2199  CG1 ILE A 301     -34.831   9.640 -59.040  1.00 20.13           C  
ANISOU 2199  CG1 ILE A 301     2557   2587   2503   -172   -455    135       C  
ATOM   2200  CG2 ILE A 301     -33.861  11.462 -60.446  1.00 18.68           C  
ANISOU 2200  CG2 ILE A 301     2415   2406   2276   -171   -476    181       C  
ATOM   2201  CD1 ILE A 301     -33.857   9.771 -57.930  1.00 20.27           C  
ANISOU 2201  CD1 ILE A 301     2572   2589   2542   -145   -407    124       C  
ATOM   2202  N   PRO A 302     -37.142  13.421 -60.240  1.00 19.96           N  
ANISOU 2202  N   PRO A 302     2469   2569   2546   -134   -597    254       N  
ATOM   2203  CA  PRO A 302     -37.512  14.727 -60.817  1.00 19.35           C  
ANISOU 2203  CA  PRO A 302     2386   2485   2480   -119   -640    298       C  
ATOM   2204  C   PRO A 302     -37.844  15.754 -59.761  1.00 19.67           C  
ANISOU 2204  C   PRO A 302     2384   2500   2589    -76   -628    308       C  
ATOM   2205  O   PRO A 302     -37.562  16.941 -59.949  1.00 23.19           O  
ANISOU 2205  O   PRO A 302     2840   2927   3045    -58   -637    337       O  
ATOM   2206  CB  PRO A 302     -38.737  14.400 -61.686  1.00 20.07           C  
ANISOU 2206  CB  PRO A 302     2461   2600   2564   -138   -704    315       C  
ATOM   2207  CG  PRO A 302     -38.642  12.936 -61.946  1.00 21.10           C  
ANISOU 2207  CG  PRO A 302     2613   2750   2653   -176   -692    279       C  
ATOM   2208  CD  PRO A 302     -38.044  12.353 -60.702  1.00 19.88           C  
ANISOU 2208  CD  PRO A 302     2449   2581   2523   -163   -627    241       C  
ATOM   2209  N   TRP A 303     -38.449  15.336 -58.654  1.00 19.00           N  
ANISOU 2209  N   TRP A 303     2255   2414   2552    -62   -607    284       N  
ATOM   2210  CA  TRP A 303     -38.653  16.256 -57.543  1.00 20.71           C  
ANISOU 2210  CA  TRP A 303     2435   2604   2828    -23   -585    285       C  
ATOM   2211  C   TRP A 303     -37.332  16.866 -57.088  1.00 22.13           C  
ANISOU 2211  C   TRP A 303     2650   2763   2997    -13   -542    278       C  
ATOM   2212  O   TRP A 303     -37.270  18.054 -56.748  1.00 23.59           O  
ANISOU 2212  O   TRP A 303     2827   2922   3216     14   -539    293       O  
ATOM   2213  CB  TRP A 303     -39.343  15.510 -56.416  1.00 20.17           C  
ANISOU 2213  CB  TRP A 303     2324   2540   2798    -17   -557    254       C  
ATOM   2214  CG  TRP A 303     -39.678  16.283 -55.193  1.00 23.32           C  
ANISOU 2214  CG  TRP A 303     2687   2918   3257     20   -528    247       C  
ATOM   2215  CD1 TRP A 303     -40.709  17.159 -55.023  1.00 21.94           C  
ANISOU 2215  CD1 TRP A 303     2465   2731   3142     49   -548    265       C  
ATOM   2216  CD2 TRP A 303     -39.021  16.180 -53.926  1.00 20.44           C  
ANISOU 2216  CD2 TRP A 303     2329   2540   2899     30   -471    216       C  
ATOM   2217  NE1 TRP A 303     -40.723  17.624 -53.731  1.00 22.10           N  
ANISOU 2217  NE1 TRP A 303     2464   2730   3202     77   -502    244       N  
ATOM   2218  CE2 TRP A 303     -39.695  17.036 -53.037  1.00 22.87           C  
ANISOU 2218  CE2 TRP A 303     2597   2828   3265     64   -456    215       C  
ATOM   2219  CE3 TRP A 303     -37.920  15.450 -53.463  1.00 19.36           C  
ANISOU 2219  CE3 TRP A 303     2228   2406   2723     15   -433    191       C  
ATOM   2220  CZ2 TRP A 303     -39.305  17.185 -51.706  1.00 19.74           C  
ANISOU 2220  CZ2 TRP A 303     2201   2417   2882     78   -405    187       C  
ATOM   2221  CZ3 TRP A 303     -37.537  15.593 -52.137  1.00 20.67           C  
ANISOU 2221  CZ3 TRP A 303     2391   2558   2905     32   -387    167       C  
ATOM   2222  CH2 TRP A 303     -38.225  16.457 -51.275  1.00 20.95           C  
ANISOU 2222  CH2 TRP A 303     2393   2576   2992     61   -374    165       C  
ATOM   2223  N   LEU A 304     -36.258  16.075 -57.096  1.00 19.84           N  
ANISOU 2223  N   LEU A 304     2395   2481   2661    -34   -510    254       N  
ATOM   2224  CA  LEU A 304     -34.940  16.601 -56.751  1.00 20.79           C  
ANISOU 2224  CA  LEU A 304     2544   2585   2769    -29   -474    248       C  
ATOM   2225  C   LEU A 304     -34.310  17.379 -57.893  1.00 21.42           C  
ANISOU 2225  C   LEU A 304     2662   2661   2817    -41   -492    279       C  
ATOM   2226  O   LEU A 304     -33.671  18.410 -57.659  1.00 22.08           O  
ANISOU 2226  O   LEU A 304     2756   2721   2914    -29   -478    290       O  
ATOM   2227  CB  LEU A 304     -33.993  15.468 -56.364  1.00 18.75           C  
ANISOU 2227  CB  LEU A 304     2306   2338   2480    -44   -434    214       C  
ATOM   2228  CG  LEU A 304     -34.263  14.775 -55.037  1.00 19.57           C  
ANISOU 2228  CG  LEU A 304     2384   2441   2611    -33   -404    184       C  
ATOM   2229  CD1 LEU A 304     -33.379  13.546 -54.895  1.00 18.47           C  
ANISOU 2229  CD1 LEU A 304     2269   2312   2438    -49   -374    158       C  
ATOM   2230  CD2 LEU A 304     -34.031  15.759 -53.905  1.00 19.18           C  
ANISOU 2230  CD2 LEU A 304     2319   2370   2599     -6   -382    180       C  
ATOM   2231  N   LEU A 305     -34.439  16.884 -59.130  1.00 20.39           N  
ANISOU 2231  N   LEU A 305     2557   2551   2639    -68   -521    293       N  
ATOM   2232  CA  LEU A 305     -33.535  17.285 -60.194  1.00 21.83           C  
ANISOU 2232  CA  LEU A 305     2788   2735   2772    -89   -522    313       C  
ATOM   2233  C   LEU A 305     -34.195  17.982 -61.378  1.00 27.70           C  
ANISOU 2233  C   LEU A 305     3546   3480   3498    -96   -577    359       C  
ATOM   2234  O   LEU A 305     -33.475  18.418 -62.287  1.00 26.23           O  
ANISOU 2234  O   LEU A 305     3404   3294   3269   -115   -577    381       O  
ATOM   2235  CB  LEU A 305     -32.755  16.063 -60.708  1.00 23.72           C  
ANISOU 2235  CB  LEU A 305     3061   2997   2955   -119   -496    285       C  
ATOM   2236  CG  LEU A 305     -31.796  15.457 -59.667  1.00 19.18           C  
ANISOU 2236  CG  LEU A 305     2478   2417   2391   -112   -441    246       C  
ATOM   2237  CD1 LEU A 305     -30.935  14.363 -60.278  1.00 18.60           C  
ANISOU 2237  CD1 LEU A 305     2440   2362   2267   -137   -413    222       C  
ATOM   2238  CD2 LEU A 305     -30.919  16.544 -59.053  1.00 20.66           C  
ANISOU 2238  CD2 LEU A 305     2664   2582   2603    -95   -415    253       C  
ATOM   2239  N   SER A 306     -35.520  18.097 -61.411  1.00 24.65           N  
ANISOU 2239  N   SER A 306     3125   3097   3144    -83   -624    376       N  
ATOM   2240  CA  SER A 306     -36.162  18.741 -62.548  1.00 26.02           C  
ANISOU 2240  CA  SER A 306     3312   3274   3301    -88   -685    424       C  
ATOM   2241  C   SER A 306     -35.630  20.166 -62.705  1.00 28.97           C  
ANISOU 2241  C   SER A 306     3707   3615   3687    -73   -683    461       C  
ATOM   2242  O   SER A 306     -35.215  20.791 -61.722  1.00 27.80           O  
ANISOU 2242  O   SER A 306     3542   3437   3583    -48   -646    450       O  
ATOM   2243  CB  SER A 306     -37.677  18.772 -62.374  1.00 28.65           C  
ANISOU 2243  CB  SER A 306     3590   3612   3685    -68   -735    437       C  
ATOM   2244  OG  SER A 306     -38.032  19.669 -61.338  1.00 32.93           O  
ANISOU 2244  OG  SER A 306     4088   4122   4301    -25   -721    441       O  
ATOM   2245  N   PRO A 307     -35.622  20.696 -63.934  1.00 28.96           N  
ANISOU 2245  N   PRO A 307     3745   3615   3642    -89   -722    506       N  
ATOM   2246  CA  PRO A 307     -35.093  22.058 -64.152  1.00 33.73           C  
ANISOU 2246  CA  PRO A 307     4376   4184   4255    -79   -720    545       C  
ATOM   2247  C   PRO A 307     -35.617  23.093 -63.165  1.00 33.71           C  
ANISOU 2247  C   PRO A 307     4329   4140   4338    -32   -721    555       C  
ATOM   2248  O   PRO A 307     -34.838  23.921 -62.678  1.00 35.34           O  
ANISOU 2248  O   PRO A 307     4549   4313   4567    -23   -685    555       O  
ATOM   2249  CB  PRO A 307     -35.529  22.362 -65.594  1.00 36.03           C  
ANISOU 2249  CB  PRO A 307     4706   4488   4496    -99   -782    599       C  
ATOM   2250  CG  PRO A 307     -35.535  21.009 -66.261  1.00 32.93           C  
ANISOU 2250  CG  PRO A 307     4334   4143   4036   -138   -788    572       C  
ATOM   2251  CD  PRO A 307     -36.034  20.051 -65.197  1.00 29.41           C  
ANISOU 2251  CD  PRO A 307     3832   3708   3635   -124   -769    521       C  
ATOM   2252  N   GLU A 308     -36.905  23.046 -62.826  1.00 30.02           N  
ANISOU 2252  N   GLU A 308     3810   3675   3923     -4   -759    560       N  
ATOM   2253  CA  GLU A 308     -37.447  23.995 -61.858  1.00 35.66           C  
ANISOU 2253  CA  GLU A 308     4480   4349   4721     43   -754    563       C  
ATOM   2254  C   GLU A 308     -36.796  23.821 -60.489  1.00 37.15           C  
ANISOU 2254  C   GLU A 308     4653   4525   4939     53   -685    510       C  
ATOM   2255  O   GLU A 308     -36.579  24.802 -59.768  1.00 38.01           O  
ANISOU 2255  O   GLU A 308     4756   4592   5095     79   -661    509       O  
ATOM   2256  CB  GLU A 308     -38.969  23.825 -61.766  1.00 41.28           C  
ANISOU 2256  CB  GLU A 308     5131   5072   5483     70   -802    573       C  
ATOM   2257  CG  GLU A 308     -39.576  24.159 -60.395  1.00 49.19           C  
ANISOU 2257  CG  GLU A 308     6072   6047   6571    113   -772    546       C  
ATOM   2258  CD  GLU A 308     -39.942  25.631 -60.249  1.00 59.34           C  
ANISOU 2258  CD  GLU A 308     7346   7281   7921    157   -787    582       C  
ATOM   2259  OE1 GLU A 308     -40.777  26.116 -61.044  1.00 63.42           O  
ANISOU 2259  OE1 GLU A 308     7850   7793   8455    174   -850    631       O  
ATOM   2260  OE2 GLU A 308     -39.393  26.304 -59.347  1.00 60.70           O  
ANISOU 2260  OE2 GLU A 308     7523   7415   8126    175   -738    561       O  
ATOM   2261  N   SER A 309     -36.466  22.576 -60.119  1.00 30.68           N  
ANISOU 2261  N   SER A 309     3830   3739   4089     31   -654    466       N  
ATOM   2262  CA  SER A 309     -35.925  22.269 -58.798  1.00 32.40           C  
ANISOU 2262  CA  SER A 309     4032   3950   4330     39   -596    417       C  
ATOM   2263  C   SER A 309     -34.444  22.604 -58.651  1.00 29.22           C  
ANISOU 2263  C   SER A 309     3669   3533   3899     22   -552    406       C  
ATOM   2264  O   SER A 309     -33.960  22.696 -57.519  1.00 29.41           O  
ANISOU 2264  O   SER A 309     3682   3544   3949     33   -510    373       O  
ATOM   2265  CB  SER A 309     -36.117  20.780 -58.480  1.00 28.10           C  
ANISOU 2265  CB  SER A 309     3470   3443   3764     22   -582    378       C  
ATOM   2266  OG  SER A 309     -37.382  20.327 -58.933  1.00 32.30           O  
ANISOU 2266  OG  SER A 309     3971   3996   4307     23   -628    392       O  
ATOM   2267  N   LEU A 310     -33.716  22.765 -59.754  1.00 29.11           N  
ANISOU 2267  N   LEU A 310     3702   3524   3833     -6   -560    431       N  
ATOM   2268  CA  LEU A 310     -32.261  22.908 -59.705  1.00 28.13           C  
ANISOU 2268  CA  LEU A 310     3613   3396   3681    -28   -516    418       C  
ATOM   2269  C   LEU A 310     -31.877  24.248 -59.084  1.00 30.91           C  
ANISOU 2269  C   LEU A 310     3965   3701   4077    -10   -499    427       C  
ATOM   2270  O   LEU A 310     -32.065  25.302 -59.696  1.00 28.69           O  
ANISOU 2270  O   LEU A 310     3703   3391   3807     -5   -525    470       O  
ATOM   2271  CB  LEU A 310     -31.688  22.781 -61.111  1.00 27.86           C  
ANISOU 2271  CB  LEU A 310     3628   3379   3580    -64   -527    446       C  
ATOM   2272  CG  LEU A 310     -31.845  21.407 -61.756  1.00 27.16           C  
ANISOU 2272  CG  LEU A 310     3548   3334   3437    -88   -535    429       C  
ATOM   2273  CD1 LEU A 310     -31.423  21.450 -63.217  1.00 30.34           C  
ANISOU 2273  CD1 LEU A 310     4005   3752   3772   -123   -549    460       C  
ATOM   2274  CD2 LEU A 310     -31.050  20.352 -60.981  1.00 22.77           C  
ANISOU 2274  CD2 LEU A 310     2981   2795   2874    -95   -484    377       C  
ATOM   2275  N   ASP A 311     -31.303  24.209 -57.885  1.00 27.26           N  
ANISOU 2275  N   ASP A 311     3487   3230   3640     -3   -458    386       N  
ATOM   2276  CA  ASP A 311     -30.881  25.414 -57.175  1.00 25.64           C  
ANISOU 2276  CA  ASP A 311     3284   2981   3478      9   -439    385       C  
ATOM   2277  C   ASP A 311     -29.473  25.814 -57.608  1.00 20.24           C  
ANISOU 2277  C   ASP A 311     2637   2291   2763    -24   -413    391       C  
ATOM   2278  O   ASP A 311     -28.522  25.045 -57.422  1.00 20.99           O  
ANISOU 2278  O   ASP A 311     2735   2413   2828    -45   -382    362       O  
ATOM   2279  CB  ASP A 311     -30.921  25.173 -55.669  1.00 25.59           C  
ANISOU 2279  CB  ASP A 311     3246   2971   3506     28   -408    337       C  
ATOM   2280  CG  ASP A 311     -32.312  24.834 -55.178  1.00 29.31           C  
ANISOU 2280  CG  ASP A 311     3677   3447   4012     60   -425    329       C  
ATOM   2281  OD1 ASP A 311     -33.268  25.507 -55.612  1.00 27.21           O  
ANISOU 2281  OD1 ASP A 311     3401   3159   3777     81   -458    362       O  
ATOM   2282  OD2 ASP A 311     -32.450  23.883 -54.380  1.00 27.24           O  
ANISOU 2282  OD2 ASP A 311     3393   3209   3747     62   -406    294       O  
ATOM   2283  N   ILE A 312     -29.335  27.004 -58.189  1.00 20.11           N  
ANISOU 2283  N   ILE A 312     2647   2237   2755    -28   -424    430       N  
ATOM   2284  CA  ILE A 312     -28.003  27.480 -58.549  1.00 21.93           C  
ANISOU 2284  CA  ILE A 312     2911   2459   2964    -63   -396    436       C  
ATOM   2285  C   ILE A 312     -27.202  27.716 -57.276  1.00 20.81           C  
ANISOU 2285  C   ILE A 312     2752   2303   2853    -64   -358    392       C  
ATOM   2286  O   ILE A 312     -27.682  28.359 -56.332  1.00 18.57           O  
ANISOU 2286  O   ILE A 312     2451   1986   2619    -37   -358    377       O  
ATOM   2287  CB  ILE A 312     -28.080  28.754 -59.400  1.00 22.80           C  
ANISOU 2287  CB  ILE A 312     3056   2527   3081    -69   -416    490       C  
ATOM   2288  CG1 ILE A 312     -28.588  28.426 -60.805  1.00 24.07           C  
ANISOU 2288  CG1 ILE A 312     3244   2711   3192    -80   -453    535       C  
ATOM   2289  CG2 ILE A 312     -26.699  29.437 -59.457  1.00 20.94           C  
ANISOU 2289  CG2 ILE A 312     2847   2271   2838   -105   -378    490       C  
ATOM   2290  CD1 ILE A 312     -29.100  29.648 -61.555  1.00 28.72           C  
ANISOU 2290  CD1 ILE A 312     3862   3254   3795    -72   -488    597       C  
ATOM   2291  N   LYS A 313     -25.979  27.189 -57.244  1.00 17.40           N  
ANISOU 2291  N   LYS A 313     2323   1896   2391    -94   -325    369       N  
ATOM   2292  CA  LYS A 313     -25.125  27.346 -56.071  1.00 20.74           C  
ANISOU 2292  CA  LYS A 313     2729   2313   2839    -99   -295    328       C  
ATOM   2293  C   LYS A 313     -24.821  28.814 -55.787  1.00 20.32           C  
ANISOU 2293  C   LYS A 313     2691   2206   2825   -105   -289    338       C  
ATOM   2294  O   LYS A 313     -24.451  29.580 -56.684  1.00 21.11           O  
ANISOU 2294  O   LYS A 313     2822   2283   2916   -127   -290    375       O  
ATOM   2295  CB  LYS A 313     -23.819  26.574 -56.259  1.00 17.95           C  
ANISOU 2295  CB  LYS A 313     2374   1997   2450   -130   -265    309       C  
ATOM   2296  CG  LYS A 313     -22.834  26.748 -55.104  1.00 19.26           C  
ANISOU 2296  CG  LYS A 313     2520   2159   2639   -139   -240    270       C  
ATOM   2297  CD  LYS A 313     -23.347  26.157 -53.801  1.00 18.66           C  
ANISOU 2297  CD  LYS A 313     2416   2093   2581   -110   -244    231       C  
ATOM   2298  CE  LYS A 313     -22.254  26.221 -52.739  1.00 17.14           C  
ANISOU 2298  CE  LYS A 313     2207   1904   2401   -124   -224    194       C  
ATOM   2299  NZ  LYS A 313     -22.743  25.763 -51.411  1.00 18.30           N  
ANISOU 2299  NZ  LYS A 313     2334   2058   2561    -98   -227    159       N  
ATOM   2300  N   GLU A 314     -24.981  29.204 -54.526  1.00 18.79           N  
ANISOU 2300  N   GLU A 314     2480   1989   2671    -87   -283    305       N  
ATOM   2301  CA  GLU A 314     -24.595  30.525 -54.055  1.00 20.51           C  
ANISOU 2301  CA  GLU A 314     2711   2153   2927    -96   -273    302       C  
ATOM   2302  C   GLU A 314     -23.678  30.389 -52.854  1.00 19.80           C  
ANISOU 2302  C   GLU A 314     2605   2073   2845   -110   -248    251       C  
ATOM   2303  O   GLU A 314     -23.868  29.510 -52.012  1.00 18.82           O  
ANISOU 2303  O   GLU A 314     2456   1980   2713    -94   -246    217       O  
ATOM   2304  CB  GLU A 314     -25.806  31.359 -53.654  1.00 20.73           C  
ANISOU 2304  CB  GLU A 314     2740   2132   3003    -57   -290    309       C  
ATOM   2305  CG  GLU A 314     -26.809  31.484 -54.746  1.00 25.78           C  
ANISOU 2305  CG  GLU A 314     3391   2765   3641    -37   -322    360       C  
ATOM   2306  CD  GLU A 314     -27.997  32.323 -54.346  1.00 29.32           C  
ANISOU 2306  CD  GLU A 314     3832   3163   4146      6   -338    368       C  
ATOM   2307  OE1 GLU A 314     -28.016  32.845 -53.209  1.00 31.05           O  
ANISOU 2307  OE1 GLU A 314     4042   3351   4403     19   -319    331       O  
ATOM   2308  OE2 GLU A 314     -28.906  32.463 -55.186  1.00 31.41           O  
ANISOU 2308  OE2 GLU A 314     4100   3420   4416     27   -371    412       O  
ATOM   2309  N   ILE A 315     -22.681  31.258 -52.775  1.00 19.67           N  
ANISOU 2309  N   ILE A 315     2602   2029   2841   -143   -233    248       N  
ATOM   2310  CA  ILE A 315     -21.850  31.354 -51.588  1.00 19.87           C  
ANISOU 2310  CA  ILE A 315     2614   2058   2879   -160   -217    200       C  
ATOM   2311  C   ILE A 315     -21.902  32.797 -51.120  1.00 21.33           C  
ANISOU 2311  C   ILE A 315     2820   2176   3108   -165   -214    195       C  
ATOM   2312  O   ILE A 315     -21.525  33.711 -51.866  1.00 19.13           O  
ANISOU 2312  O   ILE A 315     2567   1862   2841   -190   -210    226       O  
ATOM   2313  CB  ILE A 315     -20.412  30.894 -51.849  1.00 19.47           C  
ANISOU 2313  CB  ILE A 315     2551   2044   2803   -201   -200    193       C  
ATOM   2314  CG1 ILE A 315     -20.424  29.408 -52.249  1.00 20.46           C  
ANISOU 2314  CG1 ILE A 315     2656   2230   2888   -190   -200    194       C  
ATOM   2315  CG2 ILE A 315     -19.547  31.136 -50.607  1.00 16.67           C  
ANISOU 2315  CG2 ILE A 315     2180   1689   2465   -220   -191    147       C  
ATOM   2316  CD1 ILE A 315     -19.068  28.802 -52.394  1.00 18.67           C  
ANISOU 2316  CD1 ILE A 315     2409   2042   2642   -221   -181    182       C  
ATOM   2317  N   ASN A 316     -22.404  32.998 -49.902  1.00 21.81           N  
ANISOU 2317  N   ASN A 316     2874   2219   3192   -143   -213    156       N  
ATOM   2318  CA  ASN A 316     -22.550  34.327 -49.311  1.00 20.67           C  
ANISOU 2318  CA  ASN A 316     2753   2010   3092   -144   -207    141       C  
ATOM   2319  C   ASN A 316     -23.246  35.283 -50.278  1.00 20.85           C  
ANISOU 2319  C   ASN A 316     2803   1976   3144   -130   -216    190       C  
ATOM   2320  O   ASN A 316     -22.771  36.386 -50.552  1.00 20.95           O  
ANISOU 2320  O   ASN A 316     2843   1937   3181   -155   -210    204       O  
ATOM   2321  CB  ASN A 316     -21.193  34.880 -48.870  1.00 21.41           C  
ANISOU 2321  CB  ASN A 316     2852   2093   3189   -195   -194    114       C  
ATOM   2322  CG  ASN A 316     -21.320  36.142 -48.021  1.00 25.05           C  
ANISOU 2322  CG  ASN A 316     3337   2486   3693   -198   -186     85       C  
ATOM   2323  OD1 ASN A 316     -22.341  36.371 -47.368  1.00 24.22           O  
ANISOU 2323  OD1 ASN A 316     3238   2356   3610   -159   -185     66       O  
ATOM   2324  ND2 ASN A 316     -20.286  36.963 -48.032  1.00 23.65           N  
ANISOU 2324  ND2 ASN A 316     3175   2281   3530   -246   -177     78       N  
ATOM   2325  N   GLY A 317     -24.373  34.832 -50.826  1.00 19.87           N  
ANISOU 2325  N   GLY A 317     2670   1863   3016    -90   -234    220       N  
ATOM   2326  CA  GLY A 317     -25.219  35.687 -51.635  1.00 19.74           C  
ANISOU 2326  CA  GLY A 317     2676   1795   3031    -66   -250    268       C  
ATOM   2327  C   GLY A 317     -24.794  35.898 -53.075  1.00 22.59           C  
ANISOU 2327  C   GLY A 317     3061   2153   3368    -93   -261    327       C  
ATOM   2328  O   GLY A 317     -25.466  36.651 -53.791  1.00 20.64           O  
ANISOU 2328  O   GLY A 317     2836   1862   3145    -74   -279    374       O  
ATOM   2329  N   ASN A 318     -23.711  35.269 -53.529  1.00 18.86           N  
ANISOU 2329  N   ASN A 318     2586   1728   2851   -135   -249    328       N  
ATOM   2330  CA  ASN A 318     -23.288  35.344 -54.923  1.00 17.67           C  
ANISOU 2330  CA  ASN A 318     2461   1583   2668   -164   -253    382       C  
ATOM   2331  C   ASN A 318     -23.510  33.995 -55.579  1.00 20.97           C  
ANISOU 2331  C   ASN A 318     2862   2070   3034   -157   -264    392       C  
ATOM   2332  O   ASN A 318     -23.080  32.974 -55.038  1.00 20.97           O  
ANISOU 2332  O   ASN A 318     2834   2122   3013   -161   -252    353       O  
ATOM   2333  CB  ASN A 318     -21.810  35.728 -55.042  1.00 15.84           C  
ANISOU 2333  CB  ASN A 318     2241   1349   2427   -222   -224    375       C  
ATOM   2334  CG  ASN A 318     -21.558  37.199 -54.764  1.00 18.52           C  
ANISOU 2334  CG  ASN A 318     2610   1612   2815   -239   -215    380       C  
ATOM   2335  OD1 ASN A 318     -20.727  37.554 -53.923  1.00 22.79           O  
ANISOU 2335  OD1 ASN A 318     3144   2142   3375   -267   -196    338       O  
ATOM   2336  ND2 ASN A 318     -22.251  38.057 -55.490  1.00 15.97           N  
ANISOU 2336  ND2 ASN A 318     2321   1235   2511   -223   -232    431       N  
ATOM   2337  N   LYS A 319     -24.169  33.988 -56.739  1.00 19.73           N  
ANISOU 2337  N   LYS A 319     2726   1913   2857   -147   -289    445       N  
ATOM   2338  CA  LYS A 319     -24.248  32.764 -57.530  1.00 20.31           C  
ANISOU 2338  CA  LYS A 319     2793   2050   2874   -151   -297    456       C  
ATOM   2339  C   LYS A 319     -22.872  32.420 -58.083  1.00 23.31           C  
ANISOU 2339  C   LYS A 319     3183   2462   3213   -202   -265    454       C  
ATOM   2340  O   LYS A 319     -22.116  33.299 -58.504  1.00 21.50           O  
ANISOU 2340  O   LYS A 319     2981   2202   2987   -237   -247    476       O  
ATOM   2341  CB  LYS A 319     -25.255  32.911 -58.672  1.00 25.23           C  
ANISOU 2341  CB  LYS A 319     3440   2666   3482   -134   -336    514       C  
ATOM   2342  CG  LYS A 319     -26.698  33.113 -58.211  1.00 24.43           C  
ANISOU 2342  CG  LYS A 319     3318   2539   3425    -80   -370    518       C  
ATOM   2343  CD  LYS A 319     -27.673  32.862 -59.354  1.00 29.55           C  
ANISOU 2343  CD  LYS A 319     3978   3202   4047    -64   -415    570       C  
ATOM   2344  CE  LYS A 319     -29.049  33.475 -59.102  1.00 28.44           C  
ANISOU 2344  CE  LYS A 319     3821   3021   3964    -12   -452    590       C  
ATOM   2345  NZ  LYS A 319     -29.314  33.788 -57.681  1.00 34.44           N  
ANISOU 2345  NZ  LYS A 319     4548   3752   4784     19   -431    540       N  
ATOM   2346  N   ILE A 320     -22.544  31.130 -58.058  1.00 21.68           N  
ANISOU 2346  N   ILE A 320     2953   2316   2970   -206   -253    426       N  
ATOM   2347  CA  ILE A 320     -21.206  30.628 -58.345  1.00 21.17           C  
ANISOU 2347  CA  ILE A 320     2883   2287   2874   -247   -217    411       C  
ATOM   2348  C   ILE A 320     -21.221  29.934 -59.699  1.00 20.22           C  
ANISOU 2348  C   ILE A 320     2786   2202   2693   -262   -216    442       C  
ATOM   2349  O   ILE A 320     -22.201  29.272 -60.058  1.00 20.63           O  
ANISOU 2349  O   ILE A 320     2840   2274   2724   -237   -245    452       O  
ATOM   2350  CB  ILE A 320     -20.752  29.655 -57.237  1.00 22.14           C  
ANISOU 2350  CB  ILE A 320     2962   2447   3003   -237   -202    354       C  
ATOM   2351  CG1 ILE A 320     -20.902  30.311 -55.859  1.00 21.93           C  
ANISOU 2351  CG1 ILE A 320     2918   2386   3028   -221   -207    322       C  
ATOM   2352  CG2 ILE A 320     -19.330  29.124 -57.487  1.00 20.61           C  
ANISOU 2352  CG2 ILE A 320     2754   2290   2786   -275   -165    337       C  
ATOM   2353  CD1 ILE A 320     -19.976  31.480 -55.603  1.00 20.42           C  
ANISOU 2353  CD1 ILE A 320     2737   2156   2867   -256   -189    320       C  
ATOM   2354  N   THR A 321     -20.129  30.076 -60.445  1.00 21.18           N  
ANISOU 2354  N   THR A 321     2925   2333   2788   -306   -183    455       N  
ATOM   2355  CA  THR A 321     -19.947  29.349 -61.692  1.00 21.82           C  
ANISOU 2355  CA  THR A 321     3030   2454   2806   -327   -171    475       C  
ATOM   2356  C   THR A 321     -19.136  28.087 -61.444  1.00 20.35           C  
ANISOU 2356  C   THR A 321     2810   2320   2602   -332   -138    428       C  
ATOM   2357  O   THR A 321     -18.591  27.873 -60.359  1.00 16.77           O  
ANISOU 2357  O   THR A 321     2316   1873   2184   -325   -125    387       O  
ATOM   2358  CB  THR A 321     -19.233  30.213 -62.723  1.00 22.79           C  
ANISOU 2358  CB  THR A 321     3195   2557   2906   -373   -146    517       C  
ATOM   2359  OG1 THR A 321     -17.966  30.604 -62.179  1.00 22.45           O  
ANISOU 2359  OG1 THR A 321     3129   2508   2893   -404   -104    492       O  
ATOM   2360  CG2 THR A 321     -20.077  31.436 -63.072  1.00 25.46           C  
ANISOU 2360  CG2 THR A 321     3573   2840   3261   -365   -183    571       C  
ATOM   2361  N   CYS A 322     -19.029  27.261 -62.486  1.00 21.98           N  
ANISOU 2361  N   CYS A 322     3036   2563   2751   -346   -124    436       N  
ATOM   2362  CA  CYS A 322     -18.198  26.064 -62.371  1.00 20.34           C  
ANISOU 2362  CA  CYS A 322     2798   2401   2528   -351    -87    394       C  
ATOM   2363  C   CYS A 322     -16.762  26.426 -62.021  1.00 19.68           C  
ANISOU 2363  C   CYS A 322     2688   2318   2471   -381    -41    376       C  
ATOM   2364  O   CYS A 322     -16.155  25.803 -61.143  1.00 19.83           O  
ANISOU 2364  O   CYS A 322     2661   2357   2517   -370    -27    334       O  
ATOM   2365  CB  CYS A 322     -18.248  25.249 -63.660  1.00 21.44           C  
ANISOU 2365  CB  CYS A 322     2972   2574   2599   -367    -73    405       C  
ATOM   2366  SG  CYS A 322     -19.864  24.522 -63.947  1.00 20.61           S  
ANISOU 2366  SG  CYS A 322     2886   2480   2466   -333   -130    414       S  
ATOM   2367  N   ARG A 323     -16.203  27.445 -62.676  1.00 21.20           N  
ANISOU 2367  N   ARG A 323     2908   2488   2658   -420    -20    408       N  
ATOM   2368  CA  ARG A 323     -14.836  27.833 -62.344  1.00 23.93           C  
ANISOU 2368  CA  ARG A 323     3224   2835   3035   -454     24    390       C  
ATOM   2369  C   ARG A 323     -14.758  28.383 -60.929  1.00 18.59           C  
ANISOU 2369  C   ARG A 323     2510   2133   2422   -439      3    365       C  
ATOM   2370  O   ARG A 323     -13.768  28.151 -60.226  1.00 20.77           O  
ANISOU 2370  O   ARG A 323     2739   2425   2728   -448     25    330       O  
ATOM   2371  CB  ARG A 323     -14.288  28.848 -63.358  1.00 23.79           C  
ANISOU 2371  CB  ARG A 323     3246   2796   2999   -504     54    433       C  
ATOM   2372  CG  ARG A 323     -14.973  30.190 -63.354  1.00 26.02           C  
ANISOU 2372  CG  ARG A 323     3566   3019   3301   -507     20    475       C  
ATOM   2373  CD  ARG A 323     -14.516  31.042 -64.556  1.00 32.50           C  
ANISOU 2373  CD  ARG A 323     4439   3821   4090   -558     50    526       C  
ATOM   2374  NE  ARG A 323     -13.065  31.037 -64.712  1.00 27.49           N  
ANISOU 2374  NE  ARG A 323     3778   3206   3460   -605    113    508       N  
ATOM   2375  CZ  ARG A 323     -12.440  31.277 -65.856  1.00 31.60           C  
ANISOU 2375  CZ  ARG A 323     4333   3734   3939   -652    159    539       C  
ATOM   2376  NH1 ARG A 323     -13.110  31.589 -66.956  1.00 34.24           N  
ANISOU 2376  NH1 ARG A 323     4736   4055   4218   -662    146    591       N  
ATOM   2377  NH2 ARG A 323     -11.112  31.195 -65.900  1.00 35.19           N  
ANISOU 2377  NH2 ARG A 323     4753   4211   4408   -692    219    517       N  
ATOM   2378  N   GLY A 324     -15.798  29.095 -60.489  1.00 20.21           N  
ANISOU 2378  N   GLY A 324     2734   2297   2648   -415    -40    381       N  
ATOM   2379  CA  GLY A 324     -15.829  29.556 -59.111  1.00 21.54           C  
ANISOU 2379  CA  GLY A 324     2872   2440   2871   -400    -58    351       C  
ATOM   2380  C   GLY A 324     -15.914  28.408 -58.124  1.00 19.64           C  
ANISOU 2380  C   GLY A 324     2588   2236   2638   -365    -69    305       C  
ATOM   2381  O   GLY A 324     -15.278  28.437 -57.068  1.00 19.12           O  
ANISOU 2381  O   GLY A 324     2485   2173   2605   -367    -66    270       O  
ATOM   2382  N   LEU A 325     -16.700  27.382 -58.458  1.00 18.66           N  
ANISOU 2382  N   LEU A 325     2470   2139   2482   -335    -83    305       N  
ATOM   2383  CA  LEU A 325     -16.837  26.224 -57.578  1.00 15.24           C  
ANISOU 2383  CA  LEU A 325     2000   1737   2052   -303    -91    266       C  
ATOM   2384  C   LEU A 325     -15.507  25.490 -57.410  1.00 17.62           C  
ANISOU 2384  C   LEU A 325     2264   2076   2355   -318    -57    237       C  
ATOM   2385  O   LEU A 325     -15.193  24.997 -56.319  1.00 16.86           O  
ANISOU 2385  O   LEU A 325     2130   1994   2283   -301    -63    203       O  
ATOM   2386  CB  LEU A 325     -17.905  25.283 -58.133  1.00 17.85           C  
ANISOU 2386  CB  LEU A 325     2349   2087   2347   -275   -110    275       C  
ATOM   2387  CG  LEU A 325     -18.433  24.269 -57.110  1.00 21.86           C  
ANISOU 2387  CG  LEU A 325     2828   2614   2865   -238   -127    241       C  
ATOM   2388  CD1 LEU A 325     -19.218  25.002 -56.013  1.00 17.15           C  
ANISOU 2388  CD1 LEU A 325     2226   1984   2306   -215   -157    235       C  
ATOM   2389  CD2 LEU A 325     -19.290  23.215 -57.773  1.00 16.99           C  
ANISOU 2389  CD2 LEU A 325     2226   2020   2211   -220   -139    246       C  
ATOM   2390  N   VAL A 326     -14.713  25.411 -58.480  1.00 17.03           N  
ANISOU 2390  N   VAL A 326     2197   2017   2256   -349    -19    250       N  
ATOM   2391  CA  VAL A 326     -13.398  24.778 -58.407  1.00 20.35           C  
ANISOU 2391  CA  VAL A 326     2575   2471   2685   -364     19    224       C  
ATOM   2392  C   VAL A 326     -12.506  25.483 -57.390  1.00 20.68           C  
ANISOU 2392  C   VAL A 326     2578   2503   2777   -381     18    205       C  
ATOM   2393  O   VAL A 326     -11.791  24.833 -56.609  1.00 19.36           O  
ANISOU 2393  O   VAL A 326     2363   2361   2631   -370     21    173       O  
ATOM   2394  CB  VAL A 326     -12.748  24.751 -59.803  1.00 22.48           C  
ANISOU 2394  CB  VAL A 326     2865   2755   2920   -399     66    244       C  
ATOM   2395  CG1 VAL A 326     -11.265  24.459 -59.685  1.00 23.44           C  
ANISOU 2395  CG1 VAL A 326     2937   2905   3066   -420    110    219       C  
ATOM   2396  CG2 VAL A 326     -13.420  23.700 -60.676  1.00 21.14           C  
ANISOU 2396  CG2 VAL A 326     2726   2609   2699   -381     68    248       C  
ATOM   2397  N   GLU A 327     -12.512  26.817 -57.390  1.00 18.43           N  
ANISOU 2397  N   GLU A 327     2313   2178   2510   -409     13    224       N  
ATOM   2398  CA  GLU A 327     -11.665  27.539 -56.447  1.00 23.23           C  
ANISOU 2398  CA  GLU A 327     2887   2774   3164   -432     12    204       C  
ATOM   2399  C   GLU A 327     -12.085  27.259 -55.016  1.00 19.86           C  
ANISOU 2399  C   GLU A 327     2439   2348   2760   -397    -27    171       C  
ATOM   2400  O   GLU A 327     -11.243  27.190 -54.113  1.00 21.42           O  
ANISOU 2400  O   GLU A 327     2594   2560   2986   -406    -31    142       O  
ATOM   2401  CB  GLU A 327     -11.716  29.040 -56.702  1.00 21.11           C  
ANISOU 2401  CB  GLU A 327     2653   2456   2913   -467     12    230       C  
ATOM   2402  CG  GLU A 327     -11.337  29.466 -58.080  1.00 27.96           C  
ANISOU 2402  CG  GLU A 327     3550   3317   3755   -506     50    268       C  
ATOM   2403  CD  GLU A 327     -11.222  30.969 -58.169  1.00 31.86           C  
ANISOU 2403  CD  GLU A 327     4073   3758   4275   -545     52    292       C  
ATOM   2404  OE1 GLU A 327     -10.116  31.492 -57.917  1.00 36.18           O  
ANISOU 2404  OE1 GLU A 327     4591   4302   4853   -588     75    280       O  
ATOM   2405  OE2 GLU A 327     -12.248  31.628 -58.440  1.00 36.06           O  
ANISOU 2405  OE2 GLU A 327     4654   4247   4799   -532     28    323       O  
ATOM   2406  N   TYR A 328     -13.385  27.088 -54.791  1.00 20.39           N  
ANISOU 2406  N   TYR A 328     2534   2400   2813   -360    -57    177       N  
ATOM   2407  CA  TYR A 328     -13.858  26.833 -53.439  1.00 19.58           C  
ANISOU 2407  CA  TYR A 328     2416   2296   2726   -329    -89    147       C  
ATOM   2408  C   TYR A 328     -13.534  25.418 -52.992  1.00 21.66           C  
ANISOU 2408  C   TYR A 328     2644   2607   2980   -303    -89    122       C  
ATOM   2409  O   TYR A 328     -13.195  25.201 -51.823  1.00 18.52           O  
ANISOU 2409  O   TYR A 328     2218   2220   2599   -295   -107     93       O  
ATOM   2410  CB  TYR A 328     -15.350  27.100 -53.353  1.00 20.60           C  
ANISOU 2410  CB  TYR A 328     2582   2396   2849   -298   -115    160       C  
ATOM   2411  CG  TYR A 328     -15.630  28.521 -52.981  1.00 20.56           C  
ANISOU 2411  CG  TYR A 328     2600   2339   2874   -312   -125    166       C  
ATOM   2412  CD1 TYR A 328     -15.436  28.957 -51.677  1.00 22.11           C  
ANISOU 2412  CD1 TYR A 328     2782   2522   3098   -313   -139    132       C  
ATOM   2413  CD2 TYR A 328     -16.074  29.438 -53.930  1.00 23.41           C  
ANISOU 2413  CD2 TYR A 328     3000   2662   3234   -325   -122    204       C  
ATOM   2414  CE1 TYR A 328     -15.698  30.264 -51.316  1.00 20.97           C  
ANISOU 2414  CE1 TYR A 328     2661   2324   2981   -326   -146    132       C  
ATOM   2415  CE2 TYR A 328     -16.335  30.752 -53.580  1.00 22.72           C  
ANISOU 2415  CE2 TYR A 328     2934   2519   3178   -335   -131    210       C  
ATOM   2416  CZ  TYR A 328     -16.149  31.153 -52.270  1.00 24.16           C  
ANISOU 2416  CZ  TYR A 328     3103   2687   3391   -335   -141    171       C  
ATOM   2417  OH  TYR A 328     -16.404  32.448 -51.902  1.00 24.43           O  
ANISOU 2417  OH  TYR A 328     3162   2661   3458   -345   -146    171       O  
ATOM   2418  N   PHE A 329     -13.648  24.443 -53.901  1.00 19.24           N  
ANISOU 2418  N   PHE A 329     2342   2325   2643   -291    -72    133       N  
ATOM   2419  CA  PHE A 329     -13.113  23.116 -53.630  1.00 22.12           C  
ANISOU 2419  CA  PHE A 329     2671   2730   3003   -271    -64    111       C  
ATOM   2420  C   PHE A 329     -11.694  23.220 -53.095  1.00 19.25           C  
ANISOU 2420  C   PHE A 329     2259   2384   2671   -292    -54     91       C  
ATOM   2421  O   PHE A 329     -11.368  22.674 -52.041  1.00 17.90           O  
ANISOU 2421  O   PHE A 329     2056   2231   2515   -274    -73     68       O  
ATOM   2422  CB  PHE A 329     -13.114  22.279 -54.906  1.00 23.08           C  
ANISOU 2422  CB  PHE A 329     2807   2872   3092   -269    -34    124       C  
ATOM   2423  CG  PHE A 329     -14.134  21.176 -54.930  1.00 23.64           C  
ANISOU 2423  CG  PHE A 329     2894   2952   3137   -232    -49    121       C  
ATOM   2424  CD1 PHE A 329     -14.027  20.101 -54.077  1.00 28.46           C  
ANISOU 2424  CD1 PHE A 329     3477   3581   3754   -202    -59     97       C  
ATOM   2425  CD2 PHE A 329     -15.174  21.205 -55.847  1.00 26.60           C  
ANISOU 2425  CD2 PHE A 329     3312   3316   3478   -230    -54    144       C  
ATOM   2426  CE1 PHE A 329     -14.951  19.066 -54.125  1.00 28.72           C  
ANISOU 2426  CE1 PHE A 329     3527   3620   3765   -173    -69     94       C  
ATOM   2427  CE2 PHE A 329     -16.105  20.176 -55.899  1.00 27.15           C  
ANISOU 2427  CE2 PHE A 329     3394   3394   3526   -202    -67    139       C  
ATOM   2428  CZ  PHE A 329     -15.985  19.108 -55.030  1.00 27.68           C  
ANISOU 2428  CZ  PHE A 329     3436   3479   3604   -174    -73    113       C  
ATOM   2429  N   LYS A 330     -10.838  23.945 -53.814  1.00 19.41           N  
ANISOU 2429  N   LYS A 330     2272   2401   2702   -333    -24    103       N  
ATOM   2430  CA  LYS A 330      -9.442  24.060 -53.408  1.00 21.88           C  
ANISOU 2430  CA  LYS A 330     2531   2734   3049   -357    -12     85       C  
ATOM   2431  C   LYS A 330      -9.315  24.802 -52.084  1.00 20.89           C  
ANISOU 2431  C   LYS A 330     2391   2593   2953   -366    -49     66       C  
ATOM   2432  O   LYS A 330      -8.587  24.367 -51.182  1.00 19.19           O  
ANISOU 2432  O   LYS A 330     2130   2402   2758   -360    -66     42       O  
ATOM   2433  CB  LYS A 330      -8.638  24.761 -54.507  1.00 21.17           C  
ANISOU 2433  CB  LYS A 330     2440   2640   2964   -404     32    103       C  
ATOM   2434  CG  LYS A 330      -8.520  23.943 -55.791  1.00 22.98           C  
ANISOU 2434  CG  LYS A 330     2678   2891   3161   -400     76    115       C  
ATOM   2435  CD  LYS A 330      -8.092  24.782 -56.986  1.00 26.59           C  
ANISOU 2435  CD  LYS A 330     3157   3337   3608   -448    120    141       C  
ATOM   2436  CE  LYS A 330      -7.909  23.890 -58.222  1.00 28.52           C  
ANISOU 2436  CE  LYS A 330     3413   3608   3816   -445    167    147       C  
ATOM   2437  NZ  LYS A 330      -7.821  24.674 -59.505  1.00 28.48           N  
ANISOU 2437  NZ  LYS A 330     3450   3588   3782   -490    207    180       N  
ATOM   2438  N   ALA A 331     -10.023  25.926 -51.947  1.00 20.87           N  
ANISOU 2438  N   ALA A 331     2429   2548   2951   -380    -64     75       N  
ATOM   2439  CA  ALA A 331      -9.871  26.743 -50.748  1.00 23.05           C  
ANISOU 2439  CA  ALA A 331     2698   2805   3254   -395    -94     53       C  
ATOM   2440  C   ALA A 331     -10.370  26.005 -49.521  1.00 20.48           C  
ANISOU 2440  C   ALA A 331     2367   2495   2921   -355   -130     29       C  
ATOM   2441  O   ALA A 331      -9.709  26.001 -48.477  1.00 17.25           O  
ANISOU 2441  O   ALA A 331     1927   2101   2528   -363   -154      4       O  
ATOM   2442  CB  ALA A 331     -10.610  28.069 -50.914  1.00 20.87           C  
ANISOU 2442  CB  ALA A 331     2472   2474   2982   -413    -98     68       C  
ATOM   2443  N   TYR A 332     -11.525  25.352 -49.638  1.00 17.64           N  
ANISOU 2443  N   TYR A 332     2036   2133   2533   -315   -136     38       N  
ATOM   2444  CA  TYR A 332     -12.105  24.666 -48.494  1.00 18.85           C  
ANISOU 2444  CA  TYR A 332     2189   2297   2676   -279   -166     18       C  
ATOM   2445  C   TYR A 332     -11.241  23.493 -48.055  1.00 16.70           C  
ANISOU 2445  C   TYR A 332     1872   2069   2405   -265   -172      5       C  
ATOM   2446  O   TYR A 332     -10.975  23.328 -46.863  1.00 19.53           O  
ANISOU 2446  O   TYR A 332     2213   2439   2767   -259   -201    -17       O  
ATOM   2447  CB  TYR A 332     -13.515  24.201 -48.834  1.00 14.76           C  
ANISOU 2447  CB  TYR A 332     1708   1768   2133   -244   -167     32       C  
ATOM   2448  CG  TYR A 332     -14.539  25.307 -48.843  1.00 16.03           C  
ANISOU 2448  CG  TYR A 332     1909   1883   2297   -246   -173     41       C  
ATOM   2449  CD1 TYR A 332     -14.370  26.458 -48.068  1.00 18.93           C  
ANISOU 2449  CD1 TYR A 332     2284   2220   2687   -268   -184     24       C  
ATOM   2450  CD2 TYR A 332     -15.688  25.191 -49.601  1.00 17.11           C  
ANISOU 2450  CD2 TYR A 332     2076   2006   2419   -225   -169     64       C  
ATOM   2451  CE1 TYR A 332     -15.321  27.454 -48.064  1.00 15.83           C  
ANISOU 2451  CE1 TYR A 332     1928   1781   2304   -265   -187     31       C  
ATOM   2452  CE2 TYR A 332     -16.647  26.181 -49.607  1.00 17.15           C  
ANISOU 2452  CE2 TYR A 332     2113   1968   2434   -222   -177     74       C  
ATOM   2453  CZ  TYR A 332     -16.465  27.303 -48.842  1.00 16.54           C  
ANISOU 2453  CZ  TYR A 332     2043   1858   2382   -239   -183     57       C  
ATOM   2454  OH  TYR A 332     -17.445  28.271 -48.874  1.00 19.30           O  
ANISOU 2454  OH  TYR A 332     2425   2162   2748   -231   -188     67       O  
ATOM   2455  N   ILE A 333     -10.789  22.667 -49.001  1.00 19.53           N  
ANISOU 2455  N   ILE A 333     2211   2450   2758   -257   -145     17       N  
ATOM   2456  CA  ILE A 333      -9.988  21.509 -48.612  1.00 21.31           C  
ANISOU 2456  CA  ILE A 333     2392   2713   2991   -237   -150      6       C  
ATOM   2457  C   ILE A 333      -8.681  21.963 -47.972  1.00 19.23           C  
ANISOU 2457  C   ILE A 333     2080   2467   2761   -265   -163    -10       C  
ATOM   2458  O   ILE A 333      -8.207  21.359 -47.006  1.00 21.17           O  
ANISOU 2458  O   ILE A 333     2294   2736   3014   -249   -192    -24       O  
ATOM   2459  CB  ILE A 333      -9.754  20.577 -49.816  1.00 21.05           C  
ANISOU 2459  CB  ILE A 333     2351   2698   2950   -224   -111     18       C  
ATOM   2460  CG1 ILE A 333     -11.102  20.073 -50.335  1.00 26.28           C  
ANISOU 2460  CG1 ILE A 333     3062   3346   3577   -198   -107     30       C  
ATOM   2461  CG2 ILE A 333      -8.915  19.356 -49.396  1.00 22.09           C  
ANISOU 2461  CG2 ILE A 333     2435   2863   3096   -197   -115      6       C  
ATOM   2462  CD1 ILE A 333     -11.038  19.276 -51.635  1.00 28.28           C  
ANISOU 2462  CD1 ILE A 333     3322   3612   3813   -192    -69     41       C  
ATOM   2463  N   LYS A 334      -8.093  23.048 -48.479  1.00 19.52           N  
ANISOU 2463  N   LYS A 334     2108   2490   2817   -310   -145     -6       N  
ATOM   2464  CA  LYS A 334      -6.854  23.549 -47.891  1.00 23.91           C  
ANISOU 2464  CA  LYS A 334     2615   3062   3409   -343   -159    -23       C  
ATOM   2465  C   LYS A 334      -7.041  23.890 -46.414  1.00 22.14           C  
ANISOU 2465  C   LYS A 334     2397   2833   3183   -344   -210    -45       C  
ATOM   2466  O   LYS A 334      -6.137  23.676 -45.599  1.00 22.50           O  
ANISOU 2466  O   LYS A 334     2397   2906   3247   -350   -239    -60       O  
ATOM   2467  CB  LYS A 334      -6.361  24.766 -48.675  1.00 24.52           C  
ANISOU 2467  CB  LYS A 334     2693   3117   3506   -397   -130    -14       C  
ATOM   2468  CG  LYS A 334      -4.973  25.237 -48.280  1.00 31.45           C  
ANISOU 2468  CG  LYS A 334     3510   4014   4425   -438   -137    -29       C  
ATOM   2469  CD  LYS A 334      -4.567  26.458 -49.092  1.00 37.03           C  
ANISOU 2469  CD  LYS A 334     4224   4694   5151   -495   -103    -18       C  
ATOM   2470  CE  LYS A 334      -3.301  27.105 -48.521  1.00 50.08           C  
ANISOU 2470  CE  LYS A 334     5821   6361   6848   -544   -117    -38       C  
ATOM   2471  NZ  LYS A 334      -3.226  28.566 -48.830  1.00 53.47           N  
ANISOU 2471  NZ  LYS A 334     6277   6746   7292   -603   -103    -33       N  
ATOM   2472  N   ILE A 335      -8.219  24.402 -46.046  1.00 19.91           N  
ANISOU 2472  N   ILE A 335     2171   2516   2877   -336   -222    -47       N  
ATOM   2473  CA  ILE A 335      -8.495  24.684 -44.642  1.00 20.47           C  
ANISOU 2473  CA  ILE A 335     2256   2582   2939   -335   -264    -71       C  
ATOM   2474  C   ILE A 335      -8.569  23.387 -43.845  1.00 21.87           C  
ANISOU 2474  C   ILE A 335     2420   2794   3097   -293   -290    -75       C  
ATOM   2475  O   ILE A 335      -8.034  23.285 -42.733  1.00 22.07           O  
ANISOU 2475  O   ILE A 335     2425   2838   3122   -298   -329    -93       O  
ATOM   2476  CB  ILE A 335      -9.781  25.520 -44.514  1.00 22.58           C  
ANISOU 2476  CB  ILE A 335     2586   2804   3191   -333   -261    -73       C  
ATOM   2477  CG1 ILE A 335      -9.518  26.934 -45.044  1.00 27.20           C  
ANISOU 2477  CG1 ILE A 335     3183   3352   3801   -380   -244    -71       C  
ATOM   2478  CG2 ILE A 335     -10.249  25.584 -43.060  1.00 22.04           C  
ANISOU 2478  CG2 ILE A 335     2538   2732   3103   -323   -297   -100       C  
ATOM   2479  CD1 ILE A 335     -10.734  27.811 -45.073  1.00 25.11           C  
ANISOU 2479  CD1 ILE A 335     2976   3036   3530   -375   -238    -68       C  
ATOM   2480  N   TYR A 336      -9.204  22.365 -44.411  1.00 17.97           N  
ANISOU 2480  N   TYR A 336     1937   2305   2585   -253   -272    -58       N  
ATOM   2481  CA  TYR A 336      -9.293  21.088 -43.716  1.00 20.84           C  
ANISOU 2481  CA  TYR A 336     2292   2695   2932   -213   -294    -58       C  
ATOM   2482  C   TYR A 336      -7.974  20.330 -43.708  1.00 21.59           C  
ANISOU 2482  C   TYR A 336     2325   2828   3052   -208   -302    -57       C  
ATOM   2483  O   TYR A 336      -7.767  19.487 -42.826  1.00 23.29           O  
ANISOU 2483  O   TYR A 336     2525   3064   3259   -182   -334    -59       O  
ATOM   2484  CB  TYR A 336     -10.394  20.248 -44.354  1.00 17.89           C  
ANISOU 2484  CB  TYR A 336     1951   2312   2535   -177   -270    -42       C  
ATOM   2485  CG  TYR A 336     -11.769  20.807 -44.045  1.00 18.36           C  
ANISOU 2485  CG  TYR A 336     2064   2341   2572   -172   -272    -45       C  
ATOM   2486  CD1 TYR A 336     -12.130  21.110 -42.737  1.00 20.96           C  
ANISOU 2486  CD1 TYR A 336     2412   2664   2886   -173   -301    -64       C  
ATOM   2487  CD2 TYR A 336     -12.679  21.058 -45.051  1.00 16.05           C  
ANISOU 2487  CD2 TYR A 336     1801   2023   2273   -169   -244    -30       C  
ATOM   2488  CE1 TYR A 336     -13.371  21.630 -42.441  1.00 18.92           C  
ANISOU 2488  CE1 TYR A 336     2199   2377   2612   -167   -297    -69       C  
ATOM   2489  CE2 TYR A 336     -13.932  21.565 -44.765  1.00 19.89           C  
ANISOU 2489  CE2 TYR A 336     2330   2482   2747   -162   -247    -32       C  
ATOM   2490  CZ  TYR A 336     -14.268  21.849 -43.459  1.00 16.49           C  
ANISOU 2490  CZ  TYR A 336     1914   2046   2306   -160   -270    -53       C  
ATOM   2491  OH  TYR A 336     -15.506  22.361 -43.168  1.00 18.52           O  
ANISOU 2491  OH  TYR A 336     2208   2274   2555   -150   -266    -57       O  
ATOM   2492  N   GLN A 337      -7.090  20.593 -44.676  1.00 19.75           N  
ANISOU 2492  N   GLN A 337     2053   2601   2849   -230   -272    -51       N  
ATOM   2493  CA  GLN A 337      -5.788  19.932 -44.716  1.00 24.28           C  
ANISOU 2493  CA  GLN A 337     2560   3211   3456   -225   -275    -51       C  
ATOM   2494  C   GLN A 337      -4.836  20.451 -43.648  1.00 26.20           C  
ANISOU 2494  C   GLN A 337     2761   3473   3720   -252   -321    -68       C  
ATOM   2495  O   GLN A 337      -3.861  19.764 -43.324  1.00 30.04           O  
ANISOU 2495  O   GLN A 337     3190   3992   4232   -237   -341    -67       O  
ATOM   2496  CB  GLN A 337      -5.139  20.104 -46.094  1.00 22.75           C  
ANISOU 2496  CB  GLN A 337     2337   3019   3288   -244   -222    -43       C  
ATOM   2497  CG  GLN A 337      -5.699  19.182 -47.161  1.00 19.22           C  
ANISOU 2497  CG  GLN A 337     1912   2568   2823   -211   -179    -28       C  
ATOM   2498  CD  GLN A 337      -5.261  19.582 -48.547  1.00 21.47           C  
ANISOU 2498  CD  GLN A 337     2188   2850   3121   -239   -123    -20       C  
ATOM   2499  OE1 GLN A 337      -5.025  20.763 -48.823  1.00 23.68           O  
ANISOU 2499  OE1 GLN A 337     2471   3117   3411   -285   -113    -19       O  
ATOM   2500  NE2 GLN A 337      -5.156  18.604 -49.434  1.00 22.24           N  
ANISOU 2500  NE2 GLN A 337     2277   2957   3215   -213    -84    -15       N  
ATOM   2501  N   GLY A 338      -5.075  21.649 -43.121  1.00 25.24           N  
ANISOU 2501  N   GLY A 338     2667   3331   3591   -291   -340    -82       N  
ATOM   2502  CA  GLY A 338      -4.264  22.212 -42.064  1.00 24.98           C  
ANISOU 2502  CA  GLY A 338     2605   3315   3573   -323   -388   -102       C  
ATOM   2503  C   GLY A 338      -4.841  21.966 -40.686  1.00 29.32           C  
ANISOU 2503  C   GLY A 338     3189   3867   4083   -305   -438   -114       C  
ATOM   2504  O   GLY A 338      -5.632  21.045 -40.459  1.00 25.93           O  
ANISOU 2504  O   GLY A 338     2791   3437   3623   -260   -439   -103       O  
ATOM   2505  N   GLU A 339      -4.430  22.815 -39.743  1.00 29.80           N  
ANISOU 2505  N   GLU A 339     3248   3930   4143   -344   -478   -137       N  
ATOM   2506  CA  GLU A 339      -4.882  22.689 -38.364  1.00 30.38           C  
ANISOU 2506  CA  GLU A 339     3359   4009   4175   -336   -527   -152       C  
ATOM   2507  C   GLU A 339      -5.422  24.007 -37.821  1.00 28.17           C  
ANISOU 2507  C   GLU A 339     3132   3694   3877   -377   -532   -181       C  
ATOM   2508  O   GLU A 339      -5.458  24.200 -36.601  1.00 29.25           O  
ANISOU 2508  O   GLU A 339     3291   3839   3983   -390   -576   -203       O  
ATOM   2509  CB  GLU A 339      -3.755  22.161 -37.474  1.00 29.70           C  
ANISOU 2509  CB  GLU A 339     3219   3969   4098   -337   -586   -154       C  
ATOM   2510  CG  GLU A 339      -3.126  20.872 -37.980  1.00 26.65           C  
ANISOU 2510  CG  GLU A 339     2774   3613   3738   -293   -581   -127       C  
ATOM   2511  CD  GLU A 339      -4.101  19.689 -37.988  1.00 36.35           C  
ANISOU 2511  CD  GLU A 339     4044   4835   4933   -234   -567   -106       C  
ATOM   2512  OE1 GLU A 339      -5.070  19.694 -37.196  1.00 34.01           O  
ANISOU 2512  OE1 GLU A 339     3809   4525   4588   -226   -581   -113       O  
ATOM   2513  OE2 GLU A 339      -3.895  18.750 -38.789  1.00 32.29           O  
ANISOU 2513  OE2 GLU A 339     3499   4328   4442   -198   -539    -85       O  
ATOM   2514  N   GLU A 340      -5.860  24.917 -38.697  1.00 30.81           N  
ANISOU 2514  N   GLU A 340     3490   3989   4227   -398   -487   -182       N  
ATOM   2515  CA  GLU A 340      -6.524  26.123 -38.212  1.00 29.59           C  
ANISOU 2515  CA  GLU A 340     3392   3792   4058   -429   -486   -208       C  
ATOM   2516  C   GLU A 340      -7.778  25.789 -37.421  1.00 27.06           C  
ANISOU 2516  C   GLU A 340     3133   3460   3689   -394   -491   -216       C  
ATOM   2517  O   GLU A 340      -8.109  26.491 -36.463  1.00 33.43           O  
ANISOU 2517  O   GLU A 340     3980   4249   4473   -415   -509   -247       O  
ATOM   2518  CB  GLU A 340      -6.886  27.047 -39.373  1.00 32.29           C  
ANISOU 2518  CB  GLU A 340     3753   4089   4427   -448   -436   -199       C  
ATOM   2519  CG  GLU A 340      -5.816  27.173 -40.432  1.00 43.78           C  
ANISOU 2519  CG  GLU A 340     5151   5557   5927   -474   -415   -182       C  
ATOM   2520  CD  GLU A 340      -6.099  26.307 -41.663  1.00 50.85           C  
ANISOU 2520  CD  GLU A 340     6036   6460   6826   -435   -372   -147       C  
ATOM   2521  OE1 GLU A 340      -6.219  25.055 -41.517  1.00 33.46           O  
ANISOU 2521  OE1 GLU A 340     3819   4288   4606   -390   -381   -136       O  
ATOM   2522  OE2 GLU A 340      -6.201  26.895 -42.776  1.00 49.86           O  
ANISOU 2522  OE2 GLU A 340     5920   6307   6719   -453   -331   -131       O  
ATOM   2523  N   LEU A 341      -8.484  24.724 -37.799  1.00 26.06           N  
ANISOU 2523  N   LEU A 341     3014   3340   3546   -344   -471   -191       N  
ATOM   2524  CA  LEU A 341      -9.773  24.444 -37.187  1.00 25.69           C  
ANISOU 2524  CA  LEU A 341     3024   3279   3458   -313   -466   -196       C  
ATOM   2525  C   LEU A 341      -9.632  23.449 -36.041  1.00 24.83           C  
ANISOU 2525  C   LEU A 341     2915   3207   3311   -292   -506   -197       C  
ATOM   2526  O   LEU A 341      -8.716  22.623 -36.038  1.00 24.90           O  
ANISOU 2526  O   LEU A 341     2877   3253   3330   -282   -532   -181       O  
ATOM   2527  CB  LEU A 341     -10.755  23.875 -38.212  1.00 26.41           C  
ANISOU 2527  CB  LEU A 341     3129   3355   3552   -274   -423   -168       C  
ATOM   2528  CG  LEU A 341     -11.098  24.709 -39.448  1.00 28.06           C  
ANISOU 2528  CG  LEU A 341     3345   3526   3790   -286   -382   -157       C  
ATOM   2529  CD1 LEU A 341     -12.275  24.066 -40.161  1.00 24.09           C  
ANISOU 2529  CD1 LEU A 341     2866   3012   3277   -245   -351   -134       C  
ATOM   2530  CD2 LEU A 341     -11.399  26.140 -39.080  1.00 29.50           C  
ANISOU 2530  CD2 LEU A 341     3563   3666   3979   -319   -379   -184       C  
ATOM   2531  N   PRO A 342     -10.531  23.519 -35.057  1.00 24.72           N  
ANISOU 2531  N   PRO A 342     2955   3183   3255   -285   -511   -215       N  
ATOM   2532  CA  PRO A 342     -10.616  22.444 -34.065  1.00 24.24           C  
ANISOU 2532  CA  PRO A 342     2905   3154   3151   -259   -542   -209       C  
ATOM   2533  C   PRO A 342     -11.016  21.129 -34.723  1.00 21.34           C  
ANISOU 2533  C   PRO A 342     2525   2798   2787   -211   -521   -172       C  
ATOM   2534  O   PRO A 342     -11.691  21.111 -35.749  1.00 23.19           O  
ANISOU 2534  O   PRO A 342     2763   3009   3041   -195   -479   -159       O  
ATOM   2535  CB  PRO A 342     -11.695  22.937 -33.097  1.00 22.25           C  
ANISOU 2535  CB  PRO A 342     2719   2880   2856   -264   -533   -237       C  
ATOM   2536  CG  PRO A 342     -12.505  23.901 -33.883  1.00 25.77           C  
ANISOU 2536  CG  PRO A 342     3185   3279   3328   -269   -485   -246       C  
ATOM   2537  CD  PRO A 342     -11.528  24.576 -34.815  1.00 25.58           C  
ANISOU 2537  CD  PRO A 342     3117   3248   3354   -298   -486   -242       C  
ATOM   2538  N   HIS A 343     -10.575  20.025 -34.131  1.00 24.40           N  
ANISOU 2538  N   HIS A 343     2898   3218   3154   -189   -555   -155       N  
ATOM   2539  CA  HIS A 343     -10.952  18.741 -34.715  1.00 29.15           C  
ANISOU 2539  CA  HIS A 343     3492   3824   3759   -144   -535   -123       C  
ATOM   2540  C   HIS A 343     -12.275  18.261 -34.129  1.00 23.66           C  
ANISOU 2540  C   HIS A 343     2853   3116   3020   -122   -517   -121       C  
ATOM   2541  O   HIS A 343     -12.505  18.403 -32.926  1.00 26.08           O  
ANISOU 2541  O   HIS A 343     3196   3429   3283   -133   -540   -136       O  
ATOM   2542  CB  HIS A 343      -9.893  17.668 -34.443  1.00 33.01           C  
ANISOU 2542  CB  HIS A 343     3938   4349   4255   -124   -575   -100       C  
ATOM   2543  CG  HIS A 343      -8.482  18.158 -34.501  1.00 32.49           C  
ANISOU 2543  CG  HIS A 343     3814   4306   4223   -151   -608   -107       C  
ATOM   2544  ND1 HIS A 343      -7.589  17.963 -33.469  1.00 38.42           N  
ANISOU 2544  ND1 HIS A 343     4546   5090   4961   -160   -669   -108       N  
ATOM   2545  CD2 HIS A 343      -7.799  18.810 -35.473  1.00 35.28           C  
ANISOU 2545  CD2 HIS A 343     4123   4655   4625   -174   -589   -112       C  
ATOM   2546  CE1 HIS A 343      -6.419  18.481 -33.800  1.00 44.62           C  
ANISOU 2546  CE1 HIS A 343     5273   5892   5790   -186   -687   -115       C  
ATOM   2547  NE2 HIS A 343      -6.518  19.000 -35.011  1.00 39.29           N  
ANISOU 2547  NE2 HIS A 343     4581   5194   5152   -196   -636   -118       N  
ATOM   2548  N   PRO A 344     -13.152  17.685 -34.947  1.00 27.09           N  
ANISOU 2548  N   PRO A 344     3296   3534   3463    -95   -477   -104       N  
ATOM   2549  CA  PRO A 344     -14.267  16.909 -34.393  1.00 24.89           C  
ANISOU 2549  CA  PRO A 344     3060   3250   3147    -71   -463    -96       C  
ATOM   2550  C   PRO A 344     -13.748  15.772 -33.532  1.00 22.24           C  
ANISOU 2550  C   PRO A 344     2725   2942   2785    -53   -500    -76       C  
ATOM   2551  O   PRO A 344     -12.778  15.095 -33.878  1.00 25.72           O  
ANISOU 2551  O   PRO A 344     3123   3399   3249    -38   -522    -56       O  
ATOM   2552  CB  PRO A 344     -14.989  16.381 -35.638  1.00 25.85           C  
ANISOU 2552  CB  PRO A 344     3174   3353   3293    -48   -421    -77       C  
ATOM   2553  CG  PRO A 344     -14.574  17.312 -36.737  1.00 23.40           C  
ANISOU 2553  CG  PRO A 344     2836   3031   3023    -66   -406    -83       C  
ATOM   2554  CD  PRO A 344     -13.167  17.702 -36.416  1.00 26.38           C  
ANISOU 2554  CD  PRO A 344     3179   3430   3414    -88   -442    -91       C  
ATOM   2555  N   LYS A 345     -14.406  15.564 -32.395  1.00 24.42           N  
ANISOU 2555  N   LYS A 345     3047   3220   3010    -53   -507    -81       N  
ATOM   2556  CA  LYS A 345     -14.055  14.495 -31.479  1.00 24.98           C  
ANISOU 2556  CA  LYS A 345     3130   3314   3048    -37   -543    -58       C  
ATOM   2557  C   LYS A 345     -15.306  13.730 -31.067  1.00 24.20           C  
ANISOU 2557  C   LYS A 345     3080   3202   2913    -19   -513    -47       C  
ATOM   2558  O   LYS A 345     -16.423  14.265 -31.065  1.00 23.01           O  
ANISOU 2558  O   LYS A 345     2959   3031   2751    -28   -473    -66       O  
ATOM   2559  CB  LYS A 345     -13.348  15.038 -30.232  1.00 27.92           C  
ANISOU 2559  CB  LYS A 345     3517   3710   3382    -64   -594    -75       C  
ATOM   2560  CG  LYS A 345     -11.958  15.599 -30.503  1.00 29.21           C  
ANISOU 2560  CG  LYS A 345     3625   3892   3582    -82   -634    -82       C  
ATOM   2561  CD  LYS A 345     -11.626  16.698 -29.505  1.00 28.08           C  
ANISOU 2561  CD  LYS A 345     3503   3759   3406   -125   -667   -117       C  
ATOM   2562  CE  LYS A 345     -10.236  17.288 -29.747  1.00 33.80           C  
ANISOU 2562  CE  LYS A 345     4169   4503   4169   -150   -708   -125       C  
ATOM   2563  NZ  LYS A 345      -9.157  16.269 -29.546  1.00 33.28           N  
ANISOU 2563  NZ  LYS A 345     4059   4470   4114   -127   -760    -92       N  
ATOM   2564  N   SER A 346     -15.102  12.466 -30.718  1.00 23.51           N  
ANISOU 2564  N   SER A 346     2997   3125   2809      6   -532    -14       N  
ATOM   2565  CA  SER A 346     -16.193  11.660 -30.204  1.00 25.94           C  
ANISOU 2565  CA  SER A 346     3353   3423   3081     18   -506      0       C  
ATOM   2566  C   SER A 346     -16.763  12.283 -28.936  1.00 24.93           C  
ANISOU 2566  C   SER A 346     3279   3301   2894     -8   -507    -23       C  
ATOM   2567  O   SER A 346     -16.120  13.096 -28.261  1.00 24.69           O  
ANISOU 2567  O   SER A 346     3252   3287   2842    -33   -541    -44       O  
ATOM   2568  CB  SER A 346     -15.713  10.264 -29.883  1.00 23.48           C  
ANISOU 2568  CB  SER A 346     3042   3120   2760     46   -535     40       C  
ATOM   2569  OG  SER A 346     -15.002  10.313 -28.673  1.00 29.54           O  
ANISOU 2569  OG  SER A 346     3827   3912   3484     35   -588     45       O  
ATOM   2570  N   MET A 347     -17.988  11.879 -28.607  1.00 25.02           N  
ANISOU 2570  N   MET A 347     3538   3111   2859   -660   -289   -236       N  
ATOM   2571  CA  MET A 347     -18.615  12.363 -27.384  1.00 24.59           C  
ANISOU 2571  CA  MET A 347     3421   3082   2841   -670   -284   -193       C  
ATOM   2572  C   MET A 347     -17.729  12.109 -26.171  1.00 22.77           C  
ANISOU 2572  C   MET A 347     3167   2860   2626   -620   -262   -218       C  
ATOM   2573  O   MET A 347     -17.548  12.994 -25.329  1.00 22.24           O  
ANISOU 2573  O   MET A 347     3040   2830   2582   -603   -227   -212       O  
ATOM   2574  CB  MET A 347     -19.985  11.705 -27.195  1.00 25.06           C  
ANISOU 2574  CB  MET A 347     3495   3117   2909   -720   -339   -132       C  
ATOM   2575  CG  MET A 347     -21.087  12.320 -28.053  1.00 28.84           C  
ANISOU 2575  CG  MET A 347     3968   3604   3387   -774   -355    -88       C  
ATOM   2576  SD  MET A 347     -22.626  11.399 -27.883  1.00 40.85           S  
ANISOU 2576  SD  MET A 347     5511   5093   4919   -835   -426    -13       S  
ATOM   2577  CE  MET A 347     -21.993   9.735 -28.061  1.00 25.53           C  
ANISOU 2577  CE  MET A 347     3657   3090   2953   -819   -469    -55       C  
ATOM   2578  N   LEU A 348     -17.164  10.906 -26.062  1.00 22.33           N  
ANISOU 2578  N   LEU A 348     3161   2767   2556   -597   -282   -246       N  
ATOM   2579  CA  LEU A 348     -16.400  10.582 -24.859  1.00 21.66           C  
ANISOU 2579  CA  LEU A 348     3055   2689   2487   -553   -266   -264       C  
ATOM   2580  C   LEU A 348     -15.081  11.338 -24.832  1.00 21.76           C  
ANISOU 2580  C   LEU A 348     3036   2733   2498   -505   -212   -312       C  
ATOM   2581  O   LEU A 348     -14.713  11.930 -23.811  1.00 21.43           O  
ANISOU 2581  O   LEU A 348     2941   2721   2479   -482   -184   -312       O  
ATOM   2582  CB  LEU A 348     -16.152   9.077 -24.762  1.00 22.83           C  
ANISOU 2582  CB  LEU A 348     3264   2788   2621   -541   -303   -279       C  
ATOM   2583  CG  LEU A 348     -15.312   8.706 -23.535  1.00 23.69           C  
ANISOU 2583  CG  LEU A 348     3351   2903   2747   -494   -286   -299       C  
ATOM   2584  CD1 LEU A 348     -15.906   7.528 -22.835  1.00 27.24           C  
ANISOU 2584  CD1 LEU A 348     3827   3318   3205   -508   -333   -269       C  
ATOM   2585  CD2 LEU A 348     -13.865   8.396 -23.927  1.00 29.02           C  
ANISOU 2585  CD2 LEU A 348     4053   3572   3401   -441   -258   -360       C  
ATOM   2586  N   GLN A 349     -14.341  11.306 -25.940  1.00 19.78           N  
ANISOU 2586  N   GLN A 349     2820   2475   2220   -489   -197   -352       N  
ATOM   2587  CA  GLN A 349     -13.075  12.029 -26.003  1.00 22.47           C  
ANISOU 2587  CA  GLN A 349     3129   2847   2560   -445   -147   -392       C  
ATOM   2588  C   GLN A 349     -13.275  13.509 -25.691  1.00 21.18           C  
ANISOU 2588  C   GLN A 349     2896   2731   2421   -457   -115   -373       C  
ATOM   2589  O   GLN A 349     -12.552  14.088 -24.865  1.00 23.16           O  
ANISOU 2589  O   GLN A 349     3100   3010   2691   -427    -85   -385       O  
ATOM   2590  CB  GLN A 349     -12.439  11.839 -27.382  1.00 25.43           C  
ANISOU 2590  CB  GLN A 349     3552   3212   2900   -430   -137   -428       C  
ATOM   2591  CG  GLN A 349     -11.135  12.603 -27.585  1.00 26.68           C  
ANISOU 2591  CG  GLN A 349     3675   3405   3056   -386    -84   -463       C  
ATOM   2592  CD  GLN A 349     -10.016  12.065 -26.731  1.00 31.01           C  
ANISOU 2592  CD  GLN A 349     4216   3954   3613   -335    -69   -490       C  
ATOM   2593  OE1 GLN A 349      -9.935  10.860 -26.476  1.00 33.29           O  
ANISOU 2593  OE1 GLN A 349     4551   4206   3892   -320    -94   -500       O  
ATOM   2594  NE2 GLN A 349      -9.147  12.958 -26.268  1.00 32.34           N  
ANISOU 2594  NE2 GLN A 349     4326   4161   3800   -308    -29   -502       N  
ATOM   2595  N   ALA A 350     -14.274  14.131 -26.322  1.00 17.91           N  
ANISOU 2595  N   ALA A 350     2475   2324   2006   -501   -125   -341       N  
ATOM   2596  CA  ALA A 350     -14.479  15.566 -26.158  1.00 22.51           C  
ANISOU 2596  CA  ALA A 350     2996   2947   2609   -512    -95   -324       C  
ATOM   2597  C   ALA A 350     -14.969  15.890 -24.757  1.00 22.91           C  
ANISOU 2597  C   ALA A 350     3001   3014   2690   -512    -95   -293       C  
ATOM   2598  O   ALA A 350     -14.564  16.900 -24.171  1.00 18.83           O  
ANISOU 2598  O   ALA A 350     2433   2529   2191   -495    -64   -298       O  
ATOM   2599  CB  ALA A 350     -15.475  16.090 -27.196  1.00 23.99           C  
ANISOU 2599  CB  ALA A 350     3190   3137   2788   -559   -106   -294       C  
ATOM   2600  N   THR A 351     -15.849  15.046 -24.210  1.00 21.29           N  
ANISOU 2600  N   THR A 351     2813   2786   2489   -532   -132   -260       N  
ATOM   2601  CA  THR A 351     -16.322  15.262 -22.852  1.00 22.51           C  
ANISOU 2601  CA  THR A 351     2927   2956   2669   -528   -131   -229       C  
ATOM   2602  C   THR A 351     -15.194  15.056 -21.847  1.00 18.34           C  
ANISOU 2602  C   THR A 351     2385   2435   2149   -479   -112   -263       C  
ATOM   2603  O   THR A 351     -15.049  15.838 -20.902  1.00 19.56           O  
ANISOU 2603  O   THR A 351     2493   2617   2322   -462    -90   -259       O  
ATOM   2604  CB  THR A 351     -17.500  14.333 -22.556  1.00 21.16           C  
ANISOU 2604  CB  THR A 351     2779   2760   2502   -560   -176   -181       C  
ATOM   2605  OG1 THR A 351     -18.532  14.542 -23.535  1.00 20.80           O  
ANISOU 2605  OG1 THR A 351     2745   2709   2449   -608   -196   -146       O  
ATOM   2606  CG2 THR A 351     -18.060  14.613 -21.184  1.00 18.53           C  
ANISOU 2606  CG2 THR A 351     2401   2448   2193   -555   -173   -143       C  
ATOM   2607  N   ALA A 352     -14.377  14.020 -22.045  1.00 21.36           N  
ANISOU 2607  N   ALA A 352     2808   2791   2517   -455   -121   -298       N  
ATOM   2608  CA  ALA A 352     -13.233  13.806 -21.164  1.00 19.02           C  
ANISOU 2608  CA  ALA A 352     2498   2502   2228   -408   -103   -331       C  
ATOM   2609  C   ALA A 352     -12.315  15.020 -21.158  1.00 19.08           C  
ANISOU 2609  C   ALA A 352     2462   2545   2243   -385    -61   -357       C  
ATOM   2610  O   ALA A 352     -11.843  15.453 -20.097  1.00 15.09           O  
ANISOU 2610  O   ALA A 352     1918   2060   1754   -361    -44   -362       O  
ATOM   2611  CB  ALA A 352     -12.463  12.559 -21.592  1.00 15.86           C  
ANISOU 2611  CB  ALA A 352     2151   2068   1808   -384   -116   -365       C  
ATOM   2612  N   GLU A 353     -12.052  15.580 -22.335  1.00 16.36           N  
ANISOU 2612  N   GLU A 353     2122   2208   1886   -393    -44   -372       N  
ATOM   2613  CA  GLU A 353     -11.213  16.771 -22.427  1.00 16.14           C  
ANISOU 2613  CA  GLU A 353     2052   2214   1868   -375     -7   -392       C  
ATOM   2614  C   GLU A 353     -11.856  17.953 -21.711  1.00 16.52           C  
ANISOU 2614  C   GLU A 353     2050   2288   1938   -391      3   -364       C  
ATOM   2615  O   GLU A 353     -11.215  18.604 -20.882  1.00 16.81           O  
ANISOU 2615  O   GLU A 353     2050   2347   1991   -367     22   -375       O  
ATOM   2616  CB  GLU A 353     -10.936  17.095 -23.891  1.00 16.54           C  
ANISOU 2616  CB  GLU A 353     2119   2267   1898   -384      7   -408       C  
ATOM   2617  CG  GLU A 353     -10.006  16.082 -24.551  1.00 19.52           C  
ANISOU 2617  CG  GLU A 353     2541   2624   2251   -353      8   -443       C  
ATOM   2618  CD  GLU A 353      -9.747  16.395 -26.012  1.00 25.36           C  
ANISOU 2618  CD  GLU A 353     3300   3369   2968   -359     23   -457       C  
ATOM   2619  OE1 GLU A 353     -10.083  17.515 -26.451  1.00 25.10           O  
ANISOU 2619  OE1 GLU A 353     3235   3360   2942   -382     37   -443       O  
ATOM   2620  OE2 GLU A 353      -9.213  15.514 -26.720  1.00 25.71           O  
ANISOU 2620  OE2 GLU A 353     3392   3393   2985   -337     20   -482       O  
ATOM   2621  N   ALA A 354     -13.129  18.240 -22.011  1.00 17.02           N  
ANISOU 2621  N   ALA A 354     2114   2351   2003   -430    -11   -326       N  
ATOM   2622  CA  ALA A 354     -13.838  19.308 -21.309  1.00 18.10           C  
ANISOU 2622  CA  ALA A 354     2208   2511   2159   -442     -2   -295       C  
ATOM   2623  C   ALA A 354     -13.820  19.078 -19.805  1.00 18.29           C  
ANISOU 2623  C   ALA A 354     2215   2539   2197   -418     -6   -288       C  
ATOM   2624  O   ALA A 354     -13.491  19.991 -19.034  1.00 16.62           O  
ANISOU 2624  O   ALA A 354     1966   2349   1998   -400     14   -293       O  
ATOM   2625  CB  ALA A 354     -15.279  19.422 -21.811  1.00 16.77           C  
ANISOU 2625  CB  ALA A 354     2045   2338   1989   -486    -20   -248       C  
ATOM   2626  N   ASN A 355     -14.157  17.855 -19.369  1.00 16.38           N  
ANISOU 2626  N   ASN A 355     2000   2274   1949   -418    -33   -275       N  
ATOM   2627  CA  ASN A 355     -14.150  17.556 -17.941  1.00 15.59           C  
ANISOU 2627  CA  ASN A 355     1885   2177   1860   -395    -37   -266       C  
ATOM   2628  C   ASN A 355     -12.785  17.852 -17.337  1.00 17.50           C  
ANISOU 2628  C   ASN A 355     2109   2433   2109   -354    -16   -309       C  
ATOM   2629  O   ASN A 355     -12.680  18.441 -16.255  1.00 14.37           O  
ANISOU 2629  O   ASN A 355     1682   2054   1724   -336     -5   -305       O  
ATOM   2630  CB  ASN A 355     -14.504  16.088 -17.678  1.00 17.27           C  
ANISOU 2630  CB  ASN A 355     2134   2361   2067   -399    -71   -252       C  
ATOM   2631  CG  ASN A 355     -15.956  15.719 -18.020  1.00 20.16           C  
ANISOU 2631  CG  ASN A 355     2513   2715   2432   -441    -99   -200       C  
ATOM   2632  OD1 ASN A 355     -16.287  14.529 -18.035  1.00 20.32           O  
ANISOU 2632  OD1 ASN A 355     2568   2707   2447   -451   -132   -187       O  
ATOM   2633  ND2 ASN A 355     -16.816  16.705 -18.272  1.00 16.17           N  
ANISOU 2633  ND2 ASN A 355     1982   2229   1932   -466    -90   -168       N  
ATOM   2634  N   ASN A 356     -11.718  17.444 -18.023  1.00 17.25           N  
ANISOU 2634  N   ASN A 356     2096   2392   2067   -338     -9   -347       N  
ATOM   2635  CA  ASN A 356     -10.387  17.636 -17.454  1.00 16.09           C  
ANISOU 2635  CA  ASN A 356     1929   2256   1927   -300      9   -382       C  
ATOM   2636  C   ASN A 356      -9.961  19.097 -17.507  1.00 17.05           C  
ANISOU 2636  C   ASN A 356     2012   2407   2060   -298     35   -391       C  
ATOM   2637  O   ASN A 356      -9.370  19.607 -16.547  1.00 15.28           O  
ANISOU 2637  O   ASN A 356     1759   2197   1848   -276     44   -401       O  
ATOM   2638  CB  ASN A 356      -9.384  16.751 -18.175  1.00 17.48           C  
ANISOU 2638  CB  ASN A 356     2136   2417   2090   -280     10   -416       C  
ATOM   2639  CG  ASN A 356      -9.310  15.380 -17.562  1.00 16.94           C  
ANISOU 2639  CG  ASN A 356     2097   2323   2017   -264    -12   -417       C  
ATOM   2640  OD1 ASN A 356      -8.592  15.182 -16.592  1.00 18.92           O  
ANISOU 2640  OD1 ASN A 356     2333   2580   2277   -234     -8   -429       O  
ATOM   2641  ND2 ASN A 356     -10.076  14.429 -18.099  1.00 17.09           N  
ANISOU 2641  ND2 ASN A 356     2158   2312   2022   -285    -38   -402       N  
ATOM   2642  N   LEU A 357     -10.270  19.792 -18.608  1.00 15.18           N  
ANISOU 2642  N   LEU A 357     1772   2176   1819   -323     45   -386       N  
ATOM   2643  CA  LEU A 357      -9.938  21.214 -18.702  1.00 19.31           C  
ANISOU 2643  CA  LEU A 357     2258   2724   2355   -325     67   -391       C  
ATOM   2644  C   LEU A 357     -10.621  22.002 -17.601  1.00 19.00           C  
ANISOU 2644  C   LEU A 357     2193   2697   2330   -326     67   -369       C  
ATOM   2645  O   LEU A 357     -10.009  22.884 -16.986  1.00 19.27           O  
ANISOU 2645  O   LEU A 357     2198   2746   2376   -310     78   -381       O  
ATOM   2646  CB  LEU A 357     -10.337  21.765 -20.071  1.00 17.27           C  
ANISOU 2646  CB  LEU A 357     2002   2469   2089   -354     76   -384       C  
ATOM   2647  CG  LEU A 357      -9.402  21.348 -21.203  1.00 19.56           C  
ANISOU 2647  CG  LEU A 357     2311   2756   2365   -344     85   -412       C  
ATOM   2648  CD1 LEU A 357     -10.030  21.662 -22.566  1.00 17.83           C  
ANISOU 2648  CD1 LEU A 357     2105   2537   2134   -376     88   -399       C  
ATOM   2649  CD2 LEU A 357      -8.031  22.007 -21.053  1.00 16.72           C  
ANISOU 2649  CD2 LEU A 357     1919   2416   2016   -317    107   -439       C  
ATOM   2650  N   ALA A 358     -11.890  21.687 -17.330  1.00 15.37           N  
ANISOU 2650  N   ALA A 358     1743   2230   1866   -345     52   -333       N  
ATOM   2651  CA  ALA A 358     -12.611  22.365 -16.259  1.00 16.77           C  
ANISOU 2651  CA  ALA A 358     1899   2420   2054   -341     54   -307       C  
ATOM   2652  C   ALA A 358     -12.015  22.040 -14.894  1.00 18.10           C  
ANISOU 2652  C   ALA A 358     2062   2590   2226   -307     50   -321       C  
ATOM   2653  O   ALA A 358     -11.888  22.927 -14.043  1.00 17.35           O  
ANISOU 2653  O   ALA A 358     1944   2509   2138   -291     59   -323       O  
ATOM   2654  CB  ALA A 358     -14.096  21.991 -16.309  1.00 15.06           C  
ANISOU 2654  CB  ALA A 358     1692   2197   1833   -367     39   -259       C  
ATOM   2655  N   ALA A 359     -11.655  20.774 -14.661  1.00 14.38           N  
ANISOU 2655  N   ALA A 359     1612   2104   1749   -295     35   -330       N  
ATOM   2656  CA  ALA A 359     -11.075  20.394 -13.378  1.00 17.57           C  
ANISOU 2656  CA  ALA A 359     2010   2509   2155   -263     30   -341       C  
ATOM   2657  C   ALA A 359      -9.697  21.023 -13.178  1.00 16.90           C  
ANISOU 2657  C   ALA A 359     1907   2436   2079   -240     44   -380       C  
ATOM   2658  O   ALA A 359      -9.347  21.406 -12.055  1.00 16.48           O  
ANISOU 2658  O   ALA A 359     1839   2392   2031   -218     44   -386       O  
ATOM   2659  CB  ALA A 359     -11.002  18.867 -13.262  1.00 13.07           C  
ANISOU 2659  CB  ALA A 359     1469   1918   1578   -256     10   -341       C  
ATOM   2660  N   VAL A 360      -8.903  21.139 -14.252  1.00 14.49           N  
ANISOU 2660  N   VAL A 360     1602   2130   1773   -244     54   -403       N  
ATOM   2661  CA  VAL A 360      -7.620  21.834 -14.159  1.00 15.05           C  
ANISOU 2661  CA  VAL A 360     1650   2214   1854   -226     67   -433       C  
ATOM   2662  C   VAL A 360      -7.839  23.294 -13.767  1.00 17.52           C  
ANISOU 2662  C   VAL A 360     1936   2543   2179   -232     74   -426       C  
ATOM   2663  O   VAL A 360      -7.144  23.838 -12.894  1.00 15.02           O  
ANISOU 2663  O   VAL A 360     1602   2234   1871   -214     74   -440       O  
ATOM   2664  CB  VAL A 360      -6.834  21.709 -15.483  1.00 17.00           C  
ANISOU 2664  CB  VAL A 360     1900   2460   2098   -229     79   -452       C  
ATOM   2665  CG1 VAL A 360      -5.642  22.665 -15.501  1.00 20.31           C  
ANISOU 2665  CG1 VAL A 360     2287   2898   2531   -218     92   -472       C  
ATOM   2666  CG2 VAL A 360      -6.337  20.277 -15.681  1.00 14.48           C  
ANISOU 2666  CG2 VAL A 360     1610   2125   1768   -212     72   -465       C  
ATOM   2667  N   ALA A 361      -8.813  23.952 -14.401  1.00 15.90           N  
ANISOU 2667  N   ALA A 361     1730   2340   1972   -258     80   -405       N  
ATOM   2668  CA  ALA A 361      -9.064  25.354 -14.091  1.00 16.69           C  
ANISOU 2668  CA  ALA A 361     1807   2452   2081   -263     88   -399       C  
ATOM   2669  C   ALA A 361      -9.519  25.519 -12.649  1.00 14.62           C  
ANISOU 2669  C   ALA A 361     1545   2192   1819   -244     81   -388       C  
ATOM   2670  O   ALA A 361      -9.059  26.427 -11.948  1.00 16.52           O  
ANISOU 2670  O   ALA A 361     1771   2438   2066   -230     82   -400       O  
ATOM   2671  CB  ALA A 361     -10.091  25.939 -15.058  1.00 20.47           C  
ANISOU 2671  CB  ALA A 361     2286   2933   2559   -294     96   -374       C  
ATOM   2672  N   THR A 362     -10.396  24.625 -12.179  1.00 15.43           N  
ANISOU 2672  N   THR A 362     1663   2288   1910   -242     72   -364       N  
ATOM   2673  CA  THR A 362     -10.846  24.667 -10.792  1.00 17.99           C  
ANISOU 2673  CA  THR A 362     1987   2617   2231   -220     66   -350       C  
ATOM   2674  C   THR A 362      -9.688  24.453  -9.824  1.00 17.59           C  
ANISOU 2674  C   THR A 362     1934   2567   2183   -191     58   -379       C  
ATOM   2675  O   THR A 362      -9.578  25.157  -8.813  1.00 15.69           O  
ANISOU 2675  O   THR A 362     1687   2333   1941   -172     57   -384       O  
ATOM   2676  CB  THR A 362     -11.934  23.613 -10.554  1.00 21.65           C  
ANISOU 2676  CB  THR A 362     2466   3075   2685   -225     56   -314       C  
ATOM   2677  OG1 THR A 362     -13.100  23.935 -11.322  1.00 22.82           O  
ANISOU 2677  OG1 THR A 362     2614   3225   2832   -253     62   -281       O  
ATOM   2678  CG2 THR A 362     -12.312  23.554  -9.084  1.00 18.05           C  
ANISOU 2678  CG2 THR A 362     2010   2627   2223   -197     52   -299       C  
ATOM   2679  N   ALA A 363      -8.822  23.472 -10.104  1.00 15.67           N  
ANISOU 2679  N   ALA A 363     1697   2316   1940   -185     52   -399       N  
ATOM   2680  CA  ALA A 363      -7.660  23.255  -9.248  1.00 16.22           C  
ANISOU 2680  CA  ALA A 363     1762   2388   2014   -159     45   -425       C  
ATOM   2681  C   ALA A 363      -6.764  24.487  -9.199  1.00 14.68           C  
ANISOU 2681  C   ALA A 363     1546   2201   1831   -156     49   -447       C  
ATOM   2682  O   ALA A 363      -6.312  24.888  -8.120  1.00 15.45           O  
