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***  20201123_FL  ***

elNémo ID: 201123154705108902

Job options:

ID        	=	 201123154705108902
JOBID     	=	 20201123_FL
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 20201123_FL

HEADER    BIOSYNTHETIC PROTEIN                    13-JUN-18   6GS2              
TITLE     CRYSTAL STRUCTURE OF THE GATD/MURT ENZYME COMPLEX FROM STAPHYLOCOCCUS 
TITLE    2 AUREUS                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SA1707 PROTEIN;                                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: GATD;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SA1708 PROTEIN;                                            
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 SYNONYM: MURT;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 158879;                                              
SOURCE   4 STRAIN: N315;                                                        
SOURCE   5 GENE: SA1707;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN N315);            
SOURCE  10 ORGANISM_TAXID: 158879;                                              
SOURCE  11 STRAIN: N315;                                                        
SOURCE  12 GENE: SA1708;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    CELL WALL BIOSYNTHESIS, PEPTIDOGLYCAN, ANTIBIOTIC RESISTANCE,         
KEYWDS   2 BIOSYNTHETIC PROTEIN                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.M.MUCKENFUSS,E.R.NOELDEKE,V.NIEMANN,G.ZOCHER,T.STEHLE               
REVDAT   2   12-SEP-18 6GS2    1       JRNL                                     
REVDAT   1   05-SEP-18 6GS2    0                                                
JRNL        AUTH   E.R.NOLDEKE,L.M.MUCKENFUSS,V.NIEMANN,A.MULLER,E.STORK,       
JRNL        AUTH 2 G.ZOCHER,T.SCHNEIDER,T.STEHLE                                
JRNL        TITL   STRUCTURAL BASIS OF CELL WALL PEPTIDOGLYCAN AMIDATION BY THE 
JRNL        TITL 2 GATD/MURT COMPLEX OF STAPHYLOCOCCUS AUREUS.                  
JRNL        REF    SCI REP                       V.   8 12953 2018              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   30154570                                                     
JRNL        DOI    10.1038/S41598-018-31098-X                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 87852                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1503                            
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 49.0699 -  4.5358    1.00     8245   140  0.1599 0.1794        
REMARK   3     2  4.5358 -  3.6005    1.00     7987   134  0.1261 0.1559        
REMARK   3     3  3.6005 -  3.1455    1.00     7900   140  0.1499 0.2083        
REMARK   3     4  3.1455 -  2.8579    1.00     7916   136  0.1694 0.2271        
REMARK   3     5  2.8579 -  2.6531    1.00     7841   137  0.1730 0.2035        
REMARK   3     6  2.6531 -  2.4967    1.00     7828   149  0.1769 0.2598        
REMARK   3     7  2.4967 -  2.3717    1.00     7854   118  0.1856 0.2170        
REMARK   3     8  2.3717 -  2.2684    1.00     7750   146  0.2036 0.2568        
REMARK   3     9  2.2684 -  2.1811    0.97     7632   135  0.3202 0.3792        
REMARK   3    10  2.1811 -  2.1058    1.00     7780   134  0.2579 0.2961        
REMARK   3    11  2.1058 -  2.0400    0.98     7616   134  0.4376 0.4538        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011          10097                                  
REMARK   3   ANGLE     :  1.327          13668                                  
REMARK   3   CHIRALITY :  0.064           1541                                  
REMARK   3   PLANARITY :  0.006           1778                                  
REMARK   3   DIHEDRAL  : 18.109           3665                                  
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 6GS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010448.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION MAY 1, 2016            
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION MAY 1, 2016         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88009                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.6, 40% (W/V) PEG        
REMARK 280  8000, 350 MM MAGNESIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 277K                                                    
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       53.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.18000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.18000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.18500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     HIS A   247                                                      
REMARK 465     HIS A   248                                                      
REMARK 465     HIS A   249                                                      
REMARK 465     HIS A   250                                                      
REMARK 465     HIS A   251                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     TRP B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     THR B    25                                                      
REMARK 465     ASP B    26                                                      
REMARK 465     LEU B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     GLN B    30                                                      
REMARK 465     ILE B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     VAL B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     GLN B   135                                                      
REMARK 465     MET B   136                                                      
REMARK 465     ASP B   137                                                      
REMARK 465     ARG B   138                                                      
REMARK 465     PHE B   139                                                      
REMARK 465     THR B   195                                                      
REMARK 465     MET B   196                                                      
REMARK 465     GLY B   434                                                      
REMARK 465     GLY B   435                                                      
REMARK 465     GLN B   436                                                      
REMARK 465     SER B   437                                                      
REMARK 465     LEU C   244                                                      
REMARK 465     GLU C   245                                                      
REMARK 465     HIS C   246                                                      
REMARK 465     HIS C   247                                                      
REMARK 465     HIS C   248                                                      
REMARK 465     HIS C   249                                                      
REMARK 465     HIS C   250                                                      
REMARK 465     HIS C   251                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     TRP D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     ILE D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     LEU D    12                                                      
REMARK 465     ALA D    13                                                      
REMARK 465     ARG D    14                                                      
REMARK 465     LYS D    15                                                      
REMARK 465     ALA D    16                                                      
REMARK 465     SER D    17                                                      
REMARK 465     ARG D    18                                                      
REMARK 465     ALA D    19                                                      
REMARK 465     VAL D    20                                                      
REMARK 465     GLY D    21                                                      
REMARK 465     LYS D    22                                                      
REMARK 465     ARG D    23                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     THR D    25                                                      
REMARK 465     ASP D    26                                                      
REMARK 465     LEU D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     GLN D    30                                                      
REMARK 465     ILE D    31                                                      
REMARK 465     ALA D    32                                                      
REMARK 465     ARG D    33                                                      
REMARK 465     LYS D    34                                                      
REMARK 465     VAL D    35                                                      
REMARK 465     ASP D    36                                                      
REMARK 465     THR D    37                                                      
REMARK 465     ARG D   133                                                      
REMARK 465     ASP D   134                                                      
REMARK 465     GLN D   135                                                      
REMARK 465     MET D   136                                                      
REMARK 465     ASP D   137                                                      
REMARK 465     GLN D   193                                                      
REMARK 465     SER D   194                                                      
REMARK 465     THR D   195                                                      
REMARK 465     MET D   196                                                      
REMARK 465     ASN D   197                                                      
REMARK 465     GLU D   198                                                      
REMARK 465     SER D   199                                                      
REMARK 465     GLY D   434                                                      
REMARK 465     GLY D   435                                                      
REMARK 465     GLN D   436                                                      
REMARK 465     SER D   437                                                      
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  16    CG   CD1  CD2                                       
REMARK 470     LYS A  36    CE   NZ                                             
REMARK 470     GLU A  46    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  71    CD   CE   NZ                                        
REMARK 470     LYS A 102    CD   CE   NZ                                        
REMARK 470     LYS A 103    NZ                                                  
REMARK 470     ASP A 108    CG   OD1  OD2                                       
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 125    CE   NZ                                             
REMARK 470     LYS A 241    CG   CD   CE   NZ                                   
REMARK 470     SER A 242    OG                                                  
REMARK 470     ARG A 243    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A 244    CG   CD1  CD2                                       
REMARK 470     GLU A 245    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 246    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B  38    CG   OD1  OD2                                       
REMARK 470     ARG B  41    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     GLN B  46    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  76    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 101    CG   CD   CE   NZ                                   
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     ARG B 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 119    CE   NZ                                             
REMARK 470     ARG B 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 134    CG   OD1  OD2                                       
REMARK 470     GLU B 141    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 190    CD   OE1  OE2                                       
REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
REMARK 470     SER B 194    OG                                                  
REMARK 470     ASN B 197    CG   OD1  ND2                                       
REMARK 470     GLU B 198    CG   CD   OE1  OE2                                  
REMARK 470     SER B 199    OG                                                  
REMARK 470     ARG B 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 298    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 305    CD   OE1  OE2                                       
REMARK 470     ARG B 306    NE   CZ   NH1  NH2                                  
REMARK 470     SER B 325    OG                                                  
REMARK 470     GLU B 331    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 355    CG   OD1  OD2                                       
REMARK 470     LYS B 404    CE   NZ                                             
REMARK 470     LYS B 409    CE   NZ                                             
REMARK 470     GLU B 433    CD   OE1  OE2                                       
REMARK 470     GLU C  44    CD   OE1  OE2                                       
REMARK 470     GLU C  52    CD   OE1  OE2                                       
REMARK 470     ARG C  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C  68    CG   CD1  CD2                                       
REMARK 470     LYS C  71    NZ                                                  
REMARK 470     GLU C  82    CD   OE1  OE2                                       
REMARK 470     LYS C 102    CD   CE   NZ                                        
REMARK 470     LYS C 103    CE   NZ                                             
REMARK 470     GLU C 113    CD   OE1  OE2                                       
REMARK 470     LYS C 125    CE   NZ                                             
REMARK 470     LYS C 218    CD   CE   NZ                                        
REMARK 470     GLU C 223    CD   OE1  OE2                                       
REMARK 470     GLN C 239    CD   OE1  NE2                                       
REMARK 470     LYS C 241    CG   CD   CE   NZ                                   
REMARK 470     SER C 242    OG                                                  
REMARK 470     ARG C 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D  38    CG   OD1  OD2                                       
REMARK 470     VAL D  39    CG1  CG2                                            
REMARK 470     ARG D  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  42    CG   CD   CE   NZ                                   
REMARK 470     GLU D  45    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  46    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 101    NZ                                                  
REMARK 470     LYS D 103    NZ                                                  
REMARK 470     LYS D 119    CD   CE   NZ                                        
REMARK 470     GLU D 120    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 141    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 151    CD   OE1  OE2                                       
REMARK 470     LYS D 185    NZ                                                  
REMARK 470     GLU D 190    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 192    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 210    CD   OE1  NE2                                       
REMARK 470     GLN D 225    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 232    CD   OE1  NE2                                       
REMARK 470     GLU D 253    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 304    CE   NZ                                             
REMARK 470     GLU D 305    CD   OE1  OE2                                       
REMARK 470     ARG D 306    NE   CZ   NH1  NH2                                  
REMARK 470     GLU D 328    CD   OE1  OE2                                       
REMARK 470     ARG D 348    CZ   NH1  NH2                                       
REMARK 470     GLU D 389    CD   OE1  OE2                                       
REMARK 470     LYS D 404    CD   CE   NZ                                        
REMARK 470     LYS D 409    CD   CE   NZ                                        
REMARK 470     GLU D 433    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  16       40.89   -148.37                                   
REMARK 500    CYS A  94     -113.66     48.18                                   
REMARK 500    ASN A 148       81.46   -165.16                                   
REMARK 500    LYS A 181     -115.72     50.61                                   
REMARK 500    ASN A 196       69.29   -104.39                                   
REMARK 500    GLU A 245       32.37    -80.23                                   
REMARK 500    ALA B  84       43.19   -149.36                                   
REMARK 500    GLN B 193      140.30     80.72                                   
REMARK 500    ASN B 217     -124.92     50.67                                   
REMARK 500    ALA B 243       69.11   -158.16                                   
REMARK 500    GLU B 305     -122.70     59.25                                   
REMARK 500    SER C  62     -178.51    -65.16                                   
REMARK 500    CYS C  94     -114.90     45.67                                   
REMARK 500    ASN C 148       74.27   -162.82                                   
REMARK 500    LYS C 181     -114.53     50.30                                   
REMARK 500    PRO C 191      177.63    -59.47                                   
REMARK 500    VAL D  39      -71.38    -68.89                                   
REMARK 500    ASN D  80     -158.27    -98.15                                   
REMARK 500    ASN D  80     -156.30    -98.15                                   
REMARK 500    ALA D  84       46.84   -143.50                                   
REMARK 500    LEU D 172       -3.03    -59.86                                   
REMARK 500    ASN D 217     -128.04     56.99                                   
REMARK 500    GLU D 305     -122.97     57.94                                   
REMARK 500    GLU D 389       73.22   -100.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 202   SG                                                     
REMARK 620 2 CYS B 205   SG  110.9                                              
REMARK 620 3 CYS B 224   SG  114.4  97.0                                        
REMARK 620 4 CYS B 226   SG  110.9 116.6 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 262   OD2                                                    
REMARK 620 2 HOH B 634   O   101.9                                              
REMARK 620 3 HOH B 689   O    85.5  83.4                                        
REMARK 620 4 HOH B 610   O    93.8 159.0  84.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 202   SG                                                     
REMARK 620 2 CYS D 205   SG  117.4                                              
REMARK 620 3 CYS D 224   SG  113.7  98.8                                        
REMARK 620 4 CYS D 226   SG  108.1 112.8 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 144 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501                  
DBREF1 6GS2 A    1   243  UNP                  A0A0H3JN63_STAAN                 
DBREF2 6GS2 A     A0A0H3JN63                          1         243             
DBREF1 6GS2 B    1   437  UNP                  A0A0H3JUU7_STAAN                 
DBREF2 6GS2 B     A0A0H3JUU7                          1         437             
DBREF1 6GS2 C    1   243  UNP                  A0A0H3JN63_STAAN                 
DBREF2 6GS2 C     A0A0H3JN63                          1         243             
DBREF1 6GS2 D    1   437  UNP                  A0A0H3JUU7_STAAN                 
DBREF2 6GS2 D     A0A0H3JUU7                          1         437             
SEQADV 6GS2 LEU A  244  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 GLU A  245  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS A  246  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS A  247  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS A  248  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS A  249  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS A  250  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS A  251  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 LEU C  244  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 GLU C  245  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS C  246  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS C  247  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS C  248  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS C  249  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS C  250  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQADV 6GS2 HIS C  251  UNP  A0A0H3JN6           EXPRESSION TAG                 
SEQRES   1 A  251  MET HIS GLU LEU THR ILE TYR HIS PHE MET SER ASP LYS          
SEQRES   2 A  251  LEU ASN LEU TYR SER ASP ILE GLY ASN ILE ILE ALA LEU          
SEQRES   3 A  251  ARG GLN ARG ALA LYS LYS ARG ASN ILE LYS VAL ASN VAL          
SEQRES   4 A  251  VAL GLU ILE ASN GLU THR GLU GLY ILE THR PHE ASP GLU          
SEQRES   5 A  251  CYS ASP ILE PHE PHE ILE GLY GLY GLY SER ASP ARG GLU          
SEQRES   6 A  251  GLN ALA LEU ALA THR LYS GLU LEU SER LYS ILE LYS THR          
SEQRES   7 A  251  PRO LEU LYS GLU ALA ILE GLU ASP GLY MET PRO GLY LEU          
SEQRES   8 A  251  THR ILE CYS GLY GLY TYR GLN PHE LEU GLY LYS LYS TYR          
SEQRES   9 A  251  ILE THR PRO ASP GLY THR GLU LEU GLU GLY LEU GLY ILE          
SEQRES  10 A  251  LEU ASP PHE TYR THR GLU SER LYS THR ASN ARG LEU THR          
SEQRES  11 A  251  GLY ASP ILE VAL ILE GLU SER ASP THR PHE GLY THR ILE          
SEQRES  12 A  251  VAL GLY PHE GLU ASN HIS GLY GLY ARG THR TYR HIS ASP          
SEQRES  13 A  251  PHE GLY THR LEU GLY HIS VAL THR PHE GLY TYR GLY ASN          
SEQRES  14 A  251  ASN ASP GLU ASP LYS LYS GLU GLY ILE HIS TYR LYS ASN          
SEQRES  15 A  251  LEU LEU GLY THR TYR LEU HIS GLY PRO ILE LEU PRO LYS          
SEQRES  16 A  251  ASN TYR GLU ILE THR ASP TYR LEU LEU GLU LYS ALA CYS          
SEQRES  17 A  251  GLU ARG LYS GLY ILE PRO PHE GLU PRO LYS GLU ILE ASP          
SEQRES  18 A  251  ASN GLU ALA GLU ILE GLN ALA LYS GLN VAL LEU ILE ASP          
SEQRES  19 A  251  ARG ALA ASN ARG GLN LYS LYS SER ARG LEU GLU HIS HIS          
SEQRES  20 A  251  HIS HIS HIS HIS                                              
SEQRES   1 B  437  MET ARG GLN TRP THR ALA ILE HIS LEU ALA LYS LEU ALA          
SEQRES   2 B  437  ARG LYS ALA SER ARG ALA VAL GLY LYS ARG GLY THR ASP          
SEQRES   3 B  437  LEU PRO GLY GLN ILE ALA ARG LYS VAL ASP THR ASP VAL          
SEQRES   4 B  437  LEU ARG LYS LEU ALA GLU GLN VAL ASP ASP ILE VAL PHE          
SEQRES   5 B  437  ILE SER GLY THR ASN GLY LYS THR THR THR SER ASN LEU          
SEQRES   6 B  437  ILE GLY HIS THR LEU LYS ALA ASN ASN ILE GLN ILE ILE          
SEQRES   7 B  437  HIS ASN ASN GLU GLY ALA ASN MET ALA ALA GLY ILE THR          
SEQRES   8 B  437  SER ALA PHE ILE MET GLN SER THR PRO LYS THR LYS ILE          
SEQRES   9 B  437  ALA VAL ILE GLU ILE ASP GLU GLY SER ILE PRO ARG VAL          
SEQRES  10 B  437  LEU LYS GLU VAL THR PRO SER MET MET VAL PHE THR ASN          
SEQRES  11 B  437  PHE PHE ARG ASP GLN MET ASP ARG PHE GLY GLU ILE ASP          
SEQRES  12 B  437  ILE MET VAL ASN ASN ILE ALA GLU THR ILE SER ASN LYS          
SEQRES  13 B  437  GLY ILE LYS LEU LEU LEU ASN ALA ASP ASP PRO PHE VAL          
SEQRES  14 B  437  SER ARG LEU LYS ILE ALA SER ASP THR ILE VAL TYR TYR          
SEQRES  15 B  437  GLY MET LYS ALA HIS ALA HIS GLU PHE GLU GLN SER THR          
SEQRES  16 B  437  MET ASN GLU SER ARG TYR CYS PRO ASN CYS GLY ARG LEU          
SEQRES  17 B  437  LEU GLN TYR ASP TYR ILE HIS TYR ASN GLN ILE GLY HIS          
SEQRES  18 B  437  TYR HIS CYS GLN CYS GLY PHE LYS ARG GLU GLN ALA LYS          
SEQRES  19 B  437  TYR GLU ILE SER SER PHE ASP VAL ALA PRO PHE LEU TYR          
SEQRES  20 B  437  LEU ASN ILE ASN ASP GLU LYS TYR ASP MET LYS ILE ALA          
SEQRES  21 B  437  GLY ASP PHE ASN ALA TYR ASN ALA LEU ALA ALA TYR THR          
SEQRES  22 B  437  VAL LEU ARG GLU LEU GLY LEU ASN GLU GLN THR ILE LYS          
SEQRES  23 B  437  ASN GLY PHE GLU THR TYR THR SER ASP ASN GLY ARG MET          
SEQRES  24 B  437  GLN TYR PHE LYS LYS GLU ARG LYS GLU ALA MET ILE ASN          
SEQRES  25 B  437  LEU ALA LYS ASN PRO ALA GLY MET ASN ALA SER LEU SER          
SEQRES  26 B  437  VAL GLY GLU GLN LEU GLU GLY GLU LYS VAL TYR VAL ILE          
SEQRES  27 B  437  SER LEU ASN ASP ASN ALA ALA ASP GLY ARG ASP THR SER          
SEQRES  28 B  437  TRP ILE TYR ASP ALA ASP PHE GLU LYS LEU SER LYS GLN          
SEQRES  29 B  437  GLN ILE GLU ALA ILE ILE VAL THR GLY THR ARG ALA GLU          
SEQRES  30 B  437  GLU LEU GLN LEU ARG LEU LYS LEU ALA GLU VAL GLU VAL          
SEQRES  31 B  437  PRO ILE ILE VAL GLU ARG ASP ILE TYR LYS ALA THR ALA          
SEQRES  32 B  437  LYS THR MET ASP TYR LYS GLY PHE THR VAL ALA ILE PRO          
SEQRES  33 B  437  ASN TYR THR SER LEU ALA PRO MET LEU GLU GLN LEU ASN          
SEQRES  34 B  437  ARG SER PHE GLU GLY GLY GLN SER                              
SEQRES   1 C  251  MET HIS GLU LEU THR ILE TYR HIS PHE MET SER ASP LYS          
SEQRES   2 C  251  LEU ASN LEU TYR SER ASP ILE GLY ASN ILE ILE ALA LEU          
SEQRES   3 C  251  ARG GLN ARG ALA LYS LYS ARG ASN ILE LYS VAL ASN VAL          
SEQRES   4 C  251  VAL GLU ILE ASN GLU THR GLU GLY ILE THR PHE ASP GLU          
SEQRES   5 C  251  CYS ASP ILE PHE PHE ILE GLY GLY GLY SER ASP ARG GLU          
SEQRES   6 C  251  GLN ALA LEU ALA THR LYS GLU LEU SER LYS ILE LYS THR          
SEQRES   7 C  251  PRO LEU LYS GLU ALA ILE GLU ASP GLY MET PRO GLY LEU          
SEQRES   8 C  251  THR ILE CYS GLY GLY TYR GLN PHE LEU GLY LYS LYS TYR          
SEQRES   9 C  251  ILE THR PRO ASP GLY THR GLU LEU GLU GLY LEU GLY ILE          
SEQRES  10 C  251  LEU ASP PHE TYR THR GLU SER LYS THR ASN ARG LEU THR          
SEQRES  11 C  251  GLY ASP ILE VAL ILE GLU SER ASP THR PHE GLY THR ILE          
SEQRES  12 C  251  VAL GLY PHE GLU ASN HIS GLY GLY ARG THR TYR HIS ASP          
SEQRES  13 C  251  PHE GLY THR LEU GLY HIS VAL THR PHE GLY TYR GLY ASN          
SEQRES  14 C  251  ASN ASP GLU ASP LYS LYS GLU GLY ILE HIS TYR LYS ASN          
SEQRES  15 C  251  LEU LEU GLY THR TYR LEU HIS GLY PRO ILE LEU PRO LYS          
SEQRES  16 C  251  ASN TYR GLU ILE THR ASP TYR LEU LEU GLU LYS ALA CYS          
SEQRES  17 C  251  GLU ARG LYS GLY ILE PRO PHE GLU PRO LYS GLU ILE ASP          
SEQRES  18 C  251  ASN GLU ALA GLU ILE GLN ALA LYS GLN VAL LEU ILE ASP          
SEQRES  19 C  251  ARG ALA ASN ARG GLN LYS LYS SER ARG LEU GLU HIS HIS          
SEQRES  20 C  251  HIS HIS HIS HIS                                              
SEQRES   1 D  437  MET ARG GLN TRP THR ALA ILE HIS LEU ALA LYS LEU ALA          
SEQRES   2 D  437  ARG LYS ALA SER ARG ALA VAL GLY LYS ARG GLY THR ASP          
SEQRES   3 D  437  LEU PRO GLY GLN ILE ALA ARG LYS VAL ASP THR ASP VAL          
SEQRES   4 D  437  LEU ARG LYS LEU ALA GLU GLN VAL ASP ASP ILE VAL PHE          
SEQRES   5 D  437  ILE SER GLY THR ASN GLY LYS THR THR THR SER ASN LEU          
SEQRES   6 D  437  ILE GLY HIS THR LEU LYS ALA ASN ASN ILE GLN ILE ILE          
SEQRES   7 D  437  HIS ASN ASN GLU GLY ALA ASN MET ALA ALA GLY ILE THR          
SEQRES   8 D  437  SER ALA PHE ILE MET GLN SER THR PRO LYS THR LYS ILE          
SEQRES   9 D  437  ALA VAL ILE GLU ILE ASP GLU GLY SER ILE PRO ARG VAL          
SEQRES  10 D  437  LEU LYS GLU VAL THR PRO SER MET MET VAL PHE THR ASN          
SEQRES  11 D  437  PHE PHE ARG ASP GLN MET ASP ARG PHE GLY GLU ILE ASP          
SEQRES  12 D  437  ILE MET VAL ASN ASN ILE ALA GLU THR ILE SER ASN LYS          
SEQRES  13 D  437  GLY ILE LYS LEU LEU LEU ASN ALA ASP ASP PRO PHE VAL          
SEQRES  14 D  437  SER ARG LEU LYS ILE ALA SER ASP THR ILE VAL TYR TYR          
SEQRES  15 D  437  GLY MET LYS ALA HIS ALA HIS GLU PHE GLU GLN SER THR          
SEQRES  16 D  437  MET ASN GLU SER ARG TYR CYS PRO ASN CYS GLY ARG LEU          
SEQRES  17 D  437  LEU GLN TYR ASP TYR ILE HIS TYR ASN GLN ILE GLY HIS          
SEQRES  18 D  437  TYR HIS CYS GLN CYS GLY PHE LYS ARG GLU GLN ALA LYS          
SEQRES  19 D  437  TYR GLU ILE SER SER PHE ASP VAL ALA PRO PHE LEU TYR          
SEQRES  20 D  437  LEU ASN ILE ASN ASP GLU LYS TYR ASP MET LYS ILE ALA          
SEQRES  21 D  437  GLY ASP PHE ASN ALA TYR ASN ALA LEU ALA ALA TYR THR          
SEQRES  22 D  437  VAL LEU ARG GLU LEU GLY LEU ASN GLU GLN THR ILE LYS          
SEQRES  23 D  437  ASN GLY PHE GLU THR TYR THR SER ASP ASN GLY ARG MET          
SEQRES  24 D  437  GLN TYR PHE LYS LYS GLU ARG LYS GLU ALA MET ILE ASN          
SEQRES  25 D  437  LEU ALA LYS ASN PRO ALA GLY MET ASN ALA SER LEU SER          
SEQRES  26 D  437  VAL GLY GLU GLN LEU GLU GLY GLU LYS VAL TYR VAL ILE          
SEQRES  27 D  437  SER LEU ASN ASP ASN ALA ALA ASP GLY ARG ASP THR SER          
SEQRES  28 D  437  TRP ILE TYR ASP ALA ASP PHE GLU LYS LEU SER LYS GLN          
SEQRES  29 D  437  GLN ILE GLU ALA ILE ILE VAL THR GLY THR ARG ALA GLU          
SEQRES  30 D  437  GLU LEU GLN LEU ARG LEU LYS LEU ALA GLU VAL GLU VAL          
SEQRES  31 D  437  PRO ILE ILE VAL GLU ARG ASP ILE TYR LYS ALA THR ALA          
SEQRES  32 D  437  LYS THR MET ASP TYR LYS GLY PHE THR VAL ALA ILE PRO          
SEQRES  33 D  437  ASN TYR THR SER LEU ALA PRO MET LEU GLU GLN LEU ASN          
SEQRES  34 D  437  ARG SER PHE GLU GLY GLY GLN SER                              
HET    144  A 301      16                                                       
HET    PEG  A 302       7                                                       
HET     ZN  B 501       1                                                       
HET     MG  B 502       1                                                       
HET     ZN  D 501       1                                                       
HETNAM     144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM                               
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5  144    C4 H12 N O3 1+                                               
FORMUL   6  PEG    C4 H10 O3                                                    
FORMUL   7   ZN    2(ZN 2+)                                                     
FORMUL   8   MG    MG 2+                                                        
FORMUL  10  HOH   *613(H2 O)                                                    
HELIX    1 AA1 LEU A   16  LYS A   32  1                                  17    
HELIX    2 AA2 SER A   62  SER A   74  1                                  13    
HELIX    3 AA3 ILE A   76  ASP A   86  1                                  11    
HELIX    4 AA4 CYS A   94  PHE A   99  1                                   6    
HELIX    5 AA5 ASN A  196  GLY A  212  1                                  17    
HELIX    6 AA6 ASN A  222  GLU A  245  1                                  24    
HELIX    7 AA7 VAL B   39  GLN B   46  1                                   8    
HELIX    8 AA8 GLY B   58  ALA B   72  1                                  15    
HELIX    9 AA9 MET B   86  SER B   98  1                                  13    
HELIX   10 AB1 ASP B  110  GLY B  112  5                                   3    
HELIX   11 AB2 SER B  113  LYS B  119  1                                   7    
HELIX   12 AB3 GLU B  141  SER B  154  1                                  14    
HELIX   13 AB4 ASP B  166  ARG B  171  1                                   6    
HELIX   14 AB5 LEU B  172  SER B  176  5                                   5    
HELIX   15 AB6 PHE B  263  LEU B  278  1                                  16    
HELIX   16 AB7 ASN B  281  GLU B  290  1                                  10    
HELIX   17 AB8 ASN B  316  GLN B  329  1                                  14    
HELIX   18 AB9 THR B  350  ASP B  355  5                                   6    
HELIX   19 AC1 ASP B  357  GLN B  364  5                                   8    
HELIX   20 AC2 ARG B  375  ALA B  386  1                                  12    
HELIX   21 AC3 ASP B  397  THR B  405  1                                   9    
HELIX   22 AC4 MET B  406  TYR B  408  5                                   3    
HELIX   23 AC5 SER B  420  GLU B  433  1                                  14    
HELIX   24 AC6 LEU C   16  LYS C   32  1                                  17    
HELIX   25 AC7 SER C   62  LYS C   75  1                                  14    
HELIX   26 AC8 ILE C   76  ASP C   86  1                                  11    
HELIX   27 AC9 CYS C   94  PHE C   99  1                                   6    
HELIX   28 AD1 ASN C  196  GLY C  212  1                                  17    
HELIX   29 AD2 ASN C  222  ARG C  243  1                                  22    
HELIX   30 AD3 VAL D   39  GLN D   46  1                                   8    
HELIX   31 AD4 GLY D   58  ASN D   73  1                                  16    
HELIX   32 AD5 MET D   86  SER D   98  1                                  13    
HELIX   33 AD6 ASP D  110  GLY D  112  5                                   3    
HELIX   34 AD7 SER D  113  LYS D  119  1                                   7    
HELIX   35 AD8 GLY D  140  SER D  154  1                                  15    
HELIX   36 AD9 ASP D  166  ARG D  171  1                                   6    
HELIX   37 AE1 LEU D  172  SER D  176  5                                   5    
HELIX   38 AE2 PHE D  263  LEU D  278  1                                  16    
HELIX   39 AE3 ASN D  281  GLU D  290  1                                  10    
HELIX   40 AE4 ASN D  316  GLY D  327  1                                  12    
HELIX   41 AE5 GLU D  328  LEU D  330  5                                   3    
HELIX   42 AE6 THR D  350  ASP D  355  5                                   6    
HELIX   43 AE7 ASP D  357  GLN D  364  5                                   8    
HELIX   44 AE8 ARG D  375  ALA D  386  1                                  12    
HELIX   45 AE9 ASP D  397  THR D  405  1                                   9    
HELIX   46 AF1 MET D  406  TYR D  408  5                                   3    
HELIX   47 AF2 ASN D  417  PHE D  432  1                                  16    
SHEET    1 AA1 6 LYS A  36  ILE A  42  0                                        
SHEET    2 AA1 6 GLU A   3  PHE A   9  1  N  ILE A   6   O  ASN A  38           
SHEET    3 AA1 6 ILE A  55  ILE A  58  1  O  ILE A  55   N  TYR A   7           
SHEET    4 AA1 6 GLY A  90  ILE A  93  1  O  ILE A  93   N  ILE A  58           
SHEET    5 AA1 6 LEU A 183  THR A 186  1  O  LEU A 184   N  GLY A  90           
SHEET    6 AA1 6 ILE A 178  TYR A 180 -1  N  TYR A 180   O  LEU A 183           
SHEET    1 AA2 4 GLU A 111  GLU A 113  0                                        
SHEET    2 AA2 4 LYS A 103  ILE A 105 -1  N  TYR A 104   O  LEU A 112           
SHEET    3 AA2 4 TYR A 121  GLU A 136  1  O  THR A 122   N  ILE A 105           
SHEET    4 AA2 4 THR A 142  TYR A 154 -1  O  ARG A 152   N  GLU A 123           
SHEET    1 AA3 5 GLU A 111  GLU A 113  0                                        
SHEET    2 AA3 5 LYS A 103  ILE A 105 -1  N  TYR A 104   O  LEU A 112           
SHEET    3 AA3 5 TYR A 121  GLU A 136  1  O  THR A 122   N  ILE A 105           
SHEET    4 AA3 5 GLY A 161  PHE A 165 -1  O  HIS A 162   N  GLU A 136           
SHEET    5 AA3 5 LYS A 175  GLU A 176 -1  O  GLU A 176   N  GLY A 161           
SHEET    1 AA4 9 ILE B  77  HIS B  79  0                                        
SHEET    2 AA4 9 ILE B 104  GLU B 108  1  O  VAL B 106   N  ILE B  78           
SHEET    3 AA4 9 ASP B  49  SER B  54  1  N  VAL B  51   O  ILE B 107           
SHEET    4 AA4 9 MET B 125  PHE B 128  1  O  VAL B 127   N  PHE B  52           
SHEET    5 AA4 9 LYS B 159  ASN B 163  1  O  LEU B 161   N  MET B 126           
SHEET    6 AA4 9 ILE B 179  MET B 184  1  O  VAL B 180   N  LEU B 160           
SHEET    7 AA4 9 TYR B 235  VAL B 242  1  O  ILE B 237   N  GLY B 183           
SHEET    8 AA4 9 LEU B 246  ILE B 250 -1  O  ASN B 249   N  SER B 239           
SHEET    9 AA4 9 GLU B 253  ASP B 256 -1  O  TYR B 255   N  LEU B 248           
SHEET    1 AA5 2 TYR B 211  TYR B 216  0                                        
SHEET    2 AA5 2 ILE B 219  TYR B 222 -1  O  HIS B 221   N  ASP B 212           
SHEET    1 AA6 6 GLN B 300  LYS B 304  0                                        
SHEET    2 AA6 6 LYS B 307  ILE B 311 -1  O  ALA B 309   N  PHE B 302           
SHEET    3 AA6 6 PHE B 411  PRO B 416  1  O  ALA B 414   N  MET B 310           
SHEET    4 AA6 6 LYS B 334  SER B 339  1  N  VAL B 337   O  ILE B 415           
SHEET    5 AA6 6 ILE B 366  THR B 372  1  O  ILE B 370   N  TYR B 336           
SHEET    6 AA6 6 ILE B 392  VAL B 394  1  O  ILE B 393   N  VAL B 371           
SHEET    1 AA7 6 ILE C  35  ILE C  42  0                                        
SHEET    2 AA7 6 HIS C   2  PHE C   9  1  N  ILE C   6   O  VAL C  40           
SHEET    3 AA7 6 ILE C  55  ILE C  58  1  O  PHE C  57   N  PHE C   9           
SHEET    4 AA7 6 GLY C  90  ILE C  93  1  O  ILE C  93   N  ILE C  58           
SHEET    5 AA7 6 LEU C 183  THR C 186  1  O  LEU C 184   N  GLY C  90           
SHEET    6 AA7 6 ILE C 178  TYR C 180 -1  N  TYR C 180   O  LEU C 183           
SHEET    1 AA8 4 GLU C 111  GLU C 113  0                                        
SHEET    2 AA8 4 LYS C 103  ILE C 105 -1  N  TYR C 104   O  LEU C 112           
SHEET    3 AA8 4 TYR C 121  SER C 137  1  O  SER C 124   N  ILE C 105           
SHEET    4 AA8 4 GLY C 141  TYR C 154 -1  O  HIS C 149   N  LEU C 129           
SHEET    1 AA9 5 GLU C 111  GLU C 113  0                                        
SHEET    2 AA9 5 LYS C 103  ILE C 105 -1  N  TYR C 104   O  LEU C 112           
SHEET    3 AA9 5 TYR C 121  SER C 137  1  O  SER C 124   N  ILE C 105           
SHEET    4 AA9 5 GLY C 161  PHE C 165 -1  O  HIS C 162   N  GLU C 136           
SHEET    5 AA9 5 LYS C 175  GLU C 176 -1  O  GLU C 176   N  GLY C 161           
SHEET    1 AB1 9 ILE D  78  HIS D  79  0                                        
SHEET    2 AB1 9 ILE D 104  GLU D 108  1  O  VAL D 106   N  ILE D  78           
SHEET    3 AB1 9 ASP D  49  SER D  54  1  N  VAL D  51   O  ALA D 105           
SHEET    4 AB1 9 MET D 125  PHE D 128  1  O  VAL D 127   N  PHE D  52           
SHEET    5 AB1 9 LYS D 159  ASN D 163  1  O  LEU D 161   N  MET D 126           
SHEET    6 AB1 9 ILE D 179  MET D 184  1  O  VAL D 180   N  LEU D 160           
SHEET    7 AB1 9 TYR D 235  VAL D 242  1  O  ILE D 237   N  GLY D 183           
SHEET    8 AB1 9 LEU D 246  ILE D 250 -1  O  TYR D 247   N  ASP D 241           
SHEET    9 AB1 9 GLU D 253  ASP D 256 -1  O  TYR D 255   N  LEU D 248           
SHEET    1 AB2 2 GLN D 210  TYR D 216  0                                        
SHEET    2 AB2 2 ILE D 219  HIS D 223 -1  O  HIS D 221   N  ASP D 212           
SHEET    1 AB3 6 GLN D 300  LYS D 304  0                                        
SHEET    2 AB3 6 LYS D 307  ILE D 311 -1  O  ALA D 309   N  PHE D 302           
SHEET    3 AB3 6 PHE D 411  PRO D 416  1  O  ALA D 414   N  MET D 310           
SHEET    4 AB3 6 LYS D 334  SER D 339  1  N  VAL D 337   O  ILE D 415           
SHEET    5 AB3 6 ILE D 366  THR D 372  1  O  GLU D 367   N  LYS D 334           
SHEET    6 AB3 6 ILE D 392  VAL D 394  1  O  ILE D 393   N  VAL D 371           
LINK         SG  CYS B 202                ZN    ZN B 501     1555   1555  2.24  
LINK         SG  CYS B 205                ZN    ZN B 501     1555   1555  2.35  
LINK         SG  CYS B 224                ZN    ZN B 501     1555   1555  2.28  
LINK         SG  CYS B 226                ZN    ZN B 501     1555   1555  2.35  
LINK         OD2 ASP B 262                MG    MG B 502     1555   1555  1.99  
LINK         SG  CYS D 202                ZN    ZN D 501     1555   1555  2.43  
LINK         SG  CYS D 205                ZN    ZN D 501     1555   1555  2.14  
LINK         SG  CYS D 224                ZN    ZN D 501     1555   1555  2.32  
LINK         SG  CYS D 226                ZN    ZN D 501     1555   1555  2.50  
LINK        MG    MG B 502                 O   HOH B 634     1555   1555  2.06  
LINK        MG    MG B 502                 O   HOH B 689     1555   1555  2.18  
LINK        MG    MG B 502                 O   HOH B 610     1555   1555  2.20  
CISPEP   1 GLY A  190    PRO A  191          0       -11.56                     
CISPEP   2 GLU A  216    PRO A  217          0        -2.01                     
CISPEP   3 ALA B  243    PRO B  244          0         2.72                     
CISPEP   4 GLY C  190    PRO C  191          0        -8.10                     
CISPEP   5 GLU C  216    PRO C  217          0        -5.77                     
CISPEP   6 ALA D  243    PRO D  244          0        -5.93                     
SITE     1 AC1 14 ASP A 138  THR A 139  GLY A 158  THR A 159                    
SITE     2 AC1 14 HIS A 179  HOH A 409  HOH A 410  HOH A 421                    
SITE     3 AC1 14 HOH A 443  HOH A 468  HOH A 492  ASP C 138                    
SITE     4 AC1 14 THR C 139  THR C 159                                          
SITE     1 AC2  4 ILE A 213  PRO A 214  SER B 239  ASP B 241                    
SITE     1 AC3  4 CYS B 202  CYS B 205  CYS B 224  CYS B 226                    
SITE     1 AC4  5 HIS B 189  ASP B 262  HOH B 610  HOH B 634                    
SITE     2 AC4  5 HOH B 689                                                     
SITE     1 AC5  4 CYS D 202  CYS D 205  CYS D 224  CYS D 226                    
CRYST1  107.100  110.370  116.360  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      0.009337  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008594        0.00000                         
ATOM      1  N   MET A   1      56.195  37.209  42.156  1.00 54.06           N  
ANISOU    1  N   MET A   1     5136   6602   8804    904  -2982   -866       N  
ATOM      2  CA  MET A   1      55.810  37.788  40.868  1.00 57.51           C  
ANISOU    2  CA  MET A   1     5340   7336   9174    819  -2580  -1026       C  
ATOM      3  C   MET A   1      54.393  38.347  40.929  1.00 48.61           C  
ANISOU    3  C   MET A   1     4571   6275   7625    612  -2299   -664       C  
ATOM      4  O   MET A   1      53.540  37.777  41.612  1.00 46.47           O  
ANISOU    4  O   MET A   1     4620   5809   7229    589  -2474   -376       O  
ATOM      5  CB  MET A   1      55.921  36.748  39.753  1.00 66.82           C  
ANISOU    5  CB  MET A   1     6321   8463  10604    951  -2526  -1306       C  
ATOM      6  CG  MET A   1      55.566  37.292  38.378  1.00 75.87           C  
ANISOU    6  CG  MET A   1     7273   9906  11647    822  -2070  -1478       C  
ATOM      7  SD  MET A   1      55.690  36.055  37.072  1.00 85.03           S  
ANISOU    7  SD  MET A   1     8219  11011  13077    959  -1996  -1813       S  
ATOM      8  CE  MET A   1      55.031  36.970  35.667  1.00 76.93           C  
ANISOU    8  CE  MET A   1     7103  10336  11790    709  -1443  -1888       C  
ATOM      9  N   HIS A   2      54.146  39.466  40.236  1.00 43.85           N  
ANISOU    9  N   HIS A   2     3921   5942   6797    446  -1889   -699       N  
ATOM     10  CA  HIS A   2      52.791  40.013  40.169  1.00 38.61           C  
ANISOU   10  CA  HIS A   2     3554   5340   5777    283  -1641   -429       C  
ATOM     11  C   HIS A   2      51.838  38.996  39.560  1.00 34.81           C  
ANISOU   11  C   HIS A   2     3166   4739   5321    329  -1610   -380       C  
ATOM     12  O   HIS A   2      52.180  38.305  38.597  1.00 35.89           O  
ANISOU   12  O   HIS A   2     3081   4866   5688    430  -1577   -621       O  
ATOM     13  CB  HIS A   2      52.773  41.303  39.352  1.00 33.59           C  
ANISOU   13  CB  HIS A   2     2852   4966   4943    116  -1270   -521       C  
ATOM     14  CG  HIS A   2      53.491  42.424  40.021  1.00 35.18           C  
ANISOU   14  CG  HIS A   2     3033   5285   5048     31  -1284   -511       C  
ATOM     15  ND1 HIS A   2      54.466  43.161  39.393  1.00 37.70           N  
ANISOU   15  ND1 HIS A   2     3114   5802   5408    -58  -1125   -763       N  
ATOM     16  CD2 HIS A   2      53.413  42.899  41.286  1.00 35.56           C  
ANISOU   16  CD2 HIS A   2     3269   5283   4958      4  -1446   -291       C  
ATOM     17  CE1 HIS A   2      54.945  44.060  40.236  1.00 39.70           C  
ANISOU   17  CE1 HIS A   2     3413   6113   5560   -121  -1194   -686       C  
ATOM     18  NE2 HIS A   2      54.313  43.927  41.389  1.00 38.03           N  
ANISOU   18  NE2 HIS A   2     3457   5751   5243    -75  -1388   -400       N  
ATOM     19  N   GLU A   3      50.631  38.919  40.119  1.00 33.30           N  
ANISOU   19  N   GLU A   3     3290   4476   4885    240  -1609    -91       N  
ATOM     20  CA  GLU A   3      49.680  37.883  39.751  1.00 33.02           C  
ANISOU   20  CA  GLU A   3     3381   4308   4858    265  -1624    -10       C  
ATOM     21  C   GLU A   3      48.274  38.446  39.821  1.00 37.27           C  
ANISOU   21  C   GLU A   3     4162   4943   5056    101  -1391    189       C  
ATOM     22  O   GLU A   3      47.978  39.314  40.642  1.00 33.04           O  
ANISOU   22  O   GLU A   3     3770   4494   4291    -16  -1360    328       O  
ATOM     23  CB  GLU A   3      49.770  36.653  40.679  1.00 35.75           C  
ANISOU   23  CB  GLU A   3     3883   4368   5332    340  -2044    123       C  
ATOM     24  CG  GLU A   3      51.145  36.012  40.738  1.00 51.86           C  
ANISOU   24  CG  GLU A   3     5690   6261   7752    544  -2374   -100       C  
ATOM     25  CD  GLU A   3      51.245  34.869  41.753  0.52 61.72           C  
ANISOU   25  CD  GLU A   3     7167   7171   9111    604  -2876     56       C  
ATOM     26  OE1 GLU A   3      50.307  34.038  41.817  0.87 56.23           O  
ANISOU   26  OE1 GLU A   3     6723   6324   8318    540  -2954    236       O  
ATOM     27  OE2 GLU A   3      52.269  34.805  42.482  0.77 67.21           O  
ANISOU   27  OE2 GLU A   3     7808   7744   9986    701  -3215     -4       O  
ATOM     28  N   LEU A   4      47.411  37.922  38.967  1.00 29.53           N  
ANISOU   28  N   LEU A   4     3211   3946   4062    103  -1244    173       N  
ATOM     29  CA  LEU A   4      45.987  38.188  39.004  1.00 27.62           C  
ANISOU   29  CA  LEU A   4     3177   3767   3549    -25  -1068    320       C  
ATOM     30  C   LEU A   4      45.265  36.848  39.015  1.00 31.18           C  
ANISOU   30  C   LEU A   4     3757   4048   4043    -15  -1188    415       C  
ATOM     31  O   LEU A   4      45.671  35.917  38.307  1.00 30.93           O  
ANISOU   31  O   LEU A   4     3602   3894   4256    116  -1272    299       O  
ATOM     32  CB  LEU A   4      45.542  39.010  37.777  1.00 27.61           C  
ANISOU   32  CB  LEU A   4     3098   3924   3467    -53   -749    188       C  
ATOM     33  CG  LEU A   4      46.000  40.462  37.752  1.00 34.01           C  
ANISOU   33  CG  LEU A   4     3866   4898   4160   -121   -627    127       C  
ATOM     34  CD1 LEU A   4      45.705  41.073  36.367  1.00 33.13           C  
ANISOU   34  CD1 LEU A   4     3711   4881   3994   -165   -378    -14       C  
ATOM     35  CD2 LEU A   4      45.299  41.231  38.862  1.00 25.77           C  
ANISOU   35  CD2 LEU A   4     3012   3915   2865   -222   -648    286       C  
ATOM     36  N   THR A   5      44.206  36.751  39.808  1.00 31.29           N  
ANISOU   36  N   THR A   5     4010   4066   3814   -171  -1196    601       N  
ATOM     37  CA  THR A   5      43.384  35.544  39.870  1.00 32.80           C  
ANISOU   37  CA  THR A   5     4366   4116   3981   -228  -1291    708       C  
ATOM     38  C   THR A   5      42.113  35.765  39.069  1.00 28.63           C  
ANISOU   38  C   THR A   5     3847   3718   3313   -285   -991    663       C  
ATOM     39  O   THR A   5      41.448  36.805  39.216  1.00 29.96           O  
ANISOU   39  O   THR A   5     4038   4073   3272   -377   -794    646       O  
ATOM     40  CB  THR A   5      43.037  35.180  41.316  1.00 33.12           C  
ANISOU   40  CB  THR A   5     4686   4084   3813   -429  -1507    930       C  
ATOM     41  OG1 THR A   5      44.240  34.906  42.009  1.00 35.62           O  
ANISOU   41  OG1 THR A   5     5014   4235   4286   -358  -1840    969       O  
ATOM     42  CG2 THR A   5      42.175  33.950  41.385  1.00 41.75           C  
ANISOU   42  CG2 THR A   5     5986   5037   4841   -547  -1607   1048       C  
ATOM     43  N   ILE A   6      41.806  34.818  38.190  1.00 26.93           N  
ANISOU   43  N   ILE A   6     3602   3395   3234   -210   -978    616       N  
ATOM     44  CA  ILE A   6      40.560  34.814  37.429  1.00 26.37           C  
ANISOU   44  CA  ILE A   6     3556   3410   3054   -259   -738    578       C  
ATOM     45  C   ILE A   6      39.661  33.732  37.997  1.00 34.65           C  
ANISOU   45  C   ILE A   6     4817   4361   3986   -409   -848    728       C  
ATOM     46  O   ILE A   6      40.052  32.548  38.051  1.00 35.68           O  
ANISOU   46  O   ILE A   6     5016   4273   4268   -367  -1091    794       O  
ATOM     47  CB  ILE A   6      40.779  34.573  35.931  1.00 24.55           C  
ANISOU   47  CB  ILE A   6     3147   3148   3032    -98   -611    407       C  
ATOM     48  CG1 ILE A   6      41.613  35.684  35.321  1.00 45.92           C  
ANISOU   48  CG1 ILE A   6     5675   5977   5797    -28   -479    252       C  
ATOM     49  CG2 ILE A   6      39.388  34.359  35.232  1.00 25.14           C  
ANISOU   49  CG2 ILE A   6     3288   3267   2997   -153   -417    392       C  
ATOM     50  CD1 ILE A   6      41.865  35.483  33.858  1.00 49.58           C  
ANISOU   50  CD1 ILE A   6     5981   6437   6422     67   -339     69       C  
ATOM     51  N   TYR A   7      38.450  34.136  38.401  1.00 30.47           N  
ANISOU   51  N   TYR A   7     4392   3995   3189   -593   -682    755       N  
ATOM     52  CA  TYR A   7      37.398  33.200  38.808  1.00 35.33           C  
ANISOU   52  CA  TYR A   7     5198   4581   3643   -797   -710    859       C  
ATOM     53  C   TYR A   7      36.625  32.774  37.559  1.00 29.71           C  
ANISOU   53  C   TYR A   7     4407   3862   3021   -711   -539    753       C  
ATOM     54  O   TYR A   7      35.904  33.577  36.962  1.00 27.18           O  
ANISOU   54  O   TYR A   7     3981   3708   2640   -681   -298    610       O  
ATOM     55  CB  TYR A   7      36.453  33.850  39.822  1.00 35.86           C  
ANISOU   55  CB  TYR A   7     5367   4877   3382  -1059   -585    869       C  