ANISOU 2682  O   ALA A 363     1638   2302   1929   -137     40   -457       O  
ATOM   2683  CB  ALA A 363      -6.862  22.038  -9.721  1.00 14.08           C  
ANISOU 2683  CB  ALA A 363     1500   2107   1743   -153     40   -440       C  
ATOM   2684  N   LYS A 364      -6.479  25.098 -10.348  1.00 15.79           N  
ANISOU 2684  N   LYS A 364     1676   2345   1980   -176     60   -454       N  
ATOM   2685  CA  LYS A 364      -5.577  26.246 -10.315  1.00 16.36           C  
ANISOU 2685  CA  LYS A 364     1727   2424   2065   -175     60   -471       C  
ATOM   2686  C   LYS A 364      -6.256  27.447  -9.673  1.00 17.92           C  
ANISOU 2686  C   LYS A 364     1922   2623   2262   -176     58   -462       C  
ATOM   2687  O   LYS A 364      -5.627  28.189  -8.905  1.00 17.61           O  
ANISOU 2687  O   LYS A 364     1876   2585   2229   -165     48   -476       O  
ATOM   2688  CB  LYS A 364      -5.082  26.614 -11.714  1.00 15.54           C  
ANISOU 2688  CB  LYS A 364     1609   2325   1971   -195     73   -478       C  
ATOM   2689  CG  LYS A 364      -4.111  25.633 -12.328  1.00 22.13           C  
ANISOU 2689  CG  LYS A 364     2442   3160   2806   -187     77   -492       C  
ATOM   2690  CD  LYS A 364      -3.226  26.312 -13.372  1.00 30.11           C  
ANISOU 2690  CD  LYS A 364     3429   4181   3829   -197     88   -500       C  
ATOM   2691  CE  LYS A 364      -4.042  26.935 -14.505  1.00 36.63           C  
ANISOU 2691  CE  LYS A 364     4256   5008   4652   -225    101   -487       C  
ATOM   2692  NZ  LYS A 364      -3.188  27.845 -15.349  1.00 37.90           N  
ANISOU 2692  NZ  LYS A 364     4389   5183   4828   -236    111   -492       N  
ATOM   2693  N   ASP A 365      -7.537  27.652  -9.976  1.00 14.81           N  
ANISOU 2693  N   ASP A 365     1538   2229   1862   -189     67   -437       N  
ATOM   2694  CA  ASP A 365      -8.289  28.732  -9.344  1.00 18.97           C  
ANISOU 2694  CA  ASP A 365     2066   2757   2385   -185     69   -425       C  
ATOM   2695  C   ASP A 365      -8.344  28.542  -7.834  1.00 21.04           C  
ANISOU 2695  C   ASP A 365     2340   3019   2635   -154     57   -427       C  
ATOM   2696  O   ASP A 365      -8.256  29.517  -7.072  1.00 18.23           O  
ANISOU 2696  O   ASP A 365     1987   2662   2279   -141     52   -435       O  
ATOM   2697  CB  ASP A 365      -9.700  28.801  -9.939  1.00 20.78           C  
ANISOU 2697  CB  ASP A 365     2301   2988   2608   -202     82   -392       C  
ATOM   2698  CG  ASP A 365     -10.507  29.973  -9.410  1.00 29.90           C  
ANISOU 2698  CG  ASP A 365     3457   4145   3759   -195     88   -377       C  
ATOM   2699  OD1 ASP A 365      -9.975  31.107  -9.409  1.00 33.59           O  
ANISOU 2699  OD1 ASP A 365     3917   4610   4237   -196     86   -394       O  
ATOM   2700  OD2 ASP A 365     -11.681  29.762  -9.001  1.00 30.74           O  
ANISOU 2700  OD2 ASP A 365     3571   4254   3853   -188     93   -346       O  
ATOM   2701  N   THR A 366      -8.475  27.291  -7.380  1.00 16.52           N  
ANISOU 2701  N   THR A 366     1778   2446   2054   -142     52   -420       N  
ATOM   2702  CA  THR A 366      -8.469  27.041  -5.948  1.00 12.35           C  
ANISOU 2702  CA  THR A 366     1259   1919   1513   -112     41   -420       C  
ATOM   2703  C   THR A 366      -7.108  27.387  -5.355  1.00 16.58           C  
ANISOU 2703  C   THR A 366     1789   2453   2056    -98     26   -453       C  
ATOM   2704  O   THR A 366      -7.024  28.052  -4.321  1.00 16.80           O  
ANISOU 2704  O   THR A 366     1825   2481   2076    -79     17   -460       O  
ATOM   2705  CB  THR A 366      -8.833  25.587  -5.650  1.00 17.22           C  
ANISOU 2705  CB  THR A 366     1886   2536   2121   -104     37   -404       C  
ATOM   2706  OG1 THR A 366     -10.142  25.300  -6.164  1.00 15.06           O  
ANISOU 2706  OG1 THR A 366     1617   2264   1842   -120     47   -368       O  
ATOM   2707  CG2 THR A 366      -8.823  25.334  -4.152  1.00 17.69           C  
ANISOU 2707  CG2 THR A 366     1955   2600   2168    -72     27   -402       C  
ATOM   2708  N   TYR A 367      -6.026  26.943  -6.002  1.00 14.92           N  
ANISOU 2708  N   TYR A 367     1566   2242   1860   -108     23   -472       N  
ATOM   2709  CA  TYR A 367      -4.690  27.282  -5.519  1.00 17.67           C  
ANISOU 2709  CA  TYR A 367     1905   2591   2219    -98      8   -497       C  
ATOM   2710  C   TYR A 367      -4.492  28.794  -5.477  1.00 16.59           C  
ANISOU 2710  C   TYR A 367     1762   2451   2090   -106      2   -506       C  
ATOM   2711  O   TYR A 367      -3.988  29.336  -4.485  1.00 17.20           O  
ANISOU 2711  O   TYR A 367     1845   2526   2166    -92    -16   -520       O  
ATOM   2712  CB  TYR A 367      -3.628  26.617  -6.402  1.00 15.67           C  
ANISOU 2712  CB  TYR A 367     1635   2340   1980   -107     10   -510       C  
ATOM   2713  CG  TYR A 367      -2.206  26.978  -6.033  1.00 17.11           C  
ANISOU 2713  CG  TYR A 367     1799   2525   2177   -100     -6   -530       C  
ATOM   2714  CD1 TYR A 367      -1.494  26.242  -5.085  1.00 17.91           C  
ANISOU 2714  CD1 TYR A 367     1902   2627   2276    -79    -21   -538       C  
ATOM   2715  CD2 TYR A 367      -1.562  28.048  -6.648  1.00 19.05           C  
ANISOU 2715  CD2 TYR A 367     2025   2773   2439   -118     -7   -537       C  
ATOM   2716  CE1 TYR A 367      -0.171  26.575  -4.758  1.00 16.28           C  
ANISOU 2716  CE1 TYR A 367     1676   2424   2084    -75    -37   -552       C  
ATOM   2717  CE2 TYR A 367      -0.254  28.387  -6.325  1.00 19.33           C  
ANISOU 2717  CE2 TYR A 367     2041   2812   2491   -115    -24   -550       C  
ATOM   2718  CZ  TYR A 367       0.429  27.654  -5.383  1.00 17.40           C  
ANISOU 2718  CZ  TYR A 367     1798   2569   2245    -94    -40   -557       C  
ATOM   2719  OH  TYR A 367       1.716  28.016  -5.089  1.00 19.86           O  
ANISOU 2719  OH  TYR A 367     2087   2885   2573    -94    -59   -565       O  
ATOM   2720  N   ASN A 368      -4.891  29.485  -6.544  1.00 16.28           N  
ANISOU 2720  N   ASN A 368     1714   2412   2059   -130     16   -499       N  
ATOM   2721  CA  ASN A 368      -4.819  30.944  -6.586  1.00 17.28           C  
ANISOU 2721  CA  ASN A 368     1837   2534   2194   -139     11   -505       C  
ATOM   2722  C   ASN A 368      -5.515  31.579  -5.381  1.00 20.76           C  
ANISOU 2722  C   ASN A 368     2301   2968   2617   -117      3   -502       C  
ATOM   2723  O   ASN A 368      -4.918  32.388  -4.659  1.00 20.44           O  
ANISOU 2723  O   ASN A 368     2267   2920   2578   -109    -17   -519       O  
ATOM   2724  CB  ASN A 368      -5.425  31.435  -7.907  1.00 18.35           C  
ANISOU 2724  CB  ASN A 368     1963   2671   2337   -166     30   -491       C  
ATOM   2725  CG  ASN A 368      -5.485  32.954  -8.013  1.00 25.41           C  
ANISOU 2725  CG  ASN A 368     2854   3559   3241   -177     26   -493       C  
ATOM   2726  OD1 ASN A 368      -6.471  33.507  -8.492  1.00 30.41           O  
ANISOU 2726  OD1 ASN A 368     3491   4191   3871   -187     40   -476       O  
ATOM   2727  ND2 ASN A 368      -4.438  33.631  -7.564  1.00 23.44           N  
ANISOU 2727  ND2 ASN A 368     2598   3304   3003   -176      4   -512       N  
ATOM   2728  N   LYS A 369      -6.780  31.224  -5.137  1.00 18.68           N  
ANISOU 2728  N   LYS A 369     2053   2708   2336   -106     17   -479       N  
ATOM   2729  CA  LYS A 369      -7.489  31.874  -4.038  1.00 19.65           C  
ANISOU 2729  CA  LYS A 369     2199   2827   2439    -81     15   -474       C  
ATOM   2730  C   LYS A 369      -6.928  31.465  -2.684  1.00 19.06           C  
ANISOU 2730  C   LYS A 369     2138   2752   2351    -52     -5   -489       C  
ATOM   2731  O   LYS A 369      -6.864  32.292  -1.773  1.00 19.24           O  
ANISOU 2731  O   LYS A 369     2181   2767   2362    -32    -18   -500       O  
ATOM   2732  CB  LYS A 369      -8.984  31.577  -4.106  1.00 25.38           C  
ANISOU 2732  CB  LYS A 369     2933   3561   3150    -75     37   -439       C  
ATOM   2733  CG  LYS A 369      -9.615  31.997  -5.419  1.00 28.13           C  
ANISOU 2733  CG  LYS A 369     3268   3911   3511   -104     55   -422       C  
ATOM   2734  CD  LYS A 369      -9.120  33.338  -5.897  1.00 30.59           C  
ANISOU 2734  CD  LYS A 369     3573   4213   3837   -119     50   -439       C  
ATOM   2735  CE  LYS A 369      -9.363  33.519  -7.400  1.00 31.28           C  
ANISOU 2735  CE  LYS A 369     3641   4303   3941   -155     65   -426       C  
ATOM   2736  NZ  LYS A 369     -10.812  33.497  -7.769  1.00 33.47           N  
ANISOU 2736  NZ  LYS A 369     3921   4587   4209   -159     86   -390       N  
ATOM   2737  N   LYS A 370      -6.479  30.214  -2.539  1.00 17.16           N  
ANISOU 2737  N   LYS A 370     1891   2517   2111    -48     -9   -490       N  
ATOM   2738  CA  LYS A 370      -5.873  29.813  -1.273  1.00 18.33           C  
ANISOU 2738  CA  LYS A 370     2051   2666   2247    -22    -29   -503       C  
ATOM   2739  C   LYS A 370      -4.552  30.533  -1.049  1.00 19.83           C  
ANISOU 2739  C   LYS A 370     2236   2848   2452    -27    -54   -532       C  
ATOM   2740  O   LYS A 370      -4.241  30.941   0.078  1.00 18.09           O  
ANISOU 2740  O   LYS A 370     2034   2622   2218     -7    -75   -545       O  
ATOM   2741  CB  LYS A 370      -5.667  28.298  -1.236  1.00 21.44           C  
ANISOU 2741  CB  LYS A 370     2438   3068   2642    -17    -27   -496       C  
ATOM   2742  CG  LYS A 370      -6.952  27.468  -1.316  1.00 22.50           C  
ANISOU 2742  CG  LYS A 370     2578   3209   2763    -13     -9   -464       C  
ATOM   2743  CD  LYS A 370      -7.789  27.595  -0.062  1.00 27.37           C  
ANISOU 2743  CD  LYS A 370     3215   3832   3354     19     -8   -448       C  
ATOM   2744  CE  LYS A 370      -9.025  26.696  -0.151  1.00 33.12           C  
ANISOU 2744  CE  LYS A 370     3943   4569   4072     21      8   -409       C  
ATOM   2745  NZ  LYS A 370      -9.566  26.370   1.194  1.00 35.16           N  
ANISOU 2745  NZ  LYS A 370     4217   4838   4306     57      6   -391       N  
ATOM   2746  N   MET A 371      -3.762  30.709  -2.109  1.00 17.52           N  
ANISOU 2746  N   MET A 371     1918   2554   2184    -55    -55   -540       N  
ATOM   2747  CA  MET A 371      -2.512  31.442  -1.948  1.00 16.46           C  
ANISOU 2747  CA  MET A 371     1774   2413   2066    -63    -81   -561       C  
ATOM   2748  C   MET A 371      -2.778  32.903  -1.617  1.00 20.06           C  
ANISOU 2748  C   MET A 371     2248   2854   2518    -64    -93   -568       C  
ATOM   2749  O   MET A 371      -2.026  33.512  -0.847  1.00 19.13           O  
ANISOU 2749  O   MET A 371     2141   2727   2402    -59   -123   -585       O  
ATOM   2750  CB  MET A 371      -1.653  31.312  -3.204  1.00 16.31           C  
ANISOU 2750  CB  MET A 371     1722   2400   2076    -91    -75   -562       C  
ATOM   2751  CG  MET A 371      -1.020  29.927  -3.367  1.00 17.95           C  
ANISOU 2751  CG  MET A 371     1914   2618   2287    -85    -70   -561       C  
ATOM   2752  SD  MET A 371       0.231  29.554  -2.110  1.00 19.68           S  
ANISOU 2752  SD  MET A 371     2132   2838   2509    -66   -103   -576       S  
ATOM   2753  CE  MET A 371       1.592  30.527  -2.737  1.00 17.82           C  
ANISOU 2753  CE  MET A 371     1864   2603   2305    -92   -121   -583       C  
ATOM   2754  N   GLU A 372      -3.843  33.483  -2.187  1.00 18.79           N  
ANISOU 2754  N   GLU A 372     2094   2691   2353    -70    -72   -555       N  
ATOM   2755  CA  GLU A 372      -4.174  34.876  -1.882  1.00 20.95           C  
ANISOU 2755  CA  GLU A 372     2389   2950   2622    -67    -82   -561       C  
ATOM   2756  C   GLU A 372      -4.460  35.064  -0.399  1.00 20.00           C  
ANISOU 2756  C   GLU A 372     2306   2821   2471    -31    -97   -569       C  
ATOM   2757  O   GLU A 372      -4.210  36.145   0.149  1.00 20.86           O  
ANISOU 2757  O   GLU A 372     2437   2911   2576    -26   -121   -585       O  
ATOM   2758  CB  GLU A 372      -5.367  35.340  -2.718  1.00 18.36           C  
ANISOU 2758  CB  GLU A 372     2061   2623   2293    -76    -53   -540       C  
ATOM   2759  CG  GLU A 372      -5.002  35.691  -4.150  1.00 20.93           C  
ANISOU 2759  CG  GLU A 372     2355   2950   2646   -114    -45   -537       C  
ATOM   2760  CD  GLU A 372      -4.123  36.936  -4.240  1.00 24.37           C  
ANISOU 2760  CD  GLU A 372     2787   3370   3102   -131    -71   -553       C  
ATOM   2761  OE1 GLU A 372      -4.610  38.018  -3.857  1.00 24.26           O  
ANISOU 2761  OE1 GLU A 372     2797   3340   3080   -123    -78   -556       O  
ATOM   2762  OE2 GLU A 372      -2.946  36.836  -4.672  1.00 21.90           O  
ANISOU 2762  OE2 GLU A 372     2448   3061   2812   -151    -86   -561       O  
ATOM   2763  N   GLU A 373      -4.968  34.028   0.269  1.00 17.23           N  
ANISOU 2763  N   GLU A 373     1964   2482   2099     -6    -86   -558       N  
ATOM   2764  CA  GLU A 373      -5.256  34.125   1.695  1.00 20.68           C  
ANISOU 2764  CA  GLU A 373     2437   2916   2505     32    -98   -564       C  
ATOM   2765  C   GLU A 373      -3.995  34.225   2.539  1.00 20.70           C  
ANISOU 2765  C   GLU A 373     2447   2909   2508     36   -137   -590       C  
ATOM   2766  O   GLU A 373      -4.065  34.705   3.672  1.00 22.62           O  
ANISOU 2766  O   GLU A 373     2726   3142   2725     64   -155   -602       O  
ATOM   2767  CB  GLU A 373      -6.094  32.924   2.150  1.00 18.50           C  
ANISOU 2767  CB  GLU A 373     2163   2659   2208     56    -76   -541       C  
ATOM   2768  CG  GLU A 373      -7.511  32.944   1.594  1.00 23.56           C  
ANISOU 2768  CG  GLU A 373     2802   3308   2841     59    -42   -510       C  
ATOM   2769  CD  GLU A 373      -8.315  31.699   1.923  1.00 30.52           C  
ANISOU 2769  CD  GLU A 373     3680   4208   3707     75    -23   -481       C  
ATOM   2770  OE1 GLU A 373      -7.759  30.758   2.540  1.00 31.51           O  
ANISOU 2770  OE1 GLU A 373     3803   4340   3829     85    -36   -486       O  
ATOM   2771  OE2 GLU A 373      -9.511  31.665   1.549  1.00 36.34           O  
ANISOU 2771  OE2 GLU A 373     4415   4955   4439     78      3   -449       O  
ATOM   2772  N   ILE A 374      -2.847  33.794   2.027  1.00 18.58           N  
ANISOU 2772  N   ILE A 374     2148   2644   2268     10   -151   -598       N  
ATOM   2773  CA  ILE A 374      -1.617  33.848   2.805  1.00 22.17           C  
ANISOU 2773  CA  ILE A 374     2606   3091   2727     11   -190   -618       C  
ATOM   2774  C   ILE A 374      -0.566  34.768   2.204  1.00 21.34           C  
ANISOU 2774  C   ILE A 374     2483   2974   2653    -22   -215   -630       C  
ATOM   2775  O   ILE A 374       0.341  35.197   2.935  1.00 18.77           O  
ANISOU 2775  O   ILE A 374     2168   2636   2329    -24   -255   -645       O  
ATOM   2776  CB  ILE A 374      -1.025  32.440   3.012  1.00 22.11           C  
ANISOU 2776  CB  ILE A 374     2577   3101   2724     16   -189   -614       C  
ATOM   2777  CG1 ILE A 374      -0.712  31.799   1.663  1.00 22.58           C  
ANISOU 2777  CG1 ILE A 374     2596   3172   2812    -11   -168   -603       C  
ATOM   2778  CG2 ILE A 374      -1.966  31.575   3.848  1.00 22.65           C  
ANISOU 2778  CG2 ILE A 374     2666   3180   2761     50   -172   -602       C  
ATOM   2779  CD1 ILE A 374       0.225  30.642   1.772  1.00 28.00           C  
ANISOU 2779  CD1 ILE A 374     3259   3870   3510    -10   -174   -603       C  
ATOM   2780  N   CYS A 375      -0.635  35.090   0.910  1.00 18.17           N  
ANISOU 2780  N   CYS A 375     2054   2574   2275    -51   -197   -620       N  
ATOM   2781  CA ACYS A 375       0.333  36.033   0.349  0.43 20.39           C  
ANISOU 2781  CA ACYS A 375     2317   2845   2587    -82   -222   -627       C  
ATOM   2782  CA BCYS A 375       0.338  35.937   0.238  0.57 20.43           C  
ANISOU 2782  CA BCYS A 375     2317   2851   2593    -84   -219   -625       C  
ATOM   2783  C   CYS A 375      -0.319  36.973  -0.657  1.00 21.31           C  
ANISOU 2783  C   CYS A 375     2429   2953   2714   -101   -205   -619       C  
ATOM   2784  O   CYS A 375       0.346  37.497  -1.562  1.00 22.39           O  
ANISOU 2784  O   CYS A 375     2537   3090   2881   -133   -212   -615       O  
ATOM   2785  CB ACYS A 375       1.524  35.313  -0.290  0.43 22.83           C  
ANISOU 2785  CB ACYS A 375     2580   3170   2925   -103   -226   -621       C  
ATOM   2786  CB BCYS A 375       1.298  35.094  -0.599  0.57 22.38           C  
ANISOU 2786  CB BCYS A 375     2517   3117   2868   -104   -212   -617       C  
ATOM   2787  SG ACYS A 375       1.119  33.832  -1.199  0.43 24.88           S  
ANISOU 2787  SG ACYS A 375     2813   3454   3186   -100   -180   -605       S  
ATOM   2788  SG BCYS A 375       2.521  34.304   0.380  0.57 28.38           S  
ANISOU 2788  SG BCYS A 375     3269   3883   3630    -93   -243   -624       S  
ATOM   2789  N   GLY A 376      -1.606  37.226  -0.485  1.00 21.83           N  
ANISOU 2789  N   GLY A 376     2523   3015   2755    -82   -182   -614       N  
ATOM   2790  CA  GLY A 376      -2.224  38.322  -1.189  1.00 19.33           C  
ANISOU 2790  CA  GLY A 376     2211   2687   2447    -96   -172   -608       C  
ATOM   2791  C   GLY A 376      -1.570  39.632  -0.802  1.00 20.39           C  
ANISOU 2791  C   GLY A 376     2364   2794   2590   -106   -214   -625       C  
ATOM   2792  O   GLY A 376      -0.837  39.736   0.183  1.00 21.34           O  
ANISOU 2792  O   GLY A 376     2503   2902   2703    -97   -251   -641       O  
ATOM   2793  N   GLY A 377      -1.840  40.653  -1.614  1.00 20.42           N  
ANISOU 2793  N   GLY A 377     2363   2786   2610   -127   -210   -619       N  
ATOM   2794  CA  GLY A 377      -1.258  41.963  -1.370  1.00 23.05           C  
ANISOU 2794  CA  GLY A 377     2713   3090   2955   -142   -251   -633       C  
ATOM   2795  C   GLY A 377      -1.567  42.525   0.005  1.00 24.09           C  
ANISOU 2795  C   GLY A 377     2904   3196   3053   -108   -277   -652       C  
ATOM   2796  O   GLY A 377      -0.806  43.340   0.532  1.00 25.27           O  
ANISOU 2796  O   GLY A 377     3075   3319   3209   -117   -324   -668       O  
ATOM   2797  N   ASP A 378      -2.684  42.117   0.603  1.00 22.86           N  
ANISOU 2797  N   ASP A 378     2778   3047   2862    -68   -248   -650       N  
ATOM   2798  CA  ASP A 378      -3.048  42.607   1.926  1.00 22.59           C  
ANISOU 2798  CA  ASP A 378     2803   2991   2789    -28   -268   -667       C  
ATOM   2799  C   ASP A 378      -2.627  41.658   3.042  1.00 23.23           C  
ANISOU 2799  C   ASP A 378     2897   3083   2848     -4   -282   -677       C  
ATOM   2800  O   ASP A 378      -3.051  41.843   4.189  1.00 22.33           O  
ANISOU 2800  O   ASP A 378     2832   2957   2696     36   -291   -689       O  
ATOM   2801  CB  ASP A 378      -4.555  42.891   1.990  1.00 24.72           C  
ANISOU 2801  CB  ASP A 378     3100   3262   3031      6   -228   -655       C  
ATOM   2802  CG  ASP A 378      -5.414  41.664   1.711  1.00 31.87           C  
ANISOU 2802  CG  ASP A 378     3980   4203   3926     20   -180   -630       C  
ATOM   2803  OD1 ASP A 378      -4.875  40.585   1.372  1.00 26.35           O  
ANISOU 2803  OD1 ASP A 378     3243   3525   3242      2   -175   -624       O  
ATOM   2804  OD2 ASP A 378      -6.655  41.790   1.830  1.00 37.79           O  
ANISOU 2804  OD2 ASP A 378     4749   4958   4653     49   -147   -613       O  
ATOM   2805  N   LYS A 379      -1.786  40.654   2.732  1.00 20.75           N  
ANISOU 2805  N   LYS A 379     2539   2790   2555    -25   -284   -672       N  
ATOM   2806  CA  LYS A 379      -1.283  39.757   3.752  1.00 17.24           C  
ANISOU 2806  CA  LYS A 379     2103   2355   2093     -6   -300   -680       C  
ATOM   2807  C   LYS A 379       0.157  40.087   4.095  1.00 21.51           C  
ANISOU 2807  C   LYS A 379     2639   2880   2654    -30   -354   -695       C  
ATOM   2808  O   LYS A 379       0.884  40.657   3.278  1.00 19.87           O  
ANISOU 2808  O   LYS A 379     2402   2665   2482    -69   -371   -692       O  
ATOM   2809  CB  LYS A 379      -1.396  38.303   3.282  1.00 18.52           C  
ANISOU 2809  CB  LYS A 379     2224   2551   2263     -7   -265   -661       C  
ATOM   2810  CG  LYS A 379      -2.791  37.919   2.856  1.00 20.79           C  
ANISOU 2810  CG  LYS A 379     2511   2853   2535     11   -215   -641       C  
ATOM   2811  CD  LYS A 379      -3.825  38.174   3.950  1.00 22.63           C  
ANISOU 2811  CD  LYS A 379     2793   3080   2724     57   -207   -642       C  
ATOM   2812  CE  LYS A 379      -5.216  37.867   3.412  1.00 29.19           C  
ANISOU 2812  CE  LYS A 379     3617   3929   3545     70   -158   -614       C  
ATOM   2813  NZ  LYS A 379      -6.316  38.099   4.389  1.00 34.56           N  
ANISOU 2813  NZ  LYS A 379     4340   4608   4182    118   -143   -607       N  
ATOM   2814  N   PRO A 380       0.605  39.760   5.300  1.00 21.81           N  
ANISOU 2814  N   PRO A 380     2703   2914   2669     -9   -383   -709       N  
ATOM   2815  CA  PRO A 380       1.969  40.118   5.694  1.00 23.74           C  
ANISOU 2815  CA  PRO A 380     2945   3143   2933    -34   -440   -720       C  
ATOM   2816  C   PRO A 380       3.013  39.235   5.025  1.00 24.17           C  
ANISOU 2816  C   PRO A 380     2937   3222   3025    -64   -439   -705       C  
ATOM   2817  O   PRO A 380       2.727  38.154   4.505  1.00 20.84           O  
ANISOU 2817  O   PRO A 380     2482   2829   2607    -59   -398   -690       O  
ATOM   2818  CB  PRO A 380       1.959  39.913   7.212  1.00 23.95           C  
ANISOU 2818  CB  PRO A 380     3021   3162   2918      3   -466   -738       C  
ATOM   2819  CG  PRO A 380       0.926  38.895   7.429  1.00 23.47           C  
ANISOU 2819  CG  PRO A 380     2961   3127   2828     40   -416   -727       C  
ATOM   2820  CD  PRO A 380      -0.154  39.192   6.426  1.00 22.91           C  
ANISOU 2820  CD  PRO A 380     2881   3061   2763     39   -370   -713       C  
ATOM   2821  N   PHE A 381       4.248  39.731   5.047  1.00 19.32           N  
ANISOU 2821  N   PHE A 381     2308   2596   2438    -96   -487   -707       N  
ATOM   2822  CA  PHE A 381       5.388  38.946   4.603  1.00 22.22           C  
ANISOU 2822  CA  PHE A 381     2617   2986   2838   -120   -493   -691       C  
ATOM   2823  C   PHE A 381       5.390  37.585   5.283  1.00 25.48           C  
ANISOU 2823  C   PHE A 381     3027   3422   3232    -91   -477   -690       C  
ATOM   2824  O   PHE A 381       5.110  37.466   6.481  1.00 21.69           O  
ANISOU 2824  O   PHE A 381     2591   2933   2716    -61   -493   -704       O  
ATOM   2825  CB  PHE A 381       6.687  39.692   4.917  1.00 22.98           C  
ANISOU 2825  CB  PHE A 381     2709   3064   2960   -151   -556   -691       C  
ATOM   2826  CG  PHE A 381       7.934  38.886   4.667  1.00 26.00           C  
ANISOU 2826  CG  PHE A 381     3034   3471   3374   -171   -566   -672       C  
ATOM   2827  CD1 PHE A 381       8.341  38.599   3.370  1.00 25.20           C  
ANISOU 2827  CD1 PHE A 381     2872   3393   3309   -194   -537   -649       C  
ATOM   2828  CD2 PHE A 381       8.712  38.439   5.726  1.00 28.40           C  
ANISOU 2828  CD2 PHE A 381     3345   3775   3669   -164   -604   -675       C  
ATOM   2829  CE1 PHE A 381       9.489  37.872   3.131  1.00 26.92           C  
ANISOU 2829  CE1 PHE A 381     3039   3635   3556   -207   -543   -628       C  
ATOM   2830  CE2 PHE A 381       9.872  37.712   5.494  1.00 27.56           C  
ANISOU 2830  CE2 PHE A 381     3184   3692   3594   -180   -612   -654       C  
ATOM   2831  CZ  PHE A 381      10.259  37.425   4.193  1.00 25.33           C  
ANISOU 2831  CZ  PHE A 381     2842   3434   3348   -200   -580   -630       C  
ATOM   2832  N   LEU A 382       5.704  36.557   4.506  1.00 24.03           N  
ANISOU 2832  N   LEU A 382     2794   3267   3070    -98   -445   -673       N  
ATOM   2833  CA  LEU A 382       5.785  35.189   4.996  1.00 24.93           C  
ANISOU 2833  CA  LEU A 382     2897   3403   3171    -74   -429   -669       C  
ATOM   2834  C   LEU A 382       7.233  34.741   4.940  1.00 24.58           C  
ANISOU 2834  C   LEU A 382     2810   3371   3158    -93   -455   -657       C  
ATOM   2835  O   LEU A 382       7.918  34.984   3.945  1.00 24.02           O  
ANISOU 2835  O   LEU A 382     2697   3308   3123   -123   -453   -642       O  
ATOM   2836  CB  LEU A 382       4.925  34.242   4.157  1.00 27.16           C  
ANISOU 2836  CB  LEU A 382     3161   3707   3451    -62   -371   -657       C  
ATOM   2837  CG  LEU A 382       3.608  33.740   4.733  1.00 31.47           C  
ANISOU 2837  CG  LEU A 382     3744   4256   3959    -26   -342   -660       C  
ATOM   2838  CD1 LEU A 382       2.986  32.718   3.777  1.00 28.29           C  
ANISOU 2838  CD1 LEU A 382     3314   3873   3561    -24   -292   -644       C  
ATOM   2839  CD2 LEU A 382       3.843  33.123   6.101  1.00 34.79           C  
ANISOU 2839  CD2 LEU A 382     4186   4678   4353      1   -364   -667       C  
ATOM   2840  N   ALA A 383       7.697  34.112   6.013  1.00 26.00           N  
ANISOU 2840  N   ALA A 383     3000   3555   3324    -76   -478   -661       N  
ATOM   2841  CA  ALA A 383       9.011  33.498   5.989  1.00 27.24           C  
ANISOU 2841  CA  ALA A 383     3113   3728   3509    -90   -496   -646       C  
ATOM   2842  C   ALA A 383       9.092  32.537   4.804  1.00 22.64           C  
ANISOU 2842  C   ALA A 383     2482   3172   2949    -91   -448   -628       C  
ATOM   2843  O   ALA A 383       8.142  31.783   4.559  1.00 21.51           O  
ANISOU 2843  O   ALA A 383     2348   3038   2788    -69   -405   -630       O  
ATOM   2844  CB  ALA A 383       9.275  32.751   7.298  1.00 25.61           C  
ANISOU 2844  CB  ALA A 383     2925   3525   3279    -65   -518   -651       C  
ATOM   2845  N   PRO A 384      10.186  32.557   4.036  1.00 25.10           N  
ANISOU 2845  N   PRO A 384     2742   3496   3298   -115   -453   -608       N  
ATOM   2846  CA  PRO A 384      10.275  31.688   2.847  1.00 23.00           C  
ANISOU 2846  CA  PRO A 384     2435   3255   3050   -113   -406   -593       C  
ATOM   2847  C   PRO A 384       9.992  30.217   3.122  1.00 25.37           C  
ANISOU 2847  C   PRO A 384     2736   3569   3333    -81   -376   -593       C  
ATOM   2848  O   PRO A 384       9.311  29.575   2.313  1.00 24.11           O  
ANISOU 2848  O   PRO A 384     2573   3418   3169    -71   -331   -591       O  
ATOM   2849  CB  PRO A 384      11.718  31.912   2.364  1.00 21.35           C  
ANISOU 2849  CB  PRO A 384     2172   3058   2881   -138   -427   -569       C  
ATOM   2850  CG  PRO A 384      12.038  33.302   2.811  1.00 24.57           C  
ANISOU 2850  CG  PRO A 384     2595   3443   3297   -166   -479   -572       C  
ATOM   2851  CD  PRO A 384      11.324  33.491   4.132  1.00 25.10           C  
ANISOU 2851  CD  PRO A 384     2722   3487   3326   -147   -504   -598       C  
ATOM   2852  N   ASN A 385      10.468  29.668   4.244  1.00 20.67           N  
ANISOU 2852  N   ASN A 385     2149   2976   2729    -66   -402   -595       N  
ATOM   2853  CA  ASN A 385      10.188  28.261   4.530  1.00 23.20           C  
ANISOU 2853  CA  ASN A 385     2471   3309   3034    -36   -375   -594       C  
ATOM   2854  C   ASN A 385       8.707  28.030   4.817  1.00 26.00           C  
ANISOU 2854  C   ASN A 385     2870   3655   3353    -15   -350   -607       C  
ATOM   2855  O   ASN A 385       8.166  26.973   4.473  1.00 22.16           O  
ANISOU 2855  O   ASN A 385     2382   3178   2860      3   -315   -603       O  
ATOM   2856  CB  ASN A 385      11.031  27.773   5.706  1.00 22.83           C  
ANISOU 2856  CB  ASN A 385     2423   3266   2985    -25   -410   -590       C  
ATOM   2857  CG  ASN A 385      12.510  27.913   5.450  1.00 27.20           C  
ANISOU 2857  CG  ASN A 385     2928   3832   3575    -44   -434   -570       C  
ATOM   2858  OD1 ASN A 385      12.954  27.995   4.295  1.00 26.00           O  
ANISOU 2858  OD1 ASN A 385     2738   3691   3451    -58   -414   -555       O  
ATOM   2859  ND2 ASN A 385      13.290  27.937   6.523  1.00 26.16           N  
ANISOU 2859  ND2 ASN A 385     2797   3698   3443    -45   -478   -567       N  
ATOM   2860  N   ASP A 386       8.043  28.988   5.474  1.00 24.05           N  
ANISOU 2860  N   ASP A 386     2663   3391   3085    -15   -370   -621       N  
ATOM   2861  CA  ASP A 386       6.610  28.852   5.713  1.00 25.19           C  
ANISOU 2861  CA  ASP A 386     2846   3530   3196      6   -344   -629       C  
ATOM   2862  C   ASP A 386       5.829  28.947   4.413  1.00 24.28           C  
ANISOU 2862  C   ASP A 386     2721   3416   3089     -4   -303   -623       C  
ATOM   2863  O   ASP A 386       4.912  28.154   4.178  1.00 22.45           O  
ANISOU 2863  O   ASP A 386     2497   3191   2843     11   -270   -618       O  
ATOM   2864  CB  ASP A 386       6.131  29.910   6.692  1.00 22.56           C  
ANISOU 2864  CB  ASP A 386     2558   3178   2836     13   -373   -644       C  
ATOM   2865  CG  ASP A 386       6.713  29.711   8.062  1.00 34.63           C  
ANISOU 2865  CG  ASP A 386     4105   4705   4349     28   -411   -651       C  
ATOM   2866  OD1 ASP A 386       7.184  28.582   8.333  1.00 35.76           O  
ANISOU 2866  OD1 ASP A 386     4228   4863   4496     39   -407   -642       O  
ATOM   2867  OD2 ASP A 386       6.711  30.674   8.856  1.00 39.95           O  
ANISOU 2867  OD2 ASP A 386     4815   5360   5005     28   -446   -665       O  
ATOM   2868  N   LEU A 387       6.184  29.912   3.565  1.00 22.13           N  
ANISOU 2868  N   LEU A 387     2431   3138   2839    -32   -308   -622       N  
ATOM   2869  CA  LEU A 387       5.560  30.024   2.255  1.00 22.47           C  
ANISOU 2869  CA  LEU A 387     2462   3185   2892    -45   -271   -616       C  
ATOM   2870  C   LEU A 387       5.716  28.738   1.461  1.00 20.42           C  
ANISOU 2870  C   LEU A 387     2174   2942   2642    -39   -238   -604       C  
ATOM   2871  O   LEU A 387       4.768  28.276   0.820  1.00 19.51           O  
ANISOU 2871  O   LEU A 387     2066   2829   2517    -34   -204   -600       O  
ATOM   2872  CB  LEU A 387       6.167  31.195   1.492  1.00 20.05           C  
ANISOU 2872  CB  LEU A 387     2133   2872   2612    -77   -285   -613       C  
ATOM   2873  CG  LEU A 387       5.765  31.294   0.026  1.00 21.97           C  
ANISOU 2873  CG  LEU A 387     2356   3123   2869    -93   -249   -604       C  
ATOM   2874  CD1 LEU A 387       4.250  31.385  -0.104  1.00 25.25           C  
ANISOU 2874  CD1 LEU A 387     2803   3531   3259    -83   -222   -607       C  
ATOM   2875  CD2 LEU A 387       6.438  32.497  -0.605  1.00 22.65           C  
ANISOU 2875  CD2 LEU A 387     2419   3204   2983   -124   -268   -599       C  
ATOM   2876  N   GLN A 388       6.907  28.147   1.492  1.00 19.91           N  
ANISOU 2876  N   GLN A 388     2079   2889   2596    -38   -249   -598       N  
ATOM   2877  CA  GLN A 388       7.135  26.884   0.799  1.00 23.28           C  
ANISOU 2877  CA  GLN A 388     2485   3331   3031    -27   -219   -588       C  
ATOM   2878  C   GLN A 388       6.235  25.779   1.337  1.00 22.31           C  
ANISOU 2878  C   GLN A 388     2388   3206   2882     -1   -203   -590       C  
ATOM   2879  O   GLN A 388       5.642  25.012   0.567  1.00 20.82           O  
ANISOU 2879  O   GLN A 388     2201   3020   2690      4   -171   -585       O  
ATOM   2880  CB  GLN A 388       8.598  26.478   0.938  1.00 23.67           C  
ANISOU 2880  CB  GLN A 388     2498   3393   3103    -25   -236   -579       C  
ATOM   2881  CG  GLN A 388       8.871  25.110   0.374  1.00 30.85           C  
ANISOU 2881  CG  GLN A 388     3391   4315   4017     -6   -206   -570       C  
ATOM   2882  CD  GLN A 388       9.980  25.159  -0.630  1.00 42.12           C  
ANISOU 2882  CD  GLN A 388     4774   5757   5473    -15   -196   -556       C  
ATOM   2883  OE1 GLN A 388       9.822  25.719  -1.722  1.00 44.54           O  
ANISOU 2883  OE1 GLN A 388     5069   6065   5788    -32   -178   -553       O  
ATOM   2884  NE2 GLN A 388      11.130  24.617  -0.259  1.00 37.38           N  
ANISOU 2884  NE2 GLN A 388     4146   5169   4887     -4   -209   -545       N  
ATOM   2885  N   THR A 389       6.144  25.668   2.665  1.00 22.76           N  
ANISOU 2885  N   THR A 389     2467   3259   2921     15   -227   -595       N  
ATOM   2886  CA  THR A 389       5.321  24.633   3.279  1.00 24.23           C  
ANISOU 2886  CA  THR A 389     2677   3446   3084     40   -214   -592       C  
ATOM   2887  C   THR A 389       3.852  24.808   2.920  1.00 22.53           C  
ANISOU 2887  C   THR A 389     2487   3225   2850     40   -190   -590       C  
ATOM   2888  O   THR A 389       3.152  23.829   2.622  1.00 20.41           O  
ANISOU 2888  O   THR A 389     2224   2958   2574     49   -167   -580       O  
ATOM   2889  CB  THR A 389       5.499  24.668   4.795  1.00 26.25           C  
ANISOU 2889  CB  THR A 389     2952   3700   3322     57   -246   -598       C  
ATOM   2890  OG1 THR A 389       6.859  24.367   5.113  1.00 28.04           O  
ANISOU 2890  OG1 THR A 389     3153   3934   3568     56   -269   -596       O  
ATOM   2891  CG2 THR A 389       4.581  23.663   5.478  1.00 29.23           C  
ANISOU 2891  CG2 THR A 389     3353   4080   3674     83   -234   -591       C  
ATOM   2892  N   LYS A 390       3.362  26.048   2.959  1.00 23.67           N  
ANISOU 2892  N   LYS A 390     2646   3360   2987     29   -196   -596       N  
ATOM   2893  CA  LYS A 390       1.959  26.286   2.629  1.00 21.13           C  
ANISOU 2893  CA  LYS A 390     2346   3034   2648     30   -172   -590       C  
ATOM   2894  C   LYS A 390       1.709  26.100   1.138  1.00 24.58           C  
ANISOU 2894  C   LYS A 390     2764   3473   3101     10   -143   -582       C  
ATOM   2895  O   LYS A 390       0.666  25.569   0.740  1.00 23.89           O  
ANISOU 2895  O   LYS A 390     2688   3387   3003     13   -120   -570       O  
ATOM   2896  CB  LYS A 390       1.540  27.680   3.104  1.00 21.34           C  
ANISOU 2896  CB  LYS A 390     2395   3050   2662     27   -187   -598       C  
ATOM   2897  CG  LYS A 390       1.211  27.701   4.590  1.00 25.79           C  
ANISOU 2897  CG  LYS A 390     2992   3612   3196     55   -205   -603       C  
ATOM   2898  CD  LYS A 390       1.315  29.093   5.202  1.00 32.46           C  
ANISOU 2898  CD  LYS A 390     3860   4442   4030     55   -233   -618       C  
ATOM   2899  CE  LYS A 390       0.962  29.053   6.683  1.00 34.44           C  
ANISOU 2899  CE  LYS A 390     4147   4691   4246     87   -249   -622       C  
ATOM   2900  NZ  LYS A 390       1.352  30.311   7.364  1.00 37.10           N  
ANISOU 2900  NZ  LYS A 390     4511   5011   4573     87   -284   -641       N  
ATOM   2901  N   HIS A 391       2.659  26.512   0.298  1.00 19.46           N  
ANISOU 2901  N   HIS A 391     2089   2827   2478     -9   -146   -586       N  
ATOM   2902  CA  HIS A 391       2.560  26.205  -1.123  1.00 20.37           C  
ANISOU 2902  CA  HIS A 391     2186   2946   2606    -24   -118   -579       C  
ATOM   2903  C   HIS A 391       2.437  24.705  -1.349  1.00 23.67           C  
ANISOU 2903  C   HIS A 391     2606   3369   3020    -10   -101   -572       C  
ATOM   2904  O   HIS A 391       1.560  24.246  -2.088  1.00 18.91           O  
ANISOU 2904  O   HIS A 391     2012   2763   2409    -14    -78   -564       O  
ATOM   2905  CB  HIS A 391       3.779  26.736  -1.875  1.00 19.69           C  
ANISOU 2905  CB  HIS A 391     2067   2867   2548    -42   -123   -581       C  
ATOM   2906  CG  HIS A 391       4.062  25.981  -3.135  1.00 18.96           C  
ANISOU 2906  CG  HIS A 391     1955   2783   2467    -45    -96   -574       C  
ATOM   2907  ND1 HIS A 391       3.324  26.152  -4.289  1.00 16.82           N  
ANISOU 2907  ND1 HIS A 391     1686   2510   2193    -60    -71   -570       N  
ATOM   2908  CD2 HIS A 391       4.969  25.013  -3.408  1.00 21.76           C  
ANISOU 2908  CD2 HIS A 391     2291   3147   2831    -33    -90   -572       C  
ATOM   2909  CE1 HIS A 391       3.784  25.339  -5.225  1.00 20.59           C  
ANISOU 2909  CE1 HIS A 391     2150   2996   2679    -56    -51   -566       C  
ATOM   2910  NE2 HIS A 391       4.776  24.632  -4.714  1.00 18.71           N  
ANISOU 2910  NE2 HIS A 391     1899   2764   2447    -38    -61   -567       N  
ATOM   2911  N   LEU A 392       3.340  23.927  -0.744  1.00 21.93           N  
ANISOU 2911  N   LEU A 392     2375   3152   2804      7   -113   -574       N  
ATOM   2912  CA  LEU A 392       3.338  22.488  -0.975  1.00 19.85           C  
ANISOU 2912  CA  LEU A 392     2113   2890   2538     22    -99   -569       C  
ATOM   2913  C   LEU A 392       2.006  21.872  -0.558  1.00 22.53           C  
ANISOU 2913  C   LEU A 392     2482   3222   2855     31    -92   -559       C  
ATOM   2914  O   LEU A 392       1.449  21.027  -1.275  1.00 19.40           O  
ANISOU 2914  O   LEU A 392     2095   2822   2456     30    -74   -551       O  
ATOM   2915  CB  LEU A 392       4.505  21.845  -0.223  1.00 21.23           C  
ANISOU 2915  CB  LEU A 392     2274   3072   2722     40   -116   -571       C  
ATOM   2916  CG  LEU A 392       5.912  22.032  -0.805  1.00 23.12           C  
ANISOU 2916  CG  LEU A 392     2477   3321   2986     35   -118   -571       C  
ATOM   2917  CD1 LEU A 392       6.946  21.373   0.091  1.00 26.12           C  
ANISOU 2917  CD1 LEU A 392     2844   3708   3373     54   -137   -569       C  
ATOM   2918  CD2 LEU A 392       6.010  21.483  -2.232  1.00 22.03           C  
ANISOU 2918  CD2 LEU A 392     2330   3185   2856     33    -88   -568       C  
ATOM   2919  N   GLN A 393       1.476  22.299   0.591  1.00 19.59           N  
ANISOU 2919  N   GLN A 393     2127   2850   2467     40   -107   -558       N  
ATOM   2920  CA  GLN A 393       0.170  21.827   1.044  1.00 22.04           C  
ANISOU 2920  CA  GLN A 393     2461   3157   2755     50    -99   -543       C  
ATOM   2921  C   GLN A 393      -0.934  22.250   0.082  1.00 22.67           C  
ANISOU 2921  C   GLN A 393     2549   3234   2832     31    -78   -533       C  
ATOM   2922  O   GLN A 393      -1.809  21.451  -0.270  1.00 20.54           O  
ANISOU 2922  O   GLN A 393     2289   2960   2555     30    -66   -516       O  
ATOM   2923  CB  GLN A 393      -0.133  22.361   2.448  1.00 23.30           C  
ANISOU 2923  CB  GLN A 393     2637   3320   2895     67   -117   -543       C  
ATOM   2924  CG  GLN A 393      -1.599  22.154   2.883  1.00 27.97           C  
ANISOU 2924  CG  GLN A 393     3251   3913   3464     77   -106   -522       C  
ATOM   2925  CD  GLN A 393      -2.129  23.248   3.824  1.00 36.55           C  
ANISOU 2925  CD  GLN A 393     4357   5002   4529     90   -114   -524       C  
ATOM   2926  OE1 GLN A 393      -3.318  23.602   3.788  1.00 35.94           O  
ANISOU 2926  OE1 GLN A 393     4292   4926   4436     92    -99   -507       O  
ATOM   2927  NE2 GLN A 393      -1.251  23.782   4.666  1.00 32.89           N  
ANISOU 2927  NE2 GLN A 393     3896   4538   4063     99   -138   -542       N  
ATOM   2928  N   LEU A 394      -0.934  23.522  -0.321  1.00 19.58           N  
ANISOU 2928  N   LEU A 394     2153   2842   2446     15    -77   -540       N  
ATOM   2929  CA  LEU A 394      -2.020  24.008  -1.164  1.00 18.89           C  
ANISOU 2929  CA  LEU A 394     2072   2751   2355     -2    -58   -528       C  
ATOM   2930  C   LEU A 394      -1.936  23.409  -2.558  1.00 16.85           C  
ANISOU 2930  C   LEU A 394     1803   2490   2108    -19    -41   -526       C  
ATOM   2931  O   LEU A 394      -2.966  23.127  -3.180  1.00 19.13           O  
ANISOU 2931  O   LEU A 394     2103   2776   2391    -30    -26   -509       O  
ATOM   2932  CB  LEU A 394      -2.000  25.537  -1.228  1.00 18.76           C  
ANISOU 2932  CB  LEU A 394     2053   2733   2341    -13    -62   -537       C  
ATOM   2933  CG  LEU A 394      -2.373  26.242   0.071  1.00 20.04           C  
ANISOU 2933  CG  LEU A 394     2236   2894   2484      6    -77   -539       C  
ATOM   2934  CD1 LEU A 394      -2.264  27.755  -0.105  1.00 15.18           C  
ANISOU 2934  CD1 LEU A 394     1621   2272   1874     -7    -84   -550       C  
ATOM   2935  CD2 LEU A 394      -3.784  25.840   0.476  1.00 21.07           C  
ANISOU 2935  CD2 LEU A 394     2385   3027   2592     20    -63   -516       C  
ATOM   2936  N   LYS A 395      -0.721  23.206  -3.071  1.00 17.64           N  
ANISOU 2936  N   LYS A 395     1884   2592   2225    -21    -42   -539       N  
ATOM   2937  CA  LYS A 395      -0.583  22.505  -4.346  1.00 16.92           C  
ANISOU 2937  CA  LYS A 395     1788   2499   2140    -31    -25   -538       C  
ATOM   2938  C   LYS A 395      -1.147  21.093  -4.248  1.00 18.72           C  
ANISOU 2938  C   LYS A 395     2036   2720   2358    -20    -23   -527       C  
ATOM   2939  O   LYS A 395      -1.905  20.650  -5.119  1.00 17.67           O  
ANISOU 2939  O   LYS A 395     1916   2579   2220    -33    -11   -517       O  
ATOM   2940  CB  LYS A 395       0.879  22.475  -4.776  1.00 16.61           C  
ANISOU 2940  CB  LYS A 395     1724   2467   2120    -28    -26   -551       C  
ATOM   2941  CG  LYS A 395       1.146  21.582  -5.978  1.00 14.13           C  
ANISOU 2941  CG  LYS A 395     1410   2151   1808    -28     -7   -551       C  
ATOM   2942  CD  LYS A 395       2.621  21.630  -6.381  1.00 20.28           C  
ANISOU 2942  CD  LYS A 395     2161   2941   2605    -20     -5   -559       C  
ATOM   2943  CE  LYS A 395       2.899  20.747  -7.596  1.00 23.43           C  
ANISOU 2943  CE  LYS A 395     2563   3338   3002    -14     17   -560       C  
ATOM   2944  NZ  LYS A 395       4.340  20.754  -7.970  1.00 22.39           N  
ANISOU 2944  NZ  LYS A 395     2400   3221   2886     -1     23   -563       N  
ATOM   2945  N   GLU A 396      -0.805  20.379  -3.174  1.00 20.45           N  
ANISOU 2945  N   GLU A 396     2258   2938   2573      2    -37   -527       N  
ATOM   2946  CA  GLU A 396      -1.289  19.015  -3.000  1.00 21.60           C  
ANISOU 2946  CA  GLU A 396     2422   3075   2710     12    -38   -515       C  
ATOM   2947  C   GLU A 396      -2.804  18.979  -2.864  1.00 21.34           C  
ANISOU 2947  C   GLU A 396     2407   3038   2662      3    -36   -491       C  
ATOM   2948  O   GLU A 396      -3.463  18.093  -3.419  1.00 20.61           O  
ANISOU 2948  O   GLU A 396     2330   2935   2566     -4    -32   -477       O  
ATOM   2949  CB  GLU A 396      -0.618  18.377  -1.786  1.00 23.82           C  
ANISOU 2949  CB  GLU A 396     2701   3360   2991     38    -54   -518       C  
ATOM   2950  CG  GLU A 396      -1.179  17.014  -1.401  1.00 29.77           C  
ANISOU 2950  CG  GLU A 396     3472   4104   3736     49    -60   -502       C  
ATOM   2951  CD  GLU A 396      -1.021  15.965  -2.496  1.00 39.48           C  
ANISOU 2951  CD  GLU A 396     4712   5318   4971     46    -51   -504       C  
ATOM   2952  OE1 GLU A 396      -0.097  16.082  -3.343  1.00 40.07           O  
ANISOU 2952  OE1 GLU A 396     4776   5394   5056     46    -41   -521       O  
ATOM   2953  OE2 GLU A 396      -1.832  15.013  -2.509  1.00 46.40           O  
ANISOU 2953  OE2 GLU A 396     5609   6182   5840     45    -55   -487       O  
ATOM   2954  N   GLU A 397      -3.380  19.940  -2.142  1.00 18.84           N  
ANISOU 2954  N   GLU A 397     2091   2730   2338      4    -38   -485       N  
ATOM   2955  CA  GLU A 397      -4.835  20.019  -2.068  1.00 23.32           C  
ANISOU 2955  CA  GLU A 397     2671   3297   2891     -4    -32   -457       C  
ATOM   2956  C   GLU A 397      -5.452  20.243  -3.440  1.00 19.84           C  
ANISOU 2956  C   GLU A 397     2232   2850   2455    -31    -18   -449       C  
ATOM   2957  O   GLU A 397      -6.478  19.642  -3.772  1.00 19.37           O  
ANISOU 2957  O   GLU A 397     2185   2785   2390    -42    -16   -424       O  
ATOM   2958  CB  GLU A 397      -5.255  21.126  -1.101  1.00 20.28           C  
ANISOU 2958  CB  GLU A 397     2287   2922   2495      7    -34   -454       C  
ATOM   2959  CG  GLU A 397      -4.959  20.758   0.335  1.00 22.76           C  
ANISOU 2959  CG  GLU A 397     2606   3243   2799     36    -49   -454       C  
ATOM   2960  CD  GLU A 397      -5.286  21.858   1.327  1.00 28.19           C  
ANISOU 2960  CD  GLU A 397     3301   3940   3471     51    -53   -454       C  
ATOM   2961  OE1 GLU A 397      -5.876  22.893   0.936  1.00 29.17           O  
ANISOU 2961  OE1 GLU A 397     3427   4064   3592     41    -42   -451       O  
ATOM   2962  OE2 GLU A 397      -4.953  21.669   2.512  1.00 28.04           O  
ANISOU 2962  OE2 GLU A 397     3287   3926   3441     76    -66   -458       O  
ATOM   2963  N   SER A 398      -4.848  21.108  -4.253  1.00 18.50           N  
ANISOU 2963  N   SER A 398     2050   2682   2296    -45    -10   -468       N  
ATOM   2964  CA  SER A 398      -5.431  21.374  -5.560  1.00 19.13           C  
ANISOU 2964  CA  SER A 398     2132   2759   2379    -71      4   -460       C  
ATOM   2965  C   SER A 398      -5.268  20.187  -6.487  1.00 18.26           C  
ANISOU 2965  C   SER A 398     2032   2636   2270    -78      6   -461       C  
ATOM   2966  O   SER A 398      -6.147  19.920  -7.310  1.00 18.03           O  
ANISOU 2966  O   SER A 398     2016   2599   2236    -98     10   -444       O  
ATOM   2967  CB  SER A 398      -4.812  22.617  -6.182  1.00 18.36           C  
ANISOU 2967  CB  SER A 398     2017   2667   2293    -83     12   -478       C  
ATOM   2968  OG  SER A 398      -5.458  23.762  -5.677  1.00 19.23           O  
ANISOU 2968  OG  SER A 398     2126   2782   2398    -85     13   -470       O  
ATOM   2969  N   VAL A 399      -4.142  19.476  -6.384  1.00 18.46           N  
ANISOU 2969  N   VAL A 399     2055   2659   2301    -61      1   -480       N  
ATOM   2970  CA  VAL A 399      -3.966  18.265  -7.177  1.00 19.09           C  
ANISOU 2970  CA  VAL A 399     2152   2724   2379    -61      2   -482       C  
ATOM   2971  C   VAL A 399      -4.965  17.203  -6.747  1.00 18.07           C  
ANISOU 2971  C   VAL A 399     2045   2582   2240    -61    -11   -458       C  
ATOM   2972  O   VAL A 399      -5.591  16.546  -7.586  1.00 17.38           O  
ANISOU 2972  O   VAL A 399     1978   2478   2146    -77    -12   -447       O  
ATOM   2973  CB  VAL A 399      -2.518  17.759  -7.071  1.00 19.89           C  
ANISOU 2973  CB  VAL A 399     2243   2826   2489    -37      1   -505       C  
ATOM   2974  CG1 VAL A 399      -2.408  16.341  -7.633  1.00 21.66           C  
ANISOU 2974  CG1 VAL A 399     2491   3031   2707    -29      0   -507       C  
ATOM   2975  CG2 VAL A 399      -1.591  18.710  -7.799  1.00 17.56           C  
ANISOU 2975  CG2 VAL A 399     1924   2543   2204    -42     15   -522       C  
ATOM   2976  N   LYS A 400      -5.132  17.018  -5.434  1.00 20.85           N  
ANISOU 2976  N   LYS A 400     2394   2939   2589    -44    -22   -448       N  
ATOM   2977  CA  LYS A 400      -6.136  16.075  -4.945  1.00 22.08           C  
ANISOU 2977  CA  LYS A 400     2567   3085   2737    -45    -35   -418       C  
ATOM   2978  C   LYS A 400      -7.525  16.436  -5.459  1.00 22.59           C  
ANISOU 2978  C   LYS A 400     2638   3149   2795    -72    -32   -388       C  
ATOM   2979  O   LYS A 400      -8.287  15.566  -5.895  1.00 20.85           O  
ANISOU 2979  O   LYS A 400     2436   2914   2572    -87    -41   -366       O  
ATOM   2980  CB  LYS A 400      -6.124  16.043  -3.418  1.00 26.42           C  
ANISOU 2980  CB  LYS A 400     3109   3648   3283    -21    -44   -410       C  
ATOM   2981  CG  LYS A 400      -7.309  15.294  -2.796  1.00 39.47           C  
ANISOU 2981  CG  LYS A 400     4773   5297   4927    -23    -56   -371       C  
ATOM   2982  CD  LYS A 400      -7.276  15.358  -1.259  1.00 49.32           C  
ANISOU 2982  CD  LYS A 400     6012   6561   6167      4    -62   -363       C  
ATOM   2983  CE  LYS A 400      -8.573  14.848  -0.627  1.00 47.66           C  
ANISOU 2983  CE  LYS A 400     5807   6354   5948      3    -70   -317       C  
ATOM   2984  NZ  LYS A 400      -8.839  13.406  -0.907  1.00 47.88           N  
ANISOU 2984  NZ  LYS A 400     5850   6363   5981     -5    -86   -298       N  
ATOM   2985  N   LEU A 401      -7.867  17.722  -5.409  1.00 17.54           N  
ANISOU 2985  N   LEU A 401     1984   2525   2155    -78    -20   -386       N  
ATOM   2986  CA  LEU A 401      -9.141  18.176  -5.941  1.00 20.83           C  
ANISOU 2986  CA  LEU A 401     2404   2944   2568   -103    -14   -356       C  
ATOM   2987  C   LEU A 401      -9.280  17.789  -7.403  1.00 20.64           C  
ANISOU 2987  C   LEU A 401     2393   2904   2546   -130    -13   -358       C  
ATOM   2988  O   LEU A 401     -10.290  17.202  -7.812  1.00 20.66           O  
ANISOU 2988  O   LEU A 401     2409   2896   2544   -150    -22   -327       O  
ATOM   2989  CB  LEU A 401      -9.256  19.691  -5.768  1.00 19.23           C  
ANISOU 2989  CB  LEU A 401     2183   2757   2365   -102      0   -360       C  
ATOM   2990  CG  LEU A 401     -10.606  20.343  -6.082  1.00 25.00           C  
ANISOU 2990  CG  LEU A 401     2913   3495   3091   -121      9   -326       C  
ATOM   2991  CD1 LEU A 401     -10.659  21.688  -5.363  1.00 24.16           C  
ANISOU 2991  CD1 LEU A 401     2794   3404   2982   -106     19   -330       C  
ATOM   2992  CD2 LEU A 401     -10.802  20.539  -7.568  1.00 20.52           C  
ANISOU 2992  CD2 LEU A 401     2348   2919   2529   -153     16   -327       C  
ATOM   2993  N   PHE A 402      -8.278  18.138  -8.210  1.00 18.43           N  
ANISOU 2993  N   PHE A 402     2108   2622   2271   -131     -3   -391       N  
ATOM   2994  CA  PHE A 402      -8.302  17.790  -9.623  1.00 16.78           C  
ANISOU 2994  CA  PHE A 402     1915   2399   2060   -152      0   -396       C  
ATOM   2995  C   PHE A 402      -8.530  16.294  -9.823  1.00 16.41           C  
ANISOU 2995  C   PHE A 402     1898   2329   2008   -153    -18   -387       C  
ATOM   2996  O   PHE A 402      -9.368  15.883 -10.629  1.00 18.95           O  
ANISOU 2996  O   PHE A 402     2240   2637   2324   -179    -26   -368       O  
ATOM   2997  CB  PHE A 402      -6.997  18.202 -10.302  1.00 16.44           C  
ANISOU 2997  CB  PHE A 402     1862   2361   2023   -143     14   -432       C  
ATOM   2998  CG  PHE A 402      -6.844  17.599 -11.667  1.00 17.52           C  
ANISOU 2998  CG  PHE A 402     2021   2483   2154   -155     17   -441       C  
ATOM   2999  CD1 PHE A 402      -7.606  18.071 -12.719  1.00 13.87           C  
ANISOU 2999  CD1 PHE A 402     1564   2019   1686   -185     22   -429       C  
ATOM   3000  CD2 PHE A 402      -5.994  16.523 -11.882  1.00 20.56           C  
ANISOU 3000  CD2 PHE A 402     2422   2853   2535   -135     13   -461       C  
ATOM   3001  CE1 PHE A 402      -7.499  17.510 -13.977  1.00 18.94           C  
ANISOU 3001  CE1 PHE A 402     2231   2646   2319   -195     23   -438       C  
ATOM   3002  CE2 PHE A 402      -5.881  15.951 -13.144  1.00 19.53           C  
ANISOU 3002  CE2 PHE A 402     2319   2708   2395   -142     16   -470       C  
ATOM   3003  CZ  PHE A 402      -6.635  16.443 -14.187  1.00 17.72           C  
ANISOU 3003  CZ  PHE A 402     2097   2477   2158   -173     20   -459       C  
ATOM   3004  N   ARG A 403      -7.791  15.463  -9.095  1.00 17.99           N  
ANISOU 3004  N   ARG A 403     2103   2524   2210   -127    -27   -400       N  
ATOM   3005  CA  ARG A 403      -7.851  14.031  -9.354  1.00 20.62           C  
ANISOU 3005  CA  ARG A 403     2467   2830   2537   -126    -44   -396       C  
ATOM   3006  C   ARG A 403      -9.153  13.419  -8.848  1.00 22.41           C  
ANISOU 3006  C   ARG A 403     2705   3049   2762   -142    -65   -354       C  
ATOM   3007  O   ARG A 403      -9.644  12.439  -9.426  1.00 20.71           O  
ANISOU 3007  O   ARG A 403     2520   2808   2542   -158    -84   -341       O  
ATOM   3008  CB  ARG A 403      -6.637  13.345  -8.723  1.00 23.13           C  
ANISOU 3008  CB  ARG A 403     2784   3146   2860    -92    -46   -421       C  
ATOM   3009  CG  ARG A 403      -5.326  13.888  -9.262  1.00 25.75           C  
ANISOU 3009  CG  ARG A 403     3100   3487   3195    -76    -26   -457       C  
ATOM   3010  CD  ARG A 403      -4.143  13.065  -8.820  1.00 29.95           C  
ANISOU 3010  CD  ARG A 403     3633   4014   3731    -43    -28   -478       C  
ATOM   3011  NE  ARG A 403      -4.093  11.790  -9.521  1.00 32.69           N  
ANISOU 3011  NE  ARG A 403     4018   4332   4070    -39    -37   -482       N  
ATOM   3012  CZ  ARG A 403      -3.094  10.924  -9.417  1.00 38.22           C  
ANISOU 3012  CZ  ARG A 403     4728   5023   4772     -9    -37   -500       C  
ATOM   3013  NH1 ARG A 403      -2.044  11.172  -8.648  1.00 33.84           N  
ANISOU 3013  NH1 ARG A 403     4144   4487   4228     17    -30   -513       N  
ATOM   3014  NH2 ARG A 403      -3.151   9.783 -10.101  1.00 33.78           N  
ANISOU 3014  NH2 ARG A 403     4205   4429   4199     -4    -47   -505       N  
ATOM   3015  N   GLY A 404      -9.731  13.983  -7.788  1.00 19.79           N  
ANISOU 3015  N   GLY A 404     2351   2737   2432   -138    -64   -330       N  
ATOM   3016  CA  GLY A 404     -10.949  13.434  -7.225  1.00 23.98           C  
ANISOU 3016  CA  GLY A 404     2886   3265   2961   -149    -81   -283       C  
ATOM   3017  C   GLY A 404     -12.203  13.790  -7.985  1.00 21.64           C  
ANISOU 3017  C   GLY A 404     2592   2967   2662   -185    -83   -248       C  
ATOM   3018  O   GLY A 404     -13.216  13.104  -7.835  1.00 24.46           O  
ANISOU 3018  O   GLY A 404     2959   3316   3020   -202   -103   -206       O  
ATOM   3019  N   VAL A 405     -12.157  14.843  -8.802  1.00 20.51           N  
ANISOU 3019  N   VAL A 405     2441   2833   2518   -198    -65   -262       N  
ATOM   3020  CA  VAL A 405     -13.334  15.250  -9.554  1.00 21.08           C  
ANISOU 3020  CA  VAL A 405     2513   2906   2589   -232    -66   -228       C  
ATOM   3021  C   VAL A 405     -13.721  14.151 -10.526  1.00 19.77           C  
ANISOU 3021  C   VAL A 405     2382   2710   2420   -259    -91   -217       C  
ATOM   3022  O   VAL A 405     -12.898  13.661 -11.307  1.00 18.38           O  
ANISOU 3022  O   VAL A 405     2229   2515   2240   -257    -93   -253       O  
ATOM   3023  CB  VAL A 405     -13.078  16.586 -10.271  1.00 20.14           C  
ANISOU 3023  CB  VAL A 405     2379   2802   2471   -239    -41   -249       C  
ATOM   3024  CG1 VAL A 405     -14.078  16.785 -11.407  1.00 20.17           C  
ANISOU 3024  CG1 VAL A 405     2391   2800   2473   -278    -45   -221       C  
ATOM   3025  CG2 VAL A 405     -13.186  17.729  -9.260  1.00 23.97           C  
ANISOU 3025  CG2 VAL A 405     2834   3314   2958   -219    -24   -243       C  
ATOM   3026  N   LYS A 406     -14.986  13.758 -10.479  1.00 23.72           N  
ANISOU 3026  N   LYS A 406     2885   3205   2921   -285   -110   -165       N  
ATOM   3027  CA  LYS A 406     -15.485  12.703 -11.344  1.00 22.20           C  
ANISOU 3027  CA  LYS A 406     2728   2981   2725   -316   -140   -149       C  
ATOM   3028  C   LYS A 406     -15.507  13.191 -12.788  1.00 19.80           C  
ANISOU 3028  C   LYS A 406     2439   2670   2415   -342   -134   -165       C  
ATOM   3029  O   LYS A 406     -16.122  14.214 -13.096  1.00 19.33           O  
ANISOU 3029  O   LYS A 406     2358   2630   2357   -359   -120   -146       O  
ATOM   3030  CB  LYS A 406     -16.883  12.288 -10.886  1.00 23.62           C  
ANISOU 3030  CB  LYS A 406     2901   3162   2910   -340   -164    -82       C  
ATOM   3031  CG  LYS A 406     -17.366  10.992 -11.497  1.00 28.28           C  
ANISOU 3031  CG  LYS A 406     3530   3715   3499   -370   -205    -60       C  
ATOM   3032  CD  LYS A 406     -16.735   9.783 -10.831  1.00 34.95           C  
ANISOU 3032  CD  LYS A 406     4396   4538   4346   -348   -224    -75       C  
ATOM   3033  CE  LYS A 406     -17.678   9.163  -9.816  1.00 32.31           C  
ANISOU 3033  CE  LYS A 406     4047   4208   4020   -354   -247    -14       C  
ATOM   3034  NZ  LYS A 406     -17.217   7.806  -9.406  1.00 34.98           N  
ANISOU 3034  NZ  LYS A 406     4412   4516   4361   -342   -276    -22       N  
ATOM   3035  N   LYS A 407     -14.845  12.460 -13.676  1.00 18.03           N  
ANISOU 3035  N   LYS A 407     2252   2417   2182   -343   -145   -198       N  
ATOM   3036  CA  LYS A 407     -14.709  12.885 -15.061  1.00 19.19           C  
ANISOU 3036  CA  LYS A 407     2416   2558   2319   -363   -137   -219       C  
ATOM   3037  C   LYS A 407     -14.897  11.694 -15.977  1.00 20.13           C  
ANISOU 3037  C   LYS A 407     2588   2636   2426   -383   -171   -220       C  
ATOM   3038  O   LYS A 407     -14.526  10.567 -15.635  1.00 22.97           O  
ANISOU 3038  O   LYS A 407     2974   2970   2783   -368   -191   -229       O  
ATOM   3039  CB  LYS A 407     -13.324  13.482 -15.367  1.00 17.75           C  
ANISOU 3039  CB  LYS A 407     2225   2388   2133   -332   -105   -274       C  
ATOM   3040  CG  LYS A 407     -12.852  14.589 -14.434  1.00 16.28           C  
ANISOU 3040  CG  LYS A 407     1992   2235   1958   -307    -76   -284       C  
ATOM   3041  CD  LYS A 407     -11.403  14.922 -14.761  1.00 17.27           C  
ANISOU 3041  CD  LYS A 407     2113   2368   2082   -278    -53   -335       C  
ATOM   3042  CE  LYS A 407     -10.584  15.274 -13.520  1.00 17.27           C  
ANISOU 3042  CE  LYS A 407     2083   2387   2093   -243    -39   -351       C  
ATOM   3043  NZ  LYS A 407     -10.521  14.181 -12.510  1.00 17.52           N  
ANISOU 3043  NZ  LYS A 407     2125   2406   2125   -225    -58   -344       N  
ATOM   3044  N   MET A 408     -15.434  11.955 -17.163  1.00 18.01           N  
ANISOU 3044  N   MET A 408     2337   2359   2148   -417   -177   -211       N  
ATOM   3045  CA  MET A 408     -15.405  10.928 -18.188  1.00 21.83           C  
ANISOU 3045  CA  MET A 408     2879   2803   2614   -432   -206   -224       C  
ATOM   3046  C   MET A 408     -13.973  10.706 -18.652  1.00 20.66           C  
ANISOU 3046  C   MET A 408     2752   2646   2451   -394   -186   -285       C  
ATOM   3047  O   MET A 408     -13.127  11.602 -18.583  1.00 18.39           O  
ANISOU 3047  O   MET A 408     2432   2387   2168   -368   -148   -314       O  
ATOM   3048  CB  MET A 408     -16.286  11.312 -19.364  1.00 18.23           C  
ANISOU 3048  CB  MET A 408     2436   2341   2148   -476   -218   -202       C  
ATOM   3049  CG  MET A 408     -17.716  11.521 -18.957  1.00 23.46           C  
ANISOU 3049  CG  MET A 408     3075   3014   2826   -514   -238   -135       C  
ATOM   3050  SD  MET A 408     -18.799  11.005 -20.275  1.00 29.66           S  
ANISOU 3050  SD  MET A 408     3907   3766   3598   -572   -282   -103       S  
ATOM   3051  CE  MET A 408     -20.375  11.508 -19.585  1.00 24.16           C  
ANISOU 3051  CE  MET A 408     3161   3094   2923   -609   -294    -19       C  
ATOM   3052  N   GLY A 409     -13.697   9.486 -19.097  1.00 21.64           N  
ANISOU 3052  N   GLY A 409     2931   2730   2561   -388   -212   -302       N  
ATOM   3053  CA  GLY A 409     -12.405   9.141 -19.642  1.00 23.77           C  
ANISOU 3053  CA  GLY A 409     3228   2988   2814   -350   -193   -356       C  
ATOM   3054  C   GLY A 409     -11.489   8.415 -18.681  1.00 24.17           C  
ANISOU 3054  C   GLY A 409     3277   3033   2872   -307   -190   -378       C  
ATOM   3055  O   GLY A 409     -10.501   7.823 -19.124  1.00 29.25           O  
ANISOU 3055  O   GLY A 409     3953   3659   3500   -274   -182   -417       O  
ATOM   3056  N   GLY A 410     -11.778   8.457 -17.386  1.00 21.60           N  
ANISOU 3056  N   GLY A 410     2916   2723   2568   -304   -194   -352       N  
ATOM   3057  CA  GLY A 410     -11.039   7.676 -16.420  1.00 28.81           C  
ANISOU 3057  CA  GLY A 410     3829   3628   3488   -267   -196   -366       C  
ATOM   3058  C   GLY A 410      -9.924   8.466 -15.750  1.00 31.19           C  
ANISOU 3058  C   GLY A 410     4084   3967   3800   -228   -156   -393       C  
ATOM   3059  O   GLY A 410      -9.542   9.566 -16.164  1.00 29.11           O  
ANISOU 3059  O   GLY A 410     3792   3732   3536   -226   -125   -408       O  
ATOM   3060  N   GLU A 411      -9.393   7.863 -14.688  1.00 30.01           N  
ANISOU 3060  N   GLU A 411     3926   3816   3660   -199   -160   -397       N  
ATOM   3061  CA  GLU A 411      -8.299   8.481 -13.950  1.00 31.61           C  
ANISOU 3061  CA  GLU A 411     4087   4051   3874   -163   -128   -421       C  
ATOM   3062  C   GLU A 411      -7.004   8.438 -14.748  1.00 27.31           C  
ANISOU 3062  C   GLU A 411     3554   3504   3318   -130   -104   -465       C  
ATOM   3063  O   GLU A 411      -6.182   9.356 -14.643  1.00 29.64           O  
ANISOU 3063  O   GLU A 411     3811   3831   3619   -112    -73   -483       O  
ATOM   3064  CB  GLU A 411      -8.136   7.789 -12.593  1.00 32.97           C  
ANISOU 3064  CB  GLU A 411     4248   4220   4058   -142   -142   -410       C  
ATOM   3065  CG  GLU A 411      -7.106   8.418 -11.681  1.00 37.41           C  
ANISOU 3065  CG  GLU A 411     4766   4815   4632   -108   -116   -429       C  
ATOM   3066  CD  GLU A 411      -5.718   7.856 -11.904  1.00 38.64           C  
ANISOU 3066  CD  GLU A 411     4934   4962   4784    -68   -102   -467       C  
ATOM   3067  OE1 GLU A 411      -5.613   6.698 -12.363  1.00 40.03           O  
ANISOU 3067  OE1 GLU A 411     5155   5103   4950    -60   -119   -475       O  
ATOM   3068  OE2 GLU A 411      -4.733   8.576 -11.620  1.00 42.77           O  
ANISOU 3068  OE2 GLU A 411     5422   5514   5315    -45    -77   -487       O  
ATOM   3069  N   GLU A 412      -6.813   7.407 -15.571  1.00 29.56           N  
ANISOU 3069  N   GLU A 412     3893   3752   3585   -122   -117   -481       N  
ATOM   3070  CA  GLU A 412      -5.576   7.320 -16.337  1.00 30.82           C  
ANISOU 3070  CA  GLU A 412     4066   3913   3732    -86    -91   -520       C  
ATOM   3071  C   GLU A 412      -5.509   8.406 -17.399  1.00 31.41           C  
ANISOU 3071  C   GLU A 412     4127   4010   3797    -98    -65   -530       C  
ATOM   3072  O   GLU A 412      -4.440   8.984 -17.635  1.00 33.26           O  
ANISOU 3072  O   GLU A 412     4335   4269   4032    -70    -32   -553       O  
ATOM   3073  CB  GLU A 412      -5.432   5.943 -16.982  1.00 35.94           C  
ANISOU 3073  CB  GLU A 412     4781   4513   4360    -70   -112   -536       C  
ATOM   3074  CG  GLU A 412      -4.164   5.818 -17.816  1.00 41.17           C  
ANISOU 3074  CG  GLU A 412     5459   5177   5005    -26    -81   -574       C  
ATOM   3075  CD  GLU A 412      -4.078   4.508 -18.590  1.00 53.65           C  
ANISOU 3075  CD  GLU A 412     7116   6709   6560     -9   -101   -592       C  
ATOM   3076  OE1 GLU A 412      -5.095   3.777 -18.654  1.00 49.60           O  
ANISOU 3076  OE1 GLU A 412     6647   6158   6042    -40   -142   -574       O  
ATOM   3077  OE2 GLU A 412      -2.989   4.217 -19.138  1.00 50.09           O  
ANISOU 3077  OE2 GLU A 412     6682   6257   6094     36    -75   -622       O  
ATOM   3078  N   PHE A 413      -6.638   8.698 -18.050  1.00 26.56           N  
ANISOU 3078  N   PHE A 413     3529   3388   3176   -141    -81   -510       N  
ATOM   3079  CA  PHE A 413      -6.671   9.793 -19.015  1.00 26.60           C  
ANISOU 3079  CA  PHE A 413     3518   3416   3174   -157    -57   -514       C  
ATOM   3080  C   PHE A 413      -6.274  11.114 -18.363  1.00 21.36           C  
ANISOU 3080  C   PHE A 413     2788   2797   2532   -153    -29   -512       C  
ATOM   3081  O   PHE A 413      -5.488  11.883 -18.926  1.00 23.01           O  
ANISOU 3081  O   PHE A 413     2974   3030   2739   -139      1   -530       O  
ATOM   3082  CB  PHE A 413      -8.061   9.894 -19.640  1.00 26.45           C  
ANISOU 3082  CB  PHE A 413     3522   3381   3147   -207    -83   -486       C  
ATOM   3083  CG  PHE A 413      -8.177  10.955 -20.692  1.00 26.03           C  
ANISOU 3083  CG  PHE A 413     3456   3350   3085   -226    -61   -488       C  
ATOM   3084  CD1 PHE A 413      -7.629  10.766 -21.950  1.00 28.67           C  
ANISOU 3084  CD1 PHE A 413     3826   3674   3394   -213    -49   -515       C  
ATOM   3085  CD2 PHE A 413      -8.842  12.140 -20.430  1.00 22.32           C  
ANISOU 3085  CD2 PHE A 413     2940   2909   2631   -255    -53   -463       C  
ATOM   3086  CE1 PHE A 413      -7.740  11.736 -22.923  1.00 28.74           C  
ANISOU 3086  CE1 PHE A 413     3822   3704   3395   -231    -30   -516       C  
ATOM   3087  CE2 PHE A 413      -8.962  13.116 -21.407  1.00 20.31           C  
ANISOU 3087  CE2 PHE A 413     2673   2672   2370   -274    -34   -464       C  
ATOM   3088  CZ  PHE A 413      -8.406  12.913 -22.652  1.00 22.78           C  
ANISOU 3088  CZ  PHE A 413     3019   2977   2658   -262    -23   -490       C  
ATOM   3089  N   SER A 414      -6.818  11.401 -17.177  1.00 23.36           N  
ANISOU 3089  N   SER A 414     3009   3061   2804   -164    -39   -487       N  
ATOM   3090  CA  SER A 414      -6.441  12.614 -16.457  1.00 22.21           C  
ANISOU 3090  CA  SER A 414     2807   2954   2678   -159    -17   -487       C  
ATOM   3091  C   SER A 414      -4.961  12.607 -16.120  1.00 22.88           C  
ANISOU 3091  C   SER A 414     2871   3053   2768   -116      5   -515       C  
ATOM   3092  O   SER A 414      -4.255  13.600 -16.333  1.00 18.37           O  
ANISOU 3092  O   SER A 414     2266   2510   2205   -108     30   -527       O  
ATOM   3093  CB  SER A 414      -7.248  12.751 -15.166  1.00 21.95           C  
ANISOU 3093  CB  SER A 414     2753   2928   2660   -171    -33   -457       C  
ATOM   3094  OG  SER A 414      -8.595  13.066 -15.422  1.00 25.11           O  
ANISOU 3094  OG  SER A 414     3157   3326   3059   -210    -46   -424       O  
ATOM   3095  N   ARG A 415      -4.486  11.493 -15.558  1.00 23.55           N  
ANISOU 3095  N   ARG A 415     2975   3120   2852    -89     -7   -524       N  
ATOM   3096  CA  ARG A 415      -3.107  11.415 -15.098  1.00 26.38           C  
ANISOU 3096  CA  ARG A 415     3311   3493   3220    -48     11   -545       C  
ATOM   3097  C   ARG A 415      -2.137  11.536 -16.264  1.00 25.08           C  
ANISOU 3097  C   ARG A 415     3152   3335   3043    -26     37   -569       C  
ATOM   3098  O   ARG A 415      -1.133  12.255 -16.177  1.00 22.49           O  
ANISOU 3098  O   ARG A 415     2785   3036   2726     -8     61   -579       O  
ATOM   3099  CB  ARG A 415      -2.893  10.106 -14.336  1.00 27.48           C  
ANISOU 3099  CB  ARG A 415     3475   3608   3360    -24     -8   -547       C  
ATOM   3100  CG  ARG A 415      -1.442   9.714 -14.147  1.00 32.30           C  
ANISOU 3100  CG  ARG A 415     4074   4225   3973     22      9   -569       C  
ATOM   3101  CD  ARG A 415      -1.305   8.582 -13.139  1.00 34.22           C  
ANISOU 3101  CD  ARG A 415     4330   4449   4222     43    -11   -566       C  
ATOM   3102  NE  ARG A 415      -2.295   7.532 -13.347  1.00 37.75           N  
ANISOU 3102  NE  ARG A 415     4830   4857   4658     26    -41   -554       N  
ATOM   3103  CZ  ARG A 415      -2.146   6.497 -14.165  1.00 46.51           C  
ANISOU 3103  CZ  ARG A 415     5991   5932   5749     41    -48   -568       C  
ATOM   3104  NH1 ARG A 415      -1.047   6.341 -14.895  1.00 48.19           N  
ANISOU 3104  NH1 ARG A 415     6213   6147   5951     77    -22   -595       N  
ATOM   3105  NH2 ARG A 415      -3.124   5.593 -14.253  1.00 38.24           N  
ANISOU 3105  NH2 ARG A 415     4989   4847   4694     19    -81   -554       N  
ATOM   3106  N   ARG A 416      -2.435  10.868 -17.380  1.00 25.32           N  
ANISOU 3106  N   ARG A 416     3231   3339   3050    -29     33   -577       N  
ATOM   3107  CA  ARG A 416      -1.489  10.873 -18.487  1.00 25.50           C  
ANISOU 3107  CA  ARG A 416     3264   3368   3057     -2     60   -599       C  
ATOM   3108  C   ARG A 416      -1.504  12.187 -19.247  1.00 25.37           C  
ANISOU 3108  C   ARG A 416     3216   3381   3041    -22     82   -596       C  
ATOM   3109  O   ARG A 416      -0.492  12.552 -19.853  1.00 29.59           O  
ANISOU 3109  O   ARG A 416     3733   3938   3573      3    111   -609       O  
ATOM   3110  CB  ARG A 416      -1.775   9.714 -19.444  1.00 30.75           C  
ANISOU 3110  CB  ARG A 416     3999   3993   3692      5     47   -611       C  
ATOM   3111  CG  ARG A 416      -1.502   8.349 -18.850  1.00 38.84           C  
ANISOU 3111  CG  ARG A 416     5058   4986   4714     34     29   -618       C  
ATOM   3112  CD  ARG A 416      -1.541   7.266 -19.928  1.00 49.20           C  
ANISOU 3112  CD  ARG A 416     6442   6257   5993     49     20   -635       C  
ATOM   3113  NE  ARG A 416      -1.277   5.944 -19.371  1.00 59.93           N  
ANISOU 3113  NE  ARG A 416     7837   7582   7350     78      1   -642       N  
ATOM   3114  CZ  ARG A 416      -0.067   5.426 -19.205  1.00 57.24           C  
ANISOU 3114  CZ  ARG A 416     7495   7244   7008    131     22   -660       C  
ATOM   3115  NH1 ARG A 416       1.022   6.079 -19.577  1.00 49.95           N  
ANISOU 3115  NH1 ARG A 416     6535   6357   6085    162     62   -672       N  
ATOM   3116  NH2 ARG A 416       0.054   4.224 -18.646  1.00 58.96           N  
ANISOU 3116  NH2 ARG A 416     7746   7429   7226    153      1   -664       N  
ATOM   3117  N   ASN A 417      -2.624  12.918 -19.236  1.00 22.08           N  
ANISOU 3117  N   ASN A 417     2791   2969   2630    -66     70   -576       N  
ATOM   3118  CA  ASN A 417      -2.769  14.042 -20.149  1.00 21.97           C  
ANISOU 3118  CA  ASN A 417     2757   2977   2614    -88     89   -573       C  
ATOM   3119  C   ASN A 417      -2.912  15.409 -19.494  1.00 22.39           C  
ANISOU 3119  C   ASN A 417     2754   3061   2693   -109     96   -559       C  
ATOM   3120  O   ASN A 417      -2.755  16.411 -20.194  1.00 20.59           O  
ANISOU 3120  O   ASN A 417     2502   2855   2467   -120    114   -558       O  
ATOM   3121  CB  ASN A 417      -3.975  13.829 -21.075  1.00 23.00           C  
ANISOU 3121  CB  ASN A 417     2930   3084   2724   -124     71   -562       C  
ATOM   3122  CG  ASN A 417      -3.736  12.736 -22.088  1.00 27.16           C  
ANISOU 3122  CG  ASN A 417     3517   3582   3220   -105     69   -581       C  
ATOM   3123  OD1 ASN A 417      -2.972  12.918 -23.029  1.00 27.81           O  
ANISOU 3123  OD1 ASN A 417     3602   3677   3287    -83     95   -597       O  
ATOM   3124  ND2 ASN A 417      -4.377  11.593 -21.896  1.00 27.80           N  
ANISOU 3124  ND2 ASN A 417     3646   3625   3290   -111     37   -577       N  
ATOM   3125  N   TYR A 418      -3.221  15.495 -18.201  1.00 18.24           N  
ANISOU 3125  N   TYR A 418     2209   2538   2185   -113     81   -547       N  
ATOM   3126  CA  TYR A 418      -3.441  16.801 -17.583  1.00 19.27           C  
ANISOU 3126  CA  TYR A 418     2294   2693   2336   -131     85   -534       C  
ATOM   3127  C   TYR A 418      -2.718  16.994 -16.264  1.00 17.95           C  
ANISOU 3127  C   TYR A 418     2094   2540   2188   -109     83   -538       C  
ATOM   3128  O   TYR A 418      -2.467  18.143 -15.895  1.00 17.33           O  
ANISOU 3128  O   TYR A 418     1976   2483   2125   -115     91   -535       O  
ATOM   3129  CB  TYR A 418      -4.942  17.052 -17.359  1.00 16.27           C  
ANISOU 3129  CB  TYR A 418     1922   2303   1955   -168     67   -508       C  
ATOM   3130  CG  TYR A 418      -5.717  17.093 -18.656  1.00 17.85           C  
ANISOU 3130  CG  TYR A 418     2148   2494   2139   -197     66   -500       C  
ATOM   3131  CD1 TYR A 418      -6.206  15.923 -19.233  1.00 19.02           C  
ANISOU 3131  CD1 TYR A 418     2347   2612   2267   -202     49   -498       C  
ATOM   3132  CD2 TYR A 418      -5.920  18.293 -19.323  1.00 17.38           C  
ANISOU 3132  CD2 TYR A 418     2066   2455   2084   -219     82   -493       C  
ATOM   3133  CE1 TYR A 418      -6.898  15.953 -20.432  1.00 19.00           C  
ANISOU 3133  CE1 TYR A 418     2372   2599   2248   -229     45   -491       C  
ATOM   3134  CE2 TYR A 418      -6.595  18.336 -20.525  1.00 17.55           C  
ANISOU 3134  CE2 TYR A 418     2110   2468   2089   -245     81   -485       C  
ATOM   3135  CZ  TYR A 418      -7.085  17.159 -21.070  1.00 20.42           C  
ANISOU 3135  CZ  TYR A 418     2525   2802   2432   -251     62   -484       C  
ATOM   3136  OH  TYR A 418      -7.775  17.199 -22.253  1.00 20.34           O  
ANISOU 3136  OH  TYR A 418     2541   2783   2404   -279     58   -476       O  
ATOM   3137  N   LEU A 419      -2.372  15.925 -15.549  1.00 19.25           N  
ANISOU 3137  N   LEU A 419     2273   2690   2352    -84     72   -544       N  
ATOM   3138  CA  LEU A 419      -1.895  16.075 -14.181  1.00 19.35           C  
ANISOU 3138  CA  LEU A 419     2258   2714   2381    -68     65   -543       C  
ATOM   3139  C   LEU A 419      -0.560  16.811 -14.127  1.00 20.76           C  
ANISOU 3139  C   LEU A 419     2396   2918   2574    -49     83   -556       C  
ATOM   3140  O   LEU A 419      -0.402  17.765 -13.359  1.00 16.12           O  
ANISOU 3140  O   LEU A 419     1776   2348   2002    -55     80   -552       O  
ATOM   3141  CB  LEU A 419      -1.792  14.708 -13.518  1.00 20.57           C  
ANISOU 3141  CB  LEU A 419     2438   2846   2530    -45     49   -545       C  
ATOM   3142  CG  LEU A 419      -1.195  14.672 -12.118  1.00 21.59           C  
ANISOU 3142  CG  LEU A 419     2542   2986   2675    -24     41   -546       C  
ATOM   3143  CD1 LEU A 419      -1.961  15.648 -11.204  1.00 20.09           C  
ANISOU 3143  CD1 LEU A 419     2330   2810   2494    -45     32   -530       C  
ATOM   3144  CD2 LEU A 419      -1.250  13.242 -11.590  1.00 23.20           C  
ANISOU 3144  CD2 LEU A 419     2776   3166   2873     -6     24   -545       C  
ATOM   3145  N   GLN A 420       0.415  16.385 -14.933  1.00 19.88           N  
ANISOU 3145  N   GLN A 420     2288   2810   2457    -25    100   -570       N  
ATOM   3146  CA  GLN A 420       1.740  16.989 -14.827  1.00 21.57           C  
ANISOU 3146  CA  GLN A 420     2459   3049   2686     -6    115   -576       C  
ATOM   3147  C   GLN A 420       1.719  18.440 -15.278  1.00 22.38           C  
ANISOU 3147  C   GLN A 420     2529   3175   2800    -31    125   -569       C  
ATOM   3148  O   GLN A 420       2.387  19.288 -14.677  1.00 22.64           O  
ANISOU 3148  O   GLN A 420     2522   3227   2852    -31    123   -567       O  
ATOM   3149  CB  GLN A 420       2.766  16.180 -15.618  1.00 20.23           C  
ANISOU 3149  CB  GLN A 420     2300   2880   2507     30    134   -587       C  
ATOM   3150  CG  GLN A 420       3.058  14.812 -14.993  1.00 22.76           C  
ANISOU 3150  CG  GLN A 420     2645   3180   2821     61    124   -594       C  
ATOM   3151  CD  GLN A 420       4.161  14.039 -15.722  1.00 27.52           C  
ANISOU 3151  CD  GLN A 420     3257   3785   3415    102    146   -605       C  
ATOM   3152  OE1 GLN A 420       5.269  14.542 -15.908  1.00 25.63           O  
ANISOU 3152  OE1 GLN A 420     2978   3573   3187    121    165   -602       O  
ATOM   3153  NE2 GLN A 420       3.861  12.808 -16.118  1.00 26.71           N  
ANISOU 3153  NE2 GLN A 420     3206   3652   3291    119    142   -614       N  
ATOM   3154  N   GLN A 421       0.952  18.753 -16.322  1.00 20.72           N  
ANISOU 3154  N   GLN A 421     2336   2960   2578    -55    132   -566       N  
ATOM   3155  CA AGLN A 421       0.840  20.145 -16.739  0.59 23.76           C  
ANISOU 3155  CA AGLN A 421     2690   3364   2973    -80    140   -558       C  
ATOM   3156  CA BGLN A 421       0.825  20.143 -16.744  0.41 23.75           C  
ANISOU 3156  CA BGLN A 421     2689   3364   2972    -81    140   -557       C  
ATOM   3157  C   GLN A 421       0.234  21.002 -15.632  1.00 23.99           C  
ANISOU 3157  C   GLN A 421     2702   3395   3017   -101    123   -548       C  
ATOM   3158  O   GLN A 421       0.696  22.122 -15.389  1.00 22.65           O  
ANISOU 3158  O   GLN A 421     2497   3243   2866   -109    123   -546       O  
ATOM   3159  CB AGLN A 421       0.019  20.254 -18.022  0.59 25.98           C  
ANISOU 3159  CB AGLN A 421     2995   3640   3237   -103    150   -553       C  
ATOM   3160  CB BGLN A 421      -0.037  20.238 -18.002  0.41 25.97           C  
ANISOU 3160  CB BGLN A 421     2994   3637   3235   -104    149   -553       C  
ATOM   3161  CG AGLN A 421      -0.069  21.679 -18.585  0.59 29.43           C  
ANISOU 3161  CG AGLN A 421     3400   4097   3686   -129    160   -544       C  
ATOM   3162  CG BGLN A 421       0.022  21.602 -18.679  0.41 29.36           C  
ANISOU 3162  CG BGLN A 421     3392   4088   3675   -127    162   -545       C  
ATOM   3163  CD AGLN A 421       1.287  22.278 -18.935  0.59 29.35           C  
ANISOU 3163  CD AGLN A 421     3349   4114   3690   -114    178   -546       C  
ATOM   3164  CD BGLN A 421      -1.224  21.915 -19.485  0.41 28.56           C  
ANISOU 3164  CD BGLN A 421     3312   3979   3561   -160    162   -534       C  
ATOM   3165  OE1AGLN A 421       2.205  21.572 -19.358  0.59 32.00           O  
ANISOU 3165  OE1AGLN A 421     3686   4454   4017    -83    192   -553       O  
ATOM   3166  OE1BGLN A 421      -2.312  21.414 -19.195  0.41 33.02           O  
ANISOU 3166  OE1BGLN A 421     3907   4523   4116   -174    146   -528       O  
ATOM   3167  NE2AGLN A 421       1.417  23.592 -18.754  0.59 31.20           N  
ANISOU 3167  NE2AGLN A 421     3545   4364   3944   -134    176   -536       N  
ATOM   3168  NE2BGLN A 421      -1.073  22.752 -20.498  0.41 28.58           N  
ANISOU 3168  NE2BGLN A 421     3297   3998   3565   -174    178   -530       N  
ATOM   3169  N   LEU A 422      -0.796  20.492 -14.947  1.00 18.88           N  
ANISOU 3169  N   LEU A 422     2080   2730   2362   -108    106   -542       N  
ATOM   3170  CA  LEU A 422      -1.393  21.232 -13.833  1.00 18.45           C  
ANISOU 3170  CA  LEU A 422     2015   2678   2318   -120     91   -533       C  
ATOM   3171  C   LEU A 422      -0.376  21.464 -12.720  1.00 20.23           C  
ANISOU 3171  C   LEU A 422     2214   2914   2559    -99     82   -541       C  
ATOM   3172  O   LEU A 422      -0.277  22.565 -12.165  1.00 18.62           O  
ANISOU 3172  O   LEU A 422     1986   2720   2367   -108     76   -539       O  
ATOM   3173  CB  LEU A 422      -2.608  20.473 -13.292  1.00 20.32           C  
ANISOU 3173  CB  LEU A 422     2283   2896   2543   -126     76   -520       C  
ATOM   3174  CG  LEU A 422      -3.084  20.883 -11.899  1.00 19.58           C  
ANISOU 3174  CG  LEU A 422     2180   2804   2454   -124     61   -511       C  
ATOM   3175  CD1 LEU A 422      -3.588  22.322 -11.902  1.00 16.22           C  
ANISOU 3175  CD1 LEU A 422     1737   2390   2036   -145     65   -502       C  
ATOM   3176  CD2 LEU A 422      -4.161  19.929 -11.394  1.00 16.32           C  
ANISOU 3176  CD2 LEU A 422     1795   2375   2029   -126     48   -494       C  
ATOM   3177  N   GLU A 423       0.377  20.428 -12.366  1.00 20.24           N  
ANISOU 3177  N   GLU A 423     2221   2911   2559    -72     80   -549       N  
ATOM   3178  CA  GLU A 423       1.402  20.603 -11.344  1.00 21.83           C  
ANISOU 3178  CA  GLU A 423     2396   3124   2775    -53     70   -555       C  
ATOM   3179  C   GLU A 423       2.421  21.650 -11.773  1.00 21.37           C  
ANISOU 3179  C   GLU A 423     2299   3086   2734    -57     78   -556       C  
ATOM   3180  O   GLU A 423       2.801  22.516 -10.984  1.00 18.52           O  
ANISOU 3180  O   GLU A 423     1914   2733   2388    -62     64   -555       O  
ATOM   3181  CB  GLU A 423       2.075  19.264 -11.052  1.00 22.17           C  
ANISOU 3181  CB  GLU A 423     2449   3159   2814    -22     68   -561       C  
ATOM   3182  CG  GLU A 423       1.148  18.273 -10.371  1.00 20.08           C  
ANISOU 3182  CG  GLU A 423     2219   2875   2537    -18     54   -557       C  
ATOM   3183  CD  GLU A 423       1.748  16.886 -10.261  1.00 25.45           C  
ANISOU 3183  CD  GLU A 423     2915   3543   3212     12     53   -563       C  
ATOM   3184  OE1 GLU A 423       2.543  16.502 -11.150  1.00 24.67           O  
ANISOU 3184  OE1 GLU A 423     2815   3446   3111     28     70   -571       O  
ATOM   3185  OE2 GLU A 423       1.418  16.176  -9.287  1.00 23.99           O  
ANISOU 3185  OE2 GLU A 423     2743   3347   3024     21     37   -558       O  
ATOM   3186  N   SER A 424       2.851  21.597 -13.033  1.00 22.04           N  
ANISOU 3186  N   SER A 424     2379   3179   2818    -56     99   -557       N  
ATOM   3187  CA  SER A 424       3.818  22.564 -13.545  1.00 24.22           C  
ANISOU 3187  CA  SER A 424     2615   3477   3111    -61    108   -552       C  
ATOM   3188  C   SER A 424       3.254  23.987 -13.526  1.00 23.04           C  
ANISOU 3188  C   SER A 424     2451   3331   2971    -94    101   -546       C  
ATOM   3189  O   SER A 424       3.959  24.939 -13.169  1.00 23.67           O  
ANISOU 3189  O   SER A 424     2498   3424   3071   -100     91   -542       O  
ATOM   3190  CB  SER A 424       4.238  22.143 -14.960  1.00 22.72           C  
ANISOU 3190  CB  SER A 424     2427   3295   2911    -50    136   -552       C  
ATOM   3191  OG  SER A 424       5.037  23.124 -15.589  1.00 37.38           O  
ANISOU 3191  OG  SER A 424     4244   5176   4784    -58    147   -543       O  
ATOM   3192  N   GLU A 425       1.986  24.154 -13.899  1.00 21.49           N  
ANISOU 3192  N   GLU A 425     2280   3124   2763   -114    104   -543       N  
ATOM   3193  CA  GLU A 425       1.392  25.488 -13.892  1.00 21.54           C  
ANISOU 3193  CA  GLU A 425     2275   3132   2777   -142     98   -535       C  
ATOM   3194  C   GLU A 425       1.220  26.020 -12.473  1.00 21.47           C  
ANISOU 3194  C   GLU A 425     2265   3117   2776   -142     74   -537       C  
ATOM   3195  O   GLU A 425       1.373  27.225 -12.237  1.00 20.92           O  
ANISOU 3195  O   GLU A 425     2177   3052   2721   -157     64   -534       O  
ATOM   3196  CB  GLU A 425       0.058  25.475 -14.650  1.00 25.61           C  
ANISOU 3196  CB  GLU A 425     2816   3637   3276   -163    108   -528       C  
ATOM   3197  CG  GLU A 425       0.243  25.238 -16.149  1.00 22.72           C  
ANISOU 3197  CG  GLU A 425     2452   3279   2903   -167    130   -527       C  
ATOM   3198  CD  GLU A 425      -1.061  25.070 -16.927  1.00 30.35           C  
ANISOU 3198  CD  GLU A 425     3447   4233   3851   -189    136   -518       C  
ATOM   3199  OE1 GLU A 425      -2.159  25.190 -16.341  1.00 31.12           O  
ANISOU 3199  OE1 GLU A 425     3561   4320   3945   -201    124   -510       O  
ATOM   3200  OE2 GLU A 425      -0.977  24.826 -18.150  1.00 32.91           O  
ANISOU 3200  OE2 GLU A 425     3778   4561   4164   -192    152   -518       O  
ATOM   3201  N   ILE A 426       0.913  25.150 -11.509  1.00 20.12           N  
ANISOU 3201  N   ILE A 426     2115   2936   2594   -125     63   -541       N  
ATOM   3202  CA  ILE A 426       0.855  25.606 -10.125  1.00 17.45           C  
ANISOU 3202  CA  ILE A 426     1777   2594   2260   -120     41   -543       C  
ATOM   3203  C   ILE A 426       2.237  26.049  -9.664  1.00 20.63           C  
ANISOU 3203  C   ILE A 426     2149   3007   2682   -112     27   -549       C  
ATOM   3204  O   ILE A 426       2.378  27.079  -8.989  1.00 18.60           O  
ANISOU 3204  O   ILE A 426     1884   2749   2435   -121      9   -550       O  
ATOM   3205  CB  ILE A 426       0.262  24.512  -9.218  1.00 20.17           C  
ANISOU 3205  CB  ILE A 426     2149   2927   2589   -102     33   -543       C  
ATOM   3206  CG1 ILE A 426      -1.255  24.435  -9.415  1.00 15.88           C  
ANISOU 3206  CG1 ILE A 426     1631   2373   2029   -115     39   -530       C  
ATOM   3207  CG2 ILE A 426       0.601  24.779  -7.736  1.00 17.89           C  
ANISOU 3207  CG2 ILE A 426     1858   2638   2303    -88     10   -548       C  
ATOM   3208  CD1 ILE A 426      -1.888  23.187  -8.848  1.00 17.39           C  
ANISOU 3208  CD1 ILE A 426     1847   2554   2205   -101     34   -523       C  
ATOM   3209  N   ASP A 427       3.280  25.296 -10.049  1.00 19.22           N  
ANISOU 3209  N   ASP A 427     1955   2837   2509    -96     35   -550       N  
ATOM   3210  CA  ASP A 427       4.659  25.674  -9.734  1.00 22.29           C  
ANISOU 3210  CA  ASP A 427     2310   3240   2919    -90     23   -549       C  
ATOM   3211  C   ASP A 427       5.008  27.054 -10.287  1.00 23.74           C  
ANISOU 3211  C   ASP A 427     2465   3433   3121   -115     21   -542       C  
ATOM   3212  O   ASP A 427       5.707  27.836  -9.629  1.00 22.14           O  
ANISOU 3212  O   ASP A 427     2242   3234   2936   -122     -3   -539       O  
ATOM   3213  CB  ASP A 427       5.630  24.631 -10.294  1.00 23.15           C  
ANISOU 3213  CB  ASP A 427     2405   3360   3030    -67     40   -547       C  
ATOM   3214  CG  ASP A 427       5.674  23.345  -9.476  1.00 24.10           C  
ANISOU 3214  CG  ASP A 427     2546   3472   3140    -39     34   -554       C  
ATOM   3215  OD1 ASP A 427       5.122  23.298  -8.360  1.00 24.03           O  
ANISOU 3215  OD1 ASP A 427     2555   3451   3124    -38     15   -558       O  
ATOM   3216  OD2 ASP A 427       6.275  22.363  -9.962  1.00 30.86           O  
ANISOU 3216  OD2 ASP A 427     3400   4332   3992    -16     50   -554       O  
ATOM   3217  N   GLU A 428       4.549  27.366 -11.502  1.00 20.88           N  
ANISOU 3217  N   GLU A 428     2102   3074   2756   -131     42   -536       N  
ATOM   3218  CA  GLU A 428       4.779  28.699 -12.053  1.00 27.23           C  
ANISOU 3218  CA  GLU A 428     2881   3887   3579   -156     40   -527       C  
ATOM   3219  C   GLU A 428       4.096  29.769 -11.216  1.00 25.63           C  
ANISOU 3219  C   GLU A 428     2691   3670   3379   -174     16   -531       C  
ATOM   3220  O   GLU A 428       4.686  30.822 -10.938  1.00 24.15           O  
ANISOU 3220  O   GLU A 428     2482   3483   3211   -188     -5   -526       O  
ATOM   3221  CB  GLU A 428       4.282  28.775 -13.494  1.00 29.80           C  
ANISOU 3221  CB  GLU A 428     3207   4219   3897   -169     68   -520       C  
ATOM   3222  CG  GLU A 428       5.165  28.070 -14.491  1.00 33.09           C  
ANISOU 3222  CG  GLU A 428     3605   4654   4314   -152     92   -515       C  
ATOM   3223  CD  GLU A 428       4.563  28.064 -15.883  1.00 44.84           C  
ANISOU 3223  CD  GLU A 428     5103   6146   5788   -163    119   -510       C  
ATOM   3224  OE1 GLU A 428       3.703  28.932 -16.176  1.00 45.21           O  
ANISOU 3224  OE1 GLU A 428     5154   6187   5835   -190    118   -506       O  
ATOM   3225  OE2 GLU A 428       4.948  27.180 -16.678  1.00 50.54           O  
ANISOU 3225  OE2 GLU A 428     5828   6877   6498   -143    142   -511       O  
ATOM   3226  N   LEU A 429       2.844  29.528 -10.822  1.00 19.40           N  
ANISOU 3226  N   LEU A 429     1937   2866   2570   -172     18   -536       N  
ATOM   3227  CA  LEU A 429       2.139  30.502  -9.994  1.00 21.49           C  
ANISOU 3227  CA  LEU A 429     2218   3116   2832   -181     -1   -539       C  
ATOM   3228  C   LEU A 429       2.852  30.718  -8.667  1.00 20.73           C  
ANISOU 3228  C   LEU A 429     2120   3014   2742   -170    -33   -547       C  
ATOM   3229  O   LEU A 429       2.941  31.848  -8.173  1.00 19.48           O  
ANISOU 3229  O   LEU A 429     1962   2848   2593   -182    -55   -549       O  
ATOM   3230  CB  LEU A 429       0.709  30.037  -9.743  1.00 21.12           C  
ANISOU 3230  CB  LEU A 429     2206   3058   2761   -175      9   -538       C  
ATOM   3231  CG  LEU A 429      -0.264  30.143 -10.910  1.00 26.48           C  
ANISOU 3231  CG  LEU A 429     2891   3737   3433   -193     33   -528       C  
ATOM   3232  CD1 LEU A 429      -1.599  29.598 -10.459  1.00 24.06           C  
ANISOU 3232  CD1 LEU A 429     2616   3420   3104   -186     38   -522       C  
ATOM   3233  CD2 LEU A 429      -0.393  31.613 -11.328  1.00 29.38           C  
ANISOU 3233  CD2 LEU A 429     3245   4104   3815   -217     30   -522       C  
ATOM   3234  N   TYR A 430       3.333  29.635  -8.063  1.00 18.83           N  
ANISOU 3234  N   TYR A 430     1882   2777   2495   -147    -36   -552       N  
ATOM   3235  CA  TYR A 430       4.098  29.738  -6.830  1.00 21.80           C  
ANISOU 3235  CA  TYR A 430     2255   3150   2877   -137    -67   -558       C  
ATOM   3236  C   TYR A 430       5.244  30.732  -6.965  1.00 22.28           C  
ANISOU 3236  C   TYR A 430     2283   3217   2965   -155    -89   -553       C  
ATOM   3237  O   TYR A 430       5.456  31.569  -6.084  1.00 19.91           O  
ANISOU 3237  O   TYR A 430     1989   2906   2670   -161   -121   -558       O  
ATOM   3238  CB  TYR A 430       4.623  28.357  -6.456  1.00 18.03           C  
ANISOU 3238  CB  TYR A 430     1777   2679   2393   -111    -64   -560       C  
ATOM   3239  CG  TYR A 430       5.538  28.354  -5.280  1.00 21.54           C  
ANISOU 3239  CG  TYR A 430     2215   3125   2846   -101    -95   -564       C  
ATOM   3240  CD1 TYR A 430       5.216  29.061  -4.120  1.00 19.52           C  
ANISOU 3240  CD1 TYR A 430     1980   2854   2581   -102   -124   -572       C  
ATOM   3241  CD2 TYR A 430       6.732  27.631  -5.311  1.00 23.44           C  
ANISOU 3241  CD2 TYR A 430     2428   3378   3100    -89    -96   -558       C  
ATOM   3242  CE1 TYR A 430       6.074  29.054  -3.025  1.00 20.51           C  
ANISOU 3242  CE1 TYR A 430     2102   2980   2712    -93   -156   -576       C  
ATOM   3243  CE2 TYR A 430       7.593  27.621  -4.219  1.00 23.18           C  
ANISOU 3243  CE2 TYR A 430     2386   3346   3074    -81   -127   -559       C  
ATOM   3244  CZ  TYR A 430       7.257  28.332  -3.083  1.00 21.66           C  
ANISOU 3244  CZ  TYR A 430     2216   3139   2873    -85   -159   -568       C  
ATOM   3245  OH  TYR A 430       8.096  28.311  -1.995  1.00 20.54           O  
ANISOU 3245  OH  TYR A 430     2070   2998   2737    -78   -192   -569       O  
ATOM   3246  N   ILE A 431       5.979  30.664  -8.075  1.00 19.54           N  
ANISOU 3246  N   ILE A 431     1902   2886   2635   -163    -72   -540       N  
ATOM   3247  CA  ILE A 431       7.102  31.572  -8.295  1.00 21.93           C  
ANISOU 3247  CA  ILE A 431     2167   3198   2967   -181    -91   -528       C  
ATOM   3248  C   ILE A 431       6.634  33.024  -8.314  1.00 23.83           C  
ANISOU 3248  C   ILE A 431     2414   3424   3215   -208   -109   -528       C  
ATOM   3249  O   ILE A 431       7.307  33.912  -7.775  1.00 19.53           O  
ANISOU 3249  O   ILE A 431     1858   2873   2689   -223   -145   -524       O  
ATOM   3250  CB  ILE A 431       7.837  31.191  -9.592  1.00 26.58           C  
ANISOU 3250  CB  ILE A 431     2718   3811   3569   -181    -63   -511       C  
ATOM   3251  CG1 ILE A 431       8.527  29.842  -9.403  1.00 25.73           C  
ANISOU 3251  CG1 ILE A 431     2604   3716   3457   -151    -52   -510       C  
ATOM   3252  CG2 ILE A 431       8.822  32.301 -10.010  1.00 29.31           C  
ANISOU 3252  CG2 ILE A 431     3022   4169   3947   -206    -80   -491       C  
ATOM   3253  CD1 ILE A 431       9.247  29.339 -10.635  1.00 35.64           C  
ANISOU 3253  CD1 ILE A 431     3827   4995   4719   -141    -20   -494       C  
ATOM   3254  N   GLN A 432       5.478  33.294  -8.930  1.00 22.11           N  
ANISOU 3254  N   GLN A 432     2217   3200   2985   -216    -87   -531       N  
ATOM   3255  CA  GLN A 432       4.930  34.647  -8.869  1.00 21.45           C  
ANISOU 3255  CA  GLN A 432     2144   3100   2906   -238   -103   -531       C  
ATOM   3256  C   GLN A 432       4.705  35.068  -7.425  1.00 20.42           C  
ANISOU 3256  C   GLN A 432     2045   2947   2765   -229   -137   -546       C  
ATOM   3257  O   GLN A 432       5.017  36.202  -7.043  1.00 19.58           O  
ANISOU 3257  O   GLN A 432     1941   2827   2673   -246   -169   -547       O  
ATOM   3258  CB  GLN A 432       3.621  34.737  -9.656  1.00 19.57           C  
ANISOU 3258  CB  GLN A 432     1924   2858   2653   -243    -72   -530       C  
ATOM   3259  CG  GLN A 432       3.735  34.446 -11.160  1.00 19.75           C  
ANISOU 3259  CG  GLN A 432     1920   2901   2682   -254    -39   -516       C  
ATOM   3260  CD  GLN A 432       2.371  34.453 -11.846  1.00 25.10           C  
ANISOU 3260  CD  GLN A 432     2620   3574   3343   -260    -12   -515       C  
ATOM   3261  OE1 GLN A 432       1.397  34.979 -11.301  1.00 21.50           O  
ANISOU 3261  OE1 GLN A 432     2192   3102   2876   -261    -19   -519       O  
ATOM   3262  NE2 GLN A 432       2.292  33.854 -13.033  1.00 22.46           N  
ANISOU 3262  NE2 GLN A 432     2275   3255   3004   -262     18   -506       N  
ATOM   3263  N   TYR A 433       4.190  34.153  -6.600  1.00 17.85           N  
ANISOU 3263  N   TYR A 433     1748   2618   2415   -203   -132   -558       N  
ATOM   3264  CA  TYR A 433       3.917  34.479  -5.206  1.00 19.98           C  
ANISOU 3264  CA  TYR A 433     2053   2869   2669   -190   -162   -572       C  
ATOM   3265  C   TYR A 433       5.192  34.673  -4.405  1.00 18.00           C  
ANISOU 3265  C   TYR A 433     1790   2617   2434   -192   -202   -574       C  
ATOM   3266  O   TYR A 433       5.204  35.474  -3.469  1.00 19.33           O  
ANISOU 3266  O   TYR A 433     1981   2765   2597   -193   -237   -584       O  
ATOM   3267  CB  TYR A 433       3.041  33.395  -4.577  1.00 17.18           C  
ANISOU 3267  CB  TYR A 433     1728   2516   2285   -161   -144   -578       C  
ATOM   3268  CG  TYR A 433       1.601  33.647  -4.915  1.00 18.97           C  
ANISOU 3268  CG  TYR A 433     1978   2735   2493   -160   -120   -575       C  
ATOM   3269  CD1 TYR A 433       0.961  34.773  -4.415  1.00 21.09           C  
ANISOU 3269  CD1 TYR A 433     2273   2986   2753   -161   -133   -580       C  
ATOM   3270  CD2 TYR A 433       0.896  32.808  -5.759  1.00 18.84           C  
ANISOU 3270  CD2 TYR A 433     1959   2729   2469   -159    -85   -565       C  
ATOM   3271  CE1 TYR A 433      -0.345  35.049  -4.727  1.00 20.97           C  
ANISOU 3271  CE1 TYR A 433     2277   2967   2724   -159   -110   -573       C  
ATOM   3272  CE2 TYR A 433      -0.437  33.077  -6.082  1.00 19.08           C  
ANISOU 3272  CE2 TYR A 433     2009   2756   2486   -161    -65   -558       C  
ATOM   3273  CZ  TYR A 433      -1.043  34.204  -5.552  1.00 22.31           C  
ANISOU 3273  CZ  TYR A 433     2439   3149   2887   -160    -76   -560       C  
ATOM   3274  OH  TYR A 433      -2.348  34.517  -5.844  1.00 20.88           O  
ANISOU 3274  OH  TYR A 433     2275   2965   2693   -160    -55   -549       O  
ATOM   3275  N   ILE A 434       6.264  33.952  -4.748  1.00 17.39           N  
ANISOU 3275  N   ILE A 434     1676   2559   2374   -192   -199   -563       N  
ATOM   3276  CA  ILE A 434       7.557  34.212  -4.119  1.00 19.27           C  
ANISOU 3276  CA  ILE A 434     1892   2797   2631   -199   -239   -558       C  
ATOM   3277  C   ILE A 434       7.963  35.661  -4.350  1.00 21.17           C  
ANISOU 3277  C   ILE A 434     2121   3026   2895   -231   -269   -551       C  
ATOM   3278  O   ILE A 434       8.445  36.346  -3.440  1.00 22.10           O  
ANISOU 3278  O   ILE A 434     2251   3127   3019   -240   -315   -556       O  
ATOM   3279  CB  ILE A 434       8.619  33.231  -4.655  1.00 18.34           C  
ANISOU 3279  CB  ILE A 434     1732   2707   2531   -192   -224   -542       C  
ATOM   3280  CG1 ILE A 434       8.306  31.805  -4.204  1.00 22.19           C  
ANISOU 3280  CG1 ILE A 434     2235   3200   2996   -160   -203   -551       C  
ATOM   3281  CG2 ILE A 434      10.022  33.642  -4.202  1.00 20.87           C  
ANISOU 3281  CG2 ILE A 434     2019   3031   2878   -206   -265   -528       C  
ATOM   3282  CD1 ILE A 434       9.293  30.763  -4.712  1.00 19.31           C  
ANISOU 3282  CD1 ILE A 434     1833   2859   2644   -147   -185   -536       C  
ATOM   3283  N   LYS A 435       7.757  36.153  -5.570  1.00 21.09           N  
ANISOU 3283  N   LYS A 435     2090   3023   2899   -250   -246   -539       N  
ATOM   3284  CA  LYS A 435       8.161  37.515  -5.886  1.00 22.07           C  
ANISOU 3284  CA  LYS A 435     2199   3136   3049   -282   -275   -528       C  
ATOM   3285  C   LYS A 435       7.264  38.528  -5.192  1.00 20.99           C  
ANISOU 3285  C   LYS A 435     2112   2967   2897   -286   -298   -547       C  
ATOM   3286  O   LYS A 435       7.762  39.510  -4.635  1.00 20.88           O  
ANISOU 3286  O   LYS A 435     2106   2933   2896   -303   -344   -548       O  
ATOM   3287  CB  LYS A 435       8.180  37.713  -7.400  1.00 20.16           C  
ANISOU 3287  CB  LYS A 435     1920   2913   2825   -300   -242   -509       C  
ATOM   3288  CG  LYS A 435       9.367  36.982  -8.041  1.00 26.95           C  
ANISOU 3288  CG  LYS A 435     2728   3805   3705   -298   -229   -485       C  
ATOM   3289  CD  LYS A 435       9.234  36.814  -9.550  1.00 31.70           C  
ANISOU 3289  CD  LYS A 435     3301   4431   4314   -303   -184   -469       C  
ATOM   3290  CE  LYS A 435      10.264  35.794 -10.050  1.00 37.90           C  
ANISOU 3290  CE  LYS A 435     4045   5248   5108   -287   -163   -451       C  
ATOM   3291  NZ  LYS A 435      10.157  35.484 -11.507  1.00 37.49           N  
ANISOU 3291  NZ  LYS A 435     3969   5220   5055   -285   -117   -437       N  
ATOM   3292  N   HIS A 436       5.949  38.294  -5.180  1.00 18.63           N  
ANISOU 3292  N   HIS A 436     1848   2662   2569   -267   -267   -561       N  
ATOM   3293  CA  HIS A 436       5.063  39.163  -4.406  1.00 19.83           C  
ANISOU 3293  CA  HIS A 436     2049   2783   2701   -261   -285   -578       C  
ATOM   3294  C   HIS A 436       5.460  39.179  -2.939  1.00 21.65           C  
ANISOU 3294  C   HIS A 436     2311   2997   2918   -246   -327   -594       C  
ATOM   3295  O   HIS A 436       5.524  40.244  -2.316  1.00 24.72           O  
ANISOU 3295  O   HIS A 436     2728   3358   3307   -254   -367   -603       O  
ATOM   3296  CB  HIS A 436       3.610  38.711  -4.542  1.00 22.31           C  
ANISOU 3296  CB  HIS A 436     2392   3099   2986   -239   -243   -584       C  
ATOM   3297  CG  HIS A 436       3.042  38.904  -5.911  1.00 24.16           C  
ANISOU 3297  CG  HIS A 436     2606   3345   3230   -255   -207   -569       C  
ATOM   3298  ND1 HIS A 436       3.091  40.113  -6.574  1.00 23.88           N  
ANISOU 3298  ND1 HIS A 436     2560   3299   3216   -283   -217   -561       N  
ATOM   3299  CD2 HIS A 436       2.410  38.044  -6.742  1.00 19.57           C  
ANISOU 3299  CD2 HIS A 436     2014   2783   2640   -249   -164   -561       C  
ATOM   3300  CE1 HIS A 436       2.510  39.988  -7.754  1.00 26.78           C  
ANISOU 3300  CE1 HIS A 436     2909   3680   3586   -292   -179   -548       C  
ATOM   3301  NE2 HIS A 436       2.084  38.744  -7.880  1.00 24.78           N  
ANISOU 3301  NE2 HIS A 436     2657   3444   3314   -273   -147   -549       N  
ATOM   3302  N   ASN A 437       5.739  38.005  -2.371  1.00 21.37           N  
ANISOU 3302  N   ASN A 437     2274   2977   2870   -224   -321   -597       N  
ATOM   3303  CA  ASN A 437       6.101  37.927  -0.958  1.00 22.07           C  
ANISOU 3303  CA  ASN A 437     2391   3051   2942   -208   -360   -611       C  
ATOM   3304  C   ASN A 437       7.407  38.660  -0.680  1.00 23.01           C  
ANISOU 3304  C   ASN A 437     2492   3160   3089   -235   -414   -605       C  
ATOM   3305  O   ASN A 437       7.513  39.416   0.294  1.00 24.00           O  
ANISOU 3305  O   ASN A 437     2655   3258   3205   -236   -459   -619       O  
ATOM   3306  CB  ASN A 437       6.193  36.457  -0.540  1.00 19.78           C  
ANISOU 3306  CB  ASN A 437     2096   2783   2638   -181   -341   -612       C  
ATOM   3307  CG  ASN A 437       6.453  36.277   0.933  1.00 20.15           C  
ANISOU 3307  CG  ASN A 437     2175   2818   2664   -162   -376   -626       C  
ATOM   3308  OD1 ASN A 437       5.677  36.734   1.778  1.00 19.74           O  
ANISOU 3308  OD1 ASN A 437     2171   2746   2582   -144   -387   -643       O  
ATOM   3309  ND2 ASN A 437       7.538  35.576   1.257  1.00 18.78           N  
ANISOU 3309  ND2 ASN A 437     1974   2658   2503   -162   -393   -619       N  
ATOM   3310  N   ASP A 438       8.421  38.452  -1.529  1.00 23.79           N  
ANISOU 3310  N   ASP A 438     2536   3281   3223   -257   -411   -582       N  
ATOM   3311  CA AASP A 438       9.708  39.100  -1.294  0.58 24.30           C  
ANISOU 3311  CA AASP A 438     2575   3339   3318   -286   -464   -568       C  
ATOM   3312  CA BASP A 438       9.713  39.100  -1.307  0.42 24.39           C  
ANISOU 3312  CA BASP A 438     2587   3351   3330   -286   -463   -567       C  
ATOM   3313  C   ASP A 438       9.596  40.617  -1.351  1.00 26.09           C  
ANISOU 3313  C   ASP A 438     2822   3535   3557   -314   -500   -570       C  
ATOM   3314  O   ASP A 438      10.371  41.319  -0.692  1.00 23.92           O  
ANISOU 3314  O   ASP A 438     2554   3240   3295   -333   -558   -568       O  
ATOM   3315  CB AASP A 438      10.737  38.607  -2.303  0.58 23.52           C  
ANISOU 3315  CB AASP A 438     2409   3274   3254   -301   -447   -536       C  
ATOM   3316  CB BASP A 438      10.734  38.628  -2.342  0.42 23.55           C  
ANISOU 3316  CB BASP A 438     2412   3277   3258   -302   -446   -536       C  
ATOM   3317  CG AASP A 438      11.252  37.219  -1.975  0.58 23.19           C  
ANISOU 3317  CG AASP A 438     2349   3257   3207   -276   -431   -532       C  
ATOM   3318  CG BASP A 438      12.167  39.005  -1.971  0.42 24.21           C  
ANISOU 3318  CG BASP A 438     2463   3362   3374   -327   -499   -514       C  
ATOM   3319  OD1AASP A 438      11.184  36.811  -0.795  0.58 24.63           O  
ANISOU 3319  OD1AASP A 438     2563   3429   3366   -257   -451   -549       O  
ATOM   3320  OD1BASP A 438      12.427  39.338  -0.796  0.42 28.66           O  
ANISOU 3320  OD1BASP A 438     3058   3902   3928   -329   -549   -526       O  
ATOM   3321  OD2AASP A 438      11.735  36.540  -2.897  0.58 20.76           O  
ANISOU 3321  OD2AASP A 438     1994   2978   2915   -274   -398   -512       O  
ATOM   3322  OD2BASP A 438      13.043  38.967  -2.860  0.42 26.07           O  
ANISOU 3322  OD2BASP A 438     2640   3622   3642   -345   -492   -483       O  
ATOM   3323  N   SER A 439       8.648  41.142  -2.128  1.00 21.48           N  
ANISOU 3323  N   SER A 439     2247   2945   2969   -317   -470   -573       N  
ATOM   3324  CA  SER A 439       8.479  42.586  -2.191  1.00 25.24           C  
ANISOU 3324  CA  SER A 439     2745   3389   3455   -341   -503   -575       C  
ATOM   3325  C   SER A 439       8.045  43.166  -0.850  1.00 26.53           C  
ANISOU 3325  C   SER A 439     2977   3515   3589   -325   -542   -604       C  
ATOM   3326  O   SER A 439       8.152  44.380  -0.652  1.00 29.33           O  
ANISOU 3326  O   SER A 439     3356   3836   3952   -345   -585   -608       O  
ATOM   3327  CB  SER A 439       7.468  42.959  -3.281  1.00 25.55           C  
ANISOU 3327  CB  SER A 439     2782   3432   3495   -345   -458   -572       C  
ATOM   3328  OG  SER A 439       6.132  42.855  -2.812  1.00 24.86           O  
ANISOU 3328  OG  SER A 439     2746   3331   3368   -313   -433   -595       O  
ATOM   3329  N   LYS A 440       7.581  42.335   0.080  1.00 22.43           N  
ANISOU 3329  N   LYS A 440     2491   2999   3033   -288   -531   -623       N  
ATOM   3330  CA  LYS A 440       7.134  42.818   1.381  1.00 24.91           C  
ANISOU 3330  CA  LYS A 440     2873   3279   3312   -266   -564   -650       C  
ATOM   3331  C   LYS A 440       8.235  42.821   2.429  1.00 30.60           C  
ANISOU 3331  C   LYS A 440     3602   3988   4035   -274   -625   -654       C  
ATOM   3332  O   LYS A 440       7.964  43.140   3.591  1.00 37.58           O  
ANISOU 3332  O   LYS A 440     4545   4845   4887   -253   -656   -677       O  
ATOM   3333  CB  LYS A 440       5.970  41.972   1.908  1.00 24.68           C  
ANISOU 3333  CB  LYS A 440     2878   3260   3239   -220   -521   -666       C  
ATOM   3334  CG  LYS A 440       4.719  41.946   1.035  1.00 28.50           C  
ANISOU 3334  CG  LYS A 440     3361   3753   3714   -208   -463   -662       C  
ATOM   3335  CD  LYS A 440       3.741  40.909   1.584  1.00 25.16           C  
ANISOU 3335  CD  LYS A 440     2962   3346   3252   -166   -424   -669       C  
ATOM   3336  CE  LYS A 440       2.547  40.679   0.662  1.00 26.18           C  
ANISOU 3336  CE  LYS A 440     3082   3490   3376   -157   -366   -659       C  
ATOM   3337  NZ  LYS A 440       2.712  39.480  -0.252  1.00 30.18           N  
ANISOU 3337  NZ  LYS A 440     3538   4031   3897   -164   -327   -641       N  
ATOM   3338  N   ASN A 441       9.455  42.446   2.073  1.00 28.02           N  
ANISOU 3338  N   ASN A 441     3219   3682   3744   -300   -641   -630       N  
ATOM   3339  CA  ASN A 441      10.562  42.444   3.026  1.00 33.63           C  
ANISOU 3339  CA  ASN A 441     3932   4383   4462   -312   -701   -627       C  
ATOM   3340  C   ASN A 441      11.701  43.181   2.336  1.00 39.04           C  
ANISOU 3340  C   ASN A 441     4569   5068   5198   -361   -740   -597       C  
ATOM   3341  O   ASN A 441      12.481  42.599   1.578  1.00 41.66           O  
ANISOU 3341  O   ASN A 441     4834   5433   5561   -376   -722   -566       O  
ATOM   3342  CB  ASN A 441      10.943  41.037   3.454  1.00 31.60           C  
ANISOU 3342  CB  ASN A 441     3653   4159   4196   -289   -682   -623       C  
ATOM   3343  CG  ASN A 441      12.155  41.014   4.379  1.00 35.76           C  
ANISOU 3343  CG  ASN A 441     4176   4679   4733   -304   -745   -615       C  
ATOM   3344  OD1 ASN A 441      12.048  41.258   5.597  1.00 30.00           O  
ANISOU 3344  OD1 ASN A 441     3502   3923   3973   -290   -785   -638       O  
ATOM   3345  ND2 ASN A 441      13.320  40.718   3.803  1.00 33.01           N  
ANISOU 3345  ND2 ASN A 441     3761   4356   4426   -330   -753   -581       N  
ATOM   3346  N   ILE A 442      11.761  44.482   2.574  1.00 48.55           N  
ANISOU 3346  N   ILE A 442     5806   6231   6408   -385   -792   -603       N  
ATOM   3347  CA  ILE A 442      12.784  45.344   2.008  1.00 51.69           C  
ANISOU 3347  CA  ILE A 442     6164   6622   6854   -436   -837   -572       C  
ATOM   3348  C   ILE A 442      13.601  45.912   3.153  1.00 48.99           C  
ANISOU 3348  C   ILE A 442     5855   6246   6513   -455   -921   -576       C  
ATOM   3349  O   ILE A 442      13.054  46.274   4.200  1.00 52.46           O  
ANISOU 3349  O   ILE A 442     6369   6650   6913   -434   -949   -611       O  
ATOM   3350  CB  ILE A 442      12.173  46.476   1.160  1.00 50.59           C  
ANISOU 3350  CB  ILE A 442     6032   6461   6727   -455   -830   -572       C  
ATOM   3351  CG1 ILE A 442      11.308  45.892   0.041  1.00 49.47           C  
ANISOU 3351  CG1 ILE A 442     5862   6353   6582   -436   -748   -568       C  
ATOM   3352  CG2 ILE A 442      13.268  47.348   0.583  1.00 61.45           C  
ANISOU 3352  CG2 ILE A 442     7363   7830   8155   -509   -880   -535       C  
ATOM   3353  CD1 ILE A 442      12.059  44.951  -0.892  1.00 46.29           C  
ANISOU 3353  CD1 ILE A 442     5379   6000   6209   -444   -712   -533       C  
ATOM   3354  N   PHE A 443      14.911  45.974   2.961  1.00 48.72           N  
ANISOU 3354  N   PHE A 443     5765   6224   6521   -494   -962   -539       N  
ATOM   3355  CA  PHE A 443      15.776  46.661   3.905  1.00 47.80           C  
ANISOU 3355  CA  PHE A 443     5674   6073   6413   -523  -1050   -536       C  
ATOM   3356  C   PHE A 443      16.878  47.363   3.130  1.00 54.16           C  
ANISOU 3356  C   PHE A 443     6417   6882   7278   -579  -1091   -487       C  
ATOM   3357  O   PHE A 443      17.673  46.709   2.447  1.00 56.26           O  
ANISOU 3357  O   PHE A 443     6604   7193   7578   -591  -1068   -447       O  
ATOM   3358  CB  PHE A 443      16.370  45.702   4.938  1.00 37.82           C  
ANISOU 3358  CB  PHE A 443     4413   4824   5134   -506  -1069   -538       C  
ATOM   3359  CG  PHE A 443      17.245  46.395   5.934  1.00 43.67           C  
ANISOU 3359  CG  PHE A 443     5183   5529   5881   -538  -1164   -534       C  
ATOM   3360  CD1 PHE A 443      16.680  47.113   6.986  1.00 39.21           C  
ANISOU 3360  CD1 PHE A 443     4711   4911   5275   -526  -1210   -576       C  
ATOM   3361  CD2 PHE A 443      18.628  46.374   5.796  1.00 42.98           C  
ANISOU 3361  CD2 PHE A 443     5032   5457   5841   -580  -1210   -486       C  
ATOM   3362  CE1 PHE A 443      17.483  47.780   7.905  1.00 41.38           C  
ANISOU 3362  CE1 PHE A 443     5020   5148   5554   -557  -1303   -573       C  
ATOM   3363  CE2 PHE A 443      19.438  47.035   6.705  1.00 44.68           C  
ANISOU 3363  CE2 PHE A 443     5277   5639   6061   -612  -1296   -478       C  
ATOM   3364  CZ  PHE A 443      18.864  47.744   7.761  1.00 43.29           C  
ANISOU 3364  CZ  PHE A 443     5199   5410   5838   -597  -1332   -519       C  
ATOM   3365  N   HIS A 444      16.917  48.690   3.234  1.00 57.90           N  
ANISOU 3365  N   HIS A 444     6926   7309   7764   -613  -1151   -489       N  
ATOM   3366  CA  HIS A 444      17.959  49.512   2.625  1.00 61.35           C  
ANISOU 3366  CA  HIS A 444     7314   7745   8253   -667  -1192   -439       C  
ATOM   3367  C   HIS A 444      18.883  49.985   3.743  1.00 63.19           C  
ANISOU 3367  C   HIS A 444     7582   7948   8478   -685  -1261   -426       C  
ATOM   3368  O   HIS A 444      18.494  50.821   4.568  1.00 62.96           O  
ANISOU 3368  O   HIS A 444     7636   7867   8420   -681  -1300   -456       O  
ATOM   3369  CB  HIS A 444      17.351  50.683   1.853  1.00 66.97           C  
ANISOU 3369  CB  HIS A 444     8044   8430   8973   -682  -1183   -439       C  
ATOM   3370  CG  HIS A 444      16.415  50.263   0.759  1.00 71.98           C  
ANISOU 3370  CG  HIS A 444     8647   9092   9610   -663  -1111   -449       C  
ATOM   3371  ND1 HIS A 444      16.780  49.378  -0.235  1.00 72.32           N  
ANISOU 3371  ND1 HIS A 444     8608   9193   9676   -659  -1051   -415       N  
ATOM   3372  CD2 HIS A 444      15.129  50.602   0.505  1.00 71.40           C  
ANISOU 3372  CD2 HIS A 444     8621   9001   9507   -636  -1069   -483       C  
ATOM   3373  CE1 HIS A 444      15.759  49.192  -1.053  1.00 69.19           C  
ANISOU 3373  CE1 HIS A 444     8212   8813   9265   -635   -979   -429       C  
ATOM   3374  NE2 HIS A 444      14.746  49.925  -0.628  1.00 66.84           N  
ANISOU 3374  NE2 HIS A 444     7989   8470   8937   -621   -989   -468       N  
ATOM   3375  N   ALA A 445      20.105  49.440   3.768  1.00 64.21           N  
ANISOU 3375  N   ALA A 445     7649   8112   8636   -703  -1273   -381       N  
ATOM   3376  CA  ALA A 445      21.013  49.682   4.886  1.00 65.76           C  
ANISOU 3376  CA  ALA A 445     7873   8286   8826   -718  -1336   -369       C  
ATOM   3377  C   ALA A 445      21.382  51.156   5.007  1.00 69.31           C  
ANISOU 3377  C   ALA A 445     8361   8688   9287   -753  -1388   -352       C  
ATOM   3378  O   ALA A 445      21.489  51.685   6.120  1.00 72.76           O  
ANISOU 3378  O   ALA A 445     8867   9080   9697   -754  -1443   -371       O  
ATOM   3379  CB  ALA A 445      22.271  48.824   4.734  1.00 59.61           C  
ANISOU 3379  CB  ALA A 445     7011   7557   8080   -731  -1334   -317       C  
ATOM   3380  N   ALA A 446      21.590  51.836   3.876  1.00 71.30           N  
ANISOU 3380  N   ALA A 446     8567   8948   9575   -779  -1372   -316       N  
ATOM   3381  CA  ALA A 446      21.991  53.240   3.933  1.00 70.83           C  
ANISOU 3381  CA  ALA A 446     8538   8843   9531   -813  -1422   -296       C  
ATOM   3382  C   ALA A 446      20.858  54.116   4.453  1.00 74.15           C  
ANISOU 3382  C   ALA A 446     9057   9203   9913   -796  -1440   -351       C  
ATOM   3383  O   ALA A 446      21.099  55.097   5.167  1.00 72.43           O  
ANISOU 3383  O   ALA A 446     8900   8933   9687   -811  -1499   -354       O  
ATOM   3384  CB  ALA A 446      22.450  53.715   2.556  1.00 70.53           C  
ANISOU 3384  CB  ALA A 446     8426   8832   9541   -842  -1396   -244       C  
ATOM   3385  N   ARG A 447      19.614  53.773   4.104  1.00 71.74           N  
ANISOU 3385  N   ARG A 447     8771   8903   9583   -764  -1390   -393       N  
ATOM   3386  CA  ARG A 447      18.462  54.519   4.601  1.00 75.06           C  
ANISOU 3386  CA  ARG A 447     9286   9270   9964   -740  -1400   -446       C  
ATOM   3387  C   ARG A 447      18.263  54.301   6.098  1.00 74.65           C  
ANISOU 3387  C   ARG A 447     9315   9186   9861   -711  -1436   -488       C  
ATOM   3388  O   ARG A 447      17.923  55.241   6.829  1.00 75.17           O  
ANISOU 3388  O   ARG A 447     9466   9196   9901   -704  -1476   -514       O  
ATOM   3389  CB  ARG A 447      17.213  54.114   3.815  1.00 74.49           C  
ANISOU 3389  CB  ARG A 447     9206   9217   9880   -712  -1334   -475       C  
ATOM   3390  CG  ARG A 447      15.893  54.516   4.449  1.00 75.46           C  
ANISOU 3390  CG  ARG A 447     9425   9293   9952   -672  -1332   -536       C  
ATOM   3391  CD  ARG A 447      15.474  55.926   4.064  1.00 79.53           C  
ANISOU 3391  CD  ARG A 447     9980   9763  10475   -687  -1348   -537       C  
ATOM   3392  NE  ARG A 447      14.032  55.994   3.850  1.00 81.46           N  
ANISOU 3392  NE  ARG A 447    10268   9994  10690   -650  -1307   -581       N  
ATOM   3393  CZ  ARG A 447      13.360  57.102   3.567  1.00 79.34           C  
ANISOU 3393  CZ  ARG A 447    10043   9684  10418   -650  -1312   -593       C  
ATOM   3394  NH1 ARG A 447      13.965  58.276   3.481  1.00 79.39           N  
ANISOU 3394  NH1 ARG A 447    10060   9656  10449   -684  -1358   -566       N  
ATOM   3395  NH2 ARG A 447      12.047  57.029   3.365  1.00 75.10           N  
ANISOU 3395  NH2 ARG A 447     9539   9141   9854   -613  -1270   -631       N  
ATOM   3396  N   ALA A 448      18.484  53.070   6.572  1.00 71.56           N  
ANISOU 3396  N   ALA A 448     8902   8830   9457   -692  -1423   -494       N  
ATOM   3397  CA  ALA A 448      18.299  52.764   7.988  1.00 69.15           C  
ANISOU 3397  CA  ALA A 448     8670   8501   9102   -661  -1452   -532       C  
ATOM   3398  C   ALA A 448      19.354  53.448   8.852  1.00 73.10           C  
ANISOU 3398  C   ALA A 448     9200   8968   9608   -690  -1525   -510       C  
ATOM   3399  O   ALA A 448      19.030  54.002   9.911  1.00 70.15           O  
ANISOU 3399  O   ALA A 448     8915   8545   9192   -672  -1563   -544       O  
ATOM   3400  CB  ALA A 448      18.326  51.251   8.202  1.00 58.59           C  
ANISOU 3400  CB  ALA A 448     7294   7214   7754   -635  -1419   -540       C  
ATOM   3401  N   ALA A 449      20.621  53.412   8.425  1.00 70.32           N  
ANISOU 3401  N   ALA A 449     8773   8641   9305   -732  -1545   -452       N  
ATOM   3402  CA  ALA A 449      21.672  54.097   9.172  1.00 71.18           C  
ANISOU 3402  CA  ALA A 449     8904   8717   9424   -764  -1617   -425       C  
ATOM   3403  C   ALA A 449      21.455  55.604   9.185  1.00 73.81           C  
ANISOU 3403  C   ALA A 449     9298   8989   9757   -780  -1657   -430       C  
ATOM   3404  O   ALA A 449      21.816  56.278  10.158  1.00 71.14           O  
ANISOU 3404  O   ALA A 449     9025   8603   9403   -788  -1719   -435       O  
ATOM   3405  CB  ALA A 449      23.043  53.762   8.582  1.00 71.66           C  
ANISOU 3405  CB  ALA A 449     8865   8821   9540   -804  -1624   -356       C  
ATOM   3406  N   ALA A 450      20.869  56.148   8.116  1.00 76.09           N  
ANISOU 3406  N   ALA A 450     9570   9277  10065   -785  -1623   -428       N  
ATOM   3407  CA  ALA A 450      20.517  57.563   8.098  1.00 78.10           C  
ANISOU 3407  CA  ALA A 450     9885   9471  10317   -796  -1656   -437       C  
ATOM   3408  C   ALA A 450      19.370  57.854   9.062  1.00 82.68           C  
ANISOU 3408  C   ALA A 450    10575  10004  10835   -749  -1662   -503       C  
ATOM   3409  O   ALA A 450      19.415  58.833   9.817  1.00 83.95           O  
ANISOU 3409  O   ALA A 450    10814  10107  10978   -751  -1718   -515       O  
ATOM   3410  CB  ALA A 450      20.158  57.993   6.675  1.00 74.63           C  
ANISOU 3410  CB  ALA A 450     9394   9049   9913   -811  -1614   -416       C  
ATOM   3411  N   LEU A 451      18.339  57.009   9.057  1.00 85.76           N  
ANISOU 3411  N   LEU A 451    10975  10419  11191   -705  -1606   -544       N  
ATOM   3412  CA  LEU A 451      17.178  57.179   9.933  1.00 84.09           C  
ANISOU 3412  CA  LEU A 451    10865  10170  10917   -653  -1600   -605       C  
ATOM   3413  C   LEU A 451      17.570  57.188  11.410  1.00 87.01           C  
ANISOU 3413  C   LEU A 451    11304  10508  11248   -638  -1654   -622       C  
ATOM   3414  O   LEU A 451      17.469  58.217  12.083  1.00 87.53           O  
ANISOU 3414  O   LEU A 451    11451  10516  11292   -634  -1700   -638       O  
ATOM   3415  CB  LEU A 451      16.152  56.073   9.674  1.00 30.00           C  
TER    3416      LEU A 451                                                      
ATOM   3417  N   LYS B  30     -54.532 -11.822 -10.889  1.00 72.81           N  
ANISOU 3417  N   LYS B  30     9211   9555   8900   -636   1143    101       N  
ATOM   3418  CA  LYS B  30     -53.790 -10.875 -11.714  1.00 70.35           C  
ANISOU 3418  CA  LYS B  30     8864   9233   8634   -590   1098     90       C  
ATOM   3419  C   LYS B  30     -52.797 -11.600 -12.629  1.00 65.93           C  
ANISOU 3419  C   LYS B  30     8308   8654   8089   -592   1021    110       C  
ATOM   3420  O   LYS B  30     -51.934 -12.349 -12.164  1.00 65.67           O  
ANISOU 3420  O   LYS B  30     8346   8595   8011   -609    983    119       O  
ATOM   3421  CB  LYS B  30     -53.062  -9.856 -10.829  1.00 70.93           C  
ANISOU 3421  CB  LYS B  30     8988   9284   8680   -559   1095     63       C  
ATOM   3422  CG  LYS B  30     -52.480  -8.665 -11.583  1.00 71.44           C  
ANISOU 3422  CG  LYS B  30     9009   9341   8794   -509   1062     47       C  
ATOM   3423  CD  LYS B  30     -51.985  -7.591 -10.622  1.00 71.14           C  
ANISOU 3423  CD  LYS B  30     9015   9285   8729   -480   1073     18       C  
ATOM   3424  CE  LYS B  30     -50.956  -8.151  -9.644  1.00 78.72           C  
ANISOU 3424  CE  LYS B  30    10074  10213   9623   -495   1040     18       C  
ATOM   3425  NZ  LYS B  30     -50.347  -7.100  -8.767  1.00 76.17           N  
ANISOU 3425  NZ  LYS B  30     9795   9871   9276   -465   1044    -12       N  
ATOM   3426  N   LYS B  31     -52.932 -11.388 -13.935  1.00 57.20           N  
ANISOU 3426  N   LYS B  31     7126   7563   7046   -574    998    117       N  
ATOM   3427  CA  LYS B  31     -52.025 -12.016 -14.878  1.00 50.51           C  
ANISOU 3427  CA  LYS B  31     6275   6699   6217   -573    926    136       C  
ATOM   3428  C   LYS B  31     -50.706 -11.255 -14.933  1.00 40.94           C  
ANISOU 3428  C   LYS B  31     5092   5456   5006   -534    869    122       C  
ATOM   3429  O   LYS B  31     -50.619 -10.077 -14.576  1.00 38.82           O  
ANISOU 3429  O   LYS B  31     4821   5185   4745   -501    887     98       O  
ATOM   3430  CB  LYS B  31     -52.649 -12.083 -16.272  1.00 53.35           C  
ANISOU 3430  CB  LYS B  31     6540   7086   6643   -568    921    149       C  
ATOM   3431  CG  LYS B  31     -53.817 -13.047 -16.367  1.00 72.06           C  
ANISOU 3431  CG  LYS B  31     8882   9484   9012   -611    964    166       C  
ATOM   3432  CD  LYS B  31     -54.488 -12.990 -17.731  1.00 83.78           C  
ANISOU 3432  CD  LYS B  31    10269  11000  10565   -602    964    175       C  
ATOM   3433  CE  LYS B  31     -55.644 -13.982 -17.813  1.00 84.52           C  
ANISOU 3433  CE  LYS B  31    10336  11122  10657   -646   1007    192       C  
ATOM   3434  NZ  LYS B  31     -56.391 -13.850 -19.096  1.00 85.54           N  
ANISOU 3434  NZ  LYS B  31    10366  11284  10851   -636   1013    198       N  
ATOM   3435  N   ALA B  32     -49.665 -11.954 -15.375  1.00 32.46           N  
ANISOU 3435  N   ALA B  32     4048   4359   3927   -539    802    138       N  
ATOM   3436  CA  ALA B  32     -48.370 -11.316 -15.541  1.00 24.20           C  
ANISOU 3436  CA  ALA B  32     3026   3283   2885   -503    743    127       C  
ATOM   3437  C   ALA B  32     -48.466 -10.232 -16.607  1.00 27.02           C  
ANISOU 3437  C   ALA B  32     3302   3653   3311   -461    734    118       C  
ATOM   3438  O   ALA B  32     -49.262 -10.323 -17.542  1.00 25.09           O  
ANISOU 3438  O   ALA B  32     2982   3436   3114   -462    749    128       O  
ATOM   3439  CB  ALA B  32     -47.311 -12.356 -15.910  1.00 23.63           C  
ANISOU 3439  CB  ALA B  32     2995   3186   2796   -519    672    148       C  
ATOM   3440  N   GLY B  33     -47.667  -9.179 -16.443  1.00 26.59           N  
ANISOU 3440  N   GLY B  33     3263   3579   3262   -422    713     97       N  
ATOM   3441  CA  GLY B  33     -47.639  -8.101 -17.400  1.00 23.03           C  
ANISOU 3441  CA  GLY B  33     2741   3136   2874   -378    702     87       C  
ATOM   3442  C   GLY B  33     -46.436  -7.203 -17.200  1.00 24.31           C  
ANISOU 3442  C   GLY B  33     2937   3266   3032   -340    661     67       C  
ATOM   3443  O   GLY B  33     -45.697  -7.321 -16.215  1.00 20.88           O  
ANISOU 3443  O   GLY B  33     2582   2806   2545   -347    647     58       O  
ATOM   3444  N   PRO B  34     -46.222  -6.276 -18.133  1.00 23.94           N  
ANISOU 3444  N   PRO B  34     2832   3222   3044   -300    641     61       N  
ATOM   3445  CA  PRO B  34     -45.079  -5.364 -18.012  1.00 21.13           C  
ANISOU 3445  CA  PRO B  34     2503   2837   2690   -262    601     41       C  
ATOM   3446  C   PRO B  34     -45.293  -4.370 -16.885  1.00 23.96           C  
ANISOU 3446  C   PRO B  34     2891   3191   3023   -247    651     11       C  
ATOM   3447  O   PRO B  34     -46.411  -3.915 -16.641  1.00 23.97           O  
ANISOU 3447  O   PRO B  34     2855   3218   3035   -247    715      3       O  
ATOM   3448  CB  PRO B  34     -45.030  -4.669 -19.381  1.00 20.72           C  
ANISOU 3448  CB  PRO B  34     2369   2794   2711   -225    577     44       C  
ATOM   3449  CG  PRO B  34     -46.436  -4.760 -19.905  1.00 23.56           C  
ANISOU 3449  CG  PRO B  34     2653   3193   3105   -235    630     54       C  
ATOM   3450  CD  PRO B  34     -46.999  -6.053 -19.369  1.00 21.37           C  
ANISOU 3450  CD  PRO B  34     2409   2926   2783   -287    652     71       C  
ATOM   3451  N   VAL B  35     -44.212  -4.040 -16.183  1.00 20.06           N  
ANISOU 3451  N   VAL B  35     2463   2665   2494   -234    620     -5       N  
ATOM   3452  CA  VAL B  35     -44.286  -3.150 -15.029  1.00 21.68           C  
ANISOU 3452  CA  VAL B  35     2705   2863   2668   -221    662    -34       C  
ATOM   3453  C   VAL B  35     -43.277  -2.034 -15.215  1.00 19.54           C  
ANISOU 3453  C   VAL B  35     2436   2567   2420   -176    625    -56       C  
ATOM   3454  O   VAL B  35     -42.080  -2.293 -15.378  1.00 20.20           O  
ANISOU 3454  O   VAL B  35     2558   2624   2492   -170    562    -53       O  
ATOM   3455  CB  VAL B  35     -44.022  -3.876 -13.703  1.00 22.57           C  
ANISOU 3455  CB  VAL B  35     2910   2962   2705   -254    670    -37       C  
ATOM   3456  CG1 VAL B  35     -43.939  -2.856 -12.572  1.00 19.20           C  
ANISOU 3456  CG1 VAL B  35     2520   2525   2249   -235    705    -69       C  
ATOM   3457  CG2 VAL B  35     -45.124  -4.898 -13.428  1.00 24.03           C  
ANISOU 3457  CG2 VAL B  35     3091   3172   2867   -298    715    -17       C  
ATOM   3458  N   GLN B  36     -43.750  -0.799 -15.176  1.00 20.37           N  
ANISOU 3458  N   GLN B  36     2501   2683   2557   -145    666    -78       N  
ATOM   3459  CA  GLN B  36     -42.862   0.346 -15.300  1.00 19.37           C  
ANISOU 3459  CA  GLN B  36     2375   2533   2453   -101    638   -100       C  
ATOM   3460  C   GLN B  36     -42.116   0.543 -13.981  1.00 19.01           C  
ANISOU 3460  C   GLN B  36     2416   2461   2346   -103    635   -123       C  
ATOM   3461  O   GLN B  36     -42.740   0.768 -12.943  1.00 20.17           O  
ANISOU 3461  O   GLN B  36     2589   2616   2459   -114    691   -139       O  
ATOM   3462  CB  GLN B  36     -43.672   1.585 -15.675  1.00 19.54           C  
ANISOU 3462  CB  GLN B  36     2324   2573   2527    -68    686   -116       C  
ATOM   3463  CG  GLN B  36     -42.812   2.755 -16.114  1.00 20.93           C  
ANISOU 3463  CG  GLN B  36     2483   2728   2741    -21    654   -135       C  
ATOM   3464  CD  GLN B  36     -42.311   2.594 -17.530  1.00 21.30           C  
ANISOU 3464  CD  GLN B  36     2480   2773   2841     -4    597   -115       C  
ATOM   3465  OE1 GLN B  36     -42.979   1.970 -18.362  1.00 19.02           O  
ANISOU 3465  OE1 GLN B  36     2140   2508   2580    -18    600    -91       O  
ATOM   3466  NE2 GLN B  36     -41.128   3.150 -17.818  1.00 18.70           N  
ANISOU 3466  NE2 GLN B  36     2165   2414   2526     26    545   -126       N  
ATOM   3467  N   VAL B  37     -40.788   0.449 -14.008  1.00 19.81           N  
ANISOU 3467  N   VAL B  37     2563   2531   2433    -93    571   -126       N  
ATOM   3468  CA  VAL B  37     -39.978   0.594 -12.808  1.00 21.58           C  
ANISOU 3468  CA  VAL B  37     2871   2729   2599    -94    561   -148       C  
ATOM   3469  C   VAL B  37     -39.142   1.871 -12.828  1.00 19.65           C  
ANISOU 3469  C   VAL B  37     2626   2462   2377    -50    541   -176       C  
ATOM   3470  O   VAL B  37     -38.988   2.526 -11.794  1.00 21.22           O  
ANISOU 3470  O   VAL B  37     2867   2651   2545    -41    566   -204       O  
ATOM   3471  CB  VAL B  37     -39.090  -0.650 -12.579  1.00 19.09           C  
ANISOU 3471  CB  VAL B  37     2624   2395   2235   -123    507   -130       C  
ATOM   3472  CG1 VAL B  37     -39.974  -1.875 -12.353  1.00 20.94           C  
ANISOU 3472  CG1 VAL B  37     2866   2650   2440   -169    536   -105       C  
ATOM   3473  CG2 VAL B  37     -38.166  -0.878 -13.744  1.00 23.25           C  
ANISOU 3473  CG2 VAL B  37     3129   2907   2799   -108    434   -114       C  
ATOM   3474  N   LEU B  38     -38.574   2.235 -13.972  1.00 19.52           N  
ANISOU 3474  N   LEU B  38     2565   2437   2415    -22    495   -171       N  
ATOM   3475  CA  LEU B  38     -37.889   3.512 -14.117  1.00 19.72           C  
ANISOU 3475  CA  LEU B  38     2578   2443   2471     22    480   -197       C  
ATOM   3476  C   LEU B  38     -38.767   4.428 -14.952  1.00 19.18           C  
ANISOU 3476  C   LEU B  38     2420   2396   2470     50    517   -199       C  
ATOM   3477  O   LEU B  38     -39.109   4.099 -16.098  1.00 19.76           O  
ANISOU 3477  O   LEU B  38     2433   2486   2590     51    503   -175       O  
ATOM   3478  CB  LEU B  38     -36.517   3.356 -14.768  1.00 19.72           C  
ANISOU 3478  CB  LEU B  38     2595   2414   2482     38    399   -191       C  
ATOM   3479  CG  LEU B  38     -35.864   4.707 -15.066  1.00 20.26           C  
ANISOU 3479  CG  LEU B  38     2641   2464   2591     85    384   -217       C  
ATOM   3480  CD1 LEU B  38     -35.466   5.371 -13.753  1.00 21.02           C  
ANISOU 3480  CD1 LEU B  38     2801   2543   2643     92    404   -251       C  
ATOM   3481  CD2 LEU B  38     -34.656   4.559 -15.993  1.00 15.87           C  
ANISOU 3481  CD2 LEU B  38     2084   1886   2061    102    306   -206       C  
ATOM   3482  N   ILE B  39     -39.150   5.558 -14.368  1.00 19.25           N  
ANISOU 3482  N   ILE B  39     2421   2407   2486     72    566   -227       N  
ATOM   3483  CA  ILE B  39     -40.013   6.540 -15.011  1.00 20.84           C  
ANISOU 3483  CA  ILE B  39     2542   2629   2748    101    608   -233       C  
ATOM   3484  C   ILE B  39     -39.145   7.726 -15.392  1.00 19.65           C  
ANISOU 3484  C   ILE B  39     2377   2455   2636    146    580   -254       C  
ATOM   3485  O   ILE B  39     -38.337   8.190 -14.579  1.00 23.72           O  
ANISOU 3485  O   ILE B  39     2949   2944   3120    157    567   -280       O  
ATOM   3486  CB  ILE B  39     -41.166   6.971 -14.077  1.00 24.12           C  
ANISOU 3486  CB  ILE B  39     2955   3065   3143     92    689   -249       C  
ATOM   3487  CG1 ILE B  39     -42.224   5.869 -13.956  1.00 22.15           C  
ANISOU 3487  CG1 ILE B  39     2699   2845   2871     50    722   -225       C  
ATOM   3488  CG2 ILE B  39     -41.809   8.270 -14.546  1.00 18.18           C  
ANISOU 3488  CG2 ILE B  39     2131   2326   2449    130    730   -264       C  
ATOM   3489  CD1 ILE B  39     -41.906   4.799 -12.924  1.00 27.94           C  
ANISOU 3489  CD1 ILE B  39     3517   3569   3530     10    713   -220       C  
ATOM   3490  N   VAL B  40     -39.291   8.207 -16.623  1.00 19.48           N  
ANISOU 3490  N   VAL B  40     2280   2441   2681    174    569   -244       N  
ATOM   3491  CA  VAL B  40     -38.694   9.471 -17.034  1.00 21.69           C  
ANISOU 3491  CA  VAL B  40     2534   2703   3006    221    555   -265       C  
ATOM   3492  C   VAL B  40     -39.809  10.502 -17.085  1.00 22.76           C  
ANISOU 3492  C   VAL B  40     2607   2860   3179    243    623   -278       C  
ATOM   3493  O   VAL B  40     -40.791  10.341 -17.822  1.00 23.22           O  
ANISOU 3493  O   VAL B  40     2601   2948   3273    240    650   -259       O  
ATOM   3494  CB  VAL B  40     -37.965   9.370 -18.381  1.00 22.92           C  
ANISOU 3494  CB  VAL B  40     2650   2849   3211    241    491   -246       C  
ATOM   3495  CG1 VAL B  40     -37.264  10.695 -18.692  1.00 25.36           C  
ANISOU 3495  CG1 VAL B  40     2939   3134   3561    288    477   -269       C  
ATOM   3496  CG2 VAL B  40     -36.962   8.229 -18.357  1.00 19.30           C  
ANISOU 3496  CG2 VAL B  40     2249   2371   2714    215    425   -230       C  
ATOM   3497  N   LYS B  41     -39.676  11.540 -16.276  1.00 19.55           N  
ANISOU 3497  N   LYS B  41     2224   2440   2764    263    653   -311       N  
ATOM   3498  CA  LYS B  41     -40.708  12.556 -16.189  1.00 22.09           C  
ANISOU 3498  CA  LYS B  41     2495   2782   3116    284    720   -326       C  
ATOM   3499  C   LYS B  41     -40.559  13.554 -17.335  1.00 25.65           C  
ANISOU 3499  C   LYS B  41     2874   3229   3641    329    709   -327       C  
ATOM   3500  O   LYS B  41     -39.527  13.620 -18.012  1.00 21.92           O  
ANISOU 3500  O   LYS B  41     2402   2734   3191    348    649   -323       O  
ATOM   3501  CB  LYS B  41     -40.634  13.270 -14.844  1.00 20.85           C  
ANISOU 3501  CB  LYS B  41     2391   2611   2919    288    758   -361       C  
ATOM   3502  CG  LYS B  41     -40.748  12.363 -13.631  1.00 23.13           C  
ANISOU 3502  CG  LYS B  41     2754   2902   3133    245    771   -363       C  
ATOM   3503  CD  LYS B  41     -42.156  11.828 -13.445  1.00 27.63           C  
ANISOU 3503  CD  LYS B  41     3298   3509   3693    217    831   -347       C  
ATOM   3504  CE  LYS B  41     -43.141  12.940 -13.060  1.00 31.45           C  
ANISOU 3504  CE  LYS B  41     3744   4009   4196    237    904   -370       C  
ATOM   3505  NZ  LYS B  41     -42.818  13.567 -11.748  1.00 31.00           N  
ANISOU 3505  NZ  LYS B  41     3749   3935   4096    241    927   -404       N  
ATOM   3506  N   ASP B  42     -41.615  14.351 -17.539  1.00 25.25           N  
ANISOU 3506  N   ASP B  42     2763   3202   3629    348    768   -333       N  
ATOM   3507  CA  ASP B  42     -41.613  15.319 -18.627  1.00 25.02           C  
ANISOU 3507  CA  ASP B  42     2662   3174   3672    392    764   -333       C  
ATOM   3508  C   ASP B  42     -40.478  16.327 -18.485  1.00 24.61           C  
ANISOU 3508  C   ASP B  42     2634   3085   3632    427    735   -359       C  
ATOM   3509  O   ASP B  42     -40.009  16.865 -19.488  1.00 24.14           O  
ANISOU 3509  O   ASP B  42     2531   3015   3626    460    704   -355       O  
ATOM   3510  CB  ASP B  42     -42.952  16.054 -18.686  1.00 23.47           C  
ANISOU 3510  CB  ASP B  42     2403   3007   3506    405    838   -338       C  
ATOM   3511  CG  ASP B  42     -44.089  15.171 -19.139  1.00 28.93           C  
ANISOU 3511  CG  ASP B  42     3052   3738   4203    378    864   -309       C  
ATOM   3512  OD1 ASP B  42     -43.856  14.012 -19.550  1.00 30.69           O  
ANISOU 3512  OD1 ASP B  42     3285   3964   4411    351    823   -283       O  
ATOM   3513  OD2 ASP B  42     -45.237  15.652 -19.075  1.00 37.34           O  
ANISOU 3513  OD2 ASP B  42     4072   4830   5285    384    927   -313       O  
ATOM   3514  N   ASP B  43     -40.032  16.605 -17.258  1.00 21.72           N  
ANISOU 3514  N   ASP B  43     2337   2698   3218    421    745   -388       N  
ATOM   3515  CA  ASP B  43     -38.920  17.517 -17.022  1.00 21.52           C  
ANISOU 3515  CA  ASP B  43     2340   2637   3199    451    717   -415       C  
ATOM   3516  C   ASP B  43     -37.570  16.806 -17.051  1.00 23.54           C  
ANISOU 3516  C   ASP B  43     2653   2864   3427    440    641   -410       C  
ATOM   3517  O   ASP B  43     -36.563  17.387 -16.627  1.00 21.38           O  
ANISOU 3517  O   ASP B  43     2421   2559   3144    457    615   -435       O  
ATOM   3518  CB  ASP B  43     -39.114  18.266 -15.689  1.00 23.83           C  
ANISOU 3518  CB  ASP B  43     2676   2923   3457    453    767   -452       C  
ATOM   3519  CG  ASP B  43     -39.049  17.346 -14.460  1.00 25.97           C  
ANISOU 3519  CG  ASP B  43     3026   3192   3649    411    770   -456       C  
ATOM   3520  OD1 ASP B  43     -38.882  16.115 -14.603  1.00 23.10           O  
ANISOU 3520  OD1 ASP B  43     2687   2834   3257    379    736   -430       O  
ATOM   3521  OD2 ASP B  43     -39.169  17.863 -13.332  1.00 28.38           O  
ANISOU 3521  OD2 ASP B  43     3371   3492   3920    410    808   -485       O  
ATOM   3522  N   HIS B  44     -37.545  15.552 -17.511  1.00 19.93           N  
ANISOU 3522  N   HIS B  44     2200   2418   2955    410    606   -378       N  
ATOM   3523  CA  HIS B  44     -36.343  14.748 -17.713  1.00 23.26           C  
ANISOU 3523  CA  HIS B  44     2667   2816   3354    398    531   -367       C  
ATOM   3524  C   HIS B  44     -35.682  14.331 -16.410  1.00 22.80           C  
ANISOU 3524  C   HIS B  44     2703   2738   3223    374    519   -385       C  
ATOM   3525  O   HIS B  44     -34.526  13.905 -16.411  1.00 25.63           O  
ANISOU 3525  O   HIS B  44     3106   3071   3560    370    458   -384       O  
ATOM   3526  CB  HIS B  44     -35.350  15.475 -18.623  1.00 23.35           C  
ANISOU 3526  CB  HIS B  44     2652   2802   3417    438    482   -371       C  
ATOM   3527  CG  HIS B  44     -35.945  15.841 -19.942  1.00 22.19           C  
ANISOU 3527  CG  HIS B  44     2415   2674   3341    463    490   -351       C  
ATOM   3528  ND1 HIS B  44     -35.947  14.978 -21.018  1.00 19.95           N  
ANISOU 3528  ND1 HIS B  44     2097   2403   3080    453    451   -317       N  
ATOM   3529  CD2 HIS B  44     -36.618  16.948 -20.340  1.00 21.05           C  
ANISOU 3529  CD2 HIS B  44     2207   2541   3249    496    535   -361       C  
ATOM   3530  CE1 HIS B  44     -36.565  15.555 -22.035  1.00 22.48           C  
ANISOU 3530  CE1 HIS B  44     2336   2742   3464    481    470   -307       C  
ATOM   3531  NE2 HIS B  44     -36.987  16.748 -21.647  1.00 20.35           N  
ANISOU 3531  NE2 HIS B  44     2048   2472   3213    507    521   -332       N  
ATOM   3532  N   SER B  45     -36.402  14.435 -15.302  1.00 20.49           N  
ANISOU 3532  N   SER B  45     2438   2458   2891    357    576   -401       N  
ATOM   3533  CA  SER B  45     -35.981  13.801 -14.071  1.00 23.31           C  
ANISOU 3533  CA  SER B  45     2880   2803   3173    327    570   -412       C  
ATOM   3534  C   SER B  45     -36.436  12.349 -14.075  1.00 23.29           C  
ANISOU 3534  C   SER B  45     2894   2821   3136    283    564   -380       C  
ATOM   3535  O   SER B  45     -37.352  11.962 -14.811  1.00 24.31           O  
ANISOU 3535  O   SER B  45     2965   2977   3294    274    584   -355       O  
ATOM   3536  CB  SER B  45     -36.549  14.530 -12.854  1.00 24.22           C  
ANISOU 3536  CB  SER B  45     3020   2922   3259    328    634   -443       C  
ATOM   3537  OG  SER B  45     -37.945  14.326 -12.729  1.00 24.32           O  
ANISOU 3537  OG  SER B  45     2999   2970   3273    311    697   -432       O  
ATOM   3538  N   PHE B  46     -35.778  11.545 -13.241  1.00 22.36           N  
ANISOU 3538  N   PHE B  46     2853   2688   2953    255    536   -382       N  
ATOM   3539  CA  PHE B  46     -36.007  10.109 -13.169  1.00 21.63           C  
ANISOU 3539  CA  PHE B  46     2787   2608   2822    213    522   -352       C  
ATOM   3540  C   PHE B  46     -36.625   9.727 -11.832  1.00 21.70           C  
ANISOU 3540  C   PHE B  46     2849   2628   2767    182    572   -362       C  
ATOM   3541  O   PHE B  46     -36.254  10.271 -10.786  1.00 22.53           O  
ANISOU 3541  O   PHE B  46     3005   2719   2837    188    586   -392       O  
ATOM   3542  CB  PHE B  46     -34.697   9.350 -13.347  1.00 20.85           C  
ANISOU 3542  CB  PHE B  46     2739   2484   2699    204    445   -342       C  
ATOM   3543  CG  PHE B  46     -33.889   9.818 -14.504  1.00 26.07           C  
ANISOU 3543  CG  PHE B  46     3360   3128   3416    237    392   -338       C  
ATOM   3544  CD1 PHE B  46     -34.265   9.495 -15.806  1.00 25.93           C  
ANISOU 3544  CD1 PHE B  46     3275   3127   3451    241    376   -308       C  
ATOM   3545  CD2 PHE B  46     -32.732  10.557 -14.299  1.00 23.38           C  
ANISOU 3545  CD2 PHE B  46     3051   2756   3076    264    356   -363       C  
ATOM   3546  CE1 PHE B  46     -33.514   9.917 -16.892  1.00 24.56           C  
ANISOU 3546  CE1 PHE B  46     3064   2938   3330    272    327   -304       C  
ATOM   3547  CE2 PHE B  46     -31.965  10.986 -15.383  1.00 24.05           C  
ANISOU 3547  CE2 PHE B  46     3100   2825   3214    295    306   -359       C  
ATOM   3548  CZ  PHE B  46     -32.361  10.668 -16.679  1.00 25.20           C  
ANISOU 3548  CZ  PHE B  46     3176   2986   3411    299    292   -329       C  
ATOM   3549  N   GLU B  47     -37.550   8.768 -11.865  1.00 25.38           N  
ANISOU 3549  N   GLU B  47     3304   3122   3218    148    598   -337       N  
ATOM   3550  CA  GLU B  47     -38.144   8.216 -10.653  1.00 23.38           C  
ANISOU 3550  CA  GLU B  47     3102   2880   2902    114    641   -340       C  
ATOM   3551  C   GLU B  47     -38.122   6.703 -10.731  1.00 24.55           C  
ANISOU 3551  C   GLU B  47     3279   3033   3014     73    614   -308       C  
ATOM   3552  O   GLU B  47     -38.459   6.121 -11.770  1.00 23.42           O  
ANISOU 3552  O   GLU B  47     3087   2905   2906     65    598   -279       O  
ATOM   3553  CB  GLU B  47     -39.583   8.689 -10.443  1.00 22.24           C  
ANISOU 3553  CB  GLU B  47     2910   2766   2773    113    720   -345       C  
ATOM   3554  CG  GLU B  47     -39.715  10.187 -10.423  1.00 24.49           C  
ANISOU 3554  CG  GLU B  47     3160   3047   3098    154    752   -375       C  
ATOM   3555  CD  GLU B  47     -41.129  10.640 -10.130  1.00 35.96           C  
ANISOU 3555  CD  GLU B  47     4572   4530   4562    152    831   -381       C  
ATOM   3556  OE1 GLU B  47     -42.044   9.778 -10.120  1.00 33.85           O  
ANISOU 3556  OE1 GLU B  47     4293   4289   4280    119    859   -359       O  
ATOM   3557  OE2 GLU B  47     -41.313  11.864  -9.914  1.00 36.09           O  
ANISOU 3557  OE2 GLU B  47     4566   4544   4602    182    865   -408       O  
ATOM   3558  N   LEU B  48     -37.722   6.076  -9.635  1.00 20.98           N  
ANISOU 3558  N   LEU B  48     2907   2572   2494     47    608   -314       N  
ATOM   3559  CA  LEU B  48     -37.863   4.640  -9.478  1.00 22.33           C  
ANISOU 3559  CA  LEU B  48     3112   2750   2623      5    596   -285       C  
ATOM   3560  C   LEU B  48     -39.193   4.359  -8.794  1.00 25.09           C  
ANISOU 3560  C   LEU B  48     3457   3128   2947    -22    668   -282       C  
ATOM   3561  O   LEU B  48     -39.502   4.965  -7.764  1.00 24.13           O  
ANISOU 3561  O   LEU B  48     3362   3009   2798    -18    714   -308       O  
ATOM   3562  CB  LEU B  48     -36.707   4.081  -8.653  1.00 25.82           C  
ANISOU 3562  CB  LEU B  48     3644   3166   3002     -8    551   -292       C  
ATOM   3563  CG  LEU B  48     -36.676   2.572  -8.429  1.00 29.64           C  
ANISOU 3563  CG  LEU B  48     4172   3652   3436    -51    531   -263       C  
ATOM   3564  CD1 LEU B  48     -36.625   1.850  -9.759  1.00 27.53           C  
ANISOU 3564  CD1 LEU B  48     3858   3391   3211    -58    489   -230       C  
ATOM   3565  CD2 LEU B  48     -35.460   2.202  -7.586  1.00 27.65           C  
ANISOU 3565  CD2 LEU B  48     4009   3373   3124    -57    487   -273       C  
ATOM   3566  N   ASP B  49     -39.992   3.470  -9.378  1.00 23.40           N  
ANISOU 3566  N   ASP B  49     3208   2938   2746    -48    680   -251       N  
ATOM   3567  CA  ASP B  49     -41.189   2.998  -8.682  1.00 24.09           C  
ANISOU 3567  CA  ASP B  49     3300   3052   2803    -80    744   -245       C  
ATOM   3568  C   ASP B  49     -40.748   1.866  -7.771  1.00 24.02           C  
ANISOU 3568  C   ASP B  49     3374   3031   2720   -116    726   -236       C  
ATOM   3569  O   ASP B  49     -40.786   0.692  -8.137  1.00 25.41           O  
ANISOU 3569  O   ASP B  49     3557   3212   2886   -146    704   -207       O  
ATOM   3570  CB  ASP B  49     -42.265   2.550  -9.659  1.00 22.73           C  
ANISOU 3570  CB  ASP B  49     3053   2908   2674    -93    766   -218       C  
ATOM   3571  CG  ASP B  49     -43.595   2.287  -8.976  1.00 24.94           C  
ANISOU 3571  CG  ASP B  49     3327   3217   2931   -120    840   -216       C  
ATOM   3572  OD1 ASP B  49     -43.613   2.023  -7.751  1.00 22.41           O  
ANISOU 3572  OD1 ASP B  49     3072   2892   2549   -140    864   -227       O  
ATOM   3573  OD2 ASP B  49     -44.626   2.334  -9.675  1.00 26.26           O  
ANISOU 3573  OD2 ASP B  49     3425   3412   3141   -121    874   -204       O  
ATOM   3574  N   GLU B  50     -40.309   2.229  -6.563  1.00 26.04           N  
ANISOU 3574  N   GLU B  50     3695   3272   2926   -113    737   -262       N  
ATOM   3575  CA  GLU B  50     -39.803   1.222  -5.637  1.00 27.66           C  
ANISOU 3575  CA  GLU B  50     3984   3466   3058   -144    719   -255       C  
ATOM   3576  C   GLU B  50     -40.895   0.244  -5.236  1.00 24.30           C  
ANISOU 3576  C   GLU B  50     3563   3065   2603   -186    766   -234       C  
ATOM   3577  O   GLU B  50     -40.640  -0.955  -5.107  1.00 25.99           O  
ANISOU 3577  O   GLU B  50     3819   3275   2780   -217    741   -211       O  
ATOM   3578  CB  GLU B  50     -39.206   1.886  -4.396  1.00 28.26           C  
ANISOU 3578  CB  GLU B  50     4125   3524   3087   -131    728   -289       C  
ATOM   3579  CG  GLU B  50     -38.085   2.856  -4.711  1.00 29.75           C  
ANISOU 3579  CG  GLU B  50     4314   3687   3302    -91    682   -313       C  
ATOM   3580  CD  GLU B  50     -37.335   3.313  -3.464  1.00 40.92           C  
ANISOU 3580  CD  GLU B  50     5802   5083   4663    -82    680   -345       C  
ATOM   3581  OE1 GLU B  50     -37.538   2.704  -2.382  1.00 31.93           O  
ANISOU 3581  OE1 GLU B  50     4723   3949   3461   -109    704   -345       O  
ATOM   3582  OE2 GLU B  50     -36.538   4.277  -3.581  1.00 39.84           O  
ANISOU 3582  OE2 GLU B  50     5664   4926   4548    -48    654   -369       O  
ATOM   3583  N   THR B  51     -42.116   0.738  -5.031  1.00 24.20           N  
ANISOU 3583  N   THR B  51     3510   3079   2607   -186    835   -242       N  
ATOM   3584  CA  THR B  51     -43.214  -0.148  -4.661  1.00 27.38           C  
ANISOU 3584  CA  THR B  51     3914   3506   2983   -225    884   -222       C  
ATOM   3585  C   THR B  51     -43.402  -1.241  -5.704  1.00 27.37           C  
ANISOU 3585  C   THR B  51     3879   3514   3006   -249    855   -185       C  
ATOM   3586  O   THR B  51     -43.441  -2.434  -5.375  1.00 26.16           O  
ANISOU 3586  O   THR B  51     3767   3362   2812   -286    849   -164       O  
ATOM   3587  CB  THR B  51     -44.502   0.660  -4.481  1.00 26.76           C  
ANISOU 3587  CB  THR B  51     3783   3455   2930   -218    959   -236       C  
ATOM   3588  OG1 THR B  51     -44.323   1.611  -3.430  1.00 25.64           O  
ANISOU 3588  OG1 THR B  51     3678   3304   2760   -198    987   -270       O  
ATOM   3589  CG2 THR B  51     -45.681  -0.256  -4.122  1.00 28.97           C  
ANISOU 3589  CG2 THR B  51     4061   3761   3184   -259   1011   -216       C  
ATOM   3590  N   ALA B  52     -43.510  -0.849  -6.976  1.00 26.11           N  
ANISOU 3590  N   ALA B  52     3645   3361   2915   -227    837   -178       N  
ATOM   3591  CA  ALA B  52     -43.661  -1.834  -8.041  1.00 28.04           C  
ANISOU 3591  CA  ALA B  52     3853   3614   3186   -247    807   -144       C  
ATOM   3592  C   ALA B  52     -42.449  -2.752  -8.110  1.00 25.72           C  
ANISOU 3592  C   ALA B  52     3617   3294   2861   -260    736   -129       C  
ATOM   3593  O   ALA B  52     -42.592  -3.972  -8.257  1.00 27.53           O  
ANISOU 3593  O   ALA B  52     3861   3528   3072   -295    724   -102       O  
ATOM   3594  CB  ALA B  52     -43.882  -1.128  -9.379  1.00 24.15           C  
ANISOU 3594  CB  ALA B  52     3271   3132   2772   -216    797   -141       C  
ATOM   3595  N   LEU B  53     -41.246  -2.186  -7.985  1.00 22.59           N  
ANISOU 3595  N   LEU B  53     3255   2870   2459   -233    689   -147       N  
ATOM   3596  CA  LEU B  53     -40.038  -3.001  -8.035  1.00 23.86           C  
ANISOU 3596  CA  LEU B  53     3472   3005   2590   -242    620   -134       C  
ATOM   3597  C   LEU B  53     -39.966  -3.954  -6.844  1.00 27.93           C  
ANISOU 3597  C   LEU B  53     4069   3515   3028   -278    632   -129       C  
ATOM   3598  O   LEU B  53     -39.619  -5.134  -7.003  1.00 24.83           O  
ANISOU 3598  O   LEU B  53     3706   3116   2611   -306    597   -103       O  
ATOM   3599  CB  LEU B  53     -38.799  -2.095  -8.079  1.00 23.72           C  
ANISOU 3599  CB  LEU B  53     3473   2958   2581   -204    573   -158       C  
ATOM   3600  CG  LEU B  53     -37.465  -2.786  -8.395  1.00 25.05           C  
ANISOU 3600  CG  LEU B  53     3685   3100   2732   -206    493   -146       C  
ATOM   3601  CD1 LEU B  53     -37.408  -3.228  -9.852  1.00 26.66           C  
ANISOU 3601  CD1 LEU B  53     3829   3308   2991   -205    452   -119       C  
ATOM   3602  CD2 LEU B  53     -36.264  -1.902  -8.056  1.00 24.78           C  
ANISOU 3602  CD2 LEU B  53     3688   3038   2691   -172    456   -174       C  
ATOM   3603  N   ASN B  54     -40.286  -3.456  -5.642  1.00 24.03           N  
ANISOU 3603  N   ASN B  54     3612   3024   2494   -278    680   -152       N  
ATOM   3604  CA  ASN B  54     -40.267  -4.307  -4.457  1.00 27.49           C  
ANISOU 3604  CA  ASN B  54     4128   3459   2858   -311    695   -148       C  
ATOM   3605  C   ASN B  54     -41.290  -5.427  -4.572  1.00 24.81           C  
ANISOU 3605  C   ASN B  54     3775   3142   2511   -352    728   -118       C  
ATOM   3606  O   ASN B  54     -41.038  -6.555  -4.134  1.00 26.43           O  
ANISOU 3606  O   ASN B  54     4035   3340   2667   -383    713   -100       O  
ATOM   3607  CB  ASN B  54     -40.551  -3.485  -3.199  1.00 25.42           C  
ANISOU 3607  CB  ASN B  54     3900   3200   2560   -301    747   -180       C  
ATOM   3608  CG  ASN B  54     -39.404  -2.590  -2.801  1.00 27.81           C  
ANISOU 3608  CG  ASN B  54     4240   3476   2851   -267    713   -210       C  
ATOM   3609  OD1 ASN B  54     -38.275  -2.760  -3.248  1.00 26.87           O  
ANISOU 3609  OD1 ASN B  54     4139   3334   2735   -256    647   -206       O  
ATOM   3610  ND2 ASN B  54     -39.690  -1.631  -1.929  1.00 27.85           N  
ANISOU 3610  ND2 ASN B  54     4255   3484   2841   -251    758   -241       N  
ATOM   3611  N   ARG B  55     -42.458  -5.131  -5.143  1.00 26.40           N  
ANISOU 3611  N   ARG B  55     3901   3370   2758   -352    774   -113       N  
ATOM   3612  CA  ARG B  55     -43.495  -6.155  -5.261  1.00 25.91           C  
ANISOU 3612  CA  ARG B  55     3822   3332   2692   -391    809    -87       C  
ATOM   3613  C   ARG B  55     -43.006  -7.344  -6.079  1.00 28.56           C  
ANISOU 3613  C   ARG B  55     4159   3659   3032   -413    753    -54       C  
ATOM   3614  O   ARG B  55     -43.297  -8.501  -5.751  1.00 26.88           O  
ANISOU 3614  O   ARG B  55     3980   3451   2784   -451    762    -33       O  
ATOM   3615  CB  ARG B  55     -44.749  -5.547  -5.885  1.00 30.01           C  
ANISOU 3615  CB  ARG B  55     4253   3881   3267   -383    862    -88       C  
ATOM   3616  CG  ARG B  55     -45.892  -6.518  -6.070  1.00 38.81           C  
ANISOU 3616  CG  ARG B  55     5341   5022   4383   -422    900    -62       C  
ATOM   3617  CD  ARG B  55     -47.137  -5.808  -6.593  1.00 55.52           C  
ANISOU 3617  CD  ARG B  55     7373   7170   6553   -411    956    -68       C  
ATOM   3618  NE  ARG B  55     -47.674  -4.842  -5.636  1.00 56.82           N  
ANISOU 3618  NE  ARG B  55     7546   7343   6701   -397   1015    -96       N  
ATOM   3619  CZ  ARG B  55     -47.649  -3.525  -5.796  1.00 55.05           C  
ANISOU 3619  CZ  ARG B  55     7286   7119   6513   -358   1026   -121       C  
ATOM   3620  NH1 ARG B  55     -47.103  -2.968  -6.869  1.00 52.61           N  
ANISOU 3620  NH1 ARG B  55     6930   6802   6258   -326    982   -122       N  
ATOM   3621  NH2 ARG B  55     -48.194  -2.748  -4.861  1.00 47.26           N  
ANISOU 3621  NH2 ARG B  55     6310   6140   5506   -350   1082   -146       N  
ATOM   3622  N   ILE B  56     -42.238  -7.078  -7.130  1.00 27.13           N  
ANISOU 3622  N   ILE B  56     3946   3465   2896   -388    695    -51       N  
ATOM   3623  CA  ILE B  56     -41.756  -8.136  -8.007  1.00 24.11           C  
ANISOU 3623  CA  ILE B  56     3560   3075   2525   -405    640    -22       C  
ATOM   3624  C   ILE B  56     -40.519  -8.806  -7.421  1.00 27.48           C  
ANISOU 3624  C   ILE B  56     4074   3472   2895   -414    587    -18       C  
ATOM   3625  O   ILE B  56     -40.458 -10.035  -7.294  1.00 27.81           O  
ANISOU 3625  O   ILE B  56     4151   3511   2903   -449    573      6       O  
ATOM   3626  CB  ILE B  56     -41.489  -7.545  -9.404  1.00 25.48           C  
ANISOU 3626  CB  ILE B  56     3660   3249   2772   -373    602    -20       C  
ATOM   3627  CG1 ILE B  56     -42.798  -7.022  -9.996  1.00 27.23           C  
ANISOU 3627  CG1 ILE B  56     3796   3504   3047   -368    657    -20       C  
ATOM   3628  CG2 ILE B  56     -40.867  -8.566 -10.335  1.00 25.96           C  
ANISOU 3628  CG2 ILE B  56     3718   3300   2845   -387    539      9       C  
ATOM   3629  CD1 ILE B  56     -42.590  -6.060 -11.145  1.00 26.39           C  
ANISOU 3629  CD1 ILE B  56     3618   3398   3011   -327    632    -27       C  
ATOM   3630  N   LEU B  57     -39.518  -8.023  -7.029  1.00 24.15           N  
ANISOU 3630  N   LEU B  57     3687   3028   2460   -384    557    -42       N  
ATOM   3631  CA  LEU B  57     -38.236  -8.621  -6.687  1.00 21.49           C  
ANISOU 3631  CA  LEU B  57     3424   2662   2078   -388    497    -38       C  
ATOM   3632  C   LEU B  57     -38.086  -8.972  -5.207  1.00 25.71           C  
ANISOU 3632  C   LEU B  57     4045   3189   2535   -407    519    -47       C  
ATOM   3633  O   LEU B  57     -37.171  -9.728  -4.860  1.00 25.72           O  
ANISOU 3633  O   LEU B  57     4111   3170   2491   -419    475    -38       O  
ATOM   3634  CB  LEU B  57     -37.100  -7.687  -7.125  1.00 22.57           C  
ANISOU 3634  CB  LEU B  57     3556   2777   2243   -346    443    -58       C  
ATOM   3635  CG  LEU B  57     -36.872  -7.649  -8.639  1.00 25.46           C  
ANISOU 3635  CG  LEU B  57     3854   3143   2676   -331    398    -42       C  
ATOM   3636  CD1 LEU B  57     -35.956  -6.500  -9.041  1.00 22.07           C  
ANISOU 3636  CD1 LEU B  57     3410   2696   2281   -286    359    -66       C  
ATOM   3637  CD2 LEU B  57     -36.304  -8.983  -9.118  1.00 23.62           C  
ANISOU 3637  CD2 LEU B  57     3647   2900   2428   -357    344    -11       C  
ATOM   3638  N   LEU B  58     -38.947  -8.465  -4.323  1.00 28.11           N  
ANISOU 3638  N   LEU B  58     4352   3509   2819   -410    587    -64       N  
ATOM   3639  CA  LEU B  58     -38.824  -8.756  -2.900  1.00 28.26           C  
ANISOU 3639  CA  LEU B  58     4451   3521   2764   -426    611    -74       C  
ATOM   3640  C   LEU B  58     -39.817  -9.806  -2.416  1.00 33.37           C  
ANISOU 3640  C   LEU B  58     5113   4187   3378   -469    658    -51       C  
ATOM   3641  O   LEU B  58     -39.936 -10.013  -1.203  1.00 33.65           O  
ANISOU 3641  O   LEU B  58     5209   4222   3353   -484    690    -59       O  
ATOM   3642  CB  LEU B  58     -38.972  -7.479  -2.071  1.00 27.02           C  
ANISOU 3642  CB  LEU B  58     4302   3367   2599   -399    651   -111       C  
ATOM   3643  CG  LEU B  58     -37.823  -6.481  -2.201  1.00 27.32           C  
ANISOU 3643  CG  LEU B  58     4347   3382   2651   -358    604   -137       C  
ATOM   3644  CD1 LEU B  58     -37.886  -5.427  -1.104  1.00 29.50           C  
ANISOU 3644  CD1 LEU B  58     4651   3657   2901   -338    644   -174       C  
ATOM   3645  CD2 LEU B  58     -36.496  -7.200  -2.168  1.00 28.64           C  
ANISOU 3645  CD2 LEU B  58     4577   3522   2784   -362    533   -128       C  
ATOM   3646  N   SER B  59     -40.523 -10.474  -3.326  1.00 32.64           N  
ANISOU 3646  N   SER B  59     4968   4111   3323   -490    664    -25       N  
ATOM   3647  CA  SER B  59     -41.426 -11.538  -2.915  1.00 33.37           C  
ANISOU 3647  CA  SER B  59     5075   4219   3385   -533    706     -2       C  
ATOM   3648  C   SER B  59     -40.634 -12.684  -2.299  1.00 37.54           C  
ANISOU 3648  C   SER B  59     5686   4727   3849   -558    671     15       C  
ATOM   3649  O   SER B  59     -39.474 -12.925  -2.650  1.00 36.50           O  