ATOM     56  CG  TYR A   7      36.900  33.818  41.273  1.00 44.19           C  
ANISOU   56  CG  TYR A   7     6608   5915   4266  -1264   -787   1030       C  
ATOM     57  CD1 TYR A   7      38.233  33.638  41.620  1.00 44.31           C  
ANISOU   57  CD1 TYR A   7     6650   5739   4446  -1149  -1061   1130       C  
ATOM     58  CD2 TYR A   7      35.973  33.963  42.300  1.00 43.57           C  
ANISOU   58  CD2 TYR A   7     6675   6025   3854  -1592   -708   1055       C  
ATOM     59  CE1 TYR A   7      38.624  33.601  42.955  1.00 46.77           C  
ANISOU   59  CE1 TYR A   7     7164   6012   4593  -1346  -1277   1286       C  
ATOM     60  CE2 TYR A   7      36.353  33.920  43.620  1.00 45.07           C  
ANISOU   60  CE2 TYR A   7     7024   6183   3918  -1786   -871   1164       C  
ATOM     61  CZ  TYR A   7      37.674  33.742  43.944  1.00 47.46           C  
ANISOU   61  CZ  TYR A   7     7405   6273   4356  -1676  -1171   1313       C  
ATOM     62  OH  TYR A   7      38.030  33.711  45.270  1.00 59.18           O  
ANISOU   62  OH  TYR A   7     9025   7698   5761  -1853  -1316   1379       O  
ATOM     63  N   HIS A   8      36.789  31.531  37.143  1.00 31.26           N  
ANISOU   63  N   HIS A   8     4658   3847   3371   -658   -692    811       N  
ATOM     64  CA  HIS A   8      36.103  31.005  35.958  1.00 29.11           C  
ANISOU   64  CA  HIS A   8     4322   3546   3194   -577   -552    722       C  
ATOM     65  C   HIS A   8      34.910  30.195  36.456  1.00 33.55           C  
ANISOU   65  C   HIS A   8     5088   4116   3544   -832   -555    825       C  
ATOM     66  O   HIS A   8      35.071  29.071  36.941  1.00 35.22           O  
ANISOU   66  O   HIS A   8     5494   4131   3758   -936   -807    980       O  
ATOM     67  CB  HIS A   8      37.068  30.170  35.121  1.00 29.45           C  
ANISOU   67  CB  HIS A   8     4268   3365   3555   -351   -712    678       C  
ATOM     68  CG  HIS A   8      36.493  29.667  33.835  1.00 37.33           C  
ANISOU   68  CG  HIS A   8     5187   4331   4665   -253   -567    574       C  
ATOM     69  ND1 HIS A   8      37.258  29.016  32.893  1.00 39.92           N  
ANISOU   69  ND1 HIS A   8     5380   4508   5279    -46   -648    468       N  
ATOM     70  CD2 HIS A   8      35.236  29.713  33.334  1.00 37.05           C  
ANISOU   70  CD2 HIS A   8     5176   4400   4500   -333   -352    535       C  
ATOM     71  CE1 HIS A   8      36.496  28.686  31.864  1.00 39.73           C  
ANISOU   71  CE1 HIS A   8     5323   4491   5281    -14   -483    394       C  
ATOM     72  NE2 HIS A   8      35.265  29.091  32.109  1.00 36.48           N  
ANISOU   72  NE2 HIS A   8     5013   4223   4625   -180   -312    441       N  
ATOM     73  N   PHE A   9      33.714  30.770  36.358  1.00 31.82           N  
ANISOU   73  N   PHE A   9     4832   4119   3138   -948   -299    721       N  
ATOM     74  CA  PHE A   9      32.525  30.110  36.885  1.00 40.75           C  
ANISOU   74  CA  PHE A   9     6125   5324   4034  -1241   -257    771       C  
ATOM     75  C   PHE A   9      31.954  29.101  35.899  1.00 41.93           C  
ANISOU   75  C   PHE A   9     6285   5351   4295  -1190   -231    757       C  
ATOM     76  O   PHE A   9      31.927  29.341  34.692  1.00 35.30           O  
ANISOU   76  O   PHE A   9     5273   4496   3642   -953   -104    622       O  
ATOM     77  CB  PHE A   9      31.434  31.123  37.231  1.00 34.33           C  
ANISOU   77  CB  PHE A   9     5224   4828   2992  -1387      1    598       C  
ATOM     78  CG  PHE A   9      31.678  31.848  38.509  1.00 38.17           C  
ANISOU   78  CG  PHE A   9     5764   5462   3276  -1561    -30    628       C  
ATOM     79  CD1 PHE A   9      31.480  31.218  39.720  1.00 42.81           C  
ANISOU   79  CD1 PHE A   9     6586   6070   3608  -1915   -144    778       C  
ATOM     80  CD2 PHE A   9      32.125  33.158  38.499  1.00 32.35           C  
ANISOU   80  CD2 PHE A   9     4871   4833   2587  -1395     39    514       C  
ATOM     81  CE1 PHE A   9      31.735  31.882  40.910  1.00 51.24           C  
ANISOU   81  CE1 PHE A   9     7656   7237   4574  -2028   -180    756       C  
ATOM     82  CE2 PHE A   9      32.365  33.827  39.670  1.00 38.71           C  
ANISOU   82  CE2 PHE A   9     5723   5773   3212  -1547      7    536       C  
ATOM     83  CZ  PHE A   9      32.177  33.197  40.883  1.00 38.92           C  
ANISOU   83  CZ  PHE A   9     5932   5804   3053  -1852    -96    651       C  
ATOM     84  N  AMET A  10      31.499  27.963  36.432  0.53 45.15           N  
ANISOU   84  N  AMET A  10     6924   5664   4567  -1442   -367    903       N  
ATOM     85  N  BMET A  10      31.520  27.954  36.431  0.47 45.16           N  
ANISOU   85  N  BMET A  10     6926   5661   4572  -1439   -372    906       N  
ATOM     86  CA AMET A  10      30.661  27.021  35.694  0.53 46.51           C  
ANISOU   86  CA AMET A  10     7137   5770   4765  -1481   -316    889       C  
ATOM     87  CA BMET A  10      30.717  26.981  35.690  0.47 46.57           C  
ANISOU   87  CA BMET A  10     7151   5762   4783  -1474   -331    897       C  
ATOM     88  C  AMET A  10      31.325  26.556  34.405  0.53 41.95           C  
ANISOU   88  C  AMET A  10     6438   4967   4533  -1135   -387    851       C  
ATOM     89  C  BMET A  10      31.405  26.531  34.406  0.47 42.06           C  
ANISOU   89  C  BMET A  10     6454   4966   4560  -1125   -404    857       C  
ATOM     90  O  AMET A  10      30.677  26.436  33.365  0.53 41.42           O  
ANISOU   90  O  AMET A  10     6263   4927   4548  -1034   -218    732       O  
ATOM     91  O  BMET A  10      30.777  26.430  33.352  0.47 40.75           O  
ANISOU   91  O  BMET A  10     6175   4827   4480  -1017   -233    736       O  
ATOM     92  CB AMET A  10      29.293  27.631  35.394  0.53 50.80           C  
ANISOU   92  CB AMET A  10     7543   6603   5155  -1579     10    683       C  
ATOM     93  CB BMET A  10      29.331  27.543  35.382  0.47 50.90           C  
ANISOU   93  CB BMET A  10     7567   6595   5176  -1578     -6    696       C  
ATOM     94  CG AMET A  10      28.629  28.269  36.600  0.53 56.29           C  
ANISOU   94  CG AMET A  10     8275   7586   5526  -1901    128    624       C  
ATOM     95  CG BMET A  10      28.658  28.215  36.568  0.47 56.27           C  
ANISOU   95  CG BMET A  10     8278   7567   5534  -1894    118    632       C  
ATOM     96  SD AMET A  10      28.644  27.214  38.061  0.53 63.73           S  
ANISOU   96  SD AMET A  10     9533   8442   6238  -2302   -119    826       S  
ATOM     97  SD BMET A  10      28.631  27.188  38.047  0.47 63.62           S  
ANISOU   97  SD BMET A  10     9522   8426   6226  -2303   -119    827       S  
ATOM     98  CE AMET A  10      27.771  25.769  37.454  0.53 64.96           C  
ANISOU   98  CE AMET A  10     9814   8471   6395  -2425   -151    860       C  
ATOM     99  CE BMET A  10      27.781  25.731  37.439  0.47 65.00           C  
ANISOU   99  CE BMET A  10     9826   8468   6404  -2425   -157    866       C  
ATOM    100  N  ASER A  11      32.631  26.307  34.468  0.53 41.27           N  
ANISOU  100  N  ASER A  11     6356   4669   4655   -957   -639    922       N  
ATOM    101  N  BSER A  11      32.710  26.268  34.491  0.47 40.77           N  
ANISOU  101  N  BSER A  11     6298   4589   4602   -951   -661    929       N  
ATOM    102  CA ASER A  11      33.347  25.766  33.324  0.53 42.98           C  
ANISOU  102  CA ASER A  11     6439   4687   5203   -656   -724    844       C  
ATOM    103  CA BSER A  11      33.456  25.799  33.333  0.47 43.01           C  
ANISOU  103  CA BSER A  11     6434   4684   5222   -640   -735    842       C  
ATOM    104  C  ASER A  11      32.985  24.311  33.033  0.53 52.02           C  
ANISOU  104  C  ASER A  11     7750   5601   6413   -702   -909    933       C  
ATOM    105  C  BSER A  11      33.133  24.354  32.967  0.47 52.03           C  
ANISOU  105  C  BSER A  11     7727   5593   6449   -664   -916    919       C  
ATOM    106  O  ASER A  11      33.584  23.712  32.134  0.53 53.42           O  
ANISOU  106  O  ASER A  11     7823   5596   6878   -456  -1015    852       O  
ATOM    107  O  BSER A  11      33.573  23.891  31.910  0.47 52.71           O  
ANISOU  107  O  BSER A  11     7675   5544   6808   -417   -949    810       O  
ATOM    108  CB ASER A  11      34.846  25.878  33.563  0.53 42.73           C  
ANISOU  108  CB ASER A  11     6334   4515   5386   -465   -961    840       C  
ATOM    109  CB BSER A  11      34.949  25.931  33.596  0.47 42.86           C  
ANISOU  109  CB BSER A  11     6342   4531   5413   -454   -970    837       C  
ATOM    110  OG ASER A  11      35.191  25.131  34.718  0.53 47.23           O  
ANISOU  110  OG ASER A  11     7166   4892   5887   -623  -1318   1036       O  
ATOM    111  OG BSER A  11      35.300  25.156  34.730  0.47 47.52           O  
ANISOU  111  OG BSER A  11     7193   4921   5940   -606  -1333   1032       O  
ATOM    112  N  AASP A  12      32.051  23.719  33.777  0.53 56.89           N  
ANISOU  112  N  AASP A  12     8626   6226   6765  -1030   -957   1080       N  
ATOM    113  N  BASP A  12      32.411  23.625  33.818  0.47 57.00           N  
ANISOU  113  N  BASP A  12     8643   6173   6841   -978  -1044   1094       N  
ATOM    114  CA AASP A  12      31.634  22.341  33.532  0.53 66.29           C  
ANISOU  114  CA AASP A  12    10015   7191   7983  -1116  -1146   1181       C  
ATOM    115  CA BASP A  12      31.963  22.287  33.461  0.47 66.43           C  
ANISOU  115  CA BASP A  12    10012   7150   8078  -1041  -1209   1175       C  
ATOM    116  C  AASP A  12      30.437  22.378  32.590  0.53 63.49           C  
ANISOU  116  C  AASP A  12     9542   7000   7580  -1130   -817   1054       C  
ATOM    117  C  BASP A  12      30.930  22.397  32.349  0.47 63.25           C  
ANISOU  117  C  BASP A  12     9449   6903   7681   -990   -872   1027       C  
ATOM    118  O  AASP A  12      29.278  22.373  33.012  0.53 63.08           O  
ANISOU  118  O  AASP A  12     9594   7128   7247  -1436   -657   1073       O  
ATOM    119  O  BASP A  12      31.167  21.963  31.216  0.47 58.74           O  
ANISOU  119  O  BASP A  12     8746   6204   7369   -736   -872    927       O  
ATOM    120  CB AASP A  12      31.314  21.628  34.838  0.53 77.39           C  
ANISOU  120  CB AASP A  12    11808   8499   9097  -1519  -1402   1418       C  
ATOM    121  CB BASP A  12      31.371  21.572  34.680  0.47 77.27           C  
ANISOU  121  CB BASP A  12    11770   8461   9128  -1473  -1408   1404       C  
ATOM    122  CG AASP A  12      31.443  20.121  34.722  0.53 87.28           C  
ANISOU  122  CG AASP A  12    13282   9421  10459  -1529  -1765   1521       C  
ATOM    123  CG BASP A  12      31.060  20.100  34.416  0.47 86.70           C  
ANISOU  123  CG BASP A  12    13183   9391  10368  -1544  -1658   1498       C  
ATOM    124  OD1AASP A  12      32.559  19.647  34.421  0.53 90.56           O  
ANISOU  124  OD1AASP A  12    13655   9559  11195  -1234  -2077   1499       O  
ATOM    125  OD1BASP A  12      31.190  19.639  33.260  0.47 88.19           O  
ANISOU  125  OD1BASP A  12    13244   9430  10836  -1273  -1665   1411       O  
ATOM    126  OD2AASP A  12      30.433  19.410  34.930  0.53 90.65           O  
ANISOU  126  OD2AASP A  12    13856   9920  10668  -1798  -1722   1544       O  
ATOM    127  OD2BASP A  12      30.698  19.393  35.383  0.47 91.48           O  
ANISOU  127  OD2BASP A  12    14021  10001  10738  -1842  -1827   1576       O  
ATOM    128  N  ALYS A  13      30.729  22.435  31.293  0.53 61.28           N  
ANISOU  128  N  ALYS A  13     9034   6673   7578   -809   -714    896       N  
ATOM    129  N  BLYS A  13      29.789  23.007  32.672  0.47 63.70           N  
ANISOU  129  N  BLYS A  13     9501   7243   7458  -1228   -592    984       N  
ATOM    130  CA ALYS A  13      29.710  22.443  30.255  0.53 54.33           C  
ANISOU  130  CA ALYS A  13     8042   5902   6698   -774   -444    768       C  
ATOM    131  CA BLYS A  13      28.663  23.071  31.751  0.47 58.69           C  
ANISOU  131  CA BLYS A  13     8744   6751   6806  -1216   -310    837       C  
ATOM    132  C  ALYS A  13      30.178  21.552  29.117  0.53 36.40           C  
ANISOU  132  C  ALYS A  13     5707   3395   4730   -520   -559    713       C  
ATOM    133  C  BLYS A  13      28.886  24.119  30.667  0.47 53.32           C  
ANISOU  133  C  BLYS A  13     7770   6178   6313   -900    -83    628       C  
ATOM    134  O  ALYS A  13      31.366  21.264  28.988  0.53 39.12           O  
ANISOU  134  O  ALYS A  13     5994   3556   5314   -313   -779    693       O  
ATOM    135  O  BLYS A  13      28.828  23.817  29.471  0.47 52.25           O  
ANISOU  135  O  BLYS A  13     7531   5955   6368   -702    -21    537       O  
ATOM    136  CB ALYS A  13      29.440  23.860  29.730  0.53 52.17           C  
ANISOU  136  CB ALYS A  13     7528   5890   6403   -661   -119    576       C  
ATOM    137  CB BLYS A  13      27.380  23.365  32.534  0.47 59.96           C  
ANISOU  137  CB BLYS A  13     8974   7192   6617  -1586   -114    805       C  
ATOM    138  CG ALYS A  13      29.118  24.877  30.794  0.53 52.39           C  
ANISOU  138  CG ALYS A  13     7566   6158   6182   -852    -15    574       C  
ATOM    139  CD ALYS A  13      29.182  26.272  30.223  0.53 48.45           C  
ANISOU  139  CD ALYS A  13     6849   5833   5728   -675    201    387       C  
ATOM    140  CE ALYS A  13      30.543  26.535  29.597  0.53 48.27           C  
ANISOU  140  CE ALYS A  13     6707   5683   5951   -408    123    356       C  
ATOM    141  NZ ALYS A  13      30.742  27.971  29.269  0.53 45.04           N  
ANISOU  141  NZ ALYS A  13     6151   5433   5530   -305    286    215       N  
ATOM    142  N  ALEU A  14      29.231  21.129  28.280  0.53 32.21           N  
ANISOU  142  N  ALEU A  14     5163   2880   4197   -531   -409    655       N  
ATOM    143  N  BLEU A  14      29.158  25.359  31.071  0.47 51.68           N  
ANISOU  143  N  BLEU A  14     7448   6150   6037   -872     25    553       N  
ATOM    144  CA ALEU A  14      29.574  20.265  27.153  0.53 34.16           C  
ANISOU  144  CA ALEU A  14     5345   2918   4717   -303   -497    584       C  
ATOM    145  CA BLEU A  14      29.197  26.493  30.145  0.47 48.53           C  
ANISOU  145  CA BLEU A  14     6829   5867   5742   -650    230    360       C  
ATOM    146  C  ALEU A  14      30.636  20.901  26.252  0.53 29.57           C  
ANISOU  146  C  ALEU A  14     4496   2353   4387      2   -416    391       C  
ATOM    147  C  BLEU A  14      30.512  26.513  29.361  0.47 48.06           C  
ANISOU  147  C  BLEU A  14     6661   5648   5952   -378    143    334       C  
ATOM    148  O  ALEU A  14      31.594  20.236  25.846  0.53 33.37           O  
ANISOU  148  O  ALEU A  14     4908   2641   5131    198   -618    325       O  
ATOM    149  O  BLEU A  14      31.324  27.429  29.465  0.47 45.03           O  
ANISOU  149  O  BLEU A  14     6182   5322   5605   -284    155    288       O  
ATOM    150  CB ALEU A  14      28.322  19.937  26.347  0.53 33.52           C  
ANISOU  150  CB ALEU A  14     5268   2896   4573   -365   -295    531       C  
ATOM    151  CB BLEU A  14      28.999  27.798  30.911  0.47 43.25           C  
ANISOU  151  CB BLEU A  14     6101   5435   4898   -734    342    283       C  
ATOM    152  CG ALEU A  14      28.517  18.900  25.241  0.53 38.92           C  
ANISOU  152  CG ALEU A  14     5922   3358   5509   -172   -395    473       C  
ATOM    153  CG BLEU A  14      27.871  27.857  31.949  0.47 35.53           C  
ANISOU  153  CG BLEU A  14     5197   4667   3634  -1045    425    262       C  
ATOM    154  CD1ALEU A  14      28.828  17.497  25.806  0.53 29.49           C  
ANISOU  154  CD1ALEU A  14     4968   1859   4376   -241   -793    639       C  
ATOM    155  CD1BLEU A  14      27.785  29.224  32.581  0.47 29.88           C  
ANISOU  155  CD1BLEU A  14     4381   4179   2794  -1071    524    134       C  
ATOM    156  CD2ALEU A  14      27.298  18.855  24.342  0.53 39.51           C  
ANISOU  156  CD2ALEU A  14     5960   3531   5521   -209   -146    391       C  
ATOM    157  CD2BLEU A  14      26.528  27.470  31.350  0.47 29.17           C  
ANISOU  157  CD2BLEU A  14     4357   3944   2782  -1120    578    130       C  
ATOM    158  N  AASN A  15      30.488  22.176  25.926  0.53 30.94           N  
ANISOU  158  N  AASN A  15     4520   2756   4481     29   -140    277       N  
ATOM    159  N  BASN A  15      30.717  25.468  28.567  0.47 49.95           N  
ANISOU  159  N  BASN A  15     6905   5697   6376   -267     56    341       N  
ATOM    160  CA AASN A  15      31.468  22.880  25.110  0.53 33.43           C  
ANISOU  160  CA AASN A  15     4616   3117   4968    237    -43     99       C  
ATOM    161  CA BASN A  15      31.934  25.324  27.782  0.47 42.71           C  
ANISOU  161  CA BASN A  15     5853   4651   5725    -30    -20    258       C  
ATOM    162  C  AASN A  15      31.848  24.184  25.793  0.53 39.38           C  
ANISOU  162  C  AASN A  15     5321   4049   5592    189     38     98       C  
ATOM    163  C  BASN A  15      31.660  25.477  26.288  0.47 35.62           C  
ANISOU  163  C  BASN A  15     4828   3771   4935    105    177     91       C  
ATOM    164  O  AASN A  15      31.029  24.812  26.468  0.53 37.84           O  
ANISOU  164  O  AASN A  15     5207   4000   5169     26    134    163       O  
ATOM    165  O  BASN A  15      32.383  24.919  25.461  0.47 40.63           O  
ANISOU  165  O  BASN A  15     5365   4286   5788    260    127      1       O  
ATOM    166  CB AASN A  15      30.940  23.171  23.692  0.53 21.87           C  
ANISOU  166  CB AASN A  15     3048   1720   3540    317    205    -59       C  
ATOM    167  CB BASN A  15      32.603  23.975  28.084  0.47 35.50           C  
ANISOU  167  CB BASN A  15     5030   3480   4979     14   -335    355       C  
ATOM    168  CG AASN A  15      30.508  21.900  22.951  0.53 23.94           C  
ANISOU  168  CG AASN A  15     3352   1814   3929    368    143    -68       C  
ATOM    169  CG BASN A  15      34.126  24.036  27.953  0.47 39.49           C  
ANISOU  169  CG BASN A  15     5376   3895   5733    219   -488    254       C  
ATOM    170  OD1AASN A  15      31.334  21.159  22.422  0.53 28.18           O  
ANISOU  170  OD1AASN A  15     3802   2206   4700    523     16   -158       O  
ATOM    171  OD1BASN A  15      34.658  24.875  27.227  0.47 37.58           O  
ANISOU  171  OD1BASN A  15     4935   3777   5566    334   -308     85       O  
ATOM    172  ND2AASN A  15      29.208  21.660  22.908  0.53 23.61           N  
ANISOU  172  ND2AASN A  15     3427   1803   3742    241    231     -4       N  
ATOM    173  ND2BASN A  15      34.830  23.142  28.653  0.47 38.24           N  
ANISOU  173  ND2BASN A  15     5313   3517   5699    249   -842    340       N  
ATOM    174  N  ALEU A  16      33.104  24.594  25.608  0.53 39.12           N  
ANISOU  174  N  ALEU A  16     5136   4017   5711    325      0     -6       N  
ATOM    175  N  BLEU A  16      30.632  26.241  25.927  0.47 30.57           N  
ANISOU  175  N  BLEU A  16     4188   3280   4149     46    385     24       N  
ATOM    176  CA ALEU A  16      33.554  25.860  26.174  0.53 39.74           C  
ANISOU  176  CA ALEU A  16     5165   4257   5678    286     73    -15       C  
ATOM    177  CA BLEU A  16      30.152  26.242  24.551  0.47 26.42           C  
ANISOU  177  CA BLEU A  16     3607   2738   3693    134    533   -107       C  
ATOM    178  C  ALEU A  16      34.615  26.493  25.286  0.53 39.47           C  
ANISOU  178  C  ALEU A  16     4930   4285   5783    412    175   -211       C  
ATOM    179  C  BLEU A  16      30.782  27.302  23.656  0.47 18.48           C  
ANISOU  179  C  BLEU A  16     2499   1794   2728    227    653   -251       C  
ATOM    180  O  ALEU A  16      35.607  27.035  25.782  0.53 38.30           O  
ANISOU  180  O  ALEU A  16     4698   4185   5670    436    114   -241       O  
ATOM    181  O  BLEU A  16      30.737  27.160  22.441  0.47 26.67           O  
ANISOU  181  O  BLEU A  16     3502   2784   3847    293    741   -357       O  
ATOM    182  CB ALEU A  16      34.091  25.680  27.601  0.53 41.33           C  
ANISOU  182  CB ALEU A  16     5461   4401   5842    217   -169    136       C  
ATOM    183  CB BLEU A  16      28.629  26.416  24.523  0.47 26.06           C  
ANISOU  183  CB BLEU A  16     3625   2787   3490     27    651   -134       C  
ATOM    184  N  ATYR A  17      34.418  26.425  23.962  0.53 42.68           N  
ANISOU  184  N  ATYR A  17     6535   4699   4983      4    -16   -235       N  
ATOM    185  N  BTYR A  17      31.332  28.375  24.190  0.47 36.05           N  
ANISOU  185  N  BTYR A  17     5598   4041   4060   -133    198   -196       N  
ATOM    186  CA ATYR A  17      35.333  27.087  23.033  0.53 41.57           C  
ANISOU  186  CA ATYR A  17     6312   4605   4876     80    -17   -292       C  
ATOM    187  CA BTYR A  17      31.728  29.481  23.330  0.47 38.70           C  
ANISOU  187  CA BTYR A  17     5853   4439   4412    -71    220   -239       C  
ATOM    188  C  ATYR A  17      35.448  28.578  23.349  0.53 40.74           C  
ANISOU  188  C  ATYR A  17     6163   4578   4739     87     39   -287       C  
ATOM    189  C  BTYR A  17      33.238  29.590  23.205  0.47 35.68           C  
ANISOU  189  C  BTYR A  17     5474   4031   4051     -1    166   -260       C  
ATOM    190  O  ATYR A  17      36.556  29.139  23.391  0.53 35.54           O  
ANISOU  190  O  ATYR A  17     5480   3935   4087    139     17   -311       O  
ATOM    191  O  BTYR A  17      33.776  30.666  22.927  0.47 26.43           O  
ANISOU  191  O  BTYR A  17     4257   2909   2877     40    184   -282       O  
ATOM    192  CB ATYR A  17      34.877  26.896  21.576  0.53 40.55           C  
ANISOU  192  CB ATYR A  17     6117   4506   4785     88      6   -337       C  
ATOM    193  CB BTYR A  17      31.098  30.777  23.826  0.47 33.08           C  
ANISOU  193  CB BTYR A  17     5111   3801   3655    -85    285   -229       C  
ATOM    194  CG ATYR A  17      34.687  25.463  21.093  0.53 32.87           C  
ANISOU  194  CG ATYR A  17     5181   3460   3847     82    -48   -350       C  
ATOM    195  CG BTYR A  17      29.604  30.723  23.627  0.47 39.73           C  
ANISOU  195  CG BTYR A  17     5921   4686   4487   -142    340   -230       C  
ATOM    196  CD1ATYR A  17      35.118  24.389  21.840  0.53 37.18           C  
ANISOU  196  CD1ATYR A  17     5819   3913   4396     82   -126   -328       C  
ATOM    197  CD1BTYR A  17      29.062  30.766  22.351  0.47 44.89           C  
ANISOU  197  CD1BTYR A  17     6510   5372   5175   -128    355   -271       C  
ATOM    198  CD2ATYR A  17      34.073  25.199  19.861  0.53 27.93           C  
ANISOU  198  CD2ATYR A  17     4506   2856   3250     78    -27   -384       C  
ATOM    199  CD2BTYR A  17      28.739  30.566  24.697  0.47 38.90           C  
ANISOU  199  CD2BTYR A  17     5850   4592   4338   -211    375   -195       C  
ATOM    200  CE1ATYR A  17      34.933  23.081  21.392  0.53 39.28           C  
ANISOU  200  CE1ATYR A  17     6129   4103   4692     77   -182   -340       C  
ATOM    201  CE1BTYR A  17      27.691  30.687  22.151  0.47 45.06           C  
ANISOU  201  CE1BTYR A  17     6494   5436   5191   -178    400   -280       C  
ATOM    202  CE2ATYR A  17      33.894  23.907  19.403  0.53 27.52           C  
ANISOU  202  CE2ATYR A  17     4491   2735   3230     72    -79   -398       C  
ATOM    203  CE2BTYR A  17      27.361  30.492  24.499  0.47 38.15           C  
ANISOU  203  CE2BTYR A  17     5713   4546   4236   -266    427   -205       C  
ATOM    204  CZ ATYR A  17      34.330  22.852  20.174  0.53 34.27           C  
ANISOU  204  CZ ATYR A  17     5440   3493   4087     71   -157   -375       C  
ATOM    205  CZ BTYR A  17      26.850  30.553  23.226  0.47 35.07           C  
ANISOU  205  CZ BTYR A  17     5253   4188   3885   -246    437   -249       C  
ATOM    206  OH ATYR A  17      34.157  21.560  19.744  0.53 37.04           O  
ANISOU  206  OH ATYR A  17     5839   3767   4467     66   -216   -388       O  
ATOM    207  OH BTYR A  17      25.492  30.486  23.011  0.47 34.83           O  
ANISOU  207  OH BTYR A  17     5173   4210   3851   -297    483   -266       O  
ATOM    208  N  ASER A  18      34.310  29.249  23.557  0.53 37.39           N  
ANISOU  208  N  ASER A  18     5724   4202   4279     35    109   -261       N  
ATOM    209  N  BSER A  18      33.917  28.455  23.352  0.47 38.50           N  
ANISOU  209  N  BSER A  18     5883   4311   4433     13     96   -259       N  
ATOM    210  CA ASER A  18      34.374  30.666  23.900  0.53 33.66           C  
ANISOU  210  CA ASER A  18     5220   3796   3773     45    156   -258       C  
ATOM    211  CA BSER A  18      35.370  28.406  23.408  0.47 40.68           C  
ANISOU  211  CA BSER A  18     6165   4560   4731     81     34   -283       C  
ATOM    212  C  ASER A  18      35.186  30.881  25.169  0.53 35.36           C  
ANISOU  212  C  ASER A  18     5493   3983   3960     56    122   -228       C  
ATOM    213  C  BSER A  18      35.898  29.399  24.438  0.47 36.12           C  
ANISOU  213  C  BSER A  18     5603   4006   4115     90     43   -260       C  
ATOM    214  O  ASER A  18      36.119  31.697  25.192  0.53 38.63           O  
ANISOU  214  O  ASER A  18     5881   4423   4374     99    113   -247       O  
ATOM    215  O  BSER A  18      36.843  30.145  24.178  0.47 33.14           O  
ANISOU  215  O  BSER A  18     5181   3663   3748    140     37   -291       O  
ATOM    216  CB ASER A  18      32.983  31.265  24.077  0.53 33.09           C  
ANISOU  216  CB ASER A  18     5130   3777   3665     -7    228   -238       C  
ATOM    217  CB BSER A  18      35.981  28.663  22.028  0.47 39.73           C  
ANISOU  217  CB BSER A  18     5963   4478   4654    138     35   -347       C  
ATOM    218  OG ASER A  18      33.144  32.579  24.609  0.53 28.78           O  
ANISOU  218  OG ASER A  18     4573   3280   3083      7    259   -232       O  
ATOM    219  OG BSER A  18      35.377  27.842  21.047  0.47 38.30           O  
ANISOU  219  OG BSER A  18     5767   4282   4504    127     32   -369       O  
ATOM    220  N  AASP A  19      34.843  30.149  26.232  0.53 37.55           N  
ANISOU  220  N  AASP A  19     5851   4207   4208     11    102   -182       N  
ATOM    221  N  BASP A  19      35.239  29.418  25.607  0.47 36.08           N  
ANISOU  221  N  BASP A  19     5661   3987   4062     36     61   -206       N  
ATOM    222  CA AASP A  19      35.562  30.225  27.499  0.53 37.83           C  
ANISOU  222  CA AASP A  19     5957   4206   4211     19     62   -151       C  
ATOM    223  CA BASP A  19      35.659  30.157  26.799  0.47 35.29           C  
ANISOU  223  CA BASP A  19     5598   3894   3917     37     61   -176       C  
ATOM    224  C  AASP A  19      37.075  30.171  27.302  0.53 33.78           C  
ANISOU  224  C  AASP A  19     5432   3667   3735     94     -9   -187       C  
ATOM    225  C  BASP A  19      37.172  30.167  26.935  0.47 33.27           C  
ANISOU  225  C  BASP A  19     5345   3610   3685    106     -9   -202       C  
ATOM    226  O  AASP A  19      37.805  31.068  27.738  0.53 36.88           O  
ANISOU  226  O  AASP A  19     5812   4088   4114    124    -13   -192       O  
ATOM    227  O  BASP A  19      37.775  31.184  27.299  0.47 34.99           O  
ANISOU  227  O  BASP A  19     5542   3865   3886    131     -1   -207       O  
ATOM    228  CB AASP A  19      35.117  29.086  28.429  0.53 40.37           C  
ANISOU  228  CB AASP A  19     6382   4453   4504    -38     30   -101       C  
ATOM    229  CB BASP A  19      35.058  29.534  28.065  0.47 40.99           C  
ANISOU  229  CB BASP A  19     6419   4567   4590    -27     54   -117       C  
ATOM    230  CG AASP A  19      33.684  29.241  28.925  0.53 48.28           C  
ANISOU  230  CG AASP A  19     7398   5490   5455   -124    106    -63       C  
ATOM    231  CG BASP A  19      33.575  29.793  28.200  0.47 46.16           C  
ANISOU  231  CG BASP A  19     7060   5270   5208   -100    136    -93       C  
ATOM    232  OD1AASP A  19      32.856  29.858  28.217  0.53 50.92           O  
ANISOU  232  OD1AASP A  19     7654   5897   5796   -136    174    -86       O  
ATOM    233  OD1BASP A  19      32.978  30.328  27.242  0.47 51.15           O  
ANISOU  233  OD1BASP A  19     7611   5965   5860    -96    188   -125       O  
ATOM    234  OD2AASP A  19      33.387  28.741  30.039  0.53 47.32           O  
ANISOU  234  OD2AASP A  19     7368   5327   5285   -180     97    -14       O  
ATOM    235  OD2BASP A  19      33.012  29.470  29.270  0.47 51.58           O  
ANISOU  235  OD2BASP A  19     7819   5935   5843   -164    148    -47       O  
ATOM    236  N  AILE A  20      37.566  29.123  26.637  0.53 28.27           N  
ANISOU  236  N  AILE A  20     4734   2920   3086    126    -68   -217       N  
ATOM    237  N  BILE A  20      37.779  29.021  26.632  0.47 26.85           N  
ANISOU  237  N  BILE A  20     4557   2731   2912    137    -82   -222       N  
ATOM    238  CA AILE A  20      39.002  28.860  26.659  0.53 30.96           C  
ANISOU  238  CA AILE A  20     5074   3229   3460    198   -148   -254       C  
ATOM    239  CA BILE A  20      39.223  28.861  26.730  0.47 31.21           C  
ANISOU  239  CA BILE A  20     5107   3257   3494    208   -159   -258       C  
ATOM    240  C  AILE A  20      39.767  29.977  25.958  0.53 29.50           C  
ANISOU  240  C  AILE A  20     4791   3123   3294    243   -119   -304       C  
ATOM    241  C  BILE A  20      39.941  29.982  25.989  0.47 29.74           C  
ANISOU  241  C  BILE A  20     4821   3152   3328    250   -127   -308       C  
ATOM    242  O  AILE A  20      40.788  30.456  26.464  0.53 32.69           O  
ANISOU  242  O  AILE A  20     5190   3534   3696    279   -153   -317       O  
ATOM    243  O  BILE A  20      40.960  30.503  26.457  0.47 33.68           O  
ANISOU  243  O  BILE A  20     5310   3662   3825    287   -158   -323       O  
ATOM    244  CB AILE A  20      39.313  27.473  26.053  0.53 38.08           C  
ANISOU  244  CB AILE A  20     5996   4063   4410    229   -219   -284       C  
ATOM    245  CB BILE A  20      39.621  27.463  26.207  0.47 38.44           C  
ANISOU  245  CB BILE A  20     6047   4100   4457    243   -237   -288       C  
ATOM    246  CG1AILE A  20      40.798  27.335  25.738  0.53 38.50           C  
ANISOU  246  CG1AILE A  20     6010   4110   4508    317   -291   -348       C  
ATOM    247  CG1BILE A  20      41.068  27.429  25.736  0.47 39.20           C  
ANISOU  247  CG1BILE A  20     6089   4205   4602    331   -299   -358       C  
ATOM    248  CG2AILE A  20      38.533  27.231  24.799  0.53 42.52           C  
ANISOU  248  CG2AILE A  20     6502   4653   4999    211   -173   -309       C  
ATOM    249  CG2BILE A  20      38.707  27.029  25.089  0.47 41.61           C  
ANISOU  249  CG2BILE A  20     6412   4515   4882    216   -196   -303       C  
ATOM    250  CD1AILE A  20      41.652  27.247  26.985  0.53 41.46           C  
ANISOU  250  CD1AILE A  20     6453   4435   4865    345   -365   -330       C  
ATOM    251  CD1BILE A  20      42.046  27.187  26.863  0.47 43.46           C  
ANISOU  251  CD1BILE A  20     6692   4689   5133    370   -385   -351       C  
ATOM    252  N  AGLY A  21      39.280  30.424  24.801  0.53 28.50           N  
ANISOU  252  N  AGLY A  21     4591   3056   3182    235    -59   -331       N  
ATOM    253  N  BGLY A  21      39.406  30.393  24.838  0.47 28.67           N  
ANISOU  253  N  BGLY A  21     4614   3074   3206    240    -66   -334       N  
ATOM    254  CA AGLY A  21      39.979  31.468  24.065  0.53 27.66           C  
ANISOU  254  CA AGLY A  21     4402   3021   3088    265    -30   -376       C  
ATOM    255  CA BGLY A  21      40.036  31.462  24.074  0.47 27.75           C  
ANISOU  255  CA BGLY A  21     4413   3032   3100    268    -33   -378       C  
ATOM    256  C  AGLY A  21      40.040  32.786  24.815  0.53 27.14           C  
ANISOU  256  C  AGLY A  21     4339   2997   2977    249      5   -350       C  
ATOM    257  C  BGLY A  21      40.075  32.785  24.818  0.47 27.15           C  
ANISOU  257  C  BGLY A  21     4339   2997   2978    251      4   -351       C  
ATOM    258  O  AGLY A  21      41.040  33.506  24.746  0.53 26.35           O  
ANISOU  258  O  AGLY A  21     4200   2931   2882    277     -4   -380       O  
ATOM    259  O  BGLY A  21      41.069  33.515  24.754  0.47 26.27           O  
ANISOU  259  O  BGLY A  21     4190   2921   2872    278     -5   -380       O  
ATOM    260  N  AASN A  22      38.975  33.117  25.547  0.53 26.22           N  
ANISOU  260  N  AASN A  22     4267   2881   2816    203     46   -299       N  
ATOM    261  N  BASN A  22      38.998  33.112  25.534  0.47 26.19           N  
ANISOU  261  N  BASN A  22     4262   2876   2812    203     45   -300       N  
ATOM    262  CA AASN A  22      38.992  34.340  26.343  0.53 23.75           C  
ANISOU  262  CA AASN A  22     3965   2602   2457    191     74   -275       C  
ATOM    263  CA BASN A  22      39.001  34.333  26.334  0.47 23.75           C  
ANISOU  263  CA BASN A  22     3965   2602   2458    192     74   -276       C  
ATOM    264  C  AASN A  22      40.035  34.252  27.450  0.53 27.17           C  
ANISOU  264  C  AASN A  22     4445   2998   2882    215     12   -265       C  
ATOM    265  C  BASN A  22      40.038  34.249  27.446  0.47 27.17           C  
ANISOU  265  C  BASN A  22     4445   2998   2882    215     12   -265       C  
ATOM    266  O  AASN A  22      40.754  35.225  27.714  0.53 26.52           O  
ANISOU  266  O  AASN A  22     4343   2947   2787    231     11   -276       O  
ATOM    267  O  BASN A  22      40.750  35.226  27.717  0.47 26.55           O  
ANISOU  267  O  BASN A  22     4347   2951   2791    231     11   -276       O  
ATOM    268  CB AASN A  22      37.597  34.613  26.902  0.53 25.42           C  
ANISOU  268  CB AASN A  22     4210   2825   2622    140    130   -231       C  
ATOM    269  CB BASN A  22      37.602  34.594  26.892  0.47 25.45           C  
ANISOU  269  CB BASN A  22     4214   2829   2627    140    129   -231       C  
ATOM    270  CG AASN A  22      36.610  35.013  25.810  0.53 25.43           C  
ANISOU  270  CG AASN A  22     4155   2877   2629    125    190   -250       C  
ATOM    271  CG BASN A  22      36.615  35.003  25.805  0.47 25.46           C  
ANISOU  271  CG BASN A  22     4160   2881   2634    125    190   -250       C  
ATOM    272  OD1AASN A  22      36.963  35.740  24.885  0.53 24.24           O  
ANISOU  272  OD1AASN A  22     3949   2767   2493    148    206   -285       O  
ATOM    273  OD1BASN A  22      36.968  35.737  24.885  0.47 24.24           O  
ANISOU  273  OD1BASN A  22     3949   2767   2493    148    206   -285       O  
ATOM    274  ND2AASN A  22      35.384  34.509  25.894  0.53 28.03           N  
ANISOU  274  ND2AASN A  22     4499   3203   2947     83    221   -228       N  
ATOM    275  ND2BASN A  22      35.388  34.504  25.890  0.47 27.81           N  
ANISOU  275  ND2BASN A  22     4472   3176   2920     83    221   -229       N  
ATOM    276  N   ILE A  23      40.164  33.072  28.069  1.00 24.72           N  
ANISOU  276  N   ILE A  23     4198   2616   2577    218    -47   -246       N  
ATOM    277  CA  ILE A  23      41.149  32.873  29.115  1.00 33.84           C  
ANISOU  277  CA  ILE A  23     5406   3726   3724    247   -120   -238       C  
ATOM    278  C   ILE A  23      42.557  32.980  28.545  1.00 30.42           C  
ANISOU  278  C   ILE A  23     4907   3311   3340    309   -168   -301       C  
ATOM    279  O   ILE A  23      43.419  33.656  29.117  1.00 31.24           O  
ANISOU  279  O   ILE A  23     5005   3431   3435    330   -193   -311       O  
ATOM    280  CB  ILE A  23      40.928  31.512  29.805  1.00 36.77           C  
ANISOU  280  CB  ILE A  23     5873   4008   4090    235   -180   -204       C  
ATOM    281  CG1 ILE A  23      39.528  31.453  30.414  1.00 37.66           C  
ANISOU  281  CG1 ILE A  23     6046   4115   4147    161   -123   -143       C  
ATOM    282  CG2 ILE A  23      41.969  31.296  30.902  1.00 28.88           C  
ANISOU  282  CG2 ILE A  23     4936   2956   3080    272   -267   -197       C  
ATOM    283  CD1 ILE A  23      39.275  32.546  31.410  1.00 38.84           C  
ANISOU  283  CD1 ILE A  23     6220   4301   4237    136    -82   -110       C  
ATOM    284  N   ILE A  24      42.807  32.290  27.426  1.00 25.97           N  
ANISOU  284  N   ILE A  24     4291   2749   2829    336   -182   -349       N  
ATOM    285  CA  ILE A  24      44.073  32.395  26.708  1.00 25.36           C  
ANISOU  285  CA  ILE A  24     4133   2706   2798    390   -214   -421       C  
ATOM    286  C   ILE A  24      44.403  33.862  26.418  1.00 24.84           C  
ANISOU  286  C   ILE A  24     4002   2722   2714    375   -156   -437       C  
ATOM    287  O   ILE A  24      45.521  34.314  26.659  1.00 25.39           O  
ANISOU  287  O   ILE A  24     4039   2815   2794    402   -188   -470       O  
ATOM    288  CB  ILE A  24      44.019  31.578  25.409  1.00 25.43           C  
ANISOU  288  CB  ILE A  24     4091   2717   2853    411   -214   -469       C  
ATOM    289  CG1 ILE A  24      44.069  30.051  25.668  1.00 31.66           C  
ANISOU  289  CG1 ILE A  24     4943   3416   3669    442   -297   -470       C  
ATOM    290  CG2 ILE A  24      45.187  31.917  24.523  1.00 27.03           C  
ANISOU  290  CG2 ILE A  24     4194   2982   3094    453   -219   -548       C  
ATOM    291  CD1 ILE A  24      43.836  29.241  24.360  1.00 26.18           C  
ANISOU  291  CD1 ILE A  24     4206   2723   3018    459   -293   -515       C  
ATOM    292  N   ALA A  25      43.437  34.624  25.898  1.00 24.26           N  
ANISOU  292  N   ALA A  25     3913   2690   2614    331    -76   -415       N  
ATOM    293  CA  ALA A  25      43.743  36.016  25.530  1.00 23.83           C  
ANISOU  293  CA  ALA A  25     3808   2705   2541    315    -27   -431       C  
ATOM    294  C   ALA A  25      44.165  36.826  26.749  1.00 24.92           C  
ANISOU  294  C   ALA A  25     3984   2840   2643    310    -45   -403       C  
ATOM    295  O   ALA A  25      45.131  37.601  26.688  1.00 27.48           O  
ANISOU  295  O   ALA A  25     4268   3204   2971    317    -52   -435       O  
ATOM    296  CB  ALA A  25      42.547  36.662  24.827  1.00 23.28           C  
ANISOU  296  CB  ALA A  25     3731   2670   2446    276     50   -411       C  
ATOM    297  N   LEU A  26      43.473  36.638  27.876  1.00 24.66           N  
ANISOU  297  N   LEU A  26     4032   2762   2574    295    -53   -347       N  
ATOM    298  CA  LEU A  26      43.831  37.349  29.100  1.00 27.55           C  
ANISOU  298  CA  LEU A  26     4444   3122   2902    292    -74   -321       C  
ATOM    299  C   LEU A  26      45.207  36.932  29.605  1.00 29.42           C  
ANISOU  299  C   LEU A  26     4677   3334   3167    336   -158   -352       C  
ATOM    300  O   LEU A  26      46.009  37.776  30.018  1.00 27.18           O  
ANISOU  300  O   LEU A  26     4378   3076   2874    341   -173   -366       O  
ATOM    301  CB  LEU A  26      42.773  37.111  30.185  1.00 24.21           C  
ANISOU  301  CB  LEU A  26     4110   2658   2429    263    -62   -257       C  
ATOM    302  CG  LEU A  26      41.452  37.883  30.083  1.00 36.86           C  
ANISOU  302  CG  LEU A  26     5719   4298   3990    221     19   -228       C  
ATOM    303  CD1 LEU A  26      40.302  37.213  30.856  1.00 34.37           C  
ANISOU  303  CD1 LEU A  26     5474   3947   3638    187     35   -178       C  
ATOM    304  CD2 LEU A  26      41.635  39.309  30.588  1.00 23.51           C  
ANISOU  304  CD2 LEU A  26     4033   2642   2259    216     39   -222       C  
ATOM    305  N   ARG A  27      45.471  35.621  29.651  1.00 25.89           N  
ANISOU  305  N   ARG A  27     4250   2833   2753    369   -219   -364       N  
ATOM    306  CA  ARG A  27      46.779  35.142  30.101  1.00 25.76           C  
ANISOU  306  CA  ARG A  27     4228   2790   2768    423   -311   -403       C  
ATOM    307  C   ARG A  27      47.906  35.769  29.291  1.00 25.71           C  
ANISOU  307  C   ARG A  27     4114   2856   2800    444   -308   -476       C  
ATOM    308  O   ARG A  27      48.935  36.175  29.848  1.00 26.03           O  
ANISOU  308  O   ARG A  27     4137   2908   2845    466   -355   -502       O  
ATOM    309  CB  ARG A  27      46.841  33.601  30.011  1.00 26.33           C  
ANISOU  309  CB  ARG A  27     4335   2794   2876    461   -380   -415       C  
ATOM    310  CG  ARG A  27      48.208  33.034  30.362  1.00 40.67           C  
ANISOU  310  CG  ARG A  27     6138   4582   4732    531   -486   -469       C  
ATOM    311  CD  ARG A  27      48.168  31.790  31.307  1.00 43.60           C  
ANISOU  311  CD  ARG A  27     6623   4847   5096    560   -582   -439       C  
ATOM    312  NE  ARG A  27      46.996  30.933  31.140  1.00 44.79           N  
ANISOU  312  NE  ARG A  27     6842   4943   5232    524   -560   -392       N  
ATOM    313  CZ  ARG A  27      46.373  30.325  32.150  1.00 45.68           C  
ANISOU  313  CZ  ARG A  27     7080   4976   5300    496   -592   -325       C  
ATOM    314  NH1 ARG A  27      46.806  30.479  33.392  1.00 39.74           N  
ANISOU  314  NH1 ARG A  27     6403   4185   4511    506   -650   -298       N  
ATOM    315  NH2 ARG A  27      45.311  29.565  31.926  1.00 52.94           N  
ANISOU  315  NH2 ARG A  27     8053   5854   6207    454   -566   -286       N  
ATOM    316  N   GLN A  28      47.727  35.874  27.972  1.00 25.38           N  
ANISOU  316  N   GLN A  28     3998   2864   2781    431   -252   -510       N  
ATOM    317  CA  GLN A  28      48.833  36.274  27.110  1.00 25.50           C  
ANISOU  317  CA  GLN A  28     3909   2949   2831    446   -248   -585       C  
ATOM    318  C   GLN A  28      49.036  37.790  27.119  1.00 30.01           C  
ANISOU  318  C   GLN A  28     4453   3581   3368    400   -196   -579       C  
ATOM    319  O   GLN A  28      50.180  38.258  27.090  1.00 28.77           O  
ANISOU  319  O   GLN A  28     4236   3469   3228    407   -217   -629       O  
ATOM    320  CB  GLN A  28      48.595  35.773  25.685  1.00 26.36           C  
ANISOU  320  CB  GLN A  28     3956   3088   2972    449   -210   -626       C  
ATOM    321  CG  GLN A  28      48.657  34.249  25.542  1.00 31.30           C  
ANISOU  321  CG  GLN A  28     4595   3657   3641    503   -275   -652       C  
ATOM    322  CD  GLN A  28      50.039  33.705  25.860  1.00 37.10           C  
ANISOU  322  CD  GLN A  28     5291   4388   4419    570   -365   -720       C  
ATOM    323  OE1 GLN A  28      51.048  34.217  25.377  1.00 36.59           O  
ANISOU  323  OE1 GLN A  28     5133   4396   4375    578   -358   -786       O  
ATOM    324  NE2 GLN A  28      50.090  32.681  26.682  1.00 33.03           N  
ANISOU  324  NE2 GLN A  28     4847   3787   3914    615   -452   -705       N  
ATOM    325  N   ARG A  29      47.956  38.578  27.177  1.00 27.24           N  
ANISOU  325  N   ARG A  29     4148   3233   2969    352   -131   -522       N  
ATOM    326  CA  ARG A  29      48.147  40.034  27.288  1.00 24.27           C  
ANISOU  326  CA  ARG A  29     3764   2901   2556    311    -94   -514       C  
ATOM    327  C   ARG A  29      48.741  40.408  28.643  1.00 30.61           C  
ANISOU  327  C   ARG A  29     4610   3681   3341    322   -147   -497       C  
ATOM    328  O   ARG A  29      49.486  41.392  28.746  1.00 30.29           O  
ANISOU  328  O   ARG A  29     4541   3679   3289    301   -146   -517       O  
ATOM    329  CB  ARG A  29      46.823  40.783  27.086  1.00 23.66           C  
ANISOU  329  CB  ARG A  29     3731   2827   2432    270    -24   -463       C  
ATOM    330  CG  ARG A  29      46.087  40.631  25.737  1.00 26.33           C  
ANISOU  330  CG  ARG A  29     4036   3190   2779    254     33   -474       C  
ATOM    331  CD  ARG A  29      46.700  41.354  24.568  1.00 27.95           C  
ANISOU  331  CD  ARG A  29     4173   3458   2988    227     69   -520       C  
ATOM    332  NE  ARG A  29      46.717  42.839  24.664  1.00 24.92           N  
ANISOU  332  NE  ARG A  29     3810   3102   2558    184    100   -503       N  
ATOM    333  CZ  ARG A  29      47.222  43.594  23.691  1.00 29.57           C  
ANISOU  333  CZ  ARG A  29     4356   3741   3138    146    132   -536       C  
ATOM    334  NH1 ARG A  29      47.726  42.994  22.605  1.00 23.27           N  
ANISOU  334  NH1 ARG A  29     3488   2979   2373    149    144   -588       N  
ATOM    335  NH2 ARG A  29      47.246  44.916  23.779  1.00 22.94           N  
ANISOU  335  NH2 ARG A  29     3546   2916   2254    104    153   -519       N  
ATOM    336  N   ALA A  30      48.423  39.646  29.694  1.00 24.81           N  
ANISOU  336  N   ALA A  30     3948   2880   2597    348   -196   -460       N  
ATOM    337  CA  ALA A  30      49.034  39.899  31.003  1.00 27.82           C  
ANISOU  337  CA  ALA A  30     4377   3235   2960    364   -256   -446       C  
ATOM    338  C   ALA A  30      50.501  39.490  31.025  1.00 33.79           C  
ANISOU  338  C   ALA A  30     5071   4003   3765    408   -332   -514       C  
ATOM    339  O   ALA A  30      51.338  40.171  31.628  1.00 26.06           O  
ANISOU  339  O   ALA A  30     4082   3041   2780    408   -365   -530       O  
ATOM    340  CB  ALA A  30      48.281  39.154  32.099  1.00 25.35           C  
ANISOU  340  CB  ALA A  30     4168   2847   2616    374   -288   -387       C  
ATOM    341  N   LYS A  31      50.823  38.369  30.384  1.00 31.45           N  
ANISOU  341  N   LYS A  31     4732   3698   3520    449   -364   -558       N  
ATOM    342  CA  LYS A  31      52.202  37.901  30.332  1.00 32.22           C  
ANISOU  342  CA  LYS A  31     4759   3813   3670    502   -439   -635       C  
ATOM    343  C   LYS A  31      53.110  38.940  29.691  1.00 29.54           C  
ANISOU  343  C   LYS A  31     4316   3564   3342    471   -404   -693       C  
ATOM    344  O   LYS A  31      54.241  39.149  30.145  1.00 30.53           O  
ANISOU  344  O   LYS A  31     4399   3713   3487    493   -461   -740       O  
ATOM    345  CB  LYS A  31      52.252  36.583  29.561  1.00 29.17           C  
ANISOU  345  CB  LYS A  31     4341   3408   3334    550   -468   -678       C  
ATOM    346  CG  LYS A  31      53.556  35.881  29.594  1.00 35.94           C  
ANISOU  346  CG  LYS A  31     5136   4271   4247    621   -559   -762       C  
ATOM    347  CD  LYS A  31      53.367  34.378  29.233  1.00 37.62           C  
ANISOU  347  CD  LYS A  31     5369   4426   4499    680   -613   -784       C  
ATOM    348  CE  LYS A  31      54.622  33.880  28.542  1.00 39.70           C  
ANISOU  348  CE  LYS A  31     5516   4741   4827    744   -663   -897       C  
ATOM    349  NZ  LYS A  31      54.700  32.394  28.427  1.00 43.75           N  
ANISOU  349  NZ  LYS A  31     6056   5186   5382    822   -748   -931       N  
ATOM    350  N   LYS A  32      52.625  39.607  28.643  1.00 29.62           N  
ANISOU  350  N   LYS A  32     4290   3628   3338    417   -314   -690       N  
ATOM    351  CA  LYS A  32      53.376  40.691  28.009  1.00 28.17           C  
ANISOU  351  CA  LYS A  32     4025   3528   3152    369   -271   -734       C  
ATOM    352  C   LYS A  32      53.628  41.856  28.956  1.00 33.13           C  
ANISOU  352  C   LYS A  32     4691   4156   3739    334   -279   -704       C  
ATOM    353  O   LYS A  32      54.534  42.655  28.713  1.00 36.41           O  
ANISOU  353  O   LYS A  32     5042   4634   4159    299   -270   -748       O  
ATOM    354  CB  LYS A  32      52.610  41.170  26.785  1.00 36.89           C  
ANISOU  354  CB  LYS A  32     5112   4669   4234    316   -177   -721       C  
ATOM    355  CG  LYS A  32      52.281  40.051  25.791  1.00 36.09           C  
ANISOU  355  CG  LYS A  32     4976   4566   4169    348   -165   -750       C  
ATOM    356  CD  LYS A  32      53.288  39.947  24.691  1.00 43.97           C  
ANISOU  356  CD  LYS A  32     5858   5645   5203    345   -150   -840       C  
ATOM    357  CE  LYS A  32      52.692  39.255  23.408  1.00 44.09           C  
ANISOU  357  CE  LYS A  32     5847   5672   5234    351   -105   -859       C  
ATOM    358  NZ  LYS A  32      51.963  37.972  23.687  1.00 39.58           N  
ANISOU  358  NZ  LYS A  32     5331   5022   4684    409   -148   -833       N  
ATOM    359  N   ARG A  33      52.848  41.966  30.027  1.00 32.49           N  
ANISOU  359  N   ARG A  33     4716   4011   3619    339   -295   -632       N  
ATOM    360  CA  ARG A  33      53.023  42.974  31.059  1.00 26.05           C  
ANISOU  360  CA  ARG A  33     3950   3185   2762    316   -312   -601       C  
ATOM    361  C   ARG A  33      53.640  42.382  32.320  1.00 26.63           C  
ANISOU  361  C   ARG A  33     4062   3210   2848    371   -409   -604       C  
ATOM    362  O   ARG A  33      53.515  42.969  33.401  1.00 27.47           O  
ANISOU  362  O   ARG A  33     4241   3286   2912    362   -432   -563       O  
ATOM    363  CB  ARG A  33      51.676  43.639  31.372  1.00 25.40           C  
ANISOU  363  CB  ARG A  33     3960   3071   2618    282   -255   -523       C  
ATOM    364  CG  ARG A  33      51.263  44.791  30.438  1.00 29.52           C  
ANISOU  364  CG  ARG A  33     4464   3640   3112    220   -175   -517       C  
ATOM    365  CD  ARG A  33      51.117  44.410  28.963  1.00 34.59           C  
ANISOU  365  CD  ARG A  33     5038   4322   3782    207   -124   -550       C  
ATOM    366  NE  ARG A  33      50.384  45.435  28.199  1.00 37.15           N  
ANISOU  366  NE  ARG A  33     5380   4668   4066    153    -52   -527       N  
ATOM    367  CZ  ARG A  33      49.146  45.291  27.714  1.00 36.13           C  
ANISOU  367  CZ  ARG A  33     5286   4522   3919    152     -5   -492       C  
ATOM    368  NH1 ARG A  33      48.470  44.141  27.895  1.00 27.51           N  
ANISOU  368  NH1 ARG A  33     4213   3392   2846    192    -16   -474       N  
ATOM    369  NH2 ARG A  33      48.578  46.294  27.038  1.00 28.17           N  
ANISOU  369  NH2 ARG A  33     4297   3534   2874    108     48   -477       N  
ATOM    370  N   ASN A  34      54.244  41.191  32.210  1.00 28.11           N  
ANISOU  370  N   ASN A  34     4209   3383   3087    431   -473   -653       N  
ATOM    371  CA  ASN A  34      54.942  40.555  33.328  1.00 32.07           C  
ANISOU  371  CA  ASN A  34     4745   3836   3604    492   -581   -666       C  
ATOM    372  C   ASN A  34      53.994  40.291  34.492  1.00 27.72           C  
ANISOU  372  C   ASN A  34     4333   3199   2999    498   -602   -581       C  
ATOM    373  O   ASN A  34      54.298  40.556  35.652  1.00 28.03           O  