ANISOU 3649  O   SER B  59     5583   4573   3714   -548    605     19       O  
ATOM   3650  CB  SER B  59     -42.237 -12.046  -4.105  1.00 38.78           C  
ANISOU 3650  CB  SER B  59     5684   4924   4125   -549    712     23       C  
ATOM   3651  OG  SER B  59     -41.444 -12.875  -4.934  1.00 40.20           O  
ANISOU 3651  OG  SER B  59     5870   5089   4317   -556    646     47       O  
ATOM   3652  N   GLU B  60     -41.274 -13.395  -1.362  1.00 38.35           N  
ANISOU 3652  N   GLU B  60     5831   4839   3902   -591    718     24       N  
ATOM   3653  CA  GLU B  60     -40.587 -14.467  -0.649  1.00 39.53           C  
ANISOU 3653  CA  GLU B  60     6063   4970   3985   -615    692     39       C  
ATOM   3654  C   GLU B  60     -40.031 -15.519  -1.601  1.00 33.56           C  
ANISOU 3654  C   GLU B  60     5303   4202   3245   -631    633     70       C  
ATOM   3655  O   GLU B  60     -38.942 -16.055  -1.363  1.00 34.24           O  
ANISOU 3655  O   GLU B  60     5451   4265   3293   -633    581     76       O  
ATOM   3656  CB  GLU B  60     -41.531 -15.104   0.378  1.00 46.67           C  
ANISOU 3656  CB  GLU B  60     7002   5891   4841   -650    757     47       C  
ATOM   3657  CG  GLU B  60     -41.742 -14.236   1.611  1.00 58.35           C  
ANISOU 3657  CG  GLU B  60     8514   7373   6282   -636    804     17       C  
ATOM   3658  CD  GLU B  60     -42.720 -14.827   2.612  1.00 71.08           C  
ANISOU 3658  CD  GLU B  60    10157   9002   7848   -670    870     25       C  
ATOM   3659  OE1 GLU B  60     -43.691 -15.489   2.186  1.00 74.79           O  
ANISOU 3659  OE1 GLU B  60    10588   9489   8338   -699    902     47       O  
ATOM   3660  OE2 GLU B  60     -42.517 -14.622   3.829  1.00 72.40           O  
ANISOU 3660  OE2 GLU B  60    10386   9164   7958   -667    891      9       O  
ATOM   3661  N   ALA B  61     -40.737 -15.799  -2.698  1.00 31.52           N  
ANISOU 3661  N   ALA B  61     4973   3960   3042   -642    638     88       N  
ATOM   3662  CA  ALA B  61     -40.291 -16.831  -3.629  1.00 33.38           C  
ANISOU 3662  CA  ALA B  61     5201   4187   3294   -658    585    117       C  
ATOM   3663  C   ALA B  61     -38.960 -16.492  -4.303  1.00 34.66           C  
ANISOU 3663  C   ALA B  61     5368   4326   3477   -628    507    112       C  
ATOM   3664  O   ALA B  61     -38.210 -17.402  -4.672  1.00 32.82           O  
ANISOU 3664  O   ALA B  61     5162   4075   3232   -640    454    133       O  
ATOM   3665  CB  ALA B  61     -41.360 -17.069  -4.693  1.00 34.67           C  
ANISOU 3665  CB  ALA B  61     5280   4375   3518   -673    609    134       C  
ATOM   3666  N   VAL B  62     -38.640 -15.211  -4.479  1.00 33.18           N  
ANISOU 3666  N   VAL B  62     5152   4135   3319   -588    499     85       N  
ATOM   3667  CA  VAL B  62     -37.507 -14.836  -5.317  1.00 28.88           C  
ANISOU 3667  CA  VAL B  62     4595   3571   2806   -558    428     81       C  
ATOM   3668  C   VAL B  62     -36.473 -13.976  -4.603  1.00 27.77           C  
ANISOU 3668  C   VAL B  62     4505   3409   2636   -526    403     51       C  
ATOM   3669  O   VAL B  62     -35.334 -13.885  -5.086  1.00 23.52           O  
ANISOU 3669  O   VAL B  62     3980   2850   2108   -506    338     50       O  
ATOM   3670  CB  VAL B  62     -37.984 -14.123  -6.602  1.00 31.52           C  
ANISOU 3670  CB  VAL B  62     4833   3920   3222   -536    428     79       C  
ATOM   3671  CG1 VAL B  62     -39.068 -14.942  -7.311  1.00 32.82           C  
ANISOU 3671  CG1 VAL B  62     4945   4109   3418   -567    455    106       C  
ATOM   3672  CG2 VAL B  62     -38.471 -12.702  -6.290  1.00 25.74           C  
ANISOU 3672  CG2 VAL B  62     4068   3200   2513   -506    473     47       C  
ATOM   3673  N   ARG B  63     -36.798 -13.344  -3.475  1.00 28.74           N  
ANISOU 3673  N   ARG B  63     4658   3537   2724   -520    452     27       N  
ATOM   3674  CA  ARG B  63     -35.952 -12.255  -2.997  1.00 28.61           C  
ANISOU 3674  CA  ARG B  63     4668   3505   2697   -484    433     -6       C  
ATOM   3675  C   ARG B  63     -34.548 -12.724  -2.632  1.00 29.67           C  
ANISOU 3675  C   ARG B  63     4878   3611   2785   -481    369     -5       C  
ATOM   3676  O   ARG B  63     -33.589 -11.959  -2.777  1.00 27.03           O  
ANISOU 3676  O   ARG B  63     4550   3259   2462   -448    327    -25       O  
ATOM   3677  CB  ARG B  63     -36.614 -11.545  -1.820  1.00 31.90           C  
ANISOU 3677  CB  ARG B  63     5104   3934   3084   -480    500    -31       C  
ATOM   3678  CG  ARG B  63     -36.696 -12.325  -0.543  1.00 35.93           C  
ANISOU 3678  CG  ARG B  63     5693   4443   3517   -509    526    -26       C  
ATOM   3679  CD  ARG B  63     -37.261 -11.426   0.543  1.00 44.27           C  
ANISOU 3679  CD  ARG B  63     6762   5510   4548   -499    587    -56       C  
ATOM   3680  NE  ARG B  63     -37.954 -12.192   1.569  1.00 56.99           N  
ANISOU 3680  NE  ARG B  63     8418   7132   6103   -533    638    -45       N  
ATOM   3681  CZ  ARG B  63     -38.984 -11.737   2.271  1.00 63.62           C  
ANISOU 3681  CZ  ARG B  63     9247   7992   6933   -538    708    -58       C  
ATOM   3682  NH1 ARG B  63     -39.483 -10.527   2.061  1.00 59.32           N  
ANISOU 3682  NH1 ARG B  63     8648   7459   6432   -511    739    -83       N  
ATOM   3683  NH2 ARG B  63     -39.531 -12.518   3.198  1.00 62.04           N  
ANISOU 3683  NH2 ARG B  63     9093   7800   6679   -570    749    -47       N  
ATOM   3684  N   ASP B  64     -34.390 -13.971  -2.192  1.00 28.13           N  
ANISOU 3684  N   ASP B  64     4739   3409   2539   -514    360     19       N  
ATOM   3685  CA  ASP B  64     -33.065 -14.485  -1.867  1.00 29.42           C  
ANISOU 3685  CA  ASP B  64     4974   3546   2657   -512    298     22       C  
ATOM   3686  C   ASP B  64     -32.452 -15.332  -2.978  1.00 30.60           C  
ANISOU 3686  C   ASP B  64     5110   3685   2833   -520    234     50       C  
ATOM   3687  O   ASP B  64     -31.358 -15.875  -2.791  1.00 30.02           O  
ANISOU 3687  O   ASP B  64     5095   3590   2723   -521    180     57       O  
ATOM   3688  CB  ASP B  64     -33.118 -15.285  -0.566  1.00 34.87           C  
ANISOU 3688  CB  ASP B  64     5745   4235   3268   -540    324     28       C  
ATOM   3689  CG  ASP B  64     -33.328 -14.397   0.645  1.00 40.57           C  
ANISOU 3689  CG  ASP B  64     6498   4962   3954   -526    371     -4       C  
ATOM   3690  OD1 ASP B  64     -32.716 -13.298   0.705  1.00 38.08           O  
ANISOU 3690  OD1 ASP B  64     6180   4638   3652   -490    353    -34       O  
ATOM   3691  OD2 ASP B  64     -34.119 -14.796   1.524  1.00 44.60           O  
ANISOU 3691  OD2 ASP B  64     7035   5486   4424   -550    426      0       O  
ATOM   3692  N   LYS B  65     -33.115 -15.436  -4.128  1.00 25.61           N  
ANISOU 3692  N   LYS B  65     4401   3066   2262   -525    238     67       N  
ATOM   3693  CA  LYS B  65     -32.577 -16.162  -5.268  1.00 26.03           C  
ANISOU 3693  CA  LYS B  65     4433   3110   2346   -530    178     92       C  
ATOM   3694  C   LYS B  65     -31.532 -15.327  -5.999  1.00 27.39           C  
ANISOU 3694  C   LYS B  65     4584   3266   2556   -491    118     77       C  
ATOM   3695  O   LYS B  65     -31.722 -14.131  -6.231  1.00 24.64           O  
ANISOU 3695  O   LYS B  65     4190   2923   2248   -460    134     53       O  
ATOM   3696  CB  LYS B  65     -33.697 -16.525  -6.241  1.00 26.03           C  
ANISOU 3696  CB  LYS B  65     4357   3134   2401   -549    206    114       C  
ATOM   3697  CG  LYS B  65     -34.231 -17.948  -6.134  1.00 32.20           C  
ANISOU 3697  CG  LYS B  65     5159   3922   3155   -594    221    146       C  
ATOM   3698  CD  LYS B  65     -34.915 -18.186  -4.823  1.00 36.54           C  
ANISOU 3698  CD  LYS B  65     5757   4480   3647   -617    283    142       C  
ATOM   3699  CE  LYS B  65     -35.512 -19.576  -4.768  1.00 34.46           C  
ANISOU 3699  CE  LYS B  65     5509   4224   3361   -662    302    174       C  
ATOM   3700  NZ  LYS B  65     -36.330 -19.722  -3.533  1.00 40.49           N  
ANISOU 3700  NZ  LYS B  65     6310   5000   4076   -684    371    170       N  
ATOM   3701  N   GLU B  66     -30.428 -15.969  -6.374  1.00 23.79           N  
ANISOU 3701  N   GLU B  66     4162   2788   2088   -491     50     91       N  
ATOM   3702  CA  GLU B  66     -29.474 -15.330  -7.264  1.00 22.74           C  
ANISOU 3702  CA  GLU B  66     4001   2640   1998   -457    -11     81       C  
ATOM   3703  C   GLU B  66     -30.163 -14.999  -8.579  1.00 24.28           C  
ANISOU 3703  C   GLU B  66     4101   2853   2273   -449     -5     90       C  
ATOM   3704  O   GLU B  66     -30.972 -15.782  -9.090  1.00 23.67           O  
ANISOU 3704  O   GLU B  66     3990   2791   2214   -476     14    116       O  
ATOM   3705  CB  GLU B  66     -28.269 -16.240  -7.488  1.00 26.16           C  
ANISOU 3705  CB  GLU B  66     4485   3050   2405   -464    -84     99       C  
ATOM   3706  CG  GLU B  66     -27.448 -16.453  -6.221  1.00 30.35           C  
ANISOU 3706  CG  GLU B  66     5110   3563   2859   -466    -96     88       C  
ATOM   3707  CD  GLU B  66     -26.246 -17.355  -6.432  1.00 35.96           C  
ANISOU 3707  CD  GLU B  66     5871   4250   3542   -472   -168    106       C  
ATOM   3708  OE1 GLU B  66     -26.196 -18.073  -7.446  1.00 39.09           O  
ANISOU 3708  OE1 GLU B  66     6236   4646   3970   -484   -201    132       O  
ATOM   3709  OE2 GLU B  66     -25.341 -17.347  -5.581  1.00 37.04           O  
ANISOU 3709  OE2 GLU B  66     6079   4370   3625   -465   -192     93       O  
ATOM   3710  N   VAL B  67     -29.870 -13.821  -9.124  1.00 21.62           N  
ANISOU 3710  N   VAL B  67     3718   2512   1983   -410    -19     69       N  
ATOM   3711  CA  VAL B  67     -30.703 -13.247 -10.174  1.00 20.64           C  
ANISOU 3711  CA  VAL B  67     3501   2408   1932   -398      2     71       C  
ATOM   3712  C   VAL B  67     -29.942 -13.184 -11.494  1.00 21.21           C  
ANISOU 3712  C   VAL B  67     3532   2470   2057   -377    -64     81       C  
ATOM   3713  O   VAL B  67     -28.747 -12.863 -11.541  1.00 21.22           O  
ANISOU 3713  O   VAL B  67     3564   2448   2052   -354   -119     70       O  
ATOM   3714  CB  VAL B  67     -31.251 -11.860  -9.779  1.00 18.89           C  
ANISOU 3714  CB  VAL B  67     3249   2197   1730   -370     54     39       C  
ATOM   3715  CG1 VAL B  67     -30.134 -10.811  -9.730  1.00 19.39           C  
ANISOU 3715  CG1 VAL B  67     3327   2239   1801   -330     13     11       C  
ATOM   3716  CG2 VAL B  67     -32.332 -11.452 -10.747  1.00 21.51           C  
ANISOU 3716  CG2 VAL B  67     3488   2555   2131   -365     88     45       C  
ATOM   3717  N   VAL B  68     -30.646 -13.530 -12.563  1.00 20.82           N  
ANISOU 3717  N   VAL B  68     3414   2437   2058   -387    -59    102       N  
ATOM   3718  CA  VAL B  68     -30.213 -13.324 -13.936  1.00 19.48           C  
ANISOU 3718  CA  VAL B  68     3185   2265   1950   -365   -110    111       C  
ATOM   3719  C   VAL B  68     -31.085 -12.223 -14.516  1.00 19.12           C  
ANISOU 3719  C   VAL B  68     3057   2241   1968   -340    -68     97       C  
ATOM   3720  O   VAL B  68     -32.317 -12.297 -14.441  1.00 19.07           O  
ANISOU 3720  O   VAL B  68     3014   2260   1971   -357     -9    102       O  
ATOM   3721  CB  VAL B  68     -30.343 -14.620 -14.757  1.00 22.57           C  
ANISOU 3721  CB  VAL B  68     3562   2662   2353   -395   -137    147       C  
ATOM   3722  CG1 VAL B  68     -30.049 -14.346 -16.236  1.00 19.61           C  
ANISOU 3722  CG1 VAL B  68     3116   2288   2048   -371   -183    156       C  
ATOM   3723  CG2 VAL B  68     -29.431 -15.719 -14.182  1.00 22.22           C  
ANISOU 3723  CG2 VAL B  68     3602   2595   2246   -418   -180    161       C  
ATOM   3724  N   ALA B  69     -30.458 -11.196 -15.077  1.00 17.98           N  
ANISOU 3724  N   ALA B  69     2881   2086   1863   -300    -99     80       N  
ATOM   3725  CA  ALA B  69     -31.183 -10.029 -15.571  1.00 19.35           C  
ANISOU 3725  CA  ALA B  69     2980   2277   2094   -272    -61     65       C  
ATOM   3726  C   ALA B  69     -30.828  -9.840 -17.034  1.00 16.57           C  
ANISOU 3726  C   ALA B  69     2563   1925   1808   -250   -109     76       C  
ATOM   3727  O   ALA B  69     -29.677  -9.523 -17.368  1.00 17.91           O  
ANISOU 3727  O   ALA B  69     2747   2071   1986   -225   -167     70       O  
ATOM   3728  CB  ALA B  69     -30.856  -8.782 -14.747  1.00 16.44           C  
ANISOU 3728  CB  ALA B  69     2636   1898   1714   -242    -42     29       C  
ATOM   3729  N   VAL B  70     -31.813 -10.039 -17.898  1.00 17.09           N  
ANISOU 3729  N   VAL B  70     2556   2016   1920   -258    -85     94       N  
ATOM   3730  CA  VAL B  70     -31.654  -9.898 -19.337  1.00 17.46           C  
ANISOU 3730  CA  VAL B  70     2533   2068   2033   -238   -123    107       C  
ATOM   3731  C   VAL B  70     -32.327  -8.605 -19.760  1.00 16.52           C  
ANISOU 3731  C   VAL B  70     2341   1965   1969   -204    -84     89       C  
ATOM   3732  O   VAL B  70     -33.510  -8.386 -19.473  1.00 19.29           O  
ANISOU 3732  O   VAL B  70     2662   2342   2327   -214    -19     85       O  
ATOM   3733  CB  VAL B  70     -32.249 -11.094 -20.100  1.00 15.82           C  
ANISOU 3733  CB  VAL B  70     2293   1879   1840   -270   -128    140       C  
ATOM   3734  CG1 VAL B  70     -31.854 -11.007 -21.547  1.00 19.95           C  
ANISOU 3734  CG1 VAL B  70     2754   2402   2423   -249   -179    153       C  
ATOM   3735  CG2 VAL B  70     -31.762 -12.390 -19.491  1.00 21.64           C  
ANISOU 3735  CG2 VAL B  70     3106   2601   2515   -307   -154    157       C  
ATOM   3736  N   SER B  71     -31.571  -7.757 -20.437  1.00 16.48           N  
ANISOU 3736  N   SER B  71     2277   1971   2013    -55    179    -56       N  
ATOM   3737  CA  SER B  71     -32.026  -6.468 -20.920  1.00 16.49           C  
ANISOU 3737  CA  SER B  71     2233   1989   2043    -51    183    -66       C  
ATOM   3738  C   SER B  71     -31.809  -6.395 -22.430  1.00 15.63           C  
ANISOU 3738  C   SER B  71     2091   1888   1958    -42    162    -63       C  
ATOM   3739  O   SER B  71     -30.946  -7.078 -22.984  1.00 15.19           O  
ANISOU 3739  O   SER B  71     2046   1830   1894    -31    140    -56       O  
ATOM   3740  CB  SER B  71     -31.266  -5.343 -20.206  1.00 16.43           C  
ANISOU 3740  CB  SER B  71     2230   1986   2028    -36    174    -71       C  
ATOM   3741  OG  SER B  71     -31.470  -4.084 -20.811  1.00 17.26           O  
ANISOU 3741  OG  SER B  71     2295   2102   2161    -29    170    -79       O  
ATOM   3742  N   VAL B  72     -32.595  -5.556 -23.098  1.00 12.72           N  
ANISOU 3742  N   VAL B  72     1683   1532   1619    -44    167    -70       N  
ATOM   3743  CA  VAL B  72     -32.353  -5.191 -24.488  1.00 12.55           C  
ANISOU 3743  CA  VAL B  72     1630   1520   1617    -35    145    -66       C  
ATOM   3744  C   VAL B  72     -32.349  -3.670 -24.554  1.00 13.79           C  
ANISOU 3744  C   VAL B  72     1762   1684   1792    -24    140    -71       C  
ATOM   3745  O   VAL B  72     -33.168  -3.010 -23.903  1.00 14.15           O  
ANISOU 3745  O   VAL B  72     1799   1729   1848    -28    159    -81       O  
ATOM   3746  CB  VAL B  72     -33.406  -5.807 -25.444  1.00 15.39           C  
ANISOU 3746  CB  VAL B  72     1970   1883   1994    -49    151    -68       C  
ATOM   3747  CG1 VAL B  72     -34.791  -5.231 -25.173  1.00 17.64           C  
ANISOU 3747  CG1 VAL B  72     2228   2174   2301    -60    173    -78       C  
ATOM   3748  CG2 VAL B  72     -33.025  -5.571 -26.898  1.00 12.51           C  
ANISOU 3748  CG2 VAL B  72     1582   1529   1642    -39    126    -62       C  
ATOM   3749  N   ALA B  73     -31.394  -3.109 -25.293  1.00 14.87           N  
ANISOU 3749  N   ALA B  73     1890   1827   1933    -12    116    -64       N  
ATOM   3750  CA  ALA B  73     -31.225  -1.663 -25.316  1.00 13.45           C  
ANISOU 3750  CA  ALA B  73     1694   1650   1768     -4    109    -67       C  
ATOM   3751  C   ALA B  73     -30.628  -1.259 -26.654  1.00 12.93           C  
ANISOU 3751  C   ALA B  73     1610   1593   1711      1     85    -57       C  
ATOM   3752  O   ALA B  73     -29.998  -2.066 -27.341  1.00 14.13           O  
ANISOU 3752  O   ALA B  73     1765   1751   1851      2     75    -50       O  
ATOM   3753  CB  ALA B  73     -30.343  -1.176 -24.147  1.00 11.36           C  
ANISOU 3753  CB  ALA B  73     1452   1379   1485      2    107    -71       C  
ATOM   3754  N   GLY B  74     -30.845  -0.007 -27.033  1.00 14.73           N  
ANISOU 3754  N   GLY B  74     1819   1819   1958      5     78    -56       N  
ATOM   3755  CA  GLY B  74     -30.303   0.497 -28.279  1.00 13.45           C  
ANISOU 3755  CA  GLY B  74     1644   1665   1803      6     57    -44       C  
ATOM   3756  C   GLY B  74     -31.272   1.464 -28.921  1.00 15.33           C  
ANISOU 3756  C   GLY B  74     1860   1898   2066      9     52    -42       C  
ATOM   3757  O   GLY B  74     -32.242   1.893 -28.298  1.00 12.82           O  
ANISOU 3757  O   GLY B  74     1535   1571   1764     12     64    -53       O  
ATOM   3758  N   ALA B  75     -31.001   1.802 -30.185  1.00 12.65           N  
ANISOU 3758  N   ALA B  75     1510   1565   1730      8     33    -29       N  
ATOM   3759  CA  ALA B  75     -31.746   2.867 -30.852  1.00 14.96           C  
ANISOU 3759  CA  ALA B  75     1788   1852   2046     12     21    -24       C  
ATOM   3760  C   ALA B  75     -33.245   2.578 -30.835  1.00 13.89           C  
ANISOU 3760  C   ALA B  75     1633   1715   1929     16     29    -33       C  
ATOM   3761  O   ALA B  75     -33.680   1.422 -30.856  1.00 11.71           O  
ANISOU 3761  O   ALA B  75     1354   1448   1647      9     40    -39       O  
ATOM   3762  CB  ALA B  75     -31.257   3.053 -32.294  1.00 15.51           C  
ANISOU 3762  CB  ALA B  75     1853   1930   2109      7      0     -6       C  
ATOM   3763  N   PHE B  76     -34.041   3.643 -30.795  1.00 12.01           N  
ANISOU 3763  N   PHE B  76     1382   1466   1717     27     24    -37       N  
ATOM   3764  CA  PHE B  76     -35.469   3.438 -30.658  1.00 14.23           C  
ANISOU 3764  CA  PHE B  76     1639   1748   2018     32     34    -50       C  
ATOM   3765  C   PHE B  76     -36.084   2.956 -31.967  1.00 12.59           C  
ANISOU 3765  C   PHE B  76     1413   1553   1816     29     16    -41       C  
ATOM   3766  O   PHE B  76     -35.514   3.106 -33.054  1.00 14.10           O  
ANISOU 3766  O   PHE B  76     1610   1748   1998     26     -6    -24       O  
ATOM   3767  CB  PHE B  76     -36.168   4.703 -30.138  1.00 11.21           C  
ANISOU 3767  CB  PHE B  76     1246   1349   1663     50     34    -60       C  
ATOM   3768  CG  PHE B  76     -36.495   5.751 -31.198  1.00 11.90           C  
ANISOU 3768  CG  PHE B  76     1322   1427   1771     63      4    -48       C  
ATOM   3769  CD1 PHE B  76     -35.494   6.490 -31.817  1.00 12.76           C  
ANISOU 3769  CD1 PHE B  76     1451   1526   1870     61    -18    -28       C  
ATOM   3770  CD2 PHE B  76     -37.823   6.075 -31.475  1.00 12.69           C  
ANISOU 3770  CD2 PHE B  76     1393   1528   1901     79     -3    -57       C  
ATOM   3771  CE1 PHE B  76     -35.817   7.494 -32.761  1.00 14.97           C  
ANISOU 3771  CE1 PHE B  76     1728   1794   2167     72    -47    -14       C  
ATOM   3772  CE2 PHE B  76     -38.152   7.072 -32.411  1.00 15.59           C  
ANISOU 3772  CE2 PHE B  76     1753   1883   2287     95    -36    -44       C  
ATOM   3773  CZ  PHE B  76     -37.150   7.776 -33.055  1.00 14.26           C  
ANISOU 3773  CZ  PHE B  76     1611   1701   2105     91    -58    -22       C  
ATOM   3774  N   ARG B  77     -37.247   2.317 -31.831  1.00 13.87           N  
ANISOU 3774  N   ARG B  77     1554   1724   1993     26     28    -55       N  
ATOM   3775  CA  ARG B  77     -38.072   1.901 -32.958  1.00 12.77           C  
ANISOU 3775  CA  ARG B  77     1392   1597   1864     23     10    -52       C  
ATOM   3776  C   ARG B  77     -37.443   0.751 -33.749  1.00 15.20           C  
ANISOU 3776  C   ARG B  77     1715   1917   2145      7      4    -42       C  
ATOM   3777  O   ARG B  77     -37.639   0.656 -34.963  1.00 16.20           O  
ANISOU 3777  O   ARG B  77     1834   2052   2271      5    -20    -33       O  
ATOM   3778  CB  ARG B  77     -38.356   3.095 -33.885  1.00 13.60           C  
ANISOU 3778  CB  ARG B  77     1485   1695   1986     40    -22    -40       C  
ATOM   3779  CG  ARG B  77     -39.828   3.378 -34.166  1.00 18.98           C  
ANISOU 3779  CG  ARG B  77     2130   2382   2701     53    -33    -51       C  
ATOM   3780  CD  ARG B  77     -40.538   4.013 -32.966  1.00 15.05           C  
ANISOU 3780  CD  ARG B  77     1614   1875   2229     68    -11    -72       C  
ATOM   3781  NE  ARG B  77     -40.828   3.030 -31.927  1.00 11.83           N  
ANISOU 3781  NE  ARG B  77     1202   1477   1815     51     27    -90       N  
ATOM   3782  CZ  ARG B  77     -41.721   2.056 -32.040  1.00 14.93           C  
ANISOU 3782  CZ  ARG B  77     1571   1887   2215     37     37   -102       C  
ATOM   3783  NH1 ARG B  77     -42.479   1.935 -33.119  1.00 13.38           N  
ANISOU 3783  NH1 ARG B  77     1347   1702   2033     38     11    -99       N  
ATOM   3784  NH2 ARG B  77     -41.847   1.171 -31.047  1.00 11.60           N  
ANISOU 3784  NH2 ARG B  77     1154   1471   1782     18     73   -115       N  
ATOM   3785  N   LYS B  78     -36.689  -0.140 -33.084  1.00 13.94           N  
ANISOU 3785  N   LYS B  78     1578   1757   1963     -4     24    -45       N  
ATOM   3786  CA  LYS B  78     -35.906  -1.154 -33.791  1.00 14.28           C  
ANISOU 3786  CA  LYS B  78     1638   1807   1979    -15     17    -38       C  
ATOM   3787  C   LYS B  78     -36.296  -2.583 -33.413  1.00 13.31           C  
ANISOU 3787  C   LYS B  78     1522   1687   1850    -30     35    -50       C  
ATOM   3788  O   LYS B  78     -35.528  -3.515 -33.680  1.00 15.08           O  
ANISOU 3788  O   LYS B  78     1767   1912   2051    -36     35    -47       O  
ATOM   3789  CB  LYS B  78     -34.402  -0.952 -33.546  1.00 15.02           C  
ANISOU 3789  CB  LYS B  78     1758   1898   2052    -11     18    -30       C  
ATOM   3790  CG  LYS B  78     -33.827   0.354 -34.051  1.00 14.63           C  
ANISOU 3790  CG  LYS B  78     1708   1846   2005     -3      0    -16       C  
ATOM   3791  CD  LYS B  78     -34.229   0.628 -35.495  1.00 15.57           C  
ANISOU 3791  CD  LYS B  78     1816   1974   2127     -3    -25     -4       C  
ATOM   3792  CE  LYS B  78     -33.441   1.815 -36.078  1.00 20.63           C  
ANISOU 3792  CE  LYS B  78     2464   2610   2763      0    -42     13       C  
ATOM   3793  NZ  LYS B  78     -34.145   2.409 -37.271  1.00 18.04           N  
ANISOU 3793  NZ  LYS B  78     2126   2284   2443      2    -69     26       N  
ATOM   3794  N   GLY B  79     -37.466  -2.792 -32.816  1.00 13.36           N  
ANISOU 3794  N   GLY B  79     1510   1693   1874    -37     51    -63       N  
ATOM   3795  CA  GLY B  79     -37.904  -4.142 -32.512  1.00 14.76           C  
ANISOU 3795  CA  GLY B  79     1695   1869   2044    -58     68    -72       C  
ATOM   3796  C   GLY B  79     -37.442  -4.727 -31.190  1.00 14.64           C  
ANISOU 3796  C   GLY B  79     1708   1842   2011    -64     95    -75       C  
ATOM   3797  O   GLY B  79     -37.505  -5.952 -31.020  1.00 14.72           O  
ANISOU 3797  O   GLY B  79     1737   1848   2009    -81    105    -78       O  
ATOM   3798  N   LYS B  80     -37.008  -3.895 -30.241  1.00 12.51           N  
ANISOU 3798  N   LYS B  80     1447   1567   1741    -52    105    -75       N  
ATOM   3799  CA  LYS B  80     -36.554  -4.403 -28.948  1.00 15.20           C  
ANISOU 3799  CA  LYS B  80     1817   1896   2061    -57    128    -78       C  
ATOM   3800  C   LYS B  80     -37.687  -5.063 -28.173  1.00 15.01           C  
ANISOU 3800  C   LYS B  80     1789   1871   2042    -78    157    -90       C  
ATOM   3801  O   LYS B  80     -37.544  -6.196 -27.704  1.00 13.02           O  
ANISOU 3801  O   LYS B  80     1565   1610   1771    -94    170    -89       O  
ATOM   3802  CB  LYS B  80     -35.936  -3.279 -28.113  1.00 11.70           C  
ANISOU 3802  CB  LYS B  80     1382   1448   1616    -41    131    -78       C  
ATOM   3803  CG  LYS B  80     -34.669  -2.670 -28.708  1.00 11.25           C  
ANISOU 3803  CG  LYS B  80     1333   1392   1551    -26    106    -66       C  
ATOM   3804  CD  LYS B  80     -34.050  -1.590 -27.767  1.00 10.69           C  
ANISOU 3804  CD  LYS B  80     1272   1313   1477    -15    108    -68       C  
ATOM   3805  CE  LYS B  80     -34.999  -0.401 -27.541  1.00 11.72           C  
ANISOU 3805  CE  LYS B  80     1378   1442   1634     -7    114    -77       C  
ATOM   3806  NZ  LYS B  80     -35.423   0.193 -28.829  1.00 11.11           N  
ANISOU 3806  NZ  LYS B  80     1274   1370   1579     -1     92    -70       N  
ATOM   3807  N   SER B  81     -38.811  -4.356 -27.996  1.00 13.90           N  
ANISOU 3807  N   SER B  81     1614   1740   1928    -79    168   -102       N  
ATOM   3808  CA  SER B  81     -39.927  -4.922 -27.236  1.00 14.16           C  
ANISOU 3808  CA  SER B  81     1637   1776   1967   -102    200   -115       C  
ATOM   3809  C   SER B  81     -40.473  -6.170 -27.924  1.00 14.79           C  
ANISOU 3809  C   SER B  81     1713   1859   2047   -127    198   -115       C  
ATOM   3810  O   SER B  81     -40.765  -7.181 -27.272  1.00 13.35           O  
ANISOU 3810  O   SER B  81     1552   1670   1852   -153    222   -118       O  
ATOM   3811  CB  SER B  81     -41.034  -3.871 -27.061  1.00 11.95           C  
ANISOU 3811  CB  SER B  81     1312   1509   1719    -93    211   -131       C  
ATOM   3812  OG  SER B  81     -40.554  -2.736 -26.365  1.00 12.98           O  
ANISOU 3812  OG  SER B  81     1449   1633   1848    -70    214   -134       O  
ATOM   3813  N   PHE B  82     -40.611  -6.103 -29.245  1.00 12.60           N  
ANISOU 3813  N   PHE B  82     1414   1589   1783   -122    169   -112       N  
ATOM   3814  CA  PHE B  82     -40.990  -7.250 -30.064  1.00 13.70           C  
ANISOU 3814  CA  PHE B  82     1553   1730   1922   -144    160   -112       C  
ATOM   3815  C   PHE B  82     -40.116  -8.466 -29.760  1.00 15.22           C  
ANISOU 3815  C   PHE B  82     1797   1904   2082   -156    165   -104       C  
ATOM   3816  O   PHE B  82     -40.615  -9.573 -29.547  1.00 14.91           O  
ANISOU 3816  O   PHE B  82     1770   1857   2038   -184    180   -109       O  
ATOM   3817  CB  PHE B  82     -40.866  -6.816 -31.524  1.00 13.42           C  
ANISOU 3817  CB  PHE B  82     1499   1705   1896   -129    123   -107       C  
ATOM   3818  CG  PHE B  82     -41.145  -7.881 -32.540  1.00 13.94           C  
ANISOU 3818  CG  PHE B  82     1566   1773   1958   -148    107   -109       C  
ATOM   3819  CD1 PHE B  82     -40.116  -8.656 -33.051  1.00 17.00           C  
ANISOU 3819  CD1 PHE B  82     1915   2175   2370   -165    102   -121       C  
ATOM   3820  CD2 PHE B  82     -42.413  -8.029 -33.064  1.00 14.68           C  
ANISOU 3820  CD2 PHE B  82     1696   1855   2025   -146     94   -101       C  
ATOM   3821  CE1 PHE B  82     -40.364  -9.617 -34.014  1.00 15.08           C  
ANISOU 3821  CE1 PHE B  82     1673   1933   2123   -184     85   -124       C  
ATOM   3822  CE2 PHE B  82     -42.680  -8.985 -34.038  1.00 15.86           C  
ANISOU 3822  CE2 PHE B  82     1850   2005   2171   -163     79   -105       C  
ATOM   3823  CZ  PHE B  82     -41.654  -9.776 -34.519  1.00 18.41           C  
ANISOU 3823  CZ  PHE B  82     2137   2341   2516   -183     74   -117       C  
ATOM   3824  N   LEU B  83     -38.796  -8.270 -29.738  1.00 16.99           N  
ANISOU 3824  N   LEU B  83     2050   2118   2286   -134    152    -93       N  
ATOM   3825  CA  LEU B  83     -37.885  -9.369 -29.437  1.00 15.27           C  
ANISOU 3825  CA  LEU B  83     1880   1882   2039   -137    153    -86       C  
ATOM   3826  C   LEU B  83     -38.102  -9.899 -28.027  1.00 15.48           C  
ANISOU 3826  C   LEU B  83     1934   1894   2052   -155    184    -87       C  
ATOM   3827  O   LEU B  83     -38.117 -11.116 -27.803  1.00 14.11           O  
ANISOU 3827  O   LEU B  83     1794   1705   1864   -174    191    -85       O  
ATOM   3828  CB  LEU B  83     -36.447  -8.899 -29.618  1.00 14.45           C  
ANISOU 3828  CB  LEU B  83     1793   1776   1920   -108    133    -77       C  
ATOM   3829  CG  LEU B  83     -35.390  -9.835 -29.048  1.00 14.09           C  
ANISOU 3829  CG  LEU B  83     1794   1712   1846   -103    134    -71       C  
ATOM   3830  CD1 LEU B  83     -35.301 -11.076 -29.922  1.00 15.15           C  
ANISOU 3830  CD1 LEU B  83     1946   1838   1973   -111    122    -72       C  
ATOM   3831  CD2 LEU B  83     -34.049  -9.097 -28.940  1.00 11.66           C  
ANISOU 3831  CD2 LEU B  83     1494   1409   1528    -75    119    -64       C  
ATOM   3832  N   MET B  84     -38.291  -9.001 -27.062  1.00 13.93           N  
ANISOU 3832  N   MET B  84     1729   1703   1859   -149    202    -90       N  
ATOM   3833  CA  MET B  84     -38.471  -9.448 -25.686  1.00 17.63           C  
ANISOU 3833  CA  MET B  84     2228   2162   2310   -166    232    -91       C  
ATOM   3834  C   MET B  84     -39.716 -10.295 -25.528  1.00 16.77           C  
ANISOU 3834  C   MET B  84     2112   2052   2208   -204    258    -98       C  
ATOM   3835  O   MET B  84     -39.749 -11.197 -24.683  1.00 17.35           O  
ANISOU 3835  O   MET B  84     2224   2109   2259   -227    278    -94       O  
ATOM   3836  CB  MET B  84     -38.538  -8.254 -24.747  1.00 13.68           C  
ANISOU 3836  CB  MET B  84     1717   1670   1812   -153    248    -97       C  
ATOM   3837  CG  MET B  84     -37.257  -7.481 -24.730  1.00 20.43           C  
ANISOU 3837  CG  MET B  84     2585   2522   2657   -122    226    -89       C  
ATOM   3838  SD  MET B  84     -36.331  -7.629 -23.195  1.00 45.12           S  
ANISOU 3838  SD  MET B  84     5764   5633   5746   -118    237    -84       S  
ATOM   3839  CE  MET B  84     -36.646  -9.336 -22.730  1.00 17.93           C  
ANISOU 3839  CE  MET B  84     2364   2171   2278   -149    254    -77       C  
ATOM   3840  N   ASP B  85     -40.744 -10.027 -26.330  1.00 14.63           N  
ANISOU 3840  N   ASP B  85     1792   1799   1968   -213    255   -109       N  
ATOM   3841  CA  ASP B  85     -41.965 -10.810 -26.226  1.00 15.98           C  
ANISOU 3841  CA  ASP B  85     1948   1974   2148   -253    279   -119       C  
ATOM   3842  C   ASP B  85     -41.772 -12.224 -26.771  1.00 16.46           C  
ANISOU 3842  C   ASP B  85     2043   2015   2196   -275    268   -112       C  
ATOM   3843  O   ASP B  85     -42.397 -13.167 -26.278  1.00 15.05           O  
ANISOU 3843  O   ASP B  85     1881   1826   2010   -313    292   -114       O  
ATOM   3844  CB  ASP B  85     -43.095 -10.068 -26.935  1.00 16.65           C  
ANISOU 3844  CB  ASP B  85     1968   2087   2273   -253    275   -134       C  
ATOM   3845  CG  ASP B  85     -43.535  -8.829 -26.169  1.00 17.31           C  
ANISOU 3845  CG  ASP B  85     2020   2187   2371   -237    296   -145       C  
ATOM   3846  OD1 ASP B  85     -43.052  -8.627 -25.028  1.00 14.34           O  
ANISOU 3846  OD1 ASP B  85     1675   1801   1973   -233    317   -142       O  
ATOM   3847  OD2 ASP B  85     -44.353  -8.055 -26.701  1.00 17.25           O  
ANISOU 3847  OD2 ASP B  85     1958   2199   2396   -227    289   -158       O  
ATOM   3848  N   PHE B  86     -40.892 -12.409 -27.753  1.00 14.53           N  
ANISOU 3848  N   PHE B  86     1812   1763   1946   -253    233   -105       N  
ATOM   3849  CA  PHE B  86     -40.528 -13.777 -28.112  1.00 18.70           C  
ANISOU 3849  CA  PHE B  86     2382   2266   2456   -269    223   -100       C  
ATOM   3850  C   PHE B  86     -39.660 -14.425 -27.042  1.00 19.34           C  
ANISOU 3850  C   PHE B  86     2524   2319   2504   -266    233    -87       C  
ATOM   3851  O   PHE B  86     -39.740 -15.645 -26.841  1.00 19.11           O  
ANISOU 3851  O   PHE B  86     2536   2264   2461   -291    239    -84       O  
ATOM   3852  CB  PHE B  86     -39.833 -13.806 -29.471  1.00 13.74           C  
ANISOU 3852  CB  PHE B  86     1750   1640   1830   -244    185   -100       C  
ATOM   3853  CG  PHE B  86     -40.793 -13.806 -30.611  1.00 18.13           C  
ANISOU 3853  CG  PHE B  86     2264   2215   2411   -260    172   -111       C  
ATOM   3854  CD1 PHE B  86     -41.540 -14.945 -30.896  1.00 15.71           C  
ANISOU 3854  CD1 PHE B  86     1966   1897   2107   -297    176   -119       C  
ATOM   3855  CD2 PHE B  86     -40.991 -12.664 -31.370  1.00 17.02           C  
ANISOU 3855  CD2 PHE B  86     2077   2100   2289   -239    154   -114       C  
ATOM   3856  CE1 PHE B  86     -42.439 -14.954 -31.938  1.00 19.72           C  
ANISOU 3856  CE1 PHE B  86     2433   2422   2636   -313    161   -131       C  
ATOM   3857  CE2 PHE B  86     -41.896 -12.667 -32.412  1.00 18.40           C  
ANISOU 3857  CE2 PHE B  86     2215   2292   2486   -252    138   -125       C  
ATOM   3858  CZ  PHE B  86     -42.622 -13.814 -32.695  1.00 19.54           C  
ANISOU 3858  CZ  PHE B  86     2364   2428   2632   -289    141   -134       C  
ATOM   3859  N   MET B  87     -38.838 -13.634 -26.343  1.00 16.76           N  
ANISOU 3859  N   MET B  87     2208   1995   2166   -238    233    -81       N  
ATOM   3860  CA  MET B  87     -38.112 -14.167 -25.195  1.00 18.98           C  
ANISOU 3860  CA  MET B  87     2545   2252   2415   -236    242    -69       C  
ATOM   3861  C   MET B  87     -39.074 -14.647 -24.119  1.00 18.25           C  
ANISOU 3861  C   MET B  87     2469   2152   2313   -277    281    -69       C  
ATOM   3862  O   MET B  87     -38.837 -15.680 -23.482  1.00 19.66           O  
ANISOU 3862  O   MET B  87     2702   2301   2466   -293    287    -58       O  
ATOM   3863  CB  MET B  87     -37.151 -13.112 -24.637  1.00 16.52           C  
ANISOU 3863  CB  MET B  87     2234   1949   2093   -200    234    -64       C  
ATOM   3864  CG  MET B  87     -36.023 -12.813 -25.625  1.00 21.41           C  
ANISOU 3864  CG  MET B  87     2846   2572   2715   -164    198    -62       C  
ATOM   3865  SD  MET B  87     -34.845 -11.542 -25.139  1.00 29.97           S  
ANISOU 3865  SD  MET B  87     3927   3669   3793   -126    185    -58       S  
ATOM   3866  CE  MET B  87     -34.373 -12.139 -23.558  1.00 26.96           C  
ANISOU 3866  CE  MET B  87     3603   3264   3375   -131    198    -49       C  
ATOM   3867  N   LEU B  88     -40.168 -13.916 -23.911  1.00 16.52           N  
ANISOU 3867  N   LEU B  88     2204   1958   2115   -293    306    -81       N  
ATOM   3868  CA  LEU B  88     -41.174 -14.337 -22.937  1.00 16.22           C  
ANISOU 3868  CA  LEU B  88     2174   1919   2070   -336    348    -84       C  
ATOM   3869  C   LEU B  88     -41.789 -15.670 -23.329  1.00 18.53           C  
ANISOU 3869  C   LEU B  88     2483   2193   2363   -378    353    -83       C  
ATOM   3870  O   LEU B  88     -42.017 -16.533 -22.472  1.00 19.90           O  
ANISOU 3870  O   LEU B  88     2702   2346   2513   -412    378    -74       O  
ATOM   3871  CB  LEU B  88     -42.263 -13.275 -22.818  1.00 17.66           C  
ANISOU 3871  CB  LEU B  88     2292   2136   2281   -342    372   -103       C  
ATOM   3872  CG  LEU B  88     -41.913 -12.005 -22.056  1.00 17.01           C  
ANISOU 3872  CG  LEU B  88     2200   2068   2195   -312    381   -107       C  
ATOM   3873  CD1 LEU B  88     -43.004 -10.961 -22.278  1.00 17.10           C  
ANISOU 3873  CD1 LEU B  88     2142   2113   2244   -310    396   -128       C  
ATOM   3874  CD2 LEU B  88     -41.756 -12.324 -20.580  1.00 17.37           C  
ANISOU 3874  CD2 LEU B  88     2296   2101   2203   -329    413   -100       C  
ATOM   3875  N   ARG B  89     -42.071 -15.854 -24.619  1.00 19.65           N  
ANISOU 3875  N   ARG B  89     2594   2342   2530   -378    329    -91       N  
ATOM   3876  CA  ARG B  89     -42.594 -17.135 -25.082  1.00 20.72           C  
ANISOU 3876  CA  ARG B  89     2748   2458   2667   -417    329    -92       C  
ATOM   3877  C   ARG B  89     -41.663 -18.266 -24.708  1.00 19.85           C  
ANISOU 3877  C   ARG B  89     2715   2304   2523   -417    319    -75       C  
ATOM   3878  O   ARG B  89     -42.108 -19.330 -24.262  1.00 20.86           O  
ANISOU 3878  O   ARG B  89     2882   2406   2637   -459    337    -69       O  
ATOM   3879  CB  ARG B  89     -42.799 -17.111 -26.590  1.00 18.95           C  
ANISOU 3879  CB  ARG B  89     2485   2247   2470   -409    297   -103       C  
ATOM   3880  CG  ARG B  89     -44.000 -16.312 -27.014  1.00 23.03           C  
ANISOU 3880  CG  ARG B  89     2926   2802   3022   -421    306   -121       C  
ATOM   3881  CD  ARG B  89     -44.381 -16.602 -28.454  1.00 20.87           C  
ANISOU 3881  CD  ARG B  89     2622   2536   2770   -426    275   -132       C  
ATOM   3882  NE  ARG B  89     -45.529 -15.792 -28.839  1.00 20.50           N  
ANISOU 3882  NE  ARG B  89     2502   2528   2759   -433    279   -149       N  
ATOM   3883  CZ  ARG B  89     -46.059 -15.791 -30.048  1.00 24.03           C  
ANISOU 3883  CZ  ARG B  89     2911   2991   3229   -437    252   -160       C  
ATOM   3884  NH1 ARG B  89     -45.575 -16.560 -31.014  1.00 19.47           N  
ANISOU 3884  NH1 ARG B  89     2361   2396   2641   -436    222   -158       N  
ATOM   3885  NH2 ARG B  89     -47.098 -14.998 -30.295  1.00 22.53           N  
ANISOU 3885  NH2 ARG B  89     2653   2836   3071   -439    254   -175       N  
ATOM   3886  N   TYR B  90     -40.361 -18.061 -24.890  1.00 18.87           N  
ANISOU 3886  N   TYR B  90     2616   2170   2385   -370    289    -66       N  
ATOM   3887  CA  TYR B  90     -39.418 -19.102 -24.525  1.00 20.09           C  
ANISOU 3887  CA  TYR B  90     2843   2283   2509   -362    275    -51       C  
ATOM   3888  C   TYR B  90     -39.383 -19.298 -23.018  1.00 19.62           C  
ANISOU 3888  C   TYR B  90     2830   2207   2419   -378    302    -37       C  
ATOM   3889  O   TYR B  90     -39.370 -20.434 -22.535  1.00 20.27           O  
ANISOU 3889  O   TYR B  90     2971   2251   2479   -403    308    -25       O  
ATOM   3890  CB  TYR B  90     -38.028 -18.762 -25.039  1.00 19.42           C  
ANISOU 3890  CB  TYR B  90     2764   2197   2418   -306    238    -49       C  
ATOM   3891  CG  TYR B  90     -37.014 -19.779 -24.616  1.00 21.71           C  
ANISOU 3891  CG  TYR B  90     3124   2445   2678   -290    221    -35       C  
ATOM   3892  CD1 TYR B  90     -36.909 -20.999 -25.282  1.00 20.92           C  
ANISOU 3892  CD1 TYR B  90     3058   2313   2577   -298    204    -37       C  
ATOM   3893  CD2 TYR B  90     -36.169 -19.540 -23.534  1.00 21.73           C  
ANISOU 3893  CD2 TYR B  90     3161   2439   2655   -267    220    -22       C  
ATOM   3894  CE1 TYR B  90     -35.985 -21.939 -24.892  1.00 22.87           C  
ANISOU 3894  CE1 TYR B  90     3370   2519   2799   -279    187    -25       C  
ATOM   3895  CE2 TYR B  90     -35.239 -20.481 -23.139  1.00 23.97           C  
ANISOU 3895  CE2 TYR B  90     3510   2685   2913   -249    200     -9       C  
ATOM   3896  CZ  TYR B  90     -35.150 -21.673 -23.823  1.00 21.71           C  
ANISOU 3896  CZ  TYR B  90     3255   2365   2627   -253    183    -11       C  
ATOM   3897  OH  TYR B  90     -34.233 -22.610 -23.431  1.00 27.64           O  
ANISOU 3897  OH  TYR B  90     4072   3076   3355   -231    161      1       O  
ATOM   3898  N   MET B  91     -39.349 -18.202 -22.260  1.00 19.76           N  
ANISOU 3898  N   MET B  91     2825   2249   2433   -364    318    -37       N  
ATOM   3899  CA  MET B  91     -39.316 -18.334 -20.809  1.00 20.70           C  
ANISOU 3899  CA  MET B  91     2990   2355   2519   -380    345    -25       C  
ATOM   3900  C   MET B  91     -40.516 -19.130 -20.302  1.00 21.46           C  
ANISOU 3900  C   MET B  91     3102   2441   2610   -442    384    -23       C  
ATOM   3901  O   MET B  91     -40.366 -20.004 -19.442  1.00 20.22           O  
ANISOU 3901  O   MET B  91     3012   2252   2419   -464    395     -6       O  
ATOM   3902  CB  MET B  91     -39.237 -16.952 -20.160  1.00 21.18           C  
ANISOU 3902  CB  MET B  91     3019   2448   2580   -358    358    -31       C  
ATOM   3903  CG  MET B  91     -37.864 -16.252 -20.375  1.00 18.71           C  
ANISOU 3903  CG  MET B  91     2706   2139   2263   -301    320    -28       C  
ATOM   3904  SD  MET B  91     -36.437 -17.316 -20.077  1.00 21.34           S  
ANISOU 3904  SD  MET B  91     3118   2429   2561   -276    285     -8       S  
ATOM   3905  CE  MET B  91     -36.565 -17.627 -18.314  1.00 20.61           C  
ANISOU 3905  CE  MET B  91     3089   2319   2423   -301    314      8       C  
ATOM   3906  N   TYR B  92     -41.705 -18.881 -20.860  1.00 19.77           N  
ANISOU 3906  N   TYR B  92     2828   2255   2428   -472    404    -41       N  
ATOM   3907  CA  TYR B  92     -42.896 -19.594 -20.408  1.00 23.50           C  
ANISOU 3907  CA  TYR B  92     3307   2724   2899   -536    444    -42       C  
ATOM   3908  C   TYR B  92     -42.986 -21.020 -20.945  1.00 25.38           C  
ANISOU 3908  C   TYR B  92     3587   2922   3133   -567    431    -35       C  
ATOM   3909  O   TYR B  92     -43.607 -21.873 -20.301  1.00 28.26           O  
ANISOU 3909  O   TYR B  92     3989   3267   3481   -620    461    -26       O  
ATOM   3910  CB  TYR B  92     -44.158 -18.822 -20.803  1.00 20.54           C  
ANISOU 3910  CB  TYR B  92     2847   2395   2564   -555    469    -66       C  
ATOM   3911  CG  TYR B  92     -44.485 -17.699 -19.851  1.00 22.49           C  
ANISOU 3911  CG  TYR B  92     3064   2675   2808   -548    502    -75       C  
ATOM   3912  CD1 TYR B  92     -44.892 -17.968 -18.544  1.00 21.39           C  
ANISOU 3912  CD1 TYR B  92     2960   2531   2637   -586    548    -69       C  
ATOM   3913  CD2 TYR B  92     -44.384 -16.371 -20.251  1.00 20.38           C  
ANISOU 3913  CD2 TYR B  92     2738   2440   2567   -505    489    -90       C  
ATOM   3914  CE1 TYR B  92     -45.190 -16.942 -17.668  1.00 25.09           C  
ANISOU 3914  CE1 TYR B  92     3402   3029   3101   -579    580    -80       C  
ATOM   3915  CE2 TYR B  92     -44.675 -15.343 -19.385  1.00 21.51           C  
ANISOU 3915  CE2 TYR B  92     2856   2609   2707   -496    519   -101       C  
ATOM   3916  CZ  TYR B  92     -45.075 -15.633 -18.091  1.00 22.44           C  
ANISOU 3916  CZ  TYR B  92     3007   2725   2794   -532    565    -97       C  
ATOM   3917  OH  TYR B  92     -45.357 -14.606 -17.218  1.00 20.07           O  
ANISOU 3917  OH  TYR B  92     2684   2451   2489   -522    597   -111       O  
ATOM   3918  N   ASN B  93     -42.396 -21.313 -22.112  1.00 23.67           N  
ANISOU 3918  N   ASN B  93     3369   2694   2932   -538    388    -38       N  
ATOM   3919  CA  ASN B  93     -42.684 -22.575 -22.787  1.00 24.56           C  
ANISOU 3919  CA  ASN B  93     3510   2774   3049   -570    377    -38       C  
ATOM   3920  C   ASN B  93     -41.434 -23.355 -23.168  1.00 26.76           C  
ANISOU 3920  C   ASN B  93     3850   3009   3310   -533    335    -27       C  
ATOM   3921  O   ASN B  93     -41.504 -24.203 -24.058  1.00 30.47           O  
ANISOU 3921  O   ASN B  93     4332   3456   3789   -544    315    -33       O  
ATOM   3922  CB  ASN B  93     -43.536 -22.323 -24.033  1.00 26.57           C  
ANISOU 3922  CB  ASN B  93     3692   3058   3344   -583    369    -61       C  
ATOM   3923  CG  ASN B  93     -44.803 -21.552 -23.718  1.00 31.95           C  
ANISOU 3923  CG  ASN B  93     4305   3785   4048   -615    407    -76       C  
ATOM   3924  OD1 ASN B  93     -44.956 -20.390 -24.111  1.00 31.47           O  
ANISOU 3924  OD1 ASN B  93     4180   3765   4012   -585    401    -89       O  
ATOM   3925  ND2 ASN B  93     -45.711 -22.187 -22.985  1.00 34.40           N  
ANISOU 3925  ND2 ASN B  93     4631   4088   4351   -676    447    -74       N  
ATOM   3926  N   GLN B  94     -40.300 -23.099 -22.510  1.00 26.31           N  
ANISOU 3926  N   GLN B  94     3830   2939   3226   -489    321    -12       N  
ATOM   3927  CA  GLN B  94     -39.067 -23.785 -22.881  1.00 28.62           C  
ANISOU 3927  CA  GLN B  94     4174   3195   3505   -448    280     -5       C  
ATOM   3928  C   GLN B  94     -39.163 -25.292 -22.670  1.00 33.32           C  
ANISOU 3928  C   GLN B  94     4845   3733   4081   -481    279      8       C  
ATOM   3929  O   GLN B  94     -38.447 -26.050 -23.334  1.00 33.06           O  
ANISOU 3929  O   GLN B  94     4846   3668   4048   -455    245      6       O  
ATOM   3930  CB  GLN B  94     -37.882 -23.220 -22.099  1.00 27.25           C  
ANISOU 3930  CB  GLN B  94     4024   3022   3307   -398    266      8       C  
ATOM   3931  CG  GLN B  94     -38.163 -22.908 -20.659  1.00 25.15           C  
ANISOU 3931  CG  GLN B  94     3781   2759   3014   -419    299     23       C  
ATOM   3932  CD  GLN B  94     -36.994 -22.191 -20.010  1.00 31.47           C  
ANISOU 3932  CD  GLN B  94     4594   3568   3795   -368    280     31       C  
ATOM   3933  OE1 GLN B  94     -35.900 -22.748 -19.893  1.00 34.67           O  
ANISOU 3933  OE1 GLN B  94     5049   3942   4181   -333    247     42       O  
ATOM   3934  NE2 GLN B  94     -37.210 -20.941 -19.602  1.00 33.33           N  
ANISOU 3934  NE2 GLN B  94     4783   3845   4036   -361    299     23       N  
ATOM   3935  N   GLU B  95     -40.031 -25.742 -21.757  1.00 34.17           N  
ANISOU 3935  N   GLU B  95     4982   3827   4174   -538    315     19       N  
ATOM   3936  CA  GLU B  95     -40.261 -27.168 -21.538  1.00 37.94           C  
ANISOU 3936  CA  GLU B  95     5534   4248   4635   -580    317     32       C  
ATOM   3937  C   GLU B  95     -41.177 -27.797 -22.578  1.00 39.50           C  
ANISOU 3937  C   GLU B  95     5708   4441   4861   -623    318     14       C  
ATOM   3938  O   GLU B  95     -41.265 -29.027 -22.633  1.00 39.96           O  
ANISOU 3938  O   GLU B  95     5828   4447   4909   -653    312     22       O  
ATOM   3939  CB  GLU B  95     -40.876 -27.422 -20.160  1.00 42.12           C  
ANISOU 3939  CB  GLU B  95     6106   4765   5134   -632    359     53       C  
ATOM   3940  CG  GLU B  95     -40.071 -26.915 -18.990  1.00 47.05           C  
ANISOU 3940  CG  GLU B  95     6764   5389   5722   -599    360     72       C  
ATOM   3941  CD  GLU B  95     -40.830 -27.046 -17.685  1.00 62.00           C  
ANISOU 3941  CD  GLU B  95     8691   7280   7585   -656    408     89       C  
ATOM   3942  OE1 GLU B  95     -41.372 -28.142 -17.421  1.00 67.29           O  
ANISOU 3942  OE1 GLU B  95     9418   7910   8241   -711    423    102       O  
ATOM   3943  OE2 GLU B  95     -40.900 -26.049 -16.933  1.00 64.46           O  
ANISOU 3943  OE2 GLU B  95     8975   7630   7886   -648    431     88       O  
ATOM   3944  N   SER B  96     -41.891 -27.000 -23.365  1.00 38.34           N  
ANISOU 3944  N   SER B  96     5475   4344   4748   -630    326     -8       N  
ATOM   3945  CA  SER B  96     -42.748 -27.579 -24.384  1.00 39.08           C  
ANISOU 3945  CA  SER B  96     5544   4436   4868   -670    323    -27       C  
ATOM   3946  C   SER B  96     -41.939 -27.878 -25.635  1.00 40.10           C  
ANISOU 3946  C   SER B  96     5677   4551   5008   -623    276    -40       C  
ATOM   3947  O   SER B  96     -40.820 -27.393 -25.818  1.00 36.66           O  
ANISOU 3947  O   SER B  96     5242   4121   4566   -560    249    -38       O  
ATOM   3948  CB  SER B  96     -43.910 -26.649 -24.728  1.00 35.13           C  
ANISOU 3948  CB  SER B  96     4951   3997   4401   -697    347    -47       C  
ATOM   3949  OG  SER B  96     -44.634 -26.296 -23.563  1.00 42.74           O  
ANISOU 3949  OG  SER B  96     5905   4978   5355   -735    394    -39       O  
ATOM   3950  N   VAL B  97     -42.526 -28.696 -26.509  1.00 42.96           N  
ANISOU 3950  N   VAL B  97     6042   4895   5386   -659    266    -55       N  
ATOM   3951  CA  VAL B  97     -41.850 -29.037 -27.755  1.00 42.80           C  
ANISOU 3951  CA  VAL B  97     6026   4863   5374   -620    224    -71       C  
ATOM   3952  C   VAL B  97     -41.659 -27.790 -28.617  1.00 41.22           C  
ANISOU 3952  C   VAL B  97     5746   4721   5194   -576    210    -87       C  
ATOM   3953  O   VAL B  97     -40.558 -27.527 -29.118  1.00 41.31           O  
ANISOU 3953  O   VAL B  97     5761   4734   5200   -516    181    -90       O  
ATOM   3954  CB  VAL B  97     -42.624 -30.137 -28.500  1.00 41.70           C  
ANISOU 3954  CB  VAL B  97     5904   4693   5246   -672    218    -86       C  
ATOM   3955  CG1 VAL B  97     -41.853 -30.570 -29.731  1.00 40.91           C  
ANISOU 3955  CG1 VAL B  97     5818   4576   5149   -630    176   -104       C  
ATOM   3956  CG2 VAL B  97     -42.885 -31.326 -27.572  1.00 36.43           C  
ANISOU 3956  CG2 VAL B  97     5318   3965   4558   -723    236    -67       C  
ATOM   3957  N   ASP B  98     -42.717 -26.994 -28.784  1.00 35.94           N  
ANISOU 3957  N   ASP B  98     5005   4101   4550   -605    229    -98       N  
ATOM   3958  CA  ASP B  98     -42.729 -25.854 -29.711  1.00 36.66           C  
ANISOU 3958  CA  ASP B  98     5021   4246   4663   -571    213   -113       C  
ATOM   3959  C   ASP B  98     -42.905 -24.543 -28.943  1.00 38.59           C  
ANISOU 3959  C   ASP B  98     5216   4533   4913   -557    237   -106       C  
ATOM   3960  O   ASP B  98     -43.976 -23.931 -28.981  1.00 43.61           O  
ANISOU 3960  O   ASP B  98     5791   5207   5572   -585    256   -116       O  
ATOM   3961  CB  ASP B  98     -43.835 -26.025 -30.728  1.00 40.20           C  
ANISOU 3961  CB  ASP B  98     5422   4714   5138   -611    207   -135       C  
ATOM   3962  CG  ASP B  98     -43.650 -27.252 -31.595  1.00 51.90           C  
ANISOU 3962  CG  ASP B  98     6951   6155   6615   -623    181   -147       C  
ATOM   3963  OD1 ASP B  98     -42.559 -27.405 -32.185  1.00 54.23           O  
ANISOU 3963  OD1 ASP B  98     7273   6434   6897   -573    152   -150       O  
ATOM   3964  OD2 ASP B  98     -44.599 -28.063 -31.686  1.00 53.16           O  
ANISOU 3964  OD2 ASP B  98     7118   6297   6784   -683    190   -155       O  
ATOM   3965  N   TRP B  99     -41.838 -24.080 -28.291  1.00 25.21           N  
ANISOU 3965  N   TRP B  99     3546   2834   3198   -511    234    -91       N  
ATOM   3966  CA  TRP B  99     -41.955 -22.881 -27.470  1.00 26.61           C  
ANISOU 3966  CA  TRP B  99     3686   3047   3378   -498    257    -84       C  
ATOM   3967  C   TRP B  99     -42.269 -21.634 -28.289  1.00 26.57           C  
ANISOU 3967  C   TRP B  99     3601   3093   3400   -476    247    -99       C  
ATOM   3968  O   TRP B  99     -42.801 -20.668 -27.737  1.00 24.93           O  
ANISOU 3968  O   TRP B  99     3351   2918   3205   -479    270   -100       O  
ATOM   3969  CB  TRP B  99     -40.668 -22.645 -26.682  1.00 22.67           C  
ANISOU 3969  CB  TRP B  99     3230   2532   2851   -452    250    -67       C  
ATOM   3970  CG  TRP B  99     -39.491 -22.365 -27.557  1.00 21.83           C  
ANISOU 3970  CG  TRP B  99     3121   2430   2745   -395    212    -71       C  
ATOM   3971  CD1 TRP B  99     -38.579 -23.274 -28.015  1.00 24.33           C  
ANISOU 3971  CD1 TRP B  99     3486   2711   3048   -371    184    -70       C  
ATOM   3972  CD2 TRP B  99     -39.089 -21.092 -28.089  1.00 21.25           C  
ANISOU 3972  CD2 TRP B  99     2993   2397   2684   -354    199    -77       C  
ATOM   3973  NE1 TRP B  99     -37.640 -22.650 -28.798  1.00 20.63           N  
ANISOU 3973  NE1 TRP B  99     2993   2262   2582   -320    158    -77       N  
ATOM   3974  CE2 TRP B  99     -37.925 -21.310 -28.857  1.00 22.91           C  
ANISOU 3974  CE2 TRP B  99     3221   2597   2887   -311    166    -80       C  
ATOM   3975  CE3 TRP B  99     -39.597 -19.792 -27.990  1.00 21.75           C  
ANISOU 3975  CE3 TRP B  99     2996   2503   2766   -351    212    -81       C  
ATOM   3976  CZ2 TRP B  99     -37.261 -20.276 -29.528  1.00 21.34           C  
ANISOU 3976  CZ2 TRP B  99     2981   2431   2695   -269    148    -84       C  
ATOM   3977  CZ3 TRP B  99     -38.940 -18.765 -28.660  1.00 21.07           C  
ANISOU 3977  CZ3 TRP B  99     2874   2445   2688   -308    190    -85       C  
ATOM   3978  CH2 TRP B  99     -37.780 -19.015 -29.416  1.00 22.93           C  
ANISOU 3978  CH2 TRP B  99     3129   2671   2914   -270    160    -85       C  
ATOM   3979  N   VAL B 100     -41.944 -21.622 -29.586  1.00 22.69           N  
ANISOU 3979  N   VAL B 100     3093   2609   2920   -452    213   -110       N  
ATOM   3980  CA  VAL B 100     -42.010 -20.374 -30.338  1.00 24.97           C  
ANISOU 3980  CA  VAL B 100     3317   2942   3229   -423    199   -119       C  
ATOM   3981  C   VAL B 100     -43.447 -19.925 -30.556  1.00 26.70           C  
ANISOU 3981  C   VAL B 100     3473   3194   3478   -459    213   -133       C  
ATOM   3982  O   VAL B 100     -43.690 -18.733 -30.781  1.00 26.32           O  
ANISOU 3982  O   VAL B 100     3370   3183   3448   -437    210   -137       O  
ATOM   3983  CB  VAL B 100     -41.262 -20.497 -31.682  1.00 26.30           C  
ANISOU 3983  CB  VAL B 100     3488   3110   3395   -391    160   -127       C  
ATOM   3984  CG1 VAL B 100     -42.135 -21.177 -32.734  1.00 24.72           C  
ANISOU 3984  CG1 VAL B 100     3273   2911   3210   -425    147   -144       C  
ATOM   3985  CG2 VAL B 100     -40.803 -19.130 -32.160  1.00 21.44           C  
ANISOU 3985  CG2 VAL B 100     2827   2531   2788   -348    146   -126       C  
ATOM   3986  N   GLY B 101     -44.411 -20.839 -30.476  1.00 25.86           N  
ANISOU 3986  N   GLY B 101     3372   3076   3379   -512    228   -140       N  
ATOM   3987  CA  GLY B 101     -45.803 -20.439 -30.499  1.00 26.86           C  
ANISOU 3987  CA  GLY B 101     3434   3236   3534   -549    246   -154       C  
ATOM   3988  C   GLY B 101     -46.590 -20.954 -31.690  1.00 25.27           C  
ANISOU 3988  C   GLY B 101     3205   3043   3353   -578    223   -172       C  
ATOM   3989  O   GLY B 101     -46.026 -21.281 -32.739  1.00 25.74           O  
ANISOU 3989  O   GLY B 101     3281   3092   3407   -558    188   -176       O  
ATOM   3990  N   ASP B 102     -47.907 -21.035 -31.522  1.00 24.37           N  
ANISOU 3990  N   ASP B 102     3046   2950   3263   -626    244   -185       N  
ATOM   3991  CA  ASP B 102     -48.793 -21.291 -32.644  1.00 23.96           C  
ANISOU 3991  CA  ASP B 102     2951   2916   3236   -652    221   -206       C  
ATOM   3992  C   ASP B 102     -48.634 -20.176 -33.671  1.00 21.58           C  
ANISOU 3992  C   ASP B 102     2601   2650   2950   -603    184   -212       C  
ATOM   3993  O   ASP B 102     -48.526 -19.000 -33.314  1.00 23.12           O  
ANISOU 3993  O   ASP B 102     2762   2870   3153   -568    191   -207       O  
ATOM   3994  CB  ASP B 102     -50.238 -21.379 -32.151  1.00 25.85           C  
ANISOU 3994  CB  ASP B 102     3140   3180   3502   -709    253   -220       C  
ATOM   3995  CG  ASP B 102     -51.207 -21.724 -33.256  1.00 27.35           C  
ANISOU 3995  CG  ASP B 102     3284   3389   3718   -742    227   -242       C  
ATOM   3996  OD1 ASP B 102     -51.569 -20.828 -34.049  1.00 26.77           O  
ANISOU 3996  OD1 ASP B 102     3149   3354   3668   -715    200   -253       O  
ATOM   3997  OD2 ASP B 102     -51.607 -22.902 -33.351  1.00 40.65           O  
ANISOU 3997  OD2 ASP B 102     4997   5049   5400   -795    231   -249       O  
ATOM   3998  N   TYR B 103     -48.614 -20.543 -34.954  1.00 18.73           N  
ANISOU 3998  N   TYR B 103     2239   2289   2590   -602    145   -222       N  
ATOM   3999  CA  TYR B 103     -48.289 -19.548 -35.975  1.00 23.87           C  
ANISOU 3999  CA  TYR B 103     2856   2967   3246   -555    108   -224       C  
ATOM   4000  C   TYR B 103     -49.393 -18.528 -36.189  1.00 22.13           C  
ANISOU 4000  C   TYR B 103     2554   2793   3061   -554    103   -235       C  
ATOM   4001  O   TYR B 103     -49.186 -17.568 -36.942  1.00 18.99           O  
ANISOU 4001  O   TYR B 103     2129   2419   2669   -514     74   -233       O  
ATOM   4002  CB  TYR B 103     -47.957 -20.223 -37.306  1.00 19.86           C  
ANISOU 4002  CB  TYR B 103     2372   2448   2725   -554     68   -233       C  
ATOM   4003  CG  TYR B 103     -46.485 -20.533 -37.435  1.00 20.84           C  
ANISOU 4003  CG  TYR B 103     2562   2541   2815   -516     60   -221       C  
ATOM   4004  CD1 TYR B 103     -45.781 -21.062 -36.361  1.00 22.70           C  
ANISOU 4004  CD1 TYR B 103     2851   2742   3032   -515     87   -207       C  
ATOM   4005  CD2 TYR B 103     -45.801 -20.292 -38.620  1.00 20.76           C  
ANISOU 4005  CD2 TYR B 103     2557   2538   2791   -482     24   -223       C  
ATOM   4006  CE1 TYR B 103     -44.443 -21.350 -36.459  1.00 24.41           C  
ANISOU 4006  CE1 TYR B 103     3122   2933   3221   -479     78   -198       C  
ATOM   4007  CE2 TYR B 103     -44.456 -20.588 -38.735  1.00 22.10           C  
ANISOU 4007  CE2 TYR B 103     2781   2684   2932   -448     19   -216       C  
ATOM   4008  CZ  TYR B 103     -43.783 -21.116 -37.650  1.00 22.64           C  
ANISOU 4008  CZ  TYR B 103     2899   2719   2986   -445     45   -204       C  
ATOM   4009  OH  TYR B 103     -42.445 -21.414 -37.741  1.00 26.43           O  
ANISOU 4009  OH  TYR B 103     3426   3176   3439   -408     37   -198       O  
ATOM   4010  N   ASN B 104     -50.548 -18.709 -35.553  1.00 19.79           N  
ANISOU 4010  N   ASN B 104     2220   2511   2789   -598    132   -247       N  
ATOM   4011  CA  ASN B 104     -51.632 -17.744 -35.617  1.00 24.22           C  
ANISOU 4011  CA  ASN B 104     2698   3117   3387   -595    130   -260       C  
ATOM   4012  C   ASN B 104     -51.776 -16.935 -34.334  1.00 23.36           C  
ANISOU 4012  C   ASN B 104     2569   3021   3287   -583    173   -255       C  
ATOM   4013  O   ASN B 104     -52.735 -16.170 -34.205  1.00 25.03           O  
ANISOU 4013  O   ASN B 104     2711   3268   3531   -581    179   -269       O  
ATOM   4014  CB  ASN B 104     -52.955 -18.439 -35.933  1.00 22.84           C  
ANISOU 4014  CB  ASN B 104     2480   2959   3238   -653    130   -283       C  
ATOM   4015  CG  ASN B 104     -54.003 -17.461 -36.422  1.00 32.66           C  
ANISOU 4015  CG  ASN B 104     3637   4252   4522   -641    110   -299       C  
ATOM   4016  OD1 ASN B 104     -53.699 -16.563 -37.215  1.00 30.50           O  
ANISOU 4016  OD1 ASN B 104     3345   3993   4250   -592     72   -295       O  
ATOM   4017  ND2 ASN B 104     -55.229 -17.593 -35.918  1.00 34.31           N  
ANISOU 4017  ND2 ASN B 104     3789   4486   4761   -683    136   -318       N  
ATOM   4018  N   GLU B 105     -50.849 -17.090 -33.377  1.00 24.27           N  
ANISOU 4018  N   GLU B 105     2742   3107   3374   -572    201   -237       N  
ATOM   4019  CA AGLU B 105     -50.974 -16.399 -32.097  0.61 26.89           C  
ANISOU 4019  CA AGLU B 105     3061   3448   3709   -565    243   -234       C  
ATOM   4020  CA BGLU B 105     -50.952 -16.407 -32.087  0.39 26.86           C  
ANISOU 4020  CA BGLU B 105     3058   3443   3704   -564    243   -233       C  
ATOM   4021  C   GLU B 105     -50.344 -15.012 -32.177  1.00 24.88           C  
ANISOU 4021  C   GLU B 105     2790   3206   3456   -501    227   -226       C  
ATOM   4022  O   GLU B 105     -49.174 -14.884 -32.562  1.00 21.59           O  
ANISOU 4022  O   GLU B 105     2417   2770   3016   -466    203   -210       O  
ATOM   4023  CB AGLU B 105     -50.312 -17.195 -30.980  0.61 27.09           C  
ANISOU 4023  CB AGLU B 105     3157   3437   3700   -585    278   -218       C  
ATOM   4024  CB BGLU B 105     -50.236 -17.199 -31.000  0.39 27.06           C  
ANISOU 4024  CB BGLU B 105     3156   3431   3695   -582    277   -217       C  
ATOM   4025  CG AGLU B 105     -50.733 -16.765 -29.581  0.61 28.42           C  
ANISOU 4025  CG AGLU B 105     3312   3617   3870   -596    330   -219       C  
ATOM   4026  CG BGLU B 105     -50.281 -16.552 -29.625  0.39 27.96           C  
ANISOU 4026  CG BGLU B 105     3266   3552   3804   -576    321   -213       C  
ATOM   4027  CD AGLU B 105     -52.209 -17.030 -29.287  0.61 33.51           C  
ANISOU 4027  CD AGLU B 105     3900   4289   4542   -650    361   -240       C  
ATOM   4028  CD BGLU B 105     -49.657 -17.420 -28.549  0.39 31.31           C  
ANISOU 4028  CD BGLU B 105     3767   3940   4191   -599    352   -196       C  
ATOM   4029  OE1AGLU B 105     -52.815 -17.912 -29.944  0.61 34.19           O  
ANISOU 4029  OE1AGLU B 105     3977   4373   4639   -693    349   -250       O  
ATOM   4030  OE1BGLU B 105     -48.595 -18.028 -28.811  0.39 31.29           O  
ANISOU 4030  OE1BGLU B 105     3827   3902   4161   -584    330   -180       O  
ATOM   4031  OE2AGLU B 105     -52.762 -16.350 -28.391  0.61 32.89           O  
ANISOU 4031  OE2AGLU B 105     3785   4236   4476   -651    399   -249       O  
ATOM   4032  OE2BGLU B 105     -50.236 -17.505 -27.444  0.39 33.67           O  
ANISOU 4032  OE2BGLU B 105     4062   4244   4487   -631    399   -198       O  
ATOM   4033  N   PRO B 106     -51.081 -13.958 -31.822  1.00 23.98           N  
ANISOU 4033  N   PRO B 106     2616   3125   3372   -486    239   -237       N  
ATOM   4034  CA  PRO B 106     -50.474 -12.621 -31.783  1.00 23.71           C  
ANISOU 4034  CA  PRO B 106     2573   3097   3339   -428    226   -229       C  
ATOM   4035  C   PRO B 106     -49.371 -12.568 -30.734  1.00 22.61           C  
ANISOU 4035  C   PRO B 106     2493   2931   3166   -413    252   -211       C  
ATOM   4036  O   PRO B 106     -49.324 -13.376 -29.803  1.00 20.35           O  
ANISOU 4036  O   PRO B 106     2244   2628   2861   -446    287   -208       O  
ATOM   4037  CB  PRO B 106     -51.644 -11.697 -31.413  1.00 24.06           C  
ANISOU 4037  CB  PRO B 106     2542   3177   3423   -423    243   -249       C  
ATOM   4038  CG  PRO B 106     -52.878 -12.485 -31.699  1.00 30.19           C  
ANISOU 4038  CG  PRO B 106     3275   3973   4222   -473    249   -269       C  
ATOM   4039  CD  PRO B 106     -52.505 -13.929 -31.459  1.00 28.49           C  
ANISOU 4039  CD  PRO B 106     3122   3727   3977   -521    265   -260       C  
ATOM   4040  N   LEU B 107     -48.467 -11.603 -30.898  1.00 18.08           N  
ANISOU 4040  N   LEU B 107     1931   2353   2584   -364    231   -200       N  
ATOM   4041  CA  LEU B 107     -47.339 -11.423 -29.991  1.00 19.87           C  
ANISOU 4041  CA  LEU B 107     2210   2557   2781   -344    248   -184       C  
ATOM   4042  C   LEU B 107     -47.705 -10.366 -28.957  1.00 16.57           C  
ANISOU 4042  C   LEU B 107     1765   2155   2376   -328    278   -192       C  
ATOM   4043  O   LEU B 107     -48.011  -9.227 -29.312  1.00 19.33           O  
ANISOU 4043  O   LEU B 107     2071   2523   2752   -296    262   -200       O  
ATOM   4044  CB  LEU B 107     -46.081 -11.011 -30.758  1.00 18.89           C  
ANISOU 4044  CB  LEU B 107     2116   2422   2641   -304    210   -168       C  
ATOM   4045  CG  LEU B 107     -44.788 -10.939 -29.945  1.00 17.81           C  
ANISOU 4045  CG  LEU B 107     2034   2261   2471   -284    220   -152       C  
ATOM   4046  CD1 LEU B 107     -44.304 -12.331 -29.561  1.00 16.29           C  
ANISOU 4046  CD1 LEU B 107     1900   2041   2250   -311    232   -144       C  
ATOM   4047  CD2 LEU B 107     -43.709 -10.183 -30.740  1.00 15.81           C  
ANISOU 4047  CD2 LEU B 107     1790   2006   2211   -242    184   -140       C  
ATOM   4048  N   THR B 108     -47.677 -10.749 -27.689  1.00 17.95           N  
ANISOU 4048  N   THR B 108     1969   2321   2532   -350    320   -192       N  
ATOM   4049  CA  THR B 108     -48.105  -9.885 -26.602  1.00 17.67           C  
ANISOU 4049  CA  THR B 108     1910   2300   2504   -341    356   -203       C  
ATOM   4050  C   THR B 108     -47.013  -9.828 -25.545  1.00 17.66           C  
ANISOU 4050  C   THR B 108     1970   2275   2464   -329    372   -189       C  
ATOM   4051  O   THR B 108     -46.058 -10.615 -25.552  1.00 18.44           O  
ANISOU 4051  O   THR B 108     2127   2348   2533   -334    361   -170       O  
ATOM   4052  CB  THR B 108     -49.410 -10.381 -25.965  1.00 22.34           C  
ANISOU 4052  CB  THR B 108     2468   2911   3109   -387    400   -222       C  
ATOM   4053  OG1 THR B 108     -49.190 -11.676 -25.406  1.00 19.28           O  
ANISOU 4053  OG1 THR B 108     2136   2501   2690   -431    423   -211       O  
ATOM   4054  CG2 THR B 108     -50.529 -10.452 -26.994  1.00 21.66           C  
ANISOU 4054  CG2 THR B 108     2316   2851   3064   -400    381   -239       C  
ATOM   4055  N   GLY B 109     -47.182  -8.892 -24.617  1.00 19.92           N  
ANISOU 4055  N   GLY B 109     2243   2572   2754   -313    399   -199       N  
ATOM   4056  CA  GLY B 109     -46.296  -8.762 -23.480  1.00 16.90           C  
ANISOU 4056  CA  GLY B 109     1913   2172   2335   -304    417   -189       C  
ATOM   4057  C   GLY B 109     -45.914  -7.307 -23.335  1.00 21.52           C  
ANISOU 4057  C   GLY B 109     2482   2763   2931   -258    406   -195       C  
ATOM   4058  O   GLY B 109     -46.796  -6.446 -23.255  1.00 18.79           O  
ANISOU 4058  O   GLY B 109     2084   2439   2616   -246    419   -216       O  
ATOM   4059  N   PHE B 110     -44.612  -7.017 -23.328  1.00 17.26           N  
ANISOU 4059  N   PHE B 110     1985   2204   2369   -231    381   -178       N  
ATOM   4060  CA  PHE B 110     -44.165  -5.639 -23.477  1.00 17.36           C  
ANISOU 4060  CA  PHE B 110     1983   2219   2395   -188    361   -181       C  
ATOM   4061  C   PHE B 110     -44.801  -5.034 -24.721  1.00 17.80           C  
ANISOU 4061  C   PHE B 110     1983   2290   2492   -170    331   -188       C  
ATOM   4062  O   PHE B 110     -44.943  -5.695 -25.754  1.00 18.36           O  
ANISOU 4062  O   PHE B 110     2044   2362   2570   -181    308   -181       O  
ATOM   4063  CB  PHE B 110     -42.639  -5.581 -23.582  1.00 16.41           C  
ANISOU 4063  CB  PHE B 110     1911   2076   2247   -167    332   -160       C  
ATOM   4064  CG  PHE B 110     -41.917  -6.110 -22.367  1.00 17.56           C  
ANISOU 4064  CG  PHE B 110     2114   2206   2351   -178    352   -152       C  
ATOM   4065  CD1 PHE B 110     -42.000  -5.448 -21.144  1.00 17.71           C  
ANISOU 4065  CD1 PHE B 110     2142   2228   2359   -174    381   -164       C  
ATOM   4066  CD2 PHE B 110     -41.120  -7.245 -22.458  1.00 16.36           C  
ANISOU 4066  CD2 PHE B 110     2009   2036   2171   -190    340   -134       C  
ATOM   4067  CE1 PHE B 110     -41.319  -5.927 -20.024  1.00 18.60           C  
ANISOU 4067  CE1 PHE B 110     2311   2327   2430   -184    397   -155       C  
ATOM   4068  CE2 PHE B 110     -40.437  -7.735 -21.346  1.00 16.90           C  
ANISOU 4068  CE2 PHE B 110     2133   2089   2201   -198    354   -125       C  
ATOM   4069  CZ  PHE B 110     -40.527  -7.076 -20.131  1.00 15.65           C  
ANISOU 4069  CZ  PHE B 110     1984   1934   2028   -196    381   -134       C  
ATOM   4070  N   SER B 111     -45.212  -3.782 -24.615  1.00 15.66           N  
ANISOU 4070  N   SER B 111     1676   2028   2247   -142    331   -203       N  
ATOM   4071  CA  SER B 111     -45.917  -3.153 -25.719  1.00 17.85           C  
ANISOU 4071  CA  SER B 111     1901   2319   2564   -122    302   -209       C  
ATOM   4072  C   SER B 111     -44.955  -2.837 -26.854  1.00 15.85           C  
ANISOU 4072  C   SER B 111     1664   2052   2306   -100    253   -188       C  
ATOM   4073  O   SER B 111     -43.912  -2.206 -26.654  1.00 16.93           O  
ANISOU 4073  O   SER B 111     1832   2173   2427    -78    242   -177       O  
ATOM   4074  CB  SER B 111     -46.631  -1.885 -25.256  1.00 19.98           C  
ANISOU 4074  CB  SER B 111     2130   2599   2864    -94    314   -232       C  
ATOM   4075  OG  SER B 111     -47.216  -1.223 -26.364  1.00 18.63           O  
ANISOU 4075  OG  SER B 111     1912   2437   2730    -70    279   -236       O  
ATOM   4076  N   TRP B 112     -45.320  -3.287 -28.042  1.00 14.40           N  
ANISOU 4076  N   TRP B 112     1459   1877   2136   -107    226   -183       N  
ATOM   4077  CA  TRP B 112     -44.553  -3.099 -29.253  1.00 15.54           C  
ANISOU 4077  CA  TRP B 112     1616   2013   2275    -91    181   -164       C  
ATOM   4078  C   TRP B 112     -45.533  -2.697 -30.338  1.00 17.45           C  
ANISOU 4078  C   TRP B 112     1807   2271   2551    -81    153   -170       C  
ATOM   4079  O   TRP B 112     -46.711  -3.055 -30.277  1.00 18.20           O  
ANISOU 4079  O   TRP B 112     1862   2385   2669    -97    166   -188       O  
ATOM   4080  CB  TRP B 112     -43.807  -4.379 -29.657  1.00 13.68           C  
ANISOU 4080  CB  TRP B 112     1420   1768   2009   -114    175   -149       C  
ATOM   4081  CG  TRP B 112     -44.729  -5.453 -30.127  1.00 14.26           C  
ANISOU 4081  CG  TRP B 112     1474   1854   2091   -146    178   -157       C  
ATOM   4082  CD1 TRP B 112     -45.347  -6.395 -29.357  1.00 17.72           C  
ANISOU 4082  CD1 TRP B 112     1913   2294   2525   -180    213   -168       C  
ATOM   4083  CD2 TRP B 112     -45.149  -5.695 -31.475  1.00 16.75           C  
ANISOU 4083  CD2 TRP B 112     1766   2180   2420   -149    143   -156       C  
ATOM   4084  NE1 TRP B 112     -46.122  -7.213 -30.143  1.00 18.96           N  
ANISOU 4084  NE1 TRP B 112     2048   2462   2695   -206    203   -174       N  
ATOM   4085  CE2 TRP B 112     -46.016  -6.807 -31.448  1.00 18.13           C  
ANISOU 4085  CE2 TRP B 112     1927   2363   2600   -186    159   -168       C  
ATOM   4086  CE3 TRP B 112     -44.879  -5.078 -32.700  1.00 16.40           C  
ANISOU 4086  CE3 TRP B 112     1712   2138   2380   -126    101   -146       C  
ATOM   4087  CZ2 TRP B 112     -46.621  -7.317 -32.605  1.00 18.64           C  
ANISOU 4087  CZ2 TRP B 112     1967   2438   2676   -201    131   -172       C  
ATOM   4088  CZ3 TRP B 112     -45.464  -5.591 -33.849  1.00 17.96           C  
ANISOU 4088  CZ3 TRP B 112     1889   2348   2587   -138     74   -148       C  
ATOM   4089  CH2 TRP B 112     -46.337  -6.691 -33.792  1.00 18.10           C  
ANISOU 4089  CH2 TRP B 112     1891   2374   2611   -175     88   -162       C  
ATOM   4090  N   ARG B 113     -45.047  -1.958 -31.330  1.00 14.14           N  
ANISOU 4090  N   ARG B 113     1391   1847   2136    -55    112   -156       N  
ATOM   4091  CA  ARG B 113     -45.916  -1.499 -32.408  1.00 14.36           C  
ANISOU 4091  CA  ARG B 113     1376   1888   2193    -42     78   -159       C  
ATOM   4092  C   ARG B 113     -45.064  -0.819 -33.470  1.00 16.75           C  
ANISOU 4092  C   ARG B 113     1700   2180   2485    -20     36   -136       C  
ATOM   4093  O   ARG B 113     -43.902  -0.473 -33.239  1.00 13.99           O  
ANISOU 4093  O   ARG B 113     1390   1814   2113    -11     37   -122       O  
ATOM   4094  CB  ARG B 113     -46.988  -0.537 -31.895  1.00 15.14           C  
ANISOU 4094  CB  ARG B 113     1426   1996   2330    -20     87   -180       C  
ATOM   4095  CG  ARG B 113     -46.417   0.691 -31.199  1.00 18.31           C  
ANISOU 4095  CG  ARG B 113     1845   2379   2733     11     93   -179       C  
ATOM   4096  CD  ARG B 113     -47.368   1.905 -31.329  1.00 20.10           C  
ANISOU 4096  CD  ARG B 113     2026   2610   3002     47     77   -194       C  
ATOM   4097  NE  ARG B 113     -46.918   3.007 -30.484  1.00 21.42           N  
ANISOU 4097  NE  ARG B 113     2211   2758   3171     73     89   -198       N  
ATOM   4098  CZ  ARG B 113     -46.016   3.915 -30.833  1.00 19.70           C  
ANISOU 4098  CZ  ARG B 113     2026   2516   2945     95     62   -179       C  
ATOM   4099  NH1 ARG B 113     -45.458   3.918 -32.035  1.00 14.90           N  
ANISOU 4099  NH1 ARG B 113     1435   1903   2325     95     22   -153       N  
ATOM   4100  NH2 ARG B 113     -45.678   4.859 -29.959  1.00 18.38           N  
ANISOU 4100  NH2 ARG B 113     1873   2330   2780    115     76   -187       N  
ATOM   4101  N   GLY B 114     -45.668  -0.607 -34.633  1.00 14.13           N  
ANISOU 4101  N   GLY B 114     1341   1858   2169    -12     -2   -133       N  
ATOM   4102  CA  GLY B 114     -45.055   0.196 -35.665  1.00 15.29           C  
ANISOU 4102  CA  GLY B 114     1505   1997   2309     10    -43   -111       C  
ATOM   4103  C   GLY B 114     -45.234   1.670 -35.371  1.00 15.26           C  
ANISOU 4103  C   GLY B 114     1488   1980   2329     45    -52   -112       C  
ATOM   4104  O   GLY B 114     -45.592   2.080 -34.266  1.00 18.85           O  
ANISOU 4104  O   GLY B 114     1929   2431   2801     55    -24   -129       O  
ATOM   4105  N   GLY B 115     -44.989   2.478 -36.389  1.00 17.03           N  
ANISOU 4105  N   GLY B 115     1721   2197   2553     65    -94    -93       N  
ATOM   4106  CA  GLY B 115     -45.019   3.921 -36.146  1.00 16.72           C  
ANISOU 4106  CA  GLY B 115     1681   2138   2535     99   -106    -90       C  
ATOM   4107  C   GLY B 115     -43.642   4.459 -35.818  1.00 19.47           C  
ANISOU 4107  C   GLY B 115     2077   2463   2857    100    -99    -72       C  
ATOM   4108  O   GLY B 115     -42.764   3.755 -35.317  1.00 16.31           O  
ANISOU 4108  O   GLY B 115     1705   2063   2429     78    -72    -70       O  
ATOM   4109  N   SER B 116     -43.437   5.731 -36.130  1.00 18.35           N  
ANISOU 4109  N   SER B 116     1946   2300   2725    125   -125    -59       N  
ATOM   4110  CA  SER B 116     -42.117   6.324 -35.989  1.00 18.94           C  
ANISOU 4110  CA  SER B 116     2066   2354   2776    123   -124    -40       C  
ATOM   4111  C   SER B 116     -41.906   7.016 -34.646  1.00 18.66           C  
ANISOU 4111  C   SER B 116     2038   2300   2752    135    -96    -56       C  
ATOM   4112  O   SER B 116     -40.824   7.571 -34.417  1.00 19.08           O  
ANISOU 4112  O   SER B 116     2127   2335   2789    132    -95    -43       O  
ATOM   4113  CB  SER B 116     -41.872   7.321 -37.123  1.00 17.08           C  
ANISOU 4113  CB  SER B 116     1849   2102   2539    137   -168    -14       C  
ATOM   4114  OG  SER B 116     -42.806   8.380 -37.064  1.00 18.73           O  
ANISOU 4114  OG  SER B 116     2035   2295   2785    170   -189    -21       O  
ATOM   4115  N   GLU B 117     -42.902   7.030 -33.767  1.00 19.04           N  
ANISOU 4115  N   GLU B 117     2053   2353   2827    147    -74    -84       N  
ATOM   4116  CA  GLU B 117     -42.740   7.602 -32.435  1.00 19.08           C  
ANISOU 4116  CA  GLU B 117     2067   2344   2840    157    -44   -102       C  
ATOM   4117  C   GLU B 117     -42.511   6.492 -31.421  1.00 18.20           C  
ANISOU 4117  C   GLU B 117     1960   2248   2707    131      1   -116       C  
ATOM   4118  O   GLU B 117     -43.105   5.412 -31.515  1.00 16.40           O  
ANISOU 4118  O   GLU B 117     1710   2043   2477    113     14   -124       O  
ATOM   4119  CB  GLU B 117     -43.956   8.428 -32.008  1.00 19.75           C  
ANISOU 4119  CB  GLU B 117     2114   2422   2967    190    -43   -127       C  
ATOM   4120  CG  GLU B 117     -44.150   9.693 -32.812  1.00 24.72           C  
ANISOU 4120  CG  GLU B 117     2746   3028   3620    223    -88   -114       C  
ATOM   4121  CD  GLU B 117     -42.988  10.650 -32.646  1.00 28.09           C  
ANISOU 4121  CD  GLU B 117     3222   3421   4031    225    -97    -97       C  
ATOM   4122  OE1 GLU B 117     -42.581  10.914 -31.492  1.00 31.20           O  
ANISOU 4122  OE1 GLU B 117     3631   3804   4421    224    -66   -113       O  
ATOM   4123  OE2 GLU B 117     -42.460  11.117 -33.672  1.00 32.76           O  
ANISOU 4123  OE2 GLU B 117     3837   3998   4613    225   -133    -68       O  
ATOM   4124  N   ARG B 118     -41.661   6.783 -30.444  1.00 17.52           N  
ANISOU 4124  N   ARG B 118     1905   2147   2603    127     22   -119       N  
ATOM   4125  CA  ARG B 118     -41.279   5.812 -29.435  1.00 16.09           C  
ANISOU 4125  CA  ARG B 118     1739   1977   2398    104     60   -129       C  
ATOM   4126  C   ARG B 118     -42.498   5.293 -28.681  1.00 17.72           C  
ANISOU 4126  C   ARG B 118     1911   2201   2620    101     93   -156       C  
ATOM   4127  O   ARG B 118     -43.514   5.984 -28.520  1.00 14.24           O  
ANISOU 4127  O   ARG B 118     1436   1761   2213    123     95   -176       O  
ATOM   4128  CB  ARG B 118     -40.282   6.448 -28.463  1.00 16.31           C  
ANISOU 4128  CB  ARG B 118     1803   1986   2409    106     72   -131       C  
ATOM   4129  CG  ARG B 118     -40.802   7.737 -27.783  1.00 18.44           C  
ANISOU 4129  CG  ARG B 118     2065   2237   2706    134     76   -151       C  
ATOM   4130  CD  ARG B 118     -41.231   7.442 -26.362  1.00 22.01           C  
ANISOU 4130  CD  ARG B 118     2513   2697   3153    130    121   -180       C  
ATOM   4131  NE  ARG B 118     -41.688   8.615 -25.617  1.00 18.17           N  
ANISOU 4131  NE  ARG B 118     2021   2193   2689    157    130   -204       N  
ATOM   4132  CZ  ARG B 118     -40.913   9.389 -24.868  1.00 22.34           C  
ANISOU 4132  CZ  ARG B 118     2584   2700   3205    163    133   -209       C  
ATOM   4133  NH1 ARG B 118     -39.601   9.211 -24.810  1.00 18.58           N  
ANISOU 4133  NH1 ARG B 118     2146   2216   2697    144    124   -190       N  
ATOM   4134  NH2 ARG B 118     -41.472  10.353 -24.139  1.00 18.78           N  
ANISOU 4134  NH2 ARG B 118     2126   2235   2776    188    145   -236       N  
ATOM   4135  N   GLU B 119     -42.396   4.047 -28.233  1.00 15.79           N  
ANISOU 4135  N   GLU B 119     1675   1971   2353     72    120   -159       N  
ATOM   4136  CA  GLU B 119     -43.424   3.436 -27.408  1.00 17.94           C  
ANISOU 4136  CA  GLU B 119     1922   2262   2634     60    158   -183       C  
ATOM   4137  C   GLU B 119     -42.902   3.184 -26.001  1.00 18.53           C  
ANISOU 4137  C   GLU B 119     2029   2331   2681     47    196   -192       C  
ATOM   4138  O   GLU B 119     -43.391   3.803 -25.052  1.00 16.63           O  
ANISOU 4138  O   GLU B 119     1778   2089   2450     59    221   -215       O  
ATOM   4139  CB  GLU B 119     -43.933   2.144 -28.062  1.00 15.02           C  
ANISOU 4139  CB  GLU B 119     1534   1911   2261     33    158   -178       C  
ATOM   4140  CG  GLU B 119     -44.865   1.344 -27.189  1.00 18.20           C  
ANISOU 4140  CG  GLU B 119     1916   2332   2666     10    201   -200       C  
ATOM   4141  CD  GLU B 119     -46.245   1.974 -27.018  1.00 19.55           C  
ANISOU 4141  CD  GLU B 119     2032   2519   2879     27    212   -228       C  
ATOM   4142  OE1 GLU B 119     -46.522   3.030 -27.606  1.00 18.39           O  
ANISOU 4142  OE1 GLU B 119     1862   2366   2761     60    182   -229       O  
ATOM   4143  OE2 GLU B 119     -47.060   1.402 -26.281  1.00 25.62           O  
ANISOU 4143  OE2 GLU B 119     2779   3305   3652      7    251   -248       O  
ATOM   4144  N   THR B 120     -41.885   2.335 -25.841  1.00 15.21           N  
ANISOU 4144  N   THR B 120     1649   1907   2224     26    199   -175       N  
ATOM   4145  CA  THR B 120     -41.329   2.112 -24.514  1.00 16.63           C  
ANISOU 4145  CA  THR B 120     1864   2081   2375     16    229   -182       C  
ATOM   4146  C   THR B 120     -40.646   3.372 -23.993  1.00 14.77           C  
ANISOU 4146  C   THR B 120     1648   1826   2137     38    221   -186       C  
ATOM   4147  O   THR B 120     -39.908   4.050 -24.716  1.00 14.68           O  
ANISOU 4147  O   THR B 120     1645   1802   2129     52    188   -170       O  
ATOM   4148  CB  THR B 120     -40.321   0.961 -24.513  1.00 13.47           C  
ANISOU 4148  CB  THR B 120     1503   1678   1936     -7    226   -162       C  
ATOM   4149  OG1 THR B 120     -40.861  -0.161 -25.223  1.00 14.25           O  
ANISOU 4149  OG1 THR B 120     1587   1789   2039    -27    225   -157       O  
ATOM   4150  CG2 THR B 120     -40.056   0.545 -23.086  1.00 14.80           C  
ANISOU 4150  CG2 THR B 120     1704   1843   2075    -20    260   -171       C  
ATOM   4151  N   THR B 121     -40.907   3.695 -22.732  1.00 15.58           N  
ANISOU 4151  N   THR B 121     1758   1928   2233     40    253   -207       N  
ATOM   4152  CA  THR B 121     -40.181   4.751 -22.046  1.00 18.39           C  
ANISOU 4152  CA  THR B 121     2141   2265   2581     56    249   -214       C  
ATOM   4153  C   THR B 121     -39.567   4.176 -20.785  1.00 16.02           C  
ANISOU 4153  C   THR B 121     1882   1966   2240     38    276   -217       C  
ATOM   4154  O   THR B 121     -39.977   3.119 -20.302  1.00 17.91           O  
ANISOU 4154  O   THR B 121     2125   2218   2461     16    304   -220       O  
ATOM   4155  CB  THR B 121     -41.071   5.950 -21.677  1.00 19.61           C  
ANISOU 4155  CB  THR B 121     2269   2414   2767     83    260   -241       C  
ATOM   4156  OG1 THR B 121     -41.995   5.569 -20.655  1.00 19.92           O  
ANISOU 4156  OG1 THR B 121     2296   2470   2803     74    306   -267       O  
ATOM   4157  CG2 THR B 121     -41.833   6.479 -22.898  1.00 17.31           C  
ANISOU 4157  CG2 THR B 121     1935   2123   2518    104    232   -238       C  
ATOM   4158  N   GLY B 122     -38.579   4.895 -20.258  1.00 17.31           N  
ANISOU 4158  N   GLY B 122     2078   2112   2387     46    264   -217       N  
ATOM   4159  CA  GLY B 122     -37.901   4.454 -19.053  1.00 13.74           C  
ANISOU 4159  CA  GLY B 122     1667   1659   1893     32    282   -220       C  
ATOM   4160  C   GLY B 122     -37.422   3.021 -19.171  1.00 17.41           C  
ANISOU 4160  C   GLY B 122     2152   2133   2330      9    282   -199       C  
ATOM   4161  O   GLY B 122     -36.864   2.604 -20.193  1.00 15.84           O  
ANISOU 4161  O   GLY B 122     1951   1934   2135      7    253   -177       O  
ATOM   4162  N   ILE B 123     -37.637   2.254 -18.108  1.00 15.85           N  
ANISOU 4162  N   ILE B 123     1979   1942   2103     -9    313   -206       N  
ATOM   4163  CA  ILE B 123     -37.324   0.831 -18.074  1.00 17.54           C  
ANISOU 4163  CA  ILE B 123     2217   2160   2289    -32    316   -187       C  
ATOM   4164  C   ILE B 123     -38.531   0.109 -17.509  1.00 17.66           C  
ANISOU 4164  C   ILE B 123     2223   2187   2299    -54    360   -199       C  
ATOM   4165  O   ILE B 123     -39.094   0.525 -16.493  1.00 17.90           O  
ANISOU 4165  O   ILE B 123     2257   2223   2323    -56    393   -221       O  
ATOM   4166  CB  ILE B 123     -36.072   0.522 -17.229  1.00 16.02           C  
ANISOU 4166  CB  ILE B 123     2076   1958   2054    -35    306   -178       C  
ATOM   4167  CG1 ILE B 123     -34.813   1.089 -17.874  1.00 15.60           C  
ANISOU 4167  CG1 ILE B 123     2027   1896   2005    -19    263   -165       C  
ATOM   4168  CG2 ILE B 123     -35.900  -0.974 -17.031  1.00 16.88           C  
ANISOU 4168  CG2 ILE B 123     2215   2067   2133    -57    313   -161       C  
ATOM   4169  CD1 ILE B 123     -33.625   1.076 -16.937  1.00 16.46           C  
ANISOU 4169  CD1 ILE B 123     2180   1998   2077    -18    251   -162       C  
ATOM   4170  N   GLN B 124     -38.937  -0.958 -18.171  1.00 15.49           N  
ANISOU 4170  N   GLN B 124     1938   1919   2030    -71    361   -187       N  
ATOM   4171  CA  GLN B 124     -40.006  -1.794 -17.676  1.00 15.17           C  
ANISOU 4171  CA  GLN B 124     1891   1889   1983   -100    401   -195       C  
ATOM   4172  C   GLN B 124     -39.446  -3.191 -17.496  1.00 15.85           C  
ANISOU 4172  C   GLN B 124     2023   1966   2035   -124    399   -173       C  
ATOM   4173  O   GLN B 124     -38.439  -3.559 -18.112  1.00 16.76           O  
ANISOU 4173  O   GLN B 124     2156   2070   2142   -115    363   -154       O  
ATOM   4174  CB  GLN B 124     -41.212  -1.782 -18.608  1.00 15.77           C  
ANISOU 4174  CB  GLN B 124     1909   1980   2102   -103    406   -205       C  
ATOM   4175  CG  GLN B 124     -40.958  -2.280 -20.018  1.00 22.39           C  
ANISOU 4175  CG  GLN B 124     2733   2816   2958   -101    370   -186       C  
ATOM   4176  CD  GLN B 124     -42.181  -2.072 -20.905  1.00 23.73           C  
ANISOU 4176  CD  GLN B 124     2843   3003   3171   -100    370   -198       C  
ATOM   4177  OE1 GLN B 124     -43.257  -1.689 -20.401  1.00 18.77           O  
ANISOU 4177  OE1 GLN B 124     2183   2389   2560   -103    402   -221       O  
ATOM   4178  NE2 GLN B 124     -42.029  -2.311 -22.230  1.00 15.37           N  
ANISOU 4178  NE2 GLN B 124     1767   1943   2129    -95    335   -184       N  
ATOM   4179  N   ILE B 125     -40.053  -3.939 -16.583  1.00 18.57           N  
ANISOU 4179  N   ILE B 125     2388   2314   2355   -153    438   -177       N  
ATOM   4180  CA  ILE B 125     -39.634  -5.302 -16.332  1.00 18.29           C  
ANISOU 4180  CA  ILE B 125     2399   2265   2284   -178    438   -156       C  
ATOM   4181  C   ILE B 125     -40.884  -6.155 -16.371  1.00 18.58           C  
ANISOU 4181  C   ILE B 125     2418   2311   2329   -215    474   -161       C  
ATOM   4182  O   ILE B 125     -42.006  -5.663 -16.222  1.00 18.45           O  
ANISOU 4182  O   ILE B 125     2359   2315   2336   -222    506   -183       O  
ATOM   4183  CB  ILE B 125     -38.892  -5.472 -14.989  1.00 19.31           C  
ANISOU 4183  CB  ILE B 125     2591   2383   2364   -182    447   -150       C  
ATOM   4184  CG1 ILE B 125     -39.827  -5.179 -13.817  1.00 22.26           C  
ANISOU 4184  CG1 ILE B 125     2966   2770   2722   -201    499   -171       C  
ATOM   4185  CG2 ILE B 125     -37.658  -4.573 -14.945  1.00 18.00           C  
ANISOU 4185  CG2 ILE B 125     2437   2209   2192   -147    410   -148       C  
ATOM   4186  CD1 ILE B 125     -39.311  -5.702 -12.485  1.00 26.93           C  
ANISOU 4186  CD1 ILE B 125     3627   3351   3256   -217    513   -161       C  
ATOM   4187  N   TRP B 126     -40.679  -7.440 -16.614  1.00 14.38           N  
ANISOU 4187  N   TRP B 126     1917   1765   1781   -237    467   -141       N  
ATOM   4188  CA  TRP B 126     -41.797  -8.358 -16.616  1.00 18.54           C  
ANISOU 4188  CA  TRP B 126     2434   2298   2312   -279    500   -143       C  
ATOM   4189  C   TRP B 126     -42.150  -8.706 -15.180  1.00 16.90           C  
ANISOU 4189  C   TRP B 126     2267   2091   2065   -309    546   -146       C  
ATOM   4190  O   TRP B 126     -41.267  -8.921 -14.346  1.00 18.85           O  
ANISOU 4190  O   TRP B 126     2573   2320   2269   -305    539   -132       O  
ATOM   4191  CB  TRP B 126     -41.458  -9.603 -17.415  1.00 15.34           C  
ANISOU 4191  CB  TRP B 126     2052   1873   1904   -292    474   -123       C  
ATOM   4192  CG  TRP B 126     -42.652 -10.455 -17.667  1.00 19.49           C  
ANISOU 4192  CG  TRP B 126     2557   2405   2443   -336    502   -127       C  
ATOM   4193  CD1 TRP B 126     -42.900 -11.685 -17.143  1.00 18.93           C  
ANISOU 4193  CD1 TRP B 126     2530   2317   2344   -378    524   -115       C  
ATOM   4194  CD2 TRP B 126     -43.775 -10.135 -18.498  1.00 18.33           C  
ANISOU 4194  CD2 TRP B 126     2340   2284   2342   -343    509   -146       C  
ATOM   4195  NE1 TRP B 126     -44.105 -12.162 -17.607  1.00 21.62           N  
ANISOU 4195  NE1 TRP B 126     2831   2672   2711   -415    547   -126       N  
ATOM   4196  CE2 TRP B 126     -44.665 -11.227 -18.434  1.00 23.31           C  
ANISOU 4196  CE2 TRP B 126     2973   2914   2971   -394    537   -146       C  
ATOM   4197  CE3 TRP B 126     -44.118  -9.029 -19.286  1.00 20.27           C  
ANISOU 4197  CE3 TRP B 126     2522   2550   2629   -313    493   -163       C  
ATOM   4198  CZ2 TRP B 126     -45.867 -11.252 -19.136  1.00 23.48           C  
ANISOU 4198  CZ2 TRP B 126     2931   2959   3033   -414    548   -163       C  
ATOM   4199  CZ3 TRP B 126     -45.307  -9.054 -19.982  1.00 20.49           C  
ANISOU 4199  CZ3 TRP B 126     2489   2600   2695   -329    502   -178       C  
ATOM   4200  CH2 TRP B 126     -46.172 -10.158 -19.902  1.00 22.89           C  
ANISOU 4200  CH2 TRP B 126     2792   2906   2998   -380    529   -180       C  
ATOM   4201  N   SER B 127     -43.447  -8.719 -14.882  1.00 22.21           N  
ANISOU 4201  N   SER B 127     2904   2785   2750   -340    592   -164       N  
ATOM   4202  CA  SER B 127     -43.872  -8.840 -13.494  1.00 22.23           C  
ANISOU 4202  CA  SER B 127     2937   2794   2715   -369    642   -171       C  
ATOM   4203  C   SER B 127     -43.622 -10.227 -12.934  1.00 25.68           C  
ANISOU 4203  C   SER B 127     3445   3207   3107   -409    652   -145       C  
ATOM   4204  O   SER B 127     -43.563 -10.381 -11.709  1.00 25.17           O  
ANISOU 4204  O   SER B 127     3428   3139   2996   -428    683   -142       O  
ATOM   4205  CB  SER B 127     -45.351  -8.493 -13.349  1.00 21.81           C  
ANISOU 4205  CB  SER B 127     2823   2775   2690   -392    693   -200       C  
ATOM   4206  OG  SER B 127     -46.166  -9.502 -13.911  1.00 23.09           O  
ANISOU 4206  OG  SER B 127     2965   2940   2869   -433    705   -196       O  
ATOM   4207  N   GLU B 128     -43.468 -11.238 -13.788  1.00 21.88           N  
ANISOU 4207  N   GLU B 128     2974   2706   2635   -421    627   -126       N  
ATOM   4208  CA  GLU B 128     -43.226 -12.597 -13.321  1.00 24.00           C  
ANISOU 4208  CA  GLU B 128     3312   2944   2862   -457    632   -100       C  
ATOM   4209  C   GLU B 128     -41.739 -12.919 -13.437  1.00 23.22           C  
ANISOU 4209  C   GLU B 128     3270   2813   2739   -423    579    -76       C  
ATOM   4210  O   GLU B 128     -41.184 -12.984 -14.541  1.00 24.07           O  
ANISOU 4210  O   GLU B 128     3360   2911   2873   -395    535    -71       O  
ATOM   4211  CB  GLU B 128     -44.068 -13.612 -14.089  1.00 24.96           C  
ANISOU 4211  CB  GLU B 128     3414   3062   3007   -498    640    -97       C  
ATOM   4212  CG  GLU B 128     -43.959 -15.010 -13.497  1.00 25.66           C  
ANISOU 4212  CG  GLU B 128     3580   3117   3053   -542    652    -71       C  
ATOM   4213  CD  GLU B 128     -44.947 -15.988 -14.092  1.00 30.36           C  
ANISOU 4213  CD  GLU B 128     4157   3709   3669   -593    670    -72       C  
ATOM   4214  OE1 GLU B 128     -45.837 -15.566 -14.854  1.00 27.84           O  
ANISOU 4214  OE1 GLU B 128     3761   3420   3396   -598    678    -95       O  
ATOM   4215  OE2 GLU B 128     -44.836 -17.191 -13.787  1.00 41.08           O  
ANISOU 4215  OE2 GLU B 128     5579   5033   4996   -629    673    -49       O  
ATOM   4216  N   ILE B 129     -41.102 -13.112 -12.291  1.00 23.26           N  
ANISOU 4216  N   ILE B 129     3342   2802   2693   -424    583    -62       N  
ATOM   4217  CA  ILE B 129     -39.726 -13.575 -12.230  1.00 21.31           C  
ANISOU 4217  CA  ILE B 129     3155   2524   2419   -396    535    -38       C  
ATOM   4218  C   ILE B 129     -39.719 -15.077 -12.471  1.00 28.00           C  
ANISOU 4218  C   ILE B 129     4049   3336   3252   -424    527    -14       C  
ATOM   4219  O   ILE B 129     -40.417 -15.827 -11.779  1.00 26.24           O  
ANISOU 4219  O   ILE B 129     3863   3104   3002   -473    565     -6       O  
ATOM   4220  CB  ILE B 129     -39.113 -13.237 -10.865  1.00 26.50           C  
ANISOU 4220  CB  ILE B 129     3867   3177   3025   -388    541    -32       C  
ATOM   4221  CG1 ILE B 129     -39.144 -11.726 -10.614  1.00 20.21           C  
ANISOU 4221  CG1 ILE B 129     3025   2412   2243   -360    549    -59       C  
ATOM   4222  CG2 ILE B 129     -37.735 -13.850 -10.749  1.00 24.19           C  
ANISOU 4222  CG2 ILE B 129     3637   2852   2703   -360    490     -7       C  
ATOM   4223  CD1 ILE B 129     -38.400 -10.915 -11.623  1.00 22.47           C  
ANISOU 4223  CD1 ILE B 129     3266   2704   2568   -312    504    -66       C  
ATOM   4224  N   PHE B 130     -38.936 -15.525 -13.448  1.00 21.44           N  
ANISOU 4224  N   PHE B 130     3222   2485   2438   -396    479     -5       N  
ATOM   4225  CA  PHE B 130     -38.902 -16.936 -13.817  1.00 23.55           C  
ANISOU 4225  CA  PHE B 130     3533   2717   2698   -419    467     14       C  
ATOM   4226  C   PHE B 130     -37.890 -17.679 -12.964  1.00 26.18           C  
ANISOU 4226  C   PHE B 130     3954   3013   2982   -408    444     41       C  
ATOM   4227  O   PHE B 130     -36.725 -17.282 -12.889  1.00 25.24           O  
ANISOU 4227  O   PHE B 130     3847   2890   2853   -361    405     45       O  
ATOM   4228  CB  PHE B 130     -38.558 -17.099 -15.294  1.00 21.99           C  
ANISOU 4228  CB  PHE B 130     3299   2516   2542   -392    428     10       C  
ATOM   4229  CG  PHE B 130     -39.505 -16.387 -16.195  1.00 19.52           C  
ANISOU 4229  CG  PHE B 130     2902   2237   2276   -399    443    -14       C  
ATOM   4230  CD1 PHE B 130     -40.729 -16.949 -16.495  1.00 22.13           C  
ANISOU 4230  CD1 PHE B 130     3211   2572   2624   -447    474    -21       C  
ATOM   4231  CD2 PHE B 130     -39.197 -15.136 -16.699  1.00 22.67           C  
ANISOU 4231  CD2 PHE B 130     3245   2665   2702   -359    427    -30       C  
ATOM   4232  CE1 PHE B 130     -41.622 -16.286 -17.308  1.00 24.35           C  
ANISOU 4232  CE1 PHE B 130     3414   2887   2949   -451    484    -43       C  
ATOM   4233  CE2 PHE B 130     -40.082 -14.470 -17.527  1.00 21.94           C  
ANISOU 4233  CE2 PHE B 130     3081   2603   2654   -363    437    -50       C  
ATOM   4234  CZ  PHE B 130     -41.298 -15.048 -17.827  1.00 18.74           C  
ANISOU 4234  CZ  PHE B 130     2651   2203   2266   -407    465    -57       C  
ATOM   4235  N   LEU B 131     -38.337 -18.758 -12.327  1.00 24.78           N  
ANISOU 4235  N   LEU B 131     3837   2806   2771   -453    466     59       N  
ATOM   4236  CA  LEU B 131     -37.464 -19.594 -11.517  1.00 26.07           C  
ANISOU 4236  CA  LEU B 131     4091   2929   2886   -446    442     87       C  
ATOM   4237  C   LEU B 131     -36.992 -20.751 -12.380  1.00 27.50           C  
ANISOU 4237  C   LEU B 131     4301   3068   3079   -436    404    100       C  
ATOM   4238  O   LEU B 131     -37.801 -21.571 -12.819  1.00 25.48           O  
ANISOU 4238  O   LEU B 131     4049   2797   2836   -478    422    103       O  
ATOM   4239  CB  LEU B 131     -38.189 -20.096 -10.271  1.00 26.12           C  
ANISOU 4239  CB  LEU B 131     4155   2924   2845   -502    489    102       C  
ATOM   4240  CG  LEU B 131     -38.636 -18.964  -9.346  1.00 28.79           C  
ANISOU 4240  CG  LEU B 131     4468   3303   3166   -510    530     86       C  
ATOM   4241  CD1 LEU B 131     -39.437 -19.506  -8.173  1.00 31.84           C  
ANISOU 4241  CD1 LEU B 131     4910   3682   3505   -571    582     99       C  
ATOM   4242  CD2 LEU B 131     -37.410 -18.223  -8.853  1.00 30.47           C  
ANISOU 4242  CD2 LEU B 131     4699   3520   3358   -456    491     87       C  
ATOM   4243  N   ILE B 132     -35.691 -20.802 -12.633  1.00 27.10           N  
ANISOU 4243  N   ILE B 132     4269   3002   3025   -380    350    107       N  
ATOM   4244  CA  ILE B 132     -35.114 -21.701 -13.617  1.00 30.81           C  
ANISOU 4244  CA  ILE B 132     4753   3440   3514   -357    310    112       C  
ATOM   4245  C   ILE B 132     -34.029 -22.526 -12.943  1.00 37.14           C  
ANISOU 4245  C   ILE B 132     5639   4197   4275   -330    271    137       C  
ATOM   4246  O   ILE B 132     -33.151 -21.977 -12.266  1.00 39.68           O  
ANISOU 4246  O   ILE B 132     5975   4527   4574   -294    249    141       O  
ATOM   4247  CB  ILE B 132     -34.539 -20.927 -14.817  1.00 30.28           C  
ANISOU 4247  CB  ILE B 132     4613   3402   3491   -309    280     90       C  
ATOM   4248  CG1 ILE B 132     -35.616 -20.024 -15.436  1.00 27.52           C  
ANISOU 4248  CG1 ILE B 132     4181   3096   3180   -332    315     67       C  
ATOM   4249  CG2 ILE B 132     -33.965 -21.896 -15.842  1.00 32.22           C  
ANISOU 4249  CG2 ILE B 132     4874   3616   3754   -286    242     92       C  
ATOM   4250  CD1 ILE B 132     -36.768 -20.786 -16.067  1.00 28.23           C  
ANISOU 4250  CD1 ILE B 132     4259   3176   3290   -381    340     63       C  
ATOM   4251  N   ASN B 133     -34.089 -23.840 -13.128  1.00 38.86           N  
ANISOU 4251  N   ASN B 133     5915   4366   4485   -346    260    153       N  
ATOM   4252  CA  ASN B 133     -33.039 -24.725 -12.645  1.00 43.92           C  
ANISOU 4252  CA  ASN B 133     6636   4958   5093   -314    216    176       C  
ATOM   4253  C   ASN B 133     -31.881 -24.745 -13.631  1.00 44.78           C  
ANISOU 4253  C   ASN B 133     6718   5065   5231   -248    163    164       C  
ATOM   4254  O   ASN B 133     -32.074 -25.013 -14.821  1.00 45.70           O  
ANISOU 4254  O   ASN B 133     6797   5181   5385   -246    158    148       O  
ATOM   4255  CB  ASN B 133     -33.587 -26.135 -12.445  1.00 47.08           C  
ANISOU 4255  CB  ASN B 133     7113   5302   5474   -359    225    198       C  
ATOM   4256  CG  ASN B 133     -34.577 -26.208 -11.316  1.00 46.50           C  
ANISOU 4256  CG  ASN B 133     7078   5227   5362   -424    276    214       C  
ATOM   4257  OD1 ASN B 133     -35.767 -26.417 -11.532  1.00 50.50           O  
ANISOU 4257  OD1 ASN B 133     7566   5740   5881   -484    321    209       O  
ATOM   4258  ND2 ASN B 133     -34.089 -26.027 -10.096  1.00 50.08           N  
ANISOU 4258  ND2 ASN B 133     7585   5676   5767   -415    270    233       N  
ATOM   4259  N   LYS B 134     -30.686 -24.449 -13.141  1.00 44.58           N  
ANISOU 4259  N   LYS B 134     6710   5041   5187   -196    123    169       N  
ATOM   4260  CA  LYS B 134     -29.493 -24.541 -13.965  1.00 51.43           C  
ANISOU 4260  CA  LYS B 134     7556   5907   6078   -133     73    158       C  
ATOM   4261  C   LYS B 134     -28.927 -25.955 -13.905  1.00 57.91           C  
ANISOU 4261  C   LYS B 134     8456   6665   6883   -113     36    176       C  
ATOM   4262  O   LYS B 134     -29.242 -26.721 -12.985  1.00 56.19           O  
ANISOU 4262  O   LYS B 134     8318   6406   6626   -142     42    202       O  
ATOM   4263  CB  LYS B 134     -28.450 -23.518 -13.503  1.00 52.43           C  
ANISOU 4263  CB  LYS B 134     7656   6068   6197    -86     46    152       C  
ATOM   4264  CG  LYS B 134     -28.830 -22.061 -13.809  1.00 49.78           C  
ANISOU 4264  CG  LYS B 134     7235   5791   5887    -94     75    130       C  
ATOM   4265  CD  LYS B 134     -27.639 -21.105 -13.709  1.00 40.20           C  
ANISOU 4265  CD  LYS B 134     5987   4611   4678    -43     41    119       C  
ATOM   4266  CE  LYS B 134     -26.686 -21.279 -14.874  1.00 43.17           C  
ANISOU 4266  CE  LYS B 134     6325   4990   5086      5      3    105       C  
ATOM   4267  NZ  LYS B 134     -25.580 -20.292 -14.851  1.00 43.65           N  
ANISOU 4267  NZ  LYS B 134     6344   5087   5154     49    -25     93       N  
ATOM   4268  N   PRO B 135     -28.104 -26.345 -14.887  1.00 57.44           N  
ANISOU 4268  N   PRO B 135     8379   6596   6851    -64     -2    162       N  
ATOM   4269  CA  PRO B 135     -27.577 -27.721 -14.891  1.00 58.46           C  
ANISOU 4269  CA  PRO B 135     8584   6662   6968    -40    -39    176       C  
ATOM   4270  C   PRO B 135     -26.802 -28.082 -13.639  1.00 63.70           C  
ANISOU 4270  C   PRO B 135     9322   7294   7586    -14    -73    202       C  
ATOM   4271  O   PRO B 135     -26.761 -29.263 -13.270  1.00 66.99           O  
ANISOU 4271  O   PRO B 135     9822   7650   7980    -16    -91    224       O  
ATOM   4272  CB  PRO B 135     -26.677 -27.749 -16.134  1.00 62.49           C  
ANISOU 4272  CB  PRO B 135     9044   7184   7516     18    -73    150       C  
ATOM   4273  CG  PRO B 135     -27.229 -26.685 -17.024  1.00 63.25           C  
ANISOU 4273  CG  PRO B 135     9048   7339   7647     -1    -40    125       C  
ATOM   4274  CD  PRO B 135     -27.711 -25.601 -16.099  1.00 59.52           C  
ANISOU 4274  CD  PRO B 135     8554   6903   7156    -32    -10    133       C  
ATOM   4275  N   ASP B 136     -26.190 -27.103 -12.971  1.00 60.52           N  
ANISOU 4275  N   ASP B 136     8895   6931   7170     10    -84    201       N  
ATOM   4276  CA  ASP B 136     -25.451 -27.344 -11.738  1.00 58.85           C  
ANISOU 4276  CA  ASP B 136     8752   6696   6913     35   -119    225       C  
ATOM   4277  C   ASP B 136     -26.351 -27.426 -10.512  1.00 59.52           C  
ANISOU 4277  C   ASP B 136     8900   6765   6949    -25    -83    253       C  
ATOM   4278  O   ASP B 136     -25.837 -27.399  -9.390  1.00 57.72           O  
ANISOU 4278  O   ASP B 136     8725   6528   6679    -11   -107    272       O  
ATOM   4279  CB  ASP B 136     -24.388 -26.257 -11.532  1.00 62.19           C  
ANISOU 4279  CB  ASP B 136     9122   7168   7340     85   -148    211       C  
ATOM   4280  CG  ASP B 136     -24.953 -24.846 -11.635  1.00 64.80           C  
ANISOU 4280  CG  ASP B 136     9375   7561   7686     55   -105    192       C  
ATOM   4281  OD1 ASP B 136     -25.939 -24.541 -10.931  1.00 63.79           O  
ANISOU 4281  OD1 ASP B 136     9264   7439   7534      1    -62    203       O  
ATOM   4282  OD2 ASP B 136     -24.402 -24.034 -12.412  1.00 64.43           O  
ANISOU 4282  OD2 ASP B 136     9250   7557   7675     86   -115    167       O  
ATOM   4283  N   GLY B 137     -27.670 -27.518 -10.694  1.00 60.52           N  
ANISOU 4283  N   GLY B 137     9022   6892   7082    -92    -28    253       N  
ATOM   4284  CA  GLY B 137     -28.601 -27.637  -9.593  1.00 63.32           C  
ANISOU 4284  CA  GLY B 137     9433   7235   7392   -155     13    277       C  
ATOM   4285  C   GLY B 137     -29.108 -26.324  -9.030  1.00 62.73           C  
ANISOU 4285  C   GLY B 137     9307   7219   7307   -182     55    266       C  
ATOM   4286  O   GLY B 137     -30.155 -26.314  -8.373  1.00 62.92           O  
ANISOU 4286  O   GLY B 137     9356   7244   7306   -244    105    276       O  
ATOM   4287  N   LYS B 138     -28.397 -25.223  -9.268  1.00 62.84           N  
ANISOU 4287  N   LYS B 138     9253   7281   7342   -138     37    244       N  
ATOM   4288  CA  LYS B 138     -28.811 -23.921  -8.757  1.00 61.77           C  
ANISOU 4288  CA  LYS B 138     9070   7198   7200   -158     72    230       C  
ATOM   4289  C   LYS B 138     -30.170 -23.523  -9.325  1.00 58.20           C  
ANISOU 4289  C   LYS B 138     8562   6774   6779   -212    134    213       C  
ATOM   4290  O   LYS B 138     -30.464 -23.756 -10.501  1.00 55.38           O  
ANISOU 4290  O   LYS B 138     8159   6416   6465   -213    137    199       O  
ATOM   4291  CB  LYS B 138     -27.760 -22.867  -9.118  1.00 62.86           C  
ANISOU 4291  CB  LYS B 138     9142   7378   7364   -101     38    207       C  
ATOM   4292  CG  LYS B 138     -27.928 -21.524  -8.433  1.00 62.68           C  
ANISOU 4292  CG  LYS B 138     9084   7404   7329   -111     62    195       C  
ATOM   4293  CD  LYS B 138     -27.602 -21.619  -6.948  1.00 72.99           C  
ANISOU 4293  CD  LYS B 138    10466   8695   8571   -115     50    216       C  
ATOM   4294  CE  LYS B 138     -26.256 -22.302  -6.713  1.00 74.47           C  
ANISOU 4294  CE  LYS B 138    10703   8851   8740    -59    -20    232       C  
ATOM   4295  NZ  LYS B 138     -25.898 -22.359  -5.264  1.00 81.74           N  
ANISOU 4295  NZ  LYS B 138    11701   9759   9597    -61    -37    254       N  
ATOM   4296  N   LYS B 139     -31.003 -22.921  -8.477  1.00 44.82           N  
ANISOU 4296  N   LYS B 139     6867   5103   5059   -256    182    213       N  
ATOM   4297  CA  LYS B 139     -32.295 -22.380  -8.886  1.00 40.38           C  
ANISOU 4297  CA  LYS B 139     6243   4574   4524   -304    241    194       C  
ATOM   4298  C   LYS B 139     -32.160 -20.862  -8.965  1.00 37.40           C  
ANISOU 4298  C   LYS B 139     5789   4253   4169   -282    248    167       C  
ATOM   4299  O   LYS B 139     -32.011 -20.189  -7.938  1.00 38.63           O  
ANISOU 4299  O   LYS B 139     5961   4426   4290   -282    257    167       O  
ATOM   4300  CB  LYS B 139     -33.393 -22.783  -7.906  1.00 42.16           C  
ANISOU 4300  CB  LYS B 139     6520   4789   4709   -372    294    210       C  
ATOM   4301  CG  LYS B 139     -34.760 -22.210  -8.242  1.00 39.79           C  
ANISOU 4301  CG  LYS B 139     6153   4527   4439   -421    357    188       C  
ATOM   4302  CD  LYS B 139     -35.608 -23.209  -9.018  1.00 47.50           C  
ANISOU 4302  CD  LYS B 139     7129   5478   5440   -463    376    192       C  
ATOM   4303  CE  LYS B 139     -36.035 -24.379  -8.132  1.00 52.84           C  
ANISOU 4303  CE  LYS B 139     7902   6109   6067   -516    396    223       C  
ATOM   4304  NZ  LYS B 139     -36.773 -25.408  -8.916  1.00 52.91           N  
ANISOU 4304  NZ  LYS B 139     7915   6088   6101   -557    409    227       N  
ATOM   4305  N   VAL B 140     -32.202 -20.320 -10.178  1.00 33.53           N  
ANISOU 4305  N   VAL B 140     5218   3788   3732   -263    244    144       N  
ATOM   4306  CA  VAL B 140     -31.959 -18.899 -10.377  1.00 28.42           C  
ANISOU 4306  CA  VAL B 140     4501   3189   3110   -237    244    119       C  
ATOM   4307  C   VAL B 140     -33.264 -18.202 -10.733  1.00 27.76           C  
ANISOU 4307  C   VAL B 140     4353   3138   3055   -275    297     99       C  
ATOM   4308  O   VAL B 140     -34.217 -18.807 -11.235  1.00 27.96           O  
ANISOU 4308  O   VAL B 140     4370   3155   3098   -312    325     99       O  
ATOM   4309  CB  VAL B 140     -30.886 -18.637 -11.455  1.00 30.67           C  
ANISOU 4309  CB  VAL B 140     4741   3481   3432   -181    195    108       C  
ATOM   4310  CG1 VAL B 140     -29.597 -19.372 -11.102  1.00 36.36           C  
ANISOU 4310  CG1 VAL B 140     5520   4170   4126   -141    141    126       C  
ATOM   4311  CG2 VAL B 140     -31.394 -19.040 -12.841  1.00 26.40           C  
ANISOU 4311  CG2 VAL B 140     4155   2938   2936   -189    201     98       C  
ATOM   4312  N   ALA B 141     -33.298 -16.904 -10.452  1.00 23.78           N  
ANISOU 4312  N   ALA B 141     3806   2673   2558   -264    310     80       N  
ATOM   4313  CA  ALA B 141     -34.422 -16.039 -10.780  1.00 21.18           C  
ANISOU 4313  CA  ALA B 141     3409   2378   2260   -288    355     56       C  
ATOM   4314  C   ALA B 141     -34.073 -15.278 -12.048  1.00 22.11           C  
ANISOU 4314  C   ALA B 141     3452   2517   2430   -253    330     38       C  
ATOM   4315  O   ALA B 141     -32.975 -14.725 -12.150  1.00 22.48           O  
ANISOU 4315  O   ALA B 141     3492   2571   2480   -210    291     36       O  
ATOM   4316  CB  ALA B 141     -34.698 -15.060  -9.640  1.00 23.32           C  
ANISOU 4316  CB  ALA B 141     3682   2674   2504   -298    385     45       C  
ATOM   4317  N   VAL B 142     -34.980 -15.259 -13.018  1.00 20.71           N  
ANISOU 4317  N   VAL B 142     3222   2353   2294   -271    350     26       N  
ATOM   4318  CA  VAL B 142     -34.708 -14.586 -14.284  1.00 21.83           C  
ANISOU 4318  CA  VAL B 142     3298   2514   2482   -240    326     11       C  
ATOM   4319  C   VAL B 142     -35.627 -13.382 -14.414  1.00 20.68           C  
ANISOU 4319  C   VAL B 142     3087   2404   2365   -249    358    -12       C  
ATOM   4320  O   VAL B 142     -36.855 -13.519 -14.410  1.00 22.46           O  
ANISOU 4320  O   VAL B 142     3293   2639   2602   -286    398    -19       O  
ATOM   4321  CB  VAL B 142     -34.850 -15.523 -15.489  1.00 19.68           C  
ANISOU 4321  CB  VAL B 142     3016   2226   2236   -245    311     15       C  
ATOM   4322  CG1 VAL B 142     -34.460 -14.758 -16.763  1.00 20.47           C  
ANISOU 4322  CG1 VAL B 142     3052   2348   2378   -211    285      1       C  
ATOM   4323  CG2 VAL B 142     -33.971 -16.748 -15.290  1.00 16.95           C  
ANISOU 4323  CG2 VAL B 142     2739   1841   1862   -233    280     36       C  
ATOM   4324  N   LEU B 143     -35.013 -12.214 -14.554  1.00 20.52           N  
ANISOU 4324  N   LEU B 143     3035   2403   2359   -215    339    -23       N  
ATOM   4325  CA  LEU B 143     -35.685 -10.938 -14.724  1.00 19.49           C  
ANISOU 4325  CA  LEU B 143     2845   2303   2258   -213    360    -45       C  
ATOM   4326  C   LEU B 143     -35.524 -10.505 -16.174  1.00 20.77           C  
ANISOU 4326  C   LEU B 143     2951   2476   2465   -190    333    -52       C  
ATOM   4327  O   LEU B 143     -34.422 -10.583 -16.723  1.00 17.29           O  
ANISOU 4327  O   LEU B 143     2515   2028   2025   -161    294    -44       O  
ATOM   4328  CB  LEU B 143     -35.072  -9.900 -13.780  1.00 20.42           C  
ANISOU 4328  CB  LEU B 143     2974   2430   2355   -192    356    -53       C  
ATOM   4329  CG  LEU B 143     -35.362  -8.417 -13.993  1.00 21.70           C  
ANISOU 4329  CG  LEU B 143     3081   2617   2547   -176    363    -76       C  
ATOM   4330  CD1 LEU B 143     -36.763  -8.091 -13.546  1.00 24.97           C  
ANISOU 4330  CD1 LEU B 143     3470   3047   2969   -204    414    -94       C  
ATOM   4331  CD2 LEU B 143     -34.366  -7.577 -13.214  1.00 27.72           C  
ANISOU 4331  CD2 LEU B 143     3865   3381   3288   -152    344    -80       C  
ATOM   4332  N   LEU B 144     -36.616 -10.076 -16.803  1.00 21.34           N  
ANISOU 4332  N   LEU B 144     2970   2567   2573   -203    354    -67       N  
ATOM   4333  CA  LEU B 144     -36.563  -9.555 -18.164  1.00 17.28           C  
ANISOU 4333  CA  LEU B 144     2402   2064   2098   -182    330    -73       C  
ATOM   4334  C   LEU B 144     -36.820  -8.057 -18.127  1.00 19.71           C  
ANISOU 4334  C   LEU B 144     2666   2394   2429   -165    336    -90       C  
ATOM   4335  O   LEU B 144     -37.771  -7.599 -17.484  1.00 19.62           O  
ANISOU 4335  O   LEU B 144     2639   2394   2421   -180    371   -105       O  
ATOM   4336  CB  LEU B 144     -37.577 -10.245 -19.080  1.00 21.34           C  
ANISOU 4336  CB  LEU B 144     2888   2581   2638   -207    340    -75       C  
ATOM   4337  CG  LEU B 144     -37.400 -11.728 -19.383  1.00 18.89           C  
ANISOU 4337  CG  LEU B 144     2617   2247   2313   -225    331    -60       C  
ATOM   4338  CD1 LEU B 144     -38.157 -12.064 -20.647  1.00 24.29           C  
ANISOU 4338  CD1 LEU B 144     3261   2938   3031   -238    326    -67       C  
ATOM   4339  CD2 LEU B 144     -35.939 -12.082 -19.537  1.00 21.48           C  
ANISOU 4339  CD2 LEU B 144     2982   2557   2623   -194    291    -46       C  
ATOM   4340  N   MET B 145     -35.975  -7.304 -18.819  1.00 18.32           N  
ANISOU 4340  N   MET B 145     2471   2221   2267   -134    302    -89       N  
ATOM   4341  CA  MET B 145     -35.949  -5.852 -18.726  1.00 18.45           C  
ANISOU 4341  CA  MET B 145     2458   2250   2301   -115    300   -103       C  
ATOM   4342  C   MET B 145     -36.013  -5.260 -20.125  1.00 18.34           C  
ANISOU 4342  C   MET B 145     2397   2245   2325    -99    277   -104       C  
ATOM   4343  O   MET B 145     -35.165  -5.562 -20.971  1.00 18.15           O  
ANISOU 4343  O   MET B 145     2376   2218   2303    -87    246    -92       O  
ATOM   4344  CB  MET B 145     -34.687  -5.392 -17.990  1.00 17.31           C  
ANISOU 4344  CB  MET B 145     2348   2099   2131    -95    281    -99       C  
ATOM   4345  CG  MET B 145     -34.360  -3.946 -18.123  1.00 20.11           C  
ANISOU 4345  CG  MET B 145     2676   2461   2504    -73    268   -110       C  
ATOM   4346  SD  MET B 145     -33.026  -3.483 -16.963  1.00 31.65           S  
ANISOU 4346  SD  MET B 145     4180   3915   3929    -59    251   -109       S  
ATOM   4347  CE  MET B 145     -33.849  -3.744 -15.392  1.00 27.08           C  
ANISOU 4347  CE  MET B 145     3636   3335   3317    -81    295   -120       C  
ATOM   4348  N   ASP B 146     -37.013  -4.422 -20.360  1.00 15.89           N  
ANISOU 4348  N   ASP B 146     2044   1949   2046    -98    291   -119       N  
ATOM   4349  CA  ASP B 146     -37.243  -3.770 -21.637  1.00 16.68           C  
ANISOU 4349  CA  ASP B 146     2100   2057   2181    -83    269   -121       C  
ATOM   4350  C   ASP B 146     -37.020  -2.273 -21.455  1.00 15.87           C  
ANISOU 4350  C   ASP B 146     1982   1955   2092    -60    261   -130       C  
ATOM   4351  O   ASP B 146     -37.384  -1.713 -20.415  1.00 17.18           O  
ANISOU 4351  O   ASP B 146     2152   2121   2253    -60    286   -145       O  
ATOM   4352  CB  ASP B 146     -38.661  -4.069 -22.128  1.00 14.09           C  
ANISOU 4352  CB  ASP B 146     1733   1740   1880   -100    287   -130       C  
ATOM   4353  CG  ASP B 146     -38.882  -3.664 -23.576  1.00 17.49           C  
ANISOU 4353  CG  ASP B 146     2124   2179   2343    -87    258   -128       C  
ATOM   4354  OD1 ASP B 146     -37.879  -3.516 -24.321  1.00 14.80           O  
ANISOU 4354  OD1 ASP B 146     1793   1833   1998    -72    227   -114       O  
ATOM   4355  OD2 ASP B 146     -40.064  -3.511 -23.969  1.00 15.04           O  
ANISOU 4355  OD2 ASP B 146     1773   1881   2061    -93    268   -139       O  
ATOM   4356  N   THR B 147     -36.380  -1.624 -22.438  1.00 14.42           N  
ANISOU 4356  N   THR B 147     1785   1771   1924    -42    229   -122       N  
ATOM   4357  CA  THR B 147     -35.894  -0.265 -22.236  1.00 16.97           C  
ANISOU 4357  CA  THR B 147     2104   2088   2254    -22    217   -127       C  
ATOM   4358  C   THR B 147     -36.363   0.695 -23.322  1.00 15.55           C  
ANISOU 4358  C   THR B 147     1886   1911   2111     -7    198   -128       C  
ATOM   4359  O   THR B 147     -36.668   0.318 -24.460  1.00 14.06           O  
ANISOU 4359  O   THR B 147     1677   1729   1937    -10    184   -119       O  
ATOM   4360  CB  THR B 147     -34.367  -0.203 -22.200  1.00 15.00           C  
ANISOU 4360  CB  THR B 147     1884   1832   1983    -15    191   -114       C  
ATOM   4361  OG1 THR B 147     -33.874  -0.464 -23.518  1.00 12.13           O  
ANISOU 4361  OG1 THR B 147     1508   1473   1628    -11    164    -99       O  
ATOM   4362  CG2 THR B 147     -33.819  -1.227 -21.209  1.00 13.75           C  
ANISOU 4362  CG2 THR B 147     1766   1670   1788    -25    202   -111       C  
ATOM   4363  N   GLN B 148     -36.399   1.962 -22.935  1.00 14.40           N  
ANISOU 4363  N   GLN B 148     1735   1757   1978      8    197   -139       N  
ATOM   4364  CA  GLN B 148     -36.644   3.037 -23.874  1.00 15.33           C  
ANISOU 4364  CA  GLN B 148     1826   1870   2127     25    174   -137       C  
ATOM   4365  C   GLN B 148     -35.521   3.096 -24.899  1.00 14.59           C  
ANISOU 4365  C   GLN B 148     1742   1775   2027     26    141   -115       C  
ATOM   4366  O   GLN B 148     -34.346   3.186 -24.529  1.00 16.32           O  
ANISOU 4366  O   GLN B 148     1987   1989   2225     25    132   -108       O  
ATOM   4367  CB  GLN B 148     -36.729   4.346 -23.105  1.00 14.56           C  
ANISOU 4367  CB  GLN B 148     1732   1760   2040     42    180   -154       C  
ATOM   4368  CG  GLN B 148     -36.935   5.547 -23.971  1.00 14.86           C  
ANISOU 4368  CG  GLN B 148     1750   1787   2110     61    154   -151       C  
ATOM   4369  CD  GLN B 148     -36.939   6.810 -23.138  1.00 20.43           C  
ANISOU 4369  CD  GLN B 148     2464   2473   2824     77    159   -170       C  
ATOM   4370  OE1 GLN B 148     -37.495   6.827 -22.044  1.00 14.95           O  
ANISOU 4370  OE1 GLN B 148     1772   1781   2126     79    190   -193       O  
ATOM   4371  NE2 GLN B 148     -36.310   7.869 -23.646  1.00 19.52           N  
ANISOU 4371  NE2 GLN B 148     2357   2339   2719     88    130   -160       N  
ATOM   4372  N   GLY B 149     -35.872   3.020 -26.182  1.00 15.16           N  
ANISOU 4372  N   GLY B 149     1792   1853   2117     28    122   -103       N  
ATOM   4373  CA  GLY B 149     -34.857   3.160 -27.213  1.00 12.81           C  
ANISOU 4373  CA  GLY B 149     1501   1556   1812     28     93    -83       C  
ATOM   4374  C   GLY B 149     -34.140   4.500 -27.114  1.00 14.81           C  
ANISOU 4374  C   GLY B 149     1764   1793   2069     37     77    -80       C  
ATOM   4375  O   GLY B 149     -34.737   5.527 -26.780  1.00 13.66           O  
ANISOU 4375  O   GLY B 149     1611   1635   1945     50     79    -91       O  
ATOM   4376  N   THR B 150     -32.843   4.484 -27.404  1.00 12.28           N  
ANISOU 4376  N   THR B 150     1460   1474   1730     31     62    -67       N  
ATOM   4377  CA  THR B 150     -32.065   5.711 -27.364  1.00 13.84           C  
ANISOU 4377  CA  THR B 150     1669   1658   1931     33     47    -62       C  
ATOM   4378  C   THR B 150     -32.411   6.587 -28.562  1.00 13.49           C  
ANISOU 4378  C   THR B 150     1611   1605   1908     39     25    -49       C  
ATOM   4379  O   THR B 150     -32.905   6.111 -29.593  1.00 15.15           O  
ANISOU 4379  O   THR B 150     1807   1827   2123     38     16    -39       O  
ATOM   4380  CB  THR B 150     -30.562   5.403 -27.358  1.00 15.20           C  
ANISOU 4380  CB  THR B 150     1858   1838   2078     22     38    -53       C  
ATOM   4381  OG1 THR B 150     -30.233   4.523 -28.447  1.00 13.77           O  
ANISOU 4381  OG1 THR B 150     1670   1675   1887     15     30    -38       O  
ATOM   4382  CG2 THR B 150     -30.158   4.745 -26.055  1.00 13.60           C  
ANISOU 4382  CG2 THR B 150     1674   1638   1854     20     54    -65       C  
ATOM   4383  N   PHE B 151     -32.185   7.894 -28.391  1.00 12.96           N  
ANISOU 4383  N   PHE B 151     1553   1517   1853     44     14    -49       N  
ATOM   4384  CA  PHE B 151     -32.212   8.872 -29.469  1.00 15.39           C  
ANISOU 4384  CA  PHE B 151     1859   1811   2176     47    -12    -32       C  
ATOM   4385  C   PHE B 151     -33.612   9.127 -30.021  1.00 15.82           C  
ANISOU 4385  C   PHE B 151     1893   1861   2258     65    -19    -34       C  
ATOM   4386  O   PHE B 151     -33.766   9.530 -31.186  1.00 14.80           O  
ANISOU 4386  O   PHE B 151     1760   1727   2136     67    -43    -15       O  
ATOM   4387  CB  PHE B 151     -31.249   8.471 -30.590  1.00 15.29           C  
ANISOU 4387  CB  PHE B 151     1851   1816   2144     29    -26     -8       C  
ATOM   4388  CG  PHE B 151     -29.839   8.292 -30.117  1.00 15.32           C  
ANISOU 4388  CG  PHE B 151     1869   1827   2125     13    -22     -8       C  
ATOM   4389  CD1 PHE B 151     -29.162   9.343 -29.557  1.00 17.85           C  
ANISOU 4389  CD1 PHE B 151     2205   2129   2448      7    -27    -10       C  
ATOM   4390  CD2 PHE B 151     -29.206   7.074 -30.222  1.00 20.08           C  
ANISOU 4390  CD2 PHE B 151     2469   2455   2704      5    -14     -7       C  
ATOM   4391  CE1 PHE B 151     -27.864   9.188 -29.109  1.00 19.91           C  
ANISOU 4391  CE1 PHE B 151     2476   2401   2689     -8    -26    -11       C  
ATOM   4392  CE2 PHE B 151     -27.909   6.918 -29.782  1.00 22.73           C  
ANISOU 4392  CE2 PHE B 151     2814   2800   3022     -6    -13     -8       C  
ATOM   4393  CZ  PHE B 151     -27.243   7.975 -29.226  1.00 19.57           C  
ANISOU 4393  CZ  PHE B 151     2426   2385   2625    -13    -19    -10       C  
ATOM   4394  N   ASP B 152     -34.651   8.933 -29.210  1.00 14.46           N  
ANISOU 4394  N   ASP B 152     1706   1689   2101     79      0    -56       N  
ATOM   4395  CA  ASP B 152     -35.930   9.447 -29.678  1.00 17.53           C  
ANISOU 4395  CA  ASP B 152     2071   2069   2520    101    -10    -61       C  
ATOM   4396  C   ASP B 152     -35.937  10.957 -29.485  1.00 19.30           C  
ANISOU 4396  C   ASP B 152     2308   2260   2766    118    -25    -63       C  
ATOM   4397  O   ASP B 152     -35.125  11.511 -28.744  1.00 20.13           O  
ANISOU 4397  O   ASP B 152     2438   2350   2862    112    -20    -68       O  
ATOM   4398  CB  ASP B 152     -37.117   8.763 -28.985  1.00 16.09           C  
ANISOU 4398  CB  ASP B 152     1861   1901   2350    109     16    -86       C  
ATOM   4399  CG  ASP B 152     -37.266   9.130 -27.515  1.00 17.73           C  
ANISOU 4399  CG  ASP B 152     2077   2099   2561    116     44   -112       C  
ATOM   4400  OD1 ASP B 152     -37.146  10.309 -27.132  1.00 18.45           O  
ANISOU 4400  OD1 ASP B 152     2180   2165   2664    131     37   -120       O  
ATOM   4401  OD2 ASP B 152     -37.574   8.217 -26.732  1.00 16.15           O  
ANISOU 4401  OD2 ASP B 152     1871   1916   2349    107     74   -127       O  
ATOM   4402  N   SER B 153     -36.832  11.635 -30.182  1.00 21.44           N  
ANISOU 4402  N   SER B 153     2565   2518   3065    139    -47    -60       N  
ATOM   4403  CA  SER B 153     -36.741  13.086 -30.194  1.00 21.91           C  
ANISOU 4403  CA  SER B 153     2642   2539   3142    155    -68    -57       C  
ATOM   4404  C   SER B 153     -37.519  13.747 -29.074  1.00 22.54           C  
ANISOU 4404  C   SER B 153     2715   2602   3247    182    -52    -90       C  
ATOM   4405  O   SER B 153     -37.736  14.955 -29.132  1.00 19.23           O  
ANISOU 4405  O   SER B 153     2308   2149   2851    203    -71    -92       O  
ATOM   4406  CB  SER B 153     -37.191  13.636 -31.545  1.00 21.25           C  
ANISOU 4406  CB  SER B 153     2555   2444   3074    167   -106    -33       C  
ATOM   4407  OG  SER B 153     -36.151  13.439 -32.495  1.00 31.28           O  
ANISOU 4407  OG  SER B 153     3846   3721   4317    139   -122     -2       O  
ATOM   4408  N   GLN B 154     -37.942  12.990 -28.067  1.00 19.85           N  
ANISOU 4408  N   GLN B 154     2358   2282   2902    181    -16   -116       N  
ATOM   4409  CA  GLN B 154     -38.457  13.550 -26.829  1.00 20.23           C  
ANISOU 4409  CA  GLN B 154     2405   2317   2965    200      7   -150       C  
ATOM   4410  C   GLN B 154     -37.403  13.588 -25.735  1.00 20.41           C  
ANISOU 4410  C   GLN B 154     2461   2334   2959    182     26   -159       C  
ATOM   4411  O   GLN B 154     -37.663  14.134 -24.663  1.00 23.48           O  
ANISOU 4411  O   GLN B 154     2857   2710   3354    195     45   -188       O  
ATOM   4412  CB  GLN B 154     -39.659  12.737 -26.325  1.00 21.19           C  
ANISOU 4412  CB  GLN B 154     2488   2467   3097    209     38   -176       C  
ATOM   4413  CG  GLN B 154     -40.744  12.509 -27.360  1.00 25.38           C  
ANISOU 4413  CG  GLN B 154     2978   3010   3654    224     21   -170       C  
ATOM   4414  CD  GLN B 154     -41.276  13.813 -27.905  1.00 35.67           C  
ANISOU 4414  CD  GLN B 154     4277   4283   4994    260    -13   -170       C  
ATOM   4415  OE1 GLN B 154     -41.580  14.737 -27.143  1.00 42.54           O  
ANISOU 4415  OE1 GLN B 154     5151   5129   5883    285     -5   -195       O  
ATOM   4416  NE2 GLN B 154     -41.379  13.908 -29.228  1.00 34.78           N  
ANISOU 4416  NE2 GLN B 154     4158   4167   4888    264    -51   -142       N  
ATOM   4417  N   SER B 155     -36.224  13.022 -25.981  1.00 17.08           N  
ANISOU 4417  N   SER B 155     2059   1923   2506    152     21   -137       N  
ATOM   4418  CA  SER B 155     -35.275  12.705 -24.927  1.00 16.98           C  
ANISOU 4418  CA  SER B 155     2072   1916   2464    133     39   -146       C  
ATOM   4419  C   SER B 155     -33.987  13.495 -25.088  1.00 19.56           C  
ANISOU 4419  C   SER B 155     2431   2222   2780    117     16   -131       C  
ATOM   4420  O   SER B 155     -33.500  13.707 -26.205  1.00 18.44           O  
ANISOU 4420  O   SER B 155     2291   2076   2639    108     -9   -103       O  
ATOM   4421  CB  SER B 155     -34.952  11.203 -24.924  1.00 19.50           C  
ANISOU 4421  CB  SER B 155     2384   2270   2754    111     55   -137       C  
ATOM   4422  OG  SER B 155     -36.128  10.443 -24.700  1.00 19.47           O  
ANISOU 4422  OG  SER B 155     2354   2286   2759    119     79   -152       O  
ATOM   4423  N   THR B 156     -33.433  13.914 -23.961  1.00 16.85           N  
ANISOU 4423  N   THR B 156     2111   1867   2424    113     27   -149       N  
ATOM   4424  CA  THR B 156     -32.079  14.427 -23.973  1.00 17.29           C  
ANISOU 4424  CA  THR B 156     2195   1911   2465     91      8   -137       C  
ATOM   4425  C   THR B 156     -31.090  13.270 -24.071  1.00 16.39           C  
ANISOU 4425  C   THR B 156     2080   1830   2319     66     11   -122       C  
ATOM   4426  O   THR B 156     -31.427  12.092 -23.877  1.00 15.77           O  
ANISOU 4426  O   THR B 156     1988   1778   2227     66     30   -125       O  
ATOM   4427  CB  THR B 156     -31.794  15.237 -22.712  1.00 17.08           C  
ANISOU 4427  CB  THR B 156     2194   1862   2434     93     15   -165       C  
ATOM   4428  OG1 THR B 156     -31.954  14.380 -21.564  1.00 16.45           O  
ANISOU 4428  OG1 THR B 156     2114   1804   2331     92     45   -186       O  
ATOM   4429  CG2 THR B 156     -32.743  16.432 -22.616  1.00 18.91           C  
ANISOU 4429  CG2 THR B 156     2428   2057   2699    121     11   -183       C  
ATOM   4430  N   LEU B 157     -29.852  13.618 -24.393  1.00 15.64           N  
ANISOU 4430  N   LEU B 157     1999   1731   2212     44     -7   -106       N  
ATOM   4431  CA  LEU B 157     -28.800  12.615 -24.390  1.00 17.02           C  
ANISOU 4431  CA  LEU B 157     2172   1935   2358     23     -6    -96       C  
ATOM   4432  C   LEU B 157     -28.668  11.988 -23.012  1.00 14.32           C  
ANISOU 4432  C   LEU B 157     1841   1606   1994     24     13   -119       C  
ATOM   4433  O   LEU B 157     -28.437  10.779 -22.885  1.00 14.99           O  
ANISOU 4433  O   LEU B 157     1920   1717   2058     20     23   -115       O  
ATOM   4434  CB  LEU B 157     -27.483  13.250 -24.834  1.00 17.12           C  
ANISOU 4434  CB  LEU B 157     2197   1944   2365     -1    -28    -81       C  
ATOM   4435  CG  LEU B 157     -26.300  12.288 -24.899  1.00 20.28           C  
ANISOU 4435  CG  LEU B 157     2590   2376   2738    -20    -29    -72       C  
ATOM   4436  CD1 LEU B 157     -26.565  11.142 -25.885  1.00 19.70           C  
ANISOU 4436  CD1 LEU B 157     2495   2330   2659    -16    -24    -55       C  
ATOM   4437  CD2 LEU B 157     -25.045  13.052 -25.258  1.00 22.01           C  
ANISOU 4437  CD2 LEU B 157     2816   2592   2955    -46    -48    -61       C  
ATOM   4438  N   ARG B 158     -28.834  12.792 -21.962  1.00 15.37           N  
ANISOU 4438  N   ARG B 158     1993   1717   2129     31     19   -142       N  
ATOM   4439  CA  ARG B 158     -28.747  12.251 -20.614  1.00 14.91           C  
ANISOU 4439  CA  ARG B 158     1950   1670   2046     31     37   -164       C  
ATOM   4440  C   ARG B 158     -29.876  11.268 -20.339  1.00 12.35           C  
ANISOU 4440  C   ARG B 158     1612   1361   1718     44     66   -171       C  
ATOM   4441  O   ARG B 158     -29.656  10.251 -19.675  1.00 15.79           O  
ANISOU 4441  O   ARG B 158     2056   1816   2126     38     79   -174       O  
ATOM   4442  CB  ARG B 158     -28.763  13.377 -19.585  1.00 15.46           C  
ANISOU 4442  CB  ARG B 158     2044   1712   2118     35     38   -190       C  
ATOM   4443  CG  ARG B 158     -28.745  12.873 -18.153  1.00 15.16           C  
ANISOU 4443  CG  ARG B 158     2026   1685   2050     35     58   -214       C  
ATOM   4444  CD  ARG B 158     -28.631  14.041 -17.181  1.00 18.26           C  
ANISOU 4444  CD  ARG B 158     2446   2051   2442     37     56   -242       C  
ATOM   4445  NE  ARG B 158     -28.559  13.577 -15.801  1.00 20.99           N  
ANISOU 4445  NE  ARG B 158     2815   2407   2753     36     74   -264       N  
ATOM   4446  CZ  ARG B 158     -28.266  14.354 -14.766  1.00 24.49           C  
ANISOU 4446  CZ  ARG B 158     3288   2834   3184     33     72   -290       C  
ATOM   4447  NH1 ARG B 158     -28.056  15.652 -14.914  1.00 19.27           N  
ANISOU 4447  NH1 ARG B 158     2637   2141   2544     33     54   -299       N  
ATOM   4448  NH2 ARG B 158     -28.173  13.812 -13.552  1.00 21.89           N  
ANISOU 4448  NH2 ARG B 158     2982   2519   2817     30     87   -307       N  
ATOM   4449  N   ASP B 159     -31.089  11.555 -20.831  1.00 12.43           N  
ANISOU 4449  N   ASP B 159     1603   1363   1757     62     74   -175       N  
ATOM   4450  CA  ASP B 159     -32.178  10.581 -20.741  1.00 16.50           C  
ANISOU 4450  CA  ASP B 159     2099   1897   2273     70    100   -180       C  
ATOM   4451  C   ASP B 159     -31.754   9.245 -21.351  1.00 16.78           C  
ANISOU 4451  C   ASP B 159     2127   1959   2291     56     98   -158       C  
ATOM   4452  O   ASP B 159     -31.858   8.186 -20.715  1.00 13.93           O  
ANISOU 4452  O   ASP B 159     1772   1614   1907     49    117   -162       O  
ATOM   4453  CB  ASP B 159     -33.430  11.074 -21.476  1.00 15.55           C  
ANISOU 4453  CB  ASP B 159     1951   1768   2189     90    101   -183       C  
ATOM   4454  CG  ASP B 159     -34.092  12.286 -20.837  1.00 18.66           C  
ANISOU 4454  CG  ASP B 159     2349   2136   2604    110    108   -210       C  
ATOM   4455  OD1 ASP B 159     -33.830  12.614 -19.656  1.00 21.67           O  
ANISOU 4455  OD1 ASP B 159     2755   2510   2970    109    122   -233       O  
ATOM   4456  OD2 ASP B 159     -34.920  12.913 -21.545  1.00 20.92           O  
ANISOU 4456  OD2 ASP B 159     2615   2409   2925    130     99   -210       O  
ATOM   4457  N   SER B 160     -31.293   9.284 -22.607  1.00 15.87           N  
ANISOU 4457  N   SER B 160     1999   1845   2184     51     74   -134       N  
ATOM   4458  CA  SER B 160     -30.934   8.055 -23.309  1.00 15.02           C  
ANISOU 4458  CA  SER B 160     1883   1761   2063     40     71   -115       C  
ATOM   4459  C   SER B 160     -29.764   7.367 -22.629  1.00 16.06           C  
ANISOU 4459  C   SER B 160     2035   1905   2162     28     69   -114       C  
ATOM   4460  O   SER B 160     -29.746   6.136 -22.503  1.00 15.80           O  
ANISOU 4460  O   SER B 160     2004   1887   2111     25     79   -110       O  
ATOM   4461  CB  SER B 160     -30.593   8.357 -24.770  1.00 16.73           C  
ANISOU 4461  CB  SER B 160     2086   1978   2292     37     46    -92       C  
ATOM   4462  OG  SER B 160     -31.719   8.835 -25.484  1.00 17.51           O  
ANISOU 4462  OG  SER B 160     2166   2068   2420     50     43    -90       O  
ATOM   4463  N   ALA B 161     -28.771   8.147 -22.184  1.00 15.44           N  
ANISOU 4463  N   ALA B 161     1973   1817   2076     22     55   -117       N  
ATOM   4464  CA  ALA B 161     -27.621   7.545 -21.517  1.00 13.55           C  
ANISOU 4464  CA  ALA B 161     1750   1590   1807     13     49   -117       C  
ATOM   4465  C   ALA B 161     -28.026   6.918 -20.192  1.00 14.95           C  
ANISOU 4465  C   ALA B 161     1948   1769   1962     17     70   -134       C  
ATOM   4466  O   ALA B 161     -27.567   5.823 -19.846  1.00 13.99           O  
ANISOU 4466  O   ALA B 161     1838   1663   1816     14     71   -129       O  
ATOM   4467  CB  ALA B 161     -26.522   8.588 -21.309  1.00 13.18           C  
ANISOU 4467  CB  ALA B 161     1714   1534   1760      3     28   -120       C  
ATOM   4468  N   THR B 162     -28.902   7.578 -19.445  1.00 12.80           N  
ANISOU 4468  N   THR B 162     1684   1483   1697     24     88   -154       N  
ATOM   4469  CA  THR B 162     -29.287   7.019 -18.159  1.00 15.99           C  
ANISOU 4469  CA  THR B 162     2110   1891   2076     24    112   -170       C  
ATOM   4470  C   THR B 162     -30.015   5.692 -18.348  1.00 14.24           C  
ANISOU 4470  C   THR B 162     1881   1683   1847     22    132   -161       C  
ATOM   4471  O   THR B 162     -29.751   4.721 -17.629  1.00 14.14           O  
ANISOU 4471  O   THR B 162     1891   1679   1804     16    139   -160       O  
ATOM   4472  CB  THR B 162     -30.140   8.028 -17.385  1.00 16.34           C  
ANISOU 4472  CB  THR B 162     2160   1919   2130     32    130   -196       C  
ATOM   4473  OG1 THR B 162     -29.403   9.252 -17.251  1.00 17.26           O  
ANISOU 4473  OG1 THR B 162     2287   2017   2253     32    109   -203       O  
ATOM   4474  CG2 THR B 162     -30.473   7.493 -16.012  1.00 15.98           C  
ANISOU 4474  CG2 THR B 162     2141   1879   2052     29    157   -213       C  
ATOM   4475  N   VAL B 163     -30.903   5.611 -19.340  1.00 14.63           N  
ANISOU 4475  N   VAL B 163     1901   1735   1924     26    137   -155       N  
ATOM   4476  CA  VAL B 163     -31.633   4.364 -19.549  1.00 14.04           C  
ANISOU 4476  CA  VAL B 163     1818   1673   1844     21    156   -148       C  
ATOM   4477  C   VAL B 163     -30.670   3.268 -19.969  1.00 16.59           C  
ANISOU 4477  C   VAL B 163     2151   2006   2148     14    139   -129       C  
ATOM   4478  O   VAL B 163     -30.667   2.171 -19.404  1.00 12.37           O  
ANISOU 4478  O   VAL B 163     1635   1476   1588      8    150   -127       O  
ATOM   4479  CB  VAL B 163     -32.763   4.551 -20.583  1.00 15.41           C  
ANISOU 4479  CB  VAL B 163     1955   1848   2053     27    161   -147       C  
ATOM   4480  CG1 VAL B 163     -33.309   3.188 -21.030  1.00 13.28           C  
ANISOU 4480  CG1 VAL B 163     1675   1591   1778     17    172   -137       C  
ATOM   4481  CG2 VAL B 163     -33.878   5.420 -20.012  1.00 15.11           C  
ANISOU 4481  CG2 VAL B 163     1906   1802   2034     37    183   -171       C  
ATOM   4482  N   PHE B 164     -29.816   3.561 -20.949  1.00 14.28           N  
ANISOU 4482  N   PHE B 164     1845   1715   1864     16    112   -115       N  
ATOM   4483  CA  PHE B 164     -28.851   2.565 -21.405  1.00 13.10           C  
ANISOU 4483  CA  PHE B 164     1702   1578   1699     13     96   -100       C  
ATOM   4484  C   PHE B 164     -27.883   2.172 -20.287  1.00 14.09           C  
ANISOU 4484  C   PHE B 164     1858   1704   1792     13     89   -104       C  
ATOM   4485  O   PHE B 164     -27.653   0.983 -20.042  1.00 15.30           O  
ANISOU 4485  O   PHE B 164     2028   1862   1924     13     90    -98       O  
ATOM   4486  CB  PHE B 164     -28.096   3.094 -22.622  1.00 11.94           C  
ANISOU 4486  CB  PHE B 164     1535   1436   1567     14     71    -88       C  
ATOM   4487  CG  PHE B 164     -27.457   2.008 -23.438  1.00 18.24           C  
ANISOU 4487  CG  PHE B 164     2328   2248   2355     14     60    -74       C  
ATOM   4488  CD1 PHE B 164     -26.287   1.391 -23.003  1.00 12.00           C  
ANISOU 4488  CD1 PHE B 164     1552   1466   1542     16     48    -73       C  
ATOM   4489  CD2 PHE B 164     -28.032   1.594 -24.627  1.00 12.93           C  
ANISOU 4489  CD2 PHE B 164     1635   1581   1696     13     61    -65       C  
ATOM   4490  CE1 PHE B 164     -25.701   0.389 -23.748  1.00 14.11           C  
ANISOU 4490  CE1 PHE B 164     1814   1745   1802     20     39    -64       C  
ATOM   4491  CE2 PHE B 164     -27.445   0.599 -25.385  1.00 14.98           C  
ANISOU 4491  CE2 PHE B 164     1892   1853   1946     14     52    -56       C  
ATOM   4492  CZ  PHE B 164     -26.277  -0.008 -24.939  1.00 12.50           C  
ANISOU 4492  CZ  PHE B 164     1593   1546   1611     18     42    -56       C  
ATOM   4493  N   ALA B 165     -27.325   3.153 -19.579  1.00 13.39           N  
ANISOU 4493  N   ALA B 165     1780   1610   1699     13     80   -114       N  
ATOM   4494  CA  ALA B 165     -26.399   2.828 -18.497  1.00 15.16           C  
ANISOU 4494  CA  ALA B 165     2033   1836   1891     13     70   -118       C  
ATOM   4495  C   ALA B 165     -27.075   1.976 -17.428  1.00 16.01           C  
ANISOU 4495  C   ALA B 165     2170   1939   1973     11     93   -123       C  
ATOM   4496  O   ALA B 165     -26.557   0.925 -17.038  1.00 14.56           O  
ANISOU 4496  O   ALA B 165     2009   1759   1763     13     86   -115       O  
ATOM   4497  CB  ALA B 165     -25.826   4.106 -17.889  1.00 14.90           C  
ANISOU 4497  CB  ALA B 165     2007   1795   1858     11     57   -131       C  
ATOM   4498  N   LEU B 166     -28.245   2.406 -16.951  1.00 13.19           N  
ANISOU 4498  N   LEU B 166     1815   1575   1622      8    122   -137       N  
ATOM   4499  CA  LEU B 166     -28.932   1.662 -15.900  1.00 13.38           C  
ANISOU 4499  CA  LEU B 166     1868   1598   1619      1    149   -142       C  
ATOM   4500  C   LEU B 166     -29.241   0.240 -16.341  1.00 15.62           C  
ANISOU 4500  C   LEU B 166     2154   1885   1896     -4    156   -126       C  
ATOM   4501  O   LEU B 166     -29.021  -0.712 -15.585  1.00 14.89           O  
ANISOU 4501  O   LEU B 166     2097   1791   1771     -9    159   -120       O  
ATOM   4502  CB  LEU B 166     -30.222   2.388 -15.491  1.00 12.94           C  
ANISOU 4502  CB  LEU B 166     1803   1538   1577     -1    182   -162       C  
ATOM   4503  CG  LEU B 166     -29.928   3.593 -14.593  1.00 22.01           C  
ANISOU 4503  CG  LEU B 166     2966   2678   2717      3    180   -182       C  
ATOM   4504  CD1 LEU B 166     -31.195   4.420 -14.317  1.00 18.42           C  
ANISOU 4504  CD1 LEU B 166     2497   2218   2282      6    212   -205       C  
ATOM   4505  CD2 LEU B 166     -29.301   3.089 -13.290  1.00 18.28           C  
ANISOU 4505  CD2 LEU B 166     2541   2208   2198     -3    178   -185       C  
ATOM   4506  N   SER B 167     -29.737   0.070 -17.566  1.00 14.23           N  
ANISOU 4506  N   SER B 167     1944   1712   1749     -4    157   -119       N  
ATOM   4507  CA  SER B 167     -30.071  -1.280 -18.008  1.00 15.13           C  
ANISOU 4507  CA  SER B 167     2062   1828   1858    -11    163   -106       C  
ATOM   4508  C   SER B 167     -28.818  -2.142 -18.110  1.00 14.81           C  
ANISOU 4508  C   SER B 167     2042   1787   1797     -3    135    -92       C  
ATOM   4509  O   SER B 167     -28.845  -3.326 -17.748  1.00 16.69           O  
ANISOU 4509  O   SER B 167     2308   2019   2013     -8    140    -84       O  
ATOM   4510  CB  SER B 167     -30.837  -1.236 -19.333  1.00 14.88           C  
ANISOU 4510  CB  SER B 167     1990   1801   1861    -12    167   -102       C  
ATOM   4511  OG  SER B 167     -30.057  -0.700 -20.381  1.00 16.17           O  
ANISOU 4511  OG  SER B 167     2131   1969   2043     -1    139    -95       O  
ATOM   4512  N   THR B 168     -27.699  -1.554 -18.544  1.00 13.23           N  
ANISOU 4512  N   THR B 168     1829   1593   1604      9    106    -90       N  
ATOM   4513  CA  THR B 168     -26.444  -2.301 -18.604  1.00 15.35           C  
ANISOU 4513  CA  THR B 168     2111   1865   1855     20     78    -81       C  
ATOM   4514  C   THR B 168     -25.936  -2.644 -17.207  1.00 16.43           C  
ANISOU 4514  C   THR B 168     2291   1995   1955     22     72    -83       C  
ATOM   4515  O   THR B 168     -25.470  -3.766 -16.966  1.00 14.59           O  
ANISOU 4515  O   THR B 168     2085   1758   1702     29     61    -73       O  
ATOM   4516  CB  THR B 168     -25.384  -1.486 -19.348  1.00 14.72           C  
ANISOU 4516  CB  THR B 168     2004   1798   1792     28     52    -81       C  
ATOM   4517  OG1 THR B 168     -25.881  -1.095 -20.630  1.00 14.36           O  
ANISOU 4517  OG1 THR B 168     1922   1757   1776     24     57    -77       O  
ATOM   4518  CG2 THR B 168     -24.110  -2.282 -19.507  1.00 14.67           C  
ANISOU 4518  CG2 THR B 168     2002   1799   1772     42     25    -74       C  
ATOM   4519  N   MET B 169     -26.008  -1.679 -16.284  1.00 14.55           N  
ANISOU 4519  N   MET B 169     2063   1756   1709     17     78    -95       N  
ATOM   4520  CA  MET B 169     -25.507  -1.870 -14.923  1.00 15.02           C  
ANISOU 4520  CA  MET B 169     2165   1811   1730     19     70    -98       C  
ATOM   4521  C   MET B 169     -26.308  -2.911 -14.165  1.00 14.91           C  
ANISOU 4521  C   MET B 169     2191   1787   1689      9     94    -92       C  
ATOM   4522  O   MET B 169     -25.768  -3.577 -13.275  1.00 19.25           O  
ANISOU 4522  O   MET B 169     2782   2330   2202     12     81    -86       O  
ATOM   4523  CB  MET B 169     -25.553  -0.551 -14.150  1.00 14.10           C  
ANISOU 4523  CB  MET B 169     2052   1695   1612     14     74   -116       C  
ATOM   4524  CG  MET B 169     -24.632   0.505 -14.682  1.00 17.87           C  
ANISOU 4524  CG  MET B 169     2500   2180   2110     19     47   -122       C  
ATOM   4525  SD  MET B 169     -25.362   2.114 -14.329  1.00 19.91           S  
ANISOU 4525  SD  MET B 169     2749   2430   2385     11     67   -144       S  
ATOM   4526  CE  MET B 169     -24.641   2.353 -12.710  1.00 16.08           C  
ANISOU 4526  CE  MET B 169     2310   1943   1857      9     52   -157       C  
ATOM   4527  N   ILE B 170     -27.594  -3.036 -14.475  1.00 15.88           N  
ANISOU 4527  N   ILE B 170     2301   1906   1825     -5    129    -94       N  
ATOM   4528  CA  ILE B 170     -28.448  -3.979 -13.772  1.00 15.92           C  
ANISOU 4528  CA  ILE B 170     2341   1902   1805    -22    158    -89       C  
ATOM   4529  C   ILE B 170     -28.417  -5.354 -14.435  1.00 19.14           C  
ANISOU 4529  C   ILE B 170     2758   2302   2214    -22    151    -71       C  
ATOM   4530  O   ILE B 170     -28.494  -6.378 -13.750  1.00 17.25           O  
ANISOU 4530  O   ILE B 170     2563   2049   1943    -30    156    -60       O  
ATOM   4531  CB  ILE B 170     -29.886  -3.433 -13.696  1.00 16.61           C  
ANISOU 4531  CB  ILE B 170     2408   1993   1910    -39    201   -103       C  
ATOM   4532  CG1 ILE B 170     -29.942  -2.182 -12.812  1.00 21.47           C  
ANISOU 4532  CG1 ILE B 170     3028   2613   2518    -37    211   -124       C  
ATOM   4533  CG2 ILE B 170     -30.848  -4.516 -13.184  1.00 18.46           C  
ANISOU 4533  CG2 ILE B 170     2671   2220   2122    -62    235    -97       C  
ATOM   4534  CD1 ILE B 170     -29.442  -2.414 -11.365  1.00 22.50           C  
ANISOU 4534  CD1 ILE B 170     3214   2738   2597    -41    208   -124       C  
ATOM   4535  N   SER B 171     -28.279  -5.408 -15.751  1.00 18.55           N  
ANISOU 4535  N   SER B 171     2644   2232   2172    -14    139    -67       N  
ATOM   4536  CA  SER B 171     -28.397  -6.685 -16.433  1.00 18.07           C  
ANISOU 4536  CA  SER B 171     2590   2161   2113    -15    136    -54       C  
ATOM   4537  C   SER B 171     -27.109  -7.490 -16.313  1.00 17.72           C  
ANISOU 4537  C   SER B 171     2574   2109   2048      5     99    -43       C  
ATOM   4538  O   SER B 171     -26.010  -6.940 -16.182  1.00 16.65           O  
ANISOU 4538  O   SER B 171     2433   1984   1911     24     71    -47       O  
ATOM   4539  CB  SER B 171     -28.744  -6.462 -17.903  1.00 19.86           C  
ANISOU 4539  CB  SER B 171     2767   2398   2379    -14    135    -56       C  
ATOM   4540  OG  SER B 171     -27.692  -5.767 -18.539  1.00 15.40           O  
ANISOU 4540  OG  SER B 171     2177   1846   1829      6    106    -58       O  
ATOM   4541  N   SER B 172     -27.260  -8.814 -16.338  1.00 18.44           N  
ANISOU 4541  N   SER B 172     2697   2183   2125      2    100    -31       N  
ATOM   4542  CA  SER B 172     -26.125  -9.696 -16.559  1.00 18.01           C  
ANISOU 4542  CA  SER B 172     2662   2120   2062     27     64    -22       C  
ATOM   4543  C   SER B 172     -25.951 -10.036 -18.029  1.00 21.28           C  
ANISOU 4543  C   SER B 172     3040   2539   2506     38     54    -24       C  
ATOM   4544  O   SER B 172     -24.869 -10.471 -18.430  1.00 19.89           O  
ANISOU 4544  O   SER B 172     2863   2364   2330     64     23    -22       O  
ATOM   4545  CB  SER B 172     -26.290 -10.984 -15.745  1.00 16.79           C  
ANISOU 4545  CB  SER B 172     2569   1936   1873     21     65     -8       C  
ATOM   4546  OG  SER B 172     -27.552 -11.585 -16.014  1.00 16.99           O  
ANISOU 4546  OG  SER B 172     2601   1949   1904     -9     99     -4       O  
ATOM   4547  N   ILE B 173     -26.987  -9.832 -18.838  1.00 17.62           N  
ANISOU 4547  N   ILE B 173     2546   2081   2067     19     79    -28       N  
ATOM   4548  CA  ILE B 173     -26.915  -9.986 -20.286  1.00 17.67           C  
ANISOU 4548  CA  ILE B 173     2516   2096   2101     26     71    -31       C  
ATOM   4549  C   ILE B 173     -27.545  -8.754 -20.903  1.00 16.32           C  
ANISOU 4549  C   ILE B 173     2297   1946   1958     15     86    -39       C  
ATOM   4550  O   ILE B 173     -28.747  -8.521 -20.736  1.00 16.98           O  
ANISOU 4550  O   ILE B 173     2375   2028   2050     -7    114    -42       O  
ATOM   4551  CB  ILE B 173     -27.645 -11.241 -20.792  1.00 16.64           C  
ANISOU 4551  CB  ILE B 173     2403   1947   1972     13     82    -26       C  
ATOM   4552  CG1 ILE B 173     -27.105 -12.496 -20.127  1.00 22.89           C  
ANISOU 4552  CG1 ILE B 173     3250   2711   2735     23     67    -15       C  
ATOM   4553  CG2 ILE B 173     -27.466 -11.357 -22.290  1.00 18.79           C  
ANISOU 4553  CG2 ILE B 173     2641   2231   2269     22     71    -31       C  
ATOM   4554  CD1 ILE B 173     -28.030 -13.697 -20.249  1.00 26.56           C  
ANISOU 4554  CD1 ILE B 173     3746   3150   3196      0     84     -9       C  
ATOM   4555  N   GLN B 174     -26.757  -7.989 -21.638  1.00 15.35           N  
ANISOU 4555  N   GLN B 174     2141   1842   1851     30     68    -43       N  
ATOM   4556  CA  GLN B 174     -27.263  -6.815 -22.332  1.00 16.45           C  
ANISOU 4556  CA  GLN B 174     2237   1996   2016     22     76    -49       C  
ATOM   4557  C   GLN B 174     -27.303  -7.131 -23.817  1.00 16.04           C  
ANISOU 4557  C   GLN B 174     2159   1953   1983     25     70    -47       C  
ATOM   4558  O   GLN B 174     -26.266  -7.435 -24.418  1.00 15.37           O  
ANISOU 4558  O   GLN B 174     2069   1876   1896     41     49    -47       O  
ATOM   4559  CB  GLN B 174     -26.392  -5.590 -22.058  1.00 15.20           C  
ANISOU 4559  CB  GLN B 174     2064   1851   1860     32     62    -53       C  
ATOM   4560  CG  GLN B 174     -26.825  -4.354 -22.860  1.00 16.47           C  
ANISOU 4560  CG  GLN B 174     2186   2024   2049     25     67    -56       C  
ATOM   4561  CD  GLN B 174     -28.160  -3.772 -22.385  1.00 18.33           C  
ANISOU 4561  CD  GLN B 174     2418   2252   2294     11     93    -62       C  
ATOM   4562  OE1 GLN B 174     -29.244  -4.284 -22.698  1.00 15.94           O  
ANISOU 4562  OE1 GLN B 174     2111   1946   2000     -1    110    -62       O  
ATOM   4563  NE2 GLN B 174     -28.081  -2.681 -21.635  1.00 16.99           N  
ANISOU 4563  NE2 GLN B 174     2248   2082   2124     11     95    -70       N  
ATOM   4564  N   VAL B 175     -28.497  -7.102 -24.398  1.00 15.37           N  
ANISOU 4564  N   VAL B 175     2057   1867   1914      8     86    -49       N  
ATOM   4565  CA  VAL B 175     -28.650  -7.304 -25.835  1.00 14.16           C  
ANISOU 4565  CA  VAL B 175     1879   1723   1777      8     79    -48       C  
ATOM   4566  C   VAL B 175     -28.667  -5.915 -26.468  1.00 15.50           C  
ANISOU 4566  C   VAL B 175     2013   1910   1967      9     75    -49       C  
ATOM   4567  O   VAL B 175     -29.678  -5.211 -26.433  1.00 15.92           O  
ANISOU 4567  O   VAL B 175     2050   1964   2036     -2     87    -51       O  
ATOM   4568  CB  VAL B 175     -29.902  -8.113 -26.176  1.00 17.55           C  
ANISOU 4568  CB  VAL B 175     2311   2144   2214    -11     95    -50       C  
ATOM   4569  CG1 VAL B 175     -30.001  -8.323 -27.685  1.00 15.52           C  
ANISOU 4569  CG1 VAL B 175     2030   1897   1969    -11     84    -51       C  
ATOM   4570  CG2 VAL B 175     -29.878  -9.484 -25.446  1.00 16.87           C  
ANISOU 4570  CG2 VAL B 175     2268   2035   2106    -15    100    -47       C  
ATOM   4571  N   TYR B 176     -27.528  -5.518 -27.028  1.00 13.60           N  
ANISOU 4571  N   TYR B 176     1760   1682   1724     22     56    -47       N  
ATOM   4572  CA  TYR B 176     -27.391  -4.244 -27.725  1.00 13.53           C  
ANISOU 4572  CA  TYR B 176     1723   1687   1732     20     50    -45       C  
ATOM   4573  C   TYR B 176     -27.988  -4.403 -29.115  1.00 13.80           C  
ANISOU 4573  C   TYR B 176     1738   1729   1777     14     48    -42       C  
ATOM   4574  O   TYR B 176     -27.406  -5.076 -29.979  1.00 12.82           O  
ANISOU 4574  O   TYR B 176     1612   1613   1645     19     39    -41       O  
ATOM   4575  CB  TYR B 176     -25.925  -3.847 -27.799  1.00 12.77           C  
ANISOU 4575  CB  TYR B 176     1621   1603   1627     31     33    -44       C  
ATOM   4576  CG  TYR B 176     -25.634  -2.488 -28.387  1.00 13.83           C  
ANISOU 4576  CG  TYR B 176     1731   1748   1774     25     26    -39       C  
ATOM   4577  CD1 TYR B 176     -26.587  -1.472 -28.401  1.00 15.29           C  
ANISOU 4577  CD1 TYR B 176     1907   1926   1977     16     32    -37       C  
ATOM   4578  CD2 TYR B 176     -24.390  -2.224 -28.924  1.00 15.00           C  
ANISOU 4578  CD2 TYR B 176     1868   1915   1918     29     13    -38       C  
ATOM   4579  CE1 TYR B 176     -26.283  -0.223 -28.927  1.00 14.06           C  
ANISOU 4579  CE1 TYR B 176     1735   1775   1832     11     24    -31       C  
ATOM   4580  CE2 TYR B 176     -24.078  -1.002 -29.451  1.00 12.82           C  
ANISOU 4580  CE2 TYR B 176     1573   1646   1651     19      8    -32       C  
ATOM   4581  CZ  TYR B 176     -25.019  -0.001 -29.451  1.00 16.50           C  
ANISOU 4581  CZ  TYR B 176     2037   2100   2134     10     12    -27       C  
ATOM   4582  OH  TYR B 176     -24.651   1.213 -29.994  1.00 15.04           O  
ANISOU 4582  OH  TYR B 176     1839   1919   1958      0      4    -20       O  
ATOM   4583  N   ASN B 177     -29.156  -3.797 -29.318  1.00 11.19           N  
ANISOU 4583  N   ASN B 177     1392   1396   1465      4     55    -41       N  
ATOM   4584  CA  ASN B 177     -29.938  -3.995 -30.524  1.00 13.67           C  
ANISOU 4584  CA  ASN B 177     1689   1716   1790     -2     51    -39       C  
ATOM   4585  C   ASN B 177     -29.593  -2.898 -31.523  1.00 15.09           C  
ANISOU 4585  C   ASN B 177     1848   1907   1977     -1     37    -31       C  
ATOM   4586  O   ASN B 177     -29.775  -1.702 -31.237  1.00 13.31           O  
ANISOU 4586  O   ASN B 177     1615   1678   1765      0     35    -28       O  
ATOM   4587  CB  ASN B 177     -31.428  -3.984 -30.190  1.00 13.13           C  
ANISOU 4587  CB  ASN B 177     1612   1640   1738    -13     65    -45       C  
ATOM   4588  CG  ASN B 177     -32.278  -4.451 -31.342  1.00 13.38           C  
ANISOU 4588  CG  ASN B 177     1628   1677   1778    -21     60    -45       C  
ATOM   4589  OD1 ASN B 177     -32.257  -5.640 -31.706  1.00 10.55           O  
ANISOU 4589  OD1 ASN B 177     1281   1317   1409    -27     59    -48       O  
ATOM   4590  ND2 ASN B 177     -33.047  -3.531 -31.921  1.00 10.85           N  
ANISOU 4590  ND2 ASN B 177     1282   1362   1478    -22     52    -43       N  
ATOM   4591  N   LEU B 178     -29.101  -3.303 -32.686  1.00 13.12           N  
ANISOU 4591  N   LEU B 178     1596   1671   1719     -1     26    -27       N  
ATOM   4592  CA  LEU B 178     -28.690  -2.385 -33.738  1.00 15.97           C  
ANISOU 4592  CA  LEU B 178     1943   2045   2081     -3     13    -17       C  
ATOM   4593  C   LEU B 178     -29.404  -2.730 -35.033  1.00 16.00           C  
ANISOU 4593  C   LEU B 178     1938   2057   2085     -9      5    -14       C  
ATOM   4594  O   LEU B 178     -29.826  -3.864 -35.253  1.00 14.64           O  
ANISOU 4594  O   LEU B 178     1771   1883   1907    -11      8    -22       O  
ATOM   4595  CB  LEU B 178     -27.185  -2.440 -33.992  1.00 15.28           C  
ANISOU 4595  CB  LEU B 178     1857   1972   1975      1      9    -16       C  
ATOM   4596  CG  LEU B 178     -26.257  -2.246 -32.806  1.00 17.09           C  
ANISOU 4596  CG  LEU B 178     2095   2198   2201      8     12    -20       C  
ATOM   4597  CD1 LEU B 178     -25.714  -3.586 -32.346  1.00 16.28           C  
ANISOU 4597  CD1 LEU B 178     2007   2096   2084     20     15    -30       C  
ATOM   4598  CD2 LEU B 178     -25.137  -1.344 -33.231  1.00 18.44           C  
ANISOU 4598  CD2 LEU B 178     2254   2384   2368      4      5    -13       C  
ATOM   4599  N   SER B 179     -29.489  -1.741 -35.911  1.00 13.10           N  
ANISOU 4599  N   SER B 179     1560   1696   1722    -13     -7     -2       N  
ATOM   4600  CA  SER B 179     -30.118  -1.900 -37.210  1.00 15.54           C  
ANISOU 4600  CA  SER B 179     1862   2015   2029    -19    -20      2       C  
ATOM   4601  C   SER B 179     -29.057  -2.029 -38.299  1.00 15.37           C  
ANISOU 4601  C   SER B 179     1845   2013   1983    -23    -25      8       C  
ATOM   4602  O   SER B 179     -28.229  -1.125 -38.474  1.00 13.70           O  
ANISOU 4602  O   SER B 179     1632   1807   1765    -26    -27     19       O  
ATOM   4603  CB  SER B 179     -31.037  -0.715 -37.500  1.00 15.47           C  
ANISOU 4603  CB  SER B 179     1841   1998   2039    -20    -33     13       C  
ATOM   4604  OG  SER B 179     -31.781  -0.946 -38.666  1.00 17.95           O  
ANISOU 4604  OG  SER B 179     2149   2320   2351    -25    -49     17       O  
ATOM   4605  N   GLN B 180     -29.086  -3.160 -39.019  1.00 13.71           N  
ANISOU 4605  N   GLN B 180     1640   1812   1757    -24    -25     -1       N  
ATOM   4606  CA  GLN B 180     -28.356  -3.389 -40.274  1.00 13.73           C  
ANISOU 4606  CA  GLN B 180     1645   1836   1734    -28    -29      1       C  
ATOM   4607  C   GLN B 180     -26.848  -3.562 -40.145  1.00 16.09           C  
ANISOU 4607  C   GLN B 180     1947   2150   2018    -23    -18     -4       C  
ATOM   4608  O   GLN B 180     -26.250  -4.353 -40.884  1.00 14.34           O  
ANISOU 4608  O   GLN B 180     1729   1945   1775    -20    -14    -14       O  
ATOM   4609  CB  GLN B 180     -28.628  -2.250 -41.269  1.00 16.18           C  
ANISOU 4609  CB  GLN B 180     1951   2154   2042    -39    -44     20       C  
ATOM   4610  CG  GLN B 180     -30.073  -2.187 -41.732  1.00 16.94           C  
ANISOU 4610  CG  GLN B 180     2043   2243   2151    -42    -61     23       C  
ATOM   4611  CD  GLN B 180     -30.278  -1.139 -42.815  1.00 21.32           C  
ANISOU 4611  CD  GLN B 180     2599   2804   2699    -49    -81     43       C  
ATOM   4612  OE1 GLN B 180     -29.396  -0.331 -43.087  1.00 33.32           O  
ANISOU 4612  OE1 GLN B 180     4124   4330   4206    -56    -80     57       O  
ATOM   4613  NE2 GLN B 180     -31.422  -1.169 -43.450  1.00 20.93           N  
ANISOU 4613  NE2 GLN B 180     2545   2753   2654    -51   -101     46       N  
ATOM   4614  N   ASN B 181     -26.210  -2.821 -39.249  1.00 14.98           N  
ANISOU 4614  N   ASN B 181     1801   2004   1885    -20    -13      1       N  
ATOM   4615  CA  ASN B 181     -24.756  -2.792 -39.251  1.00 15.71           C  
ANISOU 4615  CA  ASN B 181     1889   2116   1964    -18     -5     -3       C  