ANISOU  373  O   ASN A  34     4434   3205   3011    510   -659   -561       O  
ATOM    374  CB  ASN A  34      56.150  41.392  33.755  1.00 34.86           C  
ANISOU  374  CB  ASN A  34     5043   4236   3966    484   -621   -714       C  
ATOM    375  CG  ASN A  34      57.229  41.402  32.683  1.00 40.49           C  
ANISOU  375  CG  ASN A  34     5611   5038   4737    483   -613   -812       C  
ATOM    376  OD1 ASN A  34      57.716  42.453  32.252  1.00 36.18           O  
ANISOU  376  OD1 ASN A  34     4999   4563   4183    423   -567   -839       O  
ATOM    377  ND2 ASN A  34      57.578  40.211  32.217  1.00 33.55           N  
ANISOU  377  ND2 ASN A  34     4682   4155   3910    546   -655   -867       N  
ATOM    378  N   ILE A  35      52.820  39.781  34.170  1.00 37.84           N  
ANISOU  378  N   ILE A  35     5666   4449   4264    485   -552   -532       N  
ATOM    379  CA  ILE A  35      51.811  39.440  35.156  1.00 34.69           C  
ANISOU  379  CA  ILE A  35     5393   3977   3811    480   -558   -453       C  
ATOM    380  C   ILE A  35      51.412  38.006  34.890  1.00 30.35           C  
ANISOU  380  C   ILE A  35     4872   3373   3287    513   -587   -449       C  
ATOM    381  O   ILE A  35      51.088  37.656  33.751  1.00 27.15           O  
ANISOU  381  O   ILE A  35     4409   2995   2913    507   -540   -471       O  
ATOM    382  CB  ILE A  35      50.579  40.364  35.066  1.00 33.77           C  
ANISOU  382  CB  ILE A  35     5313   3879   3638    418   -457   -395       C  
ATOM    383  CG1 ILE A  35      50.978  41.820  35.373  1.00 26.27           C  
ANISOU  383  CG1 ILE A  35     4349   2973   2659    386   -438   -398       C  
ATOM    384  CG2 ILE A  35      49.437  39.830  35.958  1.00 26.44           C  
ANISOU  384  CG2 ILE A  35     4503   2886   2656    408   -452   -321       C  
ATOM    385  CD1 ILE A  35      49.879  42.855  34.956  1.00 25.55           C  
ANISOU  385  CD1 ILE A  35     4272   2912   2523    332   -339   -360       C  
ATOM    386  N   LYS A  36      51.465  37.181  35.918  1.00 28.01           N  
ANISOU  386  N   LYS A  36     4670   2998   2974    547   -669   -422       N  
ATOM    387  CA  LYS A  36      51.044  35.786  35.806  1.00 33.25           C  
ANISOU  387  CA  LYS A  36     5386   3594   3653    572   -707   -409       C  
ATOM    388  C   LYS A  36      49.563  35.677  36.146  1.00 34.75           C  
ANISOU  388  C   LYS A  36     5671   3750   3782    514   -640   -325       C  
ATOM    389  O   LYS A  36      49.089  36.294  37.103  1.00 38.82           O  
ANISOU  389  O   LYS A  36     6260   4255   4235    480   -619   -271       O  
ATOM    390  CB  LYS A  36      51.863  34.904  36.748  1.00 35.46           C  
ANISOU  390  CB  LYS A  36     5733   3798   3943    636   -840   -423       C  
ATOM    391  CG  LYS A  36      51.395  33.439  36.800  1.00 43.36           C  
ANISOU  391  CG  LYS A  36     6819   4709   4947    659   -893   -400       C  
ATOM    392  CD  LYS A  36      52.262  32.615  37.753  1.00 48.58           C  
ANISOU  392  CD  LYS A  36     7558   5287   5614    728  -1038   -416       C  
ATOM    393  N   VAL A  37      48.823  34.912  35.357  1.00 32.22           N  
ANISOU  393  N   VAL A  37     5346   3416   3480    502   -605   -318       N  
ATOM    394  CA  VAL A  37      47.389  34.774  35.581  1.00 29.21           C  
ANISOU  394  CA  VAL A  37     5040   3013   3046    441   -537   -246       C  
ATOM    395  C   VAL A  37      47.114  33.416  36.211  1.00 32.16           C  
ANISOU  395  C   VAL A  37     5526   3290   3405    448   -606   -211       C  
ATOM    396  O   VAL A  37      47.628  32.394  35.749  1.00 38.06           O  
ANISOU  396  O   VAL A  37     6262   3996   4203    495   -675   -248       O  
ATOM    397  CB  VAL A  37      46.602  34.979  34.278  1.00 34.55           C  
ANISOU  397  CB  VAL A  37     5637   3745   3744    409   -441   -258       C  
ATOM    398  CG1 VAL A  37      45.208  34.375  34.395  1.00 30.98           C  
ANISOU  398  CG1 VAL A  37     5256   3259   3255    358   -394   -199       C  
ATOM    399  CG2 VAL A  37      46.560  36.477  33.920  1.00 26.16           C  
ANISOU  399  CG2 VAL A  37     4506   2767   2668    383   -364   -268       C  
ATOM    400  N   ASN A  38      46.355  33.417  37.300  1.00 29.63           N  
ANISOU  400  N   ASN A  38     5317   2930   3011    402   -594   -141       N  
ATOM    401  CA  ASN A  38      45.911  32.215  37.994  1.00 33.95           C  
ANISOU  401  CA  ASN A  38     5992   3383   3525    385   -647    -92       C  
ATOM    402  C   ASN A  38      44.425  32.026  37.728  1.00 39.76           C  
ANISOU  402  C   ASN A  38     6751   4130   4225    306   -549    -43       C  
ATOM    403  O   ASN A  38      43.617  32.896  38.066  1.00 41.17           O  
ANISOU  403  O   ASN A  38     6931   4360   4352    254   -462    -10       O  
ATOM    404  CB  ASN A  38      46.146  32.344  39.499  1.00 43.11           C  
ANISOU  404  CB  ASN A  38     7270   4493   4616    380   -703    -48       C  
ATOM    405  CG  ASN A  38      47.614  32.444  39.855  1.00 53.72           C  
ANISOU  405  CG  ASN A  38     8597   5819   5994    460   -812    -98       C  
ATOM    406  OD1 ASN A  38      48.435  31.637  39.409  1.00 53.84           O  
ANISOU  406  OD1 ASN A  38     8588   5798   6071    524   -900   -149       O  
ATOM    407  ND2 ASN A  38      47.953  33.433  40.666  1.00 52.14           N  
ANISOU  407  ND2 ASN A  38     8408   5646   5755    458   -812    -90       N  
ATOM    408  N   VAL A  39      44.053  30.896  37.150  1.00 32.82           N  
ANISOU  408  N   VAL A  39     5892   3205   3375    299   -566    -42       N  
ATOM    409  CA  VAL A  39      42.651  30.619  36.856  1.00 36.89           C  
ANISOU  409  CA  VAL A  39     6423   3731   3861    221   -479     -1       C  
ATOM    410  C   VAL A  39      42.122  29.619  37.876  1.00 36.03           C  
ANISOU  410  C   VAL A  39     6467   3531   3690    169   -519     65       C  
ATOM    411  O   VAL A  39      42.654  28.513  38.009  1.00 38.49           O  
ANISOU  411  O   VAL A  39     6853   3752   4021    199   -621     63       O  
ATOM    412  CB  VAL A  39      42.464  30.114  35.416  1.00 37.83           C  
ANISOU  412  CB  VAL A  39     6455   3867   4050    235   -458    -43       C  
ATOM    413  CG1 VAL A  39      41.004  29.877  35.147  1.00 33.07           C  
ANISOU  413  CG1 VAL A  39     5865   3281   3419    153   -370     -4       C  
ATOM    414  CG2 VAL A  39      42.998  31.153  34.444  1.00 32.90           C  
ANISOU  414  CG2 VAL A  39     5690   3334   3475    277   -416   -104       C  
ATOM    415  N   VAL A  40      41.085  30.022  38.605  1.00 39.92           N  
ANISOU  415  N   VAL A  40     7011   4049   4106     89   -441    120       N  
ATOM    416  CA  VAL A  40      40.362  29.189  39.561  1.00 37.73           C  
ANISOU  416  CA  VAL A  40     6877   3704   3754     12   -450    187       C  
ATOM    417  C   VAL A  40      39.017  28.837  38.941  1.00 36.37           C  
ANISOU  417  C   VAL A  40     6679   3564   3577    -69   -357    205       C  
ATOM    418  O   VAL A  40      38.177  29.715  38.710  1.00 36.27           O  
ANISOU  418  O   VAL A  40     6589   3643   3548   -105   -249    202       O  
ATOM    419  CB  VAL A  40      40.162  29.909  40.902  1.00 39.03           C  
ANISOU  419  CB  VAL A  40     7117   3885   3828    -26   -424    231       C  
ATOM    420  CG1 VAL A  40      39.354  29.022  41.869  1.00 36.82           C  
ANISOU  420  CG1 VAL A  40     6990   3540   3461   -120   -424    303       C  
ATOM    421  CG2 VAL A  40      41.517  30.314  41.519  1.00 32.97           C  
ANISOU  421  CG2 VAL A  40     6371   3089   3067     56   -521    210       C  
ATOM    422  N   GLU A  41      38.802  27.563  38.662  1.00 34.34           N  
ANISOU  422  N   GLU A  41     6485   3229   3335    -94   -403    220       N  
ATOM    423  CA  GLU A  41      37.522  27.074  38.161  1.00 41.40           C  
ANISOU  423  CA  GLU A  41     7369   4142   4221   -181   -326    240       C  
ATOM    424  C   GLU A  41      36.591  26.779  39.324  1.00 48.47           C  
ANISOU  424  C   GLU A  41     8386   5017   5015   -292   -286    311       C  
ATOM    425  O   GLU A  41      36.932  25.994  40.212  1.00 49.80           O  
ANISOU  425  O   GLU A  41     8699   5087   5136   -313   -367    354       O  
ATOM    426  CB  GLU A  41      37.705  25.807  37.329  1.00 46.55           C  
ANISOU  426  CB  GLU A  41     8039   4714   4932   -163   -397    223       C  
ATOM    427  CG  GLU A  41      38.420  26.028  36.020  1.00 54.40           C  
ANISOU  427  CG  GLU A  41     8902   5744   6025    -68   -416    148       C  
ATOM    428  CD  GLU A  41      38.571  24.739  35.242  1.00 68.56           C  
ANISOU  428  CD  GLU A  41    10721   7457   7872    -49   -488    128       C  
ATOM    429  OE1 GLU A  41      39.649  24.111  35.320  1.00 74.06           O  
ANISOU  429  OE1 GLU A  41    11465   8074   8601     27   -606    104       O  
ATOM    430  OE2 GLU A  41      37.600  24.346  34.566  1.00 74.26           O  
ANISOU  430  OE2 GLU A  41    11416   8194   8604   -108   -431    133       O  
ATOM    431  N   ILE A  42      35.407  27.378  39.298  1.00 49.85           N  
ANISOU  431  N   ILE A  42     8502   5284   5153   -366   -163    319       N  
ATOM    432  CA  ILE A  42      34.454  27.292  40.396  1.00 46.71           C  
ANISOU  432  CA  ILE A  42     8196   4897   4653   -477   -103    377       C  
ATOM    433  C   ILE A  42      33.185  26.650  39.866  1.00 46.79           C  
ANISOU  433  C   ILE A  42     8186   4930   4661   -576    -30    387       C  
ATOM    434  O   ILE A  42      32.427  27.279  39.119  1.00 47.41           O  
ANISOU  434  O   ILE A  42     8136   5109   4770   -582     61    351       O  
ATOM    435  CB  ILE A  42      34.151  28.669  40.995  1.00 45.01           C  
ANISOU  435  CB  ILE A  42     7928   4786   4389   -477    -18    370       C  
ATOM    436  CG1 ILE A  42      35.432  29.292  41.525  1.00 44.39           C  
ANISOU  436  CG1 ILE A  42     7872   4680   4313   -384    -95    359       C  
ATOM    437  CG2 ILE A  42      33.099  28.545  42.098  1.00 38.03           C  
ANISOU  437  CG2 ILE A  42     7130   3924   3394   -598     55    422       C  
ATOM    438  CD1 ILE A  42      35.292  30.732  41.815  1.00 47.36           C  
ANISOU  438  CD1 ILE A  42     8173   5156   4664   -360    -23    337       C  
ATOM    439  N   ASN A  43      32.931  25.413  40.265  1.00 54.69           N  
ANISOU  439  N   ASN A  43     9550   5589   5640   -802    258   1161       N  
ATOM    440  CA  ASN A  43      31.682  24.764  39.908  1.00 63.85           C  
ANISOU  440  CA  ASN A  43    10686   6638   6935   -997    389   1161       C  
ATOM    441  C   ASN A  43      30.799  24.470  41.112  1.00 67.87           C  
ANISOU  441  C   ASN A  43    11304   7165   7318  -1183    567   1297       C  
ATOM    442  O   ASN A  43      29.585  24.323  40.942  1.00 66.18           O  
ANISOU  442  O   ASN A  43    11004   6942   7200  -1370    714   1268       O  
ATOM    443  CB  ASN A  43      31.957  23.471  39.129  1.00 62.02           C  
ANISOU  443  CB  ASN A  43    10566   6145   6853   -976    296   1204       C  
ATOM    444  CG  ASN A  43      32.657  23.737  37.798  1.00 64.62           C  
ANISOU  444  CG  ASN A  43    10767   6465   7321   -809    145   1051       C  
ATOM    445  OD1 ASN A  43      32.050  24.228  36.844  1.00 64.85           O  
ANISOU  445  OD1 ASN A  43    10599   6560   7482   -851    170    895       O  
ATOM    446  ND2 ASN A  43      33.939  23.419  37.735  1.00 65.57           N  
ANISOU  446  ND2 ASN A  43    10992   6517   7404   -612    -10   1102       N  
ATOM    447  N   GLU A  44      31.379  24.399  42.311  1.00 65.36           N  
ANISOU  447  N   GLU A  44    11164   6888   6782  -1136    559   1442       N  
ATOM    448  CA  GLU A  44      30.653  24.391  43.575  1.00 59.44           C  
ANISOU  448  CA  GLU A  44    10508   6219   5858  -1286    734   1562       C  
ATOM    449  C   GLU A  44      30.821  25.762  44.212  1.00 56.33           C  
ANISOU  449  C   GLU A  44    10019   6090   5294  -1227    765   1468       C  
ATOM    450  O   GLU A  44      31.951  26.188  44.480  1.00 59.62           O  
ANISOU  450  O   GLU A  44    10481   6581   5589  -1060    621   1462       O  
ATOM    451  CB  GLU A  44      31.185  23.309  44.512  1.00 65.55           C  
ANISOU  451  CB  GLU A  44    11568   6855   6483  -1272    703   1804       C  
ATOM    452  CG  GLU A  44      31.167  21.905  43.946  1.00 75.47           C  
ANISOU  452  CG  GLU A  44    12957   7812   7906  -1310    664   1908       C  
ATOM    453  CD  GLU A  44      32.517  21.229  44.048  0.63 79.31           C  
ANISOU  453  CD  GLU A  44    13595   8185   8353  -1093    468   2013       C  
ATOM    454  OE1 GLU A  44      33.462  21.683  43.361  0.73 77.26           O  
ANISOU  454  OE1 GLU A  44    13279   7951   8124   -913    305   1916       O  
ATOM    455  OE2 GLU A  44      32.631  20.252  44.820  0.83 82.14           O  
ANISOU  455  OE2 GLU A  44    14076   8459   8673  -1087    478   2176       O  
ATOM    456  N   THR A  45      29.711  26.455  44.451  1.00 47.54           N  
ANISOU  456  N   THR A  45     8770   5118   4174  -1362    952   1388       N  
ATOM    457  CA  THR A  45      29.781  27.847  44.872  1.00 48.10           C  
ANISOU  457  CA  THR A  45     8728   5422   4124  -1303    991   1257       C  
ATOM    458  C   THR A  45      29.574  28.062  46.362  1.00 53.41           C  
ANISOU  458  C   THR A  45     9537   6231   4524  -1368   1120   1352       C  
ATOM    459  O   THR A  45      29.747  29.196  46.820  1.00 57.45           O  
ANISOU  459  O   THR A  45     9988   6929   4910  -1311   1143   1239       O  
ATOM    460  CB  THR A  45      28.746  28.693  44.125  1.00 54.07           C  
ANISOU  460  CB  THR A  45     9223   6272   5049  -1368   1111   1078       C  
ATOM    461  OG1 THR A  45      27.440  28.156  44.362  1.00 60.40           O  
ANISOU  461  OG1 THR A  45    10003   7051   5896  -1571   1308   1143       O  
ATOM    462  CG2 THR A  45      29.051  28.734  42.607  1.00 45.95           C  
ANISOU  462  CG2 THR A  45     8041   5157   4262  -1275    968    956       C  
ATOM    463  N   GLU A  46      29.210  27.026  47.121  1.00 50.61           N  
ANISOU  463  N   GLU A  46     9368   5789   4072  -1485   1209   1552       N  
ATOM    464  CA  GLU A  46      28.818  27.217  48.514  1.00 59.16           C  
ANISOU  464  CA  GLU A  46    10545   7023   4911  -1556   1358   1633       C  
ATOM    465  C   GLU A  46      29.985  27.767  49.327  1.00 64.94           C  
ANISOU  465  C   GLU A  46    11365   7892   5417  -1390   1214   1625       C  
ATOM    466  O   GLU A  46      31.091  27.216  49.307  1.00 68.91           O  
ANISOU  466  O   GLU A  46    11983   8309   5889  -1260   1017   1714       O  
ATOM    467  CB  GLU A  46      28.310  25.899  49.118  1.00 57.44           C  
ANISOU  467  CB  GLU A  46    10432   6683   4709  -1659   1430   1833       C  
ATOM    468  N   GLY A  47      29.740  28.874  50.024  1.00 66.10           N  
ANISOU  468  N   GLY A  47    11440   8257   5419  -1388   1308   1504       N  
ATOM    469  CA  GLY A  47      30.783  29.525  50.797  1.00 67.57           C  
ANISOU  469  CA  GLY A  47    11682   8593   5397  -1250   1175   1460       C  
ATOM    470  C   GLY A  47      31.887  30.166  49.986  1.00 65.79           C  
ANISOU  470  C   GLY A  47    11421   8363   5214  -1112    977   1339       C  
ATOM    471  O   GLY A  47      32.977  30.391  50.511  1.00 71.44           O  
ANISOU  471  O   GLY A  47    12190   9162   5791   -988    811   1338       O  
ATOM    472  N   ILE A  48      31.645  30.462  48.718  1.00 58.31           N  
ANISOU  472  N   ILE A  48    10312   7334   4510  -1107    970   1218       N  
ATOM    473  CA  ILE A  48      32.645  31.120  47.884  1.00 59.87           C  
ANISOU  473  CA  ILE A  48    10391   7536   4821   -952    777   1078       C  
ATOM    474  C   ILE A  48      32.650  32.614  48.181  1.00 53.54           C  
ANISOU  474  C   ILE A  48     9479   6921   3944   -928    827    877       C  
ATOM    475  O   ILE A  48      31.598  33.262  48.210  1.00 54.58           O  
ANISOU  475  O   ILE A  48     9500   7121   4116  -1013   1020    775       O  
ATOM    476  CB  ILE A  48      32.371  30.857  46.395  1.00 60.60           C  
ANISOU  476  CB  ILE A  48    10319   7479   5229   -937    742   1016       C  
ATOM    477  CG1 ILE A  48      32.868  29.465  45.990  1.00 61.44           C  
ANISOU  477  CG1 ILE A  48    10549   7383   5411   -901    615   1182       C  
ATOM    478  CG2 ILE A  48      32.963  31.959  45.539  1.00 55.10           C  
ANISOU  478  CG2 ILE A  48     9439   6841   4656   -816    637    823       C  
ATOM    479  CD1 ILE A  48      34.279  29.158  46.430  1.00 63.12           C  
ANISOU  479  CD1 ILE A  48    10907   7597   5478   -752    409   1276       C  
ATOM    480  N   THR A  49      33.833  33.171  48.392  1.00 50.08           N  
ANISOU  480  N   THR A  49     9064   6562   3403   -811    655    817       N  
ATOM    481  CA  THR A  49      33.972  34.604  48.587  1.00 51.41           C  
ANISOU  481  CA  THR A  49     9134   6879   3522   -785    680    612       C  
ATOM    482  C   THR A  49      34.800  35.201  47.461  1.00 47.92           C  
ANISOU  482  C   THR A  49     8531   6396   3281   -666    519    486       C  
ATOM    483  O   THR A  49      35.571  34.498  46.793  1.00 42.16           O  
ANISOU  483  O   THR A  49     7805   5563   2652   -580    350    567       O  
ATOM    484  CB  THR A  49      34.635  34.937  49.922  1.00 67.29           C  
ANISOU  484  CB  THR A  49    11304   9050   5215   -776    629    619       C  
ATOM    485  OG1 THR A  49      34.915  36.339  49.949  1.00 72.77           O  
ANISOU  485  OG1 THR A  49    11895   9856   5899   -745    625    397       O  
ATOM    486  CG2 THR A  49      35.943  34.167  50.078  1.00 68.65           C  
ANISOU  486  CG2 THR A  49    11572   9196   5316   -666    383    754       C  
ATOM    487  N   PHE A  50      34.653  36.521  47.280  1.00 46.00           N  
ANISOU  487  N   PHE A  50     8155   6233   3090   -657    580    288       N  
ATOM    488  CA  PHE A  50      35.333  37.255  46.224  1.00 42.03           C  
ANISOU  488  CA  PHE A  50     7490   5700   2780   -558    461    161       C  
ATOM    489  C   PHE A  50      36.585  37.985  46.713  1.00 42.00           C  
ANISOU  489  C   PHE A  50     7517   5798   2642   -494    304     77       C  
ATOM    490  O   PHE A  50      37.081  38.880  46.017  1.00 42.73           O  
ANISOU  490  O   PHE A  50     7473   5891   2873   -435    243    -57       O  
ATOM    491  CB  PHE A  50      34.371  38.247  45.554  1.00 39.38           C  
ANISOU  491  CB  PHE A  50     6974   5363   2627   -581    625      7       C  
ATOM    492  CG  PHE A  50      33.360  37.589  44.676  1.00 40.97           C  
ANISOU  492  CG  PHE A  50     7081   5462   3023   -620    719     68       C  
ATOM    493  CD1 PHE A  50      33.631  37.366  43.326  1.00 39.50           C  
ANISOU  493  CD1 PHE A  50     6768   5174   3065   -545    616     65       C  
ATOM    494  CD2 PHE A  50      32.151  37.147  45.202  1.00 38.15           C  
ANISOU  494  CD2 PHE A  50     6763   5119   2615   -736    909    131       C  
ATOM    495  CE1 PHE A  50      32.691  36.723  42.501  1.00 40.40           C  
ANISOU  495  CE1 PHE A  50     6796   5203   3351   -591    689    110       C  
ATOM    496  CE2 PHE A  50      31.215  36.497  44.394  1.00 44.78           C  
ANISOU  496  CE2 PHE A  50     7505   5870   3638   -790    986    183       C  
ATOM    497  CZ  PHE A  50      31.491  36.290  43.029  1.00 43.37           C  
ANISOU  497  CZ  PHE A  50     7202   5591   3686   -717    868    166       C  
ATOM    498  N   ASP A  51      37.119  37.609  47.874  1.00 48.80           N  
ANISOU  498  N   ASP A  51     8551   6750   3239   -508    234    159       N  
ATOM    499  CA  ASP A  51      38.302  38.294  48.394  1.00 55.71           C  
ANISOU  499  CA  ASP A  51     9449   7744   3974   -461     74     71       C  
ATOM    500  C   ASP A  51      39.545  37.969  47.585  1.00 52.93           C  
ANISOU  500  C   ASP A  51     9023   7342   3746   -343   -157    115       C  
ATOM    501  O   ASP A  51      40.449  38.803  47.480  1.00 56.24           O  
ANISOU  501  O   ASP A  51     9363   7830   4177   -304   -275     -7       O  
ATOM    502  CB  ASP A  51      38.556  37.919  49.852  1.00 61.39           C  
ANISOU  502  CB  ASP A  51    10343   8593   4390   -492     43    157       C  
ATOM    503  CG  ASP A  51      37.327  38.024  50.705  1.00 73.33           C  
ANISOU  503  CG  ASP A  51    11908  10155   5798   -592    275    149       C  
ATOM    504  OD1 ASP A  51      36.359  38.684  50.272  1.00 78.10           O  
ANISOU  504  OD1 ASP A  51    12441  10727   6508   -650    460     31       O  
ATOM    505  OD2 ASP A  51      37.332  37.444  51.813  1.00 77.81           O  
ANISOU  505  OD2 ASP A  51    12578  10803   6184   -604    274    264       O  
ATOM    506  N   GLU A  52      39.629  36.760  47.042  1.00 51.49           N  
ANISOU  506  N   GLU A  52     8868   7042   3654   -288   -220    284       N  
ATOM    507  CA  GLU A  52      40.784  36.370  46.255  1.00 53.79           C  
ANISOU  507  CA  GLU A  52     9089   7284   4064   -161   -426    330       C  
ATOM    508  C   GLU A  52      40.551  36.556  44.767  1.00 52.25           C  
ANISOU  508  C   GLU A  52     8715   6968   4169   -118   -397    262       C  
ATOM    509  O   GLU A  52      41.400  36.160  43.965  1.00 55.90           O  
ANISOU  509  O   GLU A  52     9111   7377   4752     -7   -543    302       O  
ATOM    510  CB  GLU A  52      41.173  34.921  46.554  1.00 57.56           C  
ANISOU  510  CB  GLU A  52     9718   7698   4454   -100   -531    554       C  
ATOM    511  CG  GLU A  52      41.885  34.756  47.890  1.00 69.64           C  
ANISOU  511  CG  GLU A  52    11368   9376   5717    -87   -635    630       C  
ATOM    512  CD  GLU A  52      42.972  35.808  48.114  1.00 80.83           C  
ANISOU  512  CD  GLU A  52    12655  10954   7101    -49   -770    481       C  
ATOM    513  OE1 GLU A  52      44.051  35.709  47.493  1.00 84.90           O  
ANISOU  513  OE1 GLU A  52    13061  11468   7731     61   -939    488       O  
ATOM    514  OE2 GLU A  52      42.747  36.743  48.910  1.00 83.88           O  
ANISOU  514  OE2 GLU A  52    13041  11471   7359   -134   -700    350       O  
ATOM    515  N   CYS A  53      39.438  37.172  44.381  1.00 41.10           N  
ANISOU  515  N   CYS A  53     7218   5526   2871   -193   -213    161       N  
ATOM    516  CA  CYS A  53      39.094  37.348  42.980  1.00 36.99           C  
ANISOU  516  CA  CYS A  53     6530   4906   2618   -154   -177    104       C  
ATOM    517  C   CYS A  53      39.567  38.715  42.488  1.00 37.10           C  
ANISOU  517  C   CYS A  53     6390   4976   2731   -120   -198    -66       C  
ATOM    518  O   CYS A  53      39.348  39.732  43.155  1.00 42.73           O  
ANISOU  518  O   CYS A  53     7106   5773   3358   -182   -116   -184       O  
ATOM    519  CB  CYS A  53      37.586  37.197  42.788  1.00 37.80           C  
ANISOU  519  CB  CYS A  53     6612   4950   2799   -249     27    103       C  
ATOM    520  SG  CYS A  53      37.063  37.298  41.086  1.00 42.46           S  
ANISOU  520  SG  CYS A  53     7003   5436   3692   -204     63     47       S  
ATOM    521  N   ASP A  54      40.231  38.732  41.328  1.00 31.35           N  
ANISOU  521  N   ASP A  54     5534   4196   2182    -23   -302    -77       N  
ATOM    522  CA  ASP A  54      40.582  39.968  40.625  1.00 32.96           C  
ANISOU  522  CA  ASP A  54     5577   4423   2523      8   -303   -217       C  
ATOM    523  C   ASP A  54      39.676  40.250  39.432  1.00 30.24           C  
ANISOU  523  C   ASP A  54     5095   3999   2395     20   -184   -260       C  
ATOM    524  O   ASP A  54      39.320  41.408  39.187  1.00 30.04           O  
ANISOU  524  O   ASP A  54     4973   3990   2451      3    -88   -378       O  
ATOM    525  CB  ASP A  54      42.041  39.902  40.159  1.00 27.65           C  
ANISOU  525  CB  ASP A  54     4841   3774   1891    111   -499   -200       C  
ATOM    526  CG  ASP A  54      43.018  39.941  41.320  1.00 35.86           C  
ANISOU  526  CG  ASP A  54     5974   4928   2722    100   -628   -190       C  
ATOM    527  OD1 ASP A  54      42.912  40.878  42.167  1.00 37.64           O  
ANISOU  527  OD1 ASP A  54     6231   5237   2835     16   -576   -301       O  
ATOM    528  OD2 ASP A  54      43.875  39.020  41.410  1.00 35.63           O  
ANISOU  528  OD2 ASP A  54     5993   4910   2636    180   -784    -73       O  
ATOM    529  N   ILE A  55      39.296  39.205  38.698  1.00 27.13           N  
ANISOU  529  N   ILE A  55     4698   3519   2093     51   -192   -166       N  
ATOM    530  CA  ILE A  55      38.413  39.254  37.532  1.00 28.35           C  
ANISOU  530  CA  ILE A  55     4726   3609   2435     62   -102   -191       C  
ATOM    531  C   ILE A  55      37.568  37.985  37.549  1.00 32.65           C  
ANISOU  531  C   ILE A  55     5354   4079   2974     10    -57    -89       C  
ATOM    532  O   ILE A  55      38.101  36.895  37.784  1.00 26.61           O  
ANISOU  532  O   ILE A  55     4705   3263   2143     34   -159     18       O  
ATOM    533  CB  ILE A  55      39.204  39.292  36.205  1.00 25.20           C  
ANISOU  533  CB  ILE A  55     4201   3179   2193    181   -212   -200       C  
ATOM    534  CG1 ILE A  55      40.267  40.402  36.189  1.00 25.88           C  
ANISOU  534  CG1 ILE A  55     4212   3332   2290    228   -281   -279       C  
ATOM    535  CG2 ILE A  55      38.236  39.414  34.993  1.00 22.99           C  
ANISOU  535  CG2 ILE A  55     3789   2855   2090    193   -121   -232       C  
ATOM    536  CD1 ILE A  55      41.210  40.298  34.984  1.00 23.08           C  
ANISOU  536  CD1 ILE A  55     3745   2960   2064    347   -397   -264       C  
ATOM    537  N   PHE A  56      36.265  38.097  37.285  1.00 28.20           N  
ANISOU  537  N   PHE A  56     4728   3501   2485    -61     94   -117       N  
ATOM    538  CA  PHE A  56      35.484  36.873  37.114  1.00 31.27           C  
ANISOU  538  CA  PHE A  56     5171   3808   2902   -123    129    -28       C  
ATOM    539  C   PHE A  56      35.004  36.733  35.676  1.00 31.69           C  
ANISOU  539  C   PHE A  56     5078   3813   3151    -86    129    -62       C  
ATOM    540  O   PHE A  56      34.935  37.702  34.915  1.00 27.61           O  
ANISOU  540  O   PHE A  56     4408   3342   2740    -30    151   -149       O  
ATOM    541  CB  PHE A  56      34.288  36.813  38.069  1.00 29.95           C  
ANISOU  541  CB  PHE A  56     5062   3673   2646   -260    301    -10       C  
ATOM    542  CG  PHE A  56      33.254  37.883  37.826  1.00 32.78           C  
ANISOU  542  CG  PHE A  56     5267   4099   3088   -292    459   -117       C  
ATOM    543  CD1 PHE A  56      32.230  37.687  36.927  1.00 36.91           C  
ANISOU  543  CD1 PHE A  56     5660   4601   3765   -321    531   -130       C  
ATOM    544  CD2 PHE A  56      33.310  39.076  38.515  1.00 35.35           C  
ANISOU  544  CD2 PHE A  56     5581   4512   3339   -289    533   -207       C  
ATOM    545  CE1 PHE A  56      31.276  38.675  36.708  1.00 41.03           C  
ANISOU  545  CE1 PHE A  56     6030   5194   4366   -331    673   -218       C  
ATOM    546  CE2 PHE A  56      32.368  40.060  38.309  1.00 41.83           C  
ANISOU  546  CE2 PHE A  56     6267   5382   4243   -299    684   -301       C  
ATOM    547  CZ  PHE A  56      31.346  39.858  37.403  1.00 43.37           C  
ANISOU  547  CZ  PHE A  56     6323   5563   4594   -312    754   -299       C  
ATOM    548  N   PHE A  57      34.616  35.513  35.333  1.00 25.04           N  
ANISOU  548  N   PHE A  57     4288   2876   2349   -126    111      9       N  
ATOM    549  CA  PHE A  57      34.191  35.166  33.987  1.00 28.67           C  
ANISOU  549  CA  PHE A  57     4633   3288   2974   -101     91    -23       C  
ATOM    550  C   PHE A  57      33.053  34.159  34.042  1.00 32.82           C  
ANISOU  550  C   PHE A  57     5199   3744   3529   -236    171     24       C  
ATOM    551  O   PHE A  57      33.175  33.128  34.715  1.00 31.05           O  
ANISOU  551  O   PHE A  57     5141   3429   3226   -294    152    122       O  
ATOM    552  CB  PHE A  57      35.344  34.564  33.177  1.00 31.94           C  
ANISOU  552  CB  PHE A  57     5073   3630   3433     27    -76     -2       C  
ATOM    553  CG  PHE A  57      34.941  34.166  31.786  1.00 34.97           C  
ANISOU  553  CG  PHE A  57     5353   3971   3964     55   -101    -46       C  
ATOM    554  CD1 PHE A  57      34.971  35.091  30.753  1.00 27.72           C  
ANISOU  554  CD1 PHE A  57     4260   3131   3141    138   -106   -130       C  
ATOM    555  CD2 PHE A  57      34.487  32.883  31.514  1.00 41.82           C  
ANISOU  555  CD2 PHE A  57     6300   4720   4870    -10   -116     -6       C  
ATOM    556  CE1 PHE A  57      34.579  34.730  29.466  1.00 31.16           C  
ANISOU  556  CE1 PHE A  57     4602   3548   3691    165   -134   -173       C  
ATOM    557  CE2 PHE A  57      34.094  32.521  30.225  1.00 41.95           C  
ANISOU  557  CE2 PHE A  57     6222   4707   5011      7   -146    -66       C  
ATOM    558  CZ  PHE A  57      34.143  33.456  29.201  1.00 35.77           C  
ANISOU  558  CZ  PHE A  57     5262   4025   4304     98   -158   -150       C  
ATOM    559  N   ILE A  58      31.976  34.425  33.295  1.00 32.86           N  
ANISOU  559  N   ILE A  58     5047   3788   3652   -285    252    -40       N  
ATOM    560  CA  ILE A  58      30.828  33.519  33.184  1.00 31.67           C  
ANISOU  560  CA  ILE A  58     4894   3584   3557   -428    325    -13       C  
ATOM    561  C   ILE A  58      30.504  33.358  31.708  1.00 31.98           C  
ANISOU  561  C   ILE A  58     4787   3615   3748   -393    267    -84       C  
ATOM    562  O   ILE A  58      30.009  34.297  31.073  1.00 30.27           O  
ANISOU  562  O   ILE A  58     4388   3509   3605   -353    310   -160       O  
ATOM    563  CB  ILE A  58      29.595  34.037  33.935  1.00 33.47           C  
ANISOU  563  CB  ILE A  58     5053   3907   3757   -554    509    -22       C  
ATOM    564  CG1 ILE A  58      29.998  34.552  35.318  1.00 29.79           C  
ANISOU  564  CG1 ILE A  58     4706   3489   3122   -557    568     15       C  
ATOM    565  CG2 ILE A  58      28.499  32.927  34.014  1.00 34.11           C  
ANISOU  565  CG2 ILE A  58     5154   3924   3882   -731    585     29       C  
ATOM    566  CD1 ILE A  58      28.863  35.163  36.127  1.00 39.78           C  
ANISOU  566  CD1 ILE A  58     5911   4861   4344   -660    764     -5       C  
ATOM    567  N   GLY A  59      30.765  32.175  31.161  1.00 32.31           N  
ANISOU  567  N   GLY A  59     4916   3528   3833   -402    172    -60       N  
ATOM    568  CA  GLY A  59      30.481  31.890  29.771  1.00 27.21           C  
ANISOU  568  CA  GLY A  59     4154   2873   3312   -376    107   -137       C  
ATOM    569  C   GLY A  59      29.036  31.477  29.576  1.00 29.62           C  
ANISOU  569  C   GLY A  59     4368   3194   3694   -548    198   -162       C  
ATOM    570  O   GLY A  59      28.195  31.579  30.470  1.00 36.07           O  
ANISOU  570  O   GLY A  59     5178   4050   4478   -678    329   -124       O  
ATOM    571  N   GLY A  60      28.747  30.982  28.382  1.00 30.73           N  
ANISOU  571  N   GLY A  60     4431   3312   3933   -552    126   -232       N  
ATOM    572  CA  GLY A  60      27.403  30.564  28.037  1.00 38.59           C  
ANISOU  572  CA  GLY A  60     5313   4335   5013   -719    187   -273       C  
ATOM    573  C   GLY A  60      27.314  29.075  27.746  1.00 42.26           C  
ANISOU  573  C   GLY A  60     5911   4620   5526   -833    126   -272       C  
ATOM    574  O   GLY A  60      28.270  28.454  27.281  1.00 48.11           O  
ANISOU  574  O   GLY A  60     6779   5235   6264   -735      8   -280       O  
ATOM    575  N   GLY A  61      26.141  28.513  27.995  1.00 44.00           N  
ANISOU  575  N   GLY A  61     6094   4826   5799  -1041    213   -268       N  
ATOM    576  CA  GLY A  61      25.922  27.111  27.692  1.00 36.16           C  
ANISOU  576  CA  GLY A  61     5220   3649   4872  -1179    167   -279       C  
ATOM    577  C   GLY A  61      24.570  26.914  27.058  1.00 41.95           C  
ANISOU  577  C   GLY A  61     5763   4464   5711  -1355    202   -365       C  
ATOM    578  O   GLY A  61      23.956  27.887  26.623  1.00 44.67           O  
ANISOU  578  O   GLY A  61     5876   5018   6080  -1320    231   -424       O  
ATOM    579  N   SER A  62      24.101  25.667  26.973  1.00 46.24           N  
ANISOU  579  N   SER A  62     6400   4845   6325  -1542    196   -374       N  
ATOM    580  CA  SER A  62      22.733  25.392  26.558  1.00 44.83           C  
ANISOU  580  CA  SER A  62     6040   4743   6249  -1755    241   -447       C  
ATOM    581  C   SER A  62      21.735  25.936  27.583  1.00 47.77           C  
ANISOU  581  C   SER A  62     6291   5254   6607  -1889    422   -368       C  
ATOM    582  O   SER A  62      22.075  26.251  28.726  1.00 43.89           O  
ANISOU  582  O   SER A  62     5909   4747   6020  -1855    518   -251       O  
ATOM    583  CB  SER A  62      22.522  23.896  26.409  1.00 46.27           C  
ANISOU  583  CB  SER A  62     6381   4687   6511  -1947    208   -465       C  
ATOM    584  OG  SER A  62      22.770  23.272  27.657  1.00 54.41           O  
ANISOU  584  OG  SER A  62     7640   5538   7497  -2031    302   -312       O  
ATOM    585  N   ASP A  63      20.471  26.023  27.173  1.00 52.28           N  
ANISOU  585  N   ASP A  63     6626   5969   7268  -2044    469   -437       N  
ATOM    586  CA  ASP A  63      19.461  26.536  28.091  1.00 57.73           C  
ANISOU  586  CA  ASP A  63     7175   6806   7952  -2165    652   -370       C  
ATOM    587  C   ASP A  63      19.389  25.701  29.363  1.00 52.65           C  
ANISOU  587  C   ASP A  63     6742   5991   7271  -2340    778   -233       C  
ATOM    588  O   ASP A  63      19.157  26.248  30.449  1.00 57.31           O  
ANISOU  588  O   ASP A  63     7329   6665   7782  -2349    930   -138       O  
ATOM    589  CB  ASP A  63      18.099  26.593  27.405  1.00 72.69           C  
ANISOU  589  CB  ASP A  63     8777   8878   9965  -2320    671   -465       C  
ATOM    590  CG  ASP A  63      18.162  27.278  26.063  1.00 83.44           C  
ANISOU  590  CG  ASP A  63     9946  10401  11356  -2152    530   -592       C  
ATOM    591  OD1 ASP A  63      18.097  28.529  26.027  1.00 80.71           O  
ANISOU  591  OD1 ASP A  63     9439  10252  10977  -1983    567   -590       O  
ATOM    592  OD2 ASP A  63      18.299  26.558  25.047  1.00 91.12           O  
ANISOU  592  OD2 ASP A  63    10942  11297  12381  -2186    384   -693       O  
ATOM    593  N   ARG A  64      19.599  24.386  29.253  1.00 49.48           N  
ANISOU  593  N   ARG A  64     6536   5347   6919  -2472    721   -219       N  
ATOM    594  CA  ARG A  64      19.667  23.543  30.441  1.00 56.39           C  
ANISOU  594  CA  ARG A  64     7645   6030   7749  -2616    831    -65       C  
ATOM    595  C   ARG A  64      20.872  23.912  31.288  1.00 50.52           C  
ANISOU  595  C   ARG A  64     7117   5229   6850  -2413    828     48       C  
ATOM    596  O   ARG A  64      20.747  24.136  32.495  1.00 48.10           O  
ANISOU  596  O   ARG A  64     6877   4956   6442  -2454    970    174       O  
ATOM    597  CB  ARG A  64      19.730  22.062  30.060  1.00 55.13           C  
ANISOU  597  CB  ARG A  64     7668   5591   7687  -2777    760    -77       C  
ATOM    598  CG  ARG A  64      18.726  21.190  30.797  1.00 77.30           C  
ANISOU  598  CG  ARG A  64    10509   8303  10558  -3091    914     14       C  
ATOM    599  CD  ARG A  64      19.274  19.787  31.123  1.00 84.64           C  
ANISOU  599  CD  ARG A  64    11770   8877  11511  -3186    890    108       C  
ATOM    600  NE  ARG A  64      20.689  19.664  30.778  1.00 86.04           N  
ANISOU  600  NE  ARG A  64    12156   8908  11629  -2927    732    100       N  
ATOM    601  CZ  ARG A  64      21.560  18.906  31.435  1.00 81.73           C  
ANISOU  601  CZ  ARG A  64    11918   8110  11025  -2873    722    239       C  
ATOM    602  NH1 ARG A  64      22.827  18.868  31.040  1.00 81.22           N  
ANISOU  602  NH1 ARG A  64    12001   7946  10913  -2622    575    219       N  
ATOM    603  NH2 ARG A  64      21.170  18.204  32.491  1.00 74.90           N  
ANISOU  603  NH2 ARG A  64    11208   7106  10146  -3063    864    407       N  
ATOM    604  N   GLU A  65      22.053  23.954  30.671  1.00 52.97           N  
ANISOU  604  N   GLU A  65     7533   5460   7133  -2197    665      3       N  
ATOM    605  CA  GLU A  65      23.258  24.284  31.414  1.00 47.60           C  
ANISOU  605  CA  GLU A  65     7041   4735   6311  -2003    640    103       C  
ATOM    606  C   GLU A  65      23.127  25.651  32.068  1.00 43.44           C  
ANISOU  606  C   GLU A  65     6379   4443   5682  -1910    740    121       C  
ATOM    607  O   GLU A  65      23.535  25.839  33.220  1.00 43.28           O  
ANISOU  607  O   GLU A  65     6499   4417   5529  -1879    813    238       O  
ATOM    608  CB  GLU A  65      24.470  24.232  30.486  1.00 53.82           C  
ANISOU  608  CB  GLU A  65     7903   5442   7104  -1781    452     31       C  
ATOM    609  CG  GLU A  65      24.891  22.821  30.064  1.00 62.57           C  
ANISOU  609  CG  GLU A  65     9220   6271   8283  -1828    357     32       C  
ATOM    610  CD  GLU A  65      26.026  22.819  29.026  1.00 65.98           C  
ANISOU  610  CD  GLU A  65     9693   6651   8725  -1597    180    -61       C  
ATOM    611  OE1 GLU A  65      26.190  23.828  28.282  1.00 52.95           O  
ANISOU  611  OE1 GLU A  65     7855   5195   7068  -1452    124   -162       O  
ATOM    612  OE2 GLU A  65      26.754  21.798  28.957  1.00 68.82           O  
ANISOU  612  OE2 GLU A  65    10274   6773   9100  -1557    105    -27       O  
ATOM    613  N   GLN A  66      22.536  26.612  31.352  1.00 40.84           N  
ANISOU  613  N   GLN A  66     5783   4324   5412  -1865    745      5       N  
ATOM    614  CA  GLN A  66      22.408  27.961  31.887  1.00 41.89           C  
ANISOU  614  CA  GLN A  66     5787   4665   5466  -1762    842      6       C  
ATOM    615  C   GLN A  66      21.490  27.978  33.097  1.00 44.60           C  
ANISOU  615  C   GLN A  66     6120   5071   5756  -1934   1046     96       C  
ATOM    616  O   GLN A  66      21.765  28.670  34.082  1.00 47.38           O  
ANISOU  616  O   GLN A  66     6529   5495   5978  -1864   1135    154       O  
ATOM    617  CB  GLN A  66      21.886  28.918  30.807  1.00 47.86           C  
ANISOU  617  CB  GLN A  66     6258   5616   6311  -1677    809   -125       C  
ATOM    618  CG  GLN A  66      22.961  29.662  30.047  1.00 50.94           C  
ANISOU  618  CG  GLN A  66     6639   6035   6679  -1428    668   -187       C  
ATOM    619  CD  GLN A  66      23.874  30.403  30.980  1.00 52.60           C  
ANISOU  619  CD  GLN A  66     6973   6255   6756  -1289    699   -123       C  
ATOM    620  OE1 GLN A  66      25.096  30.392  30.826  1.00 53.25           O  
ANISOU  620  OE1 GLN A  66     7189   6255   6788  -1141    581   -114       O  
ATOM    621  NE2 GLN A  66      23.284  31.038  31.980  1.00 53.16           N  
ANISOU  621  NE2 GLN A  66     6998   6434   6765  -1341    861    -84       N  
ATOM    622  N   ALA A  67      20.400  27.212  33.047  1.00 45.52           N  
ANISOU  622  N   ALA A  67     6163   5164   5967  -2166   1125    105       N  
ATOM    623  CA  ALA A  67      19.463  27.198  34.163  1.00 52.98           C  
ANISOU  623  CA  ALA A  67     7080   6183   6868  -2340   1337    194       C  
ATOM    624  C   ALA A  67      20.090  26.543  35.385  1.00 58.85           C  
ANISOU  624  C   ALA A  67     8124   6767   7469  -2380   1390    355       C  
ATOM    625  O   ALA A  67      19.883  26.998  36.518  1.00 57.41           O  
ANISOU  625  O   ALA A  67     7976   6679   7158  -2399   1545    434       O  
ATOM    626  CB  ALA A  67      18.183  26.477  33.753  1.00 55.22           C  
ANISOU  626  CB  ALA A  67     7203   6477   7300  -2593   1400    166       C  
ATOM    627  N   LEU A  68      20.859  25.472  35.168  1.00 54.76           N  
ANISOU  627  N   LEU A  68     7831   6010   6966  -2385   1265    404       N  
ATOM    628  CA  LEU A  68      21.638  24.870  36.244  1.00 50.63           C  
ANISOU  628  CA  LEU A  68     7607   5330   6299  -2375   1281    567       C  
ATOM    629  C   LEU A  68      22.665  25.852  36.803  1.00 47.67           C  
ANISOU  629  C   LEU A  68     7304   5053   5757  -2142   1241    581       C  
ATOM    630  O   LEU A  68      22.757  26.041  38.020  1.00 47.08           O  
ANISOU  630  O   LEU A  68     7347   5023   5520  -2154   1351    691       O  
ATOM    631  CB  LEU A  68      22.333  23.609  35.738  1.00 49.42           C  
ANISOU  631  CB  LEU A  68     7663   4898   6215  -2381   1136    600       C  
ATOM    632  CG  LEU A  68      21.466  22.451  35.231  1.00 55.21           C  
ANISOU  632  CG  LEU A  68     8386   5475   7116  -2627   1160    588       C  
ATOM    633  CD1 LEU A  68      22.308  21.488  34.387  1.00 59.36           C  
ANISOU  633  CD1 LEU A  68     9082   5747   7726  -2558    977    552       C  
ATOM    634  CD2 LEU A  68      20.789  21.708  36.379  1.00 57.14           C  
ANISOU  634  CD2 LEU A  68     8757   5634   7318  -2862   1343    759       C  
ATOM    635  N   ALA A  69      23.463  26.468  35.926  1.00 41.32           N  
ANISOU  635  N   ALA A  69     6433   4283   4982  -1935   1083    469       N  
ATOM    636  CA  ALA A  69      24.467  27.427  36.372  1.00 49.41           C  
ANISOU  636  CA  ALA A  69     7509   5398   5866  -1727   1034    468       C  
ATOM    637  C   ALA A  69      23.836  28.564  37.167  1.00 53.71           C  
ANISOU  637  C   ALA A  69     7930   6158   6320  -1738   1201    450       C  
ATOM    638  O   ALA A  69      24.428  29.073  38.131  1.00 50.33           O  
ANISOU  638  O   ALA A  69     7617   5783   5722  -1657   1230    500       O  
ATOM    639  CB  ALA A  69      25.222  27.984  35.164  1.00 48.46           C  
ANISOU  639  CB  ALA A  69     7287   5303   5824  -1530    863    340       C  
ATOM    640  N   THR A  70      22.638  28.990  36.771  1.00 53.06           N  
ANISOU  640  N   THR A  70     7608   6208   6344  -1832   1311    371       N  
ATOM    641  CA  THR A  70      22.005  30.100  37.469  1.00 55.19           C  
ANISOU  641  CA  THR A  70     7749   6680   6542  -1824   1480    342       C  
ATOM    642  C   THR A  70      21.553  29.682  38.861  1.00 51.19           C  
ANISOU  642  C   THR A  70     7378   6177   5894  -1976   1659    473       C  
ATOM    643  O   THR A  70      21.675  30.454  39.819  1.00 53.71           O  
ANISOU  643  O   THR A  70     7740   6611   6058  -1919   1760    485       O  
ATOM    644  CB  THR A  70      20.830  30.626  36.652  1.00 59.36           C  
ANISOU  644  CB  THR A  70     7971   7354   7228  -1869   1548    233       C  
ATOM    645  OG1 THR A  70      21.300  31.022  35.362  1.00 61.10           O  
ANISOU  645  OG1 THR A  70     8080   7577   7557  -1717   1379    124       O  
ATOM    646  CG2 THR A  70      20.195  31.821  37.343  1.00 65.09           C  
ANISOU  646  CG2 THR A  70     8561   8281   7889  -1832   1729    196       C  
ATOM    647  N   LYS A  71      21.039  28.461  38.994  1.00 49.55           N  
ANISOU  647  N   LYS A  71     7249   5845   5734  -2174   1705    572       N  
ATOM    648  CA  LYS A  71      20.623  27.985  40.308  1.00 51.69           C  
ANISOU  648  CA  LYS A  71     7663   6111   5865  -2326   1881    720       C  
ATOM    649  C   LYS A  71      21.815  27.879  41.256  1.00 51.33           C  
ANISOU  649  C   LYS A  71     7902   5995   5606  -2215   1820    829       C  
ATOM    650  O   LYS A  71      21.706  28.203  42.446  1.00 54.33           O  
ANISOU  650  O   LYS A  71     8369   6474   5800  -2237   1960    901       O  
ATOM    651  CB  LYS A  71      19.903  26.647  40.167  1.00 49.17           C  
ANISOU  651  CB  LYS A  71     7380   5642   5661  -2567   1930    810       C  
ATOM    652  CG  LYS A  71      19.088  26.233  41.396  1.00 60.20           C  
ANISOU  652  CG  LYS A  71     8845   7075   6952  -2769   2164    956       C  
ATOM    653  N   GLU A  72      22.965  27.442  40.748  1.00 45.57           N  
ANISOU  653  N   GLU A  72     7313   5109   4892  -2088   1611    839       N  
ATOM    654  CA  GLU A  72      24.164  27.400  41.581  1.00 59.90           C  
ANISOU  654  CA  GLU A  72     9372   6880   6509  -1961   1528    935       C  
ATOM    655  C   GLU A  72      24.708  28.802  41.847  1.00 52.46           C  
ANISOU  655  C   GLU A  72     8360   6120   5451  -1784   1507    828       C  
ATOM    656  O   GLU A  72      25.177  29.092  42.950  1.00 57.24           O  
ANISOU  656  O   GLU A  72     9112   6792   5844  -1742   1542    893       O  
ATOM    657  CB  GLU A  72      25.235  26.522  40.927  1.00 63.70           C  
ANISOU  657  CB  GLU A  72    10004   7146   7053  -1864   1313    975       C  
ATOM    658  CG  GLU A  72      26.466  26.271  41.797  1.00 71.31           C  
ANISOU  658  CG  GLU A  72    11223   8052   7819  -1740   1216   1103       C  
ATOM    659  CD  GLU A  72      26.228  25.247  42.909  1.00 83.25           C  
ANISOU  659  CD  GLU A  72    12967   9461   9205  -1881   1321   1316       C  
ATOM    660  OE1 GLU A  72      25.220  24.509  42.845  1.00 88.56           O  
ANISOU  660  OE1 GLU A  72    13622  10048   9979  -2083   1447   1371       O  
ATOM    661  OE2 GLU A  72      27.054  25.174  43.847  1.00 86.37           O  
ANISOU  661  OE2 GLU A  72    13558   9863   9395  -1793   1277   1434       O  
ATOM    662  N   LEU A  73      24.663  29.689  40.856  1.00 54.14           N  
ANISOU  662  N   LEU A  73     8359   6415   5797  -1681   1450    664       N  
ATOM    663  CA  LEU A  73      25.168  31.039  41.092  1.00 53.23           C  
ANISOU  663  CA  LEU A  73     8184   6450   5590  -1524   1439    560       C  
ATOM    664  C   LEU A  73      24.302  31.799  42.088  1.00 56.51           C  
ANISOU  664  C   LEU A  73     8543   7038   5890  -1594   1661    542       C  
ATOM    665  O   LEU A  73      24.812  32.661  42.810  1.00 48.77           O  
ANISOU  665  O   LEU A  73     7621   6157   4752  -1500   1676    502       O  
ATOM    666  CB  LEU A  73      25.272  31.806  39.777  1.00 47.83           C  
ANISOU  666  CB  LEU A  73     7287   5803   5082  -1399   1340    406       C  
ATOM    667  CG  LEU A  73      26.505  31.402  38.964  1.00 48.92           C  
ANISOU  667  CG  LEU A  73     7504   5810   5273  -1265   1110    403       C  
ATOM    668  CD1 LEU A  73      26.534  32.087  37.597  1.00 52.29           C  
ANISOU  668  CD1 LEU A  73     7719   6278   5871  -1154   1024    263       C  
ATOM    669  CD2 LEU A  73      27.781  31.686  39.741  1.00 49.21           C  
ANISOU  669  CD2 LEU A  73     7716   5851   5130  -1141   1016    443       C  
ATOM    670  N   SER A  74      23.008  31.470  42.178  1.00 61.12           N  
ANISOU  670  N   SER A  74     9018   7663   6543  -1763   1837    569       N  
ATOM    671  CA  SER A  74      22.137  32.189  43.103  1.00 58.43           C  
ANISOU  671  CA  SER A  74     8608   7496   6096  -1821   2066    548       C  
ATOM    672  C   SER A  74      22.506  31.942  44.562  1.00 55.09           C  
ANISOU  672  C   SER A  74     8432   7094   5407  -1860   2143    669       C  
ATOM    673  O   SER A  74      22.092  32.715  45.426  1.00 58.19           O  
ANISOU  673  O   SER A  74     8807   7642   5661  -1861   2310    629       O  
ATOM    674  CB  SER A  74      20.674  31.819  42.860  1.00 56.72           C  
ANISOU  674  CB  SER A  74     8203   7329   6019  -2001   2238    559       C  
ATOM    675  OG  SER A  74      20.433  30.475  43.236  1.00 68.00           O  
ANISOU  675  OG  SER A  74     9776   8631   7429  -2183   2273    720       O  
ATOM    676  N  ALYS A  75      23.279  30.889  44.850  0.47 54.81           N  
ANISOU  676  N  ALYS A  75     8629   6908   5290  -1882   2026    815       N  
ATOM    677  N  BLYS A  75      23.270  30.892  44.857  0.53 54.84           N  
ANISOU  677  N  BLYS A  75     8632   6913   5293  -1883   2028    815       N  
ATOM    678  CA ALYS A  75      23.777  30.665  46.203  0.47 55.18           C  
ANISOU  678  CA ALYS A  75     8922   6981   5063  -1891   2066    941       C  
ATOM    679  CA BLYS A  75      23.734  30.691  46.220  0.53 55.18           C  
ANISOU  679  CA BLYS A  75     8917   6988   5062  -1895   2075    938       C  
ATOM    680  C  ALYS A  75      24.723  31.770  46.655  0.47 54.24           C  
ANISOU  680  C  ALYS A  75     8854   6974   4779  -1718   1985    838       C  
ATOM    681  C  BLYS A  75      24.756  31.738  46.650  0.53 54.11           C  
ANISOU  681  C  BLYS A  75     8844   6954   4763  -1716   1978    842       C  
ATOM    682  O  ALYS A  75      24.968  31.911  47.857  0.47 57.95           O  
ANISOU  682  O  ALYS A  75     9487   7533   4997  -1722   2049    897       O  
ATOM    683  O  BLYS A  75      25.075  31.812  47.839  0.53 58.05           O  
ANISOU  683  O  BLYS A  75     9518   7529   5008  -1718   2028    910       O  
ATOM    684  CB ALYS A  75      24.486  29.307  46.287  0.47 56.41           C  
ANISOU  684  CB ALYS A  75     9310   6937   5188  -1920   1931   1124       C  
ATOM    685  CB BLYS A  75      24.307  29.280  46.359  0.53 56.76           C  
ANISOU  685  CB BLYS A  75     9346   6990   5231  -1946   1965   1131       C  
ATOM    686  CG ALYS A  75      23.558  28.103  46.219  0.47 58.22           C  
ANISOU  686  CG ALYS A  75     9558   7040   5522  -2130   2045   1260       C  
ATOM    687  CG BLYS A  75      23.283  28.192  46.048  0.53 58.35           C  
ANISOU  687  CG BLYS A  75     9511   7073   5587  -2152   2074   1231       C  
ATOM    688  CD ALYS A  75      24.303  26.814  45.872  0.47 57.70           C  
ANISOU  688  CD ALYS A  75     9684   6725   5514  -2126   1876   1397       C  
ATOM    689  CD BLYS A  75      23.912  26.819  45.896  0.53 58.13           C  
ANISOU  689  CD BLYS A  75     9697   6801   5590  -2180   1938   1394       C  
ATOM    690  CE ALYS A  75      25.283  26.383  46.962  0.47 57.44           C  
ANISOU  690  CE ALYS A  75     9932   6658   5235  -2048   1805   1564       C  
ATOM    691  CE BLYS A  75      22.874  25.787  45.449  0.53 56.54           C  
ANISOU  691  CE BLYS A  75     9435   6465   5581  -2392   2033   1458       C  
ATOM    692  NZ ALYS A  75      25.646  24.923  46.870  0.47 54.54           N  
ANISOU  692  NZ ALYS A  75     9737   6045   4941  -2071   1702   1734       N  
ATOM    693  NZ BLYS A  75      23.478  24.454  45.211  0.53 54.63           N  
ANISOU  693  NZ BLYS A  75     9393   5959   5405  -2401   1894   1594       N  
ATOM    694  N   ILE A  76      25.260  32.556  45.725  1.00 52.95           N  
ANISOU  694  N   ILE A  76     8557   6812   4748  -1572   1846    686       N  
ATOM    695  CA  ILE A  76      26.187  33.636  46.052  1.00 50.40           C  
ANISOU  695  CA  ILE A  76     8268   6581   4300  -1420   1761    575       C  
ATOM    696  C   ILE A  76      25.786  34.894  45.293  1.00 49.40           C  
ANISOU  696  C   ILE A  76     7901   6536   4331  -1341   1805    381       C  
ATOM    697  O   ILE A  76      26.643  35.694  44.899  1.00 49.72           O  
ANISOU  697  O   ILE A  76     7910   6585   4397  -1201   1673    272       O  
ATOM    698  CB  ILE A  76      27.641  33.257  45.726  1.00 48.14           C  
ANISOU  698  CB  ILE A  76     8107   6187   3997  -1296   1500    616       C  
ATOM    699  CG1 ILE A  76      27.724  32.724  44.295  1.00 47.01           C  
ANISOU  699  CG1 ILE A  76     7848   5899   4113  -1265   1372    604       C  
ATOM    700  CG2 ILE A  76      28.177  32.252  46.752  1.00 48.97           C  
ANISOU  700  CG2 ILE A  76     8475   6246   3886  -1336   1459    808       C  
ATOM    701  CD1 ILE A  76      29.082  32.886  43.647  1.00 39.00           C  
ANISOU  701  CD1 ILE A  76     6853   4826   3140  -1098   1136    562       C  
ATOM    702  N   LYS A  77      24.478  35.066  45.085  1.00 50.07           N  
ANISOU  702  N   LYS A  77     7812   6684   4530  -1429   1993    345       N  
ATOM    703  CA  LYS A  77      23.964  36.240  44.386  1.00 53.80           C  
ANISOU  703  CA  LYS A  77     8048   7236   5156  -1347   2054    179       C  
ATOM    704  C   LYS A  77      24.338  37.528  45.108  1.00 56.93           C  
ANISOU  704  C   LYS A  77     8479   7742   5408  -1245   2108     53       C  
ATOM    705  O   LYS A  77      24.605  38.557  44.477  1.00 52.91           O  
ANISOU  705  O   LYS A  77     7851   7245   5007  -1120   2059    -83       O  
ATOM    706  CB  LYS A  77      22.446  36.126  44.256  1.00 60.20           C  
ANISOU  706  CB  LYS A  77     8674   8121   6080  -1467   2263    182       C  
ATOM    707  CG  LYS A  77      21.735  37.363  43.743  1.00 65.79           C  
ANISOU  707  CG  LYS A  77     9137   8937   6922  -1379   2368     28       C  
ATOM    708  CD  LYS A  77      20.235  37.200  43.945  1.00 70.32           C  
ANISOU  708  CD  LYS A  77     9547   9617   7556  -1508   2601     50       C  
ATOM    709  CE  LYS A  77      19.780  35.828  43.479  1.00 73.65           C  
ANISOU  709  CE  LYS A  77     9949   9952   8083  -1672   2565    177       C  
ATOM    710  NZ  LYS A  77      18.387  35.507  43.878  1.00 77.98           N  
ANISOU  710  NZ  LYS A  77    10359  10601   8670  -1818   2773    224       N  
ATOM    711  N   THR A  78      24.369  37.492  46.422  1.00 59.92           N  
ANISOU  711  N   THR A  78     9028   8196   5541  -1300   2211     94       N  
ATOM    712  CA  THR A  78      24.524  38.745  47.139  1.00 57.06           C  
ANISOU  712  CA  THR A  78     8690   7947   5045  -1223   2295    -50       C  
ATOM    713  C   THR A  78      25.988  39.169  47.154  1.00 48.94           C  
ANISOU  713  C   THR A  78     7781   6877   3936  -1109   2077   -107       C  
ATOM    714  O   THR A  78      26.285  40.326  46.840  1.00 46.52           O  
ANISOU  714  O   THR A  78     7393   6589   3695  -1004   2057   -264       O  
ATOM    715  CB  THR A  78      23.931  38.628  48.539  1.00 56.37           C  
ANISOU  715  CB  THR A  78     8679   7963   4776  -1282   2434      0       C  
ATOM    716  OG1 THR A  78      22.510  38.716  48.435  1.00 57.01           O  
ANISOU  716  OG1 THR A  78     8559   8104   4997  -1327   2618     -8       O  
ATOM    717  CG2 THR A  78      24.453  39.732  49.443  1.00 56.25           C  
ANISOU  717  CG2 THR A  78     8732   8033   4608  -1178   2418   -133       C  
ATOM    718  N   PRO A  79      26.930  38.283  47.488  1.00 48.54           N  
ANISOU  718  N   PRO A  79     7916   6770   3756  -1124   1912     19       N  
ATOM    719  CA  PRO A  79      28.343  38.658  47.298  1.00 50.47           C  
ANISOU  719  CA  PRO A  79     8227   6979   3969  -1010   1684    -34       C  
ATOM    720  C   PRO A  79      28.701  39.029  45.863  1.00 48.81           C  
ANISOU  720  C   PRO A  79     7842   6677   4025   -909   1552   -109       C  
ATOM    721  O   PRO A  79      29.496  39.960  45.651  1.00 47.43           O  
ANISOU  721  O   PRO A  79     7641   6512   3870   -811   1456   -230       O  
ATOM    722  CB  PRO A  79      29.109  37.416  47.774  1.00 53.40           C  
ANISOU  722  CB  PRO A  79     8801   7297   4190  -1041   1540    150       C  
ATOM    723  CG  PRO A  79      28.063  36.332  47.949  1.00 53.20           C  
ANISOU  723  CG  PRO A  79     8800   7237   4177  -1175   1684    305       C  
ATOM    724  CD  PRO A  79      26.795  37.023  48.244  1.00 48.32           C  
ANISOU  724  CD  PRO A  79     8061   6726   3571  -1239   1940    214       C  
ATOM    725  N   LEU A  80      28.140  38.347  44.863  1.00 44.72           N  
ANISOU  725  N   LEU A  80     7205   6076   3712   -934   1546    -44       N  
ATOM    726  CA  LEU A  80      28.451  38.726  43.486  1.00 45.75           C  
ANISOU  726  CA  LEU A  80     7171   6137   4076   -833   1428   -115       C  
ATOM    727  C   LEU A  80      27.960  40.141  43.193  1.00 39.51           C  
ANISOU  727  C   LEU A  80     6215   5413   3384   -767   1542   -279       C  
ATOM    728  O   LEU A  80      28.693  40.961  42.636  1.00 40.89           O  
ANISOU  728  O   LEU A  80     6334   5565   3636   -658   1441   -372       O  
ATOM    729  CB  LEU A  80      27.854  37.722  42.492  1.00 44.19           C  
ANISOU  729  CB  LEU A  80     6878   5852   4062   -883   1406    -28       C  
ATOM    730  CG  LEU A  80      28.058  38.046  41.004  1.00 47.92           C  
ANISOU  730  CG  LEU A  80     7174   6269   4766   -782   1293    -96       C  
ATOM    731  CD1 LEU A  80      29.539  38.100  40.595  1.00 47.16           C  
ANISOU  731  CD1 LEU A  80     7143   6110   4664   -663   1074   -103       C  
ATOM    732  CD2 LEU A  80      27.313  37.062  40.133  1.00 47.65           C  
ANISOU  732  CD2 LEU A  80     7049   6169   4888   -853   1292    -30       C  
ATOM    733  N   LYS A  81      26.726  40.452  43.587  1.00 44.69           N  
ANISOU  733  N   LYS A  81     6793   6148   4040   -827   1763   -311       N  
ATOM    734  CA  LYS A  81      26.209  41.799  43.383  1.00 49.25           C  
ANISOU  734  CA  LYS A  81     7223   6782   4709   -749   1888   -461       C  
ATOM    735  C   LYS A  81      27.092  42.837  44.068  1.00 44.22           C  
ANISOU  735  C   LYS A  81     6696   6166   3938   -682   1859   -582       C  
ATOM    736  O   LYS A  81      27.458  43.854  43.464  1.00 37.53           O  
ANISOU  736  O   LYS A  81     5761   5287   3211   -577   1819   -693       O  
ATOM    737  CB  LYS A  81      24.775  41.895  43.899  1.00 55.41           C  
ANISOU  737  CB  LYS A  81     7918   7659   5476   -824   2142   -469       C  
ATOM    738  CG  LYS A  81      24.263  43.326  43.949  1.00 58.33           C  
ANISOU  738  CG  LYS A  81     8170   8088   5904   -730   2296   -627       C  
ATOM    739  CD  LYS A  81      23.108  43.534  42.996  1.00 59.04           C  
ANISOU  739  CD  LYS A  81     8004   8205   6223   -698   2397   -637       C  
ATOM    740  CE  LYS A  81      22.713  44.998  42.911  1.00 57.64           C  
ANISOU  740  CE  LYS A  81     7694   8044   6163   -545   2446   -757       C  
ATOM    741  NZ  LYS A  81      23.089  45.563  41.589  1.00 54.21           N  
ANISOU  741  NZ  LYS A  81     7132   7540   5925   -429   2347   -801       N  
ATOM    742  N   GLU A  82      27.453  42.588  45.331  1.00 43.77           N  
ANISOU  742  N   GLU A  82     6836   6165   3628   -746   1876   -559       N  
ATOM    743  CA  GLU A  82      28.303  43.530  46.053  1.00 45.45           C  
ANISOU  743  CA  GLU A  82     7163   6412   3694   -701   1838   -687       C  
ATOM    744  C   GLU A  82      29.663  43.663  45.385  1.00 44.82           C  
ANISOU  744  C   GLU A  82     7093   6255   3683   -624   1593   -700       C  
ATOM    745  O   GLU A  82      30.159  44.781  45.198  1.00 46.55           O  
ANISOU  745  O   GLU A  82     7273   6456   3956   -555   1566   -840       O  
ATOM    746  CB  GLU A  82      28.442  43.107  47.510  1.00 53.99           C  
ANISOU  746  CB  GLU A  82     8453   7586   4475   -785   1878   -643       C  
ATOM    747  CG  GLU A  82      27.160  43.321  48.307  1.00 68.31           C  
ANISOU  747  CG  GLU A  82    10204   9481   6269   -815   2085   -650       C  
ATOM    748  CD  GLU A  82      27.174  42.628  49.668  1.00 84.39           C  
ANISOU  748  CD  GLU A  82    12410  11603   8051   -889   2100   -550       C  
ATOM    749  OE1 GLU A  82      28.183  41.962  49.989  1.00 89.50           O  
ANISOU  749  OE1 GLU A  82    13221  12243   8543   -912   1939   -464       O  
ATOM    750  OE2 GLU A  82      26.172  42.746  50.413  1.00 87.92           O  
ANISOU  750  OE2 GLU A  82    12821  12130   8455   -914   2270   -549       O  
ATOM    751  N   ALA A  83      30.261  42.542  44.975  1.00 42.94           N  
ANISOU  751  N   ALA A  83     6897   5961   3458   -634   1422   -557       N  
ATOM    752  CA  ALA A  83      31.506  42.605  44.217  1.00 42.34           C  
ANISOU  752  CA  ALA A  83     6801   5817   3471   -551   1198   -561       C  
ATOM    753  C   ALA A  83      31.356  43.499  42.995  1.00 43.41           C  
ANISOU  753  C   ALA A  83     6741   5897   3857   -462   1208   -654       C  
ATOM    754  O   ALA A  83      32.153  44.414  42.782  1.00 45.61           O  
ANISOU  754  O   ALA A  83     6996   6157   4175   -399   1133   -756       O  
ATOM    755  CB  ALA A  83      31.955  41.205  43.797  1.00 33.44           C  
ANISOU  755  CB  ALA A  83     5723   4624   2359   -559   1044   -391       C  
ATOM    756  N   ILE A  84      30.319  43.258  42.190  1.00 41.99           N  
ANISOU  756  N   ILE A  84     6417   5692   3846   -461   1302   -618       N  
ATOM    757  CA  ILE A  84      30.108  44.059  40.987  1.00 37.11           C  
ANISOU  757  CA  ILE A  84     5610   5031   3458   -366   1310   -686       C  
ATOM    758  C   ILE A  84      29.923  45.531  41.343  1.00 37.27           C  
ANISOU  758  C   ILE A  84     5598   5074   3488   -320   1438   -841       C  
ATOM    759  O   ILE A  84      30.541  46.410  40.726  1.00 38.28           O  
ANISOU  759  O   ILE A  84     5665   5152   3729   -237   1374   -914       O  
ATOM    760  CB  ILE A  84      28.920  43.509  40.172  1.00 40.14           C  
ANISOU  760  CB  ILE A  84     5842   5413   3995   -383   1392   -622       C  
ATOM    761  CG1 ILE A  84      29.323  42.217  39.450  1.00 41.20           C  
ANISOU  761  CG1 ILE A  84     5991   5486   4179   -401   1229   -498       C  
ATOM    762  CG2 ILE A  84      28.468  44.526  39.142  1.00 29.49           C  
ANISOU  762  CG2 ILE A  84     4297   4054   2852   -280   1446   -698       C  
ATOM    763  CD1 ILE A  84      28.146  41.379  38.967  1.00 45.07           C  
ANISOU  763  CD1 ILE A  84     6381   5980   4764   -472   1306   -427       C  
ATOM    764  N   GLU A  85      29.096  45.816  42.362  1.00 39.86           N  
ANISOU  764  N   GLU A  85     5976   5472   3696   -375   1626   -893       N  
ATOM    765  CA  GLU A  85      28.867  47.198  42.795  1.00 40.49           C  
ANISOU  765  CA  GLU A  85     6046   5563   3777   -329   1766  -1054       C  
ATOM    766  C   GLU A  85      30.141  47.849  43.304  1.00 41.86           C  
ANISOU  766  C   GLU A  85     6348   5712   3844   -322   1649  -1153       C  
ATOM    767  O   GLU A  85      30.307  49.069  43.193  1.00 42.76           O  
ANISOU  767  O   GLU A  85     6424   5779   4044   -260   1687  -1281       O  
ATOM    768  CB  GLU A  85      27.798  47.268  43.895  1.00 40.54           C  
ANISOU  768  CB  GLU A  85     6087   5658   3659   -383   1968  -1079       C  
ATOM    769  CG  GLU A  85      26.394  46.937  43.453  1.00 45.24           C  
ANISOU  769  CG  GLU A  85     6513   6290   4385   -384   2110  -1011       C  
ATOM    770  CD  GLU A  85      25.956  47.726  42.228  1.00 52.31           C  
ANISOU  770  CD  GLU A  85     7197   7133   5546   -261   2118  -1042       C  
ATOM    771  OE1 GLU A  85      26.263  48.933  42.144  1.00 58.92           O  
ANISOU  771  OE1 GLU A  85     8010   7914   6463   -164   2096  -1134       O  
ATOM    772  OE2 GLU A  85      25.304  47.140  41.341  1.00 56.29           O  
ANISOU  772  OE2 GLU A  85     7558   7650   6178   -265   2139   -965       O  
ATOM    773  N   ASP A  86      31.046  47.062  43.859  1.00 41.48           N  
ANISOU  773  N   ASP A  86     6443   5693   3623   -382   1495  -1087       N  
ATOM    774  CA  ASP A  86      32.337  47.577  44.275  1.00 43.28           C  
ANISOU  774  CA  ASP A  86     6772   5917   3754   -382   1352  -1170       C  
ATOM    775  C   ASP A  86      33.294  47.810  43.106  1.00 37.76           C  
ANISOU  775  C   ASP A  86     5972   5133   3243   -309   1179  -1158       C  
ATOM    776  O   ASP A  86      34.396  48.318  43.321  1.00 36.25           O  
ANISOU  776  O   ASP A  86     5832   4936   3007   -311   1057  -1232       O  
ATOM    777  CB  ASP A  86      32.955  46.607  45.282  1.00 50.60           C  
ANISOU  777  CB  ASP A  86     7878   6925   4424   -459   1240  -1086       C  
ATOM    778  CG  ASP A  86      34.175  47.181  45.970  1.00 59.81           C  
ANISOU  778  CG  ASP A  86     9154   8127   5443   -477   1108  -1191       C  
ATOM    779  OD1 ASP A  86      34.012  48.188  46.708  1.00 65.00           O  
ANISOU  779  OD1 ASP A  86     9839   8810   6049   -486   1195  -1335       O  
ATOM    780  OD2 ASP A  86      35.283  46.620  45.766  1.00 53.44           O  
ANISOU  780  OD2 ASP A  86     8372   7322   4611   -465    894  -1113       O  
ATOM    781  N   GLY A  87      32.921  47.455  41.882  1.00 31.67           N  
ANISOU  781  N   GLY A  87     5053   4306   2673   -248   1163  -1069       N  
ATOM    782  CA  GLY A  87      33.814  47.624  40.754  1.00 29.32           C  
ANISOU  782  CA  GLY A  87     4661   3941   2539   -175   1010  -1047       C  
ATOM    783  C   GLY A  87      34.570  46.383  40.306  1.00 34.43           C  
ANISOU  783  C   GLY A  87     5326   4586   3169   -170    819   -907       C  
ATOM    784  O   GLY A  87      35.493  46.498  39.487  1.00 34.08           O  
ANISOU  784  O   GLY A  87     5218   4503   3229   -110    681   -893       O  
ATOM    785  N   MET A  88      34.227  45.215  40.818  1.00 37.04           N  
ANISOU  785  N   MET A  88     5745   4952   3375   -227    813   -802       N  
ATOM    786  CA  MET A  88      34.895  44.003  40.376  1.00 32.50           C  
ANISOU  786  CA  MET A  88     5197   4353   2798   -210    643   -669       C  
ATOM    787  C   MET A  88      34.797  43.881  38.856  1.00 28.01           C  
ANISOU  787  C   MET A  88     4468   3718   2455   -129    600   -632       C  
ATOM    788  O   MET A  88      33.697  43.971  38.300  1.00 30.31           O  
ANISOU  788  O   MET A  88     4655   3997   2863   -125    722   -634       O  
ATOM    789  CB  MET A  88      34.264  42.795  41.064  1.00 36.04           C  
ANISOU  789  CB  MET A  88     5759   4823   3113   -288    686   -555       C  
ATOM    790  CG  MET A  88      34.846  41.456  40.644  1.00 43.19           C  
ANISOU  790  CG  MET A  88     6712   5677   4022   -268    527   -411       C  
ATOM    791  SD  MET A  88      36.444  41.200  41.399  1.00 42.27           S  
ANISOU  791  SD  MET A  88     6735   5600   3725   -241    322   -378       S  
ATOM    792  CE  MET A  88      36.028  40.721  43.062  1.00 31.34           C  
ANISOU  792  CE  MET A  88     5553   4294   2059   -348    403   -323       C  
ATOM    793  N   PRO A  89      35.914  43.742  38.147  1.00 24.74           N  
ANISOU  793  N   PRO A  89     4021   3275   2104    -59    434   -605       N  
ATOM    794  CA  PRO A  89      35.849  43.506  36.707  1.00 29.63           C  
ANISOU  794  CA  PRO A  89     4503   3844   2910     20    389   -564       C  
ATOM    795  C   PRO A  89      35.369  42.096  36.449  1.00 31.49           C  
ANISOU  795  C   PRO A  89     4774   4050   3142     -4    362   -453       C  
ATOM    796  O   PRO A  89      35.662  41.174  37.220  1.00 26.94           O  
ANISOU  796  O   PRO A  89     4338   3472   2427    -51    304   -379       O  
ATOM    797  CB  PRO A  89      37.300  43.675  36.248  1.00 24.52           C  
ANISOU  797  CB  PRO A  89     3835   3190   2293     93    222   -563       C  
ATOM    798  CG  PRO A  89      37.975  44.306  37.370  1.00 26.76           C  
ANISOU  798  CG  PRO A  89     4210   3520   2439     46    200   -633       C  
ATOM    799  CD  PRO A  89      37.295  43.801  38.601  1.00 25.02           C  
ANISOU  799  CD  PRO A  89     4129   3336   2040    -46    278   -613       C  
ATOM    800  N   GLY A  90      34.621  41.949  35.359  1.00 28.51           N  
ANISOU  800  N   GLY A  90     4270   3647   2915     26    402   -441       N  
ATOM    801  CA  GLY A  90      34.046  40.671  34.990  1.00 31.94           C  
ANISOU  801  CA  GLY A  90     4721   4042   3372    -11    386   -357       C  
ATOM    802  C   GLY A  90      33.666  40.675  33.529  1.00 32.99           C  
ANISOU  802  C   GLY A  90     4696   4159   3678     55    370   -366       C  
ATOM    803  O   GLY A  90      33.374  41.729  32.948  1.00 28.26           O  
ANISOU  803  O   GLY A  90     3964   3594   3179    111    431   -428       O  
ATOM    804  N   LEU A  91      33.718  39.492  32.917  1.00 23.84           N  
ANISOU  804  N   LEU A  91     3561   2947   2552     55    283   -305       N  
ATOM    805  CA  LEU A  91      33.300  39.301  31.534  1.00 20.50           C  
ANISOU  805  CA  LEU A  91     3002   2518   2269    105    257   -316       C  
ATOM    806  C   LEU A  91      32.270  38.186  31.486  1.00 27.53           C  
ANISOU  806  C   LEU A  91     3912   3375   3175     -1    296   -278       C  
ATOM    807  O   LEU A  91      32.509  37.105  32.032  1.00 26.60           O  
ANISOU  807  O   LEU A  91     3940   3183   2982    -61    250   -213       O  
ATOM    808  CB  LEU A  91      34.492  38.958  30.638  1.00 19.56           C  
ANISOU  808  CB  LEU A  91     2884   2361   2187    218    101   -300       C  
ATOM    809  CG  LEU A  91      34.154  38.593  29.188  1.00 24.86           C  
ANISOU  809  CG  LEU A  91     3441   3030   2975    273     58   -314       C  
ATOM    810  CD1 LEU A  91      33.388  39.705  28.470  1.00 22.47           C  
ANISOU  810  CD1 LEU A  91     2959   2808   2770    311    145   -365       C  
ATOM    811  CD2 LEU A  91      35.386  38.186  28.398  1.00 21.98           C  
ANISOU  811  CD2 LEU A  91     3093   2631   2626    389    -85   -299       C  
ATOM    812  N   THR A  92      31.136  38.436  30.825  1.00 30.53           N  
ANISOU  812  N   THR A  92     4140   3806   3655    -25    376   -314       N  
ATOM    813  CA  THR A  92      30.049  37.466  30.744  1.00 28.01           C  
ANISOU  813  CA  THR A  92     3807   3469   3366   -147    421   -291       C  
ATOM    814  C   THR A  92      29.619  37.318  29.286  1.00 29.91           C  
ANISOU  814  C   THR A  92     3894   3737   3732   -102    365   -330       C  
ATOM    815  O   THR A  92      29.542  38.306  28.555  1.00 27.78           O  
ANISOU  815  O   THR A  92     3480   3546   3531     -2    375   -373       O  
ATOM    816  CB  THR A  92      28.851  37.867  31.642  1.00 28.18           C  
ANISOU  816  CB  THR A  92     3784   3560   3362   -256    599   -297       C  
ATOM    817  OG1 THR A  92      28.313  39.131  31.237  1.00 25.87           O  
ANISOU  817  OG1 THR A  92     3316   3367   3145   -182    682   -360       O  
ATOM    818  CG2 THR A  92      29.260  37.984  33.087  1.00 28.72           C  
ANISOU  818  CG2 THR A  92     4015   3615   3281   -301    654   -265       C  
ATOM    819  N   ILE A  93      29.369  36.080  28.850  1.00 27.86           N  
ANISOU  819  N   ILE A  93     3677   3409   3501   -175    303   -314       N  
ATOM    820  CA  ILE A  93      29.168  35.770  27.433  1.00 28.21           C  
ANISOU  820  CA  ILE A  93     3608   3472   3640   -131    218   -361       C  
ATOM    821  C   ILE A  93      27.801  35.113  27.239  1.00 29.86           C  
ANISOU  821  C   ILE A  93     3733   3705   3909   -282    274   -379       C  
ATOM    822  O   ILE A  93      27.494  34.106  27.890  1.00 29.77           O  
ANISOU  822  O   ILE A  93     3838   3603   3872   -425    299   -340       O  
ATOM    823  CB  ILE A  93      30.267  34.842  26.885  1.00 29.37           C  
ANISOU  823  CB  ILE A  93     3882   3506   3773    -65     69   -352       C  
ATOM    824  CG1 ILE A  93      31.675  35.355  27.207  1.00 26.45           C  
ANISOU  824  CG1 ILE A  93     3595   3115   3339     68     10   -325       C  
ATOM    825  CG2 ILE A  93      30.058  34.609  25.385  1.00 28.72           C  
ANISOU  825  CG2 ILE A  93     3682   3460   3771    -10    -13   -417       C  
ATOM    826  CD1 ILE A  93      32.002  36.742  26.645  1.00 26.87           C  
ANISOU  826  CD1 ILE A  93     3506   3277   3427    199     21   -360       C  
ATOM    827  N   CYS A  94      27.000  35.660  26.318  1.00 25.43           N  
ANISOU  827  N   CYS A  94     2966   3267   3429   -253    288   -432       N  
ATOM    828  CA  CYS A  94      25.699  35.099  25.961  1.00 26.17           C  
ANISOU  828  CA  CYS A  94     2937   3414   3591   -393    322   -463       C  
ATOM    829  C   CYS A  94      24.851  34.767  27.186  1.00 26.58           C  
ANISOU  829  C   CYS A  94     3026   3453   3621   -569    462   -419       C  
ATOM    830  O   CYS A  94      24.458  35.660  27.935  1.00 34.68           O  
ANISOU  830  O   CYS A  94     3993   4559   4624   -558    591   -403       O  
ATOM    831  CB  CYS A  94      25.879  33.850  25.080  1.00 28.70           C  
ANISOU  831  CB  CYS A  94     3319   3645   3942   -440    189   -500       C  
ATOM    832  SG  CYS A  94      26.674  34.238  23.455  1.00 38.45           S  
ANISOU  832  SG  CYS A  94     4475   4937   5197   -234     37   -563       S  
ATOM    833  N   GLY A  95      24.584  33.478  27.420  1.00 30.73           N  
ANISOU  833  N   GLY A  95     3658   3868   4150   -731    447   -399       N  
ATOM    834  CA  GLY A  95      23.736  33.105  28.545  1.00 31.49           C  
ANISOU  834  CA  GLY A  95     3785   3956   4225   -912    591   -345       C  
ATOM    835  C   GLY A  95      24.269  33.603  29.878  1.00 28.90           C  
ANISOU  835  C   GLY A  95     3597   3605   3778   -881    683   -276       C  
ATOM    836  O   GLY A  95      23.495  33.950  30.769  1.00 30.09           O  
ANISOU  836  O   GLY A  95     3703   3829   3899   -966    839   -250       O  
ATOM    837  N   GLY A  96      25.588  33.654  30.025  1.00 28.51           N  
ANISOU  837  N   GLY A  96     3710   3467   3655   -757    589   -252       N  
ATOM    838  CA  GLY A  96      26.170  34.254  31.214  1.00 34.13           C  
ANISOU  838  CA  GLY A  96     4541   4182   4246   -714    655   -205       C  
ATOM    839  C   GLY A  96      25.843  35.734  31.366  1.00 33.75           C  
ANISOU  839  C   GLY A  96     4344   4280   4201   -626    756   -255       C  
ATOM    840  O   GLY A  96      25.728  36.233  32.483  1.00 32.45           O  
ANISOU  840  O   GLY A  96     4233   4152   3946   -652    874   -235       O  
ATOM    841  N   TYR A  97      25.680  36.443  30.249  1.00 31.72           N  
ANISOU  841  N   TYR A  97     3905   4104   4043   -517    715   -320       N  
ATOM    842  CA  TYR A  97      25.236  37.836  30.261  1.00 30.95           C  
ANISOU  842  CA  TYR A  97     3652   4132   3977   -427    818   -364       C  
ATOM    843  C   TYR A  97      23.730  37.936  30.487  1.00 34.40           C  
ANISOU  843  C   TYR A  97     3925   4678   4467   -533    969   -374       C  
ATOM    844  O   TYR A  97      23.277  38.608  31.425  1.00 35.17           O  
ANISOU  844  O   TYR A  97     4009   4834   4520   -548   1123   -376       O  
ATOM    845  CB  TYR A  97      25.684  38.498  28.946  1.00 28.13           C  
ANISOU  845  CB  TYR A  97     3174   3811   3702   -262    712   -408       C  
ATOM    846  CG  TYR A  97      24.942  39.742  28.422  1.00 26.91           C  
ANISOU  846  CG  TYR A  97     2804   3788   3634   -162    792   -447       C  
ATOM    847  CD1 TYR A  97      24.464  40.750  29.262  1.00 24.50           C  
ANISOU  847  CD1 TYR A  97     2455   3538   3314   -142    952   -460       C  
ATOM    848  CD2 TYR A  97      24.792  39.919  27.054  1.00 29.20           C  
ANISOU  848  CD2 TYR A  97     2941   4141   4011    -70    705   -469       C  
ATOM    849  CE1 TYR A  97      23.833  41.879  28.731  1.00 29.59           C  
ANISOU  849  CE1 TYR A  97     2909   4284   4049    -28   1022   -488       C  
ATOM    850  CE2 TYR A  97      24.171  41.024  26.520  1.00 31.57           C  
ANISOU  850  CE2 TYR A  97     3051   4556   4389     41    766   -486       C  
ATOM    851  CZ  TYR A  97      23.690  42.010  27.358  1.00 31.61           C  
ANISOU  851  CZ  TYR A  97     3014   4600   4396     66    926   -492       C  
ATOM    852  OH  TYR A  97      23.070  43.115  26.794  1.00 29.45           O  
ANISOU  852  OH  TYR A  97     2552   4427   4210    195    989   -501       O  
ATOM    853  N   GLN A  98      22.941  37.240  29.664  1.00 36.83           N  
ANISOU  853  N   GLN A  98     4107   5021   4867   -613    930   -386       N  
ATOM    854  CA  GLN A  98      21.486  37.287  29.792  1.00 29.91           C  
ANISOU  854  CA  GLN A  98     3042   4267   4054   -720   1064   -396       C  
ATOM    855  C   GLN A  98      21.013  36.955  31.198  1.00 39.78           C  
ANISOU  855  C   GLN A  98     4388   5505   5223   -870   1225   -346       C  
ATOM    856  O   GLN A  98      20.078  37.579  31.721  1.00 36.62           O  
ANISOU  856  O   GLN A  98     3855   5223   4835   -891   1391   -355       O  
ATOM    857  CB  GLN A  98      20.852  36.307  28.817  1.00 35.24           C  
ANISOU  857  CB  GLN A  98     3610   4957   4821   -829    973   -417       C  
ATOM    858  CG  GLN A  98      21.231  36.499  27.370  1.00 34.35           C  
ANISOU  858  CG  GLN A  98     3405   4876   4772   -695    812   -468       C  
ATOM    859  CD  GLN A  98      20.753  35.324  26.525  1.00 33.46           C  
ANISOU  859  CD  GLN A  98     3243   4748   4722   -828    707   -503       C  
ATOM    860  OE1 GLN A  98      20.933  34.158  26.906  1.00 31.39           O  
ANISOU  860  OE1 GLN A  98     3144   4347   4437   -975    682   -480       O  
ATOM    861  NE2 GLN A  98      20.129  35.620  25.390  1.00 38.82           N  
ANISOU  861  NE2 GLN A  98     3701   5568   5479   -778    646   -557       N  
ATOM    862  N   PHE A  99      21.606  35.946  31.816  1.00 38.63           N  
ANISOU  862  N   PHE A  99     4465   5220   4992   -972   1186   -287       N  
ATOM    863  CA  PHE A  99      21.066  35.534  33.096  1.00 42.96           C  
ANISOU  863  CA  PHE A  99     5100   5765   5456  -1129   1344   -224       C  
ATOM    864  C   PHE A  99      21.602  36.367  34.258  1.00 42.59           C  
ANISOU  864  C   PHE A  99     5181   5733   5269  -1052   1439   -212       C  
ATOM    865  O   PHE A  99      21.315  36.040  35.412  1.00 51.22           O  
ANISOU  865  O   PHE A  99     6381   6824   6256  -1167   1567   -153       O  
ATOM    866  CB  PHE A  99      21.308  34.038  33.314  1.00 43.52           C  
ANISOU  866  CB  PHE A  99     5356   5681   5500  -1287   1281   -148       C  
ATOM    867  CG  PHE A  99      20.353  33.155  32.545  1.00 45.12           C  
ANISOU  867  CG  PHE A  99     5423   5886   5833  -1443   1261   -164       C  
ATOM    868  CD1 PHE A  99      20.505  32.964  31.174  1.00 41.25           C  
ANISOU  868  CD1 PHE A  99     4838   5385   5451  -1384   1099   -235       C  
ATOM    869  CD2 PHE A  99      19.292  32.529  33.189  1.00 56.86           C  
ANISOU  869  CD2 PHE A  99     6874   7397   7334  -1657   1407   -113       C  
ATOM    870  CE1 PHE A  99      19.620  32.162  30.458  1.00 46.47           C  
ANISOU  870  CE1 PHE A  99     5373   6058   6227  -1538   1071   -268       C  
ATOM    871  CE2 PHE A  99      18.407  31.711  32.491  1.00 55.35           C  
ANISOU  871  CE2 PHE A  99     6549   7210   7271  -1822   1385   -137       C  
ATOM    872  CZ  PHE A  99      18.572  31.525  31.122  1.00 53.50           C  
ANISOU  872  CZ  PHE A  99     6224   6964   7141  -1764   1210   -222       C  
ATOM    873  N   LEU A 100      22.341  37.451  33.996  1.00 39.79           N  
ANISOU  873  N   LEU A 100     4815   5396   4906   -868   1387   -268       N  
ATOM    874  CA  LEU A 100      22.506  38.455  35.046  1.00 39.17           C  
ANISOU  874  CA  LEU A 100     4796   5368   4720   -808   1513   -292       C  
ATOM    875  C   LEU A 100      21.228  39.232  35.262  1.00 39.79           C  
ANISOU  875  C   LEU A 100     4675   5590   4853   -814   1708   -335       C  
ATOM    876  O   LEU A 100      21.049  39.813  36.333  1.00 40.20           O  
ANISOU  876  O   LEU A 100     4781   5690   4803   -816   1859   -351       O  
ATOM    877  CB  LEU A 100      23.622  39.449  34.737  1.00 31.35           C  
ANISOU  877  CB  LEU A 100     3846   4348   3719   -626   1416   -347       C  
ATOM    878  CG  LEU A 100      25.014  38.956  34.392  1.00 36.06           C  
ANISOU  878  CG  LEU A 100     4601   4825   4277   -571   1218   -320       C  
ATOM    879  CD1 LEU A 100      25.768  40.047  33.637  1.00 40.04           C  
ANISOU  879  CD1 LEU A 100     5038   5334   4843   -393   1137   -384       C  
ATOM    880  CD2 LEU A 100      25.753  38.561  35.662  1.00 41.08           C  
ANISOU  880  CD2 LEU A 100     5474   5403   4732   -626   1219   -267       C  
ATOM    881  N   GLY A 101      20.321  39.227  34.291  1.00 38.07           N  
ANISOU  881  N   GLY A 101     4021   5270   5175   -724   1095   -318       N  
ATOM    882  CA  GLY A 101      19.087  39.974  34.405  1.00 35.78           C  
ANISOU  882  CA  GLY A 101     3504   5123   4968   -691   1163   -437       C  
ATOM    883  C   GLY A 101      18.021  39.258  35.214  1.00 41.92           C  
ANISOU  883  C   GLY A 101     4125   6050   5753   -856   1322   -384       C  
ATOM    884  O   GLY A 101      18.259  38.252  35.886  1.00 44.93           O  
ANISOU  884  O   GLY A 101     4594   6429   6050  -1002   1401   -242       O  
ATOM    885  N   LYS A 102      16.803  39.797  35.122  1.00 42.88           N  
ANISOU  885  N   LYS A 102     4003   6308   5981   -830   1369   -494       N  
ATOM    886  CA  LYS A 102      15.688  39.285  35.910  1.00 44.98           C  
ANISOU  886  CA  LYS A 102     4072   6763   6256   -984   1541   -466       C  
ATOM    887  C   LYS A 102      15.084  38.030  35.285  1.00 51.64           C  
ANISOU  887  C   LYS A 102     4856   7537   7229  -1193   1494   -372       C  
ATOM    888  O   LYS A 102      14.799  37.058  35.992  1.00 53.91           O  
ANISOU  888  O   LYS A 102     5138   7873   7473  -1396   1619   -248       O  
ATOM    889  CB  LYS A 102      14.619  40.370  36.078  1.00 53.88           C  
ANISOU  889  CB  LYS A 102     4939   8085   7449   -858   1615   -634       C  
ATOM    890  CG  LYS A 102      14.768  41.226  37.329  1.00 56.58           C  
ANISOU  890  CG  LYS A 102     5281   8587   7629   -755   1780   -708       C  
ATOM    891  N   LYS A 103      14.873  38.020  33.968  1.00 54.47           N  
ANISOU  891  N   LYS A 103     5176   7780   7741  -1158   1315   -429       N  
ATOM    892  CA  LYS A 103      14.296  36.833  33.345  1.00 56.91           C  
ANISOU  892  CA  LYS A 103     5433   8017   8173  -1368   1258   -364       C  
ATOM    893  C   LYS A 103      14.801  36.660  31.918  1.00 50.59           C  
ANISOU  893  C   LYS A 103     4757   7006   7457  -1309   1030   -390       C  
ATOM    894  O   LYS A 103      15.308  37.593  31.289  1.00 45.41           O  
ANISOU  894  O   LYS A 103     4159   6301   6795  -1104    915   -473       O  
ATOM    895  CB  LYS A 103      12.762  36.880  33.357  1.00 62.28           C  
ANISOU  895  CB  LYS A 103     5774   8908   8982  -1463   1327   -439       C  
ATOM    896  CG  LYS A 103      12.154  37.999  32.531  1.00 59.67           C  
ANISOU  896  CG  LYS A 103     5249   8659   8763  -1259   1212   -606       C  
ATOM    897  CD  LYS A 103      11.161  38.822  33.354  1.00 59.91           C  
ANISOU  897  CD  LYS A 103     4999   8967   8797  -1184   1377   -705       C  
ATOM    898  CE  LYS A 103      10.108  37.954  34.039  1.00 59.16           C  
ANISOU  898  CE  LYS A 103     4681   9061   8736  -1443   1548   -650       C  
ATOM    899  N   TYR A 104      14.660  35.429  31.430  1.00 51.53           N  
ANISOU  899  N   TYR A 104     4930   6999   7651  -1504    972   -318       N  
ATOM    900  CA  TYR A 104      14.925  35.050  30.048  1.00 47.51           C  
ANISOU  900  CA  TYR A 104     4514   6309   7227  -1493    765   -354       C  
ATOM    901  C   TYR A 104      13.689  34.329  29.536  1.00 51.83           C  
ANISOU  901  C   TYR A 104     4860   6903   7931  -1698    727   -388       C  
ATOM    902  O   TYR A 104      13.333  33.271  30.065  1.00 56.58           O  
ANISOU  902  O   TYR A 104     5461   7480   8556  -1937    824   -294       O  
ATOM    903  CB  TYR A 104      16.159  34.143  29.940  1.00 50.87           C  
ANISOU  903  CB  TYR A 104     5253   6498   7579  -1525    719   -244       C  
ATOM    904  CG  TYR A 104      16.385  33.581  28.545  1.00 56.61           C  
ANISOU  904  CG  TYR A 104     6081   7041   8386  -1537    524   -289       C  
ATOM    905  CD1 TYR A 104      15.753  32.411  28.129  1.00 59.07           C  
ANISOU  905  CD1 TYR A 104     6374   7261   8809  -1760    483   -274       C  
ATOM    906  CD2 TYR A 104      17.212  34.225  27.643  1.00 49.68           C  
ANISOU  906  CD2 TYR A 104     5320   6087   7468  -1337    384   -353       C  
ATOM    907  CE1 TYR A 104      15.948  31.904  26.858  1.00 63.18           C  
ANISOU  907  CE1 TYR A 104     6994   7620   9390  -1769    304   -338       C  
ATOM    908  CE2 TYR A 104      17.407  33.735  26.373  1.00 55.89           C  
ANISOU  908  CE2 TYR A 104     6199   6732   8306  -1342    216   -403       C  
ATOM    909  CZ  TYR A 104      16.772  32.567  25.984  1.00 63.63           C  
ANISOU  909  CZ  TYR A 104     7163   7624   9390  -1553    173   -404       C  
ATOM    910  OH  TYR A 104      16.963  32.059  24.718  1.00 66.93           O  
ANISOU  910  OH  TYR A 104     7682   7901   9846  -1559      3   -474       O  
ATOM    911  N   ILE A 105      13.032  34.890  28.519  1.00 48.84           N  
ANISOU  911  N   ILE A 105     4309   6592   7655  -1615    584   -517       N  
ATOM    912  CA  ILE A 105      11.836  34.289  27.934  1.00 52.33           C  
ANISOU  912  CA  ILE A 105     4530   7106   8248  -1803    519   -572       C  
ATOM    913  C   ILE A 105      12.238  33.516  26.686  1.00 58.60           C  
ANISOU  913  C   ILE A 105     5496   7684   9085  -1862    319   -592       C  
ATOM    914  O   ILE A 105      12.916  34.060  25.810  1.00 61.77           O  
ANISOU  914  O   ILE A 105     6026   7998   9444  -1667    172   -644       O  
ATOM    915  CB  ILE A 105      10.778  35.353  27.611  1.00 50.97           C  
ANISOU  915  CB  ILE A 105     4037   7171   8158  -1669    475   -704       C  
ATOM    916  CG1 ILE A 105      10.521  36.224  28.837  1.00 49.13           C  
ANISOU  916  CG1 ILE A 105     3666   7136   7865  -1562    676   -706       C  
ATOM    917  CG2 ILE A 105       9.458  34.694  27.168  1.00 54.99           C  
ANISOU  917  CG2 ILE A 105     4268   7805   8821  -1891    425   -759       C  
ATOM    918  CD1 ILE A 105       9.527  37.331  28.581  1.00 52.10           C  
ANISOU  918  CD1 ILE A 105     3736   7736   8324  -1386    640   -840       C  
ATOM    919  N   THR A 106      11.837  32.243  26.609  1.00 64.56           N  
ANISOU  919  N   THR A 106     6265   8347   9918  -2138    320   -553       N  
ATOM    920  CA  THR A 106      12.148  31.404  25.455  1.00 63.50           C  
ANISOU  920  CA  THR A 106     6299   8000   9828  -2215    137   -593       C  
ATOM    921  C   THR A 106      11.151  31.672  24.335  1.00 65.70           C  
ANISOU  921  C   THR A 106     6341   8407  10216  -2227    -41   -742       C  
ATOM    922  O   THR A 106      10.112  32.308  24.551  1.00 62.28           O  
ANISOU  922  O   THR A 106     5593   8222   9847  -2218     -7   -797       O  
ATOM    923  CB  THR A 106      12.140  29.929  25.855  1.00 59.58           C  
ANISOU  923  CB  THR A 106     5939   7322   9375  -2507    208   -496       C  
ATOM    924  OG1 THR A 106      10.901  29.608  26.484  1.00 61.93           O  
ANISOU  924  OG1 THR A 106     5970   7791   9771  -2752    326   -479       O  
ATOM    925  CG2 THR A 106      13.314  29.605  26.769  1.00 60.51           C  
ANISOU  925  CG2 THR A 106     6342   7280   9368  -2454    336   -342       C  
ATOM    926  N   PRO A 107      11.442  31.212  23.108  1.00 69.95           N  
ANISOU  926  N   PRO A 107     7017   8794  10768  -2233   -238   -816       N  
ATOM    927  CA  PRO A 107      10.494  31.479  22.018  1.00 70.70           C  
ANISOU  927  CA  PRO A 107     6886   9030  10947  -2240   -426   -958       C  
ATOM    928  C   PRO A 107       9.118  30.944  22.321  1.00 76.90           C  
ANISOU  928  C   PRO A 107     7366   9978  11875  -2515   -384   -990       C  
ATOM    929  O   PRO A 107       8.121  31.609  22.019  1.00 82.24           O  
ANISOU  929  O   PRO A 107     7727  10901  12618  -2467   -453  -1079       O  
ATOM    930  CB  PRO A 107      11.129  30.773  20.812  1.00 71.94           C  
ANISOU  930  CB  PRO A 107     7294   8966  11075  -2259   -613  -1020       C  
ATOM    931  CG  PRO A 107      12.544  30.562  21.184  1.00 73.11           C  
ANISOU  931  CG  PRO A 107     7780   8892  11107  -2151   -531   -921       C  
ATOM    932  CD  PRO A 107      12.554  30.357  22.649  1.00 70.20           C  
ANISOU  932  CD  PRO A 107     7397   8535  10741  -2246   -300   -786       C  
ATOM    933  N   ASP A 108       9.041  29.763  22.950  1.00 80.55           N  
ANISOU  933  N   ASP A 108     7910  10310  12387  -2804   -267   -911       N  
ATOM    934  CA  ASP A 108       7.778  29.139  23.343  1.00 80.13           C  
ANISOU  934  CA  ASP A 108     7589  10398  12460  -3109   -199   -912       C  
ATOM    935  C   ASP A 108       7.211  29.717  24.638  1.00 76.98           C  
ANISOU  935  C   ASP A 108     6955  10241  12052  -3098     31   -829       C  
ATOM    936  O   ASP A 108       6.409  29.048  25.300  1.00 67.66           O  
ANISOU  936  O   ASP A 108     5671   9125  10910  -3314    140   -733       O  
ATOM    937  CB  ASP A 108       7.958  27.621  23.475  1.00 78.54           C  
ANISOU  937  CB  ASP A 108     7642   9922  12277  -3381   -180   -812       C  
ATOM    938  N   GLY A 109       7.623  30.930  25.019  1.00 79.17           N  
ANISOU  938  N   GLY A 109     7197  10636  12248  -2807     95   -834       N  
ATOM    939  CA  GLY A 109       6.980  31.678  26.080  1.00 80.74           C  
ANISOU  939  CA  GLY A 109     7128  11109  12442  -2753    288   -813       C  
ATOM    940  C   GLY A 109       7.350  31.288  27.493  1.00 85.87           C  
ANISOU  940  C   GLY A 109     7894  11723  13008  -2866    547   -656       C  
ATOM    941  O   GLY A 109       6.857  31.918  28.437  1.00 91.55           O  
ANISOU  941  O   GLY A 109     8403  12680  13700  -2816    726   -644       O  
ATOM    942  N   THR A 110       8.196  30.281  27.678  1.00 84.42           N  
ANISOU  942  N   THR A 110     8039  11259  12776  -3003    573   -537       N  
ATOM    943  CA  THR A 110       8.600  29.889  29.022  1.00 83.48           C  
ANISOU  943  CA  THR A 110     8055  11104  12560  -3099    806   -368       C  
ATOM    944  C   THR A 110       9.504  30.961  29.631  1.00 77.86           C  
ANISOU  944  C   THR A 110     7462  10435  11688  -2782    880   -342       C  
ATOM    945  O   THR A 110      10.484  31.386  29.010  1.00 77.81           O  
ANISOU  945  O   THR A 110     7665  10278  11620  -2553    745   -376       O  
ATOM    946  CB  THR A 110       9.317  28.538  28.984  1.00 84.31           C  
ANISOU  946  CB  THR A 110     8502  10873  12659  -3294    788   -245       C  
ATOM    947  OG1 THR A 110       8.671  27.675  28.037  1.00 84.25           O  
ANISOU  947  OG1 THR A 110     8461  10762  12787  -3486    624   -303       O  
ATOM    948  CG2 THR A 110       9.299  27.881  30.355  1.00 86.10           C  
ANISOU  948  CG2 THR A 110     8810  11092  12813  -3467   1015    -44       C  
ATOM    949  N   GLU A 111       9.166  31.408  30.842  1.00 70.45           N  
ANISOU  949  N   GLU A 111     6381   9709  10676  -2779   1098   -291       N  
ATOM    950  CA  GLU A 111       9.982  32.371  31.575  1.00 70.49           C  
ANISOU  950  CA  GLU A 111     6499   9763  10520  -2515   1187   -271       C  
ATOM    951  C   GLU A 111      10.978  31.635  32.462  1.00 65.23           C  
ANISOU  951  C   GLU A 111     6146   8923   9714  -2593   1300    -88       C  
ATOM    952  O   GLU A 111      10.581  30.876  33.354  1.00 67.43           O  
ANISOU  952  O   GLU A 111     6404   9247   9969  -2830   1470     39       O  
ATOM    953  CB  GLU A 111       9.117  33.296  32.429  1.00 75.73           C  
ANISOU  953  CB  GLU A 111     6855  10759  11161  -2444   1361   -335       C  
ATOM    954  CG  GLU A 111       8.295  34.302  31.655  1.00 79.35           C  
ANISOU  954  CG  GLU A 111     7018  11398  11733  -2266   1248   -518       C  
ATOM    955  CD  GLU A 111       7.696  35.352  32.562  1.00 84.31           C  
ANISOU  955  CD  GLU A 111     7399  12321  12314  -2117   1423   -592       C  
ATOM    956  OE1 GLU A 111       8.072  35.389  33.753  1.00 85.87           O  
ANISOU  956  OE1 GLU A 111     7690  12571  12365  -2130   1622   -509       O  
ATOM    957  OE2 GLU A 111       6.851  36.138  32.088  1.00 88.37           O  
ANISOU  957  OE2 GLU A 111     7629  13017  12931  -1977   1360   -735       O  
ATOM    958  N   LEU A 112      12.264  31.845  32.198  1.00 59.98           N  
ANISOU  958  N   LEU A 112     5766   8068   8954  -2395   1201    -68       N  
ATOM    959  CA  LEU A 112      13.361  31.362  33.026  1.00 58.80           C  
ANISOU  959  CA  LEU A 112     5911   7779   8653  -2391   1283     94       C  
ATOM    960  C   LEU A 112      13.865  32.494  33.909  1.00 61.73           C  
ANISOU  960  C   LEU A 112     6281   8313   8861  -2171   1388     76       C  
ATOM    961  O   LEU A 112      14.017  33.629  33.447  1.00 58.45           O  
ANISOU  961  O   LEU A 112     5798   7963   8447  -1941   1306    -62       O  
ATOM    962  CB  LEU A 112      14.521  30.847  32.168  1.00 53.90           C  
ANISOU  962  CB  LEU A 112     5592   6858   8029  -2307   1105    118       C  
ATOM    963  CG  LEU A 112      14.628  29.371  31.791  1.00 60.60           C  
ANISOU  963  CG  LEU A 112     6626   7444   8956  -2523   1049    215       C  
ATOM    964  CD1 LEU A 112      13.497  28.539  32.409  1.00 59.06           C  
ANISOU  964  CD1 LEU A 112     6288   7315   8836  -2847   1191    302       C  
ATOM    965  CD2 LEU A 112      14.692  29.205  30.279  1.00 61.96           C  
ANISOU  965  CD2 LEU A 112     6834   7460   9248  -2481    826     83       C  
ATOM    966  N   GLU A 113      14.138  32.181  35.174  1.00 63.20           N  
ANISOU  966  N   GLU A 113     6558   8556   8900  -2245   1563    218       N  
ATOM    967  CA  GLU A 113      14.612  33.172  36.131  1.00 60.66           C  
ANISOU  967  CA  GLU A 113     6247   8399   8402  -2064   1672    198       C  
ATOM    968  C   GLU A 113      16.123  33.323  36.035  1.00 61.40           C  
ANISOU  968  C   GLU A 113     6631   8319   8378  -1882   1566    238       C  
ATOM    969  O   GLU A 113      16.851  32.326  35.974  1.00 61.93           O  
ANISOU  969  O   GLU A 113     6930   8182   8420  -1951   1516    376       O  
ATOM    970  CB  GLU A 113      14.222  32.784  37.557  1.00 61.64           C  
ANISOU  970  CB  GLU A 113     6334   8694   8392  -2227   1909    331       C  
ATOM    971  N   GLY A 114      16.588  34.574  36.019  1.00 60.63           N  
ANISOU  971  N   GLY A 114     6518   8304   8216  -1648   1531    113       N  
ATOM    972  CA  GLY A 114      17.998  34.881  36.098  1.00 52.72           C  
ANISOU  972  CA  GLY A 114     5750   7197   7083  -1482   1457    139       C  
ATOM    973  C   GLY A 114      18.413  35.214  37.519  1.00 48.93           C  
ANISOU  973  C   GLY A 114     5325   6876   6391  -1452   1611    197       C  
ATOM    974  O   GLY A 114      17.680  34.997  38.482  1.00 54.14           O  
ANISOU  974  O   GLY A 114     5879   7704   6987  -1580   1786    251       O  
ATOM    975  N   LEU A 115      19.622  35.748  37.646  1.00 43.51           N  
ANISOU  975  N   LEU A 115     4801   6148   5582  -1289   1544    183       N  
ATOM    976  CA  LEU A 115      20.116  36.123  38.963  1.00 45.31           C  
ANISOU  976  CA  LEU A 115     5092   6534   5591  -1250   1665    220       C  
ATOM    977  C   LEU A 115      19.497  37.404  39.488  1.00 52.66           C  
ANISOU  977  C   LEU A 115     5845   7684   6481  -1158   1770     48       C  
ATOM    978  O   LEU A 115      19.452  37.596  40.704  1.00 58.99           O  
ANISOU  978  O   LEU A 115     6640   8669   7106  -1179   1920     68       O  
ATOM    979  CB  LEU A 115      21.633  36.272  38.933  1.00 43.34           C  
ANISOU  979  CB  LEU A 115     5058   6186   5225  -1115   1550    252       C  
ATOM    980  CG  LEU A 115      22.279  34.931  38.589  1.00 50.13           C  
ANISOU  980  CG  LEU A 115     6103   6840   6104  -1185   1466    431       C  
ATOM    981  CD1 LEU A 115      23.715  35.107  38.126  1.00 44.64           C  
ANISOU  981  CD1 LEU A 115     5574   6030   5356  -1028   1316    426       C  
ATOM    982  CD2 LEU A 115      22.193  33.991  39.793  1.00 48.22           C  
ANISOU  982  CD2 LEU A 115     5943   6661   5719  -1325   1600    629       C  
ATOM    983  N   GLY A 116      19.018  38.281  38.613  1.00 56.37           N  
ANISOU  983  N   GLY A 116     6178   8139   7101  -1048   1695   -121       N  
ATOM    984  CA  GLY A 116      18.534  39.559  39.087  1.00 51.14           C  
ANISOU  984  CA  GLY A 116     5374   7652   6406   -924   1782   -296       C  
ATOM    985  C   GLY A 116      19.623  40.466  39.603  1.00 46.83           C  
ANISOU  985  C   GLY A 116     4976   7119   5699   -780   1761   -365       C  
ATOM    986  O   GLY A 116      19.343  41.354  40.400  1.00 49.98           O  
ANISOU  986  O   GLY A 116     5304   7681   6007   -706   1873   -488       O  
ATOM    987  N   ILE A 117      20.871  40.251  39.186  1.00 44.94           N  
ANISOU  987  N   ILE A 117     4936   6720   5420   -743   1623   -298       N  
ATOM    988  CA  ILE A 117      21.932  41.189  39.527  1.00 47.53           C  
ANISOU  988  CA  ILE A 117     5387   7056   5618   -618   1580   -381       C  
ATOM    989  C   ILE A 117      21.593  42.574  38.997  1.00 50.84           C  
ANISOU  989  C   ILE A 117     5719   7458   6141   -468   1539   -585       C  
ATOM    990  O   ILE A 117      21.799  43.587  39.676  1.00 48.74           O  
ANISOU  990  O   ILE A 117     5467   7279   5773   -382   1593   -714       O  
ATOM    991  CB  ILE A 117      23.283  40.699  38.975  1.00 46.20           C  
ANISOU  991  CB  ILE A 117     5410   6723   5420   -602   1427   -278       C  
ATOM    992  CG1 ILE A 117      23.557  39.252  39.391  1.00 43.07           C  
ANISOU  992  CG1 ILE A 117     5111   6305   4950   -728   1453    -66       C  
ATOM    993  CG2 ILE A 117      24.400  41.632  39.425  1.00 44.13           C  
ANISOU  993  CG2 ILE A 117     5257   6499   5013   -503   1389   -360       C  
ATOM    994  CD1 ILE A 117      23.784  39.100  40.840  1.00 44.41           C  
ANISOU  994  CD1 ILE A 117     5329   6651   4892   -773   1579      4       C  
ATOM    995  N   LEU A 118      21.076  42.639  37.772  1.00 43.84           N  
ANISOU  995  N   LEU A 118     4754   6450   5454   -433   1436   -617       N  
ATOM    996  CA  LEU A 118      20.683  43.886  37.143  1.00 41.58           C  
ANISOU  996  CA  LEU A 118     4393   6122   5285   -281   1379   -785       C  
ATOM    997  C   LEU A 118      19.245  43.753  36.681  1.00 46.06           C  
ANISOU  997  C   LEU A 118     4735   6745   6019   -289   1407   -823       C  
ATOM    998  O   LEU A 118      18.776  42.650  36.382  1.00 48.05           O  
ANISOU  998  O   LEU A 118     4925   6995   6336   -424   1406   -714       O  
ATOM    999  CB  LEU A 118      21.594  44.222  35.962  1.00 41.89           C  
ANISOU  999  CB  LEU A 118     4568   5960   5390   -207   1193   -783       C  
ATOM   1000  CG  LEU A 118      22.998  44.688  36.354  1.00 47.42           C  
ANISOU 1000  CG  LEU A 118     5454   6623   5941   -177   1158   -789       C  
ATOM   1001  CD1 LEU A 118      23.918  44.761  35.147  1.00 40.63           C  
ANISOU 1001  CD1 LEU A 118     4715   5584   5139   -141    990   -753       C  
ATOM   1002  CD2 LEU A 118      22.901  46.042  37.026  1.00 51.74           C  
ANISOU 1002  CD2 LEU A 118     5990   7232   6437    -73   1224   -960       C  
ATOM   1003  N   ASP A 119      18.541  44.884  36.628  1.00 42.50           N  
ANISOU 1003  N   ASP A 119     4161   6344   5643   -143   1429   -985       N  
ATOM   1004  CA  ASP A 119      17.125  44.869  36.287  1.00 46.94           C  
ANISOU 1004  CA  ASP A 119     4473   7003   6359   -126   1462  -1039       C  
ATOM   1005  C   ASP A 119      16.956  44.998  34.775  1.00 43.54           C  
ANISOU 1005  C   ASP A 119     4023   6415   6105    -57   1266  -1043       C  
ATOM   1006  O   ASP A 119      16.751  46.081  34.222  1.00 50.70           O  
ANISOU 1006  O   ASP A 119     4905   7262   7096    122   1187  -1154       O  
ATOM   1007  CB  ASP A 119      16.388  45.970  37.040  1.00 62.52           C  
ANISOU 1007  CB  ASP A 119     6306   9127   8321     19   1591  -1214       C  