ATOM   4616  C   ASN B 181     -24.288  -2.272 -37.902  1.00 17.08           C  
ANISOU 4616  C   ASN B 181     2060   2277   2151    -13     -2     -3       C  
ATOM   4617  O   ASN B 181     -25.060  -1.695 -37.134  1.00 17.77           O  
ANISOU 4617  O   ASN B 181     2150   2344   2256    -14     -5      2       O  
ATOM   4618  CB  ASN B 181     -24.231  -1.913 -40.397  1.00 16.86           C  
ANISOU 4618  CB  ASN B 181     2028   2282   2095    -34     -8     11       C  
ATOM   4619  CG  ASN B 181     -22.825  -2.292 -40.855  1.00 21.98           C  
ANISOU 4619  CG  ASN B 181     2669   2961   2723    -33      4      1       C  
ATOM   4620  OD1 ASN B 181     -22.146  -3.126 -40.254  1.00 22.68           O  
ANISOU 4620  OD1 ASN B 181     2754   3053   2811    -17     11    -16       O  
ATOM   4621  ND2 ASN B 181     -22.380  -1.650 -41.924  1.00 23.68           N  
ANISOU 4621  ND2 ASN B 181     2880   3197   2922    -51      6     13       N  
ATOM   4622  N   VAL B 182     -23.018  -2.495 -37.617  1.00 18.37           N  
ANISOU 4622  N   VAL B 182     2217   2457   2306     -7      3    -11       N  
ATOM   4623  CA  VAL B 182     -22.378  -1.923 -36.448  1.00 18.54           C  
ANISOU 4623  CA  VAL B 182     2236   2473   2337     -4      3    -12       C  
ATOM   4624  C   VAL B 182     -21.490  -0.807 -36.969  1.00 20.56           C  
ANISOU 4624  C   VAL B 182     2477   2747   2589    -22      3     -2       C  
ATOM   4625  O   VAL B 182     -20.397  -1.063 -37.488  1.00 22.61           O  
ANISOU 4625  O   VAL B 182     2723   3034   2835    -23      8     -9       O  
ATOM   4626  CB  VAL B 182     -21.587  -2.966 -35.656  1.00 17.43           C  
ANISOU 4626  CB  VAL B 182     2097   2336   2191     16      4    -29       C  
ATOM   4627  CG1 VAL B 182     -20.890  -2.298 -34.482  1.00 17.11           C  
ANISOU 4627  CG1 VAL B 182     2052   2291   2157     17      0    -30       C  
ATOM   4628  CG2 VAL B 182     -22.513  -4.076 -35.172  1.00 14.54           C  
ANISOU 4628  CG2 VAL B 182     1751   1947   1827     29      5    -36       C  
ATOM   4629  N   GLN B 183     -21.968   0.428 -36.861  1.00 14.77           N  
ANISOU 4629  N   GLN B 183     1746   1999   1867    -37     -3     13       N  
ATOM   4630  CA  GLN B 183     -21.257   1.581 -37.388  1.00 16.14           C  
ANISOU 4630  CA  GLN B 183     1912   2183   2037    -60     -4     26       C  
ATOM   4631  C   GLN B 183     -20.409   2.215 -36.296  1.00 16.47           C  
ANISOU 4631  C   GLN B 183     1948   2223   2088    -64     -5     22       C  
ATOM   4632  O   GLN B 183     -20.552   1.925 -35.107  1.00 15.94           O  
ANISOU 4632  O   GLN B 183     1885   2140   2030    -49     -8     11       O  
ATOM   4633  CB  GLN B 183     -22.235   2.618 -37.949  1.00 18.17           C  
ANISOU 4633  CB  GLN B 183     2180   2421   2302    -73    -13     47       C  
ATOM   4634  CG  GLN B 183     -23.272   2.044 -38.898  1.00 18.43           C  
ANISOU 4634  CG  GLN B 183     2220   2454   2329    -68    -17     51       C  
ATOM   4635  CD  GLN B 183     -24.228   3.082 -39.441  1.00 20.31           C  
ANISOU 4635  CD  GLN B 183     2468   2673   2576    -78    -31     71       C  
ATOM   4636  OE1 GLN B 183     -24.934   2.820 -40.414  1.00 22.17           O  
ANISOU 4636  OE1 GLN B 183     2708   2912   2803    -78    -39     77       O  
ATOM   4637  NE2 GLN B 183     -24.272   4.257 -38.816  1.00 19.23           N  
ANISOU 4637  NE2 GLN B 183     2336   2515   2456    -84    -38     80       N  
ATOM   4638  N   GLU B 184     -19.524   3.112 -36.713  1.00 14.77           N  
ANISOU 4638  N   GLU B 184     1722   2022   1869    -87     -4     30       N  
ATOM   4639  CA  GLU B 184     -18.633   3.740 -35.747  1.00 15.93           C  
ANISOU 4639  CA  GLU B 184     1861   2169   2024    -95     -7     25       C  
ATOM   4640  C   GLU B 184     -19.394   4.646 -34.775  1.00 13.76           C  
ANISOU 4640  C   GLU B 184     1604   1857   1768    -96    -17     29       C  
ATOM   4641  O   GLU B 184     -19.001   4.766 -33.605  1.00 13.59           O  
ANISOU 4641  O   GLU B 184     1582   1828   1753    -91    -22     18       O  
ATOM   4642  CB  GLU B 184     -17.545   4.509 -36.488  1.00 14.43           C  
ANISOU 4642  CB  GLU B 184     1654   2002   1825   -125     -2     33       C  
ATOM   4643  CG  GLU B 184     -16.273   4.605 -35.725  1.00 23.56           C  
ANISOU 4643  CG  GLU B 184     2790   3177   2984   -130     -3     19       C  
ATOM   4644  CD  GLU B 184     -15.649   3.238 -35.410  1.00 22.67           C  
ANISOU 4644  CD  GLU B 184     2659   3089   2864   -101      0     -4       C  
ATOM   4645  OE1 GLU B 184     -15.877   2.238 -36.148  1.00 20.33           O  
ANISOU 4645  OE1 GLU B 184     2363   2806   2557    -85      8     -9       O  
ATOM   4646  OE2 GLU B 184     -14.917   3.184 -34.409  1.00 24.51           O  
ANISOU 4646  OE2 GLU B 184     2882   3328   3104    -94     -8    -18       O  
ATOM   4647  N   ASP B 185     -20.490   5.274 -35.213  1.00 10.99           N  
ANISOU 4647  N   ASP B 185     1268   1481   1425   -100    -22     44       N  
ATOM   4648  CA  ASP B 185     -21.277   6.046 -34.252  1.00 15.63           C  
ANISOU 4648  CA  ASP B 185     1872   2035   2032    -95    -29     44       C  
ATOM   4649  C   ASP B 185     -21.944   5.138 -33.227  1.00 15.98           C  
ANISOU 4649  C   ASP B 185     1921   2069   2081    -69    -26     27       C  
ATOM   4650  O   ASP B 185     -22.099   5.531 -32.069  1.00 15.80           O  
ANISOU 4650  O   ASP B 185     1907   2028   2068    -64    -27     18       O  
ATOM   4651  CB  ASP B 185     -22.319   6.930 -34.947  1.00 15.54           C  
ANISOU 4651  CB  ASP B 185     1874   1999   2031   -100    -38     62       C  
ATOM   4652  CG  ASP B 185     -23.230   6.161 -35.869  1.00 17.23           C  
ANISOU 4652  CG  ASP B 185     2087   2220   2240    -89    -37     67       C  
ATOM   4653  OD1 ASP B 185     -22.760   5.203 -36.505  1.00 17.04           O  
ANISOU 4653  OD1 ASP B 185     2054   2224   2198    -88    -30     64       O  
ATOM   4654  OD2 ASP B 185     -24.419   6.533 -35.983  1.00 19.52           O  
ANISOU 4654  OD2 ASP B 185     2386   2488   2544    -80    -45     73       O  
ATOM   4655  N   ASP B 186     -22.322   3.924 -33.628  1.00 14.54           N  
ANISOU 4655  N   ASP B 186     1735   1899   1889    -55    -20     23       N  
ATOM   4656  CA  ASP B 186     -22.832   2.951 -32.665  1.00 15.47           C  
ANISOU 4656  CA  ASP B 186     1860   2009   2008    -34    -14      8       C  
ATOM   4657  C   ASP B 186     -21.793   2.646 -31.592  1.00 14.20           C  
ANISOU 4657  C   ASP B 186     1699   1855   1840    -29    -15     -5       C  
ATOM   4658  O   ASP B 186     -22.108   2.642 -30.397  1.00 15.25           O  
ANISOU 4658  O   ASP B 186     1845   1972   1977    -20    -15    -14       O  
ATOM   4659  CB  ASP B 186     -23.244   1.664 -33.384  1.00 13.85           C  
ANISOU 4659  CB  ASP B 186     1653   1815   1793    -24     -9      6       C  
ATOM   4660  CG  ASP B 186     -24.343   1.891 -34.411  1.00 17.97           C  
ANISOU 4660  CG  ASP B 186     2175   2331   2321    -29    -12     17       C  
ATOM   4661  OD1 ASP B 186     -25.315   2.607 -34.087  1.00 18.32           O  
ANISOU 4661  OD1 ASP B 186     2224   2354   2382    -28    -15     21       O  
ATOM   4662  OD2 ASP B 186     -24.229   1.350 -35.541  1.00 17.20           O  
ANISOU 4662  OD2 ASP B 186     2073   2251   2211    -32    -12     21       O  
ATOM   4663  N   LEU B 187     -20.540   2.384 -31.996  1.00 12.41           N  
ANISOU 4663  N   LEU B 187     1458   1656   1603    -32    -17     -8       N  
ATOM   4664  CA  LEU B 187     -19.500   2.117 -31.001  1.00 12.19           C  
ANISOU 4664  CA  LEU B 187     1426   1637   1569    -25    -23    -21       C  
ATOM   4665  C   LEU B 187     -19.258   3.329 -30.092  1.00 14.62           C  
ANISOU 4665  C   LEU B 187     1738   1931   1885    -38    -31    -22       C  
ATOM   4666  O   LEU B 187     -19.046   3.170 -28.885  1.00 14.13           O  
ANISOU 4666  O   LEU B 187     1686   1861   1820    -29    -36    -33       O  
ATOM   4667  CB  LEU B 187     -18.205   1.689 -31.689  1.00 14.38           C  
ANISOU 4667  CB  LEU B 187     1678   1949   1835    -26    -23    -26       C  
ATOM   4668  CG  LEU B 187     -18.373   0.480 -32.617  1.00 14.30           C  
ANISOU 4668  CG  LEU B 187     1665   1952   1815    -11    -16    -28       C  
ATOM   4669  CD1 LEU B 187     -17.052   0.118 -33.261  1.00 14.62           C  
ANISOU 4669  CD1 LEU B 187     1679   2029   1846    -10    -13    -37       C  
ATOM   4670  CD2 LEU B 187     -18.960  -0.716 -31.854  1.00 12.84           C  
ANISOU 4670  CD2 LEU B 187     1500   1750   1627     14    -17    -37       C  
ATOM   4671  N   GLN B 188     -19.300   4.548 -30.645  1.00 13.85           N  
ANISOU 4671  N   GLN B 188     1639   1827   1798    -61    -32    -10       N  
ATOM   4672  CA  GLN B 188     -19.083   5.734 -29.816  1.00 15.36           C  
ANISOU 4672  CA  GLN B 188     1838   2000   1998    -75    -40    -12       C  
ATOM   4673  C   GLN B 188     -20.222   5.931 -28.818  1.00 15.58           C  
ANISOU 4673  C   GLN B 188     1889   1996   2034    -62    -39    -18       C  
ATOM   4674  O   GLN B 188     -19.982   6.318 -27.662  1.00 15.88           O  
ANISOU 4674  O   GLN B 188     1937   2023   2072    -62    -44    -30       O  
ATOM   4675  CB  GLN B 188     -18.906   6.977 -30.694  1.00 15.84           C  
ANISOU 4675  CB  GLN B 188     1895   2056   2066   -104    -43      3       C  
ATOM   4676  CG  GLN B 188     -17.560   6.986 -31.442  1.00 18.84           C  
ANISOU 4676  CG  GLN B 188     2250   2470   2437   -124    -42      6       C  
ATOM   4677  CD  GLN B 188     -17.351   8.202 -32.339  1.00 30.02           C  
ANISOU 4677  CD  GLN B 188     3668   3882   3858   -158    -42     25       C  
ATOM   4678  OE1 GLN B 188     -18.123   9.167 -32.310  1.00 30.23           O  
ANISOU 4678  OE1 GLN B 188     3716   3875   3896   -165    -48     35       O  
ATOM   4679  NE2 GLN B 188     -16.279   8.162 -33.140  1.00 31.04           N  
ANISOU 4679  NE2 GLN B 188     3774   4044   3976   -179    -36     28       N  
ATOM   4680  N   HIS B 189     -21.466   5.704 -29.255  1.00 14.45           N  
ANISOU 4680  N   HIS B 189     1753   1840   1898    -52    -31    -12       N  
ATOM   4681  CA  HIS B 189     -22.606   5.746 -28.337  1.00 13.81           C  
ANISOU 4681  CA  HIS B 189     1689   1734   1824    -39    -24    -21       C  
ATOM   4682  C   HIS B 189     -22.474   4.679 -27.260  1.00 16.29           C  
ANISOU 4682  C   HIS B 189     2012   2054   2124    -24    -20    -34       C  
ATOM   4683  O   HIS B 189     -22.713   4.950 -26.077  1.00 11.98           O  
ANISOU 4683  O   HIS B 189     1483   1493   1577    -19    -18    -46       O  
ATOM   4684  CB  HIS B 189     -23.926   5.544 -29.089  1.00 17.32           C  
ANISOU 4684  CB  HIS B 189     2132   2170   2279    -31    -17    -13       C  
ATOM   4685  CG  HIS B 189     -24.235   6.627 -30.079  1.00 23.74           C  
ANISOU 4685  CG  HIS B 189     2942   2972   3106    -42    -25      3       C  
ATOM   4686  ND1 HIS B 189     -24.935   6.389 -31.243  1.00 25.07           N  
ANISOU 4686  ND1 HIS B 189     3103   3145   3278    -41    -26     15       N  
ATOM   4687  CD2 HIS B 189     -23.944   7.948 -30.081  1.00 22.92           C  
ANISOU 4687  CD2 HIS B 189     2844   2851   3012    -56    -35      8       C  
ATOM   4688  CE1 HIS B 189     -25.059   7.518 -31.921  1.00 24.26           C  
ANISOU 4688  CE1 HIS B 189     3003   3028   3185    -51    -37     29       C  
ATOM   4689  NE2 HIS B 189     -24.466   8.479 -31.237  1.00 25.51           N  
ANISOU 4689  NE2 HIS B 189     3171   3172   3348    -61    -42     26       N  
ATOM   4690  N   LEU B 190     -22.148   3.439 -27.664  1.00 11.60           N  
ANISOU 4690  N   LEU B 190     1412   1479   1517    -14    -18    -34       N  
ATOM   4691  CA  LEU B 190     -21.952   2.367 -26.686  1.00 12.40           C  
ANISOU 4691  CA  LEU B 190     1526   1582   1602      1    -17    -44       C  
ATOM   4692  C   LEU B 190     -20.877   2.751 -25.676  1.00 12.37           C  
ANISOU 4692  C   LEU B 190     1527   1583   1590     -1    -30    -53       C  
ATOM   4693  O   LEU B 190     -21.038   2.549 -24.466  1.00 13.09           O  
ANISOU 4693  O   LEU B 190     1640   1663   1672      6    -30    -63       O  
ATOM   4694  CB  LEU B 190     -21.574   1.060 -27.394  1.00 10.85           C  
ANISOU 4694  CB  LEU B 190     1323   1404   1396     12    -17    -42       C  
ATOM   4695  CG  LEU B 190     -21.368  -0.147 -26.476  1.00 12.92           C  
ANISOU 4695  CG  LEU B 190     1603   1664   1641     29    -19    -50       C  
ATOM   4696  CD1 LEU B 190     -22.649  -0.528 -25.730  1.00 13.14           C  
ANISOU 4696  CD1 LEU B 190     1656   1669   1668     32     -4    -52       C  
ATOM   4697  CD2 LEU B 190     -20.841  -1.361 -27.248  1.00 12.65           C  
ANISOU 4697  CD2 LEU B 190     1562   1646   1599     42    -22    -51       C  
ATOM   4698  N   GLN B 191     -19.765   3.296 -26.165  1.00 13.14           N  
ANISOU 4698  N   GLN B 191     1605   1697   1690    -13    -41    -52       N  
ATOM   4699  CA  GLN B 191     -18.699   3.747 -25.286  1.00 14.91           C  
ANISOU 4699  CA  GLN B 191     1828   1929   1909    -18    -57    -62       C  
ATOM   4700  C   GLN B 191     -19.207   4.808 -24.316  1.00 15.70           C  
ANISOU 4700  C   GLN B 191     1949   2003   2013    -27    -57    -68       C  
ATOM   4701  O   GLN B 191     -18.960   4.726 -23.109  1.00 13.09           O  
ANISOU 4701  O   GLN B 191     1635   1667   1670    -21    -65    -80       O  
ATOM   4702  CB  GLN B 191     -17.527   4.299 -26.105  1.00 15.75           C  
ANISOU 4702  CB  GLN B 191     1905   2058   2020    -36    -66    -59       C  
ATOM   4703  CG  GLN B 191     -16.488   4.960 -25.207  1.00 18.15           C  
ANISOU 4703  CG  GLN B 191     2205   2369   2322    -47    -83    -70       C  
ATOM   4704  CD  GLN B 191     -15.252   5.454 -25.930  1.00 18.16           C  
ANISOU 4704  CD  GLN B 191     2174   2398   2329    -69    -91    -69       C  
ATOM   4705  OE1 GLN B 191     -14.136   5.239 -25.469  1.00 23.49           O  
ANISOU 4705  OE1 GLN B 191     2831   3095   2998    -67   -106    -81       O  
ATOM   4706  NE2 GLN B 191     -15.443   6.141 -27.042  1.00 12.78           N  
ANISOU 4706  NE2 GLN B 191     1483   1716   1658    -90    -80    -56       N  
ATOM   4707  N   LEU B 192     -19.909   5.821 -24.830  1.00 13.51           N  
ANISOU 4707  N   LEU B 192     1673   1708   1754    -39    -50    -61       N  
ATOM   4708  CA  LEU B 192     -20.383   6.894 -23.957  1.00 16.49           C  
ANISOU 4708  CA  LEU B 192     2069   2059   2137    -45    -51    -71       C  
ATOM   4709  C   LEU B 192     -21.340   6.358 -22.906  1.00 15.91           C  
ANISOU 4709  C   LEU B 192     2019   1971   2054    -28    -38    -81       C  
ATOM   4710  O   LEU B 192     -21.233   6.694 -21.722  1.00 14.76           O  
ANISOU 4710  O   LEU B 192     1893   1816   1899    -28    -42    -96       O  
ATOM   4711  CB  LEU B 192     -21.074   7.985 -24.772  1.00 14.38           C  
ANISOU 4711  CB  LEU B 192     1800   1772   1892    -56    -47    -60       C  
ATOM   4712  CG  LEU B 192     -21.564   9.099 -23.851  1.00 23.24           C  
ANISOU 4712  CG  LEU B 192     2944   2864   3023    -59    -47    -73       C  
ATOM   4713  CD1 LEU B 192     -20.356   9.922 -23.372  1.00 19.33           C  
ANISOU 4713  CD1 LEU B 192     2450   2369   2524    -80    -65    -81       C  
ATOM   4714  CD2 LEU B 192     -22.624   9.959 -24.529  1.00 26.94           C  
ANISOU 4714  CD2 LEU B 192     3415   3307   3514    -58    -42    -65       C  
ATOM   4715  N   PHE B 193     -22.267   5.495 -23.316  1.00 16.08           N  
ANISOU 4715  N   PHE B 193     2040   1993   2076    -16    -23    -75       N  
ATOM   4716  CA  PHE B 193     -23.279   5.013 -22.383  1.00 17.58           C  
ANISOU 4716  CA  PHE B 193     2251   2170   2258     -5     -6    -84       C  
ATOM   4717  C   PHE B 193     -22.676   4.094 -21.332  1.00 12.79           C  
ANISOU 4717  C   PHE B 193     1663   1572   1624      3    -11    -91       C  
ATOM   4718  O   PHE B 193     -23.051   4.166 -20.152  1.00 13.75           O  
ANISOU 4718  O   PHE B 193     1810   1683   1733      6     -4   -103       O  
ATOM   4719  CB  PHE B 193     -24.395   4.305 -23.151  1.00 14.67           C  
ANISOU 4719  CB  PHE B 193     1874   1801   1899      2     10    -76       C  
ATOM   4720  CG  PHE B 193     -25.158   5.210 -24.090  1.00 13.71           C  
ANISOU 4720  CG  PHE B 193     1736   1669   1803     -2     13    -69       C  
ATOM   4721  CD1 PHE B 193     -25.223   6.576 -23.866  1.00 15.12           C  
ANISOU 4721  CD1 PHE B 193     1919   1831   1996     -7      8    -75       C  
ATOM   4722  CD2 PHE B 193     -25.806   4.686 -25.208  1.00 17.60           C  
ANISOU 4722  CD2 PHE B 193     2214   2169   2306      1     17    -58       C  
ATOM   4723  CE1 PHE B 193     -25.923   7.401 -24.733  1.00 18.43           C  
ANISOU 4723  CE1 PHE B 193     2327   2236   2439     -8      6    -67       C  
ATOM   4724  CE2 PHE B 193     -26.503   5.505 -26.074  1.00 18.15           C  
ANISOU 4724  CE2 PHE B 193     2271   2228   2397     -1     15    -51       C  
ATOM   4725  CZ  PHE B 193     -26.561   6.850 -25.847  1.00 16.64           C  
ANISOU 4725  CZ  PHE B 193     2084   2018   2221     -4      9    -54       C  
ATOM   4726  N   THR B 194     -21.744   3.217 -21.733  1.00 15.11           N  
ANISOU 4726  N   THR B 194     1948   1886   1909      8    -24    -85       N  
ATOM   4727  CA  THR B 194     -21.127   2.338 -20.753  1.00 13.61           C  
ANISOU 4727  CA  THR B 194     1778   1702   1693     19    -35    -90       C  
ATOM   4728  C   THR B 194     -20.184   3.114 -19.837  1.00 15.05           C  
ANISOU 4728  C   THR B 194     1967   1887   1866     13    -55   -102       C  
ATOM   4729  O   THR B 194     -20.068   2.777 -18.655  1.00 17.34           O  
ANISOU 4729  O   THR B 194     2285   2172   2132     20    -60   -109       O  
ATOM   4730  CB  THR B 194     -20.404   1.165 -21.439  1.00 14.03           C  
ANISOU 4730  CB  THR B 194     1818   1773   1741     32    -45    -83       C  
ATOM   4731  OG1 THR B 194     -19.425   1.643 -22.372  1.00 14.62           O  
ANISOU 4731  OG1 THR B 194     1860   1868   1828     25    -58    -80       O  
ATOM   4732  CG2 THR B 194     -21.404   0.248 -22.166  1.00 12.61           C  
ANISOU 4732  CG2 THR B 194     1639   1587   1565     37    -26    -74       C  
ATOM   4733  N   GLU B 195     -19.525   4.157 -20.350  1.00 12.90           N  
ANISOU 4733  N   GLU B 195     1672   1620   1609     -1    -66   -103       N  
ATOM   4734  CA  GLU B 195     -18.729   5.027 -19.486  1.00 15.66           C  
ANISOU 4734  CA  GLU B 195     2029   1969   1953    -12    -85   -116       C  
ATOM   4735  C   GLU B 195     -19.603   5.683 -18.430  1.00 16.39           C  
ANISOU 4735  C   GLU B 195     2153   2037   2039    -14    -73   -128       C  
ATOM   4736  O   GLU B 195     -19.247   5.717 -17.247  1.00 15.98           O  
ANISOU 4736  O   GLU B 195     2124   1983   1965    -13    -84   -141       O  
ATOM   4737  CB  GLU B 195     -18.015   6.095 -20.314  1.00 16.04           C  
ANISOU 4737  CB  GLU B 195     2049   2024   2022    -33    -95   -113       C  
ATOM   4738  CG  GLU B 195     -17.198   7.108 -19.472  1.00 18.38           C  
ANISOU 4738  CG  GLU B 195     2351   2318   2315    -50   -116   -128       C  
ATOM   4739  CD  GLU B 195     -15.923   6.528 -18.878  1.00 22.80           C  
ANISOU 4739  CD  GLU B 195     2903   2903   2857    -44   -142   -136       C  
ATOM   4740  OE1 GLU B 195     -15.691   5.303 -18.985  1.00 24.17           O  
ANISOU 4740  OE1 GLU B 195     3071   3092   3019    -24   -145   -131       O  
ATOM   4741  OE2 GLU B 195     -15.130   7.309 -18.313  1.00 27.98           O  
ANISOU 4741  OE2 GLU B 195     3557   3561   3512    -61   -162   -149       O  
ATOM   4742  N   TYR B 196     -20.763   6.195 -18.854  1.00 14.45           N  
ANISOU 4742  N   TYR B 196     1907   1773   1812    -17    -51   -126       N  
ATOM   4743  CA  TYR B 196     -21.718   6.817 -17.949  1.00 16.64           C  
ANISOU 4743  CA  TYR B 196     2210   2027   2086    -16    -35   -140       C  
ATOM   4744  C   TYR B 196     -22.172   5.846 -16.871  1.00 15.18           C  
ANISOU 4744  C   TYR B 196     2053   1842   1871     -5    -23   -146       C  
ATOM   4745  O   TYR B 196     -22.342   6.233 -15.711  1.00 17.22           O  
ANISOU 4745  O   TYR B 196     2340   2091   2112     -6    -19   -163       O  
ATOM   4746  CB  TYR B 196     -22.916   7.334 -18.754  1.00 14.43           C  
ANISOU 4746  CB  TYR B 196     1918   1732   1834    -15    -14   -136       C  
ATOM   4747  CG  TYR B 196     -23.761   8.362 -18.023  1.00 17.58           C  
ANISOU 4747  CG  TYR B 196     2335   2106   2240    -14     -1   -154       C  
ATOM   4748  CD1 TYR B 196     -23.180   9.515 -17.503  1.00 17.39           C  
ANISOU 4748  CD1 TYR B 196     2322   2068   2217    -24    -16   -168       C  
ATOM   4749  CD2 TYR B 196     -25.134   8.182 -17.862  1.00 13.21           C  
ANISOU 4749  CD2 TYR B 196     1785   1543   1693     -3     27   -160       C  
ATOM   4750  CE1 TYR B 196     -23.944  10.468 -16.839  1.00 17.27           C  
ANISOU 4750  CE1 TYR B 196     2325   2028   2209    -21     -4   -188       C  
ATOM   4751  CE2 TYR B 196     -25.902   9.125 -17.209  1.00 14.44           C  
ANISOU 4751  CE2 TYR B 196     1953   1677   1855      2     40   -180       C  
ATOM   4752  CZ  TYR B 196     -25.297  10.267 -16.695  1.00 18.98           C  
ANISOU 4752  CZ  TYR B 196     2543   2236   2431     -6     25   -195       C  
ATOM   4753  OH  TYR B 196     -26.045  11.219 -16.033  1.00 17.49           O  
ANISOU 4753  OH  TYR B 196     2370   2025   2251      1     38   -218       O  
ATOM   4754  N   GLY B 197     -22.365   4.580 -17.230  1.00 12.48           N  
ANISOU 4754  N   GLY B 197     1709   1510   1521      5    -16   -133       N  
ATOM   4755  CA  GLY B 197     -22.635   3.570 -16.222  1.00 13.99           C  
ANISOU 4755  CA  GLY B 197     1933   1702   1682     13     -8   -135       C  
ATOM   4756  C   GLY B 197     -21.463   3.351 -15.282  1.00 15.74           C  
ANISOU 4756  C   GLY B 197     2175   1932   1875     15    -36   -140       C  
ATOM   4757  O   GLY B 197     -21.632   3.323 -14.061  1.00 16.45           O  
ANISOU 4757  O   GLY B 197     2299   2014   1936     15    -33   -151       O  
ATOM   4758  N   ARG B 198     -20.256   3.194 -15.838  1.00 15.66           N  
ANISOU 4758  N   ARG B 198     2141   1938   1870     18    -64   -134       N  
ATOM   4759  CA  ARG B 198     -19.075   2.932 -15.012  1.00 18.65           C  
ANISOU 4759  CA  ARG B 198     2533   2329   2225     24    -96   -140       C  
ATOM   4760  C   ARG B 198     -18.870   4.021 -13.969  1.00 20.07           C  
ANISOU 4760  C   ARG B 198     2732   2500   2392     12   -106   -158       C  
ATOM   4761  O   ARG B 198     -18.484   3.741 -12.826  1.00 16.17           O  
ANISOU 4761  O   ARG B 198     2269   2007   1866     17   -122   -166       O  
ATOM   4762  CB  ARG B 198     -17.821   2.822 -15.885  1.00 19.88           C  
ANISOU 4762  CB  ARG B 198     2650   2507   2396     27   -123   -135       C  
ATOM   4763  CG  ARG B 198     -17.801   1.625 -16.802  1.00 26.96           C  
ANISOU 4763  CG  ARG B 198     3531   3413   3298     43   -119   -120       C  
ATOM   4764  CD  ARG B 198     -16.493   1.525 -17.598  1.00 30.41           C  
ANISOU 4764  CD  ARG B 198     3929   3877   3749     47   -143   -120       C  
ATOM   4765  NE  ARG B 198     -15.356   1.138 -16.774  1.00 37.30           N  
ANISOU 4765  NE  ARG B 198     4806   4763   4602     61   -178   -127       N  
ATOM   4766  CZ  ARG B 198     -14.290   0.489 -17.229  1.00 38.90           C  
ANISOU 4766  CZ  ARG B 198     4982   4990   4809     77   -200   -128       C  
ATOM   4767  NH1 ARG B 198     -14.174   0.160 -18.507  1.00 30.62           N  
ANISOU 4767  NH1 ARG B 198     3900   3955   3781     80   -189   -121       N  
ATOM   4768  NH2 ARG B 198     -13.323   0.151 -16.378  1.00 37.26           N  
ANISOU 4768  NH2 ARG B 198     4781   4794   4584     92   -234   -136       N  
ATOM   4769  N   LEU B 199     -19.108   5.270 -14.358  1.00 16.55           N  
ANISOU 4769  N   LEU B 199     2270   2046   1971     -3    -98   -166       N  
ATOM   4770  CA  LEU B 199     -18.933   6.408 -13.469  1.00 18.23           C  
ANISOU 4770  CA  LEU B 199     2501   2247   2177    -16   -107   -187       C  
ATOM   4771  C   LEU B 199     -19.846   6.357 -12.254  1.00 20.57           C  
ANISOU 4771  C   LEU B 199     2841   2528   2445    -12    -86   -199       C  
ATOM   4772  O   LEU B 199     -19.568   7.040 -11.267  1.00 19.30           O  
ANISOU 4772  O   LEU B 199     2706   2362   2267    -20    -97   -218       O  
ATOM   4773  CB  LEU B 199     -19.191   7.703 -14.245  1.00 18.16           C  
ANISOU 4773  CB  LEU B 199     2471   2225   2203    -31    -99   -190       C  
ATOM   4774  CG  LEU B 199     -18.209   8.082 -15.358  1.00 21.22           C  
ANISOU 4774  CG  LEU B 199     2819   2627   2617    -44   -119   -180       C  
ATOM   4775  CD1 LEU B 199     -18.744   9.278 -16.124  1.00 20.68           C  
ANISOU 4775  CD1 LEU B 199     2739   2538   2580    -58   -106   -179       C  
ATOM   4776  CD2 LEU B 199     -16.842   8.394 -14.764  1.00 23.04           C  
ANISOU 4776  CD2 LEU B 199     3046   2872   2835    -55   -154   -192       C  
ATOM   4777  N   ALA B 200     -20.945   5.603 -12.317  1.00 18.24           N  
ANISOU 4777  N   ALA B 200     2557   2228   2146     -4    -55   -191       N  
ATOM   4778  CA  ALA B 200     -21.895   5.511 -11.218  1.00 19.72           C  
ANISOU 4778  CA  ALA B 200     2783   2404   2306     -3    -28   -203       C  
ATOM   4779  C   ALA B 200     -21.700   4.260 -10.377  1.00 20.49           C  
ANISOU 4779  C   ALA B 200     2915   2508   2361      4    -33   -195       C  
ATOM   4780  O   ALA B 200     -22.532   3.971  -9.516  1.00 22.64           O  
ANISOU 4780  O   ALA B 200     3223   2774   2607      2     -7   -201       O  
ATOM   4781  CB  ALA B 200     -23.332   5.554 -11.751  1.00 16.34           C  
ANISOU 4781  CB  ALA B 200     2342   1965   1900     -2     13   -202       C  
ATOM   4782  N   MET B 201     -20.638   3.503 -10.614  1.00 19.79           N  
ANISOU 4782  N   MET B 201     2821   2434   2266     13    -66   -181       N  
ATOM   4783  CA  MET B 201     -20.479   2.192 -10.006  1.00 22.43           C  
ANISOU 4783  CA  MET B 201     3187   2771   2564     23    -74   -168       C  
ATOM   4784  C   MET B 201     -19.387   2.217  -8.946  1.00 22.22           C  
ANISOU 4784  C   MET B 201     3189   2752   2503     27   -114   -176       C  
ATOM   4785  O   MET B 201     -18.509   3.079  -8.947  1.00 19.62           O  
ANISOU 4785  O   MET B 201     2841   2431   2184     22   -142   -188       O  
ATOM   4786  CB  MET B 201     -20.140   1.137 -11.067  1.00 19.53           C  
ANISOU 4786  CB  MET B 201     2795   2412   2214     37    -84   -147       C  
ATOM   4787  CG  MET B 201     -21.250   0.905 -12.057  1.00 20.80           C  
ANISOU 4787  CG  MET B 201     2935   2566   2403     33    -47   -138       C  
ATOM   4788  SD  MET B 201     -20.699  -0.125 -13.422  1.00 21.21           S  
ANISOU 4788  SD  MET B 201     2953   2629   2478     48    -62   -119       S  
ATOM   4789  CE  MET B 201     -20.176  -1.606 -12.566  1.00 18.06           C  
ANISOU 4789  CE  MET B 201     2599   2226   2038     65    -84   -107       C  
ATOM   4790  N   GLU B 202     -19.460   1.250  -8.035  1.00 23.48           N  
ANISOU 4790  N   GLU B 202     3394   2907   2619     34   -117   -168       N  
ATOM   4791  CA  GLU B 202     -18.366   1.020  -7.105  1.00 23.79           C  
ANISOU 4791  CA  GLU B 202     3461   2954   2623     43   -162   -170       C  
ATOM   4792  C   GLU B 202     -17.068   0.785  -7.867  1.00 27.43           C  
ANISOU 4792  C   GLU B 202     3880   3433   3108     58   -205   -164       C  
ATOM   4793  O   GLU B 202     -17.048   0.109  -8.899  1.00 23.63           O  
ANISOU 4793  O   GLU B 202     3370   2955   2653     69   -201   -150       O  
ATOM   4794  CB  GLU B 202     -18.671  -0.189  -6.227  1.00 24.38           C  
ANISOU 4794  CB  GLU B 202     3594   3020   2651     50   -160   -155       C  
ATOM   4795  CG  GLU B 202     -19.862  -0.010  -5.315  1.00 24.17           C  
ANISOU 4795  CG  GLU B 202     3612   2980   2593     32   -117   -162       C  
ATOM   4796  CD  GLU B 202     -20.332  -1.323  -4.750  1.00 25.06           C  
ANISOU 4796  CD  GLU B 202     3776   3081   2665     35   -106   -141       C  
ATOM   4797  OE1 GLU B 202     -20.883  -2.146  -5.522  1.00 22.00           O  
ANISOU 4797  OE1 GLU B 202     3376   2686   2296     37    -85   -124       O  
ATOM   4798  OE2 GLU B 202     -20.112  -1.546  -3.545  1.00 25.90           O  
ANISOU 4798  OE2 GLU B 202     3937   3184   2720     33   -120   -142       O  
ATOM   4799  N   GLU B 203     -15.982   1.359  -7.363  1.00 24.76           N  
ANISOU 4799  N   GLU B 203     3537   3108   2762     58   -246   -178       N  
ATOM   4800  CA  GLU B 203     -14.678   1.098  -7.948  1.00 33.33           C  
ANISOU 4800  CA  GLU B 203     4581   4216   3867     73   -288   -176       C  
ATOM   4801  C   GLU B 203     -14.355  -0.380  -7.814  1.00 31.95           C  
ANISOU 4801  C   GLU B 203     4427   4040   3671    101   -309   -157       C  
ATOM   4802  O   GLU B 203     -14.615  -0.993  -6.778  1.00 33.50           O  
ANISOU 4802  O   GLU B 203     4680   4224   3824    107   -315   -150       O  
ATOM   4803  CB  GLU B 203     -13.611   1.945  -7.261  1.00 38.95           C  
ANISOU 4803  CB  GLU B 203     5287   4942   4569     65   -331   -196       C  
ATOM   4804  CG  GLU B 203     -13.637   3.407  -7.665  1.00 50.97           C  
ANISOU 4804  CG  GLU B 203     6778   6466   6123     37   -318   -214       C  
ATOM   4805  CD  GLU B 203     -12.713   4.257  -6.820  1.00 63.77           C  
ANISOU 4805  CD  GLU B 203     8403   8097   7729     24   -358   -236       C  
ATOM   4806  OE1 GLU B 203     -12.409   3.853  -5.673  1.00 66.75           O  
ANISOU 4806  OE1 GLU B 203     8823   8476   8063     34   -386   -240       O  
ATOM   4807  OE2 GLU B 203     -12.287   5.328  -7.307  1.00 68.96           O  
ANISOU 4807  OE2 GLU B 203     9023   8761   8417      3   -363   -249       O  
ATOM   4808  N   THR B 204     -13.807  -0.962  -8.875  1.00 29.09           N  
ANISOU 4808  N   THR B 204     4023   3691   3340    118   -319   -148       N  
ATOM   4809  CA  THR B 204     -13.563  -2.396  -8.886  1.00 34.14           C  
ANISOU 4809  CA  THR B 204     4681   4325   3964    148   -337   -131       C  
ATOM   4810  C   THR B 204     -12.434  -2.708  -9.852  1.00 35.28           C  
ANISOU 4810  C   THR B 204     4769   4495   4142    170   -365   -133       C  
ATOM   4811  O   THR B 204     -12.300  -2.063 -10.895  1.00 34.00           O  
ANISOU 4811  O   THR B 204     4553   4347   4017    158   -350   -140       O  
ATOM   4812  CB  THR B 204     -14.821  -3.177  -9.281  1.00 32.44           C  
ANISOU 4812  CB  THR B 204     4491   4087   3749    146   -293   -113       C  
ATOM   4813  OG1 THR B 204     -14.504  -4.567  -9.362  1.00 39.26           O  
ANISOU 4813  OG1 THR B 204     5374   4942   4602    175   -313    -97       O  
ATOM   4814  CG2 THR B 204     -15.344  -2.713 -10.624  1.00 31.04           C  
ANISOU 4814  CG2 THR B 204     4264   3914   3617    133   -257   -115       C  
ATOM   4815  N   PHE B 205     -11.622  -3.698  -9.495  1.00 37.62           N  
ANISOU 4815  N   PHE B 205     5077   4794   4421    203   -407   -127       N  
ATOM   4816  CA  PHE B 205     -10.559  -4.133 -10.387  1.00 40.84           C  
ANISOU 4816  CA  PHE B 205     5431   5226   4859    229   -433   -132       C  
ATOM   4817  C   PHE B 205     -11.078  -5.033 -11.498  1.00 32.52           C  
ANISOU 4817  C   PHE B 205     4368   4162   3827    242   -404   -119       C  
ATOM   4818  O   PHE B 205     -10.387  -5.220 -12.505  1.00 32.99           O  
ANISOU 4818  O   PHE B 205     4373   4243   3917    257   -410   -125       O  
ATOM   4819  CB  PHE B 205      -9.472  -4.838  -9.576  1.00 51.02           C  
ANISOU 4819  CB  PHE B 205     6736   6524   6126    264   -492   -133       C  
ATOM   4820  CG  PHE B 205      -9.057  -4.075  -8.350  1.00 60.31           C  
ANISOU 4820  CG  PHE B 205     7934   7708   7274    251   -523   -145       C  
ATOM   4821  CD1 PHE B 205      -8.310  -2.909  -8.464  1.00 65.98           C  
ANISOU 4821  CD1 PHE B 205     8601   8456   8013    231   -538   -166       C  
ATOM   4822  CD2 PHE B 205      -9.429  -4.509  -7.085  1.00 63.07           C  
ANISOU 4822  CD2 PHE B 205     8356   8034   7572    256   -537   -134       C  
ATOM   4823  CE1 PHE B 205      -7.932  -2.196  -7.340  1.00 71.04           C  
ANISOU 4823  CE1 PHE B 205     9263   9103   8627    218   -568   -179       C  
ATOM   4824  CE2 PHE B 205      -9.053  -3.803  -5.956  1.00 68.76           C  
ANISOU 4824  CE2 PHE B 205     9099   8762   8263    244   -567   -147       C  
ATOM   4825  CZ  PHE B 205      -8.302  -2.644  -6.084  1.00 72.05           C  
ANISOU 4825  CZ  PHE B 205     9464   9208   8703    225   -583   -170       C  
ATOM   4826  N   LEU B 206     -12.286  -5.564 -11.348  1.00 29.98           N  
ANISOU 4826  N   LEU B 206     4094   3809   3489    234   -370   -103       N  
ATOM   4827  CA  LEU B 206     -12.897  -6.410 -12.359  1.00 30.35           C  
ANISOU 4827  CA  LEU B 206     4137   3843   3553    242   -342    -92       C  
ATOM   4828  C   LEU B 206     -13.485  -5.558 -13.479  1.00 21.88           C  
ANISOU 4828  C   LEU B 206     3019   2780   2516    214   -301    -97       C  
ATOM   4829  O   LEU B 206     -13.668  -4.350 -13.339  1.00 21.59           O  
ANISOU 4829  O   LEU B 206     2966   2751   2485    187   -289   -106       O  
ATOM   4830  CB  LEU B 206     -13.979  -7.286 -11.722  1.00 26.42           C  
ANISOU 4830  CB  LEU B 206     3707   3307   3023    239   -322    -73       C  
ATOM   4831  CG  LEU B 206     -13.480  -8.091 -10.515  1.00 32.31           C  
ANISOU 4831  CG  LEU B 206     4510   4039   3728    263   -364    -64       C  
ATOM   4832  CD1 LEU B 206     -14.573  -8.997 -10.006  1.00 31.04           C  
ANISOU 4832  CD1 LEU B 206     4418   3840   3536    254   -339    -44       C  
ATOM   4833  CD2 LEU B 206     -12.241  -8.906 -10.876  1.00 26.77           C  
ANISOU 4833  CD2 LEU B 206     3786   3348   3038    307   -410    -67       C  
ATOM   4834  N   LYS B 207     -13.764  -6.199 -14.608  1.00 21.08           N  
ANISOU 4834  N   LYS B 207     2897   2676   2436    222   -282    -91       N  
ATOM   4835  CA  LYS B 207     -14.549  -5.532 -15.630  1.00 20.22           C  
ANISOU 4835  CA  LYS B 207     2758   2570   2354    196   -242    -92       C  
ATOM   4836  C   LYS B 207     -15.909  -5.157 -15.043  1.00 21.15           C  
ANISOU 4836  C   LYS B 207     2914   2664   2457    169   -208    -85       C  
ATOM   4837  O   LYS B 207     -16.453  -5.896 -14.213  1.00 19.55           O  
ANISOU 4837  O   LYS B 207     2765   2439   2226    172   -205    -75       O  
ATOM   4838  CB  LYS B 207     -14.720  -6.427 -16.858  1.00 17.73           C  
ANISOU 4838  CB  LYS B 207     2425   2254   2058    210   -228    -87       C  
ATOM   4839  CG  LYS B 207     -13.413  -6.664 -17.623  1.00 19.90           C  
ANISOU 4839  CG  LYS B 207     2652   2558   2352    235   -254    -98       C  
ATOM   4840  CD  LYS B 207     -13.641  -7.419 -18.928  1.00 20.17           C  
ANISOU 4840  CD  LYS B 207     2667   2592   2404    245   -235    -96       C  
ATOM   4841  CE  LYS B 207     -12.373  -7.410 -19.796  1.00 17.14           C  
ANISOU 4841  CE  LYS B 207     2226   2244   2041    265   -252   -111       C  
ATOM   4842  NZ  LYS B 207     -12.637  -7.963 -21.157  1.00 18.45           N  
ANISOU 4842  NZ  LYS B 207     2373   2414   2225    269   -230   -112       N  
ATOM   4843  N   PRO B 208     -16.466  -4.007 -15.415  1.00 20.67           N  
ANISOU 4843  N   PRO B 208     2830   2609   2416    142   -182    -91       N  
ATOM   4844  CA  PRO B 208     -17.717  -3.579 -14.782  1.00 20.71           C  
ANISOU 4844  CA  PRO B 208     2867   2593   2407    119   -151    -89       C  
ATOM   4845  C   PRO B 208     -18.913  -4.433 -15.154  1.00 19.04           C  
ANISOU 4845  C   PRO B 208     2676   2363   2197    115   -119    -77       C  
ATOM   4846  O   PRO B 208     -19.840  -4.536 -14.347  1.00 17.85           O  
ANISOU 4846  O   PRO B 208     2563   2194   2025    102    -97    -74       O  
ATOM   4847  CB  PRO B 208     -17.886  -2.140 -15.285  1.00 16.72           C  
ANISOU 4847  CB  PRO B 208     2325   2099   1929     97   -137    -99       C  
ATOM   4848  CG  PRO B 208     -17.136  -2.116 -16.575  1.00 22.61           C  
ANISOU 4848  CG  PRO B 208     3021   2866   2705    104   -146    -99       C  
ATOM   4849  CD  PRO B 208     -15.929  -2.972 -16.316  1.00 17.69           C  
ANISOU 4849  CD  PRO B 208     2398   2255   2069    130   -183   -100       C  
ATOM   4850  N   PHE B 209     -18.938  -5.039 -16.341  1.00 17.13           N  
ANISOU 4850  N   PHE B 209     2408   2124   1976    123   -113    -72       N  
ATOM   4851  CA  PHE B 209     -20.137  -5.711 -16.817  1.00 16.74           C  
ANISOU 4851  CA  PHE B 209     2372   2058   1932    114    -82    -63       C  
ATOM   4852  C   PHE B 209     -19.786  -7.101 -17.312  1.00 18.27           C  
ANISOU 4852  C   PHE B 209     2575   2243   2122    135    -95    -55       C  
ATOM   4853  O   PHE B 209     -18.616  -7.453 -17.480  1.00 19.97           O  
ANISOU 4853  O   PHE B 209     2779   2470   2339    160   -126    -58       O  
ATOM   4854  CB  PHE B 209     -20.816  -4.931 -17.938  1.00 15.06           C  
ANISOU 4854  CB  PHE B 209     2117   1853   1752     97    -57    -66       C  
ATOM   4855  CG  PHE B 209     -20.998  -3.480 -17.629  1.00 16.74           C  
ANISOU 4855  CG  PHE B 209     2314   2072   1973     80    -50    -75       C  
ATOM   4856  CD1 PHE B 209     -21.808  -3.085 -16.584  1.00 18.75           C  
ANISOU 4856  CD1 PHE B 209     2599   2313   2211     67    -31    -79       C  
ATOM   4857  CD2 PHE B 209     -20.371  -2.512 -18.387  1.00 16.29           C  
ANISOU 4857  CD2 PHE B 209     2217   2034   1940     77    -59    -81       C  
ATOM   4858  CE1 PHE B 209     -21.987  -1.751 -16.291  1.00 16.71           C  
ANISOU 4858  CE1 PHE B 209     2329   2058   1962     54    -24    -90       C  
ATOM   4859  CE2 PHE B 209     -20.542  -1.169 -18.093  1.00 19.40           C  
ANISOU 4859  CE2 PHE B 209     2601   2427   2342     61    -54    -89       C  
ATOM   4860  CZ  PHE B 209     -21.352  -0.795 -17.044  1.00 18.64           C  
ANISOU 4860  CZ  PHE B 209     2536   2316   2232     52    -37    -95       C  
ATOM   4861  N   GLN B 210     -20.832  -7.876 -17.573  1.00 17.44           N  
ANISOU 4861  N   GLN B 210     2491   2119   2017    126    -71    -46       N  
ATOM   4862  CA  GLN B 210     -20.668  -9.270 -17.943  1.00 20.09           C  
ANISOU 4862  CA  GLN B 210     2847   2439   2348    143    -81    -39       C  
ATOM   4863  C   GLN B 210     -20.835  -9.500 -19.439  1.00 21.01           C  
ANISOU 4863  C   GLN B 210     2927   2564   2493    145    -71    -42       C  
ATOM   4864  O   GLN B 210     -19.859  -9.410 -20.192  1.00 23.18           O  
ANISOU 4864  O   GLN B 210     3167   2859   2782    164    -90    -49       O  
ATOM   4865  CB  GLN B 210     -21.638 -10.114 -17.138  1.00 19.00           C  
ANISOU 4865  CB  GLN B 210     2764   2270   2184    129    -63    -27       C  
ATOM   4866  CG  GLN B 210     -21.166 -10.232 -15.691  1.00 19.57           C  
ANISOU 4866  CG  GLN B 210     2883   2332   2220    136    -82    -21       C  
ATOM   4867  CD  GLN B 210     -22.222 -10.786 -14.764  1.00 20.08           C  
ANISOU 4867  CD  GLN B 210     3003   2371   2256    113    -57     -9       C  
ATOM   4868  OE1 GLN B 210     -23.025 -10.042 -14.201  1.00 19.34           O  
ANISOU 4868  OE1 GLN B 210     2913   2281   2155     87    -29    -13       O  
ATOM   4869  NE2 GLN B 210     -22.213 -12.093 -14.582  1.00 20.54           N  
ANISOU 4869  NE2 GLN B 210     3108   2402   2296    121    -67      4       N  
ATOM   4870  N   SER B 211     -22.051  -9.779 -19.894  1.00 17.12           N  
ANISOU 4870  N   SER B 211     2439   2059   2008    123    -42    -38       N  
ATOM   4871  CA  SER B 211     -22.274 -10.214 -21.262  1.00 16.30           C  
ANISOU 4871  CA  SER B 211     2310   1959   1926    125    -35    -40       C  
ATOM   4872  C   SER B 211     -22.944  -9.116 -22.072  1.00 18.97           C  
ANISOU 4872  C   SER B 211     2605   2316   2288    104    -14    -44       C  
ATOM   4873  O   SER B 211     -23.968  -8.560 -21.656  1.00 15.41           O  
ANISOU 4873  O   SER B 211     2157   1859   1839     81      8    -43       O  
ATOM   4874  CB  SER B 211     -23.118 -11.485 -21.308  1.00 18.80           C  
ANISOU 4874  CB  SER B 211     2664   2247   2234    117    -22    -33       C  
ATOM   4875  OG  SER B 211     -22.411 -12.551 -20.702  1.00 28.92           O  
ANISOU 4875  OG  SER B 211     3987   3508   3495    140    -46    -28       O  
ATOM   4876  N   LEU B 212     -22.360  -8.826 -23.235  1.00 17.72           N  
ANISOU 4876  N   LEU B 212     2407   2178   2147    112    -22    -50       N  
ATOM   4877  CA  LEU B 212     -22.927  -7.939 -24.236  1.00 13.87           C  
ANISOU 4877  CA  LEU B 212     1883   1706   1682     95     -8    -52       C  
ATOM   4878  C   LEU B 212     -23.154  -8.746 -25.505  1.00 17.81           C  
ANISOU 4878  C   LEU B 212     2372   2205   2189     98     -5    -53       C  
ATOM   4879  O   LEU B 212     -22.265  -9.494 -25.936  1.00 15.25           O  
ANISOU 4879  O   LEU B 212     2049   1886   1861    120    -20    -58       O  
ATOM   4880  CB  LEU B 212     -21.995  -6.761 -24.519  1.00 14.62           C  
ANISOU 4880  CB  LEU B 212     1942   1826   1786     98    -19    -56       C  
ATOM   4881  CG  LEU B 212     -22.519  -5.735 -25.538  1.00 17.11           C  
ANISOU 4881  CG  LEU B 212     2224   2155   2123     81     -7    -54       C  
ATOM   4882  CD1 LEU B 212     -23.732  -5.002 -24.961  1.00 15.90           C  
ANISOU 4882  CD1 LEU B 212     2078   1989   1976     62     11    -52       C  
ATOM   4883  CD2 LEU B 212     -21.420  -4.759 -25.877  1.00 15.16           C  
ANISOU 4883  CD2 LEU B 212     1946   1931   1882     82    -20    -57       C  
ATOM   4884  N   ILE B 213     -24.346  -8.624 -26.086  1.00 12.40           N  
ANISOU 4884  N   ILE B 213     1678   1516   1516     77     14    -51       N  
ATOM   4885  CA  ILE B 213     -24.637  -9.213 -27.388  1.00 15.32           C  
ANISOU 4885  CA  ILE B 213     2037   1890   1894     76     16    -54       C  
ATOM   4886  C   ILE B 213     -24.925  -8.076 -28.367  1.00 14.65           C  
ANISOU 4886  C   ILE B 213     1914   1827   1827     64     20    -53       C  
ATOM   4887  O   ILE B 213     -25.895  -7.329 -28.180  1.00 15.63           O  
ANISOU 4887  O   ILE B 213     2029   1947   1962     46     33    -49       O  
ATOM   4888  CB  ILE B 213     -25.835 -10.176 -27.340  1.00 16.73           C  
ANISOU 4888  CB  ILE B 213     2240   2045   2071     60     30    -52       C  
ATOM   4889  CG1 ILE B 213     -25.823 -11.070 -26.083  1.00 17.82           C  
ANISOU 4889  CG1 ILE B 213     2423   2156   2190     64     30    -48       C  
ATOM   4890  CG2 ILE B 213     -25.934 -10.960 -28.665  1.00 17.30           C  
ANISOU 4890  CG2 ILE B 213     2305   2119   2148     62     27    -58       C  
ATOM   4891  CD1 ILE B 213     -24.649 -11.948 -25.974  1.00 24.43           C  
ANISOU 4891  CD1 ILE B 213     3281   2987   3014     92      8    -50       C  
ATOM   4892  N   PHE B 214     -24.091  -7.944 -29.401  1.00 12.97           N  
ANISOU 4892  N   PHE B 214     1678   1635   1616     73     11    -56       N  
ATOM   4893  CA  PHE B 214     -24.413  -7.088 -30.549  1.00 14.57           C  
ANISOU 4893  CA  PHE B 214     1851   1854   1830     60     14    -53       C  
ATOM   4894  C   PHE B 214     -25.431  -7.842 -31.385  1.00 11.87           C  
ANISOU 4894  C   PHE B 214     1514   1505   1491     51     20    -54       C  
ATOM   4895  O   PHE B 214     -25.090  -8.815 -32.062  1.00 13.19           O  
ANISOU 4895  O   PHE B 214     1688   1674   1650     60     16    -61       O  
ATOM   4896  CB  PHE B 214     -23.183  -6.781 -31.395  1.00 11.54           C  
ANISOU 4896  CB  PHE B 214     1445   1497   1443     69      5    -56       C  
ATOM   4897  CG  PHE B 214     -22.269  -5.762 -30.808  1.00 12.48           C  
ANISOU 4897  CG  PHE B 214     1550   1628   1563     70     -2    -54       C  
ATOM   4898  CD1 PHE B 214     -21.386  -6.111 -29.793  1.00 14.27           C  
ANISOU 4898  CD1 PHE B 214     1787   1853   1781     87    -11    -60       C  
ATOM   4899  CD2 PHE B 214     -22.260  -4.461 -31.293  1.00 12.35           C  
ANISOU 4899  CD2 PHE B 214     1512   1625   1557     54      0    -47       C  
ATOM   4900  CE1 PHE B 214     -20.521  -5.178 -29.253  1.00 14.39           C  
ANISOU 4900  CE1 PHE B 214     1789   1881   1799     86    -20    -60       C  
ATOM   4901  CE2 PHE B 214     -21.415  -3.513 -30.749  1.00 13.51           C  
ANISOU 4901  CE2 PHE B 214     1648   1781   1705     51     -7    -46       C  
ATOM   4902  CZ  PHE B 214     -20.539  -3.868 -29.727  1.00 11.69           C  
ANISOU 4902  CZ  PHE B 214     1424   1550   1466     66    -17    -54       C  
ATOM   4903  N   LEU B 215     -26.689  -7.445 -31.303  1.00 12.78           N  
ANISOU 4903  N   LEU B 215     1626   1612   1619     33     29    -50       N  
ATOM   4904  CA  LEU B 215     -27.752  -8.063 -32.095  1.00 12.95           C  
ANISOU 4904  CA  LEU B 215     1647   1628   1645     20     33    -52       C  
ATOM   4905  C   LEU B 215     -28.014  -7.150 -33.280  1.00 12.08           C  
ANISOU 4905  C   LEU B 215     1508   1537   1544     13     27    -47       C  
ATOM   4906  O   LEU B 215     -28.519  -6.042 -33.102  1.00 14.54           O  
ANISOU 4906  O   LEU B 215     1805   1850   1869      6     29    -41       O  
ATOM   4907  CB  LEU B 215     -29.029  -8.260 -31.272  1.00 12.47           C  
ANISOU 4907  CB  LEU B 215     1595   1549   1593      5     47    -52       C  
ATOM   4908  CG  LEU B 215     -30.173  -8.882 -32.088  1.00 13.05           C  
ANISOU 4908  CG  LEU B 215     1664   1620   1675    -12     50    -56       C  
ATOM   4909  CD1 LEU B 215     -29.789 -10.245 -32.640  1.00 12.84           C  
ANISOU 4909  CD1 LEU B 215     1659   1586   1634     -7     44    -63       C  
ATOM   4910  CD2 LEU B 215     -31.487  -8.980 -31.282  1.00 10.72           C  
ANISOU 4910  CD2 LEU B 215     1371   1312   1391    -31     67    -57       C  
ATOM   4911  N   VAL B 216     -27.656  -7.602 -34.485  1.00 13.10           N  
ANISOU 4911  N   VAL B 216     1634   1679   1664     15     20    -51       N  
ATOM   4912  CA  VAL B 216     -27.819  -6.806 -35.697  1.00 13.33           C  
ANISOU 4912  CA  VAL B 216     1643   1727   1696      8     13    -44       C  
ATOM   4913  C   VAL B 216     -29.132  -7.208 -36.370  1.00 13.74           C  
ANISOU 4913  C   VAL B 216     1692   1775   1755     -6     10    -47       C  
ATOM   4914  O   VAL B 216     -29.231  -8.280 -36.976  1.00 13.66           O  
ANISOU 4914  O   VAL B 216     1693   1763   1735     -7      8    -56       O  
ATOM   4915  CB  VAL B 216     -26.640  -6.972 -36.660  1.00 12.16           C  
ANISOU 4915  CB  VAL B 216     1490   1600   1530     16      8    -48       C  
ATOM   4916  CG1 VAL B 216     -26.834  -6.041 -37.841  1.00 13.23           C  
ANISOU 4916  CG1 VAL B 216     1609   1753   1664      4      1    -38       C  
ATOM   4917  CG2 VAL B 216     -25.303  -6.702 -35.946  1.00 11.44           C  
ANISOU 4917  CG2 VAL B 216     1397   1515   1433     30      9    -49       C  
ATOM   4918  N   ARG B 217     -30.143  -6.351 -36.273  1.00  9.62           N  
ANISOU 4918  N   ARG B 217     1154   1249   1251    -16      8    -39       N  
ATOM   4919  CA  ARG B 217     -31.381  -6.610 -36.988  1.00 11.45           C  
ANISOU 4919  CA  ARG B 217     1378   1482   1492    -29      2    -42       C  
ATOM   4920  C   ARG B 217     -31.178  -6.295 -38.460  1.00 12.99           C  
ANISOU 4920  C   ARG B 217     1565   1696   1676    -31    -14    -37       C  
ATOM   4921  O   ARG B 217     -30.372  -5.427 -38.824  1.00 11.68           O  
ANISOU 4921  O   ARG B 217     1395   1542   1502    -26    -19    -27       O  
ATOM   4922  CB  ARG B 217     -32.533  -5.758 -36.440  1.00 10.97           C  
ANISOU 4922  CB  ARG B 217     1298   1415   1456    -35      4    -38       C  
ATOM   4923  CG  ARG B 217     -32.700  -5.853 -34.929  1.00 11.09           C  
ANISOU 4923  CG  ARG B 217     1320   1413   1479    -34     23    -43       C  
ATOM   4924  CD  ARG B 217     -33.091  -7.268 -34.499  1.00 10.25           C  
ANISOU 4924  CD  ARG B 217     1233   1295   1368    -44     35    -53       C  
ATOM   4925  NE  ARG B 217     -34.540  -7.449 -34.454  1.00 13.91           N  
ANISOU 4925  NE  ARG B 217     1680   1756   1849    -61     40    -59       N  
ATOM   4926  CZ  ARG B 217     -35.275  -7.260 -33.368  1.00 13.98           C  
ANISOU 4926  CZ  ARG B 217     1682   1757   1871    -68     58    -63       C  
ATOM   4927  NH1 ARG B 217     -34.729  -6.868 -32.230  1.00 12.94           N  
ANISOU 4927  NH1 ARG B 217     1564   1617   1734    -60     71    -61       N  
ATOM   4928  NH2 ARG B 217     -36.586  -7.489 -33.416  1.00 13.21           N  
ANISOU 4928  NH2 ARG B 217     1566   1662   1792    -85     64    -71       N  
ATOM   4929  N   ASP B 218     -31.904  -7.028 -39.305  1.00 11.71           N  
ANISOU 4929  N   ASP B 218     1403   1536   1510    -40    -23    -44       N  
ATOM   4930  CA  ASP B 218     -31.907  -6.807 -40.750  1.00 12.09           C  
ANISOU 4930  CA  ASP B 218     1448   1603   1544    -44    -40    -40       C  
ATOM   4931  C   ASP B 218     -30.502  -6.893 -41.326  1.00 13.62           C  
ANISOU 4931  C   ASP B 218     1652   1812   1712    -36    -36    -40       C  
ATOM   4932  O   ASP B 218     -30.156  -6.141 -42.238  1.00 12.64           O  
ANISOU 4932  O   ASP B 218     1524   1705   1575    -39    -45    -29       O  
ATOM   4933  CB  ASP B 218     -32.538  -5.463 -41.131  1.00 12.00           C  
ANISOU 4933  CB  ASP B 218     1417   1597   1546    -47    -55    -24       C  
ATOM   4934  CG  ASP B 218     -33.920  -5.286 -40.577  1.00 15.48           C  
ANISOU 4934  CG  ASP B 218     1840   2027   2016    -52    -58    -27       C  
ATOM   4935  OD1 ASP B 218     -34.480  -6.275 -40.056  1.00 15.41           O  
ANISOU 4935  OD1 ASP B 218     1834   2008   2014    -59    -48    -40       O  
ATOM   4936  OD2 ASP B 218     -34.438  -4.145 -40.645  1.00 13.81           O  
ANISOU 4936  OD2 ASP B 218     1613   1815   1821    -48    -69    -15       O  
ATOM   4937  N   TRP B 219     -29.677  -7.793 -40.783  1.00 10.37           N  
ANISOU 4937  N   TRP B 219     1255   1394   1291    -26    -23    -52       N  
ATOM   4938  CA  TRP B 219     -28.412  -8.082 -41.440  1.00 12.02           C  
ANISOU 4938  CA  TRP B 219     1470   1621   1476    -16    -20    -58       C  
ATOM   4939  C   TRP B 219     -28.694  -8.480 -42.882  1.00 14.53           C  
ANISOU 4939  C   TRP B 219     1793   1954   1775    -25    -30    -65       C  
ATOM   4940  O   TRP B 219     -29.550  -9.331 -43.153  1.00 12.93           O  
ANISOU 4940  O   TRP B 219     1599   1741   1573    -32    -36    -76       O  
ATOM   4941  CB  TRP B 219     -27.656  -9.194 -40.712  1.00 12.11           C  
ANISOU 4941  CB  TRP B 219     1498   1621   1484      0     -9    -74       C  
ATOM   4942  CG  TRP B 219     -26.362  -9.563 -41.384  1.00 12.39           C  
ANISOU 4942  CG  TRP B 219     1535   1676   1496     14     -4    -85       C  
ATOM   4943  CD1 TRP B 219     -26.080 -10.717 -42.067  1.00 14.08           C  
ANISOU 4943  CD1 TRP B 219     1763   1892   1693     22     -4   -105       C  
ATOM   4944  CD2 TRP B 219     -25.179  -8.761 -41.447  1.00 14.05           C  
ANISOU 4944  CD2 TRP B 219     1729   1909   1699     20      2    -79       C  
ATOM   4945  NE1 TRP B 219     -24.789 -10.682 -42.540  1.00 13.91           N  
ANISOU 4945  NE1 TRP B 219     1734   1895   1655     36      4   -113       N  
ATOM   4946  CE2 TRP B 219     -24.216  -9.491 -42.176  1.00 14.75           C  
ANISOU 4946  CE2 TRP B 219     1821   2016   1767     33      8    -97       C  
ATOM   4947  CE3 TRP B 219     -24.842  -7.489 -40.965  1.00 12.45           C  
ANISOU 4947  CE3 TRP B 219     1511   1713   1505     14      3    -62       C  
ATOM   4948  CZ2 TRP B 219     -22.944  -8.997 -42.426  1.00 14.31           C  
ANISOU 4948  CZ2 TRP B 219     1748   1988   1700     39     17    -98       C  
ATOM   4949  CZ3 TRP B 219     -23.564  -7.000 -41.210  1.00 14.99           C  
ANISOU 4949  CZ3 TRP B 219     1819   2061   1817     18     10    -62       C  
ATOM   4950  CH2 TRP B 219     -22.640  -7.745 -41.944  1.00 14.56           C  
ANISOU 4950  CH2 TRP B 219     1763   2027   1741     29     18    -80       C  
ATOM   4951  N   SER B 220     -27.989  -7.852 -43.815  1.00 10.63           N  
ANISOU 4951  N   SER B 220     1294   1484   1261    -27    -31    -58       N  
ATOM   4952  CA  SER B 220     -28.331  -7.999 -45.224  1.00 14.35           C  
ANISOU 4952  CA  SER B 220     1771   1971   1709    -38    -42    -60       C  
ATOM   4953  C   SER B 220     -27.307  -8.780 -46.032  1.00 14.52           C  
ANISOU 4953  C   SER B 220     1803   2013   1701    -30    -32    -78       C  
ATOM   4954  O   SER B 220     -27.500  -8.961 -47.237  1.00 13.98           O  
ANISOU 4954  O   SER B 220     1743   1960   1609    -39    -39    -83       O  
ATOM   4955  CB  SER B 220     -28.524  -6.615 -45.847  1.00 16.53           C  
ANISOU 4955  CB  SER B 220     2038   2261   1982    -50    -54    -35       C  
ATOM   4956  OG  SER B 220     -29.533  -5.931 -45.137  1.00 16.53           O  
ANISOU 4956  OG  SER B 220     2027   2242   2012    -53    -64    -22       O  
ATOM   4957  N   PHE B 221     -26.222  -9.238 -45.422  1.00 12.96           N  
ANISOU 4957  N   PHE B 221     1606   1816   1503    -12    -16    -90       N  
ATOM   4958  CA  PHE B 221     -25.107  -9.819 -46.171  1.00 13.46           C  
ANISOU 4958  CA  PHE B 221     1673   1903   1540     -1     -3   -109       C  
ATOM   4959  C   PHE B 221     -24.764 -11.205 -45.636  1.00 14.86           C  
ANISOU 4959  C   PHE B 221     1865   2062   1721     22      3   -135       C  
ATOM   4960  O   PHE B 221     -23.615 -11.483 -45.276  1.00 14.54           O  
ANISOU 4960  O   PHE B 221     1817   2029   1677     42     15   -147       O  
ATOM   4961  CB  PHE B 221     -23.902  -8.877 -46.129  1.00 15.52           C  
ANISOU 4961  CB  PHE B 221     1914   2188   1793      0     10    -99       C  
ATOM   4962  CG  PHE B 221     -24.278  -7.417 -46.311  1.00 17.44           C  
ANISOU 4962  CG  PHE B 221     2148   2438   2041    -22      3    -69       C  
ATOM   4963  CD1 PHE B 221     -24.854  -6.979 -47.495  1.00 16.84           C  
ANISOU 4963  CD1 PHE B 221     2079   2374   1944    -41     -8    -58       C  
ATOM   4964  CD2 PHE B 221     -24.078  -6.496 -45.290  1.00 18.83           C  
ANISOU 4964  CD2 PHE B 221     2311   2604   2239    -23      3    -52       C  
ATOM   4965  CE1 PHE B 221     -25.221  -5.644 -47.667  1.00 20.31           C  
ANISOU 4965  CE1 PHE B 221     2515   2814   2387    -58    -19    -29       C  
ATOM   4966  CE2 PHE B 221     -24.437  -5.165 -45.457  1.00 18.64           C  
ANISOU 4966  CE2 PHE B 221     2282   2580   2219    -41     -5    -26       C  
ATOM   4967  CZ  PHE B 221     -25.011  -4.740 -46.643  1.00 17.36           C  
ANISOU 4967  CZ  PHE B 221     2129   2429   2039    -58    -17    -13       C  
ATOM   4968  N   PRO B 222     -25.735 -12.123 -45.616  1.00 13.76           N  
ANISOU 4968  N   PRO B 222     1744   1897   1587     18     -7   -145       N  
ATOM   4969  CA  PRO B 222     -25.424 -13.497 -45.183  1.00 14.10           C  
ANISOU 4969  CA  PRO B 222     1808   1918   1632     38     -4   -169       C  
ATOM   4970  C   PRO B 222     -24.372 -14.172 -46.044  1.00 13.84           C  
ANISOU 4970  C   PRO B 222     1780   1905   1574     58      6   -195       C  
ATOM   4971  O   PRO B 222     -23.712 -15.100 -45.571  1.00 17.12           O  
ANISOU 4971  O   PRO B 222     2207   2306   1992     84     10   -214       O  
ATOM   4972  CB  PRO B 222     -26.783 -14.214 -45.287  1.00 13.62           C  
ANISOU 4972  CB  PRO B 222     1766   1831   1579     21    -17   -174       C  
ATOM   4973  CG  PRO B 222     -27.489 -13.496 -46.374  1.00 14.56           C  
ANISOU 4973  CG  PRO B 222     1875   1971   1686     -2    -27   -164       C  
ATOM   4974  CD  PRO B 222     -27.083 -12.045 -46.216  1.00 14.43           C  
ANISOU 4974  CD  PRO B 222     1834   1976   1673     -5    -24   -139       C  
ATOM   4975  N   TYR B 223     -24.188 -13.741 -47.293  1.00 14.58           N  
ANISOU 4975  N   TYR B 223     1867   2031   1641     47      9   -197       N  
ATOM   4976  CA  TYR B 223     -23.135 -14.319 -48.118  1.00 15.60           C  
ANISOU 4976  CA  TYR B 223     1998   2184   1744     65     23   -224       C  
ATOM   4977  C   TYR B 223     -21.759 -13.871 -47.669  1.00 16.92           C  
ANISOU 4977  C   TYR B 223     2140   2374   1914     85     40   -224       C  
ATOM   4978  O   TYR B 223     -20.754 -14.469 -48.068  1.00 18.96           O  
ANISOU 4978  O   TYR B 223     2395   2651   2159    108     53   -251       O  
ATOM   4979  CB  TYR B 223     -23.343 -13.953 -49.589  1.00 15.13           C  
ANISOU 4979  CB  TYR B 223     1942   2156   1652     44     24   -225       C  
ATOM   4980  CG  TYR B 223     -23.592 -12.478 -49.796  1.00 15.62           C  
ANISOU 4980  CG  TYR B 223     1985   2237   1711     19     20   -191       C  
ATOM   4981  CD1 TYR B 223     -22.537 -11.578 -49.922  1.00 16.41           C  
ANISOU 4981  CD1 TYR B 223     2064   2370   1802     17     37   -181       C  
ATOM   4982  CD2 TYR B 223     -24.889 -11.982 -49.855  1.00 15.17           C  
ANISOU 4982  CD2 TYR B 223     1934   2166   1664     -5     -1   -169       C  
ATOM   4983  CE1 TYR B 223     -22.776 -10.218 -50.116  1.00 17.07           C  
ANISOU 4983  CE1 TYR B 223     2135   2466   1883     -8     33   -148       C  
ATOM   4984  CE2 TYR B 223     -25.138 -10.643 -50.054  1.00 15.59           C  
ANISOU 4984  CE2 TYR B 223     1975   2233   1717    -25     -7   -139       C  
ATOM   4985  CZ  TYR B 223     -24.086  -9.758 -50.180  1.00 20.67           C  
ANISOU 4985  CZ  TYR B 223     2601   2903   2348    -27     10   -127       C  
ATOM   4986  OH  TYR B 223     -24.360  -8.419 -50.374  1.00 19.59           O  
ANISOU 4986  OH  TYR B 223     2458   2775   2212    -48      1    -95       O  
ATOM   4987  N   GLU B 224     -21.688 -12.818 -46.872  1.00 14.24           N  
ANISOU 4987  N   GLU B 224     1780   2036   1593     76     39   -198       N  
ATOM   4988  CA  GLU B 224     -20.430 -12.349 -46.317  1.00 18.50           C  
ANISOU 4988  CA  GLU B 224     2294   2596   2139     91     52   -198       C  
ATOM   4989  C   GLU B 224     -20.193 -12.904 -44.921  1.00 16.45           C  
ANISOU 4989  C   GLU B 224     2038   2307   1905    116     45   -202       C  
ATOM   4990  O   GLU B 224     -19.134 -13.464 -44.646  1.00 14.92           O  
ANISOU 4990  O   GLU B 224     1836   2121   1712    146     51   -222       O  
ATOM   4991  CB  GLU B 224     -20.435 -10.821 -46.288  1.00 17.99           C  
ANISOU 4991  CB  GLU B 224     2208   2550   2077     64     53   -167       C  
ATOM   4992  CG  GLU B 224     -19.078 -10.196 -46.280  1.00 24.11           C  
ANISOU 4992  CG  GLU B 224     2954   3360   2847     67     70   -169       C  
ATOM   4993  CD  GLU B 224     -19.158  -8.677 -46.220  1.00 24.90           C  
ANISOU 4993  CD  GLU B 224     3039   3471   2950     37     70   -137       C  
ATOM   4994  OE1 GLU B 224     -20.080  -8.150 -45.570  1.00 22.91           O  
ANISOU 4994  OE1 GLU B 224     2795   3191   2717     26     55   -115       O  
ATOM   4995  OE2 GLU B 224     -18.310  -8.013 -46.833  1.00 34.55           O  
ANISOU 4995  OE2 GLU B 224     4243   4729   4157     23     85   -134       O  
ATOM   4996  N   PHE B 225     -21.172 -12.754 -44.033  1.00 14.30           N  
ANISOU 4996  N   PHE B 225     1779   2002   1654    105     32   -183       N  
ATOM   4997  CA  PHE B 225     -21.167 -13.363 -42.713  1.00 11.56           C  
ANISOU 4997  CA  PHE B 225     1445   1621   1326    124     24   -185       C  
ATOM   4998  C   PHE B 225     -22.537 -13.975 -42.504  1.00 14.58           C  
ANISOU 4998  C   PHE B 225     1857   1967   1717    111     14   -181       C  
ATOM   4999  O   PHE B 225     -23.552 -13.308 -42.715  1.00 12.25           O  
ANISOU 4999  O   PHE B 225     1559   1670   1426     83     10   -164       O  
ATOM   5000  CB  PHE B 225     -20.855 -12.347 -41.600  1.00 14.68           C  
ANISOU 5000  CB  PHE B 225     1821   2018   1738    121     23   -164       C  
ATOM   5001  CG  PHE B 225     -19.523 -11.673 -41.757  1.00 16.37           C  
ANISOU 5001  CG  PHE B 225     2003   2269   1947    129     33   -167       C  
ATOM   5002  CD1 PHE B 225     -18.367 -12.279 -41.296  1.00 16.20           C  
ANISOU 5002  CD1 PHE B 225     1973   2254   1927    162     33   -186       C  
ATOM   5003  CD2 PHE B 225     -19.421 -10.434 -42.387  1.00 17.86           C  
ANISOU 5003  CD2 PHE B 225     2170   2487   2129    103     40   -151       C  
ATOM   5004  CE1 PHE B 225     -17.135 -11.659 -41.451  1.00 15.28           C  
ANISOU 5004  CE1 PHE B 225     1822   2177   1808    167     42   -192       C  
ATOM   5005  CE2 PHE B 225     -18.191  -9.819 -42.537  1.00 18.59           C  
ANISOU 5005  CE2 PHE B 225     2232   2614   2216    105     51   -155       C  
ATOM   5006  CZ  PHE B 225     -17.054 -10.438 -42.066  1.00 14.70           C  
ANISOU 5006  CZ  PHE B 225     1726   2132   1727    136     53   -176       C  
ATOM   5007  N   SER B 226     -22.558 -15.248 -42.126  1.00 14.40           N  
ANISOU 5007  N   SER B 226     1861   1913   1696    130      9   -198       N  
ATOM   5008  CA  SER B 226     -23.802 -15.997 -42.010  1.00 17.94           C  
ANISOU 5008  CA  SER B 226     2339   2326   2150    113      1   -198       C  
ATOM   5009  C   SER B 226     -24.710 -15.402 -40.944  1.00 12.99           C  
ANISOU 5009  C   SER B 226     1712   1681   1543     92     -1   -174       C  
ATOM   5010  O   SER B 226     -24.258 -14.897 -39.912  1.00 13.43           O  
ANISOU 5010  O   SER B 226     1759   1735   1608    101      1   -162       O  
ATOM   5011  CB  SER B 226     -23.490 -17.451 -41.655  1.00 14.22           C  
ANISOU 5011  CB  SER B 226     1903   1822   1679    139     -3   -219       C  
ATOM   5012  OG  SER B 226     -22.710 -18.024 -42.675  1.00 18.59           O  
ANISOU 5012  OG  SER B 226     2456   2392   2214    160      0   -246       O  
ATOM   5013  N   TYR B 227     -26.012 -15.471 -41.193  1.00 14.05           N  
ANISOU 5013  N   TYR B 227     1853   1802   1683     64     -5   -168       N  
ATOM   5014  CA  TYR B 227     -26.949 -15.192 -40.120  1.00 14.74           C  
ANISOU 5014  CA  TYR B 227     1944   1868   1790     47     -5   -151       C  
ATOM   5015  C   TYR B 227     -26.600 -16.051 -38.910  1.00 15.44           C  
ANISOU 5015  C   TYR B 227     2060   1924   1883     63     -4   -154       C  
ATOM   5016  O   TYR B 227     -26.190 -17.210 -39.045  1.00 14.69           O  
ANISOU 5016  O   TYR B 227     1993   1810   1779     80     -7   -171       O  
ATOM   5017  CB  TYR B 227     -28.373 -15.484 -40.572  1.00 11.98           C  
ANISOU 5017  CB  TYR B 227     1599   1507   1445     16    -10   -152       C  
ATOM   5018  CG  TYR B 227     -28.880 -14.609 -41.685  1.00 14.10           C  
ANISOU 5018  CG  TYR B 227     1842   1805   1710      0    -16   -146       C  
ATOM   5019  CD1 TYR B 227     -28.803 -13.231 -41.592  1.00 13.91           C  
ANISOU 5019  CD1 TYR B 227     1790   1802   1692     -3    -15   -127       C  
ATOM   5020  CD2 TYR B 227     -29.465 -15.169 -42.821  1.00 13.12           C  
ANISOU 5020  CD2 TYR B 227     1726   1684   1575    -14    -26   -160       C  
ATOM   5021  CE1 TYR B 227     -29.293 -12.428 -42.592  1.00 12.98           C  
ANISOU 5021  CE1 TYR B 227     1654   1707   1570    -18    -24   -120       C  
ATOM   5022  CE2 TYR B 227     -29.950 -14.385 -43.827  1.00 15.19           C  
ANISOU 5022  CE2 TYR B 227     1969   1972   1831    -29    -36   -153       C  
ATOM   5023  CZ  TYR B 227     -29.863 -13.009 -43.702  1.00 15.17           C  
ANISOU 5023  CZ  TYR B 227     1940   1989   1836    -30    -35   -132       C  
ATOM   5024  OH  TYR B 227     -30.344 -12.214 -44.689  1.00 16.88           O  
ANISOU 5024  OH  TYR B 227     2141   2228   2045    -43    -48   -123       O  
ATOM   5025  N   GLY B 228     -26.757 -15.486 -37.730  1.00 14.29           N  
ANISOU 5025  N   GLY B 228     1910   1770   1748     59      1   -137       N  
ATOM   5026  CA  GLY B 228     -26.575 -16.251 -36.514  1.00 15.03           C  
ANISOU 5026  CA  GLY B 228     2036   1831   1843     70      1   -135       C  
ATOM   5027  C   GLY B 228     -25.399 -15.760 -35.692  1.00 18.20           C  
ANISOU 5027  C   GLY B 228     2431   2243   2243     96     -1   -130       C  
ATOM   5028  O   GLY B 228     -24.856 -14.667 -35.905  1.00 17.04           O  
ANISOU 5028  O   GLY B 228     2251   2127   2097     99      0   -125       O  
ATOM   5029  N   ALA B 229     -25.013 -16.603 -34.719  1.00 15.13           N  
ANISOU 5029  N   ALA B 229     2074   1823   1850    113     -7   -131       N  
ATOM   5030  CA  ALA B 229     -23.952 -16.267 -33.782  1.00 15.15           C  
ANISOU 5030  CA  ALA B 229     2075   1832   1851    139    -13   -126       C  
ATOM   5031  C   ALA B 229     -22.555 -16.517 -34.336  1.00 16.53           C  
ANISOU 5031  C   ALA B 229     2236   2026   2019    176    -23   -143       C  
ATOM   5032  O   ALA B 229     -21.595 -15.896 -33.861  1.00 18.24           O  
ANISOU 5032  O   ALA B 229     2432   2262   2236    193    -28   -140       O  
ATOM   5033  CB  ALA B 229     -24.119 -17.062 -32.481  1.00 17.68           C  
ANISOU 5033  CB  ALA B 229     2439   2112   2166    143    -18   -118       C  
ATOM   5034  N   ASP B 230     -22.406 -17.417 -35.307  1.00 16.14           N  
ANISOU 5034  N   ASP B 230     2196   1972   1964    188    -25   -162       N  
ATOM   5035  CA  ASP B 230     -21.068 -17.685 -35.821  1.00 15.00           C  
ANISOU 5035  CA  ASP B 230     2037   1849   1814    226    -31   -181       C  
ATOM   5036  C   ASP B 230     -20.654 -16.635 -36.843  1.00 16.12           C  
ANISOU 5036  C   ASP B 230     2132   2040   1954    217    -20   -185       C  
ATOM   5037  O   ASP B 230     -19.559 -16.074 -36.758  1.00 16.21           O  
ANISOU 5037  O   ASP B 230     2113   2081   1966    235    -21   -188       O  
ATOM   5038  CB  ASP B 230     -21.006 -19.088 -36.424  1.00 17.52           C  
ANISOU 5038  CB  ASP B 230     2388   2142   2127    246    -37   -204       C  
ATOM   5039  CG  ASP B 230     -19.599 -19.501 -36.763  1.00 28.51           C  
ANISOU 5039  CG  ASP B 230     3766   3550   3515    292    -44   -227       C  
ATOM   5040  OD1 ASP B 230     -18.817 -19.756 -35.818  1.00 30.68           O  
ANISOU 5040  OD1 ASP B 230     4049   3814   3793    322    -58   -226       O  
ATOM   5041  OD2 ASP B 230     -19.275 -19.550 -37.968  1.00 34.01           O  
ANISOU 5041  OD2 ASP B 230     4444   4275   4205    297    -35   -247       O  
ATOM   5042  N   GLY B 231     -21.516 -16.350 -37.820  1.00 15.96           N  
ANISOU 5042  N   GLY B 231     2105   2029   1931    188    -11   -183       N  
ATOM   5043  CA  GLY B 231     -21.269 -15.208 -38.681  1.00 14.75           C  
ANISOU 5043  CA  GLY B 231     1913   1919   1774    174     -2   -179       C  
ATOM   5044  C   GLY B 231     -21.167 -13.922 -37.885  1.00 12.36           C  
ANISOU 5044  C   GLY B 231     1587   1630   1481    161     -1   -158       C  
ATOM   5045  O   GLY B 231     -20.301 -13.081 -38.152  1.00 14.14           O  
ANISOU 5045  O   GLY B 231     1781   1889   1704    164      3   -157       O  
ATOM   5046  N   GLY B 232     -22.020 -13.778 -36.867  1.00 12.89           N  
ANISOU 5046  N   GLY B 232     1670   1669   1557    147     -3   -142       N  
ATOM   5047  CA  GLY B 232     -21.923 -12.631 -35.979  1.00 13.61           C  
ANISOU 5047  CA  GLY B 232     1745   1768   1658    137     -3   -124       C  
ATOM   5048  C   GLY B 232     -20.565 -12.529 -35.311  1.00 14.24           C  
ANISOU 5048  C   GLY B 232     1814   1860   1737    164    -10   -130       C  
ATOM   5049  O   GLY B 232     -19.952 -11.459 -35.286  1.00 12.67           O  
ANISOU 5049  O   GLY B 232     1586   1688   1541    159     -8   -124       O  
ATOM   5050  N   ALA B 233     -20.067 -13.651 -34.774  1.00 14.16           N  
ANISOU 5050  N   ALA B 233     1828   1830   1723    193    -20   -141       N  
ATOM   5051  CA  ALA B 233     -18.770 -13.639 -34.099  1.00 17.00           C  
ANISOU 5051  CA  ALA B 233     2176   2201   2083    223    -32   -148       C  
ATOM   5052  C   ALA B 233     -17.656 -13.259 -35.063  1.00 16.73           C  
ANISOU 5052  C   ALA B 233     2100   2210   2046    234    -27   -163       C  
ATOM   5053  O   ALA B 233     -16.759 -12.482 -34.710  1.00 18.72           O  
ANISOU 5053  O   ALA B 233     2322   2488   2302    238    -30   -162       O  
ATOM   5054  CB  ALA B 233     -18.481 -15.005 -33.457  1.00 18.71           C  
ANISOU 5054  CB  ALA B 233     2429   2384   2296    256    -47   -157       C  
ATOM   5055  N   LYS B 234     -17.689 -13.800 -36.279  1.00 14.56           N  
ANISOU 5055  N   LYS B 234     1822   1945   1764    238    -18   -178       N  
ATOM   5056  CA  LYS B 234     -16.662 -13.469 -37.262  1.00 16.69           C  
ANISOU 5056  CA  LYS B 234     2054   2260   2029    245     -9   -194       C  
ATOM   5057  C   LYS B 234     -16.757 -12.006 -37.666  1.00 16.22           C  
ANISOU 5057  C   LYS B 234     1964   2230   1969    209      3   -177       C  
ATOM   5058  O   LYS B 234     -15.741 -11.307 -37.784  1.00 17.83           O  
ANISOU 5058  O   LYS B 234     2131   2469   2173    210      8   -180       O  
ATOM   5059  CB  LYS B 234     -16.801 -14.368 -38.492  1.00 17.82           C  
ANISOU 5059  CB  LYS B 234     2206   2404   2159    254      0   -214       C  
ATOM   5060  CG  LYS B 234     -16.544 -15.838 -38.208  1.00 23.34           C  
ANISOU 5060  CG  LYS B 234     2936   3074   2858    293    -12   -235       C  
ATOM   5061  CD  LYS B 234     -16.697 -16.652 -39.487  1.00 26.92           C  
ANISOU 5061  CD  LYS B 234     3400   3530   3299    300     -3   -258       C  
ATOM   5062  CE  LYS B 234     -16.059 -18.030 -39.352  1.00 33.19           C  
ANISOU 5062  CE  LYS B 234     4215   4302   4094    347    -14   -285       C  
ATOM   5063  NZ  LYS B 234     -16.772 -18.889 -38.382  1.00 28.84           N  
ANISOU 5063  NZ  LYS B 234     3715   3694   3550    353    -32   -275       N  
ATOM   5064  N   PHE B 235     -17.977 -11.530 -37.908  1.00 13.65           N  
ANISOU 5064  N   PHE B 235     1653   1891   1644    178      8   -159       N  
ATOM   5065  CA  PHE B 235     -18.164 -10.128 -38.240  1.00 14.35           C  
ANISOU 5065  CA  PHE B 235     1719   2000   1734    145     15   -140       C  
ATOM   5066  C   PHE B 235     -17.649  -9.240 -37.113  1.00 18.70           C  
ANISOU 5066  C   PHE B 235     2256   2554   2297    143      9   -129       C  
ATOM   5067  O   PHE B 235     -16.877  -8.302 -37.337  1.00 15.79           O  
ANISOU 5067  O   PHE B 235     1857   2215   1928    131     14   -126       O  
ATOM   5068  CB  PHE B 235     -19.646  -9.858 -38.521  1.00 16.08           C  
ANISOU 5068  CB  PHE B 235     1956   2198   1954    118     16   -124       C  
ATOM   5069  CG  PHE B 235     -19.986  -8.403 -38.593  1.00 17.33           C  
ANISOU 5069  CG  PHE B 235     2100   2366   2119     89     18   -102       C  
ATOM   5070  CD1 PHE B 235     -19.671  -7.666 -39.714  1.00 15.71           C  
ANISOU 5070  CD1 PHE B 235     1875   2191   1902     72     26    -97       C  
ATOM   5071  CD2 PHE B 235     -20.606  -7.766 -37.526  1.00 22.22           C  
ANISOU 5071  CD2 PHE B 235     2726   2963   2753     80     12    -87       C  
ATOM   5072  CE1 PHE B 235     -19.981  -6.323 -39.778  1.00 18.40           C  
ANISOU 5072  CE1 PHE B 235     2208   2536   2249     46     26    -76       C  
ATOM   5073  CE2 PHE B 235     -20.917  -6.415 -37.584  1.00 22.85           C  
ANISOU 5073  CE2 PHE B 235     2794   3049   2840     56     13    -69       C  
ATOM   5074  CZ  PHE B 235     -20.603  -5.697 -38.709  1.00 23.15           C  
ANISOU 5074  CZ  PHE B 235     2815   3112   2868     39     18    -62       C  
ATOM   5075  N   LEU B 236     -18.045  -9.543 -35.883  1.00 15.38           N  
ANISOU 5075  N   LEU B 236     1858   2102   1885    152     -3   -124       N  
ATOM   5076  CA  LEU B 236     -17.730  -8.633 -34.797  1.00 17.20           C  
ANISOU 5076  CA  LEU B 236     2080   2332   2124    145     -9   -113       C  
ATOM   5077  C   LEU B 236     -16.270  -8.736 -34.396  1.00 18.36           C  
ANISOU 5077  C   LEU B 236     2204   2502   2271    169    -18   -127       C  
ATOM   5078  O   LEU B 236     -15.677  -7.742 -33.973  1.00 21.12           O  
ANISOU 5078  O   LEU B 236     2531   2868   2627    157    -21   -122       O  
ATOM   5079  CB  LEU B 236     -18.642  -8.903 -33.601  1.00 17.10           C  
ANISOU 5079  CB  LEU B 236     2100   2280   2116    145    -16   -104       C  
ATOM   5080  CG  LEU B 236     -18.564  -7.811 -32.532  1.00 18.30           C  
ANISOU 5080  CG  LEU B 236     2248   2430   2276    133    -21    -92       C  
ATOM   5081  CD1 LEU B 236     -19.218  -6.527 -33.026  1.00 15.95           C  
ANISOU 5081  CD1 LEU B 236     1937   2139   1985    101    -12    -78       C  
ATOM   5082  CD2 LEU B 236     -19.181  -8.283 -31.223  1.00 17.94           C  
ANISOU 5082  CD2 LEU B 236     2237   2351   2229    139    -28    -87       C  
ATOM   5083  N   GLU B 237     -15.677  -9.921 -34.531  1.00 17.65           N  
ANISOU 5083  N   GLU B 237     2118   2412   2177    202    -24   -146       N  
ATOM   5084  CA  GLU B 237     -14.253 -10.063 -34.271  1.00 22.94           C  
ANISOU 5084  CA  GLU B 237     2759   3109   2849    229    -34   -163       C  
ATOM   5085  C   GLU B 237     -13.458  -9.090 -35.131  1.00 23.52           C  
ANISOU 5085  C   GLU B 237     2786   3228   2922    209    -19   -167       C  
ATOM   5086  O   GLU B 237     -12.546  -8.413 -34.644  1.00 23.32           O  
ANISOU 5086  O   GLU B 237     2732   3226   2903    207    -26   -169       O  
ATOM   5087  CB  GLU B 237     -13.823 -11.508 -34.521  1.00 22.20           C  
ANISOU 5087  CB  GLU B 237     2677   3008   2751    270    -40   -186       C  
ATOM   5088  CG  GLU B 237     -12.468 -11.885 -33.911  1.00 30.82           C  
ANISOU 5088  CG  GLU B 237     3747   4117   3848    309    -59   -204       C  
ATOM   5089  CD  GLU B 237     -11.303 -11.308 -34.693  1.00 40.24           C  
ANISOU 5089  CD  GLU B 237     4882   5363   5043    307    -47   -220       C  
ATOM   5090  OE1 GLU B 237     -11.467 -11.127 -35.921  1.00 40.82           O  
ANISOU 5090  OE1 GLU B 237     4942   5458   5108    289    -23   -224       O  
ATOM   5091  OE2 GLU B 237     -10.237 -11.025 -34.086  1.00 43.93           O  
ANISOU 5091  OE2 GLU B 237     5318   5854   5518    321    -61   -229       O  
ATOM   5092  N   LYS B 238     -13.807  -9.000 -36.416  1.00 19.80           N  
ANISOU 5092  N   LYS B 238     2310   2772   2441    192      0   -167       N  
ATOM   5093  CA  LYS B 238     -13.163  -8.040 -37.304  1.00 19.73           C  
ANISOU 5093  CA  LYS B 238     2263   2805   2428    166     17   -167       C  
ATOM   5094  C   LYS B 238     -13.525  -6.606 -36.929  1.00 21.03           C  
ANISOU 5094  C   LYS B 238     2425   2966   2600    128     16   -142       C  
ATOM   5095  O   LYS B 238     -12.659  -5.725 -36.892  1.00 19.94           O  
ANISOU 5095  O   LYS B 238     2254   2856   2465    111     19   -141       O  
ATOM   5096  CB  LYS B 238     -13.565  -8.326 -38.749  1.00 20.76           C  
ANISOU 5096  CB  LYS B 238     2397   2947   2542    156     36   -171       C  
ATOM   5097  CG  LYS B 238     -12.852  -7.446 -39.754  1.00 30.32           C  
ANISOU 5097  CG  LYS B 238     3574   4205   3743    129     56   -171       C  
ATOM   5098  CD  LYS B 238     -13.256  -7.756 -41.194  1.00 28.80           C  
ANISOU 5098  CD  LYS B 238     3389   4024   3528    119     74   -175       C  
ATOM   5099  CE  LYS B 238     -12.262  -7.125 -42.168  1.00 40.93           C  