ATOM   1008  CG  ASP A 119      14.932  46.103  36.600  1.00 73.50           C  
ANISOU 1008  CG  ASP A 119     7410  10629   9886     78   1607  -1289       C  
ATOM   1009  OD1 ASP A 119      14.295  45.061  36.317  1.00 72.58           O  
ANISOU 1009  OD1 ASP A 119     7158  10579   9841    -79   1614  -1192       O  
ATOM   1010  OD2 ASP A 119      14.436  47.251  36.515  1.00 79.43           O  
ANISOU 1010  OD2 ASP A 119     8073  11396  10709    283   1605  -1447       O  
ATOM   1011  N   PHE A 120      17.041  43.861  34.090  1.00 39.76           N  
ANISOU 1011  N   PHE A 120     3570   5863   5675   -199   1183   -916       N  
ATOM   1012  CA  PHE A 120      16.689  43.808  32.678  1.00 35.36           C  
ANISOU 1012  CA  PHE A 120     2964   5200   5273   -161   1007   -921       C  
ATOM   1013  C   PHE A 120      16.141  42.424  32.352  1.00 38.84           C  
ANISOU 1013  C   PHE A 120     3318   5660   5780   -361    995   -821       C  
ATOM   1014  O   PHE A 120      16.094  41.532  33.202  1.00 41.07           O  
ANISOU 1014  O   PHE A 120     3598   6013   5993   -526   1123   -735       O  
ATOM   1015  CB  PHE A 120      17.879  44.190  31.789  1.00 39.41           C  
ANISOU 1015  CB  PHE A 120     3705   5508   5760    -78    846   -898       C  
ATOM   1016  CG  PHE A 120      19.046  43.212  31.827  1.00 39.94           C  
ANISOU 1016  CG  PHE A 120     3976   5476   5724   -204    824   -768       C  
ATOM   1017  CD1 PHE A 120      19.074  42.107  30.991  1.00 37.60           C  
ANISOU 1017  CD1 PHE A 120     3710   5093   5484   -315    729   -681       C  
ATOM   1018  CD2 PHE A 120      20.131  43.430  32.663  1.00 42.26           C  
ANISOU 1018  CD2 PHE A 120     4431   5763   5864   -198    887   -745       C  
ATOM   1019  CE1 PHE A 120      20.162  41.215  31.002  1.00 39.33           C  
ANISOU 1019  CE1 PHE A 120     4120   5209   5614   -399    706   -570       C  
ATOM   1020  CE2 PHE A 120      21.233  42.547  32.676  1.00 39.96           C  
ANISOU 1020  CE2 PHE A 120     4314   5389   5479   -285    855   -625       C  
ATOM   1021  CZ  PHE A 120      21.243  41.442  31.847  1.00 39.12           C  
ANISOU 1021  CZ  PHE A 120     4239   5186   5438   -375    768   -537       C  
ATOM   1022  N   TYR A 121      15.716  42.248  31.108  1.00 38.96           N  
ANISOU 1022  N   TYR A 121     3270   5606   5926   -351    837   -833       N  
ATOM   1023  CA  TYR A 121      15.202  40.958  30.684  1.00 41.89           C  
ANISOU 1023  CA  TYR A 121     3571   5972   6372   -550    804   -760       C  
ATOM   1024  C   TYR A 121      15.610  40.732  29.241  1.00 43.90           C  
ANISOU 1024  C   TYR A 121     3937   6058   6685   -524    591   -750       C  
ATOM   1025  O   TYR A 121      16.107  41.637  28.558  1.00 34.20           O  
ANISOU 1025  O   TYR A 121     2799   4747   5448   -351    478   -795       O  
ATOM   1026  CB  TYR A 121      13.677  40.860  30.853  1.00 44.58           C  
ANISOU 1026  CB  TYR A 121     3592   6514   6831   -614    871   -820       C  
ATOM   1027  CG  TYR A 121      12.923  41.678  29.844  1.00 46.31           C  
ANISOU 1027  CG  TYR A 121     3644   6770   7181   -449    726   -932       C  
ATOM   1028  CD1 TYR A 121      12.771  43.043  30.017  1.00 45.27           C  
ANISOU 1028  CD1 TYR A 121     3456   6691   7052   -210    739  -1037       C  
ATOM   1029  CD2 TYR A 121      12.370  41.085  28.705  1.00 50.04           C  
ANISOU 1029  CD2 TYR A 121     4025   7218   7769   -528    566   -933       C  
ATOM   1030  CE1 TYR A 121      12.085  43.802  29.096  1.00 53.39           C  
ANISOU 1030  CE1 TYR A 121     4343   7743   8198    -38    596  -1123       C  
ATOM   1031  CE2 TYR A 121      11.687  41.836  27.769  1.00 49.78           C  
ANISOU 1031  CE2 TYR A 121     3841   7233   7841   -365    416  -1024       C  
ATOM   1032  CZ  TYR A 121      11.544  43.200  27.974  1.00 56.07           C  
ANISOU 1032  CZ  TYR A 121     4585   8078   8641   -112    432  -1110       C  
ATOM   1033  OH  TYR A 121      10.877  43.987  27.060  1.00 58.42           O  
ANISOU 1033  OH  TYR A 121     4745   8412   9039     76    276  -1186       O  
ATOM   1034  N   THR A 122      15.393  39.497  28.793  1.00 41.53           N  
ANISOU 1034  N   THR A 122     3638   5704   6436   -709    542   -689       N  
ATOM   1035  CA  THR A 122      15.743  39.026  27.464  1.00 35.87           C  
ANISOU 1035  CA  THR A 122     3033   4836   5760   -721    353   -683       C  
ATOM   1036  C   THR A 122      14.581  38.207  26.925  1.00 43.05           C  
ANISOU 1036  C   THR A 122     3751   5803   6802   -884    295   -708       C  
ATOM   1037  O   THR A 122      13.987  37.410  27.652  1.00 42.46           O  
ANISOU 1037  O   THR A 122     3573   5800   6758  -1076    416   -665       O  
ATOM   1038  CB  THR A 122      17.017  38.175  27.509  1.00 38.05           C  
ANISOU 1038  CB  THR A 122     3584   4936   5938   -789    350   -582       C  
ATOM   1039  OG1 THR A 122      18.135  39.023  27.793  1.00 37.68           O  
ANISOU 1039  OG1 THR A 122     3697   4846   5774   -631    367   -573       O  
ATOM   1040  CG2 THR A 122      17.239  37.420  26.182  1.00 33.35           C  
ANISOU 1040  CG2 THR A 122     3090   4194   5387   -837    176   -586       C  
ATOM   1041  N   GLU A 123      14.257  38.427  25.656  1.00 45.85           N  
ANISOU 1041  N   GLU A 123     4058   6137   7225   -817    108   -777       N  
ATOM   1042  CA  GLU A 123      13.131  37.805  24.975  1.00 46.38           C  
ANISOU 1042  CA  GLU A 123     3926   6278   7419   -954     13   -828       C  
ATOM   1043  C   GLU A 123      13.684  37.192  23.700  1.00 48.38           C  
ANISOU 1043  C   GLU A 123     4360   6362   7659   -983   -175   -834       C  
ATOM   1044  O   GLU A 123      14.279  37.902  22.881  1.00 45.84           O  
ANISOU 1044  O   GLU A 123     4158   5978   7283   -802   -298   -857       O  
ATOM   1045  CB  GLU A 123      12.074  38.854  24.650  1.00 54.31           C  
ANISOU 1045  CB  GLU A 123     4658   7468   8508   -800    -50   -928       C  
ATOM   1046  CG  GLU A 123      10.644  38.427  24.812  1.00 71.96           C  
ANISOU 1046  CG  GLU A 123     6566   9903  10872   -951    -22   -979       C  
ATOM   1047  CD  GLU A 123       9.699  39.621  24.786  1.00 82.60           C  
ANISOU 1047  CD  GLU A 123     7638  11455  12291   -744    -44  -1073       C  
ATOM   1048  OE1 GLU A 123       9.880  40.512  23.923  1.00 84.38           O  
ANISOU 1048  OE1 GLU A 123     7913  11640  12509   -520   -203  -1113       O  
ATOM   1049  OE2 GLU A 123       8.792  39.678  25.642  1.00 84.89           O  
ANISOU 1049  OE2 GLU A 123     7669  11947  12640   -797    104  -1103       O  
ATOM   1050  N   SER A 124      13.541  35.886  23.536  1.00 48.43           N  
ANISOU 1050  N   SER A 124     4407   6285   7708  -1210   -190   -812       N  
ATOM   1051  CA  SER A 124      14.127  35.262  22.361  1.00 55.61           C  
ANISOU 1051  CA  SER A 124     5511   7027   8593  -1231   -357   -834       C  
ATOM   1052  C   SER A 124      13.051  34.978  21.326  1.00 50.56           C  
ANISOU 1052  C   SER A 124     4687   6469   8056  -1320   -527   -937       C  
ATOM   1053  O   SER A 124      11.891  34.738  21.657  1.00 55.00           O  
ANISOU 1053  O   SER A 124     4993   7178   8728  -1465   -492   -969       O  
ATOM   1054  CB  SER A 124      14.870  33.976  22.718  1.00 66.62           C  
ANISOU 1054  CB  SER A 124     7133   8223   9956  -1395   -289   -755       C  
ATOM   1055  OG  SER A 124      13.958  32.994  23.150  1.00 79.17           O  
ANISOU 1055  OG  SER A 124     8595   9835  11651  -1655   -227   -743       O  
ATOM   1056  N   LYS A 125      13.438  35.059  20.065  1.00 50.50           N  
ANISOU 1056  N   LYS A 125     4799   6388   8001  -1229   -713   -993       N  
ATOM   1057  CA  LYS A 125      12.596  34.648  18.958  1.00 48.01           C  
ANISOU 1057  CA  LYS A 125     4361   6129   7751  -1322   -903  -1097       C  
ATOM   1058  C   LYS A 125      13.280  33.507  18.225  1.00 57.15           C  
ANISOU 1058  C   LYS A 125     5770   7078   8865  -1439   -988  -1121       C  
ATOM   1059  O   LYS A 125      14.428  33.147  18.505  1.00 58.81           O  
ANISOU 1059  O   LYS A 125     6239   7111   8994  -1409   -908  -1055       O  
ATOM   1060  CB  LYS A 125      12.311  35.798  17.991  1.00 50.21           C  
ANISOU 1060  CB  LYS A 125     4546   6533   7997  -1097  -1074  -1155       C  
ATOM   1061  CG  LYS A 125      11.851  37.085  18.635  1.00 55.81           C  
ANISOU 1061  CG  LYS A 125     5065   7404   8735   -912   -999  -1135       C  
ATOM   1062  CD  LYS A 125      11.497  38.103  17.569  1.00 59.76           C  
ANISOU 1062  CD  LYS A 125     5487   8004   9214   -697  -1194  -1183       C  
ATOM   1063  N   THR A 126      12.555  32.941  17.268  1.00 62.84           N  
ANISOU 1063  N   THR A 126     6406   7829   9640  -1566  -1157  -1229       N  
ATOM   1064  CA  THR A 126      13.110  31.862  16.467  1.00 65.79           C  
ANISOU 1064  CA  THR A 126     7016   8008   9974  -1672  -1254  -1286       C  
ATOM   1065  C   THR A 126      14.042  32.397  15.391  1.00 62.93           C  
ANISOU 1065  C   THR A 126     6854   7599   9459  -1450  -1380  -1315       C  
ATOM   1066  O   THR A 126      15.101  31.812  15.146  1.00 66.13           O  
ANISOU 1066  O   THR A 126     7531   7816   9781  -1431  -1364  -1308       O  
ATOM   1067  CB  THR A 126      11.978  31.044  15.861  1.00 68.62           C  
ANISOU 1067  CB  THR A 126     7212   8419  10441  -1912  -1391  -1407       C  
ATOM   1068  OG1 THR A 126      11.159  30.561  16.926  1.00 64.44           O  
ANISOU 1068  OG1 THR A 126     6495   7940  10050  -2136  -1248  -1363       O  
ATOM   1069  CG2 THR A 126      12.527  29.871  15.090  1.00 70.69           C  
ANISOU 1069  CG2 THR A 126     7734   8456  10668  -2032  -1483  -1486       C  
ATOM   1070  N   ASN A 127      13.682  33.507  14.747  1.00 59.84           N  
ANISOU 1070  N   ASN A 127     6335   7377   9023  -1272  -1500  -1341       N  
ATOM   1071  CA  ASN A 127      14.606  34.134  13.811  1.00 55.19           C  
ANISOU 1071  CA  ASN A 127     5941   6755   8274  -1061  -1594  -1339       C  
ATOM   1072  C   ASN A 127      15.744  34.762  14.605  1.00 54.10           C  
ANISOU 1072  C   ASN A 127     5956   6536   8064   -908  -1423  -1218       C  
ATOM   1073  O   ASN A 127      15.506  35.561  15.514  1.00 56.88           O  
ANISOU 1073  O   ASN A 127     6179   6969   8462   -837  -1311  -1149       O  
ATOM   1074  CB  ASN A 127      13.891  35.174  12.958  1.00 55.11           C  
ANISOU 1074  CB  ASN A 127     5766   6939   8236   -912  -1768  -1375       C  
ATOM   1075  CG  ASN A 127      13.204  36.228  13.795  1.00 72.40           C  
ANISOU 1075  CG  ASN A 127     7718   9277  10514   -808  -1690  -1315       C  
ATOM   1076  OD1 ASN A 127      12.521  35.908  14.769  1.00 78.13           O  
ANISOU 1076  OD1 ASN A 127     8261  10054  11369   -941  -1573  -1309       O  
ATOM   1077  ND2 ASN A 127      13.393  37.496  13.434  1.00 75.36           N  
ANISOU 1077  ND2 ASN A 127     8102   9716  10816   -568  -1746  -1268       N  
ATOM   1078  N   ARG A 128      16.975  34.388  14.273  1.00 42.06           N  
ANISOU 1078  N   ARG A 128     4697   4860   6423   -860  -1402  -1203       N  
ATOM   1079  CA  ARG A 128      18.142  34.806  15.023  1.00 42.02           C  
ANISOU 1079  CA  ARG A 128     4839   4778   6347   -745  -1245  -1097       C  
ATOM   1080  C   ARG A 128      18.795  36.031  14.403  1.00 37.37           C  
ANISOU 1080  C   ARG A 128     4324   4244   5629   -530  -1295  -1061       C  
ATOM   1081  O   ARG A 128      18.756  36.256  13.190  1.00 40.65           O  
ANISOU 1081  O   ARG A 128     4781   4704   5962   -466  -1449  -1114       O  
ATOM   1082  CB  ARG A 128      19.167  33.673  15.114  1.00 39.95           C  
ANISOU 1082  CB  ARG A 128     4811   4328   6040   -807  -1181  -1093       C  
ATOM   1083  CG  ARG A 128      18.603  32.420  15.737  1.00 46.82           C  
ANISOU 1083  CG  ARG A 128     5652   5101   7037  -1028  -1128  -1108       C  
ATOM   1084  CD  ARG A 128      19.538  31.249  15.560  1.00 49.95           C  
ANISOU 1084  CD  ARG A 128     6298   5287   7392  -1067  -1107  -1125       C  
ATOM   1085  NE  ARG A 128      20.643  31.291  16.503  1.00 49.70           N  
ANISOU 1085  NE  ARG A 128     6396   5178   7310   -978   -951  -1008       N  
ATOM   1086  CZ  ARG A 128      20.754  30.524  17.589  1.00 51.05           C  
ANISOU 1086  CZ  ARG A 128     6613   5237   7546  -1082   -823   -926       C  
ATOM   1087  NH1 ARG A 128      19.820  29.621  17.900  1.00 40.89           N  
ANISOU 1087  NH1 ARG A 128     5263   3885   6388  -1300   -818   -943       N  
ATOM   1088  NH2 ARG A 128      21.831  30.647  18.360  1.00 48.03           N  
ANISOU 1088  NH2 ARG A 128     6346   4810   7093   -974   -704   -822       N  
ATOM   1089  N   LEU A 129      19.424  36.806  15.260  1.00 40.28           N  
ANISOU 1089  N   LEU A 129     4722   4609   5975   -431  -1160   -969       N  
ATOM   1090  CA  LEU A 129      20.317  37.871  14.835  1.00 33.66           C  
ANISOU 1090  CA  LEU A 129     4000   3778   5011   -257  -1169   -918       C  
ATOM   1091  C   LEU A 129      21.685  37.251  14.561  1.00 33.38           C  
ANISOU 1091  C   LEU A 129     4193   3632   4858   -248  -1125   -905       C  
ATOM   1092  O   LEU A 129      22.359  36.788  15.480  1.00 28.59           O  
ANISOU 1092  O   LEU A 129     3653   2951   4260   -283   -990   -860       O  
ATOM   1093  CB  LEU A 129      20.352  38.946  15.914  1.00 32.09           C  
ANISOU 1093  CB  LEU A 129     3727   3618   4848   -175  -1046   -844       C  
ATOM   1094  CG  LEU A 129      18.937  39.411  16.299  1.00 34.64           C  
ANISOU 1094  CG  LEU A 129     3801   4057   5303   -180  -1070   -873       C  
ATOM   1095  CD1 LEU A 129      18.950  40.497  17.380  1.00 34.66           C  
ANISOU 1095  CD1 LEU A 129     3738   4094   5336    -83   -943   -823       C  
ATOM   1096  CD2 LEU A 129      18.190  39.911  15.075  1.00 31.94           C  
ANISOU 1096  CD2 LEU A 129     3383   3801   4952    -99  -1265   -917       C  
ATOM   1097  N   THR A 130      22.110  37.245  13.303  1.00 31.64           N  
ANISOU 1097  N   THR A 130     4088   3415   4517   -191  -1237   -945       N  
ATOM   1098  CA  THR A 130      23.274  36.466  12.911  1.00 32.70           C  
ANISOU 1098  CA  THR A 130     4417   3462   4546   -185  -1206   -965       C  
ATOM   1099  C   THR A 130      24.074  37.198  11.854  1.00 34.82           C  
ANISOU 1099  C   THR A 130     4803   3783   4645    -59  -1259   -949       C  
ATOM   1100  O   THR A 130      23.502  37.681  10.873  1.00 36.56           O  
ANISOU 1100  O   THR A 130     4994   4083   4813    -22  -1397   -976       O  
ATOM   1101  CB  THR A 130      22.825  35.103  12.357  1.00 37.27           C  
ANISOU 1101  CB  THR A 130     5031   3971   5160   -305  -1289  -1080       C  
ATOM   1102  OG1 THR A 130      22.065  34.435  13.362  1.00 43.14           O  
ANISOU 1102  OG1 THR A 130     5666   4662   6064   -446  -1229  -1078       O  
ATOM   1103  CG2 THR A 130      24.033  34.222  11.950  1.00 39.86           C  
ANISOU 1103  CG2 THR A 130     5568   4193   5385   -274  -1253  -1120       C  
ATOM   1104  N   GLY A 131      25.379  37.249  12.044  1.00 26.98           N  
ANISOU 1104  N   GLY A 131     3936   2756   3559      0  -1153   -901       N  
ATOM   1105  CA  GLY A 131      26.290  37.702  11.019  1.00 30.37           C  
ANISOU 1105  CA  GLY A 131     4490   3237   3813     92  -1180   -891       C  
ATOM   1106  C   GLY A 131      27.502  38.371  11.648  1.00 27.32           C  
ANISOU 1106  C   GLY A 131     4155   2857   3370    152  -1042   -794       C  
ATOM   1107  O   GLY A 131      27.717  38.307  12.857  1.00 26.27           O  
ANISOU 1107  O   GLY A 131     3979   2681   3321    127   -932   -751       O  
ATOM   1108  N   ASP A 132      28.297  39.004  10.786  1.00 26.55           N  
ANISOU 1108  N   ASP A 132     4149   2824   3116    221  -1050   -762       N  
ATOM   1109  CA  ASP A 132      29.413  39.823  11.246  1.00 26.54           C  
ANISOU 1109  CA  ASP A 132     4182   2849   3053    260   -934   -670       C  
ATOM   1110  C   ASP A 132      28.902  41.029  12.026  1.00 31.35           C  
ANISOU 1110  C   ASP A 132     4707   3452   3754    261   -914   -590       C  
ATOM   1111  O   ASP A 132      27.872  41.620  11.687  1.00 35.27           O  
ANISOU 1111  O   ASP A 132     5148   3959   4295    278  -1013   -584       O  
ATOM   1112  CB  ASP A 132      30.250  40.312  10.063  1.00 34.23           C  
ANISOU 1112  CB  ASP A 132     5263   3906   3837    311   -949   -645       C  
ATOM   1113  CG  ASP A 132      30.936  39.177   9.294  1.00 42.71           C  
ANISOU 1113  CG  ASP A 132     6427   5002   4797    332   -944   -738       C  
ATOM   1114  OD1 ASP A 132      31.250  38.116   9.890  1.00 44.10           O  
ANISOU 1114  OD1 ASP A 132     6605   5114   5036    325   -886   -795       O  
ATOM   1115  OD2 ASP A 132      31.152  39.357   8.073  1.00 44.76           O  
ANISOU 1115  OD2 ASP A 132     6765   5343   4898    365  -1000   -753       O  
ATOM   1116  N   ILE A 133      29.625  41.415  13.070  1.00 27.47           N  
ANISOU 1116  N   ILE A 133     4204   2948   3286    253   -792   -537       N  
ATOM   1117  CA  ILE A 133      29.257  42.609  13.809  1.00 25.36           C  
ANISOU 1117  CA  ILE A 133     3878   2666   3092    261   -764   -479       C  
ATOM   1118  C   ILE A 133      30.487  43.492  13.997  1.00 28.12           C  
ANISOU 1118  C   ILE A 133     4295   3036   3353    265   -677   -409       C  
ATOM   1119  O   ILE A 133      31.588  43.009  14.276  1.00 25.98           O  
ANISOU 1119  O   ILE A 133     4055   2797   3020    247   -593   -409       O  
ATOM   1120  CB  ILE A 133      28.564  42.274  15.148  1.00 27.27           C  
ANISOU 1120  CB  ILE A 133     4007   2873   3481    221   -708   -501       C  
ATOM   1121  CG1 ILE A 133      28.237  43.561  15.926  1.00 26.02           C  
ANISOU 1121  CG1 ILE A 133     3797   2704   3387    245   -669   -463       C  
ATOM   1122  CG2 ILE A 133      29.378  41.271  15.990  1.00 24.17           C  
ANISOU 1122  CG2 ILE A 133     3632   2470   3083    182   -604   -508       C  
ATOM   1123  CD1 ILE A 133      27.199  43.327  17.014  1.00 22.86           C  
ANISOU 1123  CD1 ILE A 133     3263   2298   3125    218   -634   -498       C  
ATOM   1124  N   VAL A 134      30.297  44.788  13.778  1.00 26.56           N  
ANISOU 1124  N   VAL A 134     4122   2819   3151    288   -704   -351       N  
ATOM   1125  CA  VAL A 134      31.323  45.804  13.936  1.00 24.42           C  
ANISOU 1125  CA  VAL A 134     3917   2548   2812    266   -631   -283       C  
ATOM   1126  C   VAL A 134      30.735  46.865  14.861  1.00 25.58           C  
ANISOU 1126  C   VAL A 134     4024   2620   3075    276   -613   -269       C  
ATOM   1127  O   VAL A 134      29.657  47.393  14.581  1.00 29.00           O  
ANISOU 1127  O   VAL A 134     4436   3006   3578    336   -698   -265       O  
ATOM   1128  CB  VAL A 134      31.739  46.407  12.584  1.00 22.47           C  
ANISOU 1128  CB  VAL A 134     3782   2328   2428    278   -683   -216       C  
ATOM   1129  CG1 VAL A 134      32.855  47.440  12.770  1.00 22.43           C  
ANISOU 1129  CG1 VAL A 134     3844   2320   2358    221   -596   -140       C  
ATOM   1130  CG2 VAL A 134      32.181  45.272  11.618  1.00 25.67           C  
ANISOU 1130  CG2 VAL A 134     4222   2821   2711    285   -704   -258       C  
ATOM   1131  N   ILE A 135      31.419  47.143  15.975  1.00 26.03           N  
ANISOU 1131  N   ILE A 135     4065   2674   3150    228   -506   -273       N  
ATOM   1132  CA  ILE A 135      30.981  48.102  16.987  1.00 23.86           C  
ANISOU 1132  CA  ILE A 135     3760   2331   2973    235   -471   -285       C  
ATOM   1133  C   ILE A 135      32.056  49.170  17.144  1.00 25.85           C  
ANISOU 1133  C   ILE A 135     4101   2555   3165    176   -412   -240       C  
ATOM   1134  O   ILE A 135      33.248  48.853  17.127  1.00 24.93           O  
ANISOU 1134  O   ILE A 135     4006   2514   2953    108   -353   -223       O  
ATOM   1135  CB  ILE A 135      30.744  47.391  18.337  1.00 30.60           C  
ANISOU 1135  CB  ILE A 135     4510   3219   3898    213   -395   -348       C  
ATOM   1136  CG1 ILE A 135      29.694  46.297  18.192  1.00 22.80           C  
ANISOU 1136  CG1 ILE A 135     3435   2251   2976    238   -445   -386       C  
ATOM   1137  CG2 ILE A 135      30.469  48.390  19.495  1.00 25.05           C  
ANISOU 1137  CG2 ILE A 135     3782   2468   3267    215   -336   -380       C  
ATOM   1138  CD1 ILE A 135      30.205  44.977  18.749  1.00 30.22           C  
ANISOU 1138  CD1 ILE A 135     4347   3243   3891    189   -384   -403       C  
ATOM   1139  N   GLU A 136      31.646  50.430  17.340  1.00 24.27           N  
ANISOU 1139  N   GLU A 136     3948   2246   3027    199   -427   -228       N  
ATOM   1140  CA  GLU A 136      32.580  51.504  17.625  1.00 22.94           C  
ANISOU 1140  CA  GLU A 136     3870   2023   2824    120   -370   -199       C  
ATOM   1141  C   GLU A 136      32.344  52.006  19.045  1.00 31.16           C  
ANISOU 1141  C   GLU A 136     4869   3018   3954    113   -306   -280       C  
ATOM   1142  O   GLU A 136      31.287  52.580  19.347  1.00 31.09           O  
ANISOU 1142  O   GLU A 136     4847   2916   4050    201   -336   -318       O  
ATOM   1143  CB  GLU A 136      32.449  52.658  16.611  1.00 26.52           C  
ANISOU 1143  CB  GLU A 136     4459   2354   3262    141   -438   -110       C  
ATOM   1144  CG  GLU A 136      32.766  52.268  15.168  1.00 28.26           C  
ANISOU 1144  CG  GLU A 136     4739   2639   3360    138   -494    -23       C  
ATOM   1145  CD  GLU A 136      34.215  51.846  14.937  1.00 33.59           C  
ANISOU 1145  CD  GLU A 136     5426   3437   3900     20   -412      4       C  
ATOM   1146  OE1 GLU A 136      35.063  52.022  15.838  1.00 30.98           O  
ANISOU 1146  OE1 GLU A 136     5067   3134   3569    -71   -323    -28       O  
ATOM   1147  OE2 GLU A 136      34.506  51.300  13.848  1.00 40.52           O  
ANISOU 1147  OE2 GLU A 136     6330   4402   4664     25   -440     48       O  
ATOM   1148  N   SER A 137      33.350  51.835  19.893  1.00 26.44           N  
ANISOU 1148  N   SER A 137     4248   2495   3303     16   -221   -311       N  
ATOM   1149  CA  SER A 137      33.290  52.145  21.315  1.00 23.02           C  
ANISOU 1149  CA  SER A 137     3772   2059   2915     -6   -154   -399       C  
ATOM   1150  C   SER A 137      34.313  53.221  21.634  1.00 25.90           C  
ANISOU 1150  C   SER A 137     4225   2375   3240   -120   -113   -404       C  
ATOM   1151  O   SER A 137      35.367  53.281  20.993  1.00 26.47           O  
ANISOU 1151  O   SER A 137     4341   2491   3225   -212   -107   -340       O  
ATOM   1152  CB  SER A 137      33.604  50.866  22.140  1.00 20.59           C  
ANISOU 1152  CB  SER A 137     3354   1906   2564    -27    -99   -431       C  
ATOM   1153  OG  SER A 137      33.835  51.141  23.505  1.00 25.08           O  
ANISOU 1153  OG  SER A 137     3891   2509   3128    -71    -30   -504       O  
ATOM   1154  N   ASP A 138      34.008  54.084  22.625  1.00 31.38           N  
ANISOU 1154  N   ASP A 138     4943   2985   3995   -122    -81   -491       N  
ATOM   1155  CA  ASP A 138      35.014  55.039  23.087  1.00 32.84           C  
ANISOU 1155  CA  ASP A 138     5207   3128   4143   -257    -41   -521       C  
ATOM   1156  C   ASP A 138      36.027  54.388  24.027  1.00 36.83           C  
ANISOU 1156  C   ASP A 138     5621   3820   4552   -357     19   -565       C  
ATOM   1157  O   ASP A 138      37.196  54.772  24.035  1.00 59.54           O  
ANISOU 1157  O   ASP A 138     8524   6740   7359   -496     39   -555       O  
ATOM   1158  CB  ASP A 138      34.387  56.295  23.763  1.00 32.17           C  
ANISOU 1158  CB  ASP A 138     5207   2862   4154   -224    -34   -616       C  
ATOM   1159  CG  ASP A 138      33.320  55.975  24.815  1.00 36.60           C  
ANISOU 1159  CG  ASP A 138     5672   3459   4776   -107     -1   -726       C  
ATOM   1160  OD1 ASP A 138      33.360  54.893  25.435  1.00 34.66           O  
ANISOU 1160  OD1 ASP A 138     5303   3388   4477   -109     38   -744       O  
ATOM   1161  OD2 ASP A 138      32.401  56.818  25.007  1.00 35.92           O  
ANISOU 1161  OD2 ASP A 138     5635   3222   4792     -4    -11   -790       O  
ATOM   1162  N   THR A 139      35.606  53.427  24.818  1.00 29.87           N  
ANISOU 1162  N   THR A 139     4630   3054   3664   -294     45   -608       N  
ATOM   1163  CA  THR A 139      36.470  52.738  25.767  1.00 33.89           C  
ANISOU 1163  CA  THR A 139     5056   3744   4077   -361     90   -636       C  
ATOM   1164  C   THR A 139      37.220  51.567  25.116  1.00 33.61           C  
ANISOU 1164  C   THR A 139     4957   3848   3965   -362     79   -547       C  
ATOM   1165  O   THR A 139      38.395  51.334  25.404  1.00 27.71           O  
ANISOU 1165  O   THR A 139     4167   3238   3125   -442     97   -540       O  
ATOM   1166  CB  THR A 139      35.609  52.229  26.920  1.00 38.01           C  
ANISOU 1166  CB  THR A 139     5506   4317   4618   -287    129   -706       C  
ATOM   1167  OG1 THR A 139      34.835  53.321  27.428  1.00 44.61           O  
ANISOU 1167  OG1 THR A 139     6397   5023   5528   -258    145   -803       O  
ATOM   1168  CG2 THR A 139      36.465  51.601  28.026  1.00 37.30           C  
ANISOU 1168  CG2 THR A 139     5346   4413   4414   -348    168   -729       C  
ATOM   1169  N   PHE A 140      36.568  50.844  24.214  1.00 20.34           N  
ANISOU 1169  N   PHE A 140     3269   2140   2321   -270     43   -488       N  
ATOM   1170  CA  PHE A 140      37.145  49.636  23.637  1.00 21.97           C  
ANISOU 1170  CA  PHE A 140     3424   2460   2462   -246     34   -426       C  
ATOM   1171  C   PHE A 140      37.519  49.787  22.174  1.00 27.87           C  
ANISOU 1171  C   PHE A 140     4227   3182   3179   -255      0   -357       C  
ATOM   1172  O   PHE A 140      37.749  48.776  21.497  1.00 29.34           O  
ANISOU 1172  O   PHE A 140     4386   3439   3323   -206    -14   -320       O  
ATOM   1173  CB  PHE A 140      36.172  48.481  23.806  1.00 19.03           C  
ANISOU 1173  CB  PHE A 140     3000   2091   2138   -147     24   -424       C  
ATOM   1174  CG  PHE A 140      35.725  48.312  25.209  1.00 26.19           C  
ANISOU 1174  CG  PHE A 140     3857   3034   3061   -142     70   -477       C  
ATOM   1175  CD1 PHE A 140      36.652  48.047  26.200  1.00 24.46           C  
ANISOU 1175  CD1 PHE A 140     3599   2944   2752   -189    108   -487       C  
ATOM   1176  CD2 PHE A 140      34.387  48.463  25.554  1.00 30.15           C  
ANISOU 1176  CD2 PHE A 140     4342   3459   3655    -89     76   -517       C  
ATOM   1177  CE1 PHE A 140      36.249  47.913  27.537  1.00 21.62           C  
ANISOU 1177  CE1 PHE A 140     3201   2634   2379   -188    154   -532       C  
ATOM   1178  CE2 PHE A 140      33.967  48.317  26.871  1.00 27.76           C  
ANISOU 1178  CE2 PHE A 140     3989   3211   3349    -91    135   -566       C  
ATOM   1179  CZ  PHE A 140      34.899  48.035  27.869  1.00 23.69           C  
ANISOU 1179  CZ  PHE A 140     3453   2821   2728   -142    175   -570       C  
ATOM   1180  N   GLY A 141      37.589  51.017  21.667  1.00 21.74           N  
ANISOU 1180  N   GLY A 141     3540   2302   2417   -316    -13   -339       N  
ATOM   1181  CA  GLY A 141      37.933  51.187  20.261  1.00 24.29           C  
ANISOU 1181  CA  GLY A 141     3927   2612   2691   -332    -40   -258       C  
ATOM   1182  C   GLY A 141      36.982  50.401  19.368  1.00 31.59           C  
ANISOU 1182  C   GLY A 141     4856   3508   3640   -210   -100   -231       C  
ATOM   1183  O   GLY A 141      35.796  50.258  19.654  1.00 28.61           O  
ANISOU 1183  O   GLY A 141     4463   3053   3355   -126   -135   -264       O  
ATOM   1184  N   THR A 142      37.509  49.848  18.285  1.00 31.68           N  
ANISOU 1184  N   THR A 142     4877   3597   3562   -204   -109   -180       N  
ATOM   1185  CA  THR A 142      36.686  49.113  17.340  1.00 29.26           C  
ANISOU 1185  CA  THR A 142     4585   3271   3260   -103   -176   -166       C  
ATOM   1186  C   THR A 142      36.575  47.655  17.787  1.00 28.05           C  
ANISOU 1186  C   THR A 142     4344   3194   3118    -40   -168   -218       C  
ATOM   1187  O   THR A 142      37.595  46.968  17.913  1.00 30.96           O  
ANISOU 1187  O   THR A 142     4668   3682   3412    -51   -119   -223       O  
ATOM   1188  CB  THR A 142      37.301  49.188  15.944  1.00 25.24           C  
ANISOU 1188  CB  THR A 142     4142   2817   2631   -124   -187    -99       C  
ATOM   1189  OG1 THR A 142      37.294  50.546  15.466  1.00 26.53           O  
ANISOU 1189  OG1 THR A 142     4411   2882   2787   -187   -201    -27       O  
ATOM   1190  CG2 THR A 142      36.523  48.289  15.009  1.00 22.83           C  
ANISOU 1190  CG2 THR A 142     3848   2516   2312    -23   -261   -108       C  
ATOM   1191  N   ILE A 143      35.358  47.189  18.054  1.00 24.21           N  
ANISOU 1191  N   ILE A 143     3830   2641   2728     27   -212   -254       N  
ATOM   1192  CA  ILE A 143      35.136  45.790  18.444  1.00 22.10           C  
ANISOU 1192  CA  ILE A 143     3501   2413   2484     71   -207   -292       C  
ATOM   1193  C   ILE A 143      34.550  45.042  17.255  1.00 27.62           C  
ANISOU 1193  C   ILE A 143     4229   3093   3173    127   -283   -299       C  
ATOM   1194  O   ILE A 143      33.609  45.521  16.609  1.00 30.32           O  
ANISOU 1194  O   ILE A 143     4596   3371   3554    151   -357   -293       O  
ATOM   1195  CB  ILE A 143      34.182  45.645  19.642  1.00 20.87           C  
ANISOU 1195  CB  ILE A 143     3281   2211   2436     80   -192   -329       C  
ATOM   1196  CG1 ILE A 143      34.584  46.548  20.826  1.00 25.46           C  
ANISOU 1196  CG1 ILE A 143     3846   2806   3023     27   -127   -342       C  
ATOM   1197  CG2 ILE A 143      34.141  44.163  20.078  1.00 18.83           C  
ANISOU 1197  CG2 ILE A 143     2980   1986   2189    103   -175   -344       C  
ATOM   1198  CD1 ILE A 143      33.443  46.718  21.852  1.00 24.54           C  
ANISOU 1198  CD1 ILE A 143     3675   2643   3007     43   -109   -387       C  
ATOM   1199  N   VAL A 144      35.057  43.844  17.006  1.00 22.14           N  
ANISOU 1199  N   VAL A 144     3530   2451   2430    156   -273   -320       N  
ATOM   1200  CA  VAL A 144      34.685  43.055  15.840  1.00 24.59           C  
ANISOU 1200  CA  VAL A 144     3882   2752   2708    202   -341   -349       C  
ATOM   1201  C   VAL A 144      34.457  41.604  16.268  1.00 26.57           C  
ANISOU 1201  C   VAL A 144     4110   2975   3012    231   -339   -398       C  
ATOM   1202  O   VAL A 144      35.194  41.075  17.102  1.00 19.12           O  
ANISOU 1202  O   VAL A 144     3141   2062   2060    239   -273   -392       O  
ATOM   1203  CB  VAL A 144      35.805  43.157  14.788  1.00 33.43           C  
ANISOU 1203  CB  VAL A 144     5056   3965   3679    211   -321   -331       C  
ATOM   1204  CG1 VAL A 144      35.523  42.285  13.668  1.00 40.21           C  
ANISOU 1204  CG1 VAL A 144     5965   4827   4486    263   -383   -381       C  
ATOM   1205  CG2 VAL A 144      35.976  44.626  14.312  1.00 28.60           C  
ANISOU 1205  CG2 VAL A 144     4491   3360   3017    161   -324   -261       C  
ATOM   1206  N   GLY A 145      33.460  40.955  15.675  1.00 25.00           N  
ANISOU 1206  N   GLY A 145     3924   2714   2861    243   -419   -444       N  
ATOM   1207  CA  GLY A 145      33.228  39.534  15.918  1.00 24.96           C  
ANISOU 1207  CA  GLY A 145     3924   2653   2908    254   -424   -492       C  
ATOM   1208  C   GLY A 145      32.036  39.015  15.132  1.00 33.49           C  
ANISOU 1208  C   GLY A 145     5013   3670   4042    238   -528   -554       C  
ATOM   1209  O   GLY A 145      31.670  39.578  14.085  1.00 31.81           O  
ANISOU 1209  O   GLY A 145     4822   3485   3778    249   -605   -566       O  
ATOM   1210  N   PHE A 146      31.405  37.965  15.669  1.00 24.90           N  
ANISOU 1210  N   PHE A 146     3907   2499   3054    202   -533   -586       N  
ATOM   1211  CA  PHE A 146      30.328  37.230  15.036  1.00 27.02           C  
ANISOU 1211  CA  PHE A 146     4177   2704   3386    160   -629   -659       C  
ATOM   1212  C   PHE A 146      29.211  37.075  16.058  1.00 30.25           C  
ANISOU 1212  C   PHE A 146     4486   3066   3943     77   -615   -643       C  
ATOM   1213  O   PHE A 146      29.472  36.786  17.226  1.00 28.79           O  
ANISOU 1213  O   PHE A 146     4283   2857   3799     55   -523   -593       O  
ATOM   1214  CB  PHE A 146      30.833  35.869  14.526  1.00 26.25           C  
ANISOU 1214  CB  PHE A 146     4183   2537   3254    185   -641   -729       C  
ATOM   1215  CG  PHE A 146      29.767  34.999  13.945  1.00 26.51           C  
ANISOU 1215  CG  PHE A 146     4229   2487   3358    118   -741   -821       C  
ATOM   1216  CD1 PHE A 146      29.205  35.290  12.710  1.00 29.87           C  
ANISOU 1216  CD1 PHE A 146     4660   2961   3728    117   -858   -888       C  
ATOM   1217  CD2 PHE A 146      29.317  33.869  14.637  1.00 27.00           C  
ANISOU 1217  CD2 PHE A 146     4300   2420   3537     44   -724   -836       C  
ATOM   1218  CE1 PHE A 146      28.188  34.458  12.172  1.00 32.19           C  
ANISOU 1218  CE1 PHE A 146     4955   3190   4087     38   -965   -989       C  
ATOM   1219  CE2 PHE A 146      28.330  33.069  14.126  1.00 27.02           C  
ANISOU 1219  CE2 PHE A 146     4310   2341   3614    -46   -816   -926       C  
ATOM   1220  CZ  PHE A 146      27.765  33.348  12.883  1.00 32.18           C  
ANISOU 1220  CZ  PHE A 146     4957   3056   4215    -52   -941  -1013       C  
ATOM   1221  N   GLU A 147      27.982  37.345  15.644  1.00 27.60           N  
ANISOU 1221  N   GLU A 147     4072   2741   3675     34   -702   -679       N  
ATOM   1222  CA  GLU A 147      26.838  37.227  16.531  1.00 25.57           C  
ANISOU 1222  CA  GLU A 147     3691   2468   3556    -51   -684   -673       C  
ATOM   1223  C   GLU A 147      25.893  36.215  15.894  1.00 32.58           C  
ANISOU 1223  C   GLU A 147     4562   3304   4514   -137   -782   -756       C  
ATOM   1224  O   GLU A 147      25.845  36.064  14.665  1.00 33.09           O  
ANISOU 1224  O   GLU A 147     4680   3377   4517   -114   -893   -825       O  
ATOM   1225  CB  GLU A 147      26.129  38.592  16.784  1.00 23.62           C  
ANISOU 1225  CB  GLU A 147     3324   2301   3349    -21   -693   -646       C  
ATOM   1226  CG  GLU A 147      25.294  39.064  15.562  1.00 29.50           C  
ANISOU 1226  CG  GLU A 147     4027   3090   4090      9   -841   -694       C  
ATOM   1227  CD  GLU A 147      24.765  40.506  15.645  1.00 37.52           C  
ANISOU 1227  CD  GLU A 147     4959   4165   5131     84   -863   -659       C  
ATOM   1228  OE1 GLU A 147      24.352  40.988  16.739  1.00 33.01           O  
ANISOU 1228  OE1 GLU A 147     4288   3609   4644     80   -780   -638       O  
ATOM   1229  OE2 GLU A 147      24.761  41.155  14.582  1.00 40.22           O  
ANISOU 1229  OE2 GLU A 147     5344   4535   5402    154   -965   -654       O  
ATOM   1230  N   ASN A 148      25.184  35.494  16.745  1.00 25.74           N  
ANISOU 1230  N   ASN A 148     3627   2388   3765   -247   -738   -751       N  
ATOM   1231  CA  ASN A 148      24.270  34.451  16.311  1.00 31.25           C  
ANISOU 1231  CA  ASN A 148     4303   3022   4549   -368   -819   -829       C  
ATOM   1232  C   ASN A 148      23.375  34.101  17.486  1.00 36.78           C  
ANISOU 1232  C   ASN A 148     4878   3714   5382   -499   -739   -789       C  
ATOM   1233  O   ASN A 148      23.631  33.118  18.190  1.00 37.91           O  
ANISOU 1233  O   ASN A 148     5094   3747   5562   -576   -661   -750       O  
ATOM   1234  CB  ASN A 148      25.029  33.196  15.830  1.00 27.90           C  
ANISOU 1234  CB  ASN A 148     4058   2459   4082   -376   -834   -878       C  
ATOM   1235  CG  ASN A 148      24.095  32.106  15.333  1.00 34.04           C  
ANISOU 1235  CG  ASN A 148     4835   3148   4952   -520   -926   -976       C  
ATOM   1236  OD1 ASN A 148      22.936  32.376  14.979  1.00 32.35           O  
ANISOU 1236  OD1 ASN A 148     4477   3011   4802   -599  -1015  -1026       O  
ATOM   1237  ND2 ASN A 148      24.588  30.865  15.303  1.00 37.55           N  
ANISOU 1237  ND2 ASN A 148     5436   3425   5407   -554   -911  -1008       N  
ATOM   1238  N   HIS A 149      22.331  34.885  17.724  1.00 31.99           N  
ANISOU 1238  N   HIS A 149     4085   3224   4845   -521   -751   -791       N  
ATOM   1239  CA  HIS A 149      21.554  34.689  18.938  1.00 34.14           C  
ANISOU 1239  CA  HIS A 149     4223   3524   5224   -635   -645   -746       C  
ATOM   1240  C   HIS A 149      20.080  34.973  18.686  1.00 37.58           C  
ANISOU 1240  C   HIS A 149     4437   4074   5767   -707   -718   -808       C  
ATOM   1241  O   HIS A 149      19.732  35.900  17.952  1.00 33.84           O  
ANISOU 1241  O   HIS A 149     3885   3696   5275   -604   -819   -849       O  
ATOM   1242  CB  HIS A 149      22.111  35.559  20.080  1.00 30.28           C  
ANISOU 1242  CB  HIS A 149     3722   3095   4689   -549   -507   -659       C  
ATOM   1243  CG  HIS A 149      22.115  37.034  19.800  1.00 30.84           C  
ANISOU 1243  CG  HIS A 149     3729   3270   4718   -405   -539   -671       C  
ATOM   1244  ND1 HIS A 149      21.158  37.883  20.304  1.00 27.48           N  
ANISOU 1244  ND1 HIS A 149     3121   2958   4363   -387   -511   -682       N  
ATOM   1245  CD2 HIS A 149      23.004  37.823  19.140  1.00 32.51           C  
ANISOU 1245  CD2 HIS A 149     4046   3480   4826   -271   -585   -665       C  
ATOM   1246  CE1 HIS A 149      21.428  39.126  19.932  1.00 26.75           C  
ANISOU 1246  CE1 HIS A 149     3038   2904   4220   -242   -550   -685       C  
ATOM   1247  NE2 HIS A 149      22.550  39.119  19.236  1.00 31.54           N  
ANISOU 1247  NE2 HIS A 149     3821   3443   4720   -182   -592   -668       N  
ATOM   1248  N   GLY A 150      19.222  34.122  19.250  1.00 44.07           N  
ANISOU 1248  N   GLY A 150     5159   4885   6701   -889   -674   -810       N  
ATOM   1249  CA  GLY A 150      17.795  34.375  19.215  1.00 33.92           C  
ANISOU 1249  CA  GLY A 150     3620   3741   5528   -971   -718   -864       C  
ATOM   1250  C   GLY A 150      17.355  35.429  20.204  1.00 38.98           C  
ANISOU 1250  C   GLY A 150     4087   4530   6193   -897   -604   -821       C  
ATOM   1251  O   GLY A 150      16.329  36.082  19.988  1.00 35.96           O  
ANISOU 1251  O   GLY A 150     3489   4296   5879   -866   -661   -875       O  
ATOM   1252  N   GLY A 151      18.117  35.619  21.277  1.00 34.37           N  
ANISOU 1252  N   GLY A 151     3592   3916   5550   -856   -450   -735       N  
ATOM   1253  CA  GLY A 151      17.667  36.465  22.357  1.00 38.49           C  
ANISOU 1253  CA  GLY A 151     3959   4573   6091   -811   -321   -709       C  
ATOM   1254  C   GLY A 151      17.778  37.936  21.987  1.00 37.18           C  
ANISOU 1254  C   GLY A 151     3757   4481   5887   -596   -375   -744       C  
ATOM   1255  O   GLY A 151      18.755  38.374  21.383  1.00 33.34           O  
ANISOU 1255  O   GLY A 151     3440   3919   5309   -476   -437   -733       O  
ATOM   1256  N   ARG A 152      16.727  38.682  22.317  1.00 37.94           N  
ANISOU 1256  N   ARG A 152     3627   4727   6060   -552   -352   -787       N  
ATOM   1257  CA  ARG A 152      16.744  40.141  22.335  1.00 37.55           C  
ANISOU 1257  CA  ARG A 152     3539   4736   5991   -344   -361   -811       C  
ATOM   1258  C   ARG A 152      16.790  40.588  23.787  1.00 37.33           C  
ANISOU 1258  C   ARG A 152     3465   4773   5945   -328   -168   -790       C  
ATOM   1259  O   ARG A 152      15.873  40.288  24.563  1.00 36.71           O  
ANISOU 1259  O   ARG A 152     3197   4817   5935   -423    -65   -805       O  
ATOM   1260  CB  ARG A 152      15.511  40.728  21.651  1.00 37.96           C  
ANISOU 1260  CB  ARG A 152     3367   4913   6142   -265   -483   -886       C  
ATOM   1261  CG  ARG A 152      15.575  40.766  20.156  1.00 34.02           C  
ANISOU 1261  CG  ARG A 152     2935   4369   5622   -206   -693   -910       C  
ATOM   1262  CD  ARG A 152      15.326  39.377  19.542  1.00 34.85           C  
ANISOU 1262  CD  ARG A 152     3043   4445   5754   -405   -775   -934       C  
ATOM   1263  NE  ARG A 152      15.196  39.505  18.092  1.00 37.77           N  
ANISOU 1263  NE  ARG A 152     3443   4815   6094   -339   -988   -977       N  
ATOM   1264  CZ  ARG A 152      15.331  38.520  17.215  1.00 42.99           C  
ANISOU 1264  CZ  ARG A 152     4193   5413   6727   -456  -1099  -1012       C  
ATOM   1265  NH1 ARG A 152      15.629  37.290  17.607  1.00 35.65           N  
ANISOU 1265  NH1 ARG A 152     3348   4385   5811   -643  -1022  -1005       N  
ATOM   1266  NH2 ARG A 152      15.187  38.788  15.932  1.00 42.63           N  
ANISOU 1266  NH2 ARG A 152     4168   5396   6632   -375  -1291  -1053       N  
ATOM   1267  N   THR A 153      17.855  41.292  24.151  1.00 37.25           N  
ANISOU 1267  N   THR A 153     3623   4696   5835   -220   -117   -760       N  
ATOM   1268  CA  THR A 153      18.042  41.804  25.500  1.00 37.88           C  
ANISOU 1268  CA  THR A 153     3690   4834   5869   -193     53   -754       C  
ATOM   1269  C   THR A 153      17.689  43.290  25.527  1.00 36.67           C  
ANISOU 1269  C   THR A 153     3464   4727   5743      1     43   -827       C  
ATOM   1270  O   THR A 153      18.158  44.058  24.683  1.00 36.21           O  
ANISOU 1270  O   THR A 153     3513   4579   5665    128    -72   -833       O  
ATOM   1271  CB  THR A 153      19.483  41.587  25.970  1.00 37.53           C  
ANISOU 1271  CB  THR A 153     3876   4691   5691   -212    113   -683       C  
ATOM   1272  OG1 THR A 153      19.673  40.211  26.288  1.00 44.51           O  
ANISOU 1272  OG1 THR A 153     4811   5542   6559   -379    159   -611       O  
ATOM   1273  CG2 THR A 153      19.795  42.435  27.189  1.00 28.52           C  
ANISOU 1273  CG2 THR A 153     2745   3611   4482   -147    252   -700       C  
ATOM   1274  N   TYR A 154      16.865  43.682  26.489  1.00 38.06           N  
ANISOU 1274  N   TYR A 154     3463   5036   5961     25    167   -881       N  
ATOM   1275  CA  TYR A 154      16.365  45.051  26.628  1.00 38.78           C  
ANISOU 1275  CA  TYR A 154     3464   5172   6097    223    172   -969       C  
ATOM   1276  C   TYR A 154      16.818  45.557  27.989  1.00 36.14           C  
ANISOU 1276  C   TYR A 154     3185   4871   5676    245    348   -996       C  
ATOM   1277  O   TYR A 154      16.241  45.168  29.006  1.00 38.56           O  
ANISOU 1277  O   TYR A 154     3353   5320   5978    165    499  -1013       O  
ATOM   1278  CB  TYR A 154      14.839  45.086  26.482  1.00 37.64           C  
ANISOU 1278  CB  TYR A 154     3024   5189   6089    256    154  -1039       C  
ATOM   1279  CG  TYR A 154      14.364  44.524  25.155  1.00 39.58           C  
ANISOU 1279  CG  TYR A 154     3206   5425   6409    215    -33  -1022       C  
ATOM   1280  CD1 TYR A 154      14.504  45.253  23.989  1.00 41.07           C  
ANISOU 1280  CD1 TYR A 154     3470   5524   6610    372   -214  -1026       C  
ATOM   1281  CD2 TYR A 154      13.785  43.261  25.067  1.00 43.67           C  
ANISOU 1281  CD2 TYR A 154     3600   6018   6975      8    -32  -1001       C  
ATOM   1282  CE1 TYR A 154      14.089  44.758  22.772  1.00 39.03           C  
ANISOU 1282  CE1 TYR A 154     3163   5273   6395    338   -394  -1018       C  
ATOM   1283  CE2 TYR A 154      13.368  42.753  23.850  1.00 42.56           C  
ANISOU 1283  CE2 TYR A 154     3408   5869   6892    -37   -214  -1006       C  
ATOM   1284  CZ  TYR A 154      13.527  43.508  22.700  1.00 44.97           C  
ANISOU 1284  CZ  TYR A 154     3788   6106   7194    134   -397  -1018       C  
ATOM   1285  OH  TYR A 154      13.112  43.030  21.465  1.00 43.43           O  
ANISOU 1285  OH  TYR A 154     3547   5921   7032     95   -588  -1029       O  
ATOM   1286  N   HIS A 155      17.873  46.380  28.018  1.00 34.61           N  
ANISOU 1286  N   HIS A 155     3195   4555   5401    335    333   -997       N  
ATOM   1287  CA  HIS A 155      18.324  47.020  29.254  1.00 36.20           C  
ANISOU 1287  CA  HIS A 155     3457   4784   5513    369    479  -1048       C  
ATOM   1288  C   HIS A 155      18.565  48.510  29.037  1.00 35.84           C  
ANISOU 1288  C   HIS A 155     3502   4631   5485    559    429  -1127       C  
ATOM   1289  O   HIS A 155      18.731  48.975  27.907  1.00 37.27           O  
ANISOU 1289  O   HIS A 155     3759   4687   5714    643    279  -1104       O  
ATOM   1290  CB  HIS A 155      19.593  46.333  29.846  1.00 35.55           C  
ANISOU 1290  CB  HIS A 155     3558   4666   5283    231    539   -963       C  
ATOM   1291  CG  HIS A 155      20.862  46.542  29.076  1.00 34.16           C  
ANISOU 1291  CG  HIS A 155     3598   4333   5049    245    425   -910       C  
ATOM   1292  ND1 HIS A 155      21.612  47.699  29.168  1.00 36.33           N  
ANISOU 1292  ND1 HIS A 155     4006   4521   5275    338    413   -957       N  
ATOM   1293  CD2 HIS A 155      21.569  45.700  28.282  1.00 35.11           C  
ANISOU 1293  CD2 HIS A 155     3824   4375   5140    165    335   -816       C  
ATOM   1294  CE1 HIS A 155      22.697  47.579  28.423  1.00 33.82           C  
ANISOU 1294  CE1 HIS A 155     3849   4095   4905    307    321   -887       C  
ATOM   1295  NE2 HIS A 155      22.701  46.371  27.883  1.00 32.20           N  
ANISOU 1295  NE2 HIS A 155     3629   3899   4706    213    275   -805       N  
ATOM   1296  N  AASP A 156      18.595  49.251  30.146  0.45 35.75           N  
ANISOU 1296  N  AASP A 156     3495   4662   5425    620    559  -1220       N  
ATOM   1297  N  BASP A 156      18.586  49.261  30.143  0.55 35.38           N  
ANISOU 1297  N  BASP A 156     3447   4616   5380    621    558  -1221       N  
ATOM   1298  CA AASP A 156      18.773  50.699  30.130  0.45 38.55           C  
ANISOU 1298  CA AASP A 156     3946   4899   5802    794    534  -1316       C  
ATOM   1299  CA BASP A 156      18.778  50.710  30.113  0.55 38.72           C  
ANISOU 1299  CA BASP A 156     3969   4918   5825    795    531  -1315       C  
ATOM   1300  C  AASP A 156      20.145  51.131  30.657  0.45 37.55           C  
ANISOU 1300  C  AASP A 156     4049   4674   5543    740    567  -1318       C  
ATOM   1301  C  BASP A 156      20.151  51.136  30.644  0.55 37.52           C  
ANISOU 1301  C  BASP A 156     4047   4669   5540    741    565  -1317       C  
ATOM   1302  O  AASP A 156      20.298  52.247  31.153  0.45 37.68           O  
ANISOU 1302  O  AASP A 156     4142   4626   5550    842    607  -1427       O  
ATOM   1303  O  BASP A 156      20.314  52.253  31.134  0.55 37.52           O  
ANISOU 1303  O  BASP A 156     4124   4601   5529    842    604  -1425       O  
ATOM   1304  CB AASP A 156      17.660  51.376  30.931  0.45 39.58           C  
ANISOU 1304  CB AASP A 156     3899   5145   5995    934    647  -1459       C  
ATOM   1305  CB BASP A 156      17.670  51.418  30.897  0.55 39.26           C  
ANISOU 1305  CB BASP A 156     3863   5096   5957    941    641  -1460       C  
ATOM   1306  CG AASP A 156      16.313  51.305  30.234  0.45 43.85           C  
ANISOU 1306  CG AASP A 156     4204   5766   6690   1039    579  -1476       C  
ATOM   1307  CG BASP A 156      17.573  52.904  30.560  0.55 42.74           C  
ANISOU 1307  CG BASP A 156     4387   5378   6476   1162    575  -1557       C  
ATOM   1308  OD1AASP A 156      16.289  51.300  28.987  0.45 45.15           O  
ANISOU 1308  OD1AASP A 156     4399   5830   6925   1078    407  -1406       O  
ATOM   1309  OD1BASP A 156      18.055  53.289  29.472  0.55 42.93           O  
ANISOU 1309  OD1BASP A 156     4554   5223   6534   1203    419  -1487       O  
ATOM   1310  OD2AASP A 156      15.273  51.264  30.934  0.45 51.22           O  
ANISOU 1310  OD2AASP A 156     4913   6881   7667   1084    697  -1563       O  
ATOM   1311  OD2BASP A 156      17.032  53.690  31.381  0.55 51.74           O  
ANISOU 1311  OD2BASP A 156     5461   6562   7635   1296    680  -1702       O  
ATOM   1312  N   PHE A 157      21.152  50.274  30.541  1.00 37.45           N  
ANISOU 1312  N   PHE A 157     4147   4649   5432    585    546  -1208       N  
ATOM   1313  CA  PHE A 157      22.497  50.579  31.028  1.00 38.46           C  
ANISOU 1313  CA  PHE A 157     4465   4719   5430    520    568  -1204       C  
ATOM   1314  C   PHE A 157      23.449  50.920  29.871  1.00 31.78           C  
ANISOU 1314  C   PHE A 157     3785   3703   4586    518    427  -1132       C  
ATOM   1315  O   PHE A 157      23.098  50.846  28.692  1.00 30.01           O  
ANISOU 1315  O   PHE A 157     3545   3409   4448    565    312  -1077       O  
ATOM   1316  CB  PHE A 157      23.041  49.396  31.831  1.00 41.92           C  
ANISOU 1316  CB  PHE A 157     4905   5285   5739    362    652  -1128       C  
ATOM   1317  CG  PHE A 157      22.153  48.980  32.978  1.00 41.41           C  
ANISOU 1317  CG  PHE A 157     4688   5400   5647    336    803  -1173       C  
ATOM   1318  CD1 PHE A 157      22.234  49.623  34.194  1.00 39.12           C  
ANISOU 1318  CD1 PHE A 157     4413   5191   5260    361    924  -1282       C  
ATOM   1319  CD2 PHE A 157      21.238  47.942  32.836  1.00 44.62           C  
ANISOU 1319  CD2 PHE A 157     4936   5902   6115    274    828  -1109       C  
ATOM   1320  CE1 PHE A 157      21.407  49.249  35.256  1.00 47.61           C  
ANISOU 1320  CE1 PHE A 157     5345   6455   6289    335   1079  -1322       C  
ATOM   1321  CE2 PHE A 157      20.417  47.565  33.892  1.00 45.77           C  
ANISOU 1321  CE2 PHE A 157     4935   6228   6229    231    982  -1139       C  
ATOM   1322  CZ  PHE A 157      20.502  48.218  35.103  1.00 45.54           C  
ANISOU 1322  CZ  PHE A 157     4919   6293   6090    267   1113  -1242       C  
ATOM   1323  N   GLY A 158      24.678  51.302  30.221  1.00 38.90           N  
ANISOU 1323  N   GLY A 158     4842   4556   5382    455    438  -1135       N  
ATOM   1324  CA  GLY A 158      25.704  51.479  29.206  1.00 31.74           C  
ANISOU 1324  CA  GLY A 158     4080   3525   4455    418    329  -1054       C  
ATOM   1325  C   GLY A 158      25.983  50.180  28.468  1.00 29.91           C  
ANISOU 1325  C   GLY A 158     3827   3338   4201    338    272   -928       C  
ATOM   1326  O   GLY A 158      25.675  49.098  28.942  1.00 25.25           O  
ANISOU 1326  O   GLY A 158     3146   2861   3588    279    326   -895       O  
ATOM   1327  N   THR A 159      26.532  50.297  27.266  1.00 31.88           N  
ANISOU 1327  N   THR A 159     4168   3488   4457    338    165   -858       N  
ATOM   1328  CA  THR A 159      26.810  49.145  26.418  1.00 25.35           C  
ANISOU 1328  CA  THR A 159     3338   2686   3609    282    102   -758       C  
ATOM   1329  C   THR A 159      28.268  49.203  25.961  1.00 26.08           C  
ANISOU 1329  C   THR A 159     3567   2742   3602    217     69   -700       C  
ATOM   1330  O   THR A 159      29.009  50.148  26.262  1.00 25.51           O  
ANISOU 1330  O   THR A 159     3582   2625   3485    199     88   -730       O  
ATOM   1331  CB  THR A 159      25.862  49.098  25.204  1.00 33.05           C  
ANISOU 1331  CB  THR A 159     4260   3612   4684    358     -6   -736       C  
ATOM   1332  OG1 THR A 159      26.210  50.126  24.282  1.00 33.94           O  
ANISOU 1332  OG1 THR A 159     4488   3604   4804    417    -92   -715       O  
ATOM   1333  CG2 THR A 159      24.363  49.260  25.603  1.00 24.74           C  
ANISOU 1333  CG2 THR A 159     3044   2610   3746    439     19   -807       C  
ATOM   1334  N   LEU A 160      28.684  48.172  25.233  1.00 23.97           N  
ANISOU 1334  N   LEU A 160     3311   2499   3299    177     23   -623       N  
ATOM   1335  CA  LEU A 160      30.018  48.153  24.643  1.00 24.71           C  
ANISOU 1335  CA  LEU A 160     3508   2581   3299    129     -8   -568       C  
ATOM   1336  C   LEU A 160      30.144  49.125  23.488  1.00 28.82           C  
ANISOU 1336  C   LEU A 160     4115   2999   3835    164    -87   -546       C  
ATOM   1337  O   LEU A 160      31.259  49.419  23.068  1.00 31.33           O  
ANISOU 1337  O   LEU A 160     4520   3310   4075    114    -95   -507       O  
ATOM   1338  CB  LEU A 160      30.381  46.742  24.146  1.00 26.18           C  
ANISOU 1338  CB  LEU A 160     3686   2818   3445    100    -32   -507       C  
ATOM   1339  CG  LEU A 160      30.334  45.658  25.242  1.00 28.37           C  
ANISOU 1339  CG  LEU A 160     3903   3176   3700     60     42   -499       C  
ATOM   1340  CD1 LEU A 160      30.760  44.216  24.736  1.00 28.71           C  
ANISOU 1340  CD1 LEU A 160     3966   3231   3712     43     14   -439       C  
ATOM   1341  CD2 LEU A 160      31.167  46.079  26.447  1.00 28.45           C  
ANISOU 1341  CD2 LEU A 160     3931   3256   3624     21    118   -517       C  
ATOM   1342  N   GLY A 161      29.041  49.604  22.939  1.00 26.67           N  
ANISOU 1342  N   GLY A 161     3818   2658   3656    250   -148   -560       N  
ATOM   1343  CA  GLY A 161      29.175  50.622  21.918  1.00 28.48           C  
ANISOU 1343  CA  GLY A 161     4152   2778   3890    290   -224   -521       C  
ATOM   1344  C   GLY A 161      28.133  50.574  20.821  1.00 29.47           C  
ANISOU 1344  C   GLY A 161     4249   2870   4079    384   -335   -493       C  
ATOM   1345  O   GLY A 161      27.248  49.716  20.791  1.00 23.79           O  
ANISOU 1345  O   GLY A 161     3412   2215   3411    409   -359   -514       O  
ATOM   1346  N   HIS A 162      28.247  51.518  19.909  1.00 30.34           N  
ANISOU 1346  N   HIS A 162     4469   2878   4181    427   -408   -439       N  
ATOM   1347  CA  HIS A 162      27.339  51.612  18.789  1.00 30.25           C  
ANISOU 1347  CA  HIS A 162     4447   2839   4207    527   -533   -399       C  
ATOM   1348  C   HIS A 162      27.723  50.631  17.688  1.00 30.32           C  
ANISOU 1348  C   HIS A 162     4477   2924   4120    481   -595   -342       C  
ATOM   1349  O   HIS A 162      28.893  50.520  17.320  1.00 29.00           O  
ANISOU 1349  O   HIS A 162     4406   2771   3840    399   -565   -293       O  
ATOM   1350  CB  HIS A 162      27.344  53.027  18.237  1.00 28.09           C  
ANISOU 1350  CB  HIS A 162     4309   2416   3949    598   -591   -345       C  
ATOM   1351  CG  HIS A 162      26.448  53.188  17.064  1.00 28.39           C  
ANISOU 1351  CG  HIS A 162     4345   2432   4009    716   -735   -288       C  
ATOM   1352  ND1 HIS A 162      25.080  53.135  17.177  1.00 27.76           N  
ANISOU 1352  ND1 HIS A 162     4122   2381   4044    844   -797   -342       N  
ATOM   1353  CD2 HIS A 162      26.719  53.351  15.749  1.00 30.15           C  
ANISOU 1353  CD2 HIS A 162     4681   2634   4141    724   -833   -183       C  
ATOM   1354  CE1 HIS A 162      24.540  53.277  15.980  1.00 31.24           C  
ANISOU 1354  CE1 HIS A 162     4586   2816   4468    932   -941   -273       C  
ATOM   1355  NE2 HIS A 162      25.513  53.426  15.096  1.00 32.88           N  
ANISOU 1355  NE2 HIS A 162     4960   2989   4545    863   -965   -173       N  
ATOM   1356  N   VAL A 163      26.720  49.949  17.140  1.00 25.41           N  
ANISOU 1356  N   VAL A 163     3759   2357   3540    534   -683   -359       N  
ATOM   1357  CA  VAL A 163      26.929  48.903  16.144  1.00 23.86           C  
ANISOU 1357  CA  VAL A 163     3575   2234   3258    494   -747   -338       C  
ATOM   1358  C   VAL A 163      26.858  49.553  14.763  1.00 30.72           C  
ANISOU 1358  C   VAL A 163     4549   3068   4056    558   -871   -259       C  
ATOM   1359  O   VAL A 163      25.786  49.979  14.337  1.00 28.78           O  
ANISOU 1359  O   VAL A 163     4255   2806   3873    661   -980   -255       O  
ATOM   1360  CB  VAL A 163      25.871  47.799  16.279  1.00 25.61           C  
ANISOU 1360  CB  VAL A 163     3641   2531   3558    491   -785   -406       C  
ATOM   1361  CG1 VAL A 163      25.960  46.786  15.121  1.00 25.18           C  
ANISOU 1361  CG1 VAL A 163     3616   2532   3420    459   -875   -404       C  
ATOM   1362  CG2 VAL A 163      25.949  47.137  17.658  1.00 26.12           C  
ANISOU 1362  CG2 VAL A 163     3619   2629   3677    419   -655   -460       C  
ATOM   1363  N   THR A 164      27.986  49.623  14.052  1.00 24.67           N  
ANISOU 1363  N   THR A 164     3917   2306   3149    501   -856   -192       N  
ATOM   1364  CA  THR A 164      27.948  50.161  12.695  1.00 28.62           C  
ANISOU 1364  CA  THR A 164     4530   2793   3553    550   -968   -103       C  
ATOM   1365  C   THR A 164      27.619  49.108  11.656  1.00 26.86           C  
ANISOU 1365  C   THR A 164     4282   2675   3249    556  -1067   -127       C  
ATOM   1366  O   THR A 164      27.294  49.469  10.521  1.00 33.39           O  
ANISOU 1366  O   THR A 164     5177   3513   3995    615  -1187    -65       O  
ATOM   1367  CB  THR A 164      29.280  50.831  12.311  1.00 30.35           C  
ANISOU 1367  CB  THR A 164     4908   2979   3643    475   -902    -10       C  
ATOM   1368  OG1 THR A 164      30.371  49.931  12.578  1.00 29.51           O  
ANISOU 1368  OG1 THR A 164     4788   2966   3459    373   -797    -47       O  
ATOM   1369  CG2 THR A 164      29.489  52.138  13.110  1.00 26.28           C  
ANISOU 1369  CG2 THR A 164     4454   2324   3206    470   -840     21       C  
ATOM   1370  N   PHE A 165      27.673  47.825  12.012  1.00 25.25           N  
ANISOU 1370  N   PHE A 165     3993   2542   3060    498  -1026   -217       N  
ATOM   1371  CA  PHE A 165      27.223  46.754  11.117  1.00 25.77           C  
ANISOU 1371  CA  PHE A 165     4030   2688   3072    497  -1126   -271       C  
ATOM   1372  C   PHE A 165      26.789  45.583  11.984  1.00 25.07           C  
ANISOU 1372  C   PHE A 165     3812   2618   3096    443  -1081   -373       C  
ATOM   1373  O   PHE A 165      27.576  45.130  12.820  1.00 32.74           O  
ANISOU 1373  O   PHE A 165     4787   3577   4074    383   -955   -390       O  
ATOM   1374  CB  PHE A 165      28.337  46.312  10.160  1.00 29.07           C  
ANISOU 1374  CB  PHE A 165     4576   3168   3303    457  -1108   -249       C  
ATOM   1375  CG  PHE A 165      27.937  45.191   9.220  1.00 30.14           C  
ANISOU 1375  CG  PHE A 165     4703   3379   3368    455  -1209   -328       C  
ATOM   1376  CD1 PHE A 165      27.990  43.866   9.620  1.00 31.22           C  
ANISOU 1376  CD1 PHE A 165     4787   3526   3550    401  -1169   -434       C  
ATOM   1377  CD2 PHE A 165      27.508  45.473   7.929  1.00 38.75           C  
ANISOU 1377  CD2 PHE A 165     5856   4525   4344    507  -1351   -298       C  
ATOM   1378  CE1 PHE A 165      27.620  42.835   8.733  1.00 36.53           C  
ANISOU 1378  CE1 PHE A 165     5470   4248   4162    390  -1267   -525       C  
ATOM   1379  CE2 PHE A 165      27.145  44.460   7.049  1.00 38.40           C  
ANISOU 1379  CE2 PHE A 165     5812   4556   4222    498  -1452   -389       C  
ATOM   1380  CZ  PHE A 165      27.196  43.140   7.455  1.00 37.43           C  
ANISOU 1380  CZ  PHE A 165     5637   4428   4155    435  -1409   -512       C  
ATOM   1381  N   GLY A 166      25.567  45.092  11.790  1.00 36.20           N  
ANISOU 1381  N   GLY A 166     5108   4060   4588    458  -1186   -435       N  
ATOM   1382  CA  GLY A 166      25.006  43.999  12.595  1.00 28.38           C  
ANISOU 1382  CA  GLY A 166     3990   3078   3714    385  -1147   -522       C  
ATOM   1383  C   GLY A 166      23.867  44.482  13.480  1.00 31.62           C  
ANISOU 1383  C   GLY A 166     4237   3490   4288    415  -1141   -539       C  
ATOM   1384  O   GLY A 166      23.251  45.512  13.245  1.00 32.74           O  
ANISOU 1384  O   GLY A 166     4345   3632   4463    514  -1213   -507       O  
ATOM   1385  N   TYR A 167      23.613  43.744  14.552  1.00 31.39           N  
ANISOU 1385  N   TYR A 167     4109   3462   4357    336  -1046   -586       N  
ATOM   1386  CA  TYR A 167      22.441  44.042  15.371  1.00 28.33           C  
ANISOU 1386  CA  TYR A 167     3540   3108   4117    354  -1030   -618       C  
ATOM   1387  C   TYR A 167      22.784  44.449  16.799  1.00 26.94           C  
ANISOU 1387  C   TYR A 167     3343   2904   3988    345   -866   -604       C  
ATOM   1388  O   TYR A 167      22.379  45.527  17.256  1.00 26.69           O  
ANISOU 1388  O   TYR A 167     3260   2867   4013    434   -845   -600       O  
ATOM   1389  CB  TYR A 167      21.518  42.826  15.387  1.00 36.94           C  
ANISOU 1389  CB  TYR A 167     4494   4251   5290    250  -1070   -691       C  
ATOM   1390  CG  TYR A 167      20.906  42.462  14.051  1.00 38.85           C  
ANISOU 1390  CG  TYR A 167     4717   4543   5502    253  -1253   -732       C  
ATOM   1391  CD1 TYR A 167      19.928  43.262  13.471  1.00 35.15           C  
ANISOU 1391  CD1 TYR A 167     4141   4144   5069    358  -1387   -734       C  
ATOM   1392  CD2 TYR A 167      21.276  41.292  13.396  1.00 40.27           C  
ANISOU 1392  CD2 TYR A 167     4984   4703   5615    159  -1296   -777       C  
ATOM   1393  CE1 TYR A 167      19.356  42.918  12.253  1.00 38.88           C  
ANISOU 1393  CE1 TYR A 167     4590   4685   5498    360  -1569   -775       C  
ATOM   1394  CE2 TYR A 167      20.708  40.933  12.189  1.00 48.81           C  
ANISOU 1394  CE2 TYR A 167     6052   5840   6655    152  -1468   -834       C  
ATOM   1395  CZ  TYR A 167      19.743  41.750  11.621  1.00 50.68           C  
ANISOU 1395  CZ  TYR A 167     6174   6166   6915    247  -1608   -830       C  
ATOM   1396  OH  TYR A 167      19.170  41.387  10.423  1.00 60.72           O  
ANISOU 1396  OH  TYR A 167     7426   7514   8130    239  -1794   -889       O  
ATOM   1397  N   GLY A 168      23.477  43.594  17.536  1.00 28.21           N  
ANISOU 1397  N   GLY A 168     3544   3050   4126    247   -753   -603       N  
ATOM   1398  CA  GLY A 168      23.760  43.854  18.926  1.00 23.96           C  
ANISOU 1398  CA  GLY A 168     2980   2509   3613    228   -605   -595       C  
ATOM   1399  C   GLY A 168      22.699  43.241  19.812  1.00 34.19           C  
ANISOU 1399  C   GLY A 168     4106   3864   5020    161   -547   -636       C  
ATOM   1400  O   GLY A 168      22.237  42.124  19.549  1.00 28.05           O  
ANISOU 1400  O   GLY A 168     3279   3099   4278     69   -582   -656       O  
ATOM   1401  N   ASN A 169      22.297  43.975  20.855  1.00 25.06           N  
ANISOU 1401  N   ASN A 169     2861   2744   3915    199   -453   -653       N  
ATOM   1402  CA  ASN A 169      21.396  43.422  21.859  1.00 25.92           C  
ANISOU 1402  CA  ASN A 169     2807   2932   4108    124   -361   -683       C  
ATOM   1403  C   ASN A 169      20.054  43.017  21.262  1.00 30.06           C  
ANISOU 1403  C   ASN A 169     3157   3525   4741    101   -456   -729       C  
ATOM   1404  O   ASN A 169      19.479  42.007  21.667  1.00 30.39           O  
ANISOU 1404  O   ASN A 169     3097   3613   4837    -30   -412   -738       O  
ATOM   1405  CB  ASN A 169      21.194  44.433  22.989  1.00 30.48           C  
ANISOU 1405  CB  ASN A 169     3324   3552   4706    194   -246   -713       C  
ATOM   1406  CG  ASN A 169      22.401  44.499  23.915  1.00 36.22           C  
ANISOU 1406  CG  ASN A 169     4186   4249   5328    160   -129   -679       C  
ATOM   1407  OD1 ASN A 169      23.047  43.480  24.155  1.00 30.94           O  
ANISOU 1407  OD1 ASN A 169     3586   3568   4601     60    -91   -630       O  
ATOM   1408  ND2 ASN A 169      22.729  45.698  24.413  1.00 31.15           N  
ANISOU 1408  ND2 ASN A 169     3586   3589   4660    248    -82   -708       N  
ATOM   1409  N   ASN A 170      19.524  43.791  20.320  1.00 30.50           N  
ANISOU 1409  N   ASN A 170     3169   3593   4827    219   -589   -752       N  
ATOM   1410  CA  ASN A 170      18.183  43.512  19.803  1.00 32.35           C  
ANISOU 1410  CA  ASN A 170     3203   3925   5165    209   -691   -804       C  
ATOM   1411  C   ASN A 170      18.073  44.038  18.379  1.00 36.50           C  
ANISOU 1411  C   ASN A 170     3776   4433   5661    322   -883   -800       C  
ATOM   1412  O   ASN A 170      19.061  44.480  17.784  1.00 35.15           O  
ANISOU 1412  O   ASN A 170     3803   4170   5384    381   -922   -750       O  
ATOM   1413  CB  ASN A 170      17.098  44.125  20.693  1.00 31.50           C  
ANISOU 1413  CB  ASN A 170     2873   3931   5166    272   -613   -855       C  
ATOM   1414  CG  ASN A 170      17.336  45.610  20.953  1.00 42.86           C  
ANISOU 1414  CG  ASN A 170     4366   5324   6593    463   -589   -857       C  
ATOM   1415  OD1 ASN A 170      17.387  46.416  20.024  1.00 40.49           O  
ANISOU 1415  OD1 ASN A 170     4134   4970   6279    600   -721   -840       O  
ATOM   1416  ND2 ASN A 170      17.502  45.965  22.220  1.00 38.80           N  
ANISOU 1416  ND2 ASN A 170     3839   4826   6078    468   -422   -877       N  
ATOM   1417  N   ASP A 171      16.848  44.007  17.847  1.00 32.43           N  
ANISOU 1417  N   ASP A 171     3067   4024   5232    348  -1003   -849       N  
ATOM   1418  CA  ASP A 171      16.624  44.369  16.453  1.00 37.25           C  
ANISOU 1418  CA  ASP A 171     3709   4644   5802    446  -1206   -842       C  
ATOM   1419  C   ASP A 171      16.787  45.868  16.200  1.00 42.29           C  
ANISOU 1419  C   ASP A 171     4423   5229   6417    661  -1251   -794       C  
ATOM   1420  O   ASP A 171      17.099  46.256  15.072  1.00 44.22           O  
ANISOU 1420  O   ASP A 171     4795   5434   6571    739  -1390   -747       O  
ATOM   1421  CB  ASP A 171      15.220  43.948  16.000  1.00 46.63           C  
ANISOU 1421  CB  ASP A 171     4645   5983   7090    419  -1335   -912       C  
ATOM   1422  CG  ASP A 171      14.906  42.471  16.279  1.00 55.41           C  
ANISOU 1422  CG  ASP A 171     5668   7135   8249    182  -1293   -964       C  
ATOM   1423  OD1 ASP A 171      14.583  42.133  17.433  1.00 55.18           O  
ANISOU 1423  OD1 ASP A 171     5519   7144   8301     88  -1135   -979       O  
ATOM   1424  OD2 ASP A 171      14.937  41.653  15.337  1.00 52.11           O  
ANISOU 1424  OD2 ASP A 171     5304   6709   7785     85  -1418   -993       O  
ATOM   1425  N   GLU A 172      16.571  46.727  17.210  1.00 39.99           N  
ANISOU 1425  N   GLU A 172     4066   4931   6198    758  -1136   -807       N  
ATOM   1426  CA  GLU A 172      16.371  48.161  16.961  1.00 50.41           C  
ANISOU 1426  CA  GLU A 172     5417   6198   7539    979  -1200   -781       C  
ATOM   1427  C   GLU A 172      17.471  49.093  17.460  1.00 41.98           C  
ANISOU 1427  C   GLU A 172     4569   4972   6411   1033  -1093   -733       C  
ATOM   1428  O   GLU A 172      17.707  50.114  16.813  1.00 44.05           O  
ANISOU 1428  O   GLU A 172     4964   5134   6640   1172  -1181   -674       O  
ATOM   1429  CB  GLU A 172      15.052  48.649  17.580  1.00 55.58           C  
ANISOU 1429  CB  GLU A 172     5805   6968   8343   1103  -1184   -856       C  
ATOM   1430  CG  GLU A 172      13.818  47.819  17.230  1.00 67.66           C  
ANISOU 1430  CG  GLU A 172     7062   8687   9957   1043  -1281   -917       C  
ATOM   1431  CD  GLU A 172      13.546  46.705  18.239  1.00 76.45           C  
ANISOU 1431  CD  GLU A 172     8025   9899  11123    833  -1122   -974       C  
ATOM   1432  OE1 GLU A 172      12.634  45.891  17.975  1.00 81.07           O  
ANISOU 1432  OE1 GLU A 172     8399  10629  11774    730  -1189  -1023       O  
ATOM   1433  OE2 GLU A 172      14.237  46.646  19.287  1.00 72.83           O  
ANISOU 1433  OE2 GLU A 172     7661   9377  10635    764   -936   -967       O  
ATOM   1434  N   ASP A 173      18.123  48.792  18.599  1.00 33.71           N  
ANISOU 1434  N   ASP A 173     3562   3901   5347    923   -911   -755       N  
ATOM   1435  CA  ASP A 173      18.973  49.769  19.289  1.00 35.11           C  
ANISOU 1435  CA  ASP A 173     3897   3954   5489    974   -803   -741       C  
ATOM   1436  C   ASP A 173      20.288  50.055  18.565  1.00 35.18           C  
ANISOU 1436  C   ASP A 173     4163   3834   5368    940   -841   -651       C  
ATOM   1437  O   ASP A 173      20.876  51.122  18.775  1.00 37.28           O  
ANISOU 1437  O   ASP A 173     4571   3978   5614   1005   -805   -628       O  
ATOM   1438  CB  ASP A 173      19.321  49.302  20.708  1.00 39.72           C  
ANISOU 1438  CB  ASP A 173     4446   4577   6068    858   -610   -790       C  
ATOM   1439  CG  ASP A 173      18.132  49.277  21.641  1.00 44.51           C  
ANISOU 1439  CG  ASP A 173     4813   5310   6788    897   -526   -879       C  
ATOM   1440  OD1 ASP A 173      17.065  49.806  21.285  1.00 51.33           O  
ANISOU 1440  OD1 ASP A 173     5531   6223   7749   1043   -610   -917       O  
ATOM   1441  OD2 ASP A 173      18.267  48.706  22.750  1.00 48.13           O  
ANISOU 1441  OD2 ASP A 173     5223   5834   7230    784   -373   -910       O  
ATOM   1442  N   LYS A 174      20.812  49.104  17.793  1.00 32.99           N  
ANISOU 1442  N   LYS A 174     3951   3583   5000    828   -895   -608       N  
ATOM   1443  CA  LYS A 174      22.167  49.211  17.236  1.00 32.52           C  
ANISOU 1443  CA  LYS A 174     4114   3439   4805    772   -893   -532       C  
ATOM   1444  C   LYS A 174      23.211  49.476  18.331  1.00 36.31           C  
ANISOU 1444  C   LYS A 174     4684   3864   5248    703   -733   -537       C  
ATOM   1445  O   LYS A 174      24.149  50.263  18.149  1.00 29.30           O  
ANISOU 1445  O   LYS A 174     3961   2882   4291    705   -718   -485       O  
ATOM   1446  CB  LYS A 174      22.233  50.301  16.154  1.00 41.20           C  
ANISOU 1446  CB  LYS A 174     5342   4451   5862    892  -1019   -453       C  
ATOM   1447  CG  LYS A 174      21.452  50.026  14.874  1.00 42.36           C  
ANISOU 1447  CG  LYS A 174     5439   4663   5991    954  -1201   -429       C  
ATOM   1448  CD  LYS A 174      22.216  48.993  14.023  1.00 55.88           C  
ANISOU 1448  CD  LYS A 174     7245   6423   7565    831  -1233   -404       C  
ATOM   1449  CE  LYS A 174      21.413  48.475  12.834  1.00 57.70           C  
ANISOU 1449  CE  LYS A 174     7411   6747   7765    861  -1412   -413       C  
ATOM   1450  NZ  LYS A 174      20.574  47.307  13.225  1.00 56.86           N  
ANISOU 1450  NZ  LYS A 174     7108   6747   7751    778  -1414   -515       N  
ATOM   1451  N   LYS A 175      23.050  48.804  19.478  1.00 25.91           N  
ANISOU 1451  N   LYS A 175     3258   2614   3971    629   -615   -596       N  
ATOM   1452  CA  LYS A 175      24.007  48.833  20.582  1.00 34.70           C  
ANISOU 1452  CA  LYS A 175     4438   3714   5034    551   -471   -606       C  
ATOM   1453  C   LYS A 175      24.265  47.405  21.036  1.00 29.03           C  
ANISOU 1453  C   LYS A 175     3671   3076   4282    423   -407   -607       C  
ATOM   1454  O   LYS A 175      23.354  46.565  21.012  1.00 28.37           O  
ANISOU 1454  O   LYS A 175     3456   3060   4263    393   -428   -633       O  
ATOM   1455  CB  LYS A 175      23.508  49.675  21.784  1.00 29.07           C  
ANISOU 1455  CB  LYS A 175     3656   2997   4394    615   -374   -680       C  
ATOM   1456  CG  LYS A 175      23.031  51.090  21.388  1.00 28.65           C  
ANISOU 1456  CG  LYS A 175     3642   2838   4404    772   -444   -691       C  
ATOM   1457  CD  LYS A 175      24.223  51.943  20.952  1.00 26.51           C  
ANISOU 1457  CD  LYS A 175     3589   2432   4051    755   -461   -629       C  
ATOM   1458  CE  LYS A 175      23.728  53.340  20.468  1.00 28.18           C  
ANISOU 1458  CE  LYS A 175     3872   2503   4333    915   -542   -619       C  
ATOM   1459  NZ  LYS A 175      23.042  53.165  19.198  1.00 28.96           N  
ANISOU 1459  NZ  LYS A 175     3937   2619   4447    996   -695   -555       N  
ATOM   1460  N   GLU A 176      25.500  47.120  21.445  1.00 27.31           N  
ANISOU 1460  N   GLU A 176     3559   2850   3967    346   -333   -577       N  
ATOM   1461  CA  GLU A 176      25.892  45.735  21.741  1.00 26.83           C  
ANISOU 1461  CA  GLU A 176     3488   2839   3866    245   -289   -560       C  
ATOM   1462  C   GLU A 176      26.244  45.595  23.209  1.00 29.10           C  
ANISOU 1462  C   GLU A 176     3754   3173   4129    193   -153   -572       C  
ATOM   1463  O   GLU A 176      26.979  46.424  23.755  1.00 25.53           O  
ANISOU 1463  O   GLU A 176     3368   2709   3624    203   -101   -579       O  
ATOM   1464  CB  GLU A 176      27.087  45.268  20.892  1.00 26.59           C  
ANISOU 1464  CB  GLU A 176     3589   2785   3728    214   -329   -509       C  
ATOM   1465  CG  GLU A 176      27.880  44.061  21.511  1.00 20.66           C  
ANISOU 1465  CG  GLU A 176     2864   2067   2920    136   -255   -486       C  
ATOM   1466  CD  GLU A 176      27.013  42.795  21.693  1.00 31.76           C  
ANISOU 1466  CD  GLU A 176     4187   3483   4396     81   -256   -499       C  
ATOM   1467  OE1 GLU A 176      27.332  41.953  22.568  1.00 29.48           O  
ANISOU 1467  OE1 GLU A 176     3901   3211   4090     23   -178   -475       O  
ATOM   1468  OE2 GLU A 176      25.988  42.659  20.990  1.00 28.91           O  
ANISOU 1468  OE2 GLU A 176     3758   3117   4109     89   -339   -530       O  
ATOM   1469  N   GLY A 177      25.721  44.545  23.840  1.00 27.96           N  
ANISOU 1469  N   GLY A 177     3523   3083   4016    127   -100   -572       N  
ATOM   1470  CA  GLY A 177      26.260  44.114  25.109  1.00 24.67           C  
ANISOU 1470  CA  GLY A 177     3118   2718   3538     65     17   -553       C  
ATOM   1471  C   GLY A 177      25.887  45.024  26.272  1.00 30.84           C  
ANISOU 1471  C   GLY A 177     3839   3553   4325     91    114   -609       C  
ATOM   1472  O   GLY A 177      24.970  45.853  26.187  1.00 26.63           O  
ANISOU 1472  O   GLY A 177     3227   3019   3874    163    102   -670       O  
ATOM   1473  N   ILE A 178      26.635  44.872  27.373  1.00 28.92           N  
ANISOU 1473  N   ILE A 178     3791   3686   3511    219     69   -854       N  
ATOM   1474  CA  ILE A 178      26.433  45.695  28.563  1.00 29.92           C  
ANISOU 1474  CA  ILE A 178     3931   3821   3618    248     74   -882       C  
ATOM   1475  C   ILE A 178      27.787  46.077  29.156  1.00 30.61           C  
ANISOU 1475  C   ILE A 178     4104   3819   3708    218     69   -824       C  
ATOM   1476  O   ILE A 178      28.741  45.294  29.139  1.00 22.76           O  
ANISOU 1476  O   ILE A 178     3133   2790   2725    149     85   -766       O  
ATOM   1477  CB  ILE A 178      25.551  44.984  29.617  1.00 27.52           C  
ANISOU 1477  CB  ILE A 178     3549   3611   3296    201    131   -928       C  
ATOM   1478  CG1 ILE A 178      25.139  45.966  30.720  1.00 24.72           C  
ANISOU 1478  CG1 ILE A 178     3196   3287   2909    257    132   -979       C  
ATOM   1479  CG2 ILE A 178      26.279  43.808  30.214  1.00 29.81           C  
ANISOU 1479  CG2 ILE A 178     3856   3879   3590     96    180   -869       C  
ATOM   1480  CD1 ILE A 178      23.931  45.519  31.535  1.00 28.88           C  
ANISOU 1480  CD1 ILE A 178     3625   3939   3408    239    186  -1044       C  
ATOM   1481  N   HIS A 179      27.883  47.309  29.640  1.00 23.63           N  
ANISOU 1481  N   HIS A 179     3266   2897   2814    275     40   -846       N  
ATOM   1482  CA  HIS A 179      29.072  47.785  30.344  1.00 23.42           C  
ANISOU 1482  CA  HIS A 179     3310   2798   2789    244     31   -812       C  
ATOM   1483  C   HIS A 179      28.548  48.564  31.552  1.00 28.12           C  
ANISOU 1483  C   HIS A 179     3906   3422   3358    288     31   -879       C  
ATOM   1484  O   HIS A 179      28.072  49.696  31.407  1.00 30.07           O  
ANISOU 1484  O   HIS A 179     4178   3642   3605    372     -6   -924       O  
ATOM   1485  CB  HIS A 179      29.938  48.658  29.439  1.00 24.47           C  
ANISOU 1485  CB  HIS A 179     3519   2829   2948    263    -11   -769       C  
ATOM   1486  CG  HIS A 179      31.144  49.223  30.111  1.00 29.65           C  
ANISOU 1486  CG  HIS A 179     4238   3415   3613    223    -23   -747       C  
ATOM   1487  ND1 HIS A 179      31.960  50.153  29.505  1.00 32.02           N  
ANISOU 1487  ND1 HIS A 179     4610   3619   3939    223    -54   -713       N  
ATOM   1488  CD2 HIS A 179      31.690  48.973  31.326  1.00 28.96           C  
ANISOU 1488  CD2 HIS A 179     4148   3346   3510    177     -8   -755       C  
ATOM   1489  CE1 HIS A 179      32.952  50.457  30.324  1.00 31.86           C  
ANISOU 1489  CE1 HIS A 179     4619   3561   3924    172    -58   -711       C  
ATOM   1490  NE2 HIS A 179      32.822  49.737  31.425  1.00 28.62           N  
ANISOU 1490  NE2 HIS A 179     4165   3224   3487    150    -35   -737       N  
ATOM   1491  N   TYR A 180      28.607  47.933  32.720  1.00 24.04           N  
ANISOU 1491  N   TYR A 180     3363   2960   2811    239     71   -884       N  
ATOM   1492  CA  TYR A 180      28.099  48.475  33.973  1.00 30.02           C  
ANISOU 1492  CA  TYR A 180     4110   3770   3527    275     81   -950       C  
ATOM   1493  C   TYR A 180      29.232  48.423  34.981  1.00 28.93           C  
ANISOU 1493  C   TYR A 180     4019   3605   3369    226     82   -924       C  
ATOM   1494  O   TYR A 180      29.655  47.336  35.375  1.00 27.27           O  
ANISOU 1494  O   TYR A 180     3796   3425   3141    159    118   -874       O  
ATOM   1495  CB  TYR A 180      26.895  47.664  34.465  1.00 33.17           C  
ANISOU 1495  CB  TYR A 180     4418   4294   3891    264    139   -987       C  
ATOM   1496  CG  TYR A 180      26.373  48.121  35.800  1.00 39.49           C  
ANISOU 1496  CG  TYR A 180     5199   5169   4635    298    160  -1054       C  
ATOM   1497  CD1 TYR A 180      25.554  49.249  35.909  1.00 41.38           C  
ANISOU 1497  CD1 TYR A 180     5426   5433   4864    402    131  -1143       C  
ATOM   1498  CD2 TYR A 180      26.699  47.434  36.950  1.00 36.40           C  
ANISOU 1498  CD2 TYR A 180     4807   4827   4196    238    207  -1029       C  
ATOM   1499  CE1 TYR A 180      25.081  49.658  37.133  1.00 40.72           C  
ANISOU 1499  CE1 TYR A 180     5320   5427   4723    440    152  -1213       C  
ATOM   1500  CE2 TYR A 180      26.227  47.819  38.159  1.00 41.26           C  
ANISOU 1500  CE2 TYR A 180     5404   5524   4749    271    230  -1089       C  
ATOM   1501  CZ  TYR A 180      25.418  48.936  38.255  1.00 47.73           C  
ANISOU 1501  CZ  TYR A 180     6203   6374   5559    371    203  -1186       C  
ATOM   1502  OH  TYR A 180      24.967  49.315  39.494  1.00 49.13           O  
ANISOU 1502  OH  TYR A 180     6359   6641   5667    409    228  -1255       O  
ATOM   1503  N   LYS A 181      29.697  49.590  35.426  1.00 33.64           N  
ANISOU 1503  N   LYS A 181     4671   4145   3966    263     40   -962       N  
ATOM   1504  CA  LYS A 181      30.931  49.694  36.204  1.00 26.91           C  
ANISOU 1504  CA  LYS A 181     3864   3259   3102    218     24   -945       C  
ATOM   1505  C   LYS A 181      32.060  48.952  35.486  1.00 25.76           C  
ANISOU 1505  C   LYS A 181     3732   3065   2989    147     23   -858       C  
ATOM   1506  O   LYS A 181      32.442  49.308  34.366  1.00 26.05           O  
ANISOU 1506  O   LYS A 181     3796   3028   3075    143     -2   -827       O  
ATOM   1507  CB  LYS A 181      30.704  49.180  37.628  1.00 30.92           C  
ANISOU 1507  CB  LYS A 181     4343   3868   3539    208     61   -970       C  
ATOM   1508  CG  LYS A 181      29.749  50.089  38.459  1.00 44.40           C  
ANISOU 1508  CG  LYS A 181     6038   5627   5205    286     58  -1071       C  
ATOM   1509  CD  LYS A 181      29.487  49.544  39.872  1.00 47.37           C  
ANISOU 1509  CD  LYS A 181     6383   6120   5494    277    105  -1092       C  
ATOM   1510  CE  LYS A 181      28.897  50.613  40.803  1.00 44.75           C  
ANISOU 1510  CE  LYS A 181     6053   5833   5117    358     89  -1203       C  
ATOM   1511  NZ  LYS A 181      27.634  51.141  40.275  1.00 46.61           N  
ANISOU 1511  NZ  LYS A 181     6248   6092   5370    434     92  -1265       N  
ATOM   1512  N   ASN A 182      32.594  47.897  36.071  1.00 27.83           N  
ANISOU 1512  N   ASN A 182     3979   3373   3221     95     50   -815       N  
ATOM   1513  CA  ASN A 182      33.593  47.136  35.333  1.00 31.97           C  
ANISOU 1513  CA  ASN A 182     4510   3861   3776     43     48   -741       C  
ATOM   1514  C   ASN A 182      33.080  45.788  34.862  1.00 26.82           C  
ANISOU 1514  C   ASN A 182     3820   3246   3123     18     93   -695       C  
ATOM   1515  O   ASN A 182      33.883  44.914  34.540  1.00 30.34           O  
ANISOU 1515  O   ASN A 182     4272   3677   3580    -20     97   -637       O  
ATOM   1516  CB  ASN A 182      34.850  46.962  36.169  1.00 23.21           C  
ANISOU 1516  CB  ASN A 182     3421   2757   2642     11     30   -724       C  
ATOM   1517  CG  ASN A 182      35.542  48.276  36.418  1.00 30.49           C  
ANISOU 1517  CG  ASN A 182     4378   3627   3581     16    -19   -772       C  
ATOM   1518  OD1 ASN A 182      35.608  49.114  35.527  1.00 29.25           O  
ANISOU 1518  OD1 ASN A 182     4245   3395   3475     19    -42   -778       O  
ATOM   1519  ND2 ASN A 182      36.039  48.472  37.626  1.00 24.05           N  
ANISOU 1519  ND2 ASN A 182     3570   2848   2721     15    -36   -808       N  
ATOM   1520  N   LEU A 183      31.768  45.590  34.848  1.00 26.24           N  
ANISOU 1520  N   LEU A 183     3707   3224   3039     38    125   -726       N  
ATOM   1521  CA  LEU A 183      31.174  44.338  34.388  1.00 25.40           C  
ANISOU 1521  CA  LEU A 183     3562   3150   2940      2    169   -695       C  
ATOM   1522  C   LEU A 183      30.845  44.478  32.912  1.00 29.91           C  
ANISOU 1522  C   LEU A 183     4116   3688   3560     20    149   -697       C  
ATOM   1523  O   LEU A 183      30.153  45.429  32.518  1.00 31.30           O  
ANISOU 1523  O   LEU A 183     4281   3866   3744     76    126   -746       O  
ATOM   1524  CB  LEU A 183      29.910  44.002  35.180  1.00 26.36           C  
ANISOU 1524  CB  LEU A 183     3634   3359   3021     -1    221   -732       C  
ATOM   1525  CG  LEU A 183      28.904  42.959  34.631  1.00 34.34           C  
ANISOU 1525  CG  LEU A 183     4587   4411   4049    -41    269   -730       C  
ATOM   1526  CD1 LEU A 183      29.508  41.570  34.375  1.00 33.91           C  
ANISOU 1526  CD1 LEU A 183     4556   4318   4012   -109    293   -657       C  
ATOM   1527  CD2 LEU A 183      27.751  42.813  35.588  1.00 35.78           C  
ANISOU 1527  CD2 LEU A 183     4717   4692   4184    -50    326   -772       C  
ATOM   1528  N   LEU A 184      31.358  43.551  32.100  1.00 24.08           N  
ANISOU 1528  N   LEU A 184     3379   2921   2848    -17    154   -647       N  
ATOM   1529  CA  LEU A 184      31.078  43.512  30.670  1.00 27.78           C  
ANISOU 1529  CA  LEU A 184     3830   3372   3353     -1    137   -648       C  
ATOM   1530  C   LEU A 184      30.228  42.296  30.313  1.00 30.12           C  
ANISOU 1530  C   LEU A 184     4075   3710   3658    -37    175   -656       C  
ATOM   1531  O   LEU A 184      30.403  41.207  30.880  1.00 26.88           O  
ANISOU 1531  O   LEU A 184     3669   3304   3242    -92    212   -626       O  
ATOM   1532  CB  LEU A 184      32.365  43.457  29.860  1.00 21.48           C  
ANISOU 1532  CB  LEU A 184     3070   2513   2577    -13    111   -596       C  
ATOM   1533  CG  LEU A 184      33.415  44.448  30.313  1.00 27.11           C  
ANISOU 1533  CG  LEU A 184     3829   3184   3287     -7     81   -584       C  
ATOM   1534  CD1 LEU A 184      34.653  44.257  29.449  1.00 28.22           C  
ANISOU 1534  CD1 LEU A 184     3990   3285   3449    -29     66   -534       C  
ATOM   1535  CD2 LEU A 184      32.837  45.885  30.220  1.00 24.57           C  
ANISOU 1535  CD2 LEU A 184     3526   2841   2967     47     53   -627       C  
ATOM   1536  N   GLY A 185      29.322  42.480  29.359  1.00 27.47           N  
ANISOU 1536  N   GLY A 185     3697   3403   3338     -5    163   -698       N  
ATOM   1537  CA  GLY A 185      28.516  41.379  28.875  1.00 25.48           C  
ANISOU 1537  CA  GLY A 185     3389   3191   3103    -45    191   -720       C  
ATOM   1538  C   GLY A 185      28.323  41.478  27.386  1.00 29.92           C  
ANISOU 1538  C   GLY A 185     3932   3753   3685     -7    154   -739       C  
ATOM   1539  O   GLY A 185      28.179  42.596  26.855  1.00 24.95           O  
ANISOU 1539  O   GLY A 185     3312   3122   3046     67    113   -755       O  
ATOM   1540  N   THR A 186      28.312  40.340  26.683  1.00 22.31           N  
ANISOU 1540  N   THR A 186     2948   2785   2744    -50    166   -737       N  
ATOM   1541  CA  THR A 186      28.273  40.428  25.235  1.00 22.26           C  
ANISOU 1541  CA  THR A 186     2929   2783   2744     -8    126   -753       C  
ATOM   1542  C   THR A 186      27.653  39.174  24.655  1.00 28.16           C  
ANISOU 1542  C   THR A 186     3623   3560   3516    -58    143   -795       C  
ATOM   1543  O   THR A 186      27.614  38.120  25.293  1.00 32.34           O  
ANISOU 1543  O   THR A 186     4149   4072   4065   -136    187   -788       O  
ATOM   1544  CB  THR A 186      29.680  40.649  24.645  1.00 27.91           C  
ANISOU 1544  CB  THR A 186     3713   3433   3458      9    102   -689       C  
ATOM   1545  OG1 THR A 186      29.585  40.961  23.250  1.00 22.51           O  
ANISOU 1545  OG1 THR A 186     3023   2765   2765     64     64   -701       O  
ATOM   1546  CG2 THR A 186      30.564  39.392  24.798  1.00 27.31           C  
ANISOU 1546  CG2 THR A 186     3661   3314   3401    -52    126   -650       C  
ATOM   1547  N   TYR A 187      27.216  39.296  23.409  1.00 32.67           N  
ANISOU 1547  N   TYR A 187     4160   4169   4084    -11    106   -838       N  
ATOM   1548  CA  TYR A 187      26.802  38.172  22.591  1.00 29.93           C  
ANISOU 1548  CA  TYR A 187     3767   3844   3760    -50    107   -886       C  
ATOM   1549  C   TYR A 187      27.890  37.724  21.619  1.00 30.72           C  
ANISOU 1549  C   TYR A 187     3917   3894   3861    -37     85   -850       C  
ATOM   1550  O   TYR A 187      27.677  36.753  20.889  1.00 30.00           O  
ANISOU 1550  O   TYR A 187     3798   3812   3789    -65     82   -894       O  
ATOM   1551  CB  TYR A 187      25.543  38.545  21.795  1.00 30.84           C  
ANISOU 1551  CB  TYR A 187     3799   4058   3862      3     73   -974       C  
ATOM   1552  CG  TYR A 187      24.216  38.477  22.539  1.00 29.21           C  
ANISOU 1552  CG  TYR A 187     3502   3931   3664    -31    102  -1045       C  
ATOM   1553  CD1 TYR A 187      23.576  37.254  22.776  1.00 31.52           C  
ANISOU 1553  CD1 TYR A 187     3735   4246   3996   -136    145  -1094       C  
ATOM   1554  CD2 TYR A 187      23.575  39.638  22.948  1.00 27.82           C  
ANISOU 1554  CD2 TYR A 187     3299   3812   3458     43     86  -1068       C  
ATOM   1555  CE1 TYR A 187      22.334  37.202  23.420  1.00 38.47           C  
ANISOU 1555  CE1 TYR A 187     4519   5216   4881   -177    180  -1163       C  
ATOM   1556  CE2 TYR A 187      22.349  39.601  23.600  1.00 31.75           C  
ANISOU 1556  CE2 TYR A 187     3701   4404   3958     20    115  -1142       C  
ATOM   1557  CZ  TYR A 187      21.729  38.382  23.833  1.00 36.71           C  
ANISOU 1557  CZ  TYR A 187     4260   5067   4622    -95    165  -1188       C  
ATOM   1558  OH  TYR A 187      20.512  38.365  24.465  1.00 38.01           O  
ANISOU 1558  OH  TYR A 187     4318   5337   4786   -128    201  -1263       O  
ATOM   1559  N   LEU A 188      29.026  38.420  21.557  1.00 23.57           N  
ANISOU 1559  N   LEU A 188     3079   2943   2935      2     71   -779       N  
ATOM   1560  CA  LEU A 188      29.982  38.166  20.477  1.00 26.55           C  
ANISOU 1560  CA  LEU A 188     3488   3298   3301     28     50   -753       C  
ATOM   1561  C   LEU A 188      30.726  36.847  20.657  1.00 27.85           C  
ANISOU 1561  C   LEU A 188     3676   3411   3496    -30     75   -738       C  
ATOM   1562  O   LEU A 188      31.143  36.489  21.761  1.00 25.54           O  
ANISOU 1562  O   LEU A 188     3412   3071   3221    -76    105   -701       O  
ATOM   1563  CB  LEU A 188      30.998  39.297  20.356  1.00 21.58           C  
ANISOU 1563  CB  LEU A 188     2916   2640   2642     73     35   -682       C  
ATOM   1564  CG  LEU A 188      30.681  40.383  19.306  1.00 28.16           C  
ANISOU 1564  CG  LEU A 188     3755   3510   3433    154     -3   -683       C  
ATOM   1565  CD1 LEU A 188      29.328  41.043  19.617  1.00 25.96           C  
ANISOU 1565  CD1 LEU A 188     3437   3277   3149    193    -20   -735       C  
ATOM   1566  CD2 LEU A 188      31.832  41.430  19.254  1.00 28.71           C  
ANISOU 1566  CD2 LEU A 188     3894   3532   3483    173     -6   -601       C  
ATOM   1567  N   HIS A 189      30.886  36.144  19.545  1.00 32.06           N  
ANISOU 1567  N   HIS A 189     4198   3955   4029    -17     58   -771       N  
ATOM   1568  CA  HIS A 189      31.722  34.962  19.384  1.00 32.71           C  
ANISOU 1568  CA  HIS A 189     4310   3986   4133    -43     69   -764       C  
ATOM   1569  C   HIS A 189      33.055  35.332  18.738  1.00 32.72           C  
ANISOU 1569  C   HIS A 189     4346   3985   4101      8     55   -713       C  
ATOM   1570  O   HIS A 189      33.239  36.436  18.191  1.00 30.27           O  
ANISOU 1570  O   HIS A 189     4038   3712   3750     56     37   -686       O  
ATOM   1571  CB  HIS A 189      31.019  33.924  18.500  1.00 33.12           C  
ANISOU 1571  CB  HIS A 189     4322   4056   4205    -59     57   -851       C  
ATOM   1572  CG  HIS A 189      29.690  33.472  19.016  1.00 51.95           C  
ANISOU 1572  CG  HIS A 189     6658   6454   6627   -125     76   -912       C  
ATOM   1573  ND1 HIS A 189      28.791  32.777  18.234  1.00 60.23           N  
ANISOU 1573  ND1 HIS A 189     7651   7540   7695   -147     60  -1009       N  
ATOM   1574  CD2 HIS A 189      29.112  33.593  20.232  1.00 58.93           C  
ANISOU 1574  CD2 HIS A 189     7533   7328   7530   -180    112   -896       C  
ATOM   1575  CE1 HIS A 189      27.709  32.505  18.941  1.00 57.38           C  
ANISOU 1575  CE1 HIS A 189     7243   7191   7367   -220     89  -1049       C  
ATOM   1576  NE2 HIS A 189      27.881  32.982  20.158  1.00 57.53           N  
ANISOU 1576  NE2 HIS A 189     7291   7183   7384   -239    123   -978       N  
ATOM   1577  N   GLY A 190      33.963  34.356  18.725  1.00 29.17           N  
ANISOU 1577  N   GLY A 190     3924   3493   3668     -1     63   -703       N  
ATOM   1578  CA  GLY A 190      35.280  34.550  18.165  1.00 25.20           C  
ANISOU 1578  CA  GLY A 190     3440   3000   3134     42     57   -663       C  
ATOM   1579  C   GLY A 190      36.359  33.664  18.764  1.00 26.85           C  
ANISOU 1579  C   GLY A 190     3683   3155   3364     34     70   -636       C  
ATOM   1580  O   GLY A 190      37.236  33.168  18.056  1.00 28.32           O  
ANISOU 1580  O   GLY A 190     3871   3352   3536     72     62   -644       O  
ATOM   1581  N   PRO A 191      36.385  33.521  20.091  1.00 24.17           N  
ANISOU 1581  N   PRO A 191     3369   2765   3049     -4     87   -601       N  
ATOM   1582  CA  PRO A 191      35.660  34.272  21.110  1.00 22.60           C  
ANISOU 1582  CA  PRO A 191     3169   2564   2853    -40    100   -580       C  
ATOM   1583  C   PRO A 191      36.047  35.764  21.056  1.00 25.55           C  
ANISOU 1583  C   PRO A 191     3537   2978   3194    -16     90   -542       C  
ATOM   1584  O   PRO A 191      36.926  36.156  20.269  1.00 27.68           O  
ANISOU 1584  O   PRO A 191     3804   3274   3439     17     80   -523       O  
ATOM   1585  CB  PRO A 191      36.107  33.607  22.419  1.00 26.64           C  
ANISOU 1585  CB  PRO A 191     3723   3018   3382    -68    119   -541       C  
ATOM   1586  CG  PRO A 191      37.407  33.035  22.099  1.00 28.84           C  
ANISOU 1586  CG  PRO A 191     4020   3282   3654    -28    107   -524       C  
ATOM   1587  CD  PRO A 191      37.300  32.544  20.705  1.00 22.49           C  
ANISOU 1587  CD  PRO A 191     3196   2498   2853      0     93   -578       C  
ATOM   1588  N   ILE A 192      35.392  36.574  21.879  1.00 26.72           N  
ANISOU 1588  N   ILE A 192     3684   3127   3341    -34     96   -534       N  
ATOM   1589  CA  ILE A 192      35.481  38.025  21.716  1.00 25.55           C  
ANISOU 1589  CA  ILE A 192     3538   3002   3169    -11     82   -511       C  
ATOM   1590  C   ILE A 192      36.893  38.540  21.998  1.00 27.01           C  
ANISOU 1590  C   ILE A 192     3745   3175   3341    -12     81   -458       C  
ATOM   1591  O   ILE A 192      37.381  39.419  21.281  1.00 26.31           O  
ANISOU 1591  O   ILE A 192     3661   3102   3233      6     73   -435       O  
ATOM   1592  CB  ILE A 192      34.422  38.732  22.584  1.00 23.63           C  
ANISOU 1592  CB  ILE A 192     3288   2761   2928    -21     86   -527       C  
ATOM   1593  CG1 ILE A 192      34.391  40.229  22.247  1.00 20.59           C  
ANISOU 1593  CG1 ILE A 192     2918   2385   2521     16     66   -511       C  
ATOM   1594  CG2 ILE A 192      34.647  38.495  24.074  1.00 21.24           C  
ANISOU 1594  CG2 ILE A 192     3005   2432   2634    -58    107   -506       C  
ATOM   1595  CD1 ILE A 192      33.439  41.073  23.095  1.00 23.63           C  
ANISOU 1595  CD1 ILE A 192     3300   2773   2906     24     64   -533       C  
ATOM   1596  N   LEU A 193      37.603  37.980  23.016  1.00 25.33           N  
ANISOU 1596  N   LEU A 193     3546   2940   3139    -32     90   -438       N  
ATOM   1597  CA  LEU A 193      38.833  38.672  23.450  1.00 26.03           C  
ANISOU 1597  CA  LEU A 193     3642   3031   3216    -38     84   -400       C  
ATOM   1598  C   LEU A 193      40.055  38.570  22.540  1.00 23.90           C  
ANISOU 1598  C   LEU A 193     3356   2791   2935    -22     81   -383       C  
ATOM   1599  O   LEU A 193      40.775  39.577  22.428  1.00 24.36           O  
ANISOU 1599  O   LEU A 193     3411   2863   2983    -37     80   -358       O  
ATOM   1600  CB  LEU A 193      39.279  38.236  24.845  1.00 22.89           C  
ANISOU 1600  CB  LEU A 193     3259   2617   2820    -52     85   -386       C  
ATOM   1601  CG  LEU A 193      38.385  38.622  26.030  1.00 21.01           C  
ANISOU 1601  CG  LEU A 193     3037   2367   2580    -72     92   -393       C  
ATOM   1602  CD1 LEU A 193      39.116  38.413  27.325  1.00 20.37           C  
ANISOU 1602  CD1 LEU A 193     2972   2284   2483    -78     88   -372       C  
ATOM   1603  CD2 LEU A 193      37.891  40.079  25.888  1.00 20.21           C  
ANISOU 1603  CD2 LEU A 193     2934   2268   2475    -72     84   -404       C  
ATOM   1604  N   PRO A 194      40.344  37.420  21.875  1.00 21.13           N  
ANISOU 1604  N   PRO A 194     2994   2451   2584      4     83   -400       N  
ATOM   1605  CA  PRO A 194      41.593  37.353  21.091  1.00 21.32           C  
ANISOU 1605  CA  PRO A 194     2991   2519   2589     24     84   -389       C  
ATOM   1606  C   PRO A 194      41.810  38.549  20.161  1.00 20.76           C  
ANISOU 1606  C   PRO A 194     2910   2483   2493     14     92   -366       C  
ATOM   1607  O   PRO A 194      42.887  39.135  20.207  1.00 26.72           O  
ANISOU 1607  O   PRO A 194     3648   3267   3239     -7    100   -339       O  
ATOM   1608  CB  PRO A 194      41.470  36.013  20.334  1.00 24.06           C  
ANISOU 1608  CB  PRO A 194     3334   2867   2939     63     82   -427       C  
ATOM   1609  CG  PRO A 194      40.736  35.129  21.291  1.00 26.46           C  
ANISOU 1609  CG  PRO A 194     3670   3110   3274     52     80   -441       C  
ATOM   1610  CD  PRO A 194      39.671  36.107  21.913  1.00 23.87           C  
ANISOU 1610  CD  PRO A 194     3351   2768   2951     12     85   -432       C  
ATOM   1611  N   LYS A 195      40.834  38.929  19.332  1.00 25.45           N  
ANISOU 1611  N   LYS A 195     3516   3078   3074     27     91   -374       N  
ATOM   1612  CA  LYS A 195      40.999  40.076  18.430  1.00 25.53           C  
ANISOU 1612  CA  LYS A 195     3536   3113   3053     25    100   -339       C  
ATOM   1613  C   LYS A 195      40.839  41.415  19.156  1.00 29.40           C  
ANISOU 1613  C   LYS A 195     4057   3557   3555    -11     98   -308       C  
ATOM   1614  O   LYS A 195      41.388  42.423  18.705  1.00 22.16           O  
ANISOU 1614  O   LYS A 195     3156   2642   2622    -33    110   -265       O  
ATOM   1615  CB  LYS A 195      39.960  40.063  17.282  1.00 26.86           C  
ANISOU 1615  CB  LYS A 195     3712   3302   3192     69     91   -360       C  
ATOM   1616  CG  LYS A 195      40.181  39.052  16.148  1.00 33.12           C  
ANISOU 1616  CG  LYS A 195     4477   4152   3956    109     93   -392       C  
ATOM   1617  CD  LYS A 195      39.178  39.264  14.978  1.00 30.13           C  
ANISOU 1617  CD  LYS A 195     4105   3807   3535    156     78   -413       C  
ATOM   1618  CE  LYS A 195      37.742  38.965  15.410  1.00 29.37           C  
ANISOU 1618  CE  LYS A 195     4007   3683   3469    164     53   -466       C  
ATOM   1619  NZ  LYS A 195      37.570  37.533  15.865  1.00 34.75           N  
ANISOU 1619  NZ  LYS A 195     4665   4344   4193    151     50   -525       N  
ATOM   1620  N   ASN A 196      40.065  41.462  20.234  1.00 20.74           N  
ANISOU 1620  N   ASN A 196     2976   2420   2486    -18     84   -329       N  
ATOM   1621  CA  ASN A 196      39.625  42.737  20.806  1.00 20.83           C  
ANISOU 1621  CA  ASN A 196     3022   2386   2505    -33     76   -316       C  
ATOM   1622  C   ASN A 196      40.428  43.035  22.078  1.00 22.94           C  
ANISOU 1622  C   ASN A 196     3289   2633   2795    -78     74   -311       C  
ATOM   1623  O   ASN A 196      39.920  42.986  23.202  1.00 23.24           O  
ANISOU 1623  O   ASN A 196     3334   2651   2847    -81     65   -335       O  
ATOM   1624  CB  ASN A 196      38.107  42.695  21.024  1.00 21.57           C  
ANISOU 1624  CB  ASN A 196     3123   2467   2604      1     61   -354       C  
ATOM   1625  CG  ASN A 196      37.333  42.595  19.689  1.00 22.25           C  
ANISOU 1625  CG  ASN A 196     3206   2586   2663     51     53   -366       C  
ATOM   1626  OD1 ASN A 196      37.430  43.495  18.866  1.00 28.55           O  
ANISOU 1626  OD1 ASN A 196     4035   3380   3433     71     50   -331       O  
ATOM   1627  ND2 ASN A 196      36.593  41.478  19.457  1.00 22.24           N  
ANISOU 1627  ND2 ASN A 196     3170   2614   2665     70     49   -414       N  
ATOM   1628  N   TYR A 197      41.727  43.325  21.859  1.00 21.05           N  
ANISOU 1628  N   TYR A 197     3034   2412   2552   -114     85   -283       N  
ATOM   1629  CA  TYR A 197      42.721  43.451  22.925  1.00 25.58           C  
ANISOU 1629  CA  TYR A 197     3588   2991   3141   -155     80   -288       C  
ATOM   1630  C   TYR A 197      42.425  44.615  23.844  1.00 27.11           C  
ANISOU 1630  C   TYR A 197     3818   3130   3352   -184     65   -296       C  
ATOM   1631  O   TYR A 197      42.879  44.602  24.996  1.00 22.91           O  
ANISOU 1631  O   TYR A 197     3273   2602   2828   -205     51   -318       O  
ATOM   1632  CB  TYR A 197      44.149  43.641  22.366  1.00 22.83           C  
ANISOU 1632  CB  TYR A 197     3201   2689   2786   -194     97   -264       C  
ATOM   1633  CG  TYR A 197      44.254  44.765  21.372  1.00 27.34           C  
ANISOU 1633  CG  TYR A 197     3801   3239   3349   -228    119   -223       C  
ATOM   1634  CD1 TYR A 197      43.927  44.557  20.026  1.00 27.15           C  
ANISOU 1634  CD1 TYR A 197     3785   3239   3292   -193    138   -199       C  
ATOM   1635  CD2 TYR A 197      44.592  46.054  21.786  1.00 22.55           C  
ANISOU 1635  CD2 TYR A 197     3224   2581   2763   -291    120   -209       C  
ATOM   1636  CE1 TYR A 197      43.950  45.614  19.112  1.00 25.58           C  
ANISOU 1636  CE1 TYR A 197     3629   3017   3075   -217    159   -148       C  
ATOM   1637  CE2 TYR A 197      44.619  47.114  20.891  1.00 27.31           C  
ANISOU 1637  CE2 TYR A 197     3874   3145   3359   -323    142   -161       C  
ATOM   1638  CZ  TYR A 197      44.311  46.878  19.558  1.00 31.43           C  
ANISOU 1638  CZ  TYR A 197     4407   3694   3841   -284    164   -124       C  
ATOM   1639  OH  TYR A 197      44.355  47.916  18.679  1.00 31.33           O  
ANISOU 1639  OH  TYR A 197     4451   3642   3810   -311    188    -65       O  
ATOM   1640  N   GLU A 198      41.702  45.621  23.354  1.00 26.12           N  
ANISOU 1640  N   GLU A 198     3742   2955   3229   -178     65   -283       N  
ATOM   1641  CA  GLU A 198      41.352  46.745  24.218  1.00 26.47           C  
ANISOU 1641  CA  GLU A 198     3828   2937   3291   -194     47   -301       C  
ATOM   1642  C   GLU A 198      40.393  46.295  25.301  1.00 27.06           C  
ANISOU 1642  C   GLU A 198     3901   3017   3364   -158     32   -346       C  