ANISOU 5099  CE  LYS B 238     4888   5612   5050     98     97   -181       C  
ATOM   5100  NZ  LYS B 238     -12.714  -7.167 -43.586  1.00 38.43           N  
ANISOU 5100  NZ  LYS B 238     4584   5310   4707     79    115   -179       N  
ATOM   5101  N   ARG B 239     -14.810  -6.352 -36.659  1.00 19.19           N  
ANISOU 5101  N   ARG B 239     2223   2698   2369    113     13   -123       N  
ATOM   5102  CA  ARG B 239     -15.279  -4.987 -36.470  1.00 19.88           C  
ANISOU 5102  CA  ARG B 239     2311   2779   2463     78     13   -100       C  
ATOM   5103  C   ARG B 239     -14.734  -4.367 -35.187  1.00 23.56           C  
ANISOU 5103  C   ARG B 239     2770   3241   2942     78      0    -98       C  
ATOM   5104  O   ARG B 239     -14.487  -3.158 -35.150  1.00 18.93           O  
ANISOU 5104  O   ARG B 239     2169   2663   2360     50      1    -87       O  
ATOM   5105  CB  ARG B 239     -16.808  -4.960 -36.465  1.00 21.80           C  
ANISOU 5105  CB  ARG B 239     2588   2987   2709     68     12    -84       C  
ATOM   5106  CG  ARG B 239     -17.385  -3.555 -36.338  1.00 24.27           C  
ANISOU 5106  CG  ARG B 239     2902   3289   3030     37     12    -63       C  
ATOM   5107  CD  ARG B 239     -17.014  -2.708 -37.555  1.00 23.67           C  
ANISOU 5107  CD  ARG B 239     2807   3240   2945     10     22    -54       C  
ATOM   5108  NE  ARG B 239     -18.199  -2.327 -38.312  1.00 32.06           N  
ANISOU 5108  NE  ARG B 239     3888   4289   4006     -7     23    -37       N  
ATOM   5109  CZ  ARG B 239     -18.500  -2.754 -39.533  1.00 28.15           C  
ANISOU 5109  CZ  ARG B 239     3397   3806   3494    -10     30    -37       C  
ATOM   5110  NH1 ARG B 239     -17.703  -3.571 -40.201  1.00 26.05           N  
ANISOU 5110  NH1 ARG B 239     3118   3566   3212      2     40    -55       N  
ATOM   5111  NH2 ARG B 239     -19.624  -2.333 -40.106  1.00 25.97           N  
ANISOU 5111  NH2 ARG B 239     3136   3515   3218    -24     26    -21       N  
ATOM   5112  N   LEU B 240     -14.533  -5.167 -34.134  1.00 19.03           N  
ANISOU 5112  N   LEU B 240     2208   2652   2371    108    -15   -109       N  
ATOM   5113  CA  LEU B 240     -14.077  -4.651 -32.850  1.00 19.26           C  
ANISOU 5113  CA  LEU B 240     2235   2675   2408    109    -31   -108       C  
ATOM   5114  C   LEU B 240     -12.602  -4.901 -32.586  1.00 20.03           C  
ANISOU 5114  C   LEU B 240     2299   2804   2507    128    -42   -127       C  
ATOM   5115  O   LEU B 240     -12.123  -4.563 -31.502  1.00 17.20           O  
ANISOU 5115  O   LEU B 240     1938   2443   2154    132    -59   -129       O  
ATOM   5116  CB  LEU B 240     -14.881  -5.261 -31.702  1.00 18.95           C  
ANISOU 5116  CB  LEU B 240     2236   2597   2369    125    -43   -104       C  
ATOM   5117  CG  LEU B 240     -16.305  -4.791 -31.454  1.00 25.02           C  
ANISOU 5117  CG  LEU B 240     3033   3333   3140    105    -36    -87       C  
ATOM   5118  CD1 LEU B 240     -16.831  -5.503 -30.223  1.00 20.00           C  
ANISOU 5118  CD1 LEU B 240     2432   2666   2500    122    -45    -87       C  
ATOM   5119  CD2 LEU B 240     -16.349  -3.288 -31.278  1.00 19.81           C  
ANISOU 5119  CD2 LEU B 240     2361   2676   2488     75    -34    -76       C  
ATOM   5120  N   LYS B 241     -11.880  -5.488 -33.535  1.00 18.47           N  
ANISOU 5120  N   LYS B 241     2076   2637   2305    142    -32   -143       N  
ATOM   5121  CA  LYS B 241     -10.494  -5.838 -33.283  1.00 18.20           C  
ANISOU 5121  CA  LYS B 241     2006   2635   2275    167    -43   -164       C  
ATOM   5122  C   LYS B 241      -9.681  -4.594 -32.958  1.00 20.19           C  
ANISOU 5122  C   LYS B 241     2223   2913   2535    138    -46   -162       C  
ATOM   5123  O   LYS B 241      -9.808  -3.557 -33.617  1.00 19.21           O  
ANISOU 5123  O   LYS B 241     2087   2801   2411     98    -29   -150       O  
ATOM   5124  CB  LYS B 241      -9.892  -6.553 -34.489  1.00 23.42           C  
ANISOU 5124  CB  LYS B 241     2640   3328   2929    183    -26   -184       C  
ATOM   5125  CG  LYS B 241      -8.564  -7.193 -34.151  1.00 27.25           C  
ANISOU 5125  CG  LYS B 241     3091   3842   3422    221    -40   -211       C  
ATOM   5126  CD  LYS B 241      -7.981  -7.952 -35.312  1.00 34.59           C  
ANISOU 5126  CD  LYS B 241     3994   4803   4345    241    -22   -235       C  
ATOM   5127  CE  LYS B 241      -6.744  -8.686 -34.832  1.00 36.39           C  
ANISOU 5127  CE  LYS B 241     4189   5054   4584    287    -41   -264       C  
ATOM   5128  NZ  LYS B 241      -6.246  -9.700 -35.808  1.00 38.65           N  
ANISOU 5128  NZ  LYS B 241     4457   5362   4865    321    -27   -292       N  
ATOM   5129  N   VAL B 242      -8.878  -4.698 -31.912  1.00 18.94           N  
ANISOU 5129  N   VAL B 242     2052   2761   2384    157    -70   -174       N  
ATOM   5130  CA  VAL B 242      -7.964  -3.640 -31.507  1.00 22.54           C  
ANISOU 5130  CA  VAL B 242     2472   3244   2849    132    -78   -177       C  
ATOM   5131  C   VAL B 242      -6.638  -3.862 -32.210  1.00 21.70           C  
ANISOU 5131  C   VAL B 242     2307   3191   2747    141    -71   -200       C  
ATOM   5132  O   VAL B 242      -6.055  -4.942 -32.115  1.00 18.82           O  
ANISOU 5132  O   VAL B 242     1929   2837   2383    186    -82   -221       O  
ATOM   5133  CB  VAL B 242      -7.768  -3.634 -29.984  1.00 24.26           C  
ANISOU 5133  CB  VAL B 242     2704   3443   3070    148   -111   -178       C  
ATOM   5134  CG1 VAL B 242      -6.686  -2.615 -29.602  1.00 24.30           C  
ANISOU 5134  CG1 VAL B 242     2666   3480   3085    123   -122   -186       C  
ATOM   5135  CG2 VAL B 242      -9.100  -3.372 -29.261  1.00 21.89           C  
ANISOU 5135  CG2 VAL B 242     2460   3093   2764    137   -114   -157       C  
ATOM   5136  N   SER B 243      -6.157  -2.844 -32.916  1.00 22.52           N  
ANISOU 5136  N   SER B 243     2377   3327   2853     98    -51   -197       N  
ATOM   5137  CA  SER B 243      -4.834  -2.882 -33.513  1.00 25.37           C  
ANISOU 5137  CA  SER B 243     2676   3744   3219     98    -41   -221       C  
ATOM   5138  C   SER B 243      -4.049  -1.687 -33.008  1.00 26.91           C  
ANISOU 5138  C   SER B 243     2838   3962   3426     60    -49   -220       C  
ATOM   5139  O   SER B 243      -4.548  -0.556 -33.041  1.00 20.83           O  
ANISOU 5139  O   SER B 243     2086   3174   2654     13    -42   -198       O  
ATOM   5140  CB  SER B 243      -4.889  -2.860 -35.039  1.00 24.78           C  
ANISOU 5140  CB  SER B 243     2588   3696   3133     78     -3   -220       C  
ATOM   5141  OG  SER B 243      -3.671  -2.349 -35.557  1.00 24.50           O  
ANISOU 5141  OG  SER B 243     2491   3715   3101     54     13   -236       O  
ATOM   5142  N   GLY B 244      -2.821  -1.938 -32.553  1.00 23.07           N  
ANISOU 5142  N   GLY B 244     2302   3512   2951     79    -66   -246       N  
ATOM   5143  CA  GLY B 244      -1.983  -0.845 -32.109  1.00 23.23           C  
ANISOU 5143  CA  GLY B 244     2285   3559   2983     40    -75   -249       C  
ATOM   5144  C   GLY B 244      -1.677   0.164 -33.194  1.00 21.31           C  
ANISOU 5144  C   GLY B 244     2013   3347   2738    -19    -40   -241       C  
ATOM   5145  O   GLY B 244      -1.234   1.273 -32.877  1.00 25.16           O  
ANISOU 5145  O   GLY B 244     2482   3843   3233    -64    -44   -236       O  
ATOM   5146  N   ASN B 245      -1.926  -0.183 -34.460  1.00 21.43           N  
ANISOU 5146  N   ASN B 245     2027   3375   2739    -21     -5   -239       N  
ATOM   5147  CA  ASN B 245      -1.663   0.693 -35.593  1.00 21.54           C  
ANISOU 5147  CA  ASN B 245     2020   3420   2746    -77     31   -230       C  
ATOM   5148  C   ASN B 245      -2.891   1.450 -36.095  1.00 26.61           C  
ANISOU 5148  C   ASN B 245     2719   4019   3374   -115     45   -194       C  
ATOM   5149  O   ASN B 245      -2.746   2.287 -36.991  1.00 27.05           O  
ANISOU 5149  O   ASN B 245     2766   4092   3420   -165     72   -180       O  
ATOM   5150  CB  ASN B 245      -1.069  -0.115 -36.741  1.00 19.15           C  
ANISOU 5150  CB  ASN B 245     1679   3165   2434    -59     62   -252       C  
ATOM   5151  CG  ASN B 245       0.099  -0.957 -36.295  1.00 23.17           C  
ANISOU 5151  CG  ASN B 245     2130   3716   2958    -14     47   -291       C  
ATOM   5152  OD1 ASN B 245       1.006  -0.466 -35.623  1.00 22.85           O  
ANISOU 5152  OD1 ASN B 245     2047   3701   2934    -27     30   -303       O  
ATOM   5153  ND2 ASN B 245       0.064  -2.237 -36.624  1.00 23.61           N  
ANISOU 5153  ND2 ASN B 245     2187   3776   3009     42     50   -311       N  
ATOM   5154  N   GLN B 246      -4.084   1.178 -35.574  1.00 22.88           N  
ANISOU 5154  N   GLN B 246     2303   3491   2899    -91     28   -178       N  
ATOM   5155  CA  GLN B 246      -5.224   2.018 -35.925  1.00 20.79           C  
ANISOU 5155  CA  GLN B 246     2087   3186   2626   -126     36   -145       C  
ATOM   5156  C   GLN B 246      -5.069   3.396 -35.315  1.00 24.06           C  
ANISOU 5156  C   GLN B 246     2505   3587   3051   -172     25   -131       C  
ATOM   5157  O   GLN B 246      -4.460   3.561 -34.256  1.00 22.39           O  
ANISOU 5157  O   GLN B 246     2275   3379   2854   -167      1   -144       O  
ATOM   5158  CB  GLN B 246      -6.545   1.463 -35.403  1.00 26.55           C  
ANISOU 5158  CB  GLN B 246     2872   3863   3354    -92     20   -133       C  
ATOM   5159  CG  GLN B 246      -6.718  -0.014 -35.394  1.00 34.05           C  
ANISOU 5159  CG  GLN B 246     3827   4812   4299    -37     16   -151       C  
ATOM   5160  CD  GLN B 246      -8.053  -0.376 -34.775  1.00 31.34           C  
ANISOU 5160  CD  GLN B 246     3539   4413   3954    -16      1   -136       C  
ATOM   5161  OE1 GLN B 246      -8.132  -0.820 -33.618  1.00 21.06           O  
ANISOU 5161  OE1 GLN B 246     2251   3091   2660     13    -23   -143       O  
ATOM   5162  NE2 GLN B 246      -9.119  -0.146 -35.535  1.00 31.39           N  
ANISOU 5162  NE2 GLN B 246     3577   4397   3951    -32     15   -116       N  
ATOM   5163  N   HIS B 247      -5.668   4.385 -35.975  1.00 22.07           N  
ANISOU 5163  N   HIS B 247     2280   3315   2792   -216     40   -104       N  
ATOM   5164  CA  HIS B 247      -5.832   5.684 -35.351  1.00 21.64           C  
ANISOU 5164  CA  HIS B 247     2244   3230   2747   -255     26    -87       C  
ATOM   5165  C   HIS B 247      -6.373   5.512 -33.938  1.00 19.49           C  
ANISOU 5165  C   HIS B 247     2000   2919   2487   -223     -6    -92       C  
ATOM   5166  O   HIS B 247      -7.276   4.702 -33.686  1.00 20.20           O  
ANISOU 5166  O   HIS B 247     2120   2982   2573   -183    -12    -91       O  
ATOM   5167  CB  HIS B 247      -6.764   6.558 -36.189  1.00 22.68           C  
ANISOU 5167  CB  HIS B 247     2417   3331   2870   -290     40    -55       C  
ATOM   5168  CG  HIS B 247      -6.765   7.992 -35.771  1.00 20.62           C  
ANISOU 5168  CG  HIS B 247     2173   3042   2618   -337     30    -39       C  
ATOM   5169  ND1 HIS B 247      -7.397   8.435 -34.628  1.00 22.36           N  
ANISOU 5169  ND1 HIS B 247     2426   3216   2853   -327      4    -36       N  
ATOM   5170  CD2 HIS B 247      -6.197   9.083 -36.336  1.00 25.58           C  
ANISOU 5170  CD2 HIS B 247     2792   3681   3245   -395     43    -25       C  
ATOM   5171  CE1 HIS B 247      -7.223   9.738 -34.510  1.00 24.66           C  
ANISOU 5171  CE1 HIS B 247     2728   3489   3152   -374      0    -23       C  
ATOM   5172  NE2 HIS B 247      -6.497  10.156 -35.533  1.00 26.23           N  
ANISOU 5172  NE2 HIS B 247     2903   3721   3342   -417     23    -15       N  
ATOM   5173  N   GLU B 248      -5.786   6.264 -33.011  1.00 21.02           N  
ANISOU 5173  N   GLU B 248     2182   3110   2694   -244    -25    -99       N  
ATOM   5174  CA  GLU B 248      -6.089   6.093 -31.597  1.00 21.47           C  
ANISOU 5174  CA  GLU B 248     2262   3138   2759   -215    -55   -108       C  
ATOM   5175  C   GLU B 248      -7.574   6.258 -31.306  1.00 21.96           C  
ANISOU 5175  C   GLU B 248     2382   3144   2818   -204    -58    -89       C  
ATOM   5176  O   GLU B 248      -8.095   5.623 -30.383  1.00 18.96           O  
ANISOU 5176  O   GLU B 248     2025   2741   2437   -166    -75    -95       O  
ATOM   5177  CB  GLU B 248      -5.268   7.086 -30.770  1.00 29.20           C  
ANISOU 5177  CB  GLU B 248     3223   4122   3750   -250    -74   -117       C  
ATOM   5178  CG  GLU B 248      -5.569   8.560 -31.094  1.00 34.14           C  
ANISOU 5178  CG  GLU B 248     3872   4721   4380   -306    -66    -95       C  
ATOM   5179  CD  GLU B 248      -5.109   9.527 -30.001  1.00 49.77           C  
ANISOU 5179  CD  GLU B 248     5852   6686   6371   -334    -91   -104       C  
ATOM   5180  OE1 GLU B 248      -4.502   9.065 -29.006  1.00 50.46           O  
ANISOU 5180  OE1 GLU B 248     5921   6790   6463   -310   -115   -127       O  
ATOM   5181  OE2 GLU B 248      -5.364  10.747 -30.138  1.00 56.46           O  
ANISOU 5181  OE2 GLU B 248     6724   7505   7224   -378    -88    -88       O  
ATOM   5182  N   GLU B 249      -8.272   7.103 -32.072  1.00 18.17           N  
ANISOU 5182  N   GLU B 249     1927   2641   2337   -235    -43    -65       N  
ATOM   5183  CA  GLU B 249      -9.707   7.266 -31.875  1.00 20.80           C  
ANISOU 5183  CA  GLU B 249     2311   2923   2670   -222    -46    -49       C  
ATOM   5184  C   GLU B 249     -10.447   5.960 -32.131  1.00 18.26           C  
ANISOU 5184  C   GLU B 249     2000   2599   2338   -177    -40    -51       C  
ATOM   5185  O   GLU B 249     -11.359   5.586 -31.378  1.00 19.53           O  
ANISOU 5185  O   GLU B 249     2191   2728   2500   -150    -49    -51       O  
ATOM   5186  CB  GLU B 249     -10.228   8.371 -32.795  1.00 16.94           C  
ANISOU 5186  CB  GLU B 249     1843   2414   2181   -261    -34    -23       C  
ATOM   5187  CG  GLU B 249     -11.725   8.579 -32.739  1.00 27.87           C  
ANISOU 5187  CG  GLU B 249     3273   3750   3567   -246    -36     -7       C  
ATOM   5188  CD  GLU B 249     -12.191   9.671 -33.693  1.00 30.75           C  
ANISOU 5188  CD  GLU B 249     3659   4093   3932   -282    -29     20       C  
ATOM   5189  OE1 GLU B 249     -11.705  10.827 -33.575  1.00 26.35           O  
ANISOU 5189  OE1 GLU B 249     3104   3526   3382   -321    -34     26       O  
ATOM   5190  OE2 GLU B 249     -13.021   9.356 -34.572  1.00 24.06           O  
ANISOU 5190  OE2 GLU B 249     2826   3238   3076   -271    -20     34       O  
ATOM   5191  N   LEU B 250     -10.058   5.245 -33.181  1.00 17.69           N  
ANISOU 5191  N   LEU B 250     1904   2561   2256   -171    -23    -54       N  
ATOM   5192  CA  LEU B 250     -10.676   3.958 -33.470  1.00 16.18           C  
ANISOU 5192  CA  LEU B 250     1723   2369   2056   -131    -18    -58       C  
ATOM   5193  C   LEU B 250     -10.256   2.911 -32.450  1.00 18.26           C  
ANISOU 5193  C   LEU B 250     1978   2638   2321    -90    -34    -80       C  
ATOM   5194  O   LEU B 250     -11.086   2.125 -31.979  1.00 16.30           O  
ANISOU 5194  O   LEU B 250     1758   2365   2071    -58    -41    -81       O  
ATOM   5195  CB  LEU B 250     -10.297   3.523 -34.880  1.00 15.35           C  
ANISOU 5195  CB  LEU B 250     1596   2300   1938   -137      5    -58       C  
ATOM   5196  CG  LEU B 250     -10.811   4.495 -35.936  1.00 17.85           C  
ANISOU 5196  CG  LEU B 250     1928   2606   2247   -176     20    -32       C  
ATOM   5197  CD1 LEU B 250     -10.168   4.214 -37.278  1.00 22.69           C  
ANISOU 5197  CD1 LEU B 250     2516   3263   2843   -191     44    -34       C  
ATOM   5198  CD2 LEU B 250     -12.307   4.324 -36.003  1.00 20.79           C  
ANISOU 5198  CD2 LEU B 250     2343   2937   2619   -160     15    -18       C  
ATOM   5199  N   GLN B 251      -8.961   2.883 -32.126  1.00 17.75           N  
ANISOU 5199  N   GLN B 251     1874   2608   2261    -91    -42    -98       N  
ATOM   5200  CA  GLN B 251      -8.421   1.973 -31.122  1.00 19.61           C  
ANISOU 5200  CA  GLN B 251     2101   2852   2499    -52    -64   -119       C  
ATOM   5201  C   GLN B 251      -9.141   2.126 -29.799  1.00 17.01           C  
ANISOU 5201  C   GLN B 251     1811   2481   2171    -41    -85   -115       C  
ATOM   5202  O   GLN B 251      -9.559   1.143 -29.176  1.00 18.97           O  
ANISOU 5202  O   GLN B 251     2082   2712   2413     -4    -96   -119       O  
ATOM   5203  CB  GLN B 251      -6.950   2.291 -30.893  1.00 23.36           C  
ANISOU 5203  CB  GLN B 251     2525   3369   2981    -64    -74   -137       C  
ATOM   5204  CG  GLN B 251      -5.949   1.493 -31.604  1.00 27.78           C  
ANISOU 5204  CG  GLN B 251     3038   3978   3541    -46    -64   -156       C  
ATOM   5205  CD  GLN B 251      -4.580   1.717 -30.987  1.00 24.87           C  
ANISOU 5205  CD  GLN B 251     2620   3646   3183    -50    -83   -178       C  
ATOM   5206  OE1 GLN B 251      -4.300   1.222 -29.898  1.00 27.75           O  
ANISOU 5206  OE1 GLN B 251     2987   4005   3551    -18   -113   -191       O  
ATOM   5207  NE2 GLN B 251      -3.748   2.513 -31.651  1.00 25.11           N  
ANISOU 5207  NE2 GLN B 251     2609   3714   3219    -93    -66   -181       N  
ATOM   5208  N   ASN B 252      -9.252   3.366 -29.332  1.00 15.74           N  
ANISOU 5208  N   ASN B 252     1660   2303   2017    -75    -91   -107       N  
ATOM   5209  CA  ASN B 252      -9.674   3.575 -27.962  1.00 18.60           C  
ANISOU 5209  CA  ASN B 252     2055   2634   2380    -66   -111   -109       C  
ATOM   5210  C   ASN B 252     -11.128   3.213 -27.757  1.00 17.86           C  
ANISOU 5210  C   ASN B 252     2007   2499   2280    -48   -104    -97       C  
ATOM   5211  O   ASN B 252     -11.483   2.756 -26.669  1.00 15.47           O  
ANISOU 5211  O   ASN B 252     1730   2176   1970    -25   -118   -102       O  
ATOM   5212  CB  ASN B 252      -9.403   5.011 -27.542  1.00 17.45           C  
ANISOU 5212  CB  ASN B 252     1908   2479   2242   -106   -119   -107       C  
ATOM   5213  CG  ASN B 252      -7.930   5.273 -27.381  1.00 24.71           C  
ANISOU 5213  CG  ASN B 252     2783   3439   3168   -122   -133   -123       C  
ATOM   5214  OD1 ASN B 252      -7.151   4.331 -27.239  1.00 24.74           O  
ANISOU 5214  OD1 ASN B 252     2758   3473   3169    -93   -143   -139       O  
ATOM   5215  ND2 ASN B 252      -7.529   6.539 -27.419  1.00 26.39           N  
ANISOU 5215  ND2 ASN B 252     2987   3652   3389   -167   -134   -120       N  
ATOM   5216  N   VAL B 253     -11.981   3.406 -28.769  1.00 14.48           N  
ANISOU 5216  N   VAL B 253     1590   2059   1853    -59    -83    -81       N  
ATOM   5217  CA  VAL B 253     -13.381   3.030 -28.591  1.00 16.25           C  
ANISOU 5217  CA  VAL B 253     1852   2249   2075    -43    -76    -72       C  
ATOM   5218  C   VAL B 253     -13.501   1.516 -28.472  1.00 16.56           C  
ANISOU 5218  C   VAL B 253     1897   2291   2103     -5    -77    -79       C  
ATOM   5219  O   VAL B 253     -14.272   1.002 -27.652  1.00 13.93           O  
ANISOU 5219  O   VAL B 253     1595   1932   1765     13    -81    -79       O  
ATOM   5220  CB  VAL B 253     -14.265   3.606 -29.718  1.00 21.05           C  
ANISOU 5220  CB  VAL B 253     2468   2844   2687    -63    -58    -53       C  
ATOM   5221  CG1 VAL B 253     -13.953   2.975 -31.052  1.00 20.02           C  
ANISOU 5221  CG1 VAL B 253     2315   2741   2549    -61    -44    -51       C  
ATOM   5222  CG2 VAL B 253     -15.759   3.415 -29.383  1.00 20.84           C  
ANISOU 5222  CG2 VAL B 253     2477   2781   2662    -50    -53    -46       C  
ATOM   5223  N   ARG B 254     -12.688   0.783 -29.234  1.00 14.36           N  
ANISOU 5223  N   ARG B 254     1590   2045   1821      7    -74    -87       N  
ATOM   5224  CA  ARG B 254     -12.696  -0.675 -29.153  1.00 17.29           C  
ANISOU 5224  CA  ARG B 254     1968   2416   2184     45    -78    -97       C  
ATOM   5225  C   ARG B 254     -12.074  -1.169 -27.850  1.00 17.94           C  
ANISOU 5225  C   ARG B 254     2056   2497   2262     70   -103   -109       C  
ATOM   5226  O   ARG B 254     -12.602  -2.091 -27.222  1.00 14.67           O  
ANISOU 5226  O   ARG B 254     1674   2061   1840     96   -109   -110       O  
ATOM   5227  CB  ARG B 254     -11.966  -1.264 -30.364  1.00 15.13           C  
ANISOU 5227  CB  ARG B 254     1662   2179   1909     52    -67   -105       C  
ATOM   5228  CG  ARG B 254     -12.754  -1.113 -31.660  1.00 14.92           C  
ANISOU 5228  CG  ARG B 254     1640   2150   1879     35    -44    -92       C  
ATOM   5229  CD  ARG B 254     -11.862  -1.044 -32.904  1.00 18.97           C  
ANISOU 5229  CD  ARG B 254     2115   2704   2389     23    -29    -98       C  
ATOM   5230  NE  ARG B 254     -12.673  -0.947 -34.114  1.00 22.02           N  
ANISOU 5230  NE  ARG B 254     2513   3087   2768      8    -10    -85       N  
ATOM   5231  CZ  ARG B 254     -13.375   0.124 -34.477  1.00 26.85           C  
ANISOU 5231  CZ  ARG B 254     3138   3683   3382    -24     -4    -64       C  
ATOM   5232  NH1 ARG B 254     -13.308   1.268 -33.800  1.00 16.10           N  
ANISOU 5232  NH1 ARG B 254     1778   2308   2030    -47    -12    -56       N  
ATOM   5233  NH2 ARG B 254     -14.180   0.042 -35.536  1.00 23.85           N  
ANISOU 5233  NH2 ARG B 254     2771   3297   2993    -32      8    -53       N  
ATOM   5234  N   LYS B 255     -10.937  -0.592 -27.443  1.00 15.76           N  
ANISOU 5234  N   LYS B 255     1751   2246   1991     61   -118   -120       N  
ATOM   5235  CA  LYS B 255     -10.360  -0.941 -26.149  1.00 15.71           C  
ANISOU 5235  CA  LYS B 255     1752   2238   1979     83   -147   -131       C  
ATOM   5236  C   LYS B 255     -11.364  -0.716 -25.032  1.00 17.29           C  
ANISOU 5236  C   LYS B 255     2001   2398   2171     81   -152   -122       C  
ATOM   5237  O   LYS B 255     -11.513  -1.560 -24.140  1.00 17.54           O  
ANISOU 5237  O   LYS B 255     2061   2413   2189    108   -167   -125       O  
ATOM   5238  CB  LYS B 255      -9.100  -0.124 -25.883  1.00 18.16           C  
ANISOU 5238  CB  LYS B 255     2022   2580   2297     65   -163   -143       C  
ATOM   5239  CG  LYS B 255      -7.919  -0.476 -26.751  1.00 17.95           C  
ANISOU 5239  CG  LYS B 255     1942   2599   2278     72   -161   -158       C  
ATOM   5240  CD  LYS B 255      -6.707   0.376 -26.319  1.00 25.48           C  
ANISOU 5240  CD  LYS B 255     2855   3584   3241     51   -180   -171       C  
ATOM   5241  CE  LYS B 255      -5.427  -0.082 -26.998  1.00 30.75           C  
ANISOU 5241  CE  LYS B 255     3463   4303   3917     63   -180   -190       C  
ATOM   5242  NZ  LYS B 255      -4.238   0.630 -26.448  1.00 31.69           N  
ANISOU 5242  NZ  LYS B 255     3539   4454   4046     44   -202   -206       N  
ATOM   5243  N   HIS B 256     -12.062   0.423 -25.066  1.00 15.62           N  
ANISOU 5243  N   HIS B 256     1801   2170   1965     48   -139   -112       N  
ATOM   5244  CA  HIS B 256     -13.063   0.717 -24.049  1.00 16.77           C  
ANISOU 5244  CA  HIS B 256     1990   2279   2103     46   -139   -107       C  
ATOM   5245  C   HIS B 256     -14.112  -0.382 -23.969  1.00 14.95           C  
ANISOU 5245  C   HIS B 256     1793   2025   1863     68   -128   -100       C  
ATOM   5246  O   HIS B 256     -14.440  -0.867 -22.882  1.00 15.44           O  
ANISOU 5246  O   HIS B 256     1889   2068   1910     83   -137   -101       O  
ATOM   5247  CB  HIS B 256     -13.744   2.057 -24.336  1.00 15.24           C  
ANISOU 5247  CB  HIS B 256     1801   2070   1921     12   -124    -98       C  
ATOM   5248  CG  HIS B 256     -14.849   2.368 -23.376  1.00 14.82           C  
ANISOU 5248  CG  HIS B 256     1788   1981   1862     11   -119    -96       C  
ATOM   5249  ND1 HIS B 256     -14.659   3.142 -22.250  1.00 19.41           N  
ANISOU 5249  ND1 HIS B 256     2384   2552   2438      1   -133   -105       N  
ATOM   5250  CD2 HIS B 256     -16.142   1.967 -23.341  1.00 17.73           C  
ANISOU 5250  CD2 HIS B 256     2185   2325   2228     19   -101    -88       C  
ATOM   5251  CE1 HIS B 256     -15.791   3.224 -21.574  1.00 18.35           C  
ANISOU 5251  CE1 HIS B 256     2286   2389   2298      4   -121   -103       C  
ATOM   5252  NE2 HIS B 256     -16.707   2.521 -22.215  1.00 17.75           N  
ANISOU 5252  NE2 HIS B 256     2216   2304   2224     14   -102    -93       N  
ATOM   5253  N   ILE B 257     -14.666  -0.767 -25.118  1.00 13.68           N  
ANISOU 5253  N   ILE B 257     1625   1865   1708     68   -108    -92       N  
ATOM   5254  CA  ILE B 257     -15.742  -1.751 -25.148  1.00 14.11           C  
ANISOU 5254  CA  ILE B 257     1709   1896   1755     83    -96    -86       C  
ATOM   5255  C   ILE B 257     -15.245  -3.104 -24.637  1.00 16.08           C  
ANISOU 5255  C   ILE B 257     1973   2145   1991    116   -112    -93       C  
ATOM   5256  O   ILE B 257     -15.895  -3.752 -23.806  1.00 16.18           O  
ANISOU 5256  O   ILE B 257     2024   2132   1991    127   -112    -89       O  
ATOM   5257  CB  ILE B 257     -16.324  -1.830 -26.571  1.00 15.21           C  
ANISOU 5257  CB  ILE B 257     1835   2039   1904     74    -75    -78       C  
ATOM   5258  CG1 ILE B 257     -17.088  -0.529 -26.872  1.00 16.05           C  
ANISOU 5258  CG1 ILE B 257     1941   2135   2023     45    -63    -68       C  
ATOM   5259  CG2 ILE B 257     -17.227  -3.059 -26.741  1.00 15.07           C  
ANISOU 5259  CG2 ILE B 257     1843   2004   1880     91    -66    -75       C  
ATOM   5260  CD1 ILE B 257     -17.329  -0.263 -28.368  1.00 15.26           C  
ANISOU 5260  CD1 ILE B 257     1821   2047   1931     31    -49    -60       C  
ATOM   5261  N   HIS B 258     -14.064  -3.533 -25.091  1.00 16.77           N  
ANISOU 5261  N   HIS B 258     2030   2260   2081    133   -125   -103       N  
ATOM   5262  CA  HIS B 258     -13.504  -4.784 -24.589  1.00 18.92           C  
ANISOU 5262  CA  HIS B 258     2316   2531   2342    169   -145   -110       C  
ATOM   5263  C   HIS B 258     -13.269  -4.719 -23.089  1.00 19.07           C  
ANISOU 5263  C   HIS B 258     2362   2538   2347    177   -169   -112       C  
ATOM   5264  O   HIS B 258     -13.465  -5.711 -22.380  1.00 18.68           O  
ANISOU 5264  O   HIS B 258     2349   2467   2282    201   -181   -109       O  
ATOM   5265  CB  HIS B 258     -12.196  -5.112 -25.298  1.00 18.84           C  
ANISOU 5265  CB  HIS B 258     2261   2558   2340    188   -156   -125       C  
ATOM   5266  CG  HIS B 258     -12.374  -5.502 -26.725  1.00 18.94           C  
ANISOU 5266  CG  HIS B 258     2255   2583   2360    188   -134   -126       C  
ATOM   5267  ND1 HIS B 258     -13.035  -6.651 -27.102  1.00 24.88           N  
ANISOU 5267  ND1 HIS B 258     3035   3314   3106    207   -126   -124       N  
ATOM   5268  CD2 HIS B 258     -11.994  -4.890 -27.871  1.00 16.53           C  
ANISOU 5268  CD2 HIS B 258     1910   2307   2064    169   -118   -129       C  
ATOM   5269  CE1 HIS B 258     -13.051  -6.731 -28.421  1.00 26.42           C  
ANISOU 5269  CE1 HIS B 258     3206   3526   3306    201   -107   -128       C  
ATOM   5270  NE2 HIS B 258     -12.428  -5.674 -28.911  1.00 22.62           N  
ANISOU 5270  NE2 HIS B 258     2684   3076   2833    178   -101   -130       N  
ATOM   5271  N   SER B 259     -12.859  -3.554 -22.583  1.00 14.65           N  
ANISOU 5271  N   SER B 259     1787   1989   1790    156   -177   -115       N  
ATOM   5272  CA  SER B 259     -12.582  -3.438 -21.160  1.00 15.22           C  
ANISOU 5272  CA  SER B 259     1886   2052   1846    162   -202   -118       C  
ATOM   5273  C   SER B 259     -13.850  -3.497 -20.318  1.00 18.17           C  
ANISOU 5273  C   SER B 259     2312   2388   2203    154   -189   -108       C  
ATOM   5274  O   SER B 259     -13.770  -3.784 -19.123  1.00 18.05           O  
ANISOU 5274  O   SER B 259     2331   2360   2166    165   -207   -108       O  
ATOM   5275  CB  SER B 259     -11.817  -2.142 -20.876  1.00 17.28           C  
ANISOU 5275  CB  SER B 259     2118   2334   2115    139   -215   -128       C  
ATOM   5276  OG  SER B 259     -12.715  -1.031 -20.827  1.00 18.31           O  
ANISOU 5276  OG  SER B 259     2260   2446   2250    106   -193   -121       O  
ATOM   5277  N   CYS B 260     -15.019  -3.261 -20.909  1.00 19.33           N  
ANISOU 5277  N   CYS B 260     2466   2520   2359    136   -157    -99       N  
ATOM   5278  CA  CYS B 260     -16.239  -3.148 -20.119  1.00 18.87           C  
ANISOU 5278  CA  CYS B 260     2449   2432   2287    124   -140    -92       C  
ATOM   5279  C   CYS B 260     -16.938  -4.471 -19.856  1.00 19.26           C  
ANISOU 5279  C   CYS B 260     2538   2458   2321    139   -133    -83       C  
ATOM   5280  O   CYS B 260     -17.685  -4.578 -18.876  1.00 17.81           O  
ANISOU 5280  O   CYS B 260     2395   2253   2119    133   -125    -79       O  
ATOM   5281  CB  CYS B 260     -17.224  -2.215 -20.816  1.00 18.29           C  
ANISOU 5281  CB  CYS B 260     2364   2353   2233     97   -111    -87       C  
ATOM   5282  SG  CYS B 260     -16.755  -0.528 -20.659  1.00 22.92           S  
ANISOU 5282  SG  CYS B 260     2928   2950   2832     73   -117    -95       S  
ATOM   5283  N   PHE B 261     -16.745  -5.465 -20.715  1.00 15.52           N  
ANISOU 5283  N   PHE B 261     2056   1988   1854    157   -134    -82       N  
ATOM   5284  CA  PHE B 261     -17.563  -6.670 -20.708  1.00 18.93           C  
ANISOU 5284  CA  PHE B 261     2523   2394   2275    165   -122    -73       C  
ATOM   5285  C   PHE B 261     -16.676  -7.899 -20.670  1.00 19.41           C  
ANISOU 5285  C   PHE B 261     2595   2454   2326    200   -148    -75       C  
ATOM   5286  O   PHE B 261     -15.693  -7.980 -21.413  1.00 18.78           O  
ANISOU 5286  O   PHE B 261     2478   2398   2259    217   -162    -85       O  
ATOM   5287  CB  PHE B 261     -18.463  -6.719 -21.946  1.00 17.38           C  
ANISOU 5287  CB  PHE B 261     2311   2197   2097    151    -95    -69       C  
ATOM   5288  CG  PHE B 261     -19.490  -5.644 -21.968  1.00 19.03           C  
ANISOU 5288  CG  PHE B 261     2513   2402   2316    122    -70    -66       C  
ATOM   5289  CD1 PHE B 261     -20.694  -5.812 -21.299  1.00 16.77           C  
ANISOU 5289  CD1 PHE B 261     2259   2091   2020    108    -50    -61       C  
ATOM   5290  CD2 PHE B 261     -19.250  -4.457 -22.641  1.00 16.64           C  
ANISOU 5290  CD2 PHE B 261     2172   2118   2031    108    -67    -70       C  
ATOM   5291  CE1 PHE B 261     -21.647  -4.800 -21.310  1.00 15.58           C  
ANISOU 5291  CE1 PHE B 261     2099   1938   1881     86    -28    -61       C  
ATOM   5292  CE2 PHE B 261     -20.193  -3.446 -22.649  1.00 18.37           C  
ANISOU 5292  CE2 PHE B 261     2388   2330   2262     85    -48    -67       C  
ATOM   5293  CZ  PHE B 261     -21.386  -3.617 -21.976  1.00 14.19           C  
ANISOU 5293  CZ  PHE B 261     1888   1779   1725     77    -29    -64       C  
ATOM   5294  N   THR B 262     -17.026  -8.858 -19.816  1.00 19.21           N  
ANISOU 5294  N   THR B 262     2620   2400   2278    211   -155    -67       N  
ATOM   5295  CA  THR B 262     -16.255 -10.091 -19.796  1.00 21.51           C  
ANISOU 5295  CA  THR B 262     2928   2684   2562    247   -182    -68       C  
ATOM   5296  C   THR B 262     -16.608 -10.998 -20.959  1.00 21.24           C  
ANISOU 5296  C   THR B 262     2889   2641   2540    255   -168    -69       C  
ATOM   5297  O   THR B 262     -15.779 -11.812 -21.360  1.00 22.23           O  
ANISOU 5297  O   THR B 262     3008   2770   2670    288   -188    -77       O  
ATOM   5298  CB  THR B 262     -16.447 -10.831 -18.469  1.00 23.38           C  
ANISOU 5298  CB  THR B 262     3227   2889   2766    256   -197    -57       C  
ATOM   5299  OG1 THR B 262     -17.805 -11.274 -18.365  1.00 27.35           O  
ANISOU 5299  OG1 THR B 262     3769   3363   3261    232   -166    -44       O  
ATOM   5300  CG2 THR B 262     -16.140  -9.890 -17.296  1.00 23.79           C  
ANISOU 5300  CG2 THR B 262     3286   2950   2802    246   -210    -58       C  
ATOM   5301  N   ASN B 263     -17.802 -10.866 -21.527  1.00 20.14           N  
ANISOU 5301  N   ASN B 263     2752   2492   2410    227   -135    -63       N  
ATOM   5302  CA  ASN B 263     -18.134 -11.610 -22.730  1.00 21.74           C  
ANISOU 5302  CA  ASN B 263     2946   2690   2625    231   -123    -67       C  
ATOM   5303  C   ASN B 263     -18.853 -10.704 -23.708  1.00 19.96           C  
ANISOU 5303  C   ASN B 263     2684   2482   2418    201    -95    -68       C  
ATOM   5304  O   ASN B 263     -19.805 -10.013 -23.338  1.00 19.07           O  
ANISOU 5304  O   ASN B 263     2577   2363   2306    173    -75    -60       O  
ATOM   5305  CB  ASN B 263     -18.993 -12.841 -22.425  1.00 23.72           C  
ANISOU 5305  CB  ASN B 263     3251   2901   2862    229   -116    -57       C  
ATOM   5306  CG  ASN B 263     -18.546 -14.049 -23.217  1.00 35.78           C  
ANISOU 5306  CG  ASN B 263     4784   4418   4394    258   -128    -64       C  
ATOM   5307  OD1 ASN B 263     -18.924 -14.219 -24.380  1.00 36.47           O  
ANISOU 5307  OD1 ASN B 263     4851   4511   4495    250   -112    -71       O  
ATOM   5308  ND2 ASN B 263     -17.700 -14.880 -22.604  1.00 36.90           N  
ANISOU 5308  ND2 ASN B 263     4953   4544   4522    293   -158    -65       N  
ATOM   5309  N   ILE B 264     -18.394 -10.715 -24.953  1.00 18.18           N  
ANISOU 5309  N   ILE B 264     2422   2279   2208    209    -94    -77       N  
ATOM   5310  CA  ILE B 264     -19.007  -9.946 -26.024  1.00 18.82           C  
ANISOU 5310  CA  ILE B 264     2471   2376   2305    184    -71    -77       C  
ATOM   5311  C   ILE B 264     -19.266 -10.891 -27.187  1.00 20.45           C  
ANISOU 5311  C   ILE B 264     2677   2578   2515    190    -64    -83       C  
ATOM   5312  O   ILE B 264     -18.354 -11.588 -27.645  1.00 18.84           O  
ANISOU 5312  O   ILE B 264     2465   2383   2310    218    -77    -94       O  
ATOM   5313  CB  ILE B 264     -18.126  -8.773 -26.486  1.00 18.53           C  
ANISOU 5313  CB  ILE B 264     2387   2375   2278    179    -75    -83       C  
ATOM   5314  CG1 ILE B 264     -17.807  -7.814 -25.324  1.00 15.49           C  
ANISOU 5314  CG1 ILE B 264     2003   1993   1890    172    -85    -80       C  
ATOM   5315  CG2 ILE B 264     -18.806  -8.059 -27.663  1.00 14.42           C  
ANISOU 5315  CG2 ILE B 264     1840   1867   1771    154    -54    -79       C  
ATOM   5316  CD1 ILE B 264     -16.809  -6.724 -25.700  1.00 20.59           C  
ANISOU 5316  CD1 ILE B 264     2605   2673   2547    166    -92    -86       C  
ATOM   5317  N   SER B 265     -20.508 -10.922 -27.649  1.00 16.72           N  
ANISOU 5317  N   SER B 265     2212   2092   2047    166    -44    -77       N  
ATOM   5318  CA  SER B 265     -20.933 -11.824 -28.698  1.00 15.44           C  
ANISOU 5318  CA  SER B 265     2056   1924   1888    167    -38    -82       C  
ATOM   5319  C   SER B 265     -21.701 -11.019 -29.721  1.00 15.00           C  
ANISOU 5319  C   SER B 265     1972   1884   1843    141    -21    -80       C  
ATOM   5320  O   SER B 265     -21.975  -9.840 -29.526  1.00 13.53           O  
ANISOU 5320  O   SER B 265     1767   1709   1665    123    -15    -72       O  
ATOM   5321  CB  SER B 265     -21.809 -12.944 -28.136  1.00 19.14           C  
ANISOU 5321  CB  SER B 265     2572   2353   2347    163    -34    -77       C  
ATOM   5322  OG  SER B 265     -21.081 -13.672 -27.176  1.00 26.93           O  
ANISOU 5322  OG  SER B 265     3590   3322   3321    189    -53    -77       O  
ATOM   5323  N   CYS B 266     -22.076 -11.667 -30.810  1.00 14.23           N  
ANISOU 5323  N   CYS B 266     1874   1786   1747    139    -16    -86       N  
ATOM   5324  CA  CYS B 266     -22.799 -10.956 -31.849  1.00 14.61           C  
ANISOU 5324  CA  CYS B 266     1897   1849   1804    115     -5    -83       C  
ATOM   5325  C   CYS B 266     -23.647 -11.960 -32.607  1.00 14.02           C  
ANISOU 5325  C   CYS B 266     1840   1759   1728    108      0    -89       C  
ATOM   5326  O   CYS B 266     -23.161 -13.041 -32.954  1.00 12.79           O  
ANISOU 5326  O   CYS B 266     1700   1596   1565    127     -7   -101       O  
ATOM   5327  CB  CYS B 266     -21.821 -10.236 -32.788  1.00 12.92           C  
ANISOU 5327  CB  CYS B 266     1647   1671   1590    121     -7    -88       C  
ATOM   5328  SG  CYS B 266     -22.546  -9.510 -34.271  1.00 14.32           S  
ANISOU 5328  SG  CYS B 266     1801   1868   1772     96      2    -83       S  
ATOM   5329  N   PHE B 267     -24.908 -11.600 -32.847  1.00 13.55           N  
ANISOU 5329  N   PHE B 267     1777   1695   1677     81      9    -82       N  
ATOM   5330  CA  PHE B 267     -25.838 -12.420 -33.602  1.00 16.04           C  
ANISOU 5330  CA  PHE B 267     2104   1999   1993     68     13    -87       C  
ATOM   5331  C   PHE B 267     -26.399 -11.589 -34.749  1.00 14.67           C  
ANISOU 5331  C   PHE B 267     1900   1847   1826     51     14    -84       C  
ATOM   5332  O   PHE B 267     -26.868 -10.464 -34.534  1.00 13.49           O  
ANISOU 5332  O   PHE B 267     1732   1707   1688     38     18    -74       O  
ATOM   5333  CB  PHE B 267     -26.960 -12.932 -32.689  1.00 13.88           C  
ANISOU 5333  CB  PHE B 267     1855   1694   1723     49     21    -82       C  
ATOM   5334  CG  PHE B 267     -27.765 -14.053 -33.271  1.00 15.29           C  
ANISOU 5334  CG  PHE B 267     2054   1855   1902     36     23    -90       C  
ATOM   5335  CD1 PHE B 267     -28.749 -13.803 -34.219  1.00 14.50           C  
ANISOU 5335  CD1 PHE B 267     1934   1766   1811     14     25    -92       C  
ATOM   5336  CD2 PHE B 267     -27.563 -15.356 -32.839  1.00 15.12           C  
ANISOU 5336  CD2 PHE B 267     2072   1803   1870     44     19    -95       C  
ATOM   5337  CE1 PHE B 267     -29.502 -14.839 -34.741  1.00 15.57           C  
ANISOU 5337  CE1 PHE B 267     2085   1884   1945     -2     24   -101       C  
ATOM   5338  CE2 PHE B 267     -28.315 -16.397 -33.361  1.00 16.44           C  
ANISOU 5338  CE2 PHE B 267     2259   1949   2037     29     20   -103       C  
ATOM   5339  CZ  PHE B 267     -29.285 -16.135 -34.306  1.00 14.66           C  
ANISOU 5339  CZ  PHE B 267     2012   1738   1821      4     23   -107       C  
ATOM   5340  N   LEU B 268     -26.346 -12.142 -35.962  1.00 12.75           N  
ANISOU 5340  N   LEU B 268     1656   1613   1576     52     10    -95       N  
ATOM   5341  CA  LEU B 268     -26.835 -11.469 -37.160  1.00 14.79           C  
ANISOU 5341  CA  LEU B 268     1892   1893   1836     37      8    -92       C  
ATOM   5342  C   LEU B 268     -28.198 -12.038 -37.515  1.00 15.25           C  
ANISOU 5342  C   LEU B 268     1958   1936   1900     15      8    -95       C  
ATOM   5343  O   LEU B 268     -28.314 -13.228 -37.823  1.00 16.54           O  
ANISOU 5343  O   LEU B 268     2144   2085   2056     16      6   -108       O  
ATOM   5344  CB  LEU B 268     -25.868 -11.646 -38.331  1.00 13.33           C  
ANISOU 5344  CB  LEU B 268     1699   1732   1634     49      5   -103       C  
ATOM   5345  CG  LEU B 268     -24.422 -11.260 -38.066  1.00 16.37           C  
ANISOU 5345  CG  LEU B 268     2072   2136   2013     70      7   -105       C  
ATOM   5346  CD1 LEU B 268     -23.584 -11.500 -39.309  1.00 10.49           C  
ANISOU 5346  CD1 LEU B 268     1318   1418   1251     80      8   -118       C  
ATOM   5347  CD2 LEU B 268     -24.349  -9.787 -37.659  1.00 12.29           C  
ANISOU 5347  CD2 LEU B 268     1532   1632   1506     59      8    -87       C  
ATOM   5348  N   LEU B 269     -29.220 -11.188 -37.493  1.00 15.25           N  
ANISOU 5348  N   LEU B 269     1940   1941   1915     -4      8    -85       N  
ATOM   5349  CA  LEU B 269     -30.570 -11.640 -37.733  1.00 15.15           C  
ANISOU 5349  CA  LEU B 269     1928   1917   1912    -26      7    -88       C  
ATOM   5350  C   LEU B 269     -31.066 -11.184 -39.107  1.00 14.76           C  
ANISOU 5350  C   LEU B 269     1859   1888   1860    -36     -6    -88       C  
ATOM   5351  O   LEU B 269     -30.832 -10.038 -39.500  1.00 13.45           O  
ANISOU 5351  O   LEU B 269     1674   1742   1696    -33    -11    -76       O  
ATOM   5352  CB  LEU B 269     -31.483 -11.082 -36.645  1.00 15.36           C  
ANISOU 5352  CB  LEU B 269     1945   1933   1958    -38     17    -80       C  
ATOM   5353  CG  LEU B 269     -32.783 -11.768 -36.260  1.00 15.06           C  
ANISOU 5353  CG  LEU B 269     1912   1879   1933    -62     24    -85       C  
ATOM   5354  CD1 LEU B 269     -32.549 -13.159 -35.725  1.00 11.24           C  
ANISOU 5354  CD1 LEU B 269     1465   1368   1437    -63     30    -93       C  
ATOM   5355  CD2 LEU B 269     -33.447 -10.898 -35.199  1.00 16.94           C  
ANISOU 5355  CD2 LEU B 269     2134   2115   2188    -69     37    -77       C  
ATOM   5356  N   PRO B 270     -31.750 -12.047 -39.858  1.00 14.69           N  
ANISOU 5356  N   PRO B 270     1858   1875   1847    -49    -14    -99       N  
ATOM   5357  CA  PRO B 270     -32.302 -11.617 -41.143  1.00 13.26           C  
ANISOU 5357  CA  PRO B 270     1661   1714   1663    -60    -30    -99       C  
ATOM   5358  C   PRO B 270     -33.386 -10.579 -40.928  1.00 14.87           C  
ANISOU 5358  C   PRO B 270     1836   1923   1890    -71    -35    -86       C  
ATOM   5359  O   PRO B 270     -33.970 -10.471 -39.850  1.00 12.81           O  
ANISOU 5359  O   PRO B 270     1570   1650   1649    -77    -24    -84       O  
ATOM   5360  CB  PRO B 270     -32.900 -12.905 -41.737  1.00 14.69           C  
ANISOU 5360  CB  PRO B 270     1860   1885   1838    -74    -36   -117       C  
ATOM   5361  CG  PRO B 270     -32.346 -14.035 -40.892  1.00 14.07           C  
ANISOU 5361  CG  PRO B 270     1812   1779   1755    -66    -23   -127       C  
ATOM   5362  CD  PRO B 270     -32.103 -13.444 -39.536  1.00 11.16           C  
ANISOU 5362  CD  PRO B 270     1438   1402   1399    -58     -9   -113       C  
ATOM   5363  N   HIS B 271     -33.690  -9.858 -41.995  1.00 13.05           N  
ANISOU 5363  N   HIS B 271     1590   1712   1655    -75    -53    -80       N  
ATOM   5364  CA  HIS B 271     -34.895  -9.048 -42.005  1.00 15.12           C  
ANISOU 5364  CA  HIS B 271     1826   1979   1941    -84    -64    -72       C  
ATOM   5365  C   HIS B 271     -36.112  -9.947 -41.768  1.00 14.25           C  
ANISOU 5365  C   HIS B 271     1710   1857   1847   -104    -64    -86       C  
ATOM   5366  O   HIS B 271     -36.176 -11.059 -42.301  1.00 15.81           O  
ANISOU 5366  O   HIS B 271     1925   2050   2031   -115    -68   -100       O  
ATOM   5367  CB  HIS B 271     -35.021  -8.319 -43.340  1.00 16.67           C  
ANISOU 5367  CB  HIS B 271     2012   2195   2125    -85    -89    -63       C  
ATOM   5368  CG  HIS B 271     -35.971  -7.161 -43.322  1.00 16.32           C  
ANISOU 5368  CG  HIS B 271     1941   2155   2105    -84   -104    -50       C  
ATOM   5369  ND1 HIS B 271     -37.338  -7.322 -43.259  1.00 14.24           N  
ANISOU 5369  ND1 HIS B 271     1656   1890   1866    -96   -114    -57       N  
ATOM   5370  CD2 HIS B 271     -35.751  -5.826 -43.408  1.00 15.61           C  
ANISOU 5370  CD2 HIS B 271     1842   2070   2020    -74   -112    -31       C  
ATOM   5371  CE1 HIS B 271     -37.920  -6.132 -43.278  1.00 17.06           C  
ANISOU 5371  CE1 HIS B 271     1989   2251   2242    -87   -129    -45       C  
ATOM   5372  NE2 HIS B 271     -36.978  -5.208 -43.382  1.00 15.34           N  
ANISOU 5372  NE2 HIS B 271     1782   2035   2012    -74   -129    -28       N  
ATOM   5373  N   PRO B 272     -37.092  -9.502 -40.979  1.00 14.97           N  
ANISOU 5373  N   PRO B 272     1778   1944   1967   -111    -58    -84       N  
ATOM   5374  CA  PRO B 272     -38.284 -10.324 -40.721  1.00 13.10           C  
ANISOU 5374  CA  PRO B 272     1531   1699   1746   -134    -55    -98       C  
ATOM   5375  C   PRO B 272     -39.294 -10.323 -41.853  1.00 15.48           C  
ANISOU 5375  C   PRO B 272     1810   2016   2054   -148    -83   -104       C  
ATOM   5376  O   PRO B 272     -40.320 -11.012 -41.750  1.00 17.10           O  
ANISOU 5376  O   PRO B 272     2004   2220   2275   -171    -83   -118       O  
ATOM   5377  CB  PRO B 272     -38.882  -9.662 -39.475  1.00 11.89           C  
ANISOU 5377  CB  PRO B 272     1356   1542   1621   -134    -37    -94       C  
ATOM   5378  CG  PRO B 272     -38.516  -8.215 -39.646  1.00 15.93           C  
ANISOU 5378  CG  PRO B 272     1852   2063   2136   -111    -47    -79       C  
ATOM   5379  CD  PRO B 272     -37.107  -8.250 -40.209  1.00 13.75           C  
ANISOU 5379  CD  PRO B 272     1605   1790   1830    -98    -52    -71       C  
ATOM   5380  N   GLY B 273     -39.041  -9.573 -42.913  1.00 15.87           N  
ANISOU 5380  N   GLY B 273     1855   2082   2091   -136   -107    -94       N  
ATOM   5381  CA  GLY B 273     -39.965  -9.461 -44.019  1.00 15.51           C  
ANISOU 5381  CA  GLY B 273     1791   2054   2049   -146   -139    -98       C  
ATOM   5382  C   GLY B 273     -40.713  -8.138 -43.997  1.00 16.48           C  
ANISOU 5382  C   GLY B 273     1877   2186   2197   -134   -155    -86       C  
ATOM   5383  O   GLY B 273     -40.857  -7.482 -42.964  1.00 14.21           O  
ANISOU 5383  O   GLY B 273     1574   1892   1932   -124   -138    -81       O  
ATOM   5384  N   LEU B 274     -41.204  -7.742 -45.173  1.00 17.08           N  
ANISOU 5384  N   LEU B 274     1943   2280   2268   -133   -191    -82       N  
ATOM   5385  CA  LEU B 274     -41.831  -6.433 -45.293  1.00 17.45           C  
ANISOU 5385  CA  LEU B 274     1960   2333   2336   -117   -213    -68       C  
ATOM   5386  C   LEU B 274     -43.184  -6.369 -44.584  1.00 18.43           C  
ANISOU 5386  C   LEU B 274     2040   2459   2503   -122   -212    -81       C  
ATOM   5387  O   LEU B 274     -43.615  -5.281 -44.187  1.00 16.34           O  
ANISOU 5387  O   LEU B 274     1749   2194   2264   -103   -217    -74       O  
ATOM   5388  CB  LEU B 274     -41.950  -6.061 -46.769  1.00 20.51           C  
ANISOU 5388  CB  LEU B 274     2353   2737   2702   -114   -255    -58       C  
ATOM   5389  CG  LEU B 274     -40.564  -5.727 -47.367  1.00 17.70           C  
ANISOU 5389  CG  LEU B 274     2037   2382   2307   -106   -252    -41       C  
ATOM   5390  CD1 LEU B 274     -40.666  -5.331 -48.836  1.00 26.65           C  
ANISOU 5390  CD1 LEU B 274     3181   3532   3413   -106   -292    -29       C  
ATOM   5391  CD2 LEU B 274     -39.855  -4.644 -46.571  1.00 21.55           C  
ANISOU 5391  CD2 LEU B 274     2527   2858   2804    -87   -234    -23       C  
ATOM   5392  N   LYS B 275     -43.867  -7.504 -44.409  1.00 16.19           N  
ANISOU 5392  N   LYS B 275     1746   2176   2228   -148   -203   -102       N  
ATOM   5393  CA  LYS B 275     -45.098  -7.492 -43.620  1.00 19.32           C  
ANISOU 5393  CA  LYS B 275     2098   2577   2665   -157   -194   -117       C  
ATOM   5394  C   LYS B 275     -44.818  -7.051 -42.189  1.00 16.95           C  
ANISOU 5394  C   LYS B 275     1796   2263   2381   -146   -154   -114       C  
ATOM   5395  O   LYS B 275     -45.507  -6.178 -41.651  1.00 15.41           O  
ANISOU 5395  O   LYS B 275     1565   2073   2217   -132   -153   -115       O  
ATOM   5396  CB  LYS B 275     -45.763  -8.869 -43.619  1.00 21.68           C  
ANISOU 5396  CB  LYS B 275     2393   2878   2968   -193   -187   -139       C  
ATOM   5397  CG  LYS B 275     -46.524  -9.230 -44.868  1.00 30.82           C  
ANISOU 5397  CG  LYS B 275     3535   4053   4123   -208   -228   -149       C  
ATOM   5398  CD  LYS B 275     -47.662 -10.190 -44.522  1.00 32.75           C  
ANISOU 5398  CD  LYS B 275     3750   4303   4392   -244   -219   -174       C  
ATOM   5399  CE  LYS B 275     -48.070 -11.044 -45.718  1.00 37.69           C  
ANISOU 5399  CE  LYS B 275     4381   4938   5003   -269   -254   -187       C  
ATOM   5400  NZ  LYS B 275     -47.491 -12.435 -45.616  1.00 44.96           N  
ANISOU 5400  NZ  LYS B 275     5348   5837   5898   -297   -232   -198       N  
ATOM   5401  N   VAL B 276     -43.801  -7.645 -41.558  1.00 13.88           N  
ANISOU 5401  N   VAL B 276     1446   1858   1970   -151   -124   -111       N  
ATOM   5402  CA  VAL B 276     -43.444  -7.252 -40.198  1.00 17.37           C  
ANISOU 5402  CA  VAL B 276     1892   2287   2422   -142    -89   -108       C  
ATOM   5403  C   VAL B 276     -43.071  -5.775 -40.153  1.00 15.50           C  
ANISOU 5403  C   VAL B 276     1648   2050   2191   -110    -99    -92       C  
ATOM   5404  O   VAL B 276     -43.493  -5.037 -39.256  1.00 14.60           O  
ANISOU 5404  O   VAL B 276     1512   1934   2103    -98    -84    -95       O  
ATOM   5405  CB  VAL B 276     -42.297  -8.128 -39.662  1.00 17.22           C  
ANISOU 5405  CB  VAL B 276     1920   2250   2374   -148    -63   -106       C  
ATOM   5406  CG1 VAL B 276     -41.735  -7.531 -38.386  1.00 14.63           C  
ANISOU 5406  CG1 VAL B 276     1600   1910   2049   -134    -34    -99       C  
ATOM   5407  CG2 VAL B 276     -42.787  -9.583 -39.427  1.00 16.20           C  
ANISOU 5407  CG2 VAL B 276     1799   2113   2243   -182    -48   -123       C  
ATOM   5408  N   ALA B 277     -42.270  -5.324 -41.118  1.00 12.23           N  
ANISOU 5408  N   ALA B 277     1256   1638   1754    -96   -123    -76       N  
ATOM   5409  CA  ALA B 277     -41.761  -3.957 -41.045  1.00 16.84           C  
ANISOU 5409  CA  ALA B 277     1841   2216   2340    -70   -131    -58       C  
ATOM   5410  C   ALA B 277     -42.847  -2.927 -41.351  1.00 16.42           C  
ANISOU 5410  C   ALA B 277     1750   2170   2319    -54   -158    -57       C  
ATOM   5411  O   ALA B 277     -42.847  -1.842 -40.762  1.00 15.65           O  
ANISOU 5411  O   ALA B 277     1644   2063   2239    -33   -154    -51       O  
ATOM   5412  CB  ALA B 277     -40.572  -3.773 -41.994  1.00 14.93           C  
ANISOU 5412  CB  ALA B 277     1634   1976   2064    -65   -146    -41       C  
ATOM   5413  N   THR B 278     -43.775  -3.233 -42.265  1.00 14.50           N  
ANISOU 5413  N   THR B 278     1485   1942   2083    -62   -188    -63       N  
ATOM   5414  CA  THR B 278     -44.592  -2.177 -42.872  1.00 16.44           C  
ANISOU 5414  CA  THR B 278     1702   2195   2351    -40   -226    -57       C  
ATOM   5415  C   THR B 278     -46.103  -2.384 -42.826  1.00 19.39           C  
ANISOU 5415  C   THR B 278     2022   2583   2761    -44   -238    -78       C  
ATOM   5416  O   THR B 278     -46.835  -1.412 -43.063  1.00 18.23           O  
ANISOU 5416  O   THR B 278     1846   2440   2641    -20   -266    -75       O  
ATOM   5417  CB  THR B 278     -44.197  -1.962 -44.346  1.00 19.24           C  
ANISOU 5417  CB  THR B 278     2079   2555   2675    -38   -267    -38       C  
ATOM   5418  OG1 THR B 278     -44.729  -3.022 -45.148  1.00 18.20           O  
ANISOU 5418  OG1 THR B 278     1942   2440   2532    -60   -284    -51       O  
ATOM   5419  CG2 THR B 278     -42.684  -1.922 -44.501  1.00 14.75           C  
ANISOU 5419  CG2 THR B 278     1559   1977   2067    -40   -252    -21       C  
ATOM   5420  N   ASN B 279     -46.600  -3.585 -42.571  1.00 15.62           N  
ANISOU 5420  N   ASN B 279     1532   2115   2287    -74   -219    -98       N  
ATOM   5421  CA  ASN B 279     -48.043  -3.801 -42.631  1.00 17.72           C  
ANISOU 5421  CA  ASN B 279     1744   2400   2588    -82   -233   -119       C  
ATOM   5422  C   ASN B 279     -48.684  -3.404 -41.305  1.00 18.40           C  
ANISOU 5422  C   ASN B 279     1793   2486   2712    -74   -198   -135       C  
ATOM   5423  O   ASN B 279     -48.370  -4.007 -40.273  1.00 17.60           O  
ANISOU 5423  O   ASN B 279     1706   2376   2605    -93   -153   -142       O  
ATOM   5424  CB  ASN B 279     -48.349  -5.260 -42.961  1.00 19.26           C  
ANISOU 5424  CB  ASN B 279     1942   2605   2772   -122   -229   -135       C  
ATOM   5425  CG  ASN B 279     -49.809  -5.480 -43.386  1.00 25.22           C  
ANISOU 5425  CG  ASN B 279     2639   3384   3558   -134   -255   -156       C  
ATOM   5426  OD1 ASN B 279     -50.745  -5.013 -42.726  1.00 20.59           O  
ANISOU 5426  OD1 ASN B 279     2003   2809   3013   -125   -246   -170       O  
ATOM   5427  ND2 ASN B 279     -49.999  -6.172 -44.504  1.00 24.72           N  
ANISOU 5427  ND2 ASN B 279     2584   3332   3478   -153   -288   -159       N  
ATOM   5428  N   PRO B 280     -49.584  -2.414 -41.283  1.00 20.85           N  
ANISOU 5428  N   PRO B 280     2058   2805   3059    -47   -218   -140       N  
ATOM   5429  CA  PRO B 280     -50.176  -1.994 -39.998  1.00 17.68           C  
ANISOU 5429  CA  PRO B 280     1621   2404   2692    -37   -181   -159       C  
ATOM   5430  C   PRO B 280     -51.028  -3.076 -39.340  1.00 23.33           C  
ANISOU 5430  C   PRO B 280     2302   3137   3424    -75   -147   -185       C  
ATOM   5431  O   PRO B 280     -51.207  -3.051 -38.114  1.00 20.75           O  
ANISOU 5431  O   PRO B 280     1964   2809   3111    -79   -102   -199       O  
ATOM   5432  CB  PRO B 280     -51.022  -0.771 -40.381  1.00 20.68           C  
ANISOU 5432  CB  PRO B 280     1957   2792   3109      3   -219   -161       C  
ATOM   5433  CG  PRO B 280     -51.382  -1.009 -41.820  1.00 23.18           C  
ANISOU 5433  CG  PRO B 280     2267   3122   3418     -1   -274   -154       C  
ATOM   5434  CD  PRO B 280     -50.172  -1.705 -42.430  1.00 19.90           C  
ANISOU 5434  CD  PRO B 280     1915   2695   2951    -24   -275   -133       C  
ATOM   5435  N   ASN B 281     -51.541  -4.035 -40.102  1.00 19.38           N  
ANISOU 5435  N   ASN B 281     1790   2653   2920   -105   -166   -194       N  
ATOM   5436  CA  ASN B 281     -52.353  -5.090 -39.509  1.00 21.98           C  
ANISOU 5436  CA  ASN B 281     2090   2998   3265   -146   -133   -218       C  
ATOM   5437  C   ASN B 281     -51.514  -6.187 -38.870  1.00 24.78           C  
ANISOU 5437  C   ASN B 281     2497   3333   3586   -181    -91   -214       C  
ATOM   5438  O   ASN B 281     -52.074  -7.090 -38.241  1.00 25.88           O  
ANISOU 5438  O   ASN B 281     2622   3479   3733   -219    -58   -231       O  
ATOM   5439  CB  ASN B 281     -53.273  -5.695 -40.575  1.00 25.38           C  
ANISOU 5439  CB  ASN B 281     2485   3452   3707   -168   -173   -231       C  
ATOM   5440  CG  ASN B 281     -54.044  -4.636 -41.330  1.00 30.46           C  
ANISOU 5440  CG  ASN B 281     3081   4113   4381   -130   -224   -233       C  
ATOM   5441  OD1 ASN B 281     -53.979  -4.560 -42.556  1.00 34.29           O  
ANISOU 5441  OD1 ASN B 281     3575   4601   4852   -122   -275   -222       O  
ATOM   5442  ND2 ASN B 281     -54.738  -3.776 -40.593  1.00 28.30           N  
ANISOU 5442  ND2 ASN B 281     2757   3848   4146   -104   -210   -247       N  
ATOM   5443  N   PHE B 282     -50.193  -6.130 -39.016  1.00 20.24           N  
ANISOU 5443  N   PHE B 282     1982   2735   2974   -169    -93   -192       N  
ATOM   5444  CA  PHE B 282     -49.337  -7.148 -38.427  1.00 21.58           C  
ANISOU 5444  CA  PHE B 282     2204   2885   3112   -195    -58   -187       C  
ATOM   5445  C   PHE B 282     -49.432  -7.097 -36.906  1.00 20.51           C  
ANISOU 5445  C   PHE B 282     2064   2742   2985   -202     -5   -195       C  
ATOM   5446  O   PHE B 282     -49.373  -6.020 -36.303  1.00 21.12           O  
ANISOU 5446  O   PHE B 282     2129   2819   3076   -171      4   -193       O  
ATOM   5447  CB  PHE B 282     -47.894  -6.943 -38.891  1.00 18.72           C  
ANISOU 5447  CB  PHE B 282     1898   2502   2711   -175    -71   -163       C  
ATOM   5448  CG  PHE B 282     -46.895  -7.800 -38.168  1.00 19.71           C  
ANISOU 5448  CG  PHE B 282     2076   2606   2807   -191    -37   -158       C  
ATOM   5449  CD1 PHE B 282     -46.813  -9.162 -38.424  1.00 19.49           C  
ANISOU 5449  CD1 PHE B 282     2074   2571   2761   -225    -33   -164       C  
ATOM   5450  CD2 PHE B 282     -46.023  -7.239 -37.240  1.00 16.78           C  
ANISOU 5450  CD2 PHE B 282     1731   2220   2426   -172    -12   -147       C  
ATOM   5451  CE1 PHE B 282     -45.883  -9.947 -37.767  1.00 16.60           C  
ANISOU 5451  CE1 PHE B 282     1758   2181   2367   -235     -5   -159       C  
ATOM   5452  CE2 PHE B 282     -45.094  -8.021 -36.581  1.00 16.74           C  
ANISOU 5452  CE2 PHE B 282     1773   2195   2392   -183     14   -142       C  
ATOM   5453  CZ  PHE B 282     -45.022  -9.374 -36.845  1.00 14.22           C  
ANISOU 5453  CZ  PHE B 282     1480   1868   2056   -213     17   -147       C  
ATOM   5454  N   ASP B 283     -49.597  -8.263 -36.281  1.00 18.07           N  
ANISOU 5454  N   ASP B 283     1770   2429   2668   -242     28   -204       N  
ATOM   5455  CA  ASP B 283     -49.686  -8.271 -34.826  1.00 21.68           C  
ANISOU 5455  CA  ASP B 283     2229   2880   3128   -252     79   -210       C  
ATOM   5456  C   ASP B 283     -48.830  -9.378 -34.223  1.00 21.13           C  
ANISOU 5456  C   ASP B 283     2222   2785   3023   -279    107   -201       C  
ATOM   5457  O   ASP B 283     -49.145  -9.907 -33.146  1.00 19.53           O  
ANISOU 5457  O   ASP B 283     2024   2578   2818   -307    149   -208       O  
ATOM   5458  CB  ASP B 283     -51.143  -8.367 -34.356  1.00 20.29           C  
ANISOU 5458  CB  ASP B 283     1991   2731   2989   -276    101   -236       C  
ATOM   5459  CG  ASP B 283     -51.849  -9.626 -34.821  1.00 26.52           C  
ANISOU 5459  CG  ASP B 283     2769   3527   3781   -326     99   -248       C  
ATOM   5460  OD1 ASP B 283     -51.259 -10.472 -35.522  1.00 25.73           O  
ANISOU 5460  OD1 ASP B 283     2711   3410   3654   -341     79   -238       O  
ATOM   5461  OD2 ASP B 283     -53.029  -9.772 -34.467  1.00 33.61           O  
ANISOU 5461  OD2 ASP B 283     3614   4449   4709   -351    118   -269       O  
ATOM   5462  N   GLY B 284     -47.737  -9.728 -34.893  1.00 15.97           N  
ANISOU 5462  N   GLY B 284     1617   2113   2339   -269     84   -185       N  
ATOM   5463  CA  GLY B 284     -46.767 -10.634 -34.327  1.00 16.51           C  
ANISOU 5463  CA  GLY B 284     1746   2154   2374   -283    105   -175       C  
ATOM   5464  C   GLY B 284     -46.919 -12.082 -34.712  1.00 18.54           C  
ANISOU 5464  C   GLY B 284     2027   2399   2618   -322    103   -180       C  
ATOM   5465  O   GLY B 284     -46.109 -12.900 -34.258  1.00 20.30           O  
ANISOU 5465  O   GLY B 284     2304   2596   2813   -331    118   -172       O  
ATOM   5466  N   LYS B 285     -47.925 -12.433 -35.518  1.00 16.93           N  
ANISOU 5466  N   LYS B 285     1786   2212   2434   -345     85   -195       N  
ATOM   5467  CA  LYS B 285     -48.157 -13.833 -35.859  1.00 19.66           C  
ANISOU 5467  CA  LYS B 285     2156   2545   2770   -388     84   -203       C  
ATOM   5468  C   LYS B 285     -47.004 -14.378 -36.691  1.00 18.00           C  
ANISOU 5468  C   LYS B 285     1999   2313   2527   -374     58   -193       C  
ATOM   5469  O   LYS B 285     -46.574 -13.751 -37.668  1.00 15.67           O  
ANISOU 5469  O   LYS B 285     1698   2028   2226   -343     24   -187       O  
ATOM   5470  CB  LYS B 285     -49.476 -13.995 -36.622  1.00 16.06           C  
ANISOU 5470  CB  LYS B 285     1645   2115   2343   -415     64   -222       C  
ATOM   5471  CG  LYS B 285     -50.693 -13.670 -35.792  1.00 22.31           C  
ANISOU 5471  CG  LYS B 285     2378   2929   3168   -435     94   -237       C  
ATOM   5472  CD  LYS B 285     -51.960 -13.631 -36.632  1.00 26.51           C  
ANISOU 5472  CD  LYS B 285     2846   3493   3733   -453     67   -257       C  
ATOM   5473  CE  LYS B 285     -53.173 -13.314 -35.762  1.00 30.17           C  
ANISOU 5473  CE  LYS B 285     3247   3983   4233   -473    101   -275       C  
ATOM   5474  NZ  LYS B 285     -54.459 -13.430 -36.525  1.00 37.20           N  
ANISOU 5474  NZ  LYS B 285     4070   4906   5158   -496     75   -298       N  
ATOM   5475  N   LEU B 286     -46.522 -15.565 -36.316  1.00 16.54           N  
ANISOU 5475  N   LEU B 286     1867   2097   2319   -396     74   -191       N  
ATOM   5476  CA  LEU B 286     -45.369 -16.143 -37.001  1.00 16.49           C  
ANISOU 5476  CA  LEU B 286     1914   2070   2283   -380     53   -185       C  
ATOM   5477  C   LEU B 286     -45.662 -16.451 -38.465  1.00 18.58           C  
ANISOU 5477  C   LEU B 286     2168   2345   2546   -386     15   -197       C  
ATOM   5478  O   LEU B 286     -44.744 -16.417 -39.295  1.00 18.55           O  
ANISOU 5478  O   LEU B 286     2189   2338   2520   -360     -9   -192       O  
ATOM   5479  CB  LEU B 286     -44.911 -17.410 -36.273  1.00 17.89           C  
ANISOU 5479  CB  LEU B 286     2150   2209   2439   -403     76   -183       C  
ATOM   5480  CG  LEU B 286     -44.211 -17.106 -34.946  1.00 18.93           C  
ANISOU 5480  CG  LEU B 286     2308   2326   2559   -385    106   -167       C  
ATOM   5481  CD1 LEU B 286     -44.398 -18.251 -33.971  1.00 19.83           C  
ANISOU 5481  CD1 LEU B 286     2464   2409   2663   -423    136   -166       C  
ATOM   5482  CD2 LEU B 286     -42.724 -16.839 -35.175  1.00 15.00           C  
ANISOU 5482  CD2 LEU B 286     1846   1818   2037   -340     91   -155       C  
ATOM   5483  N   LYS B 287     -46.923 -16.749 -38.810  1.00 16.97           N  
ANISOU 5483  N   LYS B 287     1925   2156   2365   -422      7   -213       N  
ATOM   5484  CA  LYS B 287     -47.260 -17.022 -40.207  1.00 19.72           C  
ANISOU 5484  CA  LYS B 287     2262   2517   2712   -430    -33   -225       C  
ATOM   5485  C   LYS B 287     -47.029 -15.816 -41.106  1.00 18.55           C  
ANISOU 5485  C   LYS B 287     2089   2397   2564   -389    -66   -218       C  
ATOM   5486  O   LYS B 287     -47.010 -15.977 -42.327  1.00 20.82           O  
ANISOU 5486  O   LYS B 287     2379   2693   2839   -388   -102   -224       O  
ATOM   5487  CB  LYS B 287     -48.724 -17.479 -40.357  1.00 16.36           C  
ANISOU 5487  CB  LYS B 287     1793   2107   2315   -477    -37   -245       C  
ATOM   5488  CG  LYS B 287     -49.736 -16.379 -40.037  1.00 20.70           C  
ANISOU 5488  CG  LYS B 287     2270   2693   2901   -471    -35   -248       C  
ATOM   5489  CD  LYS B 287     -51.196 -16.875 -40.154  1.00 24.28           C  
ANISOU 5489  CD  LYS B 287     2674   3165   3386   -520    -37   -271       C  
ATOM   5490  CE  LYS B 287     -52.170 -15.721 -39.950  1.00 31.72           C  
ANISOU 5490  CE  LYS B 287     3539   4146   4366   -505    -39   -277       C  
ATOM   5491  NZ  LYS B 287     -53.586 -16.163 -39.822  1.00 35.88           N  
ANISOU 5491  NZ  LYS B 287     4010   4696   4928   -553    -33   -300       N  
ATOM   5492  N   GLU B 288     -46.845 -14.616 -40.542  1.00 18.05           N  
ANISOU 5492  N   GLU B 288     2002   2345   2511   -357    -56   -204       N  
ATOM   5493  CA  GLU B 288     -46.542 -13.430 -41.335  1.00 21.62           C  
ANISOU 5493  CA  GLU B 288     2436   2817   2961   -318    -87   -193       C  
ATOM   5494  C   GLU B 288     -45.091 -12.986 -41.197  1.00 17.82           C  
ANISOU 5494  C   GLU B 288     1996   2322   2452   -283    -80   -174       C  
ATOM   5495  O   GLU B 288     -44.717 -11.934 -41.724  1.00 18.18           O  
ANISOU 5495  O   GLU B 288     2032   2381   2494   -252   -100   -161       O  
ATOM   5496  CB  GLU B 288     -47.504 -12.307 -40.963  1.00 18.72           C  
ANISOU 5496  CB  GLU B 288     2009   2474   2630   -307    -88   -193       C  
ATOM   5497  CG  GLU B 288     -48.937 -12.745 -41.225  1.00 24.73           C  
ANISOU 5497  CG  GLU B 288     2723   3254   3421   -342    -98   -214       C  
ATOM   5498  CD  GLU B 288     -49.970 -11.731 -40.795  1.00 33.97           C  
ANISOU 5498  CD  GLU B 288     3827   4449   4630   -331    -97   -220       C  
ATOM   5499  OE1 GLU B 288     -49.606 -10.747 -40.111  1.00 31.61           O  
ANISOU 5499  OE1 GLU B 288     3524   4148   4337   -299    -81   -208       O  
ATOM   5500  OE2 GLU B 288     -51.157 -11.937 -41.132  1.00 39.02           O  
ANISOU 5500  OE2 GLU B 288     4418   5110   5296   -354   -112   -238       O  
ATOM   5501  N   ILE B 289     -44.256 -13.788 -40.549  1.00 17.04           N  
ANISOU 5501  N   ILE B 289     1944   2198   2334   -287    -54   -172       N  
ATOM   5502  CA  ILE B 289     -42.845 -13.486 -40.355  1.00 16.31           C  
ANISOU 5502  CA  ILE B 289     1887   2093   2216   -256    -47   -157       C  
ATOM   5503  C   ILE B 289     -42.022 -14.365 -41.289  1.00 18.24           C  
ANISOU 5503  C   ILE B 289     2173   2327   2429   -254    -62   -162       C  
ATOM   5504  O   ILE B 289     -42.327 -15.553 -41.457  1.00 19.35           O  
ANISOU 5504  O   ILE B 289     2335   2453   2566   -281    -62   -177       O  
ATOM   5505  CB  ILE B 289     -42.458 -13.707 -38.886  1.00 15.82           C  
ANISOU 5505  CB  ILE B 289     1846   2010   2155   -257    -10   -151       C  
ATOM   5506  CG1 ILE B 289     -43.331 -12.837 -37.967  1.00 16.17           C  
ANISOU 5506  CG1 ILE B 289     1849   2067   2229   -259      9   -150       C  
ATOM   5507  CG2 ILE B 289     -41.001 -13.445 -38.677  1.00 15.17           C  
ANISOU 5507  CG2 ILE B 289     1799   1917   2048   -225     -5   -138       C  
ATOM   5508  CD1 ILE B 289     -42.967 -12.941 -36.500  1.00 14.25           C  
ANISOU 5508  CD1 ILE B 289     1627   1806   1981   -260     46   -144       C  
ATOM   5509  N   ASP B 290     -40.979 -13.782 -41.898  1.00 19.23           N  
ANISOU 5509  N   ASP B 290     2312   2460   2533   -224    -75   -152       N  
ATOM   5510  CA AASP B 290     -40.158 -14.534 -42.836  0.58 20.33           C  
ANISOU 5510  CA AASP B 290     2487   2594   2642   -219    -87   -159       C  
ATOM   5511  CA BASP B 290     -40.119 -14.512 -42.824  0.42 20.22           C  
ANISOU 5511  CA BASP B 290     2475   2581   2628   -218    -87   -159       C  
ATOM   5512  C   ASP B 290     -39.561 -15.767 -42.166  1.00 20.42           C  
ANISOU 5512  C   ASP B 290     2542   2574   2642   -225    -66   -168       C  
ATOM   5513  O   ASP B 290     -39.148 -15.734 -41.006  1.00 14.81           O  
ANISOU 5513  O   ASP B 290     1843   1848   1935   -217    -42   -159       O  
ATOM   5514  CB AASP B 290     -39.058 -13.647 -43.413  0.58 20.65           C  
ANISOU 5514  CB AASP B 290     2534   2651   2662   -187    -96   -146       C  
ATOM   5515  CB BASP B 290     -38.971 -13.609 -43.282  0.42 20.59           C  
ANISOU 5515  CB BASP B 290     2527   2641   2654   -185    -93   -145       C  
ATOM   5516  CG AASP B 290     -39.496 -12.944 -44.684  0.58 23.06           C  
ANISOU 5516  CG AASP B 290     2818   2982   2962   -186   -128   -143       C  
ATOM   5517  CG BASP B 290     -37.938 -14.349 -44.101  0.42 21.98           C  
ANISOU 5517  CG BASP B 290     2740   2814   2797   -175    -97   -154       C  
ATOM   5518  OD1AASP B 290     -40.719 -12.898 -44.950  0.58 25.69           O  
ANISOU 5518  OD1AASP B 290     3122   3324   3314   -205   -144   -149       O  
ATOM   5519  OD1BASP B 290     -38.191 -14.582 -45.302  0.42 24.46           O  
ANISOU 5519  OD1BASP B 290     3056   3141   3096   -183   -120   -164       O  
ATOM   5520  OD2AASP B 290     -38.621 -12.469 -45.434  0.58 24.86           O  
ANISOU 5520  OD2AASP B 290     3058   3223   3165   -168   -136   -135       O  
ATOM   5521  OD2BASP B 290     -36.869 -14.701 -43.552  0.42 21.13           O  
ANISOU 5521  OD2BASP B 290     2659   2692   2678   -158    -79   -153       O  
ATOM   5522  N   ASP B 291     -39.532 -16.877 -42.917  1.00 20.27           N  
ANISOU 5522  N   ASP B 291     2551   2544   2607   -238    -77   -185       N  
ATOM   5523  CA  ASP B 291     -39.097 -18.149 -42.335  1.00 18.46           C  
ANISOU 5523  CA  ASP B 291     2367   2279   2369   -245    -61   -194       C  
ATOM   5524  C   ASP B 291     -37.642 -18.116 -41.878  1.00 20.19           C  
ANISOU 5524  C   ASP B 291     2614   2487   2570   -209    -48   -186       C  
ATOM   5525  O   ASP B 291     -37.311 -18.686 -40.834  1.00 18.53           O  
ANISOU 5525  O   ASP B 291     2432   2249   2361   -208    -30   -183       O  
ATOM   5526  CB  ASP B 291     -39.319 -19.291 -43.327  1.00 22.48           C  
ANISOU 5526  CB  ASP B 291     2900   2776   2864   -264    -79   -217       C  
ATOM   5527  CG  ASP B 291     -40.789 -19.644 -43.477  1.00 29.43           C  
ANISOU 5527  CG  ASP B 291     3758   3658   3766   -308    -88   -228       C  
ATOM   5528  OD1 ASP B 291     -41.526 -19.543 -42.464  1.00 36.57           O  
ANISOU 5528  OD1 ASP B 291     4644   4557   4694   -328    -70   -221       O  
ATOM   5529  OD2 ASP B 291     -41.214 -20.005 -44.601  1.00 32.32           O  
ANISOU 5529  OD2 ASP B 291     4124   4034   4124   -322   -113   -244       O  
ATOM   5530  N   GLU B 292     -36.748 -17.469 -42.638  1.00 18.52           N  
ANISOU 5530  N   GLU B 292     2398   2298   2341   -180    -58   -183       N  
ATOM   5531  CA  GLU B 292     -35.355 -17.502 -42.206  1.00 18.68           C  
ANISOU 5531  CA  GLU B 292     2441   2310   2345   -147    -46   -178       C  
ATOM   5532  C   GLU B 292     -35.158 -16.656 -40.953  1.00 15.21           C  
ANISOU 5532  C   GLU B 292     1987   1871   1920   -137    -29   -158       C  
ATOM   5533  O   GLU B 292     -34.352 -17.016 -40.091  1.00 15.65           O  
ANISOU 5533  O   GLU B 292     2068   1908   1971   -120    -17   -155       O  
ATOM   5534  CB  GLU B 292     -34.401 -17.068 -43.329  1.00 18.73           C  
ANISOU 5534  CB  GLU B 292     2446   2343   2329   -123    -57   -181       C  
ATOM   5535  CG  GLU B 292     -32.918 -17.339 -42.956  1.00 17.74           C  
ANISOU 5535  CG  GLU B 292     2343   2209   2187    -89    -45   -183       C  
ATOM   5536  CD  GLU B 292     -31.951 -17.342 -44.132  1.00 21.83           C  
ANISOU 5536  CD  GLU B 292     2867   2750   2679    -69    -51   -195       C  
ATOM   5537  OE1 GLU B 292     -32.307 -16.828 -45.204  1.00 19.41           O  
ANISOU 5537  OE1 GLU B 292     2544   2469   2362    -79    -64   -195       O  
ATOM   5538  OE2 GLU B 292     -30.818 -17.870 -43.981  1.00 18.64           O  
ANISOU 5538  OE2 GLU B 292     2482   2338   2262    -42    -43   -205       O  
ATOM   5539  N   PHE B 293     -35.913 -15.561 -40.811  1.00 15.16           N  
ANISOU 5539  N   PHE B 293     1944   1885   1933   -146    -30   -146       N  
ATOM   5540  CA  PHE B 293     -35.941 -14.847 -39.535  1.00 14.02           C  
ANISOU 5540  CA  PHE B 293     1787   1737   1804   -141    -13   -131       C  
ATOM   5541  C   PHE B 293     -36.370 -15.780 -38.411  1.00 14.99           C  
ANISOU 5541  C   PHE B 293     1933   1830   1934   -159      6   -135       C  
ATOM   5542  O   PHE B 293     -35.760 -15.797 -37.337  1.00 16.04           O  
ANISOU 5542  O   PHE B 293     2084   1947   2062   -147     21   -126       O  
ATOM   5543  CB  PHE B 293     -36.887 -13.643 -39.617  1.00 12.90           C  
ANISOU 5543  CB  PHE B 293     1601   1617   1683   -148    -18   -123       C  
ATOM   5544  CG  PHE B 293     -37.031 -12.883 -38.322  1.00 15.51           C  
ANISOU 5544  CG  PHE B 293     1918   1945   2030   -144      1   -111       C  
ATOM   5545  CD1 PHE B 293     -37.958 -13.276 -37.357  1.00 13.70           C  
ANISOU 5545  CD1 PHE B 293     1686   1703   1818   -167     20   -115       C  
ATOM   5546  CD2 PHE B 293     -36.253 -11.760 -38.078  1.00 15.95           C  
ANISOU 5546  CD2 PHE B 293     1965   2011   2084   -120      2    -98       C  
ATOM   5547  CE1 PHE B 293     -38.090 -12.567 -36.152  1.00 16.80           C  
ANISOU 5547  CE1 PHE B 293     2068   2094   2222   -163     40   -107       C  
ATOM   5548  CE2 PHE B 293     -36.377 -11.051 -36.900  1.00 16.60           C  
ANISOU 5548  CE2 PHE B 293     2038   2090   2180   -116     19    -91       C  
ATOM   5549  CZ  PHE B 293     -37.295 -11.445 -35.930  1.00 17.21           C  
ANISOU 5549  CZ  PHE B 293     2113   2155   2271   -136     38    -96       C  
ATOM   5550  N   ILE B 294     -37.429 -16.564 -38.642  1.00 15.27           N  
ANISOU 5550  N   ILE B 294     1969   1855   1977   -192      4   -146       N  
ATOM   5551  CA  ILE B 294     -37.950 -17.434 -37.588  1.00 18.29           C  
ANISOU 5551  CA  ILE B 294     2374   2209   2366   -217     23   -147       C  
ATOM   5552  C   ILE B 294     -36.903 -18.464 -37.180  1.00 17.31           C  
ANISOU 5552  C   ILE B 294     2304   2052   2221   -202     27   -148       C  
ATOM   5553  O   ILE B 294     -36.661 -18.681 -35.988  1.00 15.17           O  
ANISOU 5553  O   ILE B 294     2057   1760   1947   -201     44   -139       O  
ATOM   5554  CB  ILE B 294     -39.255 -18.108 -38.042  1.00 18.33           C  
ANISOU 5554  CB  ILE B 294     2369   2211   2385   -259     19   -161       C  
ATOM   5555  CG1 ILE B 294     -40.350 -17.069 -38.259  1.00 16.13           C  
ANISOU 5555  CG1 ILE B 294     2032   1965   2131   -271     15   -160       C  
ATOM   5556  CG2 ILE B 294     -39.702 -19.170 -37.015  1.00 21.01           C  
ANISOU 5556  CG2 ILE B 294     2741   2517   2726   -290     41   -162       C  
ATOM   5557  CD1 ILE B 294     -41.678 -17.665 -38.705  1.00 18.79           C  
ANISOU 5557  CD1 ILE B 294     2350   2305   2485   -312      9   -175       C  
ATOM   5558  N   LYS B 295     -36.273 -19.120 -38.167  1.00 16.54           N  
ANISOU 5558  N   LYS B 295     2228   1949   2108   -189     10   -161       N  
ATOM   5559  CA  LYS B 295     -35.222 -20.091 -37.857  1.00 21.54           C  
ANISOU 5559  CA  LYS B 295     2911   2550   2722   -167     11   -165       C  
ATOM   5560  C   LYS B 295     -34.162 -19.480 -36.952  1.00 18.02           C  
ANISOU 5560  C   LYS B 295     2468   2107   2270   -134     19   -150       C  
ATOM   5561  O   LYS B 295     -33.751 -20.074 -35.952  1.00 17.66           O  
ANISOU 5561  O   LYS B 295     2459   2032   2219   -127     27   -144       O  
ATOM   5562  CB  LYS B 295     -34.567 -20.603 -39.144  1.00 20.94           C  
ANISOU 5562  CB  LYS B 295     2849   2478   2631   -149     -8   -183       C  
ATOM   5563  CG  LYS B 295     -35.457 -21.473 -40.009  1.00 24.44           C  
ANISOU 5563  CG  LYS B 295     3302   2910   3075   -180    -19   -202       C  
ATOM   5564  CD  LYS B 295     -34.727 -21.928 -41.274  1.00 28.30           C  
ANISOU 5564  CD  LYS B 295     3806   3404   3543   -159    -36   -222       C  
ATOM   5565  CE  LYS B 295     -35.538 -22.988 -42.021  1.00 35.52           C  
ANISOU 5565  CE  LYS B 295     4741   4298   4456   -191    -48   -244       C  
ATOM   5566  NZ  LYS B 295     -35.795 -24.193 -41.167  1.00 40.98           N  
ANISOU 5566  NZ  LYS B 295     5479   4939   5153   -210    -40   -246       N  
ATOM   5567  N   ASN B 296     -33.706 -18.279 -37.294  1.00 16.71           N  
ANISOU 5567  N   ASN B 296     2267   1976   2105   -113     15   -144       N  
ATOM   5568  CA  ASN B 296     -32.619 -17.678 -36.535  1.00 13.99           C  
ANISOU 5568  CA  ASN B 296     1923   1636   1755    -82     20   -132       C  
ATOM   5569  C   ASN B 296     -33.099 -17.170 -35.181  1.00 16.54           C  
ANISOU 5569  C   ASN B 296     2242   1953   2088    -95     37   -117       C  
ATOM   5570  O   ASN B 296     -32.367 -17.245 -34.188  1.00 18.08           O  
ANISOU 5570  O   ASN B 296     2459   2135   2275    -77     42   -109       O  
ATOM   5571  CB  ASN B 296     -31.981 -16.575 -37.371  1.00 11.85           C  
ANISOU 5571  CB  ASN B 296     1619   1403   1482    -62     11   -130       C  
ATOM   5572  CG  ASN B 296     -31.013 -17.145 -38.387  1.00 15.98           C  
ANISOU 5572  CG  ASN B 296     2155   1931   1986    -39      0   -145       C  
ATOM   5573  OD1 ASN B 296     -29.890 -17.488 -38.036  1.00 17.51           O  
ANISOU 5573  OD1 ASN B 296     2367   2117   2170    -11      0   -148       O  
ATOM   5574  ND2 ASN B 296     -31.457 -17.300 -39.636  1.00 14.08           N  
ANISOU 5574  ND2 ASN B 296     1906   1703   1740    -51    -10   -157       N  
ATOM   5575  N   LEU B 297     -34.329 -16.656 -35.127  1.00 16.78           N  
ANISOU 5575  N   LEU B 297     2243   1995   2136   -123     45   -114       N  
ATOM   5576  CA  LEU B 297     -34.955 -16.317 -33.851  1.00 16.82           C  
ANISOU 5576  CA  LEU B 297     2246   1994   2150   -140     66   -105       C  
ATOM   5577  C   LEU B 297     -34.982 -17.519 -32.909  1.00 21.81           C  
ANISOU 5577  C   LEU B 297     2927   2589   2772   -153     77   -103       C  
ATOM   5578  O   LEU B 297     -34.660 -17.394 -31.721  1.00 18.71           O  
ANISOU 5578  O   LEU B 297     2553   2185   2371   -148     90    -92       O  
ATOM   5579  CB  LEU B 297     -36.370 -15.792 -34.111  1.00 15.83           C  
ANISOU 5579  CB  LEU B 297     2080   1887   2049   -169     72   -108       C  
ATOM   5580  CG  LEU B 297     -37.158 -15.232 -32.931  1.00 16.54           C  
ANISOU 5580  CG  LEU B 297     2155   1980   2151   -186     96   -102       C  
ATOM   5581  CD1 LEU B 297     -36.579 -13.881 -32.496  1.00 16.75           C  
ANISOU 5581  CD1 LEU B 297     2161   2024   2180   -158     97    -92       C  
ATOM   5582  CD2 LEU B 297     -38.636 -15.111 -33.289  1.00 18.17           C  