ATOM   1643  O   GLU A 198      40.468  46.778  26.441  1.00 23.43           O  
ANISOU 1643  O   GLU A 198     3452   2539   2913   -174     16   -376       O  
ATOM   1644  CB  GLU A 198      40.782  47.906  23.390  1.00 25.90           C  
ANISOU 1644  CB  GLU A 198     3821   2802   3219   -181     47   -274       C  
ATOM   1645  CG  GLU A 198      41.878  48.781  22.765  1.00 27.96           C  
ANISOU 1645  CG  GLU A 198     4104   3032   3487   -248     66   -226       C  
ATOM   1646  CD  GLU A 198      41.499  49.468  21.428  1.00 43.35           C  
ANISOU 1646  CD  GLU A 198     6114   4944   5414   -225     80   -169       C  
ATOM   1647  OE1 GLU A 198      41.256  48.776  20.397  1.00 36.40           O  
ANISOU 1647  OE1 GLU A 198     5214   4120   4498   -181     93   -147       O  
ATOM   1648  OE2 GLU A 198      41.479  50.730  21.404  1.00 53.97           O  
ANISOU 1648  OE2 GLU A 198     7533   6199   6775   -248     77   -145       O  
ATOM   1649  N   ILE A 199      39.555  45.297  25.008  1.00 21.03           N  
ANISOU 1649  N   ILE A 199     3117   2285   2588   -114     38   -356       N  
ATOM   1650  CA  ILE A 199      38.678  44.779  26.052  1.00 23.89           C  
ANISOU 1650  CA  ILE A 199     3471   2660   2946    -94     36   -393       C  
ATOM   1651  C   ILE A 199      39.490  43.984  27.069  1.00 25.23           C  
ANISOU 1651  C   ILE A 199     3618   2858   3110   -118     37   -394       C  
ATOM   1652  O   ILE A 199      39.308  44.136  28.287  1.00 21.70           O  
ANISOU 1652  O   ILE A 199     3178   2413   2653   -120     30   -418       O  
ATOM   1653  CB  ILE A 199      37.567  43.910  25.457  1.00 22.23           C  
ANISOU 1653  CB  ILE A 199     3242   2476   2730    -58     46   -407       C  
ATOM   1654  CG1 ILE A 199      36.727  44.682  24.460  1.00 20.83           C  
ANISOU 1654  CG1 ILE A 199     3082   2284   2547    -18     36   -410       C  
ATOM   1655  CG2 ILE A 199      36.701  43.317  26.569  1.00 20.54           C  
ANISOU 1655  CG2 ILE A 199     3014   2280   2511    -54     56   -440       C  
ATOM   1656  CD1 ILE A 199      35.569  43.824  23.998  1.00 20.73           C  
ANISOU 1656  CD1 ILE A 199     3037   2312   2529     15     41   -442       C  
ATOM   1657  N   THR A 200      40.375  43.102  26.570  1.00 24.91           N  
ANISOU 1657  N   THR A 200     3551   2846   3067   -124     43   -371       N  
ATOM   1658  CA  THR A 200      41.269  42.323  27.430  1.00 28.92           C  
ANISOU 1658  CA  THR A 200     4040   3384   3565   -129     37   -369       C  
ATOM   1659  C   THR A 200      42.082  43.239  28.351  1.00 22.72           C  
ANISOU 1659  C   THR A 200     3253   2602   2778   -160     16   -383       C  
ATOM   1660  O   THR A 200      42.161  43.012  29.563  1.00 21.97           O  
ANISOU 1660  O   THR A 200     3161   2524   2662   -154      3   -398       O  
ATOM   1661  CB  THR A 200      42.202  41.457  26.568  1.00 28.57           C  
ANISOU 1661  CB  THR A 200     3965   3371   3520   -120     43   -350       C  
ATOM   1662  OG1 THR A 200      41.463  40.814  25.511  1.00 23.94           O  
ANISOU 1662  OG1 THR A 200     3380   2778   2937    -95     58   -348       O  
ATOM   1663  CG2 THR A 200      42.899  40.353  27.411  1.00 26.76           C  
ANISOU 1663  CG2 THR A 200     3724   3169   3276    -98     32   -348       C  
ATOM   1664  N   ASP A 201      42.704  44.269  27.771  1.00 23.53           N  
ANISOU 1664  N   ASP A 201     3353   2690   2898   -197     13   -377       N  
ATOM   1665  CA  ASP A 201      43.526  45.202  28.532  1.00 27.04           C  
ANISOU 1665  CA  ASP A 201     3792   3132   3349   -242     -8   -400       C  
ATOM   1666  C   ASP A 201      42.693  46.000  29.534  1.00 23.70           C  
ANISOU 1666  C   ASP A 201     3410   2670   2924   -236    -24   -437       C  
ATOM   1667  O   ASP A 201      43.151  46.258  30.648  1.00 22.83           O  
ANISOU 1667  O   ASP A 201     3292   2578   2803   -249    -48   -472       O  
ATOM   1668  CB  ASP A 201      44.260  46.144  27.577  1.00 26.27           C  
ANISOU 1668  CB  ASP A 201     3691   3013   3276   -297      3   -381       C  
ATOM   1669  CG  ASP A 201      45.388  45.447  26.807  1.00 31.62           C  
ANISOU 1669  CG  ASP A 201     4310   3757   3949   -310     18   -357       C  
ATOM   1670  OD1 ASP A 201      45.666  44.246  27.047  1.00 23.08           O  
ANISOU 1670  OD1 ASP A 201     3194   2729   2847   -267     13   -360       O  
ATOM   1671  OD2 ASP A 201      46.003  46.108  25.954  1.00 24.89           O  
ANISOU 1671  OD2 ASP A 201     3448   2900   3109   -361     38   -334       O  
ATOM   1672  N   TYR A 202      41.456  46.354  29.169  1.00 23.89           N  
ANISOU 1672  N   TYR A 202     3473   2652   2954   -207    -14   -438       N  
ATOM   1673  CA  TYR A 202      40.542  46.991  30.115  1.00 25.44           C  
ANISOU 1673  CA  TYR A 202     3700   2824   3142   -184    -26   -482       C  
ATOM   1674  C   TYR A 202      40.371  46.146  31.368  1.00 24.50           C  
ANISOU 1674  C   TYR A 202     3563   2760   2985   -163    -28   -502       C  
ATOM   1675  O   TYR A 202      40.476  46.650  32.489  1.00 26.37           O  
ANISOU 1675  O   TYR A 202     3809   3006   3204   -166    -47   -543       O  
ATOM   1676  CB  TYR A 202      39.176  47.233  29.459  1.00 22.73           C  
ANISOU 1676  CB  TYR A 202     3383   2451   2803   -139    -15   -483       C  
ATOM   1677  CG  TYR A 202      38.150  47.848  30.388  1.00 24.14           C  
ANISOU 1677  CG  TYR A 202     3584   2620   2969   -103    -25   -536       C  
ATOM   1678  CD1 TYR A 202      37.352  47.049  31.211  1.00 25.43           C  
ANISOU 1678  CD1 TYR A 202     3724   2839   3100    -76     -9   -557       C  
ATOM   1679  CD2 TYR A 202      38.011  49.239  30.483  1.00 23.51           C  
ANISOU 1679  CD2 TYR A 202     3553   2473   2908    -96    -49   -567       C  
ATOM   1680  CE1 TYR A 202      36.398  47.626  32.087  1.00 26.44           C  
ANISOU 1680  CE1 TYR A 202     3862   2976   3208    -39    -13   -612       C  
ATOM   1681  CE2 TYR A 202      37.058  49.823  31.348  1.00 25.05           C  
ANISOU 1681  CE2 TYR A 202     3765   2664   3087    -50    -60   -627       C  
ATOM   1682  CZ  TYR A 202      36.265  49.007  32.150  1.00 25.96           C  
ANISOU 1682  CZ  TYR A 202     3844   2856   3165    -20    -41   -651       C  
ATOM   1683  OH  TYR A 202      35.342  49.569  33.008  1.00 30.27           O  
ANISOU 1683  OH  TYR A 202     4397   3416   3688     27    -47   -715       O  
ATOM   1684  N   LEU A 203      40.062  44.860  31.204  1.00 25.04           N  
ANISOU 1684  N   LEU A 203     3614   2863   3038   -142     -5   -473       N  
ATOM   1685  CA  LEU A 203      39.793  44.054  32.381  1.00 21.47           C  
ANISOU 1685  CA  LEU A 203     3160   2452   2544   -124      1   -479       C  
ATOM   1686  C   LEU A 203      41.054  43.894  33.206  1.00 25.95           C  
ANISOU 1686  C   LEU A 203     3715   3057   3087   -133    -26   -480       C  
ATOM   1687  O   LEU A 203      41.003  43.972  34.437  1.00 23.03           O  
ANISOU 1687  O   LEU A 203     3355   2720   2677   -121    -37   -504       O  
ATOM   1688  CB  LEU A 203      39.214  42.680  31.994  1.00 23.57           C  
ANISOU 1688  CB  LEU A 203     3420   2729   2805   -109     33   -445       C  
ATOM   1689  CG  LEU A 203      37.873  42.641  31.250  1.00 25.09           C  
ANISOU 1689  CG  LEU A 203     3610   2906   3016   -100     58   -454       C  
ATOM   1690  CD1 LEU A 203      37.681  41.347  30.470  1.00 20.75           C  
ANISOU 1690  CD1 LEU A 203     3049   2355   2479   -101     80   -426       C  
ATOM   1691  CD2 LEU A 203      36.734  42.791  32.273  1.00 26.94           C  
ANISOU 1691  CD2 LEU A 203     3849   3166   3222    -89     77   -486       C  
ATOM   1692  N   LEU A 204      42.201  43.683  32.553  1.00 21.76           N  
ANISOU 1692  N   LEU A 204     3157   2536   2576   -149    -38   -460       N  
ATOM   1693  CA  LEU A 204      43.438  43.519  33.319  1.00 23.59           C  
ANISOU 1693  CA  LEU A 204     3362   2820   2783   -151    -70   -471       C  
ATOM   1694  C   LEU A 204      43.859  44.832  33.981  1.00 24.72           C  
ANISOU 1694  C   LEU A 204     3501   2962   2929   -186   -101   -526       C  
ATOM   1695  O   LEU A 204      44.349  44.840  35.114  1.00 27.75           O  
ANISOU 1695  O   LEU A 204     3875   3395   3273   -174   -132   -557       O  
ATOM   1696  CB  LEU A 204      44.567  43.012  32.420  1.00 26.37           C  
ANISOU 1696  CB  LEU A 204     3671   3196   3153   -157    -73   -447       C  
ATOM   1697  CG  LEU A 204      44.424  41.647  31.744  1.00 24.93           C  
ANISOU 1697  CG  LEU A 204     3489   3014   2968   -117    -51   -404       C  
ATOM   1698  CD1 LEU A 204      45.419  41.518  30.613  1.00 21.87           C  
ANISOU 1698  CD1 LEU A 204     3055   2649   2604   -128    -50   -394       C  
ATOM   1699  CD2 LEU A 204      44.617  40.525  32.802  1.00 24.86           C  
ANISOU 1699  CD2 LEU A 204     3496   3037   2911    -65    -64   -388       C  
ATOM   1700  N   GLU A 205      43.704  45.954  33.285  1.00 26.15           N  
ANISOU 1700  N   GLU A 205     3695   3085   3156   -227    -98   -541       N  
ATOM   1701  CA  GLU A 205      44.169  47.203  33.877  1.00 23.38           C  
ANISOU 1701  CA  GLU A 205     3348   2717   2819   -269   -129   -599       C  
ATOM   1702  C   GLU A 205      43.314  47.602  35.076  1.00 23.61           C  
ANISOU 1702  C   GLU A 205     3412   2745   2812   -236   -143   -648       C  
ATOM   1703  O   GLU A 205      43.842  48.110  36.073  1.00 25.06           O  
ANISOU 1703  O   GLU A 205     3588   2958   2976   -247   -179   -706       O  
ATOM   1704  CB  GLU A 205      44.199  48.322  32.827  1.00 24.41           C  
ANISOU 1704  CB  GLU A 205     3502   2766   3008   -322   -119   -593       C  
ATOM   1705  CG  GLU A 205      45.125  49.461  33.268  1.00 34.95           C  
ANISOU 1705  CG  GLU A 205     4829   4081   4370   -393   -150   -648       C  
ATOM   1706  CD  GLU A 205      45.088  50.679  32.339  1.00 51.13           C  
ANISOU 1706  CD  GLU A 205     6924   6027   6477   -452   -136   -637       C  
ATOM   1707  OE1 GLU A 205      44.040  50.940  31.704  1.00 50.50           O  
ANISOU 1707  OE1 GLU A 205     6900   5880   6406   -415   -117   -608       O  
ATOM   1708  OE2 GLU A 205      46.123  51.384  32.257  1.00 58.63           O  
ANISOU 1708  OE2 GLU A 205     7853   6962   7461   -536   -146   -659       O  
ATOM   1709  N   LYS A 206      41.989  47.427  34.990  1.00 24.13           N  
ANISOU 1709  N   LYS A 206     3511   2788   2869   -194   -115   -636       N  
ATOM   1710  CA  LYS A 206      41.159  47.721  36.156  1.00 24.95           C  
ANISOU 1710  CA  LYS A 206     3638   2912   2929   -157   -120   -686       C  
ATOM   1711  C   LYS A 206      41.539  46.810  37.313  1.00 25.53           C  
ANISOU 1711  C   LYS A 206     3695   3074   2933   -131   -128   -683       C  
ATOM   1712  O   LYS A 206      41.530  47.224  38.473  1.00 26.99           O  
ANISOU 1712  O   LYS A 206     3887   3296   3071   -114   -152   -737       O  
ATOM   1713  CB  LYS A 206      39.662  47.572  35.839  1.00 23.22           C  
ANISOU 1713  CB  LYS A 206     3439   2675   2707   -117    -83   -675       C  
ATOM   1714  CG  LYS A 206      39.100  48.572  34.802  1.00 23.21           C  
ANISOU 1714  CG  LYS A 206     3466   2591   2761   -117    -83   -684       C  
ATOM   1715  CD  LYS A 206      39.162  50.048  35.331  1.00 28.63           C  
ANISOU 1715  CD  LYS A 206     4191   3223   3464   -120   -119   -756       C  
ATOM   1716  CE  LYS A 206      38.755  51.056  34.205  1.00 30.75           C  
ANISOU 1716  CE  LYS A 206     4506   3390   3788   -117   -122   -749       C  
ATOM   1717  NZ  LYS A 206      38.945  52.475  34.696  1.00 41.46           N  
ANISOU 1717  NZ  LYS A 206     5913   4670   5169   -127   -159   -818       N  
ATOM   1718  N   ALA A 207      41.911  45.572  37.010  1.00 23.38           N  
ANISOU 1718  N   ALA A 207     3405   2832   2648   -121   -113   -620       N  
ATOM   1719  CA  ALA A 207      42.272  44.654  38.086  1.00 30.11           C  
ANISOU 1719  CA  ALA A 207     4255   3758   3427    -85   -121   -605       C  
ATOM   1720  C   ALA A 207      43.590  45.067  38.730  1.00 24.31           C  
ANISOU 1720  C   ALA A 207     3490   3074   2673    -93   -178   -649       C  
ATOM   1721  O   ALA A 207      43.741  44.985  39.957  1.00 24.88           O  
ANISOU 1721  O   ALA A 207     3568   3211   2674    -60   -202   -676       O  
ATOM   1722  CB  ALA A 207      42.342  43.213  37.551  1.00 25.80           C  
ANISOU 1722  CB  ALA A 207     3710   3214   2878    -65    -94   -528       C  
ATOM   1723  N   CYS A 208      44.564  45.491  37.911  1.00 25.37           N  
ANISOU 1723  N   CYS A 208     3586   3190   2865   -138   -198   -659       N  
ATOM   1724  CA  CYS A 208      45.844  45.938  38.455  1.00 28.93           C  
ANISOU 1724  CA  CYS A 208     3990   3697   3305   -160   -252   -713       C  
ATOM   1725  C   CYS A 208      45.660  47.187  39.302  1.00 29.44           C  
ANISOU 1725  C   CYS A 208     4070   3752   3363   -182   -283   -801       C  
ATOM   1726  O   CYS A 208      46.206  47.281  40.408  1.00 35.45           O  
ANISOU 1726  O   CYS A 208     4812   4588   4068   -162   -328   -855       O  
ATOM   1727  CB  CYS A 208      46.841  46.204  37.331  1.00 25.01           C  
ANISOU 1727  CB  CYS A 208     3443   3185   2876   -219   -255   -707       C  
ATOM   1728  SG  CYS A 208      47.389  44.713  36.412  1.00 29.75           S  
ANISOU 1728  SG  CYS A 208     4008   3819   3475   -181   -233   -627       S  
ATOM   1729  N   GLU A 209      44.883  48.157  38.803  1.00 26.86           N  
ANISOU 1729  N   GLU A 209     3781   3335   3090   -214   -263   -821       N  
ATOM   1730  CA  GLU A 209      44.636  49.369  39.580  1.00 28.51           C  
ANISOU 1730  CA  GLU A 209     4016   3520   3297   -227   -294   -912       C  
ATOM   1731  C   GLU A 209      44.006  49.026  40.915  1.00 26.48           C  
ANISOU 1731  C   GLU A 209     3778   3336   2947   -156   -300   -940       C  
ATOM   1732  O   GLU A 209      44.423  49.540  41.953  1.00 28.86           O  
ANISOU 1732  O   GLU A 209     4071   3687   3208   -151   -346  -1020       O  
ATOM   1733  CB  GLU A 209      43.715  50.334  38.836  1.00 29.37           C  
ANISOU 1733  CB  GLU A 209     4177   3514   3470   -245   -270   -919       C  
ATOM   1734  CG  GLU A 209      44.311  51.029  37.661  1.00 40.84           C  
ANISOU 1734  CG  GLU A 209     5629   4881   5006   -321   -266   -902       C  
ATOM   1735  CD  GLU A 209      43.288  51.885  36.922  0.40 44.96           C  
ANISOU 1735  CD  GLU A 209     6218   5288   5578   -315   -244   -896       C  
ATOM   1736  OE1 GLU A 209      42.160  52.083  37.446  0.76 47.64           O  
ANISOU 1736  OE1 GLU A 209     6594   5619   5887   -251   -240   -927       O  
ATOM   1737  OE2 GLU A 209      43.621  52.352  35.811  0.70 42.12           O  
ANISOU 1737  OE2 GLU A 209     5872   4852   5278   -369   -230   -858       O  
ATOM   1738  N   ARG A 210      42.980  48.166  40.901  1.00 25.92           N  
ANISOU 1738  N   ARG A 210     3732   3278   2840   -106   -252   -878       N  
ATOM   1739  CA  ARG A 210      42.311  47.794  42.146  1.00 33.13           C  
ANISOU 1739  CA  ARG A 210     4664   4266   3656    -46   -243   -893       C  
ATOM   1740  C   ARG A 210      43.261  47.070  43.099  1.00 34.56           C  
ANISOU 1740  C   ARG A 210     4825   4550   3756    -15   -279   -887       C  
ATOM   1741  O   ARG A 210      43.150  47.218  44.316  1.00 38.22           O  
ANISOU 1741  O   ARG A 210     5300   5088   4135     25   -300   -935       O  
ATOM   1742  CB  ARG A 210      41.085  46.927  41.836  1.00 31.90           C  
ANISOU 1742  CB  ARG A 210     4531   4103   3485    -18   -176   -820       C  
ATOM   1743  CG  ARG A 210      39.910  47.710  41.210  1.00 33.84           C  
ANISOU 1743  CG  ARG A 210     4795   4278   3784    -22   -147   -847       C  
ATOM   1744  CD  ARG A 210      38.791  46.765  40.679  1.00 25.88           C  
ANISOU 1744  CD  ARG A 210     3789   3269   2775     -9    -81   -777       C  
ATOM   1745  NE  ARG A 210      38.374  45.781  41.667  1.00 32.45           N  
ANISOU 1745  NE  ARG A 210     4628   4184   3519     20    -46   -743       N  
ATOM   1746  CZ  ARG A 210      37.416  45.961  42.570  1.00 30.45           C  
ANISOU 1746  CZ  ARG A 210     4381   3988   3200     50    -18   -779       C  
ATOM   1747  NH1 ARG A 210      37.144  44.980  43.402  1.00 30.72           N  
ANISOU 1747  NH1 ARG A 210     4427   4095   3151     65     21   -730       N  
ATOM   1748  NH2 ARG A 210      36.752  47.112  42.660  1.00 31.94           N  
ANISOU 1748  NH2 ARG A 210     4569   4163   3404     70    -27   -863       N  
ATOM   1749  N   LYS A 211      44.209  46.298  42.579  1.00 26.59           N  
ANISOU 1749  N   LYS A 211     3784   3555   2763    -23   -291   -833       N  
ATOM   1750  CA  LYS A 211      45.102  45.574  43.472  1.00 35.59           C  
ANISOU 1750  CA  LYS A 211     4907   4797   3820     26   -331   -826       C  
ATOM   1751  C   LYS A 211      46.308  46.410  43.898  1.00 37.52           C  
ANISOU 1751  C   LYS A 211     5096   5091   4067      0   -406   -922       C  
ATOM   1752  O   LYS A 211      46.916  46.116  44.931  1.00 38.79           O  
ANISOU 1752  O   LYS A 211     5243   5355   4140     51   -454   -949       O  
ATOM   1753  CB  LYS A 211      45.555  44.273  42.793  1.00 31.96           C  
ANISOU 1753  CB  LYS A 211     4439   4335   3368     48   -314   -729       C  
ATOM   1754  CG  LYS A 211      46.383  43.376  43.638  1.00 40.73           C  
ANISOU 1754  CG  LYS A 211     5545   5542   4389    119   -354   -706       C  
ATOM   1755  CD  LYS A 211      46.853  42.146  42.866  1.00 42.69           C  
ANISOU 1755  CD  LYS A 211     5790   5772   4657    148   -341   -620       C  
ATOM   1756  CE  LYS A 211      47.759  41.329  43.763  1.00 35.01           C  
ANISOU 1756  CE  LYS A 211     4817   4897   3589    236   -393   -602       C  
ATOM   1757  NZ  LYS A 211      47.818  39.928  43.352  1.00 39.47           N  
ANISOU 1757  NZ  LYS A 211     5421   5432   4145    291   -369   -503       N  
ATOM   1758  N   GLY A 212      46.627  47.472  43.165  1.00 32.98           N  
ANISOU 1758  N   GLY A 212     4496   4448   3588    -79   -418   -976       N  
ATOM   1759  CA  GLY A 212      47.806  48.264  43.459  1.00 28.85           C  
ANISOU 1759  CA  GLY A 212     3914   3966   3083   -126   -483  -1071       C  
ATOM   1760  C   GLY A 212      49.096  47.689  42.897  1.00 30.91           C  
ANISOU 1760  C   GLY A 212     4098   4279   3367   -144   -506  -1046       C  
ATOM   1761  O   GLY A 212      50.141  47.779  43.550  1.00 32.98           O  
ANISOU 1761  O   GLY A 212     4298   4640   3593   -139   -569  -1113       O  
ATOM   1762  N   ILE A 213      49.046  47.077  41.716  1.00 32.56           N  
ANISOU 1762  N   ILE A 213     4305   4438   3630   -156   -459   -959       N  
ATOM   1763  CA  ILE A 213      50.242  46.610  41.014  1.00 37.13           C  
ANISOU 1763  CA  ILE A 213     4805   5064   4238   -175   -472   -942       C  
ATOM   1764  C   ILE A 213      50.285  47.302  39.656  1.00 34.60           C  
ANISOU 1764  C   ILE A 213     4473   4649   4024   -273   -431   -928       C  
ATOM   1765  O   ILE A 213      49.249  47.757  39.142  1.00 32.28           O  
ANISOU 1765  O   ILE A 213     4245   4249   3772   -297   -387   -901       O  
ATOM   1766  CB  ILE A 213      50.266  45.068  40.876  1.00 32.69           C  
ANISOU 1766  CB  ILE A 213     4253   4543   3625    -82   -457   -849       C  
ATOM   1767  CG1 ILE A 213      49.117  44.564  40.018  1.00 28.67           C  
ANISOU 1767  CG1 ILE A 213     3812   3933   3149    -76   -385   -760       C  
ATOM   1768  CG2 ILE A 213      50.186  44.399  42.214  1.00 29.23           C  
ANISOU 1768  CG2 ILE A 213     3844   4188   3073     17   -492   -846       C  
ATOM   1769  CD1 ILE A 213      49.363  43.147  39.491  1.00 34.41           C  
ANISOU 1769  CD1 ILE A 213     4539   4676   3861    -11   -368   -678       C  
ATOM   1770  N   PRO A 214      51.463  47.412  39.044  1.00 34.07           N  
ANISOU 1770  N   PRO A 214     4320   4625   3999   -330   -443   -947       N  
ATOM   1771  CA  PRO A 214      51.560  48.120  37.759  1.00 40.18           C  
ANISOU 1771  CA  PRO A 214     5087   5314   4865   -431   -398   -928       C  
ATOM   1772  C   PRO A 214      50.995  47.310  36.601  1.00 39.09           C  
ANISOU 1772  C   PRO A 214     4981   5127   4744   -398   -338   -826       C  
ATOM   1773  O   PRO A 214      50.934  46.078  36.617  1.00 33.83           O  
ANISOU 1773  O   PRO A 214     4314   4508   4032   -311   -335   -775       O  
ATOM   1774  CB  PRO A 214      53.071  48.335  37.576  1.00 37.43           C  
ANISOU 1774  CB  PRO A 214     4621   5059   4542   -498   -427   -982       C  
ATOM   1775  CG  PRO A 214      53.685  47.170  38.301  1.00 36.92           C  
ANISOU 1775  CG  PRO A 214     4501   5131   4395   -390   -473   -985       C  
ATOM   1776  CD  PRO A 214      52.800  47.033  39.552  1.00 32.91           C  
ANISOU 1776  CD  PRO A 214     4074   4617   3815   -310   -501   -997       C  
ATOM   1777  N   PHE A 215      50.587  48.036  35.567  1.00 30.30           N  
ANISOU 1777  N   PHE A 215     3902   3915   3697   -468   -293   -798       N  
ATOM   1778  CA  PHE A 215      50.144  47.423  34.318  1.00 32.70           C  
ANISOU 1778  CA  PHE A 215     4227   4178   4020   -448   -239   -713       C  
ATOM   1779  C   PHE A 215      51.034  48.025  33.234  1.00 33.80           C  
ANISOU 1779  C   PHE A 215     4313   4313   4215   -546   -213   -708       C  
ATOM   1780  O   PHE A 215      50.728  49.077  32.666  1.00 29.47           O  
ANISOU 1780  O   PHE A 215     3810   3670   3717   -621   -187   -701       O  
ATOM   1781  CB  PHE A 215      48.634  47.676  34.071  1.00 29.74           C  
ANISOU 1781  CB  PHE A 215     3950   3694   3654   -423   -207   -678       C  
ATOM   1782  CG  PHE A 215      48.113  47.048  32.790  1.00 29.70           C  
ANISOU 1782  CG  PHE A 215     3965   3654   3664   -400   -158   -601       C  
ATOM   1783  CD1 PHE A 215      47.910  45.682  32.703  1.00 32.48           C  
ANISOU 1783  CD1 PHE A 215     4311   4050   3980   -323   -149   -559       C  
ATOM   1784  CD2 PHE A 215      47.855  47.830  31.668  1.00 32.00           C  
ANISOU 1784  CD2 PHE A 215     4287   3869   4004   -454   -124   -572       C  
ATOM   1785  CE1 PHE A 215      47.447  45.084  31.511  1.00 35.31           C  
ANISOU 1785  CE1 PHE A 215     4684   4380   4353   -303   -108   -503       C  
ATOM   1786  CE2 PHE A 215      47.386  47.263  30.497  1.00 34.55           C  
ANISOU 1786  CE2 PHE A 215     4624   4173   4330   -427    -84   -510       C  
ATOM   1787  CZ  PHE A 215      47.180  45.885  30.404  1.00 35.03           C  
ANISOU 1787  CZ  PHE A 215     4669   4283   4358   -353    -78   -481       C  
ATOM   1788  N   GLU A 216      52.178  47.388  32.984  1.00 31.59           N  
ANISOU 1788  N   GLU A 216     3938   4142   3924   -544   -219   -712       N  
ATOM   1789  CA  GLU A 216      53.210  48.079  32.197  1.00 29.22           C  
ANISOU 1789  CA  GLU A 216     3566   3867   3671   -656   -195   -726       C  
ATOM   1790  C   GLU A 216      53.993  47.029  31.445  1.00 33.32           C  
ANISOU 1790  C   GLU A 216     4001   4490   4169   -614   -177   -696       C  
ATOM   1791  O   GLU A 216      54.273  45.968  32.021  1.00 27.48           O  
ANISOU 1791  O   GLU A 216     3226   3836   3380   -514   -213   -707       O  
ATOM   1792  CB  GLU A 216      54.180  48.885  33.070  1.00 34.08           C  
ANISOU 1792  CB  GLU A 216     4111   4537   4301   -736   -241   -820       C  
ATOM   1793  CG  GLU A 216      53.604  50.131  33.734  1.00 55.44           C  
ANISOU 1793  CG  GLU A 216     6892   7134   7038   -798   -260   -869       C  
ATOM   1794  CD  GLU A 216      53.327  51.268  32.749  1.00 69.58           C  
ANISOU 1794  CD  GLU A 216     8745   8793   8899   -909   -207   -834       C  
ATOM   1795  OE1 GLU A 216      53.958  51.287  31.671  1.00 73.14           O  
ANISOU 1795  OE1 GLU A 216     9149   9265   9376   -975   -159   -791       O  
ATOM   1796  OE2 GLU A 216      52.477  52.142  33.054  1.00 73.59           O  
ANISOU 1796  OE2 GLU A 216     9351   9177   9431   -923   -214   -848       O  
ATOM   1797  N   PRO A 217      54.393  47.289  30.186  1.00 37.42           N  
ANISOU 1797  N   PRO A 217     4490   5009   4720   -683   -121   -658       N  
ATOM   1798  CA  PRO A 217      54.139  48.487  29.373  1.00 36.61           C  
ANISOU 1798  CA  PRO A 217     4437   4804   4668   -798    -71   -627       C  
ATOM   1799  C   PRO A 217      52.711  48.562  28.866  1.00 37.64           C  
ANISOU 1799  C   PRO A 217     4695   4807   4801   -751    -45   -562       C  
ATOM   1800  O   PRO A 217      52.119  47.539  28.513  1.00 30.86           O  
ANISOU 1800  O   PRO A 217     3857   3958   3909   -653    -37   -521       O  
ATOM   1801  CB  PRO A 217      55.104  48.318  28.200  1.00 39.58           C  
ANISOU 1801  CB  PRO A 217     4725   5263   5049   -850    -19   -600       C  
ATOM   1802  CG  PRO A 217      55.220  46.839  28.034  1.00 35.83           C  
ANISOU 1802  CG  PRO A 217     4206   4884   4524   -720    -30   -587       C  
ATOM   1803  CD  PRO A 217      55.163  46.277  29.439  1.00 35.54           C  
ANISOU 1803  CD  PRO A 217     4165   4883   4456   -634   -102   -640       C  
ATOM   1804  N   LYS A 218      52.137  49.761  28.827  1.00 34.78           N  
ANISOU 1804  N   LYS A 218     4416   4322   4478   -819    -35   -556       N  
ATOM   1805  CA  LYS A 218      50.746  49.838  28.410  1.00 37.17           C  
ANISOU 1805  CA  LYS A 218     4830   4516   4776   -759    -19   -504       C  
ATOM   1806  C   LYS A 218      50.585  49.597  26.921  1.00 32.58           C  
ANISOU 1806  C   LYS A 218     4263   3927   4188   -755     37   -425       C  
ATOM   1807  O   LYS A 218      49.541  49.128  26.493  1.00 34.96           O  
ANISOU 1807  O   LYS A 218     4622   4192   4468   -673     45   -386       O  
ATOM   1808  CB  LYS A 218      50.141  51.184  28.799  1.00 39.59           C  
ANISOU 1808  CB  LYS A 218     5229   4692   5123   -810    -31   -525       C  
ATOM   1809  CG  LYS A 218      50.232  51.413  30.285  1.00 50.95           C  
ANISOU 1809  CG  LYS A 218     6655   6145   6559   -805    -89   -613       C  
ATOM   1810  CD  LYS A 218      49.066  52.233  30.801  1.00 59.94           C  
ANISOU 1810  CD  LYS A 218     7902   7163   7711   -777   -109   -635       C  
ATOM   1811  CE  LYS A 218      49.330  52.699  32.229  1.00 62.84           C  
ANISOU 1811  CE  LYS A 218     8256   7544   8078   -793   -165   -734       C  
ATOM   1812  NZ  LYS A 218      49.375  51.577  33.212  1.00 57.50           N  
ANISOU 1812  NZ  LYS A 218     7523   6988   7338   -705   -199   -764       N  
ATOM   1813  N   GLU A 219      51.584  49.902  26.113  1.00 37.02           N  
ANISOU 1813  N   GLU A 219     4770   4533   4763   -841     78   -403       N  
ATOM   1814  CA  GLU A 219      51.421  49.791  24.673  1.00 43.67           C  
ANISOU 1814  CA  GLU A 219     5634   5371   5588   -838    135   -326       C  
ATOM   1815  C   GLU A 219      52.345  48.708  24.150  1.00 42.66           C  
ANISOU 1815  C   GLU A 219     5394   5388   5425   -812    155   -327       C  
ATOM   1816  O   GLU A 219      53.570  48.805  24.280  1.00 40.81           O  
ANISOU 1816  O   GLU A 219     5060   5246   5200   -883    163   -360       O  
ATOM   1817  CB  GLU A 219      51.667  51.129  23.982  1.00 57.33           C  
ANISOU 1817  CB  GLU A 219     7416   7016   7350   -959    180   -282       C  
ATOM   1818  CG  GLU A 219      50.353  51.789  23.602  1.00 72.91           C  
ANISOU 1818  CG  GLU A 219     9529   8847   9328   -919    181   -232       C  
ATOM   1819  CD  GLU A 219      50.271  53.242  24.009  1.00 85.10           C  
ANISOU 1819  CD  GLU A 219    11157  10254  10925  -1009    174   -241       C  
ATOM   1820  OE1 GLU A 219      51.031  54.061  23.449  1.00 90.56           O  
ANISOU 1820  OE1 GLU A 219    11854  10915  11641  -1131    220   -206       O  
ATOM   1821  OE2 GLU A 219      49.445  53.564  24.892  1.00 89.54           O  
ANISOU 1821  OE2 GLU A 219    11781  10737  11503   -960    126   -285       O  
ATOM   1822  N   ILE A 220      51.750  47.661  23.590  1.00 45.42           N  
ANISOU 1822  N   ILE A 220     5756   5764   5737   -705    159   -300       N  
ATOM   1823  CA  ILE A 220      52.486  46.551  23.043  1.00 39.16           C  
ANISOU 1823  CA  ILE A 220     4872   5098   4909   -656    174   -306       C  
ATOM   1824  C   ILE A 220      52.015  46.307  21.612  1.00 39.95           C  
ANISOU 1824  C   ILE A 220     5009   5195   4977   -623    221   -245       C  
ATOM   1825  O   ILE A 220      51.152  47.010  21.079  1.00 33.32           O  
ANISOU 1825  O   ILE A 220     4261   4259   4139   -637    240   -196       O  
ATOM   1826  CB  ILE A 220      52.351  45.286  23.913  1.00 35.76           C  
ANISOU 1826  CB  ILE A 220     4416   4711   4460   -544    121   -350       C  
ATOM   1827  CG1 ILE A 220      50.884  44.861  24.055  1.00 24.56           C  
ANISOU 1827  CG1 ILE A 220     3097   3199   3035   -462    103   -331       C  
ATOM   1828  CG2 ILE A 220      52.939  45.553  25.294  1.00 31.67           C  
ANISOU 1828  CG2 ILE A 220     3856   4219   3959   -572     73   -410       C  
ATOM   1829  CD1 ILE A 220      50.697  43.475  24.720  1.00 27.88           C  
ANISOU 1829  CD1 ILE A 220     3506   3652   3434   -356     65   -358       C  
ATOM   1830  N   ASP A 221      52.610  45.291  20.995  1.00 39.29           N  
ANISOU 1830  N   ASP A 221     4849   5223   4858   -569    237   -254       N  
ATOM   1831  CA  ASP A 221      52.350  44.972  19.598  1.00 35.40           C  
ANISOU 1831  CA  ASP A 221     4372   4756   4323   -534    282   -210       C  
ATOM   1832  C   ASP A 221      50.958  44.368  19.444  1.00 27.02           C  
ANISOU 1832  C   ASP A 221     3396   3619   3250   -435    255   -201       C  
ATOM   1833  O   ASP A 221      50.624  43.380  20.104  1.00 31.44           O  
ANISOU 1833  O   ASP A 221     3953   4178   3814   -355    213   -241       O  
ATOM   1834  CB  ASP A 221      53.433  44.022  19.103  1.00 47.11           C  
ANISOU 1834  CB  ASP A 221     5740   6387   5771   -495    300   -241       C  
ATOM   1835  CG  ASP A 221      53.174  43.514  17.707  1.00 49.90           C  
ANISOU 1835  CG  ASP A 221     6104   6784   6072   -440    340   -211       C  
ATOM   1836  OD1 ASP A 221      52.778  44.328  16.829  1.00 46.86           O  
ANISOU 1836  OD1 ASP A 221     5778   6359   5667   -488    384   -149       O  
ATOM   1837  OD2 ASP A 221      53.405  42.303  17.503  1.00 39.93           O  
ANISOU 1837  OD2 ASP A 221     4793   5595   4783   -343    325   -253       O  
ATOM   1838  N   ASN A 222      50.126  45.001  18.615  1.00 25.11           N  
ANISOU 1838  N   ASN A 222     3234   3312   2993   -442    279   -149       N  
ATOM   1839  CA  ASN A 222      48.765  44.547  18.358  1.00 32.53           C  
ANISOU 1839  CA  ASN A 222     4246   4192   3921   -357    255   -146       C  
ATOM   1840  C   ASN A 222      48.559  44.172  16.888  1.00 27.96           C  
ANISOU 1840  C   ASN A 222     3672   3666   3286   -310    288   -119       C  
ATOM   1841  O   ASN A 222      47.415  44.039  16.450  1.00 30.96           O  
ANISOU 1841  O   ASN A 222     4112   4001   3650   -251    272   -112       O  
ATOM   1842  CB  ASN A 222      47.744  45.621  18.781  1.00 27.83           C  
ANISOU 1842  CB  ASN A 222     3746   3475   3353   -380    238   -123       C  
ATOM   1843  CG  ASN A 222      47.895  46.042  20.240  1.00 34.14           C  
ANISOU 1843  CG  ASN A 222     4545   4226   4201   -422    204   -158       C  
ATOM   1844  OD1 ASN A 222      47.952  45.206  21.141  1.00 36.64           O  
ANISOU 1844  OD1 ASN A 222     4825   4568   4527   -383    172   -205       O  
ATOM   1845  ND2 ASN A 222      47.986  47.361  20.472  1.00 30.94           N  
ANISOU 1845  ND2 ASN A 222     4185   3748   3822   -500    212   -136       N  
ATOM   1846  N   GLU A 223      49.646  44.005  16.124  1.00 28.61           N  
ANISOU 1846  N   GLU A 223     3864   3243   3763   -748    106   -724       N  
ATOM   1847  CA  GLU A 223      49.552  43.896  14.667  1.00 35.35           C  
ANISOU 1847  CA  GLU A 223     4670   4196   4566   -822    218   -704       C  
ATOM   1848  C   GLU A 223      48.694  42.706  14.242  1.00 39.74           C  
ANISOU 1848  C   GLU A 223     5156   4781   5164   -617    279   -755       C  
ATOM   1849  O   GLU A 223      47.799  42.845  13.400  1.00 30.22           O  
ANISOU 1849  O   GLU A 223     4052   3534   3898   -586    309   -726       O  
ATOM   1850  CB  GLU A 223      50.948  43.774  14.059  1.00 42.51           C  
ANISOU 1850  CB  GLU A 223     5348   5335   5470  -1000    287   -724       C  
ATOM   1851  CG  GLU A 223      51.251  44.751  12.952  1.00 57.02           C  
ANISOU 1851  CG  GLU A 223     7241   7230   7195  -1238    344   -618       C  
ATOM   1852  CD  GLU A 223      50.745  46.161  13.240  1.00 66.71           C  
ANISOU 1852  CD  GLU A 223     8769   8197   8379  -1361    228   -505       C  
ATOM   1853  OE1 GLU A 223      49.774  46.594  12.577  1.00 64.33           O  
ANISOU 1853  OE1 GLU A 223     8663   7786   7995  -1322    239   -440       O  
ATOM   1854  OE2 GLU A 223      51.311  46.836  14.132  1.00 68.57           O  
ANISOU 1854  OE2 GLU A 223     9056   8331   8668  -1481    106   -495       O  
ATOM   1855  N   ALA A 224      48.974  41.521  14.797  1.00 34.41           N  
ANISOU 1855  N   ALA A 224     4309   4163   4603   -482    275   -829       N  
ATOM   1856  CA  ALA A 224      48.185  40.335  14.452  1.00 32.10           C  
ANISOU 1856  CA  ALA A 224     3954   3852   4390   -309    295   -875       C  
ATOM   1857  C   ALA A 224      46.706  40.557  14.745  1.00 27.65           C  
ANISOU 1857  C   ALA A 224     3558   3125   3824   -210    260   -792       C  
ATOM   1858  O   ALA A 224      45.833  40.174  13.952  1.00 25.83           O  
ANISOU 1858  O   ALA A 224     3341   2870   3603   -154    273   -800       O  
ATOM   1859  CB  ALA A 224      48.696  39.133  15.241  1.00 24.72           C  
ANISOU 1859  CB  ALA A 224     2851   2945   3597   -181    260   -933       C  
ATOM   1860  N   GLU A 225      46.413  41.188  15.881  1.00 24.62           N  
ANISOU 1860  N   GLU A 225     3291   2647   3418   -176    208   -721       N  
ATOM   1861  CA  GLU A 225      45.033  41.468  16.250  1.00 24.96           C  
ANISOU 1861  CA  GLU A 225     3466   2580   3437    -55    188   -639       C  
ATOM   1862  C   GLU A 225      44.400  42.427  15.250  1.00 24.74           C  
ANISOU 1862  C   GLU A 225     3595   2504   3300   -113    195   -613       C  
ATOM   1863  O   GLU A 225      43.255  42.233  14.811  1.00 28.05           O  
ANISOU 1863  O   GLU A 225     4038   2892   3728    -22    199   -579       O  
ATOM   1864  CB  GLU A 225      44.978  42.046  17.676  1.00 27.59           C  
ANISOU 1864  CB  GLU A 225     3903   2861   3720     24    132   -594       C  
ATOM   1865  CG  GLU A 225      45.269  41.076  18.851  1.00 22.69           C  
ANISOU 1865  CG  GLU A 225     3153   2287   3180    136    116   -574       C  
ATOM   1866  CD  GLU A 225      46.758  40.836  19.080  1.00 32.18           C  
ANISOU 1866  CD  GLU A 225     4241   3567   4419     42     84   -652       C  
ATOM   1867  OE1 GLU A 225      47.574  41.255  18.223  1.00 33.53           O  
ANISOU 1867  OE1 GLU A 225     4384   3784   4572   -122     98   -718       O  
ATOM   1868  OE2 GLU A 225      47.121  40.221  20.119  1.00 30.82           O  
ANISOU 1868  OE2 GLU A 225     3993   3430   4288    136     46   -634       O  
ATOM   1869  N   ILE A 226      45.128  43.487  14.903  1.00 30.42           N  
ANISOU 1869  N   ILE A 226     4423   3212   3925   -273    182   -612       N  
ATOM   1870  CA  ILE A 226      44.627  44.471  13.952  1.00 28.88           C  
ANISOU 1870  CA  ILE A 226     4402   2954   3618   -340    175   -559       C  
ATOM   1871  C   ILE A 226      44.346  43.819  12.598  1.00 30.02           C  
ANISOU 1871  C   ILE A 226     4456   3204   3748   -346    239   -584       C  
ATOM   1872  O   ILE A 226      43.282  44.040  12.002  1.00 28.53           O  
ANISOU 1872  O   ILE A 226     4362   2967   3510   -271    220   -548       O  
ATOM   1873  CB  ILE A 226      45.618  45.646  13.851  1.00 30.75           C  
ANISOU 1873  CB  ILE A 226     4755   3147   3782   -554    137   -524       C  
ATOM   1874  CG1 ILE A 226      45.580  46.466  15.156  1.00 27.48           C  
ANISOU 1874  CG1 ILE A 226     4508   2573   3362   -507     22   -523       C  
ATOM   1875  CG2 ILE A 226      45.345  46.496  12.577  1.00 30.57           C  
ANISOU 1875  CG2 ILE A 226     4881   3091   3642   -668    147   -439       C  
ATOM   1876  CD1 ILE A 226      46.745  47.494  15.322  1.00 33.62           C  
ANISOU 1876  CD1 ILE A 226     5370   3281   4123   -748    -63   -507       C  
ATOM   1877  N   GLN A 227      45.266  42.969  12.109  1.00 31.57           N  
ANISOU 1877  N   GLN A 227     4460   3556   3981   -405    301   -664       N  
ATOM   1878  CA  GLN A 227      45.050  42.315  10.811  1.00 30.42           C  
ANISOU 1878  CA  GLN A 227     4239   3525   3796   -380    346   -726       C  
ATOM   1879  C   GLN A 227      43.837  41.398  10.848  1.00 29.75           C  
ANISOU 1879  C   GLN A 227     4118   3370   3816   -206    296   -761       C  
ATOM   1880  O   GLN A 227      43.085  41.299   9.866  1.00 32.65           O  
ANISOU 1880  O   GLN A 227     4523   3753   4128   -166    277   -780       O  
ATOM   1881  CB  GLN A 227      46.285  41.519  10.379  1.00 32.31           C  
ANISOU 1881  CB  GLN A 227     4270   3959   4046   -422    417   -835       C  
ATOM   1882  CG  GLN A 227      47.512  42.359  10.054  1.00 38.99           C  
ANISOU 1882  CG  GLN A 227     5091   4944   4779   -626    486   -783       C  
ATOM   1883  CD  GLN A 227      48.750  41.497   9.778  1.00 45.66           C  
ANISOU 1883  CD  GLN A 227     5679   6027   5642   -625    565   -899       C  
ATOM   1884  OE1 GLN A 227      48.649  40.404   9.217  1.00 38.28           O  
ANISOU 1884  OE1 GLN A 227     4635   5181   4730   -474    582  -1037       O  
ATOM   1885  NE2 GLN A 227      49.920  41.989  10.180  1.00 47.72           N  
ANISOU 1885  NE2 GLN A 227     5842   6389   5901   -784    594   -855       N  
ATOM   1886  N   ALA A 228      43.630  40.709  11.965  1.00 26.16           N  
ANISOU 1886  N   ALA A 228     3581   2844   3513   -111    264   -758       N  
ATOM   1887  CA  ALA A 228      42.448  39.858  12.061  1.00 25.42           C  
ANISOU 1887  CA  ALA A 228     3433   2679   3545     15    210   -748       C  
ATOM   1888  C   ALA A 228      41.155  40.689  12.088  1.00 30.27           C  
ANISOU 1888  C   ALA A 228     4182   3222   4096     70    179   -642       C  
ATOM   1889  O   ALA A 228      40.149  40.301  11.464  1.00 22.79           O  
ANISOU 1889  O   ALA A 228     3207   2265   3187    127    132   -645       O  
ATOM   1890  CB  ALA A 228      42.553  38.959  13.288  1.00 22.20           C  
ANISOU 1890  CB  ALA A 228     2906   2223   3305     87    191   -720       C  
ATOM   1891  N   LYS A 229      41.144  41.810  12.840  1.00 28.62           N  
ANISOU 1891  N   LYS A 229     4116   2961   3797     74    184   -562       N  
ATOM   1892  CA  LYS A 229      39.982  42.712  12.825  1.00 25.24           C  
ANISOU 1892  CA  LYS A 229     3832   2471   3288    164    147   -480       C  
ATOM   1893  C   LYS A 229      39.694  43.223  11.417  1.00 25.98           C  
ANISOU 1893  C   LYS A 229     4025   2578   3267    115    125   -491       C  
ATOM   1894  O   LYS A 229      38.541  43.293  10.997  1.00 27.97           O  
ANISOU 1894  O   LYS A 229     4295   2823   3510    212     78   -458       O  
ATOM   1895  CB  LYS A 229      40.205  43.927  13.732  1.00 22.83           C  
ANISOU 1895  CB  LYS A 229     3707   2084   2883    185    130   -435       C  
ATOM   1896  CG  LYS A 229      40.196  43.713  15.250  1.00 22.53           C  
ANISOU 1896  CG  LYS A 229     3626   2044   2891    296    135   -409       C  
ATOM   1897  CD  LYS A 229      40.189  45.116  15.918  1.00 23.34           C  
ANISOU 1897  CD  LYS A 229     3967   2044   2859    355     77   -401       C  
ATOM   1898  CE  LYS A 229      40.177  45.081  17.435  1.00 26.53           C  
ANISOU 1898  CE  LYS A 229     4367   2468   3245    500     72   -394       C  
ATOM   1899  NZ  LYS A 229      40.220  46.469  17.959  1.00 34.03           N  
ANISOU 1899  NZ  LYS A 229     5579   3292   4057    567    -19   -432       N  
ATOM   1900  N   GLN A 230      40.734  43.592  10.680  1.00 29.10           N  
ANISOU 1900  N   GLN A 230     4473   3019   3563    -36    159   -522       N  
ATOM   1901  CA  GLN A 230      40.538  44.249   9.391  1.00 31.82           C  
ANISOU 1901  CA  GLN A 230     4946   3391   3754    -88    145   -494       C  
ATOM   1902  C   GLN A 230      39.822  43.352   8.375  1.00 33.64           C  
ANISOU 1902  C   GLN A 230     5075   3710   3997    -15    116   -567       C  
ATOM   1903  O   GLN A 230      39.111  43.852   7.495  1.00 29.74           O  
ANISOU 1903  O   GLN A 230     4690   3221   3387     21     65   -529       O  
ATOM   1904  CB  GLN A 230      41.891  44.699   8.843  1.00 25.92           C  
ANISOU 1904  CB  GLN A 230     4227   2724   2898   -284    212   -485       C  
ATOM   1905  CG  GLN A 230      41.768  45.690   7.685  1.00 32.34           C  
ANISOU 1905  CG  GLN A 230     5222   3547   3520   -365    201   -387       C  
ATOM   1906  CD  GLN A 230      41.139  46.990   8.158  1.00 35.04           C  
ANISOU 1906  CD  GLN A 230     5813   3677   3825   -332    110   -269       C  
ATOM   1907  OE1 GLN A 230      41.442  47.473   9.242  1.00 40.08           O  
ANISOU 1907  OE1 GLN A 230     6512   4187   4528   -349     80   -254       O  
ATOM   1908  NE2 GLN A 230      40.248  47.540   7.361  1.00 38.95           N  
ANISOU 1908  NE2 GLN A 230     6457   4132   4210   -260     47   -200       N  
ATOM   1909  N   VAL A 231      39.994  42.032   8.462  1.00 33.90           N  
ANISOU 1909  N   VAL A 231     4912   3796   4171     15    121   -676       N  
ATOM   1910  CA  VAL A 231      39.275  41.145   7.545  1.00 28.49           C  
ANISOU 1910  CA  VAL A 231     4144   3159   3522     85     48   -770       C  
ATOM   1911  C   VAL A 231      37.771  41.343   7.686  1.00 29.22           C  
ANISOU 1911  C   VAL A 231     4257   3179   3668    192    -45   -692       C  
ATOM   1912  O   VAL A 231      37.041  41.442   6.691  1.00 30.53           O  
ANISOU 1912  O   VAL A 231     4464   3383   3753    234   -123   -713       O  
ATOM   1913  CB  VAL A 231      39.661  39.679   7.794  1.00 30.78           C  
ANISOU 1913  CB  VAL A 231     4242   3453   4000    109     32   -899       C  
ATOM   1914  CG1 VAL A 231      38.933  38.769   6.805  1.00 32.50           C  
ANISOU 1914  CG1 VAL A 231     4396   3685   4266    174    -86  -1024       C  
ATOM   1915  CG2 VAL A 231      41.164  39.484   7.708  1.00 28.18           C  
ANISOU 1915  CG2 VAL A 231     3863   3227   3617     39    125   -984       C  
ATOM   1916  N   LEU A 232      37.279  41.398   8.927  1.00 24.23           N  
ANISOU 1916  N   LEU A 232     3580   2468   3157    251    -38   -598       N  
ATOM   1917  CA  LEU A 232      35.841  41.547   9.098  1.00 31.87           C  
ANISOU 1917  CA  LEU A 232     4516   3417   4176    369   -110   -515       C  
ATOM   1918  C   LEU A 232      35.373  42.978   8.818  1.00 34.31           C  
ANISOU 1918  C   LEU A 232     5032   3705   4299    435   -129   -435       C  
ATOM   1919  O   LEU A 232      34.296  43.169   8.246  1.00 37.13           O  
ANISOU 1919  O   LEU A 232     5391   4088   4630    526   -215   -409       O  
ATOM   1920  CB  LEU A 232      35.420  41.111  10.499  1.00 33.37           C  
ANISOU 1920  CB  LEU A 232     4569   3581   4528    432    -79   -423       C  
ATOM   1921  CG  LEU A 232      35.648  39.634  10.853  1.00 41.02           C  
ANISOU 1921  CG  LEU A 232     5334   4534   5718    379    -92   -457       C  
ATOM   1922  CD1 LEU A 232      34.952  39.267  12.175  1.00 34.82           C  
ANISOU 1922  CD1 LEU A 232     4406   3753   5072    447    -62   -303       C  
ATOM   1923  CD2 LEU A 232      35.199  38.688   9.701  1.00 37.43           C  
ANISOU 1923  CD2 LEU A 232     4783   4076   5364    343   -214   -565       C  
ATOM   1924  N   ILE A 233      36.156  43.989   9.207  1.00 32.54           N  
ANISOU 1924  N   ILE A 233     4988   3419   3958    392    -75   -395       N  
ATOM   1925  CA  ILE A 233      35.807  45.366   8.852  1.00 28.23           C  
ANISOU 1925  CA  ILE A 233     4679   2802   3244    444   -123   -320       C  
ATOM   1926  C   ILE A 233      35.664  45.497   7.348  1.00 31.22           C  
ANISOU 1926  C   ILE A 233     5130   3240   3492    402   -176   -332       C  
ATOM   1927  O   ILE A 233      34.707  46.107   6.856  1.00 31.30           O  
ANISOU 1927  O   ILE A 233     5237   3233   3421    519   -265   -277       O  
ATOM   1928  CB  ILE A 233      36.848  46.351   9.400  1.00 26.26           C  
ANISOU 1928  CB  ILE A 233     4619   2444   2915    349    -86   -285       C  
ATOM   1929  CG1 ILE A 233      36.733  46.443  10.925  1.00 30.08           C  
ANISOU 1929  CG1 ILE A 233     5080   2871   3479    458    -69   -277       C  
ATOM   1930  CG2 ILE A 233      36.665  47.754   8.780  1.00 30.47           C  
ANISOU 1930  CG2 ILE A 233     5435   2861   3282    356   -162   -199       C  
ATOM   1931  CD1 ILE A 233      37.949  47.002  11.551  1.00 32.54           C  
ANISOU 1931  CD1 ILE A 233     5507   3097   3761    332    -49   -288       C  
ATOM   1932  N   ASP A 234      36.603  44.911   6.587  1.00 29.42           N  
ANISOU 1932  N   ASP A 234     4850   3107   3223    260   -125   -408       N  
ATOM   1933  CA  ASP A 234      36.542  45.075   5.139  1.00 33.79           C  
ANISOU 1933  CA  ASP A 234     5486   3754   3598    235   -165   -418       C  
ATOM   1934  C   ASP A 234      35.333  44.350   4.585  1.00 37.10           C  
ANISOU 1934  C   ASP A 234     5788   4233   4075    365   -282   -487       C  
ATOM   1935  O   ASP A 234      34.629  44.876   3.719  1.00 37.04           O  
ANISOU 1935  O   ASP A 234     5891   4254   3930    436   -374   -445       O  
ATOM   1936  CB  ASP A 234      37.807  44.552   4.453  1.00 38.26           C  
ANISOU 1936  CB  ASP A 234     5995   4461   4080     92    -70   -500       C  
ATOM   1937  CG  ASP A 234      39.047  45.392   4.746  1.00 52.71           C  
ANISOU 1937  CG  ASP A 234     7929   6270   5830    -77     34   -405       C  
ATOM   1938  OD1 ASP A 234      38.917  46.493   5.335  1.00 51.47           O  
ANISOU 1938  OD1 ASP A 234     7944   5952   5662    -93      5   -279       O  
ATOM   1939  OD2 ASP A 234      40.165  44.929   4.389  1.00 54.84           O  
ANISOU 1939  OD2 ASP A 234     8098   6687   6052   -189    134   -466       O  
ATOM   1940  N   ARG A 235      35.088  43.131   5.073  1.00 35.06           N  
ANISOU 1940  N   ARG A 235     5306   3986   4029    386   -299   -582       N  
ATOM   1941  CA  ARG A 235      33.939  42.360   4.612  1.00 31.44           C  
ANISOU 1941  CA  ARG A 235     4708   3565   3673    472   -438   -645       C  
ATOM   1942  C   ARG A 235      32.639  43.070   4.950  1.00 36.39           C  
ANISOU 1942  C   ARG A 235     5348   4160   4317    609   -514   -523       C  
ATOM   1943  O   ARG A 235      31.738  43.174   4.113  1.00 38.11           O  
ANISOU 1943  O   ARG A 235     5571   4435   4475    690   -644   -531       O  
ATOM   1944  CB  ARG A 235      33.966  40.965   5.235  1.00 33.03           C  
ANISOU 1944  CB  ARG A 235     4676   3736   4138    439   -451   -731       C  
ATOM   1945  CG  ARG A 235      32.939  40.024   4.700  1.00 38.24           C  
ANISOU 1945  CG  ARG A 235     5179   4410   4940    475   -621   -811       C  
ATOM   1946  CD  ARG A 235      33.465  38.596   4.847  1.00 43.79           C  
ANISOU 1946  CD  ARG A 235     5732   5059   5847    405   -652   -948       C  
ATOM   1947  NE  ARG A 235      33.099  38.053   6.140  1.00 40.83           N  
ANISOU 1947  NE  ARG A 235     5187   4593   5732    383   -628   -833       N  
ATOM   1948  CZ  ARG A 235      33.549  36.907   6.637  1.00 40.33           C  
ANISOU 1948  CZ  ARG A 235     5002   4440   5882    323   -642   -884       C  
ATOM   1949  NH1 ARG A 235      34.425  36.171   5.955  1.00 31.97           N  
ANISOU 1949  NH1 ARG A 235     3972   3363   4811    302   -682  -1084       N  
ATOM   1950  NH2 ARG A 235      33.115  36.510   7.827  1.00 37.15           N  
ANISOU 1950  NH2 ARG A 235     4451   3976   5690    302   -615   -728       N  
ATOM   1951  N   ALA A 236      32.522  43.557   6.185  1.00 34.74           N  
ANISOU 1951  N   ALA A 236     5141   3882   4178    662   -441   -419       N  
ATOM   1952  CA  ALA A 236      31.379  44.385   6.552  1.00 34.35           C  
ANISOU 1952  CA  ALA A 236     5122   3824   4106    837   -495   -311       C  
ATOM   1953  C   ALA A 236      31.204  45.569   5.601  1.00 41.54           C  
ANISOU 1953  C   ALA A 236     6286   4710   4787    903   -570   -267       C  
ATOM   1954  O   ALA A 236      30.078  45.904   5.228  1.00 41.45           O  
ANISOU 1954  O   ALA A 236     6260   4742   4748   1056   -685   -228       O  
ATOM   1955  CB  ALA A 236      31.531  44.885   7.991  1.00 34.80           C  
ANISOU 1955  CB  ALA A 236     5203   3817   4201    906   -394   -234       C  
ATOM   1956  N   ASN A 237      32.302  46.228   5.217  1.00 36.59           N  
ANISOU 1956  N   ASN A 237     5884   4019   3999    786   -512   -252       N  
ATOM   1957  CA  ASN A 237      32.193  47.375   4.313  1.00 33.31           C  
ANISOU 1957  CA  ASN A 237     5732   3560   3365    824   -586   -167       C  
ATOM   1958  C   ASN A 237      31.736  46.953   2.932  1.00 40.87           C  
ANISOU 1958  C   ASN A 237     6658   4654   4215    838   -691   -215       C  
ATOM   1959  O   ASN A 237      30.914  47.632   2.311  1.00 47.04           O  
ANISOU 1959  O   ASN A 237     7557   5438   4878    973   -815   -148       O  
ATOM   1960  CB  ASN A 237      33.527  48.101   4.201  1.00 32.70           C  