ANISOU 5582  CD2 LEU B 297     2322   2200   2381   -218    101   -111       C  
ATOM   5583  N   LYS B 298     -35.344 -18.698 -33.427  1.00 17.31           N  
ANISOU 5583  N   LYS B 298     2382   1996   2199   -172     72   -113       N  
ATOM   5584  CA  LYS B 298     -35.362 -19.901 -32.604  1.00 22.03           C  
ANISOU 5584  CA  LYS B 298     3033   2552   2785   -187     81   -110       C  
ATOM   5585  C   LYS B 298     -33.969 -20.385 -32.229  1.00 20.16           C  
ANISOU 5585  C   LYS B 298     2838   2293   2527   -148     69   -105       C  
ATOM   5586  O   LYS B 298     -33.843 -21.218 -31.332  1.00 21.58           O  
ANISOU 5586  O   LYS B 298     3066   2437   2695   -154     74    -98       O  
ATOM   5587  CB  LYS B 298     -36.120 -21.007 -33.322  1.00 20.76           C  
ANISOU 5587  CB  LYS B 298     2889   2371   2628   -219     76   -123       C  
ATOM   5588  CG  LYS B 298     -37.599 -20.716 -33.459  1.00 22.12           C  
ANISOU 5588  CG  LYS B 298     3022   2561   2821   -264     88   -127       C  
ATOM   5589  CD  LYS B 298     -38.189 -21.554 -34.561  1.00 26.12           C  
ANISOU 5589  CD  LYS B 298     3532   3060   3333   -288     74   -145       C  
ATOM   5590  CE  LYS B 298     -38.346 -22.970 -34.127  1.00 29.69           C  
ANISOU 5590  CE  LYS B 298     4041   3464   3775   -315     79   -146       C  
ATOM   5591  NZ  LYS B 298     -38.788 -23.794 -35.278  1.00 36.47           N  
ANISOU 5591  NZ  LYS B 298     4906   4313   4638   -336     62   -166       N  
ATOM   5592  N   ILE B 299     -32.925 -19.899 -32.887  1.00 18.97           N  
ANISOU 5592  N   ILE B 299     2671   2163   2373   -110     53   -110       N  
ATOM   5593  CA  ILE B 299     -31.568 -20.152 -32.413  1.00 18.41           C  
ANISOU 5593  CA  ILE B 299     2629   2079   2286    -69     42   -107       C  
ATOM   5594  C   ILE B 299     -31.134 -19.092 -31.412  1.00 18.43           C  
ANISOU 5594  C   ILE B 299     2616   2100   2288    -55     49    -92       C  
ATOM   5595  O   ILE B 299     -30.589 -19.405 -30.356  1.00 16.70           O  
ANISOU 5595  O   ILE B 299     2431   1859   2056    -42     49    -83       O  
ATOM   5596  CB  ILE B 299     -30.603 -20.223 -33.611  1.00 15.53           C  
ANISOU 5596  CB  ILE B 299     2253   1730   1917    -36     24   -122       C  
ATOM   5597  CG1 ILE B 299     -30.802 -21.547 -34.354  1.00 23.52           C  
ANISOU 5597  CG1 ILE B 299     3300   2713   2925    -42     14   -139       C  
ATOM   5598  CG2 ILE B 299     -29.179 -20.062 -33.144  1.00 17.22           C  
ANISOU 5598  CG2 ILE B 299     2476   1947   2121      9     14   -120       C  
ATOM   5599  CD1 ILE B 299     -30.638 -21.411 -35.815  1.00 23.67           C  
ANISOU 5599  CD1 ILE B 299     3293   2757   2943    -34      4   -157       C  
ATOM   5600  N   LEU B 300     -31.380 -17.825 -31.749  1.00 16.07           N  
ANISOU 5600  N   LEU B 300     2267   1838   2001    -58     54    -91       N  
ATOM   5601  CA  LEU B 300     -31.005 -16.703 -30.894  1.00 17.67           C  
ANISOU 5601  CA  LEU B 300     2452   2058   2204    -46     60    -80       C  
ATOM   5602  C   LEU B 300     -31.516 -16.859 -29.466  1.00 15.39           C  
ANISOU 5602  C   LEU B 300     2190   1749   1909    -65     78    -68       C  
ATOM   5603  O   LEU B 300     -30.749 -16.742 -28.502  1.00 16.61           O  
ANISOU 5603  O   LEU B 300     2366   1896   2050    -46     75    -60       O  
ATOM   5604  CB  LEU B 300     -31.550 -15.410 -31.506  1.00 15.70           C  
ANISOU 5604  CB  LEU B 300     2151   1844   1972    -55     64    -80       C  
ATOM   5605  CG  LEU B 300     -31.474 -14.153 -30.651  1.00 17.94           C  
ANISOU 5605  CG  LEU B 300     2413   2143   2260    -50     73    -71       C  
ATOM   5606  CD1 LEU B 300     -30.032 -13.765 -30.436  1.00 19.57           C  
ANISOU 5606  CD1 LEU B 300     2623   2358   2455    -17     60    -68       C  
ATOM   5607  CD2 LEU B 300     -32.251 -13.018 -31.324  1.00 13.32           C  
ANISOU 5607  CD2 LEU B 300     1781   1585   1695    -61     75    -72       C  
ATOM   5608  N   ILE B 301     -32.816 -17.088 -29.310  1.00 15.75           N  
ANISOU 5608  N   ILE B 301     2233   1787   1963   -103     96    -69       N  
ATOM   5609  CA  ILE B 301     -33.468 -16.957 -28.006  1.00 20.35           C  
ANISOU 5609  CA  ILE B 301     2829   2361   2541   -127    120    -59       C  
ATOM   5610  C   ILE B 301     -32.952 -18.022 -27.040  1.00 15.99           C  
ANISOU 5610  C   ILE B 301     2340   1771   1964   -124    119    -49       C  
ATOM   5611  O   ILE B 301     -32.486 -17.666 -25.951  1.00 15.38           O  
ANISOU 5611  O   ILE B 301     2280   1691   1872   -113    122    -39       O  
ATOM   5612  CB  ILE B 301     -35.003 -17.017 -28.124  1.00 18.75           C  
ANISOU 5612  CB  ILE B 301     2606   2164   2356   -170    142    -64       C  
ATOM   5613  CG1 ILE B 301     -35.544 -15.900 -29.020  1.00 22.80           C  
ANISOU 5613  CG1 ILE B 301     3057   2713   2894   -169    139    -73       C  
ATOM   5614  CG2 ILE B 301     -35.647 -16.981 -26.745  1.00 20.36           C  
ANISOU 5614  CG2 ILE B 301     2826   2359   2551   -196    171    -56       C  
ATOM   5615  CD1 ILE B 301     -35.211 -14.573 -28.550  1.00 21.10           C  
ANISOU 5615  CD1 ILE B 301     2815   2520   2682   -149    142    -68       C  
ATOM   5616  N   PRO B 302     -33.024 -19.322 -27.357  1.00 16.57           N  
ANISOU 5616  N   PRO B 302     2453   1812   2031   -133    112    -51       N  
ATOM   5617  CA  PRO B 302     -32.446 -20.311 -26.423  1.00 18.18           C  
ANISOU 5617  CA  PRO B 302     2721   1975   2210   -126    106    -40       C  
ATOM   5618  C   PRO B 302     -30.952 -20.119 -26.204  1.00 20.23           C  
ANISOU 5618  C   PRO B 302     2992   2237   2457    -74     80    -37       C  
ATOM   5619  O   PRO B 302     -30.455 -20.360 -25.098  1.00 19.17           O  
ANISOU 5619  O   PRO B 302     2898   2082   2302    -64     76    -24       O  
ATOM   5620  CB  PRO B 302     -32.753 -21.661 -27.091  1.00 18.39           C  
ANISOU 5620  CB  PRO B 302     2782   1968   2238   -141     98    -46       C  
ATOM   5621  CG  PRO B 302     -33.866 -21.388 -28.054  1.00 22.45           C  
ANISOU 5621  CG  PRO B 302     3250   2505   2776   -173    110    -59       C  
ATOM   5622  CD  PRO B 302     -33.611 -19.981 -28.541  1.00 18.61           C  
ANISOU 5622  CD  PRO B 302     2703   2066   2303   -151    106    -64       C  
ATOM   5623  N   TRP B 303     -30.218 -19.680 -27.226  1.00 18.73           N  
ANISOU 5623  N   TRP B 303     2766   2071   2278    -43     62    -49       N  
ATOM   5624  CA  TRP B 303     -28.804 -19.366 -27.040  1.00 20.92           C  
ANISOU 5624  CA  TRP B 303     3042   2358   2547      3     40    -49       C  
ATOM   5625  C   TRP B 303     -28.618 -18.315 -25.947  1.00 23.25           C  
ANISOU 5625  C   TRP B 303     3327   2672   2836      5     48    -39       C  
ATOM   5626  O   TRP B 303     -27.707 -18.427 -25.117  1.00 24.82           O  
ANISOU 5626  O   TRP B 303     3553   2861   3018     31     33    -32       O  
ATOM   5627  CB  TRP B 303     -28.223 -18.900 -28.370  1.00 15.60           C  
ANISOU 5627  CB  TRP B 303     2324   1716   1888     26     28    -65       C  
ATOM   5628  CG  TRP B 303     -26.811 -18.406 -28.383  1.00 22.25           C  
ANISOU 5628  CG  TRP B 303     3149   2578   2726     69      9    -68       C  
ATOM   5629  CD1 TRP B 303     -25.675 -19.145 -28.204  1.00 25.83           C  
ANISOU 5629  CD1 TRP B 303     3630   3016   3169    108    -14    -72       C  
ATOM   5630  CD2 TRP B 303     -26.375 -17.069 -28.692  1.00 21.93           C  
ANISOU 5630  CD2 TRP B 303     3058   2580   2695     78      9    -70       C  
ATOM   5631  NE1 TRP B 303     -24.564 -18.342 -28.345  1.00 26.18           N  
ANISOU 5631  NE1 TRP B 303     3638   3093   3215    138    -26    -78       N  
ATOM   5632  CE2 TRP B 303     -24.967 -17.068 -28.652  1.00 24.62           C  
ANISOU 5632  CE2 TRP B 303     3395   2930   3030    118    -11    -76       C  
ATOM   5633  CE3 TRP B 303     -27.043 -15.875 -28.976  1.00 16.55           C  
ANISOU 5633  CE3 TRP B 303     2335   1927   2028     56     24    -68       C  
ATOM   5634  CZ2 TRP B 303     -24.210 -15.914 -28.888  1.00 18.08           C  
ANISOU 5634  CZ2 TRP B 303     2522   2139   2207    131    -15    -78       C  
ATOM   5635  CZ3 TRP B 303     -26.290 -14.728 -29.213  1.00 19.56           C  
ANISOU 5635  CZ3 TRP B 303     2677   2341   2413     71     18    -69       C  
ATOM   5636  CH2 TRP B 303     -24.888 -14.759 -29.162  1.00 20.53           C  
ANISOU 5636  CH2 TRP B 303     2798   2473   2529    106      0    -74       C  
ATOM   5637  N   LEU B 304     -29.505 -17.314 -25.902  1.00 19.62           N  
ANISOU 5637  N   LEU B 304     2830   2236   2388    -21     69    -38       N  
ATOM   5638  CA  LEU B 304     -29.433 -16.289 -24.862  1.00 20.45           C  
ANISOU 5638  CA  LEU B 304     2926   2356   2487    -22     79    -31       C  
ATOM   5639  C   LEU B 304     -29.933 -16.784 -23.512  1.00 21.31           C  
ANISOU 5639  C   LEU B 304     3083   2439   2574    -44     95    -18       C  
ATOM   5640  O   LEU B 304     -29.383 -16.409 -22.471  1.00 19.52           O  
ANISOU 5640  O   LEU B 304     2875   2212   2329    -32     91    -11       O  
ATOM   5641  CB  LEU B 304     -30.250 -15.064 -25.270  1.00 17.60           C  
ANISOU 5641  CB  LEU B 304     2511   2027   2148    -40     96    -37       C  
ATOM   5642  CG  LEU B 304     -29.741 -14.242 -26.444  1.00 20.47           C  
ANISOU 5642  CG  LEU B 304     2828   2421   2530    -20     82    -45       C  
ATOM   5643  CD1 LEU B 304     -30.729 -13.128 -26.774  1.00 18.42           C  
ANISOU 5643  CD1 LEU B 304     2523   2185   2291    -40     98    -48       C  
ATOM   5644  CD2 LEU B 304     -28.381 -13.690 -26.117  1.00 20.57           C  
ANISOU 5644  CD2 LEU B 304     2837   2445   2533     13     63    -44       C  
ATOM   5645  N   LEU B 305     -30.998 -17.594 -23.501  1.00 23.52           N  
ANISOU 5645  N   LEU B 305     3384   2698   2854    -80    114    -16       N  
ATOM   5646  CA  LEU B 305     -31.800 -17.796 -22.303  1.00 19.95           C  
ANISOU 5646  CA  LEU B 305     2965   2231   2385   -114    141     -5       C  
ATOM   5647  C   LEU B 305     -31.850 -19.222 -21.787  1.00 24.49           C  
ANISOU 5647  C   LEU B 305     3608   2761   2937   -128    140      7       C  
ATOM   5648  O   LEU B 305     -32.499 -19.447 -20.763  1.00 24.11           O  
ANISOU 5648  O   LEU B 305     3592   2699   2869   -160    164     18       O  
ATOM   5649  CB  LEU B 305     -33.250 -17.342 -22.546  1.00 17.87           C  
ANISOU 5649  CB  LEU B 305     2662   1987   2142   -155    175    -13       C  
ATOM   5650  CG  LEU B 305     -33.415 -15.879 -22.920  1.00 22.74           C  
ANISOU 5650  CG  LEU B 305     3214   2644   2781   -145    179    -24       C  
ATOM   5651  CD1 LEU B 305     -34.887 -15.521 -23.087  1.00 22.35           C  
ANISOU 5651  CD1 LEU B 305     3127   2612   2754   -182    210    -33       C  
ATOM   5652  CD2 LEU B 305     -32.750 -15.033 -21.848  1.00 19.07           C  
ANISOU 5652  CD2 LEU B 305     2758   2188   2300   -126    179    -19       C  
ATOM   5653  N   SER B 306     -31.245 -20.193 -22.471  1.00 24.04           N  
ANISOU 5653  N   SER B 306     3575   2678   2880   -108    113      5       N  
ATOM   5654  CA  SER B 306     -31.342 -21.566 -21.990  1.00 31.54           C  
ANISOU 5654  CA  SER B 306     4595   3579   3809   -122    110     18       C  
ATOM   5655  C   SER B 306     -30.718 -21.663 -20.598  1.00 27.66           C  
ANISOU 5655  C   SER B 306     4157   3070   3284   -109    103     36       C  
ATOM   5656  O   SER B 306     -29.858 -20.854 -20.243  1.00 26.63           O  
ANISOU 5656  O   SER B 306     4009   2961   3148    -75     88     36       O  
ATOM   5657  CB  SER B 306     -30.655 -22.547 -22.947  1.00 30.25           C  
ANISOU 5657  CB  SER B 306     4451   3390   3652    -93     80     10       C  
ATOM   5658  OG  SER B 306     -29.239 -22.436 -22.893  1.00 33.52           O  
ANISOU 5658  OG  SER B 306     4870   3807   4059    -38     46      9       O  
ATOM   5659  N   PRO B 307     -31.161 -22.620 -19.778  1.00 35.90           N  
ANISOU 5659  N   PRO B 307     5267   4073   4302   -139    113     54       N  
ATOM   5660  CA  PRO B 307     -30.598 -22.735 -18.421  1.00 37.01           C  
ANISOU 5660  CA  PRO B 307     5464   4195   4405   -128    105     73       C  
ATOM   5661  C   PRO B 307     -29.080 -22.735 -18.388  1.00 37.14           C  
ANISOU 5661  C   PRO B 307     5490   4207   4414    -66     58     74       C  
ATOM   5662  O   PRO B 307     -28.494 -22.103 -17.502  1.00 38.88           O  
ANISOU 5662  O   PRO B 307     5717   4442   4615    -47     49     80       O  
ATOM   5663  CB  PRO B 307     -31.195 -24.056 -17.925  1.00 37.49           C  
ANISOU 5663  CB  PRO B 307     5599   4202   4443   -166    115     92       C  
ATOM   5664  CG  PRO B 307     -32.525 -24.105 -18.592  1.00 34.62           C  
ANISOU 5664  CG  PRO B 307     5201   3850   4104   -218    151     81       C  
ATOM   5665  CD  PRO B 307     -32.301 -23.534 -19.974  1.00 33.04           C  
ANISOU 5665  CD  PRO B 307     4928   3682   3942   -191    137     57       C  
ATOM   5666  N   GLU B 308     -28.426 -23.381 -19.360  1.00 39.36           N  
ANISOU 5666  N   GLU B 308     5769   4474   4712    -32     29     63       N  
ATOM   5667  CA  GLU B 308     -26.966 -23.370 -19.402  1.00 39.32           C  
ANISOU 5667  CA  GLU B 308     5764   4470   4704     30    -14     59       C  
ATOM   5668  C   GLU B 308     -26.402 -21.964 -19.577  1.00 36.64           C  
ANISOU 5668  C   GLU B 308     5356   4186   4379     53    -17     46       C  
ATOM   5669  O   GLU B 308     -25.323 -21.663 -19.059  1.00 42.22           O  
ANISOU 5669  O   GLU B 308     6066   4902   5075     92    -45     48       O  
ATOM   5670  CB  GLU B 308     -26.457 -24.272 -20.531  1.00 39.03           C  
ANISOU 5670  CB  GLU B 308     5731   4412   4686     61    -39     45       C  
ATOM   5671  CG  GLU B 308     -27.551 -24.871 -21.421  1.00 43.33           C  
ANISOU 5671  CG  GLU B 308     6273   4941   5248     20    -15     38       C  
ATOM   5672  CD  GLU B 308     -28.117 -26.185 -20.880  1.00 50.92           C  
ANISOU 5672  CD  GLU B 308     7317   5842   6190    -10    -12     55       C  
ATOM   5673  OE1 GLU B 308     -27.349 -27.171 -20.744  1.00 42.91           O  
ANISOU 5673  OE1 GLU B 308     6356   4783   5163     25    -46     61       O  
ATOM   5674  OE2 GLU B 308     -29.336 -26.225 -20.588  1.00 52.76           O  
ANISOU 5674  OE2 GLU B 308     7558   6071   6419    -68     23     64       O  
ATOM   5675  N   SER B 309     -27.099 -21.090 -20.301  1.00 36.61           N  
ANISOU 5675  N   SER B 309     5291   4220   4401     29     10     33       N  
ATOM   5676  CA  SER B 309     -26.521 -19.809 -20.700  1.00 34.63           C  
ANISOU 5676  CA  SER B 309     4974   4016   4166     52      5     20       C  
ATOM   5677  C   SER B 309     -26.755 -18.686 -19.698  1.00 37.64           C  
ANISOU 5677  C   SER B 309     5344   4422   4537     36     21     25       C  
ATOM   5678  O   SER B 309     -26.218 -17.587 -19.890  1.00 38.28           O  
ANISOU 5678  O   SER B 309     5377   4538   4630     54     15     15       O  
ATOM   5679  CB  SER B 309     -27.085 -19.373 -22.052  1.00 33.54           C  
ANISOU 5679  CB  SER B 309     4778   3905   4062     38     20      3       C  
ATOM   5680  OG  SER B 309     -26.946 -20.396 -23.019  1.00 37.01           O  
ANISOU 5680  OG  SER B 309     5229   4324   4511     50      7     -5       O  
ATOM   5681  N   LEU B 310     -27.535 -18.926 -18.647  1.00 31.94           N  
ANISOU 5681  N   LEU B 310     4664   3680   3790      2     44     39       N  
ATOM   5682  CA  LEU B 310     -27.992 -17.855 -17.764  1.00 34.34           C  
ANISOU 5682  CA  LEU B 310     4954   4008   4084    -18     68     40       C  
ATOM   5683  C   LEU B 310     -26.884 -17.511 -16.773  1.00 34.98           C  
ANISOU 5683  C   LEU B 310     5059   4092   4139     13     40     47       C  
ATOM   5684  O   LEU B 310     -26.637 -18.249 -15.819  1.00 38.01           O  
ANISOU 5684  O   LEU B 310     5507   4446   4490     14     28     63       O  
ATOM   5685  CB  LEU B 310     -29.272 -18.272 -17.051  1.00 31.38           C  
ANISOU 5685  CB  LEU B 310     4615   3615   3692    -69    107     51       C  
ATOM   5686  CG  LEU B 310     -30.493 -18.516 -17.940  1.00 30.44           C  
ANISOU 5686  CG  LEU B 310     4466   3498   3600   -106    137     43       C  
ATOM   5687  CD1 LEU B 310     -31.681 -19.018 -17.123  1.00 31.25           C  
ANISOU 5687  CD1 LEU B 310     4606   3584   3683   -158    176     54       C  
ATOM   5688  CD2 LEU B 310     -30.858 -17.254 -18.705  1.00 24.16           C  
ANISOU 5688  CD2 LEU B 310     3594   2747   2839   -105    149     25       C  
ATOM   5689  N   ASP B 311     -26.223 -16.375 -16.990  1.00 32.80           N  
ANISOU 5689  N   ASP B 311     4734   3851   3878     35     28     34       N  
ATOM   5690  CA  ASP B 311     -25.172 -15.910 -16.089  1.00 35.00           C  
ANISOU 5690  CA  ASP B 311     5026   4138   4135     62      0     36       C  
ATOM   5691  C   ASP B 311     -25.790 -15.156 -14.913  1.00 26.97           C  
ANISOU 5691  C   ASP B 311     4024   3129   3093     34     26     39       C  
ATOM   5692  O   ASP B 311     -26.513 -14.171 -15.108  1.00 25.82           O  
ANISOU 5692  O   ASP B 311     3836   3007   2966     13     56     28       O  
ATOM   5693  CB  ASP B 311     -24.192 -15.007 -16.835  1.00 36.19           C  
ANISOU 5693  CB  ASP B 311     5116   4323   4312     93    -23     20       C  
ATOM   5694  CG  ASP B 311     -23.863 -15.528 -18.226  1.00 47.82           C  
ANISOU 5694  CG  ASP B 311     6558   5797   5813    112    -35     12       C  
ATOM   5695  OD1 ASP B 311     -23.550 -16.738 -18.339  1.00 51.64           O  
ANISOU 5695  OD1 ASP B 311     7080   6251   6288    129    -53     18       O  
ATOM   5696  OD2 ASP B 311     -23.928 -14.729 -19.197  1.00 42.01           O  
ANISOU 5696  OD2 ASP B 311     5765   5090   5106    110    -26     -1       O  
ATOM   5697  N   ILE B 312     -25.508 -15.619 -13.695  1.00 24.44           N  
ANISOU 5697  N   ILE B 312     3766   2788   2732     35     14     54       N  
ATOM   5698  CA  ILE B 312     -25.963 -14.905 -12.511  1.00 21.67           C  
ANISOU 5698  CA  ILE B 312     3434   2446   2353     11     37     55       C  
ATOM   5699  C   ILE B 312     -25.304 -13.535 -12.476  1.00 20.89           C  
ANISOU 5699  C   ILE B 312     3288   2382   2266     30     24     38       C  
ATOM   5700  O   ILE B 312     -24.092 -13.398 -12.698  1.00 19.74           O  
ANISOU 5700  O   ILE B 312     3127   2246   2127     66    -18     34       O  
ATOM   5701  CB  ILE B 312     -25.656 -15.719 -11.249  1.00 24.70           C  
ANISOU 5701  CB  ILE B 312     3900   2801   2685     12     20     75       C  
ATOM   5702  CG1 ILE B 312     -26.575 -16.942 -11.193  1.00 30.11           C  
ANISOU 5702  CG1 ILE B 312     4635   3450   3357    -20     45     93       C  
ATOM   5703  CG2 ILE B 312     -25.803 -14.853  -9.994  1.00 19.72           C  
ANISOU 5703  CG2 ILE B 312     3288   2185   2020     -3     34     73       C  
ATOM   5704  CD1 ILE B 312     -25.897 -18.182 -10.681  1.00 36.25           C  
ANISOU 5704  CD1 ILE B 312     5487   4186   4102      0      8    115       C  
ATOM   5705  N   LYS B 313     -26.112 -12.509 -12.218  1.00 19.88           N  
ANISOU 5705  N   LYS B 313     3135   2276   2144      4     59     26       N  
ATOM   5706  CA  LYS B 313     -25.598 -11.151 -12.123  1.00 20.09           C  
ANISOU 5706  CA  LYS B 313     3121   2330   2181     16     50      9       C  
ATOM   5707  C   LYS B 313     -24.524 -11.041 -11.048  1.00 21.25           C  
ANISOU 5707  C   LYS B 313     3305   2476   2292     37     13     12       C  
ATOM   5708  O   LYS B 313     -24.719 -11.475  -9.909  1.00 23.39           O  
ANISOU 5708  O   LYS B 313     3637   2732   2520     25     18     24       O  
ATOM   5709  CB  LYS B 313     -26.737 -10.184 -11.819  1.00 16.71           C  
ANISOU 5709  CB  LYS B 313     2673   1917   1759    -14     95     -4       C  
ATOM   5710  CG  LYS B 313     -26.266  -8.740 -11.616  1.00 16.94           C  
ANISOU 5710  CG  LYS B 313     2668   1970   1797     -4     86    -22       C  
ATOM   5711  CD  LYS B 313     -25.800  -8.114 -12.919  1.00 18.32           C  
ANISOU 5711  CD  LYS B 313     2780   2162   2018     14     70    -32       C  
ATOM   5712  CE  LYS B 313     -25.299  -6.671 -12.693  1.00 15.85           C  
ANISOU 5712  CE  LYS B 313     2439   1869   1714     21     60    -48       C  
ATOM   5713  NZ  LYS B 313     -24.692  -6.151 -13.953  1.00 16.02           N  
ANISOU 5713  NZ  LYS B 313     2406   1906   1776     36     40    -54       N  
ATOM   5714  N   GLU B 314     -23.393 -10.438 -11.411  1.00 19.39           N  
ANISOU 5714  N   GLU B 314     3034   2259   2073     66    -23      2       N  
ATOM   5715  CA  GLU B 314     -22.341 -10.099 -10.466  1.00 23.16           C  
ANISOU 5715  CA  GLU B 314     3534   2743   2523     85    -60      1       C  
ATOM   5716  C   GLU B 314     -22.078  -8.600 -10.487  1.00 22.09           C  
ANISOU 5716  C   GLU B 314     3353   2636   2406     82    -60    -20       C  
ATOM   5717  O   GLU B 314     -22.040  -7.974 -11.552  1.00 20.69           O  
ANISOU 5717  O   GLU B 314     3117   2475   2269     84    -55    -31       O  
ATOM   5718  CB  GLU B 314     -21.040 -10.868 -10.770  1.00 22.22           C  
ANISOU 5718  CB  GLU B 314     3417   2619   2405    124   -112      7       C  
ATOM   5719  CG  GLU B 314     -21.190 -12.350 -10.535  1.00 26.32           C  
ANISOU 5719  CG  GLU B 314     3995   3104   2901    130   -120     28       C  
ATOM   5720  CD  GLU B 314     -19.929 -13.141 -10.815  1.00 34.01           C  
ANISOU 5720  CD  GLU B 314     4972   4071   3878    175   -172     32       C  
ATOM   5721  OE1 GLU B 314     -18.822 -12.558 -10.778  1.00 39.99           O  
ANISOU 5721  OE1 GLU B 314     5699   4853   4644    200   -208     20       O  
ATOM   5722  OE2 GLU B 314     -20.053 -14.356 -11.068  1.00 34.74           O  
ANISOU 5722  OE2 GLU B 314     5099   4134   3967    184   -178     46       O  
ATOM   5723  N   ILE B 315     -21.894  -8.031  -9.300  1.00 20.67           N  
ANISOU 5723  N   ILE B 315     3203   2460   2192     76    -66    -26       N  
ATOM   5724  CA  ILE B 315     -21.482  -6.645  -9.145  1.00 20.67           C  
ANISOU 5724  CA  ILE B 315     3169   2481   2202     75    -74    -46       C  
ATOM   5725  C   ILE B 315     -20.309  -6.624  -8.185  1.00 25.22           C  
ANISOU 5725  C   ILE B 315     3775   3063   2746     94   -121    -47       C  
ATOM   5726  O   ILE B 315     -20.410  -7.147  -7.068  1.00 23.08           O  
ANISOU 5726  O   ILE B 315     3565   2777   2428     90   -126    -37       O  
ATOM   5727  CB  ILE B 315     -22.616  -5.750  -8.627  1.00 21.73           C  
ANISOU 5727  CB  ILE B 315     3308   2618   2332     46    -28    -59       C  
ATOM   5728  CG1 ILE B 315     -23.770  -5.744  -9.628  1.00 17.68           C  
ANISOU 5728  CG1 ILE B 315     2759   2104   1856     30     15    -60       C  
ATOM   5729  CG2 ILE B 315     -22.089  -4.335  -8.394  1.00 20.89           C  
ANISOU 5729  CG2 ILE B 315     3175   2530   2234     46    -41    -81       C  
ATOM   5730  CD1 ILE B 315     -25.060  -5.093  -9.103  1.00 17.90           C  
ANISOU 5730  CD1 ILE B 315     2791   2132   1877      3     65    -73       C  
ATOM   5731  N   ASN B 316     -19.193  -6.043  -8.625  1.00 24.71           N  
ANISOU 5731  N   ASN B 316     3666   3017   2704    112   -158    -58       N  
ATOM   5732  CA  ASN B 316     -18.016  -5.891  -7.777  1.00 28.25           C  
ANISOU 5732  CA  ASN B 316     4132   3476   3127    129   -207    -63       C  
ATOM   5733  C   ASN B 316     -17.575  -7.246  -7.224  1.00 28.29           C  
ANISOU 5733  C   ASN B 316     4189   3462   3097    152   -239    -43       C  
ATOM   5734  O   ASN B 316     -17.172  -7.368  -6.065  1.00 29.49           O  
ANISOU 5734  O   ASN B 316     4389   3609   3205    157   -266    -40       O  
ATOM   5735  CB  ASN B 316     -18.291  -4.884  -6.657  1.00 28.77           C  
ANISOU 5735  CB  ASN B 316     4224   3545   3164    108   -198    -78       C  
ATOM   5736  CG  ASN B 316     -17.023  -4.361  -6.008  1.00 30.39           C  
ANISOU 5736  CG  ASN B 316     4427   3766   3353    121   -250    -90       C  
ATOM   5737  OD1 ASN B 316     -15.933  -4.464  -6.567  1.00 32.07           O  
ANISOU 5737  OD1 ASN B 316     4602   3995   3590    143   -289    -92       O  
ATOM   5738  ND2 ASN B 316     -17.164  -3.799  -4.816  1.00 30.85           N  
ANISOU 5738  ND2 ASN B 316     4526   3823   3372    107   -250   -100       N  
ATOM   5739  N   GLY B 317     -17.693  -8.280  -8.056  1.00 28.28           N  
ANISOU 5739  N   GLY B 317     4183   3449   3115    166   -236    -29       N  
ATOM   5740  CA  GLY B 317     -17.229  -9.609  -7.713  1.00 28.70           C  
ANISOU 5740  CA  GLY B 317     4283   3480   3143    192   -269    -10       C  
ATOM   5741  C   GLY B 317     -18.174 -10.454  -6.886  1.00 32.39           C  
ANISOU 5741  C   GLY B 317     4826   3914   3566    174   -245     11       C  
ATOM   5742  O   GLY B 317     -17.794 -11.560  -6.480  1.00 31.85           O  
ANISOU 5742  O   GLY B 317     4808   3823   3472    195   -276     29       O  
ATOM   5743  N   ASN B 318     -19.391  -9.986  -6.623  1.00 25.70           N  
ANISOU 5743  N   ASN B 318     3990   3064   2710    136   -192      8       N  
ATOM   5744  CA  ASN B 318     -20.332 -10.722  -5.790  1.00 26.02           C  
ANISOU 5744  CA  ASN B 318     4102   3078   2707    112   -164     27       C  
ATOM   5745  C   ASN B 318     -21.558 -11.081  -6.609  1.00 25.56           C  
ANISOU 5745  C   ASN B 318     4027   3009   2675     86   -111     31       C  
ATOM   5746  O   ASN B 318     -22.069 -10.256  -7.370  1.00 22.13           O  
ANISOU 5746  O   ASN B 318     3536   2593   2280     73    -80     15       O  
ATOM   5747  CB  ASN B 318     -20.749  -9.906  -4.559  1.00 26.27           C  
ANISOU 5747  CB  ASN B 318     4167   3118   2698     86   -145     18       C  
ATOM   5748  CG  ASN B 318     -19.553  -9.450  -3.728  1.00 31.61           C  
ANISOU 5748  CG  ASN B 318     4857   3807   3346    108   -199     11       C  
ATOM   5749  OD1 ASN B 318     -18.654 -10.236  -3.428  1.00 33.34           O  
ANISOU 5749  OD1 ASN B 318     5107   4015   3546    137   -249     25       O  
ATOM   5750  ND2 ASN B 318     -19.536  -8.173  -3.366  1.00 27.61           N  
ANISOU 5750  ND2 ASN B 318     4328   3323   2841     95   -191    -13       N  
ATOM   5751  N   LYS B 319     -22.012 -12.319  -6.470  1.00 25.05           N  
ANISOU 5751  N   LYS B 319     4014   2913   2589     79   -103     54       N  
ATOM   5752  CA  LYS B 319     -23.268 -12.709  -7.087  1.00 23.56           C  
ANISOU 5752  CA  LYS B 319     3818   2714   2420     48    -51     58       C  
ATOM   5753  C   LYS B 319     -24.419 -12.048  -6.347  1.00 22.56           C  
ANISOU 5753  C   LYS B 319     3703   2596   2272      6      2     50       C  
ATOM   5754  O   LYS B 319     -24.394 -11.910  -5.123  1.00 26.29           O  
ANISOU 5754  O   LYS B 319     4227   3067   2696     -4      2     54       O  
ATOM   5755  CB  LYS B 319     -23.418 -14.224  -7.090  1.00 26.89           C  
ANISOU 5755  CB  LYS B 319     4296   3097   2824     48    -59     84       C  
ATOM   5756  CG  LYS B 319     -22.278 -14.928  -7.797  1.00 27.91           C  
ANISOU 5756  CG  LYS B 319     4415   3215   2974     94   -112     88       C  
ATOM   5757  CD  LYS B 319     -22.651 -16.362  -8.126  1.00 34.59           C  
ANISOU 5757  CD  LYS B 319     5306   4021   3817     91   -109    109       C  
ATOM   5758  CE  LYS B 319     -21.428 -17.152  -8.565  1.00 35.37           C  
ANISOU 5758  CE  LYS B 319     5409   4105   3926    143   -168    114       C  
ATOM   5759  NZ  LYS B 319     -20.643 -16.416  -9.595  1.00 39.62           N  
ANISOU 5759  NZ  LYS B 319     5864   4678   4512    173   -186     89       N  
ATOM   5760  N   ILE B 320     -25.432 -11.637  -7.095  1.00 21.11           N  
ANISOU 5760  N   ILE B 320     3472   2424   2125    -17     48     38       N  
ATOM   5761  CA  ILE B 320     -26.463 -10.737  -6.599  1.00 20.53           C  
ANISOU 5761  CA  ILE B 320     3387   2367   2045    -49     98     22       C  
ATOM   5762  C   ILE B 320     -27.783 -11.484  -6.535  1.00 23.14           C  
ANISOU 5762  C   ILE B 320     3741   2684   2368    -88    149     32       C  
ATOM   5763  O   ILE B 320     -28.128 -12.234  -7.456  1.00 22.74           O  
ANISOU 5763  O   ILE B 320     3674   2621   2346    -92    155     41       O  
ATOM   5764  CB  ILE B 320     -26.576  -9.495  -7.507  1.00 20.30           C  
ANISOU 5764  CB  ILE B 320     3278   2365   2069    -42    107     -3       C  
ATOM   5765  CG1 ILE B 320     -25.231  -8.771  -7.589  1.00 22.68           C  
ANISOU 5765  CG1 ILE B 320     3557   2681   2380     -8     57    -12       C  
ATOM   5766  CG2 ILE B 320     -27.679  -8.560  -7.034  1.00 19.60           C  
ANISOU 5766  CG2 ILE B 320     3176   2293   1980    -70    159    -22       C  
ATOM   5767  CD1 ILE B 320     -24.722  -8.269  -6.252  1.00 25.02           C  
ANISOU 5767  CD1 ILE B 320     3896   2982   2630     -7     41    -18       C  
ATOM   5768  N   THR B 321     -28.520 -11.271  -5.453  1.00 20.85           N  
ANISOU 5768  N   THR B 321     3487   2397   2039   -119    188     30       N  
ATOM   5769  CA  THR B 321     -29.875 -11.782  -5.339  1.00 20.38           C  
ANISOU 5769  CA  THR B 321     3439   2332   1973   -162    245     34       C  
ATOM   5770  C   THR B 321     -30.875 -10.738  -5.823  1.00 21.75           C  
ANISOU 5770  C   THR B 321     3543   2534   2188   -177    291      6       C  
ATOM   5771  O   THR B 321     -30.547  -9.564  -6.010  1.00 20.72           O  
ANISOU 5771  O   THR B 321     3368   2425   2080   -156    280    -16       O  
ATOM   5772  CB  THR B 321     -30.183 -12.163  -3.893  1.00 23.43           C  
ANISOU 5772  CB  THR B 321     3903   2708   2291   -191    268     46       C  
ATOM   5773  OG1 THR B 321     -30.067 -10.992  -3.077  1.00 25.19           O  
ANISOU 5773  OG1 THR B 321     4122   2955   2493   -188    276     24       O  
ATOM   5774  CG2 THR B 321     -29.203 -13.204  -3.410  1.00 23.76           C  
ANISOU 5774  CG2 THR B 321     4017   2718   2291   -174    218     76       C  
ATOM   5775  N   CYS B 322     -32.120 -11.182  -6.018  1.00 20.33           N  
ANISOU 5775  N   CYS B 322     3353   2354   2017   -213    340      6       N  
ATOM   5776  CA  CYS B 322     -33.178 -10.259  -6.405  1.00 20.81           C  
ANISOU 5776  CA  CYS B 322     3348   2442   2115   -227    385    -22       C  
ATOM   5777  C   CYS B 322     -33.271  -9.102  -5.434  1.00 24.32           C  
ANISOU 5777  C   CYS B 322     3795   2907   2538   -226    404    -45       C  
ATOM   5778  O   CYS B 322     -33.431  -7.947  -5.848  1.00 22.51           O  
ANISOU 5778  O   CYS B 322     3508   2698   2345   -210    409    -71       O  
ATOM   5779  CB  CYS B 322     -34.516 -10.982  -6.480  1.00 22.63           C  
ANISOU 5779  CB  CYS B 322     3577   2671   2349   -272    437    -18       C  
ATOM   5780  SG  CYS B 322     -34.602 -12.130  -7.846  1.00 21.61           S  
ANISOU 5780  SG  CYS B 322     3430   2521   2259   -274    418      0       S  
ATOM   5781  N   ARG B 323     -33.166  -9.400  -4.133  1.00 23.54           N  
ANISOU 5781  N   ARG B 323     3765   2802   2377   -243    415    -37       N  
ATOM   5782  CA  ARG B 323     -33.217  -8.362  -3.113  1.00 23.95           C  
ANISOU 5782  CA  ARG B 323     3828   2872   2400   -243    434    -60       C  
ATOM   5783  C   ARG B 323     -32.035  -7.410  -3.245  1.00 23.51           C  
ANISOU 5783  C   ARG B 323     3755   2821   2357   -201    381    -72       C  
ATOM   5784  O   ARG B 323     -32.196  -6.191  -3.157  1.00 26.75           O  
ANISOU 5784  O   ARG B 323     4130   3250   2784   -191    393   -101       O  
ATOM   5785  CB  ARG B 323     -33.244  -9.006  -1.723  1.00 27.20           C  
ANISOU 5785  CB  ARG B 323     4325   3274   2735   -270    450    -45       C  
ATOM   5786  CG  ARG B 323     -33.325  -8.035  -0.565  1.00 35.98           C  
ANISOU 5786  CG  ARG B 323     5459   4405   3808   -274    472    -70       C  
ATOM   5787  CD  ARG B 323     -33.562  -8.770   0.757  1.00 42.26           C  
ANISOU 5787  CD  ARG B 323     6340   5191   4524   -309    498    -53       C  
ATOM   5788  NE  ARG B 323     -32.383  -9.511   1.193  1.00 50.98           N  
ANISOU 5788  NE  ARG B 323     7515   6271   5585   -293    439    -21       N  
ATOM   5789  CZ  ARG B 323     -31.379  -8.980   1.882  1.00 56.77           C  
ANISOU 5789  CZ  ARG B 323     8280   7005   6285   -268    396    -26       C  
ATOM   5790  NH1 ARG B 323     -31.374  -7.699   2.221  1.00 50.10           N  
ANISOU 5790  NH1 ARG B 323     7408   6184   5445   -257    406    -61       N  
ATOM   5791  NH2 ARG B 323     -30.354  -9.752   2.238  1.00 55.43           N  
ANISOU 5791  NH2 ARG B 323     8171   6812   6078   -252    341      4       N  
ATOM   5792  N   GLY B 324     -30.833  -7.952  -3.447  1.00 21.73           N  
ANISOU 5792  N   GLY B 324     3554   2579   2124   -176    323    -50       N  
ATOM   5793  CA  GLY B 324     -29.669  -7.098  -3.605  1.00 20.72           C  
ANISOU 5793  CA  GLY B 324     3406   2458   2010   -140    272    -61       C  
ATOM   5794  C   GLY B 324     -29.698  -6.282  -4.883  1.00 23.57           C  
ANISOU 5794  C   GLY B 324     3686   2831   2438   -122    266    -77       C  
ATOM   5795  O   GLY B 324     -29.170  -5.165  -4.924  1.00 22.06           O  
ANISOU 5795  O   GLY B 324     3468   2651   2263   -103    247    -97       O  
ATOM   5796  N   LEU B 325     -30.314  -6.818  -5.939  1.00 19.74           N  
ANISOU 5796  N   LEU B 325     3165   2342   1993   -128    281    -69       N  
ATOM   5797  CA  LEU B 325     -30.461  -6.062  -7.179  1.00 19.23           C  
ANISOU 5797  CA  LEU B 325     3027   2289   1990   -114    278    -83       C  
ATOM   5798  C   LEU B 325     -31.351  -4.845  -6.978  1.00 20.33           C  
ANISOU 5798  C   LEU B 325     3131   2446   2147   -121    317   -113       C  
ATOM   5799  O   LEU B 325     -31.102  -3.786  -7.569  1.00 18.00           O  
ANISOU 5799  O   LEU B 325     2791   2160   1889   -102    303   -129       O  
ATOM   5800  CB  LEU B 325     -31.037  -6.948  -8.281  1.00 19.18           C  
ANISOU 5800  CB  LEU B 325     2994   2276   2016   -122    288    -70       C  
ATOM   5801  CG  LEU B 325     -30.939  -6.407  -9.708  1.00 19.44           C  
ANISOU 5801  CG  LEU B 325     2960   2319   2109   -104    271    -77       C  
ATOM   5802  CD1 LEU B 325     -29.505  -6.517 -10.217  1.00 21.34           C  
ANISOU 5802  CD1 LEU B 325     3200   2555   2355    -73    215    -66       C  
ATOM   5803  CD2 LEU B 325     -31.891  -7.156 -10.626  1.00 20.31           C  
ANISOU 5803  CD2 LEU B 325     3044   2426   2248   -121    294    -70       C  
ATOM   5804  N   VAL B 326     -32.407  -4.984  -6.170  1.00 21.33           N  
ANISOU 5804  N   VAL B 326     3278   2578   2248   -149    368   -122       N  
ATOM   5805  CA  VAL B 326     -33.212  -3.818  -5.813  1.00 22.76           C  
ANISOU 5805  CA  VAL B 326     3431   2776   2442   -153    407   -154       C  
ATOM   5806  C   VAL B 326     -32.331  -2.750  -5.188  1.00 22.43           C  
ANISOU 5806  C   VAL B 326     3404   2736   2384   -132    379   -171       C  
ATOM   5807  O   VAL B 326     -32.441  -1.560  -5.511  1.00 21.59           O  
ANISOU 5807  O   VAL B 326     3256   2637   2312   -117    380   -195       O  
ATOM   5808  CB  VAL B 326     -34.357  -4.215  -4.863  1.00 23.66           C  
ANISOU 5808  CB  VAL B 326     3572   2897   2520   -188    467   -161       C  
ATOM   5809  CG1 VAL B 326     -35.052  -2.955  -4.304  1.00 22.79           C  
ANISOU 5809  CG1 VAL B 326     3438   2805   2415   -186    505   -200       C  
ATOM   5810  CG2 VAL B 326     -35.349  -5.093  -5.575  1.00 24.59           C  
ANISOU 5810  CG2 VAL B 326     3663   3016   2663   -211    497   -150       C  
ATOM   5811  N   GLU B 327     -31.445  -3.155  -4.279  1.00 22.40           N  
ANISOU 5811  N   GLU B 327     3460   2724   2327   -132    353   -159       N  
ATOM   5812  CA  GLU B 327     -30.612  -2.171  -3.602  1.00 23.91           C  
ANISOU 5812  CA  GLU B 327     3667   2917   2499   -116    326   -176       C  
ATOM   5813  C   GLU B 327     -29.709  -1.450  -4.590  1.00 20.77           C  
ANISOU 5813  C   GLU B 327     3224   2520   2149    -89    279   -179       C  
ATOM   5814  O   GLU B 327     -29.512  -0.232  -4.486  1.00 18.09           O  
ANISOU 5814  O   GLU B 327     2866   2184   1823    -78    273   -204       O  
ATOM   5815  CB  GLU B 327     -29.792  -2.840  -2.502  1.00 22.32           C  
ANISOU 5815  CB  GLU B 327     3540   2709   2233   -120    300   -160       C  
ATOM   5816  CG  GLU B 327     -30.615  -3.250  -1.282  1.00 25.14           C  
ANISOU 5816  CG  GLU B 327     3952   3068   2532   -150    348   -162       C  
ATOM   5817  CD  GLU B 327     -31.470  -2.122  -0.734  1.00 26.66           C  
ANISOU 5817  CD  GLU B 327     4129   3277   2725   -158    395   -201       C  
ATOM   5818  OE1 GLU B 327     -30.967  -0.990  -0.572  1.00 23.76           O  
ANISOU 5818  OE1 GLU B 327     3750   2913   2366   -140    375   -225       O  
ATOM   5819  OE2 GLU B 327     -32.667  -2.365  -0.487  1.00 33.69           O  
ANISOU 5819  OE2 GLU B 327     5017   4176   3608   -183    454   -208       O  
ATOM   5820  N   TYR B 328     -29.155  -2.182  -5.560  1.00 19.52           N  
ANISOU 5820  N   TYR B 328     3047   2355   2014    -78    247   -155       N  
ATOM   5821  CA  TYR B 328     -28.279  -1.544  -6.542  1.00 18.87           C  
ANISOU 5821  CA  TYR B 328     2921   2275   1975    -55    206   -156       C  
ATOM   5822  C   TYR B 328     -29.069  -0.652  -7.483  1.00 17.77           C  
ANISOU 5822  C   TYR B 328     2721   2140   1889    -53    229   -172       C  
ATOM   5823  O   TYR B 328     -28.592   0.416  -7.881  1.00 21.49           O  
ANISOU 5823  O   TYR B 328     3164   2614   2389    -40    208   -186       O  
ATOM   5824  CB  TYR B 328     -27.497  -2.597  -7.321  1.00 19.35           C  
ANISOU 5824  CB  TYR B 328     2979   2329   2043    -43    169   -129       C  
ATOM   5825  CG  TYR B 328     -26.190  -2.923  -6.644  1.00 19.62           C  
ANISOU 5825  CG  TYR B 328     3053   2361   2041    -30    122   -119       C  
ATOM   5826  CD1 TYR B 328     -25.143  -2.007  -6.649  1.00 18.97           C  
ANISOU 5826  CD1 TYR B 328     2954   2286   1967    -15     84   -131       C  
ATOM   5827  CD2 TYR B 328     -26.006  -4.131  -5.978  1.00 19.41           C  
ANISOU 5827  CD2 TYR B 328     3083   2323   1970    -34    114    -98       C  
ATOM   5828  CE1 TYR B 328     -23.935  -2.297  -6.019  1.00 17.98           C  
ANISOU 5828  CE1 TYR B 328     2861   2162   1810     -2     37   -125       C  
ATOM   5829  CE2 TYR B 328     -24.811  -4.425  -5.350  1.00 19.07           C  
ANISOU 5829  CE2 TYR B 328     3075   2277   1893    -18     66    -90       C  
ATOM   5830  CZ  TYR B 328     -23.782  -3.506  -5.374  1.00 18.52           C  
ANISOU 5830  CZ  TYR B 328     2982   2219   1835     -1     27   -104       C  
ATOM   5831  OH  TYR B 328     -22.596  -3.805  -4.748  1.00 22.58           O  
ANISOU 5831  OH  TYR B 328     3528   2734   2318     15    -23    -97       O  
ATOM   5832  N   PHE B 329     -30.285  -1.058  -7.827  1.00 16.45           N  
ANISOU 5832  N   PHE B 329     2536   1975   1738    -66    270   -172       N  
ATOM   5833  CA  PHE B 329     -31.136  -0.198  -8.634  1.00 22.81           C  
ANISOU 5833  CA  PHE B 329     3287   2787   2594    -62    292   -189       C  
ATOM   5834  C   PHE B 329     -31.422   1.114  -7.913  1.00 21.06           C  
ANISOU 5834  C   PHE B 329     3064   2567   2370    -58    308   -220       C  
ATOM   5835  O   PHE B 329     -31.389   2.190  -8.528  1.00 19.44           O  
ANISOU 5835  O   PHE B 329     2822   2359   2204    -44    297   -234       O  
ATOM   5836  CB  PHE B 329     -32.434  -0.931  -8.977  1.00 22.63           C  
ANISOU 5836  CB  PHE B 329     3246   2768   2584    -80    334   -185       C  
ATOM   5837  CG  PHE B 329     -32.896  -0.707 -10.380  1.00 24.97           C  
ANISOU 5837  CG  PHE B 329     3483   3067   2936    -72    330   -183       C  
ATOM   5838  CD1 PHE B 329     -32.474   0.409 -11.090  1.00 31.25           C  
ANISOU 5838  CD1 PHE B 329     4244   3862   3768    -51    305   -192       C  
ATOM   5839  CD2 PHE B 329     -33.733  -1.608 -10.998  1.00 29.30           C  
ANISOU 5839  CD2 PHE B 329     4013   3619   3500    -86    351   -172       C  
ATOM   5840  CE1 PHE B 329     -32.897   0.623 -12.384  1.00 29.80           C  
ANISOU 5840  CE1 PHE B 329     4010   3680   3632    -44    300   -189       C  
ATOM   5841  CE2 PHE B 329     -34.153  -1.404 -12.296  1.00 28.51           C  
ANISOU 5841  CE2 PHE B 329     3860   3523   3449    -78    344   -171       C  
ATOM   5842  CZ  PHE B 329     -33.738  -0.288 -12.987  1.00 31.90           C  
ANISOU 5842  CZ  PHE B 329     4257   3951   3911    -56    318   -179       C  
ATOM   5843  N   LYS B 330     -31.695   1.045  -6.604  1.00 18.05           N  
ANISOU 5843  N   LYS B 330     2728   2189   1943    -71    334   -233       N  
ATOM   5844  CA  LYS B 330     -31.929   2.264  -5.833  1.00 20.18           C  
ANISOU 5844  CA  LYS B 330     3003   2460   2206    -67    351   -266       C  
ATOM   5845  C   LYS B 330     -30.659   3.093  -5.727  1.00 20.63           C  
ANISOU 5845  C   LYS B 330     3070   2509   2261    -51    302   -272       C  
ATOM   5846  O   LYS B 330     -30.691   4.315  -5.904  1.00 18.72           O  
ANISOU 5846  O   LYS B 330     2805   2261   2046    -40    298   -295       O  
ATOM   5847  CB  LYS B 330     -32.463   1.925  -4.436  1.00 23.93           C  
ANISOU 5847  CB  LYS B 330     3527   2941   2624    -86    391   -278       C  
ATOM   5848  CG  LYS B 330     -33.874   1.325  -4.441  1.00 25.38           C  
ANISOU 5848  CG  LYS B 330     3695   3136   2812   -106    449   -281       C  
ATOM   5849  CD  LYS B 330     -34.502   1.245  -3.043  1.00 30.03           C  
ANISOU 5849  CD  LYS B 330     4328   3735   3347   -127    497   -299       C  
ATOM   5850  CE  LYS B 330     -33.724   0.328  -2.113  1.00 31.09           C  
ANISOU 5850  CE  LYS B 330     4535   3864   3415   -142    479   -276       C  
ATOM   5851  NZ  LYS B 330     -34.531  -0.095  -0.920  1.00 32.72           N  
ANISOU 5851  NZ  LYS B 330     4785   4081   3566   -171    534   -285       N  
ATOM   5852  N   ALA B 331     -29.528   2.439  -5.455  1.00 19.01           N  
ANISOU 5852  N   ALA B 331     2898   2301   2023    -52    263   -251       N  
ATOM   5853  CA  ALA B 331     -28.263   3.154  -5.356  1.00 19.95           C  
ANISOU 5853  CA  ALA B 331     3023   2416   2141    -40    214   -256       C  
ATOM   5854  C   ALA B 331     -27.919   3.831  -6.678  1.00 17.44           C  
ANISOU 5854  C   ALA B 331     2651   2095   1881    -27    190   -253       C  
ATOM   5855  O   ALA B 331     -27.594   5.020  -6.713  1.00 20.08           O  
ANISOU 5855  O   ALA B 331     2973   2424   2234    -22    176   -272       O  
ATOM   5856  CB  ALA B 331     -27.154   2.189  -4.927  1.00 17.91           C  
ANISOU 5856  CB  ALA B 331     2804   2159   1842    -40    175   -232       C  
ATOM   5857  N   TYR B 332     -28.011   3.088  -7.784  1.00 16.09           N  
ANISOU 5857  N   TYR B 332     2448   1926   1738    -25    186   -229       N  
ATOM   5858  CA  TYR B 332     -27.604   3.632  -9.073  1.00 19.77           C  
ANISOU 5858  CA  TYR B 332     2867   2391   2254    -14    161   -223       C  
ATOM   5859  C   TYR B 332     -28.492   4.799  -9.490  1.00 18.89           C  
ANISOU 5859  C   TYR B 332     2723   2272   2181    -10    184   -244       C  
ATOM   5860  O   TYR B 332     -27.995   5.821  -9.978  1.00 18.49           O  
ANISOU 5860  O   TYR B 332     2653   2215   2158     -4    161   -251       O  
ATOM   5861  CB  TYR B 332     -27.638   2.529 -10.131  1.00 16.80           C  
ANISOU 5861  CB  TYR B 332     2469   2019   1895    -13    156   -196       C  
ATOM   5862  CG  TYR B 332     -26.541   1.492  -9.989  1.00 18.01           C  
ANISOU 5862  CG  TYR B 332     2646   2176   2020     -9    123   -175       C  
ATOM   5863  CD1 TYR B 332     -25.327   1.813  -9.394  1.00 13.74           C  
ANISOU 5863  CD1 TYR B 332     2126   1638   1458     -4     85   -179       C  
ATOM   5864  CD2 TYR B 332     -26.721   0.191 -10.454  1.00 16.14           C  
ANISOU 5864  CD2 TYR B 332     2412   1940   1781    -10    127   -153       C  
ATOM   5865  CE1 TYR B 332     -24.312   0.878  -9.285  1.00 17.35           C  
ANISOU 5865  CE1 TYR B 332     2601   2099   1894      4     51   -162       C  
ATOM   5866  CE2 TYR B 332     -25.708  -0.759 -10.339  1.00 19.85           C  
ANISOU 5866  CE2 TYR B 332     2905   2410   2228     -2     93   -136       C  
ATOM   5867  CZ  TYR B 332     -24.507  -0.402  -9.757  1.00 17.33           C  
ANISOU 5867  CZ  TYR B 332     2602   2095   1889      7     55   -140       C  
ATOM   5868  OH  TYR B 332     -23.498  -1.333  -9.636  1.00 18.18           O  
ANISOU 5868  OH  TYR B 332     2729   2204   1976     19     20   -124       O  
ATOM   5869  N   ILE B 333     -29.807   4.672  -9.294  1.00 16.90           N  
ANISOU 5869  N   ILE B 333     2465   2022   1933    -14    229   -255       N  
ATOM   5870  CA  ILE B 333     -30.716   5.723  -9.739  1.00 20.31           C  
ANISOU 5870  CA  ILE B 333     2863   2448   2407     -5    249   -275       C  
ATOM   5871  C   ILE B 333     -30.502   6.974  -8.912  1.00 19.57           C  
ANISOU 5871  C   ILE B 333     2788   2342   2304      0    246   -305       C  
ATOM   5872  O   ILE B 333     -30.563   8.094  -9.431  1.00 22.88           O  
ANISOU 5872  O   ILE B 333     3185   2749   2761     12    236   -317       O  
ATOM   5873  CB  ILE B 333     -32.175   5.238  -9.686  1.00 23.81           C  
ANISOU 5873  CB  ILE B 333     3291   2900   2857    -10    297   -282       C  
ATOM   5874  CG1 ILE B 333     -32.420   4.252 -10.824  1.00 23.55           C  
ANISOU 5874  CG1 ILE B 333     3229   2874   2846    -13    294   -255       C  
ATOM   5875  CG2 ILE B 333     -33.143   6.399  -9.806  1.00 25.72           C  
ANISOU 5875  CG2 ILE B 333     3503   3135   3133      4    320   -311       C  
ATOM   5876  CD1 ILE B 333     -33.812   3.666 -10.838  1.00 29.50           C  
ANISOU 5876  CD1 ILE B 333     3963   3638   3607    -23    338   -260       C  
ATOM   5877  N   LYS B 334     -30.202   6.797  -7.626  1.00 20.62           N  
ANISOU 5877  N   LYS B 334     2968   2479   2388     -8    252   -316       N  
ATOM   5878  CA  LYS B 334     -29.958   7.935  -6.746  1.00 22.17           C  
ANISOU 5878  CA  LYS B 334     3189   2665   2571     -5    249   -347       C  
ATOM   5879  C   LYS B 334     -28.777   8.759  -7.238  1.00 24.04           C  
ANISOU 5879  C   LYS B 334     3418   2889   2827     -1    200   -344       C  
ATOM   5880  O   LYS B 334     -28.806   9.998  -7.196  1.00 21.76           O  
ANISOU 5880  O   LYS B 334     3126   2583   2559      5    195   -367       O  
ATOM   5881  CB  LYS B 334     -29.712   7.429  -5.331  1.00 22.49           C  
ANISOU 5881  CB  LYS B 334     3285   2714   2548    -17    258   -355       C  
ATOM   5882  CG  LYS B 334     -29.672   8.495  -4.254  1.00 28.99           C  
ANISOU 5882  CG  LYS B 334     4139   3528   3347    -16    264   -392       C  
ATOM   5883  CD  LYS B 334     -29.546   7.825  -2.886  1.00 30.05           C  
ANISOU 5883  CD  LYS B 334     4330   3673   3413    -30    277   -396       C  
ATOM   5884  CE  LYS B 334     -29.536   8.833  -1.752  1.00 42.72           C  
ANISOU 5884  CE  LYS B 334     5972   5272   4989    -31    285   -436       C  
ATOM   5885  NZ  LYS B 334     -29.347   8.160  -0.425  1.00 42.33           N  
ANISOU 5885  NZ  LYS B 334     5982   5234   4866    -46    294   -437       N  
ATOM   5886  N   ILE B 335     -27.736   8.083  -7.726  1.00 20.94           N  
ANISOU 5886  N   ILE B 335     3023   2504   2430     -6    163   -316       N  
ATOM   5887  CA  ILE B 335     -26.603   8.774  -8.332  1.00 21.80           C  
ANISOU 5887  CA  ILE B 335     3117   2606   2561     -6    119   -310       C  
ATOM   5888  C   ILE B 335     -27.057   9.562  -9.553  1.00 19.71           C  
ANISOU 5888  C   ILE B 335     2810   2328   2352      2    120   -308       C  
ATOM   5889  O   ILE B 335     -26.734  10.746  -9.704  1.00 22.77           O  
ANISOU 5889  O   ILE B 335     3193   2698   2760      2    104   -322       O  
ATOM   5890  CB  ILE B 335     -25.497   7.764  -8.685  1.00 20.10           C  
ANISOU 5890  CB  ILE B 335     2899   2405   2332    -10     85   -281       C  
ATOM   5891  CG1 ILE B 335     -24.953   7.153  -7.397  1.00 20.31           C  
ANISOU 5891  CG1 ILE B 335     2973   2440   2302    -15     75   -285       C  
ATOM   5892  CG2 ILE B 335     -24.397   8.433  -9.512  1.00 23.12           C  
ANISOU 5892  CG2 ILE B 335     3256   2786   2743    -13     44   -274       C  
ATOM   5893  CD1 ILE B 335     -24.263   5.853  -7.605  1.00 23.25           C  
ANISOU 5893  CD1 ILE B 335     3350   2827   2658    -13     53   -256       C  
ATOM   5894  N   TYR B 336     -27.827   8.925 -10.440  1.00 20.64           N  
ANISOU 5894  N   TYR B 336     2898   2453   2493      7    139   -291       N  
ATOM   5895  CA  TYR B 336     -28.263   9.632 -11.644  1.00 20.66           C  
ANISOU 5895  CA  TYR B 336     2861   2443   2545     15    137   -286       C  
ATOM   5896  C   TYR B 336     -29.292  10.717 -11.348  1.00 22.49           C  
ANISOU 5896  C   TYR B 336     3091   2657   2799     27    161   -315       C  
ATOM   5897  O   TYR B 336     -29.412  11.668 -12.134  1.00 21.98           O  
ANISOU 5897  O   TYR B 336     3006   2574   2772     35    149   -316       O  
ATOM   5898  CB  TYR B 336     -28.801   8.638 -12.669  1.00 19.83           C  
ANISOU 5898  CB  TYR B 336     2725   2351   2457     18    147   -261       C  
ATOM   5899  CG  TYR B 336     -27.696   7.765 -13.257  1.00 17.03           C  
ANISOU 5899  CG  TYR B 336     2366   2011   2093     10    117   -233       C  
ATOM   5900  CD1 TYR B 336     -26.516   8.330 -13.736  1.00 15.92           C  
ANISOU 5900  CD1 TYR B 336     2219   1867   1962      5     81   -226       C  
ATOM   5901  CD2 TYR B 336     -27.826   6.387 -13.298  1.00 19.66           C  
ANISOU 5901  CD2 TYR B 336     2703   2360   2408      8    126   -216       C  
ATOM   5902  CE1 TYR B 336     -25.508   7.542 -14.274  1.00 17.34           C  
ANISOU 5902  CE1 TYR B 336     2391   2064   2135      1     56   -204       C  
ATOM   5903  CE2 TYR B 336     -26.815   5.587 -13.822  1.00 18.45           C  
ANISOU 5903  CE2 TYR B 336     2546   2217   2247      6     99   -194       C  
ATOM   5904  CZ  TYR B 336     -25.662   6.172 -14.296  1.00 17.81           C  
ANISOU 5904  CZ  TYR B 336     2454   2137   2177      4     65   -189       C  
ATOM   5905  OH  TYR B 336     -24.677   5.366 -14.814  1.00 18.81           O  
ANISOU 5905  OH  TYR B 336     2572   2278   2296      4     41   -171       O  
ATOM   5906  N   GLN B 337     -30.029  10.606 -10.237  1.00 19.71           N  
ANISOU 5906  N   GLN B 337     2760   2308   2420     29    195   -340       N  
ATOM   5907  CA  GLN B 337     -30.946  11.679  -9.847  1.00 20.06           C  
ANISOU 5907  CA  GLN B 337     2803   2335   2483     44    219   -373       C  
ATOM   5908  C   GLN B 337     -30.195  12.886  -9.298  1.00 21.32           C  
ANISOU 5908  C   GLN B 337     2991   2473   2638     43    196   -395       C  
ATOM   5909  O   GLN B 337     -30.702  14.013  -9.348  1.00 23.58           O  
ANISOU 5909  O   GLN B 337     3272   2735   2953     58    201   -419       O  
ATOM   5910  CB  GLN B 337     -31.939  11.174  -8.805  1.00 21.21           C  
ANISOU 5910  CB  GLN B 337     2963   2496   2600     44    267   -395       C  
ATOM   5911  CG  GLN B 337     -33.019  10.258  -9.334  1.00 22.04           C  
ANISOU 5911  CG  GLN B 337     3035   2619   2719     45    299   -383       C  
ATOM   5912  CD  GLN B 337     -33.734   9.557  -8.206  1.00 25.24           C  
ANISOU 5912  CD  GLN B 337     3462   3044   3085     35    344   -398       C  
ATOM   5913  OE1 GLN B 337     -33.154   9.344  -7.137  1.00 24.60           O  
ANISOU 5913  OE1 GLN B 337     3426   2966   2956     23    345   -405       O  
ATOM   5914  NE2 GLN B 337     -34.996   9.201  -8.425  1.00 23.54           N  
ANISOU 5914  NE2 GLN B 337     3215   2841   2889     39    383   -405       N  
ATOM   5915  N   GLY B 338     -29.018  12.675  -8.738  1.00 21.16           N  
ANISOU 5915  N   GLY B 338     2999   2457   2582     27    169   -390       N  
ATOM   5916  CA  GLY B 338     -28.186  13.771  -8.300  1.00 23.66           C  
ANISOU 5916  CA  GLY B 338     3340   2753   2895     22    141   -409       C  
ATOM   5917  C   GLY B 338     -27.397  14.365  -9.451  1.00 26.30           C  
ANISOU 5917  C   GLY B 338     3652   3074   3268     16    102   -388       C  
ATOM   5918  O   GLY B 338     -27.751  14.241 -10.629  1.00 23.08           O  
ANISOU 5918  O   GLY B 338     3210   2666   2895     22    102   -366       O  
ATOM   5919  N   GLU B 339     -26.305  15.037  -9.088  1.00 25.92           N  
ANISOU 5919  N   GLU B 339     3625   3014   3209      1     69   -397       N  
ATOM   5920  CA  GLU B 339     -25.472  15.742 -10.052  1.00 25.65           C  
ANISOU 5920  CA  GLU B 339     3574   2965   3206    -11     34   -381       C  
ATOM   5921  C   GLU B 339     -23.990  15.465  -9.833  1.00 26.58           C  
ANISOU 5921  C   GLU B 339     3700   3100   3301    -34     -3   -371       C  
ATOM   5922  O   GLU B 339     -23.154  16.287 -10.215  1.00 26.06           O  
ANISOU 5922  O   GLU B 339     3630   3019   3251    -51    -33   -369       O  
ATOM   5923  CB  GLU B 339     -25.748  17.249  -9.997  1.00 23.49           C  
ANISOU 5923  CB  GLU B 339     3314   2651   2960     -7     30   -407       C  
ATOM   5924  CG  GLU B 339     -27.147  17.649 -10.447  1.00 23.89           C  
ANISOU 5924  CG  GLU B 339     3349   2684   3045     20     59   -415       C  
ATOM   5925  CD  GLU B 339     -27.391  17.324 -11.917  1.00 31.54           C  
ANISOU 5925  CD  GLU B 339     4277   3657   4049     25     54   -379       C  
ATOM   5926  OE1 GLU B 339     -26.395  17.199 -12.675  1.00 31.05           O  
ANISOU 5926  OE1 GLU B 339     4204   3602   3992      5     25   -352       O  
ATOM   5927  OE2 GLU B 339     -28.574  17.199 -12.314  1.00 31.49           O  
ANISOU 5927  OE2 GLU B 339     4251   3650   4065     47     79   -380       O  
ATOM   5928  N   GLU B 340     -23.649  14.340  -9.200  1.00 22.83           N  
ANISOU 5928  N   GLU B 340     3235   2653   2786    -36     -3   -364       N  
ATOM   5929  CA  GLU B 340     -22.241  14.000  -9.010  1.00 25.75           C  
ANISOU 5929  CA  GLU B 340     3607   3042   3134    -53    -41   -355       C  
ATOM   5930  C   GLU B 340     -21.524  13.813 -10.346  1.00 24.80           C  
ANISOU 5930  C   GLU B 340     3447   2932   3045    -62    -63   -324       C  
ATOM   5931  O   GLU B 340     -20.386  14.266 -10.518  1.00 23.69           O  
ANISOU 5931  O   GLU B 340     3298   2794   2909    -81    -96   -323       O  
ATOM   5932  CB  GLU B 340     -22.113  12.728  -8.169  1.00 27.75           C  
ANISOU 5932  CB  GLU B 340     3880   3322   3341    -48    -38   -350       C  
ATOM   5933  CG  GLU B 340     -20.680  12.214  -8.048  1.00 28.38           C  
ANISOU 5933  CG  GLU B 340     3957   3424   3401    -59    -80   -338       C  
ATOM   5934  CD  GLU B 340     -20.601  10.820  -7.437  1.00 37.09           C  
ANISOU 5934  CD  GLU B 340     5079   4551   4464    -50    -79   -325       C  
ATOM   5935  OE1 GLU B 340     -21.669  10.200  -7.222  1.00 33.94           O  
ANISOU 5935  OE1 GLU B 340     4691   4151   4052    -38    -42   -322       O  
ATOM   5936  OE2 GLU B 340     -19.468  10.351  -7.164  1.00 34.28           O  
ANISOU 5936  OE2 GLU B 340     4724   4213   4087    -54   -115   -318       O  
ATOM   5937  N   LEU B 341     -22.195  13.135 -11.333  1.00 23.87           N  
ANISOU 5937  N   LEU B 341     3301   2822   2947    -50    -43   -300       N  
ATOM   5938  CA  LEU B 341     -21.519  12.733 -12.555  1.00 22.78           C  
ANISOU 5938  CA  LEU B 341     3126   2700   2830    -56    -60   -271       C  
ATOM   5939  C   LEU B 341     -21.495  13.866 -13.575  1.00 23.03           C  
ANISOU 5939  C   LEU B 341     3140   2710   2902    -67    -68   -266       C  
ATOM   5940  O   LEU B 341     -22.377  14.731 -13.579  1.00 23.61           O  
ANISOU 5940  O   LEU B 341     3223   2754   2994    -60    -53   -278       O  
ATOM   5941  CB  LEU B 341     -22.207  11.514 -13.168  1.00 20.87           C  
ANISOU 5941  CB  LEU B 341     2867   2475   2589    -41    -38   -250       C  
ATOM   5942  CG  LEU B 341     -22.319  10.297 -12.242  1.00 25.76           C  
ANISOU 5942  CG  LEU B 341     3507   3111   3168    -31    -29   -251       C  
ATOM   5943  CD1 LEU B 341     -22.703   9.066 -13.032  1.00 27.77           C  
ANISOU 5943  CD1 LEU B 341     3742   3383   3428    -21    -15   -226       C  
ATOM   5944  CD2 LEU B 341     -21.026  10.055 -11.474  1.00 26.61           C  
ANISOU 5944  CD2 LEU B 341     3630   3235   3245    -40    -62   -255       C  
ATOM   5945  N   PRO B 342     -20.481  13.878 -14.440  1.00 20.01           N  
ANISOU 5945  N   PRO B 342     2732   2340   2531    -84    -91   -247       N  
ATOM   5946  CA  PRO B 342     -20.494  14.810 -15.570  1.00 18.03           C  
ANISOU 5946  CA  PRO B 342     2465   2070   2317    -97    -96   -234       C  
ATOM   5947  C   PRO B 342     -21.687  14.533 -16.461  1.00 22.08           C  
ANISOU 5947  C   PRO B 342     2963   2576   2849    -77    -71   -219       C  
ATOM   5948  O   PRO B 342     -22.139  13.395 -16.583  1.00 22.45           O  
ANISOU 5948  O   PRO B 342     2999   2644   2886    -61    -56   -209       O  
ATOM   5949  CB  PRO B 342     -19.170  14.523 -16.295  1.00 19.77           C  
ANISOU 5949  CB  PRO B 342     2657   2318   2538   -119   -119   -216       C  
ATOM   5950  CG  PRO B 342     -18.785  13.144 -15.860  1.00 21.63           C  
ANISOU 5950  CG  PRO B 342     2885   2588   2745   -106   -121   -213       C  
ATOM   5951  CD  PRO B 342     -19.325  12.968 -14.469  1.00 18.54           C  
ANISOU 5951  CD  PRO B 342     2529   2189   2327    -91   -112   -236       C  
ATOM   5952  N   HIS B 343     -22.197  15.591 -17.075  1.00 21.67           N  
ANISOU 5952  N   HIS B 343     2913   2493   2827    -79    -71   -217       N  
ATOM   5953  CA  HIS B 343     -23.358  15.481 -17.949  1.00 26.24           C  
ANISOU 5953  CA  HIS B 343     3478   3063   3429    -59    -53   -203       C  
ATOM   5954  C   HIS B 343     -22.938  14.880 -19.286  1.00 26.04           C  
ANISOU 5954  C   HIS B 343     3422   3061   3411    -68    -60   -171       C  
ATOM   5955  O   HIS B 343     -21.938  15.313 -19.865  1.00 22.81           O  
ANISOU 5955  O   HIS B 343     3005   2654   3006    -93    -79   -159       O  
ATOM   5956  CB  HIS B 343     -23.991  16.855 -18.188  1.00 26.61           C  
ANISOU 5956  CB  HIS B 343     3538   3067   3505    -55    -56   -211       C  
ATOM   5957  CG  HIS B 343     -24.578  17.489 -16.962  1.00 33.59           C  
ANISOU 5957  CG  HIS B 343     4451   3925   4385    -41    -45   -246       C  
ATOM   5958  ND1 HIS B 343     -24.753  18.854 -16.847  1.00 35.23           N  
ANISOU 5958  ND1 HIS B 343     4680   4090   4614    -42    -55   -261       N  
ATOM   5959  CD2 HIS B 343     -25.053  16.950 -15.812  1.00 28.21           C  
ANISOU 5959  CD2 HIS B 343     3783   3256   3681    -26    -24   -270       C  
ATOM   5960  CE1 HIS B 343     -25.300  19.130 -15.674  1.00 32.76           C  
ANISOU 5960  CE1 HIS B 343     4392   3765   4292    -26    -40   -295       C  
ATOM   5961  NE2 HIS B 343     -25.496  17.993 -15.028  1.00 30.44           N  
ANISOU 5961  NE2 HIS B 343     4092   3504   3969    -18    -20   -301       N  
ATOM   5962  N   PRO B 344     -23.672  13.902 -19.809  1.00 25.71           N  
ANISOU 5962  N   PRO B 344     3363   3037   3370    -51    -43   -159       N  
ATOM   5963  CA  PRO B 344     -23.443  13.491 -21.196  1.00 25.74           C  
ANISOU 5963  CA  PRO B 344     3341   3056   3383    -58    -48   -131       C  
ATOM   5964  C   PRO B 344     -23.654  14.673 -22.129  1.00 27.58           C  
ANISOU 5964  C   PRO B 344     3575   3260   3643    -66    -59   -118       C  
ATOM   5965  O   PRO B 344     -24.576  15.473 -21.958  1.00 26.57           O  
ANISOU 5965  O   PRO B 344     3461   3101   3534    -52    -55   -128       O  
ATOM   5966  CB  PRO B 344     -24.489  12.393 -21.424  1.00 19.71           C  
ANISOU 5966  CB  PRO B 344     2564   2307   2617    -35    -28   -126       C  
ATOM   5967  CG  PRO B 344     -24.839  11.912 -20.048  1.00 24.93           C  
ANISOU 5967  CG  PRO B 344     3243   2971   3258    -23    -12   -149       C  
ATOM   5968  CD  PRO B 344     -24.753  13.129 -19.175  1.00 21.77           C  
ANISOU 5968  CD  PRO B 344     2867   2543   2862    -27    -18   -171       C  
ATOM   5969  N   LYS B 345     -22.776  14.795 -23.106  1.00 22.17           N  
ANISOU 5969  N   LYS B 345     2878   2587   2960    -89    -73    -96       N  
ATOM   5970  CA  LYS B 345     -22.859  15.893 -24.041  1.00 25.05           C  
ANISOU 5970  CA  LYS B 345     3248   2924   3345   -102    -85    -80       C  
ATOM   5971  C   LYS B 345     -22.697  15.360 -25.454  1.00 25.94           C  
ANISOU 5971  C   LYS B 345     3339   3059   3457   -110    -86    -51       C  
ATOM   5972  O   LYS B 345     -21.982  14.382 -25.688  1.00 23.10           O  
ANISOU 5972  O   LYS B 345     2960   2738   3080   -117    -82    -45       O  
ATOM   5973  CB  LYS B 345     -21.808  16.960 -23.710  1.00 29.82           C  
ANISOU 5973  CB  LYS B 345     3870   3511   3951   -133   -102    -85       C  
ATOM   5974  CG  LYS B 345     -22.260  17.807 -22.537  1.00 34.45           C  
ANISOU 5974  CG  LYS B 345     4484   4061   4544   -123   -104   -113       C  
ATOM   5975  CD  LYS B 345     -21.165  18.634 -21.934  1.00 31.86           C  
ANISOU 5975  CD  LYS B 345     4172   3721   4211   -154   -121   -125       C  
ATOM   5976  CE  LYS B 345     -21.687  19.290 -20.672  1.00 30.74           C  
ANISOU 5976  CE  LYS B 345     4061   3548   4072   -139   -119   -158       C  
ATOM   5977  NZ  LYS B 345     -22.860  20.179 -20.971  1.00 35.46           N  
ANISOU 5977  NZ  LYS B 345     4677   4100   4697   -117   -116   -160       N  
ATOM   5978  N   SER B 346     -23.416  15.979 -26.383  1.00 28.50           N  
ANISOU 5978  N   SER B 346     3669   3361   3800   -106    -91    -34       N  
ATOM   5979  CA  SER B 346     -23.250  15.633 -27.782  1.00 27.30           C  
ANISOU 5979  CA  SER B 346     3502   3228   3644   -117    -94     -5       C  
ATOM   5980  C   SER B 346     -21.861  16.033 -28.241  1.00 28.84           C  
ANISOU 5980  C   SER B 346     3695   3433   3828   -157   -103      8       C  
ATOM   5981  O   SER B 346     -21.184  16.847 -27.606  1.00 26.62           O  
ANISOU 5981  O   SER B 346     3427   3136   3550   -177   -111     -2       O  
ATOM   5982  CB  SER B 346     -24.278  16.345 -28.649  1.00 30.94           C  
ANISOU 5982  CB  SER B 346     3974   3658   4125   -105   -103     12       C  
ATOM   5983  OG  SER B 346     -24.001  17.730 -28.648  1.00 29.66           O  
ANISOU 5983  OG  SER B 346     3838   3455   3976   -122   -119     16       O  
ATOM   5984  N   MET B 347     -21.449  15.454 -29.373  1.00 26.21           N  
ANISOU 5984  N   MET B 347     3575   3783   2600   -753   -570    -27       N  
ATOM   5985  CA  MET B 347     -20.161  15.794 -29.968  1.00 30.93           C  
ANISOU 5985  CA  MET B 347     4241   4342   3170   -791   -513    -56       C  
ATOM   5986  C   MET B 347     -19.973  17.304 -30.059  1.00 25.63           C  
ANISOU 5986  C   MET B 347     3580   3650   2510   -770   -554    -41       C  
ATOM   5987  O   MET B 347     -18.951  17.832 -29.609  1.00 27.97           O  
ANISOU 5987  O   MET B 347     3867   3933   2829   -738   -507    -70       O  
ATOM   5988  CB  MET B 347     -20.035  15.147 -31.348  1.00 26.44           C  
ANISOU 5988  CB  MET B 347     3772   3747   2526   -895   -499    -54       C  
ATOM   5989  CG  MET B 347     -20.015  13.619 -31.315  1.00 30.43           C  
ANISOU 5989  CG  MET B 347     4281   4266   3015   -923   -442    -76       C  
ATOM   5990  SD  MET B 347     -20.291  12.893 -32.950  1.00 39.15           S  
ANISOU 5990  SD  MET B 347     5504   5344   4028  -1048   -449    -60       S  
ATOM   5991  CE  MET B 347     -21.946  13.527 -33.302  1.00 30.06           C  
ANISOU 5991  CE  MET B 347     4339   4215   2869  -1058   -580      5       C  
ATOM   5992  N   LEU B 348     -20.963  18.020 -30.612  1.00 25.71           N  
ANISOU 5992  N   LEU B 348     3607   3658   2504   -786   -641      7       N  
ATOM   5993  CA  LEU B 348     -20.787  19.456 -30.817  1.00 25.97           C  
ANISOU 5993  CA  LEU B 348     3661   3666   2540   -771   -678     23       C  
ATOM   5994  C   LEU B 348     -20.726  20.191 -29.486  1.00 26.60           C  
ANISOU 5994  C   LEU B 348     3658   3761   2689   -673   -679     17       C  
ATOM   5995  O   LEU B 348     -19.840  21.025 -29.272  1.00 25.24           O  
ANISOU 5995  O   LEU B 348     3494   3567   2528   -652   -651     -4       O  
ATOM   5996  CB  LEU B 348     -21.898  20.044 -31.692  1.00 23.39           C  
ANISOU 5996  CB  LEU B 348     3370   3336   2182   -807   -772     80       C  
ATOM   5997  CG  LEU B 348     -21.722  21.567 -31.886  1.00 24.43           C  
ANISOU 5997  CG  LEU B 348     3523   3440   2318   -789   -808     98       C  
ATOM   5998  CD1 LEU B 348     -20.353  21.909 -32.465  1.00 25.73           C  
ANISOU 5998  CD1 LEU B 348     3761   3564   2452   -831   -748     60       C  
ATOM   5999  CD2 LEU B 348     -22.800  22.171 -32.755  1.00 29.15           C  
ANISOU 5999  CD2 LEU B 348     4155   4034   2886   -822   -900    157       C  
ATOM   6000  N   GLN B 349     -21.652  19.887 -28.576  1.00 26.36           N  
ANISOU 6000  N   GLN B 349     3546   3768   2703   -613   -709     34       N  
ATOM   6001  CA  GLN B 349     -21.640  20.541 -27.272  1.00 25.61           C  
ANISOU 6001  CA  GLN B 349     3372   3685   2672   -519   -708     28       C  
ATOM   6002  C   GLN B 349     -20.319  20.302 -26.548  1.00 24.46           C  
ANISOU 6002  C   GLN B 349     3208   3536   2549   -494   -621    -27       C  
ATOM   6003  O   GLN B 349     -19.671  21.248 -26.090  1.00 23.10           O  
ANISOU 6003  O   GLN B 349     3028   3348   2400   -458   -607    -40       O  
ATOM   6004  CB  GLN B 349     -22.816  20.054 -26.425  1.00 27.17           C  
ANISOU 6004  CB  GLN B 349     3488   3923   2913   -464   -745     52       C  
ATOM   6005  CG  GLN B 349     -22.881  20.695 -25.046  1.00 30.09           C  
ANISOU 6005  CG  GLN B 349     3777   4305   3349   -366   -745     47       C  
ATOM   6006  CD  GLN B 349     -23.393  22.118 -25.115  1.00 35.82           C  
ANISOU 6006  CD  GLN B 349     4508   5015   4087   -336   -808     87       C  
ATOM   6007  OE1 GLN B 349     -24.018  22.512 -26.099  1.00 38.65           O  
ANISOU 6007  OE1 GLN B 349     4913   5362   4410   -380   -866    128       O  
ATOM   6008  NE2 GLN B 349     -23.130  22.898 -24.071  1.00 37.61           N  
ANISOU 6008  NE2 GLN B 349     4690   5239   4362   -263   -796     77       N  
ATOM   6009  N   ALA B 350     -19.894  19.040 -26.449  1.00 27.25           N  
ANISOU 6009  N   ALA B 350     3556   3903   2896   -514   -560    -58       N  
ATOM   6010  CA  ALA B 350     -18.680  18.734 -25.695  1.00 25.62           C  
ANISOU 6010  CA  ALA B 350     3323   3698   2715   -485   -477   -106       C  
ATOM   6011  C   ALA B 350     -17.449  19.353 -26.342  1.00 21.18           C  
ANISOU 6011  C   ALA B 350     2826   3098   2122   -527   -437   -128       C  
ATOM   6012  O   ALA B 350     -16.554  19.846 -25.647  1.00 22.76           O  
ANISOU 6012  O   ALA B 350     3000   3295   2351   -489   -397   -154       O  
ATOM   6013  CB  ALA B 350     -18.509  17.223 -25.562  1.00 25.61           C  
ANISOU 6013  CB  ALA B 350     3307   3717   2708   -502   -419   -132       C  
ATOM   6014  N   THR B 351     -17.381  19.344 -27.672  1.00 25.36           N  
ANISOU 6014  N   THR B 351     3442   3601   2593   -607   -446   -117       N  
ATOM   6015  CA  THR B 351     -16.217  19.922 -28.334  1.00 23.13           C  
ANISOU 6015  CA  THR B 351     3226   3282   2280   -649   -407   -137       C  
ATOM   6016  C   THR B 351     -16.210  21.435 -28.192  1.00 21.10           C  
ANISOU 6016  C   THR B 351     2971   3008   2038   -619   -452   -121       C  
ATOM   6017  O   THR B 351     -15.160  22.034 -27.938  1.00 19.95           O  
ANISOU 6017  O   THR B 351     2831   2847   1901   -608   -412   -146       O  
ATOM   6018  CB  THR B 351     -16.189  19.529 -29.809  1.00 24.73           C  
ANISOU 6018  CB  THR B 351     3525   3457   2414   -744   -407   -128       C  
ATOM   6019  OG1 THR B 351     -16.185  18.103 -29.915  1.00 25.39           O  
ANISOU 6019  OG1 THR B 351     3610   3554   2483   -772   -361   -144       O  
ATOM   6020  CG2 THR B 351     -14.938  20.081 -30.475  1.00 22.88           C  
ANISOU 6020  CG2 THR B 351     3359   3185   2151   -787   -361   -151       C  
ATOM   6021  N   ALA B 352     -17.378  22.063 -28.355  1.00 22.42           N  
ANISOU 6021  N   ALA B 352     3134   3178   2207   -606   -536    -78       N  
ATOM   6022  CA  ALA B 352     -17.497  23.501 -28.147  1.00 22.61           C  
ANISOU 6022  CA  ALA B 352     3157   3186   2247   -570   -580    -59       C  
ATOM   6023  C   ALA B 352     -17.084  23.887 -26.731  1.00 20.98           C  
ANISOU 6023  C   ALA B 352     2875   2995   2100   -488   -552    -81       C  
ATOM   6024  O   ALA B 352     -16.411  24.903 -26.522  1.00 19.63           O  
ANISOU 6024  O   ALA B 352     2717   2805   1938   -472   -542    -91       O  
ATOM   6025  CB  ALA B 352     -18.934  23.952 -28.432  1.00 20.90           C  
ANISOU 6025  CB  ALA B 352     2935   2976   2029   -561   -672     -4       C  
ATOM   6026  N   GLU B 353     -17.473  23.090 -25.742  1.00 19.76           N  
ANISOU 6026  N   GLU B 353     2645   2876   1987   -438   -539    -88       N  
ATOM   6027  CA  GLU B 353     -17.073  23.396 -24.374  1.00 22.43           C  
ANISOU 6027  CA  GLU B 353     2912   3229   2381   -363   -511   -110       C  
ATOM   6028  C   GLU B 353     -15.570  23.231 -24.194  1.00 19.29           C  
ANISOU 6028  C   GLU B 353     2526   2824   1981   -377   -430   -156       C  
ATOM   6029  O   GLU B 353     -14.906  24.108 -23.633  1.00 21.62           O  
ANISOU 6029  O   GLU B 353     2810   3109   2295   -347   -415   -169       O  
ATOM   6030  CB  GLU B 353     -17.852  22.520 -23.396  1.00 22.41           C  
ANISOU 6030  CB  GLU B 353     2827   3266   2420   -308   -515   -107       C  
ATOM   6031  CG  GLU B 353     -19.317  22.926 -23.314  1.00 25.02           C  
ANISOU 6031  CG  GLU B 353     3133   3606   2767   -276   -597    -59       C  
ATOM   6032  CD  GLU B 353     -20.106  22.094 -22.324  1.00 29.69           C  
ANISOU 6032  CD  GLU B 353     3643   4237   3402   -221   -601    -55       C  
ATOM   6033  OE1 GLU B 353     -19.483  21.419 -21.478  1.00 31.50           O  
ANISOU 6033  OE1 GLU B 353     3827   4484   3659   -192   -543    -92       O  
ATOM   6034  OE2 GLU B 353     -21.350  22.111 -22.405  1.00 30.63           O  
ANISOU 6034  OE2 GLU B 353     3741   4368   3528   -206   -664    -15       O  
ATOM   6035  N   ALA B 354     -15.011  22.119 -24.675  1.00 20.54           N  
ANISOU 6035  N   ALA B 354     2706   2985   2113   -425   -375   -179       N  
ATOM   6036  CA  ALA B 354     -13.567  21.940 -24.587  1.00 19.91           C  
ANISOU 6036  CA  ALA B 354     2637   2898   2029   -441   -296   -218       C  
ATOM   6037  C   ALA B 354     -12.834  23.061 -25.315  1.00 20.33           C  
ANISOU 6037  C   ALA B 354     2758   2914   2053   -480   -298   -219       C  
ATOM   6038  O   ALA B 354     -11.842  23.590 -24.802  1.00 19.86           O  
ANISOU 6038  O   ALA B 354     2686   2850   2010   -462   -259   -242       O  
ATOM   6039  CB  ALA B 354     -13.162  20.578 -25.149  1.00 21.68           C  
ANISOU 6039  CB  ALA B 354     2886   3126   2226   -491   -237   -236       C  
ATOM   6040  N   ASN B 355     -13.305  23.439 -26.514  1.00 20.18           N  
ANISOU 6040  N   ASN B 355     2812   2867   1987   -535   -343   -193       N  
ATOM   6041  CA  ASN B 355     -12.652  24.528 -27.243  1.00 19.54           C  
ANISOU 6041  CA  ASN B 355     2800   2749   1876   -573   -347   -193       C  
ATOM   6042  C   ASN B 355     -12.690  25.818 -26.437  1.00 23.55           C  
ANISOU 6042  C   ASN B 355     3277   3254   2417   -515   -378   -186       C  
ATOM   6043  O   ASN B 355     -11.691  26.552 -26.360  1.00 21.27           O  
ANISOU 6043  O   ASN B 355     3007   2947   2126   -521   -348   -206       O  
ATOM   6044  CB  ASN B 355     -13.320  24.767 -28.600  1.00 19.61           C  
ANISOU 6044  CB  ASN B 355     2888   2731   1832   -635   -401   -162       C  
ATOM   6045  CG  ASN B 355     -13.162  23.613 -29.572  1.00 21.69           C  
ANISOU 6045  CG  ASN B 355     3202   2989   2051   -706   -367   -170       C  
ATOM   6046  OD1 ASN B 355     -13.875  23.560 -30.572  1.00 22.36           O  
ANISOU 6046  OD1 ASN B 355     3341   3059   2094   -755   -413   -142       O  
ATOM   6047  ND2 ASN B 355     -12.249  22.689 -29.291  1.00 18.89           N  
ANISOU 6047  ND2 ASN B 355     2831   2643   1702   -711   -287   -205       N  
ATOM   6048  N   ASN B 356     -13.843  26.117 -25.834  1.00 20.64           N  
ANISOU 6048  N   ASN B 356     2862   2901   2079   -461   -438   -158       N  
ATOM   6049  CA  ASN B 356     -13.963  27.352 -25.071  1.00 22.96           C  
ANISOU 6049  CA  ASN B 356     3131   3189   2404   -405   -467   -148       C  
ATOM   6050  C   ASN B 356     -13.165  27.292 -23.780  1.00 20.79           C  
ANISOU 6050  C   ASN B 356     2792   2934   2173   -354   -414   -182       C  
ATOM   6051  O   ASN B 356     -12.493  28.266 -23.424  1.00 20.81           O  
ANISOU 6051  O   ASN B 356     2804   2921   2182   -340   -403   -193       O  
ATOM   6052  CB  ASN B 356     -15.428  27.660 -24.792  1.00 21.21           C  
ANISOU 6052  CB  ASN B 356     2877   2977   2203   -360   -542   -106       C  
ATOM   6053  CG  ASN B 356     -16.084  28.409 -25.942  1.00 22.53           C  
ANISOU 6053  CG  ASN B 356     3113   3117   2331   -399   -604    -67       C  
ATOM   6054  OD1 ASN B 356     -16.089  29.641 -25.975  1.00 21.48           O  
ANISOU 6054  OD1 ASN B 356     3006   2959   2197   -385   -632    -52       O  
ATOM   6055  ND2 ASN B 356     -16.609  27.665 -26.907  1.00 23.67           N  
ANISOU 6055  ND2 ASN B 356     3291   3263   2440   -452   -625    -49       N  
ATOM   6056  N   LEU B 357     -13.219  26.162 -23.067  1.00 18.98           N  
ANISOU 6056  N   LEU B 357     2501   2739   1973   -327   -382   -198       N  
ATOM   6057  CA  LEU B 357     -12.421  26.034 -21.850  1.00 18.84           C  
ANISOU 6057  CA  LEU B 357     2421   2741   1995   -281   -330   -229       C  
ATOM   6058  C   LEU B 357     -10.945  26.245 -22.147  1.00 22.25           C  
ANISOU 6058  C   LEU B 357     2889   3158   2406   -323   -270   -260       C  
ATOM   6059  O   LEU B 357     -10.253  26.977 -21.420  1.00 20.39           O  
ANISOU 6059  O   LEU B 357     2634   2921   2191   -297   -251   -274       O  
ATOM   6060  CB  LEU B 357     -12.658  24.672 -21.201  1.00 18.49           C  
ANISOU 6060  CB  LEU B 357     2313   2735   1979   -255   -300   -241       C  
ATOM   6061  CG  LEU B 357     -14.022  24.553 -20.504  1.00 21.26           C  
ANISOU 6061  CG  LEU B 357     2607   3107   2365   -196   -354   -215       C  
ATOM   6062  CD1 LEU B 357     -14.365  23.096 -20.172  1.00 20.61           C  
ANISOU 6062  CD1 LEU B 357     2476   3057   2297   -185   -328   -225       C  
ATOM   6063  CD2 LEU B 357     -14.085  25.416 -19.253  1.00 20.31           C  
ANISOU 6063  CD2 LEU B 357     2435   2991   2290   -125   -366   -216       C  
ATOM   6064  N   ALA B 358     -10.446  25.635 -23.227  1.00 18.87           N  
ANISOU 6064  N   ALA B 358     2516   2718   1937   -389   -238   -268       N  
ATOM   6065  CA  ALA B 358      -9.030  25.784 -23.548  1.00 17.71           C  
ANISOU 6065  CA  ALA B 358     2402   2557   1771   -429   -176