ANISOU 1960  CB  ASN A 237     5872   3397   3157    645   -497   -105       C  
ATOM   1961  CG  ASN A 237      33.806  48.958   5.401  1.00 40.76           C  
ANISOU 1961  CG  ASN A 237     7023   4235   4228    667   -467    -44       C  
ATOM   1962  OD1 ASN A 237      32.878  49.368   6.097  1.00 42.45           O  
ANISOU 1962  OD1 ASN A 237     7252   4381   4495    872   -530    -25       O  
ATOM   1963  ND2 ASN A 237      35.081  49.236   5.659  1.00 43.52           N  
ANISOU 1963  ND2 ASN A 237     7460   4520   4557    470   -381    -22       N  
ATOM   1964  N   ARG A 238      32.291  45.858   2.417  1.00 42.99           N  
ANISOU 1964  N   ARG A 238     6788   5039   4509    721   -658   -344       N  
ATOM   1965  CA  ARG A 238      31.797  45.305   1.166  1.00 44.51           C  
ANISOU 1965  CA  ARG A 238     6934   5371   4607    760   -784   -438       C  
ATOM   1966  C   ARG A 238      30.310  45.015   1.251  1.00 43.49           C  
ANISOU 1966  C   ARG A 238     6646   5263   4617    917   -948   -451       C  
ATOM   1967  O   ARG A 238      29.575  45.227   0.286  1.00 44.99           O  
ANISOU 1967  O   ARG A 238     6884   5532   4678   1015  -1100   -455       O  
ATOM   1968  CB  ARG A 238      32.560  44.033   0.832  1.00 45.79           C  
ANISOU 1968  CB  ARG A 238     6949   5629   4822    651   -741   -618       C  
ATOM   1969  CG  ARG A 238      33.559  44.188  -0.264  1.00 54.92           C  
ANISOU 1969  CG  ARG A 238     8244   6917   5705    573   -676   -650       C  
ATOM   1970  CD  ARG A 238      34.840  43.505   0.107  1.00 55.17           C  
ANISOU 1970  CD  ARG A 238     8180   6982   5799    448   -522   -745       C  
ATOM   1971  NE  ARG A 238      34.667  42.119   0.540  1.00 52.10           N  
ANISOU 1971  NE  ARG A 238     7562   6566   5668    467   -576   -926       N  
ATOM   1972  CZ  ARG A 238      35.564  41.501   1.304  1.00 47.87           C  
ANISOU 1972  CZ  ARG A 238     6915   5993   5281    390   -464   -985       C  
ATOM   1973  NH1 ARG A 238      36.639  42.181   1.686  1.00 38.33           N  
ANISOU 1973  NH1 ARG A 238     5786   4793   3983    288   -299   -887       N  
ATOM   1974  NH2 ARG A 238      35.395  40.233   1.687  1.00 44.73           N  
ANISOU 1974  NH2 ARG A 238     6331   5538   5127    408   -535  -1129       N  
ATOM   1975  N   GLN A 239      29.850  44.520   2.397  1.00 45.45           N  
ANISOU 1975  N   GLN A 239     6685   5465   5120    941   -922   -445       N  
ATOM   1976  CA  GLN A 239      28.447  44.145   2.510  1.00 51.29           C  
ANISOU 1976  CA  GLN A 239     7208   6265   6016   1062  -1065   -438       C  
ATOM   1977  C   GLN A 239      27.546  45.369   2.518  1.00 53.59           C  
ANISOU 1977  C   GLN A 239     7614   6554   6193   1264  -1133   -309       C  
ATOM   1978  O   GLN A 239      26.431  45.314   1.992  1.00 60.52           O  
ANISOU 1978  O   GLN A 239     8383   7528   7085   1384  -1299   -310       O  
ATOM   1979  CB  GLN A 239      28.219  43.305   3.768  1.00 53.31           C  
ANISOU 1979  CB  GLN A 239     7195   6500   6560   1022   -995   -420       C  
ATOM   1980  CG  GLN A 239      28.854  41.915   3.737  1.00 62.70           C  
ANISOU 1980  CG  GLN A 239     8237   7668   7917    851   -988   -552       C  
ATOM   1981  CD  GLN A 239      28.582  41.130   5.020  1.00 71.70           C  
ANISOU 1981  CD  GLN A 239     9126   8777   9341    808   -926   -482       C  
ATOM   1982  OE1 GLN A 239      27.448  40.729   5.284  1.00 75.25           O  
ANISOU 1982  OE1 GLN A 239     9342   9285   9966    844  -1017   -415       O  
ATOM   1983  NE2 GLN A 239      29.621  40.924   5.830  1.00 72.62           N  
ANISOU 1983  NE2 GLN A 239     9277   8819   9496    726   -771   -477       N  
ATOM   1984  N   LYS A 240      28.006  46.478   3.101  1.00 51.32           N  
ANISOU 1984  N   LYS A 240     7550   6151   5800   1315  -1032   -206       N  
ATOM   1985  CA  LYS A 240      27.193  47.692   3.118  1.00 55.21           C  
ANISOU 1985  CA  LYS A 240     8191   6603   6182   1542  -1117    -99       C  
ATOM   1986  C   LYS A 240      27.049  48.288   1.721  1.00 64.71           C  
ANISOU 1986  C   LYS A 240     9609   7825   7151   1583  -1259    -71       C  
ATOM   1987  O   LYS A 240      25.936  48.603   1.283  1.00 72.38           O  
ANISOU 1987  O   LYS A 240    10545   8868   8087   1776  -1420    -41       O  
ATOM   1988  CB  LYS A 240      27.789  48.720   4.084  1.00 55.95           C  
ANISOU 1988  CB  LYS A 240     8507   6523   6229   1583  -1007    -22       C  
ATOM   1989  CG  LYS A 240      27.852  48.255   5.531  1.00 58.71           C  
ANISOU 1989  CG  LYS A 240     8666   6879   6764   1591   -875    -38       C  
ATOM   1990  CD  LYS A 240      28.104  49.417   6.494  1.00 67.33           C  
ANISOU 1990  CD  LYS A 240     9986   7809   7787   1723   -829     14       C  
ATOM   1991  CE  LYS A 240      29.563  49.853   6.491  1.00 66.05           C  
ANISOU 1991  CE  LYS A 240    10081   7473   7542   1507   -756     15       C  
ATOM   1992  NZ  LYS A 240      29.928  50.596   7.736  1.00 64.37           N  
ANISOU 1992  NZ  LYS A 240    10013   7110   7333   1589   -707     20       N  
ATOM   1993  N   LYS A 241      28.164  48.463   1.004  1.00 68.95           N  
ANISOU 1993  N   LYS A 241    10360   8324   7514   1412  -1201    -66       N  
ATOM   1994  CA  LYS A 241      28.084  49.013  -0.348  1.00 72.36           C  
ANISOU 1994  CA  LYS A 241    11005   8803   7686   1445  -1321    -11       C  
ATOM   1995  C   LYS A 241      27.159  48.185  -1.234  1.00 75.25           C  
ANISOU 1995  C   LYS A 241    11176   9360   8055   1522  -1496   -123       C  
ATOM   1996  O   LYS A 241      26.521  48.724  -2.143  1.00 82.05           O  
ANISOU 1996  O   LYS A 241    12161  10277   8738   1660  -1659    -69       O  
ATOM   1997  CB  LYS A 241      29.480  49.106  -0.970  1.00 70.45           C  
ANISOU 1997  CB  LYS A 241    10948   8563   7258   1222  -1197     16       C  
ATOM   1998  N   SER A 242      27.053  46.883  -0.973  1.00 74.10           N  
ANISOU 1998  N   SER A 242    10735   9301   8119   1438  -1489   -277       N  
ATOM   1999  CA  SER A 242      26.168  46.043  -1.772  1.00 73.53           C  
ANISOU 1999  CA  SER A 242    10470   9381   8087   1488  -1693   -403       C  
ATOM   2000  C   SER A 242      24.704  46.377  -1.512  1.00 75.52           C  
ANISOU 2000  C   SER A 242    10567   9678   8449   1697  -1852   -336       C  
ATOM   2001  O   SER A 242      23.878  46.327  -2.432  1.00 80.13           O  
ANISOU 2001  O   SER A 242    11113  10382   8951   1803  -2068   -375       O  
ATOM   2002  CB  SER A 242      26.448  44.567  -1.482  1.00 71.92           C  
ANISOU 2002  CB  SER A 242    10004   9202   8119   1330  -1669   -576       C  
ATOM   2003  N   ARG A 243      24.360  46.723  -0.269  1.00 75.04           N  
ANISOU 2003  N   ARG A 243    10405   9550   8557   1777  -1752   -242       N  
ATOM   2004  CA  ARG A 243      22.978  47.080   0.044  1.00 77.30           C  
ANISOU 2004  CA  ARG A 243    10512   9923   8935   2007  -1877   -173       C  
ATOM   2005  C   ARG A 243      22.641  48.480  -0.461  1.00 78.65           C  
ANISOU 2005  C   ARG A 243    10977  10045   8861   2238  -1975    -60       C  
ATOM   2006  O   ARG A 243      21.572  48.694  -1.046  1.00 79.91           O  
ANISOU 2006  O   ARG A 243    11058  10325   8981   2425  -2177    -46       O  
ATOM   2007  CB  ARG A 243      22.727  46.968   1.553  1.00 72.57           C  
ANISOU 2007  CB  ARG A 243     9699   9313   8560   2048  -1723   -112       C  
ATOM   2008  CG  ARG A 243      22.767  45.536   2.091  1.00 67.10           C  
ANISOU 2008  CG  ARG A 243     8668   8679   8148   1843  -1668   -179       C  
ATOM   2009  N   LEU A 244      23.545  49.444  -0.248  1.00 78.29           N  
ANISOU 2009  N   LEU A 244    11274   9811   8660   2224  -1854     27       N  
ATOM   2010  CA  LEU A 244      23.334  50.793  -0.763  1.00 79.47           C  
ANISOU 2010  CA  LEU A 244    11755   9855   8584   2418  -1964    154       C  
ATOM   2011  C   LEU A 244      23.203  50.798  -2.282  1.00 90.62           C  
ANISOU 2011  C   LEU A 244    13294  11369   9768   2415  -2140    157       C  
ATOM   2012  O   LEU A 244      22.367  51.526  -2.833  1.00 95.20           O  
ANISOU 2012  O   LEU A 244    13977  11971  10225   2650  -2329    234       O  
ATOM   2013  CB  LEU A 244      24.479  51.702  -0.314  1.00 74.34           C  
ANISOU 2013  CB  LEU A 244    11452   8955   7837   2324  -1818    250       C  
ATOM   2014  N   GLU A 245      23.999  49.979  -2.978  1.00 97.20           N  
ANISOU 2014  N   GLU A 245    14119  12283  10528   2180  -2091     65       N  
ATOM   2015  CA  GLU A 245      23.833  49.739  -4.408  1.00103.00           C  
ANISOU 2015  CA  GLU A 245    14921  13177  11037   2187  -2260     22       C  
ATOM   2016  C   GLU A 245      22.724  48.725  -4.711  1.00105.86           C  
ANISOU 2016  C   GLU A 245    14933  13736  11553   2257  -2462   -139       C  
ATOM   2017  O   GLU A 245      22.834  47.962  -5.683  1.00110.52           O  
ANISOU 2017  O   GLU A 245    15486  14468  12040   2179  -2569   -277       O  
ATOM   2018  CB  GLU A 245      25.159  49.269  -5.015  1.00100.64           C  
ANISOU 2018  CB  GLU A 245    14748  12918  10573   1940  -2119    -33       C  
ATOM   2019  N   HIS A 246      21.671  48.676  -3.897  1.00101.68           N  
ANISOU 2019  N   HIS A 246    14135  13231  11269   2401  -2521   -128       N  
ATOM   2020  CA  HIS A 246      20.536  47.793  -4.150  1.00 98.77           C  
ANISOU 2020  CA  HIS A 246    13401  13050  11076   2448  -2733   -244       C  
ATOM   2021  C   HIS A 246      19.205  48.549  -4.076  1.00100.67           C  
ANISOU 2021  C   HIS A 246    13540  13376  11333   2753  -2908   -144       C  
ATOM   2022  O   HIS A 246      19.168  49.781  -3.973  1.00 97.29           O  
ANISOU 2022  O   HIS A 246    13375  12843  10746   2955  -2892      0       O  
ATOM   2023  CB  HIS A 246      20.519  46.624  -3.163  1.00 92.26           C  
ANISOU 2023  CB  HIS A 246    12213  12235  10606   2269  -2626   -332       C  
TER    2024      HIS A 246                                                      
ATOM   2025  N   ASP B  38      25.537 -11.694 -23.501  1.00 82.43           N  
ANISOU 2025  N   ASP B  38    12098  10703   8520  -1370  -3192   -947       N  
ATOM   2026  CA  ASP B  38      26.362 -12.767 -24.048  1.00 88.25           C  
ANISOU 2026  CA  ASP B  38    12973  11479   9079  -1392  -3049  -1147       C  
ATOM   2027  C   ASP B  38      27.798 -12.319 -24.358  1.00 97.85           C  
ANISOU 2027  C   ASP B  38    14346  12798  10035  -1371  -2817  -1191       C  
ATOM   2028  O   ASP B  38      28.678 -13.145 -24.592  1.00101.18           O  
ANISOU 2028  O   ASP B  38    14852  13252  10339  -1362  -2647  -1361       O  
ATOM   2029  CB  ASP B  38      25.722 -13.332 -25.315  1.00 82.10           C  
ANISOU 2029  CB  ASP B  38    12288  10720   8187  -1464  -3213  -1198       C  
ATOM   2030  N   VAL B  39      28.036 -11.008 -24.356  1.00 97.58           N  
ANISOU 2030  N   VAL B  39    14339  12810   9926  -1360  -2805  -1036       N  
ATOM   2031  CA  VAL B  39      29.328 -10.492 -24.804  1.00 94.27           C  
ANISOU 2031  CA  VAL B  39    14068  12494   9255  -1356  -2596  -1056       C  
ATOM   2032  C   VAL B  39      30.364 -10.550 -23.686  1.00 85.21           C  
ANISOU 2032  C   VAL B  39    12862  11344   8171  -1293  -2354  -1121       C  
ATOM   2033  O   VAL B  39      31.531 -10.882 -23.929  1.00 87.64           O  
ANISOU 2033  O   VAL B  39    13254  11720   8324  -1276  -2133  -1240       O  
ATOM   2034  CB  VAL B  39      29.159  -9.066 -25.357  1.00 93.13           C  
ANISOU 2034  CB  VAL B  39    13994  12393   8997  -1384  -2689   -856       C  
ATOM   2035  CG1 VAL B  39      27.799  -8.509 -24.967  1.00 94.95           C  
ANISOU 2035  CG1 VAL B  39    14086  12535   9455  -1379  -2944   -693       C  
ATOM   2036  CG2 VAL B  39      30.268  -8.159 -24.861  1.00 88.91           C  
ANISOU 2036  CG2 VAL B  39    13488  11905   8387  -1355  -2480   -802       C  
ATOM   2037  N   LEU B  40      29.959 -10.234 -22.452  1.00 70.05           N  
ANISOU 2037  N   LEU B  40    10787   9346   6483  -1253  -2390  -1047       N  
ATOM   2038  CA  LEU B  40      30.884 -10.310 -21.326  1.00 67.83           C  
ANISOU 2038  CA  LEU B  40    10413   9059   6299  -1175  -2143  -1099       C  
ATOM   2039  C   LEU B  40      31.594 -11.657 -21.278  1.00 68.63           C  
ANISOU 2039  C   LEU B  40    10559   9158   6360  -1163  -1999  -1314       C  
ATOM   2040  O   LEU B  40      32.798 -11.723 -21.002  1.00 68.71           O  
ANISOU 2040  O   LEU B  40    10590   9220   6297  -1119  -1757  -1392       O  
ATOM   2041  CB  LEU B  40      30.142 -10.054 -20.015  1.00 63.13           C  
ANISOU 2041  CB  LEU B  40     9563   8372   6051  -1090  -2156   -993       C  
ATOM   2042  CG  LEU B  40      30.978 -10.179 -18.740  1.00 62.52           C  
ANISOU 2042  CG  LEU B  40     9349   8284   6120   -990  -1894  -1032       C  
ATOM   2043  CD1 LEU B  40      32.223  -9.313 -18.788  1.00 64.60           C  
ANISOU 2043  CD1 LEU B  40     9691   8635   6218   -975  -1697  -1011       C  
ATOM   2044  CD2 LEU B  40      30.155  -9.835 -17.517  1.00 62.06           C  
ANISOU 2044  CD2 LEU B  40     9057   8146   6376   -916  -1918   -918       C  
ATOM   2045  N   ARG B  41      30.865 -12.738 -21.567  1.00 67.50           N  
ANISOU 2045  N   ARG B  41    10407   8952   6289  -1191  -2133  -1406       N  
ATOM   2046  CA  ARG B  41      31.448 -14.074 -21.510  1.00 63.62           C  
ANISOU 2046  CA  ARG B  41     9933   8435   5806  -1164  -1999  -1603       C  
ATOM   2047  C   ARG B  41      32.623 -14.195 -22.471  1.00 61.94           C  
ANISOU 2047  C   ARG B  41     9864   8334   5338  -1156  -1814  -1711       C  
ATOM   2048  O   ARG B  41      33.709 -14.637 -22.083  1.00 64.18           O  
ANISOU 2048  O   ARG B  41    10142   8634   5608  -1094  -1594  -1824       O  
ATOM   2049  CB  ARG B  41      30.373 -15.123 -21.813  1.00 66.20           C  
ANISOU 2049  CB  ARG B  41    10224   8673   6255  -1207  -2189  -1666       C  
ATOM   2050  CG  ARG B  41      30.659 -16.517 -21.258  1.00 65.68           C  
ANISOU 2050  CG  ARG B  41    10118   8518   6321  -1174  -2096  -1836       C  
ATOM   2051  N   LYS B  42      32.435 -13.772 -23.724  1.00 61.03           N  
ANISOU 2051  N   LYS B  42     9869   8296   5024  -1211  -1901  -1670       N  
ATOM   2052  CA  LYS B  42      33.517 -13.861 -24.703  1.00 66.55           C  
ANISOU 2052  CA  LYS B  42    10702   9104   5480  -1201  -1733  -1765       C  
ATOM   2053  C   LYS B  42      34.685 -12.946 -24.341  1.00 65.73           C  
ANISOU 2053  C   LYS B  42    10600   9077   5299  -1160  -1512  -1705       C  
ATOM   2054  O   LYS B  42      35.846 -13.290 -24.602  1.00 63.76           O  
ANISOU 2054  O   LYS B  42    10389   8889   4947  -1113  -1301  -1818       O  
ATOM   2055  CB  LYS B  42      32.996 -13.542 -26.108  1.00 56.08           C  
ANISOU 2055  CB  LYS B  42     9513   7843   3953  -1276  -1887  -1717       C  
ATOM   2056  N   LEU B  43      34.413 -11.791 -23.735  1.00 63.23           N  
ANISOU 2056  N   LEU B  43    10231   8752   5041  -1174  -1559  -1531       N  
ATOM   2057  CA  LEU B  43      35.511 -10.923 -23.313  1.00 66.14           C  
ANISOU 2057  CA  LEU B  43    10590   9186   5356  -1144  -1349  -1476       C  
ATOM   2058  C   LEU B  43      36.303 -11.562 -22.181  1.00 60.33           C  
ANISOU 2058  C   LEU B  43     9739   8418   4766  -1062  -1152  -1590       C  
ATOM   2059  O   LEU B  43      37.538 -11.578 -22.207  1.00 62.62           O  
ANISOU 2059  O   LEU B  43    10032   8774   4985  -1015   -926  -1655       O  
ATOM   2060  CB  LEU B  43      34.978  -9.550 -22.890  1.00 64.73           C  
ANISOU 2060  CB  LEU B  43    10383   8992   5221  -1180  -1460  -1268       C  
ATOM   2061  CG  LEU B  43      34.425  -8.683 -24.025  1.00 61.54           C  
ANISOU 2061  CG  LEU B  43    10099   8628   4656  -1254  -1624  -1124       C  
ATOM   2062  CD1 LEU B  43      33.931  -7.349 -23.516  1.00 55.61           C  
ANISOU 2062  CD1 LEU B  43     9309   7842   3979  -1273  -1735   -919       C  
ATOM   2063  CD2 LEU B  43      35.493  -8.484 -25.062  1.00 62.25           C  
ANISOU 2063  CD2 LEU B  43    10322   8831   4498  -1276  -1454  -1158       C  
ATOM   2064  N   ALA B  44      35.599 -12.103 -21.185  1.00 59.00           N  
ANISOU 2064  N   ALA B  44     9462   8144   4811  -1041  -1242  -1610       N  
ATOM   2065  CA  ALA B  44      36.244 -12.696 -20.017  1.00 56.70           C  
ANISOU 2065  CA  ALA B  44     9057   7811   4675   -964  -1073  -1701       C  
ATOM   2066  C   ALA B  44      37.063 -13.933 -20.379  1.00 56.83           C  
ANISOU 2066  C   ALA B  44     9101   7833   4659   -906   -930  -1893       C  
ATOM   2067  O   ALA B  44      38.112 -14.191 -19.776  1.00 52.38           O  
ANISOU 2067  O   ALA B  44     8472   7285   4146   -828   -724  -1961       O  
ATOM   2068  CB  ALA B  44      35.183 -13.046 -18.980  1.00 53.83           C  
ANISOU 2068  CB  ALA B  44     8509   7325   4620   -915  -1192  -1634       C  
ATOM   2069  N   GLU B  45      36.597 -14.717 -21.354  1.00 66.14           N  
ANISOU 2069  N   GLU B  45    10366   8996   5770   -936  -1043  -1980       N  
ATOM   2070  CA  GLU B  45      37.342 -15.902 -21.770  1.00 67.09           C  
ANISOU 2070  CA  GLU B  45    10519   9110   5861   -873   -924  -2167       C  
ATOM   2071  C   GLU B  45      38.712 -15.536 -22.336  1.00 58.89           C  
ANISOU 2071  C   GLU B  45     9533   8185   4656   -823   -708  -2194       C  
ATOM   2072  O   GLU B  45      39.643 -16.348 -22.282  1.00 55.03           O  
ANISOU 2072  O   GLU B  45     9033   7685   4191   -735   -553  -2324       O  
ATOM   2073  CB  GLU B  45      36.524 -16.697 -22.791  1.00 68.28           C  
ANISOU 2073  CB  GLU B  45    10760   9233   5952   -930  -1098  -2254       C  
ATOM   2074  CG  GLU B  45      35.321 -17.417 -22.198  1.00 72.33           C  
ANISOU 2074  CG  GLU B  45    11202   9610   6672   -969  -1285  -2264       C  
ATOM   2075  CD  GLU B  45      34.271 -17.782 -23.242  1.00 85.49           C  
ANISOU 2075  CD  GLU B  45    12944  11263   8275  -1056  -1504  -2282       C  
ATOM   2076  OE1 GLU B  45      34.610 -17.871 -24.446  1.00 88.89           O  
ANISOU 2076  OE1 GLU B  45    13496  11780   8499  -1071  -1486  -2353       O  
ATOM   2077  OE2 GLU B  45      33.096 -17.970 -22.854  1.00 88.83           O  
ANISOU 2077  OE2 GLU B  45    13301  11591   8861  -1108  -1698  -2221       O  
ATOM   2078  N   GLN B  46      38.864 -14.323 -22.859  1.00 53.21           N  
ANISOU 2078  N   GLN B  46     8871   7564   3784   -876   -698  -2063       N  
ATOM   2079  CA  GLN B  46      40.152 -13.899 -23.394  1.00 64.45           C  
ANISOU 2079  CA  GLN B  46    10337   9093   5058   -845   -492  -2070       C  
ATOM   2080  C   GLN B  46      41.152 -13.494 -22.318  1.00 67.31           C  
ANISOU 2080  C   GLN B  46    10573   9465   5538   -776   -294  -2035       C  
ATOM   2081  O   GLN B  46      42.301 -13.195 -22.655  1.00 72.08           O  
ANISOU 2081  O   GLN B  46    11186  10149   6054   -748   -112  -2042       O  
ATOM   2082  CB  GLN B  46      39.962 -12.732 -24.369  1.00 70.40           C  
ANISOU 2082  CB  GLN B  46    11203   9940   5604   -939   -552  -1932       C  
ATOM   2083  N   VAL B  47      40.757 -13.480 -21.046  1.00 60.74           N  
ANISOU 2083  N   VAL B  47     9619   8558   4902   -754   -324  -1999       N  
ATOM   2084  CA  VAL B  47      41.613 -13.033 -19.954  1.00 56.55           C  
ANISOU 2084  CA  VAL B  47     8956   8041   4489   -695   -155  -1959       C  
ATOM   2085  C   VAL B  47      41.981 -14.242 -19.111  1.00 59.27           C  
ANISOU 2085  C   VAL B  47     9204   8302   5014   -594    -77  -2082       C  
ATOM   2086  O   VAL B  47      41.099 -14.911 -18.555  1.00 66.93           O  
ANISOU 2086  O   VAL B  47    10141   9176   6115   -596   -198  -2119       O  
ATOM   2087  CB  VAL B  47      40.921 -11.970 -19.089  1.00 52.33           C  
ANISOU 2087  CB  VAL B  47     8357   7495   4032   -748   -239  -1814       C  
ATOM   2088  CG1 VAL B  47      41.912 -11.396 -18.091  1.00 42.28           C  
ANISOU 2088  CG1 VAL B  47     6953   6257   2853   -693    -55  -1776       C  
ATOM   2089  CG2 VAL B  47      40.306 -10.883 -19.968  1.00 51.84           C  
ANISOU 2089  CG2 VAL B  47     8412   7480   3805   -853   -371  -1679       C  
ATOM   2090  N   ASP B  48      43.282 -14.507 -18.986  1.00 51.81           N  
ANISOU 2090  N   ASP B  48     8208   7388   4089   -510    119  -2135       N  
ATOM   2091  CA  ASP B  48      43.711 -15.719 -18.298  1.00 57.18           C  
ANISOU 2091  CA  ASP B  48     8812   7981   4933   -408    190  -2245       C  
ATOM   2092  C   ASP B  48      43.370 -15.669 -16.811  1.00 53.18           C  
ANISOU 2092  C   ASP B  48     8156   7416   4634   -380    176  -2197       C  
ATOM   2093  O   ASP B  48      42.833 -16.632 -16.250  1.00 55.98           O  
ANISOU 2093  O   ASP B  48     8474   7667   5129   -351    111  -2264       O  
ATOM   2094  CB  ASP B  48      45.207 -15.934 -18.521  1.00 67.50           C  
ANISOU 2094  CB  ASP B  48    10091   9339   6218   -328    394  -2294       C  
ATOM   2095  CG  ASP B  48      45.574 -16.002 -20.002  1.00 78.55           C  
ANISOU 2095  CG  ASP B  48    11633  10808   7403   -355    424  -2353       C  
ATOM   2096  OD1 ASP B  48      44.744 -16.487 -20.811  1.00 77.27           O  
ANISOU 2096  OD1 ASP B  48    11595  10617   7147   -397    286  -2415       O  
ATOM   2097  OD2 ASP B  48      46.689 -15.558 -20.354  1.00 83.20           O  
ANISOU 2097  OD2 ASP B  48    12205  11486   7920   -337    582  -2338       O  
ATOM   2098  N   ASP B  49      43.648 -14.547 -16.160  1.00 43.76           N  
ANISOU 2098  N   ASP B  49     6874   6287   3465   -391    235  -2084       N  
ATOM   2099  CA  ASP B  49      43.426 -14.411 -14.727  1.00 47.61           C  
ANISOU 2099  CA  ASP B  49     7211   6741   4139   -353    239  -2042       C  
ATOM   2100  C   ASP B  49      42.374 -13.338 -14.481  1.00 49.83           C  
ANISOU 2100  C   ASP B  49     7486   7037   4411   -435    110  -1920       C  
ATOM   2101  O   ASP B  49      42.552 -12.184 -14.887  1.00 53.04           O  
ANISOU 2101  O   ASP B  49     7937   7521   4695   -496    126  -1833       O  
ATOM   2102  CB  ASP B  49      44.740 -14.075 -14.014  1.00 54.71           C  
ANISOU 2102  CB  ASP B  49     7988   7688   5113   -273    416  -2010       C  
ATOM   2103  CG  ASP B  49      45.717 -15.241 -14.017  1.00 67.19           C  
ANISOU 2103  CG  ASP B  49     9539   9228   6761   -175    523  -2110       C  
ATOM   2104  OD1 ASP B  49      46.456 -15.407 -15.015  1.00 72.45           O  
ANISOU 2104  OD1 ASP B  49    10283   9935   7310   -171    599  -2157       O  
ATOM   2105  OD2 ASP B  49      45.725 -16.018 -13.036  1.00 68.19           O  
ANISOU 2105  OD2 ASP B  49     9568   9283   7059   -100    529  -2144       O  
ATOM   2106  N   ILE B  50      41.290 -13.710 -13.806  1.00 39.87           N  
ANISOU 2106  N   ILE B  50     6151   5668   3328   -412    -27  -1859       N  
ATOM   2107  CA  ILE B  50      40.271 -12.759 -13.387  1.00 36.83           C  
ANISOU 2107  CA  ILE B  50     5711   5257   3027   -440   -153  -1690       C  
ATOM   2108  C   ILE B  50      40.176 -12.838 -11.873  1.00 34.87           C  
ANISOU 2108  C   ILE B  50     5287   4953   3008   -353   -116  -1628       C  
ATOM   2109  O   ILE B  50      39.877 -13.910 -11.323  1.00 34.99           O  
ANISOU 2109  O   ILE B  50     5245   4887   3163   -304   -137  -1674       O  
ATOM   2110  CB  ILE B  50      38.912 -13.042 -14.040  1.00 43.41           C  
ANISOU 2110  CB  ILE B  50     6613   6023   3859   -506   -363  -1662       C  
ATOM   2111  CG1 ILE B  50      38.993 -12.874 -15.553  1.00 37.69           C  
ANISOU 2111  CG1 ILE B  50     6079   5364   2878   -600   -413  -1714       C  
ATOM   2112  CG2 ILE B  50      37.844 -12.154 -13.440  1.00 43.98           C  
ANISOU 2112  CG2 ILE B  50     6590   6055   4066   -512   -484  -1493       C  
ATOM   2113  CD1 ILE B  50      37.737 -13.265 -16.260  1.00 41.77           C  
ANISOU 2113  CD1 ILE B  50     6671   5819   3380   -669   -632  -1707       C  
ATOM   2114  N   VAL B  51      40.467 -11.722 -11.205  1.00 31.79           N  
ANISOU 2114  N   VAL B  51     4821   4607   2651   -336    -57  -1526       N  
ATOM   2115  CA  VAL B  51      40.405 -11.608  -9.750  1.00 34.83           C  
ANISOU 2115  CA  VAL B  51     5051   4957   3224   -259    -17  -1461       C  
ATOM   2116  C   VAL B  51      39.177 -10.779  -9.399  1.00 36.40           C  
ANISOU 2116  C   VAL B  51     5201   5113   3518   -280   -141  -1321       C  
ATOM   2117  O   VAL B  51      39.051  -9.631  -9.840  1.00 34.16           O  
ANISOU 2117  O   VAL B  51     4959   4863   3156   -328   -174  -1243       O  
ATOM   2118  CB  VAL B  51      41.664 -10.945  -9.165  1.00 36.10           C  
ANISOU 2118  CB  VAL B  51     5155   5198   3364   -221    142  -1462       C  
ATOM   2119  CG1 VAL B  51      41.612 -10.970  -7.642  1.00 33.45           C  
ANISOU 2119  CG1 VAL B  51     4673   4828   3208   -140    176  -1410       C  
ATOM   2120  CG2 VAL B  51      42.951 -11.599  -9.688  1.00 42.22           C  
ANISOU 2120  CG2 VAL B  51     5974   6032   4034   -205    274  -1600       C  
ATOM   2121  N   PHE B  52      38.280 -11.345  -8.605  1.00 32.81           N  
ANISOU 2121  N   PHE B  52     4653   4578   3236   -243   -206  -1284       N  
ATOM   2122  CA  PHE B  52      37.172 -10.585  -8.048  1.00 29.03           C  
ANISOU 2122  CA  PHE B  52     4091   4059   2880   -243   -293  -1158       C  
ATOM   2123  C   PHE B  52      37.468 -10.245  -6.598  1.00 28.88           C  
ANISOU 2123  C   PHE B  52     3945   4046   2982   -166   -188  -1113       C  
ATOM   2124  O   PHE B  52      37.931 -11.097  -5.835  1.00 31.44           O  
ANISOU 2124  O   PHE B  52     4216   4359   3370   -111   -110  -1161       O  
ATOM   2125  CB  PHE B  52      35.854 -11.354  -8.106  1.00 30.79           C  
ANISOU 2125  CB  PHE B  52     4279   4195   3224   -262   -435  -1135       C  
ATOM   2126  CG  PHE B  52      35.172 -11.301  -9.427  1.00 30.81           C  
ANISOU 2126  CG  PHE B  52     4389   4187   3132   -346   -590  -1135       C  
ATOM   2127  CD1 PHE B  52      35.801 -10.741 -10.530  1.00 38.13           C  
ANISOU 2127  CD1 PHE B  52     5454   5183   3852   -400   -586  -1163       C  
ATOM   2128  CD2 PHE B  52      33.897 -11.805  -9.574  1.00 35.61           C  
ANISOU 2128  CD2 PHE B  52     4958   4720   3853   -378   -744  -1103       C  
ATOM   2129  CE1 PHE B  52      35.160 -10.700 -11.768  1.00 38.87           C  
ANISOU 2129  CE1 PHE B  52     5660   5272   3835   -482   -742  -1158       C  
ATOM   2130  CE2 PHE B  52      33.263 -11.775 -10.805  1.00 41.91           C  
ANISOU 2130  CE2 PHE B  52     5856   5510   4557   -460   -907  -1104       C  
ATOM   2131  CZ  PHE B  52      33.898 -11.209 -11.903  1.00 37.46           C  
ANISOU 2131  CZ  PHE B  52     5445   5019   3770   -510   -910  -1130       C  
ATOM   2132  N   ILE B  53      37.150  -9.014  -6.208  1.00 28.68           N  
ANISOU 2132  N   ILE B  53     3876   4031   2991   -163   -196  -1020       N  
ATOM   2133  CA  ILE B  53      37.305  -8.563  -4.833  1.00 27.06           C  
ANISOU 2133  CA  ILE B  53     3559   3831   2891    -96   -108   -979       C  
ATOM   2134  C   ILE B  53      35.927  -8.259  -4.287  1.00 29.64           C  
ANISOU 2134  C   ILE B  53     3794   4096   3370    -81   -191   -887       C  
ATOM   2135  O   ILE B  53      35.206  -7.421  -4.853  1.00 30.71           O  
ANISOU 2135  O   ILE B  53     3948   4212   3509   -115   -287   -822       O  
ATOM   2136  CB  ILE B  53      38.191  -7.316  -4.719  1.00 26.56           C  
ANISOU 2136  CB  ILE B  53     3514   3828   2751    -98    -28   -964       C  
ATOM   2137  CG1 ILE B  53      39.570  -7.549  -5.305  1.00 28.54           C  
ANISOU 2137  CG1 ILE B  53     3838   4148   2856   -119     63  -1052       C  
ATOM   2138  CG2 ILE B  53      38.266  -6.891  -3.270  1.00 30.25           C  
ANISOU 2138  CG2 ILE B  53     3873   4297   3325    -31     48   -932       C  
ATOM   2139  CD1 ILE B  53      39.718  -7.123  -6.755  1.00 35.10           C  
ANISOU 2139  CD1 ILE B  53     4798   5009   3531   -202     18  -1056       C  
ATOM   2140  N   SER B  54      35.573  -8.885  -3.164  1.00 30.07           N  
ANISOU 2140  N   SER B  54     3749   4124   3554    -28   -149   -875       N  
ATOM   2141  CA  SER B  54      34.286  -8.572  -2.559  1.00 28.79           C  
ANISOU 2141  CA  SER B  54     3483   3912   3544    -11   -201   -790       C  
ATOM   2142  C   SER B  54      34.370  -8.691  -1.037  1.00 28.67           C  
ANISOU 2142  C   SER B  54     3367   3907   3619     58    -87   -772       C  
ATOM   2143  O   SER B  54      35.446  -8.861  -0.458  1.00 28.78           O  
ANISOU 2143  O   SER B  54     3394   3967   3573     93     15   -817       O  
ATOM   2144  CB  SER B  54      33.176  -9.457  -3.137  1.00 37.24           C  
ANISOU 2144  CB  SER B  54     4537   4918   4694    -54   -326   -775       C  
ATOM   2145  OG  SER B  54      31.896  -8.969  -2.732  1.00 35.81           O  
ANISOU 2145  OG  SER B  54     4247   4697   4663    -44   -385   -688       O  
ATOM   2146  N   GLY B  55      33.210  -8.628  -0.397  1.00 30.31           N  
ANISOU 2146  N   GLY B  55     3471   4076   3971     77   -109   -705       N  
ATOM   2147  CA  GLY B  55      33.091  -8.338   1.016  1.00 33.68           C  
ANISOU 2147  CA  GLY B  55     3806   4520   4472    139     -3   -673       C  
ATOM   2148  C   GLY B  55      32.371  -7.019   1.234  1.00 31.60           C  
ANISOU 2148  C   GLY B  55     3486   4246   4275    161    -15   -621       C  
ATOM   2149  O   GLY B  55      32.048  -6.292   0.300  1.00 36.34           O  
ANISOU 2149  O   GLY B  55     4120   4823   4863    131   -110   -600       O  
ATOM   2150  N   THR B  56      32.091  -6.731   2.499  1.00 28.11           N  
ANISOU 2150  N   THR B  56     2959   3818   3904    217     80   -598       N  
ATOM   2151  CA  THR B  56      31.251  -5.564   2.732  1.00 31.50           C  
ANISOU 2151  CA  THR B  56     3320   4222   4425    247     71   -556       C  
ATOM   2152  C   THR B  56      32.055  -4.275   2.872  1.00 31.71           C  
ANISOU 2152  C   THR B  56     3403   4273   4373    271    117   -586       C  
ATOM   2153  O   THR B  56      31.525  -3.204   2.586  1.00 39.73           O  
ANISOU 2153  O   THR B  56     4402   5248   5444    283     70   -556       O  
ATOM   2154  CB  THR B  56      30.335  -5.780   3.948  1.00 39.78           C  
ANISOU 2154  CB  THR B  56     4241   5269   5606    294    153   -518       C  
ATOM   2155  OG1 THR B  56      31.102  -6.067   5.112  1.00 41.35           O  
ANISOU 2155  OG1 THR B  56     4449   5524   5737    331    283   -548       O  
ATOM   2156  CG2 THR B  56      29.366  -6.946   3.698  1.00 48.81           C  
ANISOU 2156  CG2 THR B  56     5313   6373   6859    255     91   -473       C  
ATOM   2157  N  AASN B  57      33.323  -4.377   3.270  0.53 32.50           N  
ANISOU 2157  N  AASN B  57     3566   4429   4352    276    197   -642       N  
ATOM   2158  N  BASN B  57      33.310  -4.321   3.305  0.47 32.65           N  
ANISOU 2158  N  BASN B  57     3584   4448   4374    279    199   -642       N  
ATOM   2159  CA AASN B  57      34.209  -3.244   3.500  0.53 34.00           C  
ANISOU 2159  CA AASN B  57     3807   4644   4468    288    246   -679       C  
ATOM   2160  CA BASN B  57      34.114  -3.105   3.287  0.47 33.65           C  
ANISOU 2160  CA BASN B  57     3768   4590   4428    282    227   -672       C  
ATOM   2161  C  AASN B  57      35.536  -3.484   2.797  0.53 33.06           C  
ANISOU 2161  C  AASN B  57     3787   4569   4207    242    245   -727       C  
ATOM   2162  C  BASN B  57      35.552  -3.444   2.946  0.47 32.65           C  
ANISOU 2162  C  BASN B  57     3728   4519   4157    249    255   -729       C  
ATOM   2163  O  AASN B  57      35.875  -4.618   2.448  0.53 30.00           O  
ANISOU 2163  O  AASN B  57     3422   4200   3777    222    235   -748       O  
ATOM   2164  O  BASN B  57      35.982  -4.600   3.010  0.47 31.85           O  
ANISOU 2164  O  BASN B  57     3634   4448   4019    245    275   -754       O  
ATOM   2165  CB AASN B  57      34.467  -3.028   4.999  0.53 36.33           C  
ANISOU 2165  CB AASN B  57     4056   4980   4768    348    366   -707       C  
ATOM   2166  CB BASN B  57      34.073  -2.332   4.614  0.47 36.46           C  
ANISOU 2166  CB BASN B  57     4072   4959   4822    344    327   -689       C  
ATOM   2167  CG AASN B  57      33.700  -1.856   5.554  0.53 36.08           C  
ANISOU 2167  CG AASN B  57     3972   4910   4828    393    391   -694       C  
ATOM   2168  CG BASN B  57      34.985  -2.922   5.670  0.47 34.18           C  
ANISOU 2168  CG BASN B  57     3788   4742   4456    368    428   -736       C  
ATOM   2169  OD1AASN B  57      32.586  -2.003   6.058  0.53 33.76           O  
ANISOU 2169  OD1AASN B  57     3586   4592   4648    429    410   -659       O  
ATOM   2170  OD1BASN B  57      36.181  -2.633   5.725  0.47 33.93           O  
ANISOU 2170  OD1BASN B  57     3815   4753   4322    355    457   -786       O  
ATOM   2171  ND2AASN B  57      34.294  -0.671   5.451  0.53 41.03           N  
ANISOU 2171  ND2AASN B  57     4651   5525   5415    390    394   -724       N  
ATOM   2172  ND2BASN B  57      34.413  -3.736   6.531  0.47 39.83           N  
ANISOU 2172  ND2BASN B  57     4438   5472   5224    400    478   -713       N  
ATOM   2173  N   GLY B  58      36.289  -2.399   2.587  1.00 28.95           N  
ANISOU 2173  N   GLY B  58     3320   4058   3621    225    259   -749       N  
ATOM   2174  CA  GLY B  58      37.644  -2.508   2.115  1.00 22.47           C  
ANISOU 2174  CA  GLY B  58     2573   3292   2674    185    287   -799       C  
ATOM   2175  C   GLY B  58      37.814  -2.919   0.662  1.00 22.85           C  
ANISOU 2175  C   GLY B  58     2699   3338   2646    120    216   -796       C  
ATOM   2176  O   GLY B  58      38.957  -3.065   0.223  1.00 24.64           O  
ANISOU 2176  O   GLY B  58     2980   3616   2766     86    254   -844       O  
ATOM   2177  N   LYS B  59      36.729  -3.058  -0.110  1.00 25.20           N  
ANISOU 2177  N   LYS B  59     3002   3582   2992     99    114   -745       N  
ATOM   2178  CA  LYS B  59      36.853  -3.554  -1.482  1.00 27.78           C  
ANISOU 2178  CA  LYS B  59     3414   3912   3228     35     40   -750       C  
ATOM   2179  C   LYS B  59      37.735  -2.644  -2.322  1.00 27.00           C  
ANISOU 2179  C   LYS B  59     3411   3840   3007    -24     47   -753       C  
ATOM   2180  O   LYS B  59      38.598  -3.120  -3.064  1.00 28.10           O  
ANISOU 2180  O   LYS B  59     3622   4029   3025    -68     72   -802       O  
ATOM   2181  CB  LYS B  59      35.482  -3.682  -2.153  1.00 24.73           C  
ANISOU 2181  CB  LYS B  59     3017   3462   2917     17    -93   -687       C  
ATOM   2182  CG  LYS B  59      34.572  -4.732  -1.558  1.00 37.45           C  
ANISOU 2182  CG  LYS B  59     4536   5045   4648     51   -108   -680       C  
ATOM   2183  CD  LYS B  59      33.401  -5.018  -2.500  1.00 39.49           C  
ANISOU 2183  CD  LYS B  59     4795   5250   4960     11   -258   -632       C  
ATOM   2184  CE  LYS B  59      32.399  -3.875  -2.532  1.00 39.88           C  
ANISOU 2184  CE  LYS B  59     4792   5246   5114     27   -335   -550       C  
ATOM   2185  NZ  LYS B  59      31.656  -3.781  -1.247  1.00 35.99           N  
ANISOU 2185  NZ  LYS B  59     4159   4731   4783     98   -271   -526       N  
ATOM   2186  N   THR B  60      37.546  -1.332  -2.202  1.00 27.37           N  
ANISOU 2186  N   THR B  60     3460   3850   3089    -26     32   -703       N  
ATOM   2187  CA  THR B  60      38.212  -0.402  -3.104  1.00 35.03           C  
ANISOU 2187  CA  THR B  60     4528   4828   3954    -95     22   -680       C  
ATOM   2188  C   THR B  60      39.704  -0.317  -2.804  1.00 24.58           C  
ANISOU 2188  C   THR B  60     3220   3578   2542   -115    145   -749       C  
ATOM   2189  O   THR B  60      40.535  -0.451  -3.710  1.00 32.21           O  
ANISOU 2189  O   THR B  60     4263   4596   3379   -179    169   -771       O  
ATOM   2190  CB  THR B  60      37.543   0.979  -3.031  1.00 40.99           C  
ANISOU 2190  CB  THR B  60     5279   5501   4794    -88    -37   -601       C  
ATOM   2191  OG1 THR B  60      36.166   0.858  -3.407  1.00 39.71           O  
ANISOU 2191  OG1 THR B  60     5090   5275   4722    -70   -162   -535       O  
ATOM   2192  CG2 THR B  60      38.241   1.962  -3.981  1.00 41.87           C  
ANISOU 2192  CG2 THR B  60     5501   5611   4797   -171    -50   -561       C  
ATOM   2193  N   THR B  61      40.070  -0.124  -1.533  1.00 25.32           N  
ANISOU 2193  N   THR B  61     3237   3684   2700    -61    224   -786       N  
ATOM   2194  CA  THR B  61      41.487  -0.111  -1.193  1.00 26.37           C  
ANISOU 2194  CA  THR B  61     3367   3891   2763    -78    327   -853       C  
ATOM   2195  C   THR B  61      42.167  -1.422  -1.585  1.00 25.07           C  
ANISOU 2195  C   THR B  61     3209   3796   2520    -81    367   -917       C  
ATOM   2196  O   THR B  61      43.243  -1.415  -2.192  1.00 32.96           O  
ANISOU 2196  O   THR B  61     4247   4855   3421   -132    423   -954       O  
ATOM   2197  CB  THR B  61      41.668   0.182   0.296  1.00 33.27           C  
ANISOU 2197  CB  THR B  61     4159   4769   3714    -16    386   -886       C  
ATOM   2198  OG1 THR B  61      41.162   1.493   0.572  1.00 36.56           O  
ANISOU 2198  OG1 THR B  61     4580   5114   4199    -16    358   -844       O  
ATOM   2199  CG2 THR B  61      43.155   0.149   0.653  1.00 27.84           C  
ANISOU 2199  CG2 THR B  61     3455   4161   2961    -34    474   -955       C  
ATOM   2200  N   THR B  62      41.553  -2.562  -1.262  1.00 28.78           N  
ANISOU 2200  N   THR B  62     3639   4256   3040    -28    344   -930       N  
ATOM   2201  CA  THR B  62      42.125  -3.843  -1.697  1.00 28.13           C  
ANISOU 2201  CA  THR B  62     3571   4218   2898    -25    373   -995       C  
ATOM   2202  C   THR B  62      42.299  -3.847  -3.208  1.00 29.64           C  
ANISOU 2202  C   THR B  62     3865   4424   2971   -101    344   -999       C  
ATOM   2203  O   THR B  62      43.398  -4.084  -3.727  1.00 24.45           O  
ANISOU 2203  O   THR B  62     3239   3831   2218   -131    416  -1060       O  
ATOM   2204  CB  THR B  62      41.233  -5.014  -1.234  1.00 24.56           C  
ANISOU 2204  CB  THR B  62     3074   3726   2532     30    333   -992       C  
ATOM   2205  OG1 THR B  62      41.075  -4.979   0.184  1.00 26.59           O  
ANISOU 2205  OG1 THR B  62     3245   3980   2879     96    371   -980       O  
ATOM   2206  CG2 THR B  62      41.812  -6.417  -1.612  1.00 23.20           C  
ANISOU 2206  CG2 THR B  62     2917   3579   2319     43    360  -1066       C  
ATOM   2207  N   SER B  63      41.237  -3.495  -3.931  1.00 27.60           N  
ANISOU 2207  N   SER B  63     3661   4110   2715   -136    239   -933       N  
ATOM   2208  CA  SER B  63      41.301  -3.510  -5.390  1.00 30.75           C  
ANISOU 2208  CA  SER B  63     4174   4526   2982   -214    196   -930       C  
ATOM   2209  C   SER B  63      42.370  -2.571  -5.920  1.00 28.59           C  
ANISOU 2209  C   SER B  63     3959   4306   2597   -281    268   -926       C  
ATOM   2210  O   SER B  63      43.103  -2.909  -6.868  1.00 27.42           O  
ANISOU 2210  O   SER B  63     3886   4220   2314   -334    315   -974       O  
ATOM   2211  CB  SER B  63      39.943  -3.136  -5.973  1.00 31.64           C  
ANISOU 2211  CB  SER B  63     4327   4567   3128   -238     50   -842       C  
ATOM   2212  OG  SER B  63      39.998  -3.174  -7.374  1.00 42.41           O  
ANISOU 2212  OG  SER B  63     5814   5953   4345   -317     -2   -837       O  
ATOM   2213  N   ASN B  64      42.457  -1.380  -5.335  1.00 25.82           N  
ANISOU 2213  N   ASN B  64     3578   3931   2303   -285    281   -873       N  
ATOM   2214  CA  ASN B  64      43.390  -0.373  -5.833  1.00 37.31           C  
ANISOU 2214  CA  ASN B  64     5086   5421   3668   -363    341   -853       C  
ATOM   2215  C   ASN B  64      44.821  -0.786  -5.577  1.00 26.26           C  
ANISOU 2215  C   ASN B  64     3644   4114   2221   -365    478   -945       C  
ATOM   2216  O   ASN B  64      45.690  -0.597  -6.434  1.00 33.08           O  
ANISOU 2216  O   ASN B  64     4565   5040   2965   -440    545   -960       O  
ATOM   2217  CB  ASN B  64      43.120   0.974  -5.174  1.00 32.67           C  
ANISOU 2217  CB  ASN B  64     4472   4766   3175   -361    317   -783       C  
ATOM   2218  CG  ASN B  64      41.890   1.638  -5.730  1.00 35.36           C  
ANISOU 2218  CG  ASN B  64     4871   5017   3548   -377    184   -678       C  
ATOM   2219  OD1 ASN B  64      41.345   1.203  -6.738  1.00 35.44           O  
ANISOU 2219  OD1 ASN B  64     4955   5026   3484   -408    105   -648       O  
ATOM   2220  ND2 ASN B  64      41.461   2.704  -5.093  1.00 33.54           N  
ANISOU 2220  ND2 ASN B  64     4608   4708   3428   -354    153   -625       N  
ATOM   2221  N   LEU B  65      45.074  -1.388  -4.416  1.00 25.35           N  
ANISOU 2221  N   LEU B  65     3422   4012   2198   -283    520  -1005       N  
ATOM   2222  CA  LEU B  65      46.417  -1.864  -4.123  1.00 28.91           C  
ANISOU 2222  CA  LEU B  65     3814   4548   2622   -273    635  -1092       C  
ATOM   2223  C   LEU B  65      46.847  -2.923  -5.122  1.00 29.65           C  
ANISOU 2223  C   LEU B  65     3955   4696   2613   -286    677  -1160       C  
ATOM   2224  O   LEU B  65      47.987  -2.900  -5.601  1.00 31.54           O  
ANISOU 2224  O   LEU B  65     4194   5013   2775   -328    777  -1211       O  
ATOM   2225  CB  LEU B  65      46.485  -2.391  -2.694  1.00 24.35           C  
ANISOU 2225  CB  LEU B  65     3125   3968   2157   -177    649  -1130       C  
ATOM   2226  CG  LEU B  65      46.927  -1.368  -1.641  1.00 31.27           C  
ANISOU 2226  CG  LEU B  65     3939   4845   3096   -175    675  -1119       C  
ATOM   2227  CD1 LEU B  65      46.754  -1.988  -0.275  1.00 31.10           C  
ANISOU 2227  CD1 LEU B  65     3831   4821   3165    -80    670  -1145       C  
ATOM   2228  CD2 LEU B  65      48.396  -0.915  -1.847  1.00 28.78           C  
ANISOU 2228  CD2 LEU B  65     3598   4609   2729   -236    768  -1162       C  
ATOM   2229  N   ILE B  66      45.944  -3.856  -5.466  1.00 32.02           N  
ANISOU 2229  N   ILE B  66     4294   4955   2916   -254    603  -1168       N  
ATOM   2230  CA  ILE B  66      46.296  -4.878  -6.452  1.00 31.34           C  
ANISOU 2230  CA  ILE B  66     4267   4910   2730   -266    638  -1248       C  
ATOM   2231  C   ILE B  66      46.571  -4.228  -7.796  1.00 35.06           C  
ANISOU 2231  C   ILE B  66     4856   5425   3041   -372    658  -1226       C  
ATOM   2232  O   ILE B  66      47.601  -4.481  -8.433  1.00 34.48           O  
ANISOU 2232  O   ILE B  66     4804   5432   2866   -404    768  -1297       O  
ATOM   2233  CB  ILE B  66      45.184  -5.931  -6.571  1.00 26.72           C  
ANISOU 2233  CB  ILE B  66     3709   4258   2186   -224    538  -1258       C  
ATOM   2234  CG1 ILE B  66      45.008  -6.659  -5.255  1.00 28.70           C  
ANISOU 2234  CG1 ILE B  66     3848   4472   2586   -126    535  -1275       C  
ATOM   2235  CG2 ILE B  66      45.508  -6.907  -7.753  1.00 27.85           C  
ANISOU 2235  CG2 ILE B  66     3941   4435   2207   -248    565  -1352       C  
ATOM   2236  CD1 ILE B  66      43.679  -7.335  -5.094  1.00 26.55           C  
ANISOU 2236  CD1 ILE B  66     3578   4114   2394    -97    424  -1242       C  
ATOM   2237  N   GLY B  67      45.652  -3.365  -8.236  1.00 34.99           N  
ANISOU 2237  N   GLY B  67     4923   5363   3007   -426    554  -1121       N  
ATOM   2238  CA  GLY B  67      45.781  -2.759  -9.548  1.00 35.25           C  
ANISOU 2238  CA  GLY B  67     5088   5431   2875   -532    553  -1079       C  
ATOM   2239  C   GLY B  67      46.972  -1.832  -9.651  1.00 30.08           C  
ANISOU 2239  C   GLY B  67     4424   4842   2164   -599    676  -1066       C  
ATOM   2240  O   GLY B  67      47.659  -1.803 -10.673  1.00 31.33           O  
ANISOU 2240  O   GLY B  67     4662   5075   2166   -676    757  -1088       O  
ATOM   2241  N   HIS B  68      47.246  -1.078  -8.591  1.00 35.45           N  
ANISOU 2241  N   HIS B  68     5006   5497   2967   -577    697  -1034       N  
ATOM   2242  CA  HIS B  68      48.410  -0.196  -8.600  1.00 29.75           C  
ANISOU 2242  CA  HIS B  68     4260   4830   2214   -648    809  -1025       C  
ATOM   2243  C   HIS B  68      49.694  -1.006  -8.700  1.00 30.15           C  
ANISOU 2243  C   HIS B  68     4246   4989   2220   -637    958  -1144       C  
ATOM   2244  O   HIS B  68      50.598  -0.662  -9.467  1.00 36.11           O  
ANISOU 2244  O   HIS B  68     5034   5822   2866   -723   1066  -1152       O  
ATOM   2245  CB  HIS B  68      48.393   0.675  -7.337  1.00 28.80           C  
ANISOU 2245  CB  HIS B  68     4044   4652   2246   -618    788   -987       C  
ATOM   2246  CG  HIS B  68      49.678   1.394  -7.047  1.00 36.85           C  
ANISOU 2246  CG  HIS B  68     5000   5727   3276   -676    901  -1003       C  
ATOM   2247  ND1 HIS B  68      49.929   2.678  -7.483  1.00 37.23           N  
ANISOU 2247  ND1 HIS B  68     5104   5752   3288   -784    911   -917       N  
ATOM   2248  CD2 HIS B  68      50.760   1.029  -6.316  1.00 32.38           C  
ANISOU 2248  CD2 HIS B  68     4309   5229   2764   -642    996  -1092       C  
ATOM   2249  CE1 HIS B  68      51.120   3.061  -7.061  1.00 34.08           C  
ANISOU 2249  CE1 HIS B  68     4618   5409   2923   -823   1015   -956       C  
ATOM   2250  NE2 HIS B  68      51.643   2.080  -6.346  1.00 35.89           N  
ANISOU 2250  NE2 HIS B  68     4732   5698   3208   -736   1064  -1063       N  
ATOM   2251  N   THR B  69      49.794  -2.090  -7.924  1.00 33.07           N  
ANISOU 2251  N   THR B  69     4520   5363   2681   -529    969  -1234       N  
ATOM   2252  CA  THR B  69      51.018  -2.887  -7.913  1.00 29.75           C  
ANISOU 2252  CA  THR B  69     4013   4996   2293   -481   1070  -1309       C  
ATOM   2253  C   THR B  69      51.222  -3.593  -9.239  1.00 37.63           C  
ANISOU 2253  C   THR B  69     5101   6017   3178   -498   1103  -1337       C  
ATOM   2254  O   THR B  69      52.355  -3.727  -9.712  1.00 39.03           O  
ANISOU 2254  O   THR B  69     5243   6244   3341   -508   1201  -1360       O  
ATOM   2255  CB  THR B  69      50.989  -3.907  -6.776  1.00 32.08           C  
ANISOU 2255  CB  THR B  69     4198   5248   2743   -350   1032  -1351       C  
ATOM   2256  OG1 THR B  69      50.917  -3.221  -5.530  1.00 31.18           O  
ANISOU 2256  OG1 THR B  69     4001   5121   2726   -332   1009  -1327       O  
ATOM   2257  CG2 THR B  69      52.242  -4.775  -6.793  1.00 35.00           C  
ANISOU 2257  CG2 THR B  69     4484   5642   3172   -289   1105  -1400       C  
ATOM   2258  N   LEU B  70      50.142  -4.046  -9.865  1.00 40.33           N  
ANISOU 2258  N   LEU B  70     5559   6328   3436   -505   1020  -1343       N  
ATOM   2259  CA  LEU B  70      50.307  -4.679 -11.163  1.00 34.53           C  
ANISOU 2259  CA  LEU B  70     4924   5616   2578   -525   1046  -1376       C  
ATOM   2260  C   LEU B  70      50.737  -3.653 -12.213  1.00 40.28           C  
ANISOU 2260  C   LEU B  70     5747   6409   3150   -651   1107  -1315       C  
ATOM   2261  O   LEU B  70      51.682  -3.892 -12.971  1.00 40.38           O  
ANISOU 2261  O   LEU B  70     5763   6472   3106   -663   1208  -1343       O  
ATOM   2262  CB  LEU B  70      49.023  -5.396 -11.570  1.00 32.59           C  
ANISOU 2262  CB  LEU B  70     4783   5321   2278   -513    925  -1401       C  
ATOM   2263  CG  LEU B  70      48.642  -6.611 -10.720  1.00 38.80           C  
ANISOU 2263  CG  LEU B  70     5491   6044   3208   -396    878  -1469       C  
ATOM   2264  CD1 LEU B  70      47.195  -6.972 -10.987  1.00 33.43           C  
ANISOU 2264  CD1 LEU B  70     4906   5316   2480   -417    741  -1479       C  
ATOM   2265  CD2 LEU B  70      49.546  -7.818 -10.999  1.00 32.39           C  
ANISOU 2265  CD2 LEU B  70     4644   5230   2434   -318    953  -1552       C  
ATOM   2266  N   LYS B  71      50.085  -2.482 -12.247  1.00 36.58           N  
ANISOU 2266  N   LYS B  71     5355   5936   2609   -750   1053  -1226       N  
ATOM   2267  CA  LYS B  71      50.447  -1.490 -13.263  1.00 38.75           C  
ANISOU 2267  CA  LYS B  71     5737   6262   2726   -882   1105  -1147       C  
ATOM   2268  C   LYS B  71      51.865  -0.963 -13.064  1.00 41.35           C  
ANISOU 2268  C   LYS B  71     5957   6647   3108   -912   1253  -1146       C  
ATOM   2269  O   LYS B  71      52.546  -0.660 -14.039  1.00 47.72           O  
ANISOU 2269  O   LYS B  71     6819   7511   3802   -989   1341  -1120       O  
ATOM   2270  CB  LYS B  71      49.467  -0.317 -13.257  1.00 41.86           C  
ANISOU 2270  CB  LYS B  71     6226   6597   3082   -963    985  -1014       C  
ATOM   2271  CG  LYS B  71      48.079  -0.607 -13.844  1.00 47.96           C  
ANISOU 2271  CG  LYS B  71     7123   7302   3799   -956    807   -964       C  
ATOM   2272  CD  LYS B  71      47.265   0.691 -13.891  1.00 55.97           C  
ANISOU 2272  CD  LYS B  71     8199   8224   4843  -1010    671   -792       C  
ATOM   2273  CE  LYS B  71      45.797   0.452 -14.198  1.00 63.72           C  
ANISOU 2273  CE  LYS B  71     9257   9122   5832   -980    470   -735       C  
ATOM   2274  NZ  LYS B  71      44.923   0.879 -13.044  1.00 70.45           N  
ANISOU 2274  NZ  LYS B  71    10001   9857   6908   -898    357   -676       N  
ATOM   2275  N   ALA B  72      52.324  -0.839 -11.817  1.00 42.58           N  
ANISOU 2275  N   ALA B  72     5958   6790   3431   -856   1278  -1173       N  
ATOM   2276  CA  ALA B  72      53.678  -0.356 -11.561  1.00 43.01           C  
ANISOU 2276  CA  ALA B  72     5896   6898   3549   -889   1402  -1179       C  
ATOM   2277  C   ALA B  72      54.742  -1.312 -12.065  1.00 49.78           C  
ANISOU 2277  C   ALA B  72     6690   7804   4421   -831   1499  -1254       C  
ATOM   2278  O   ALA B  72      55.912  -0.923 -12.136  1.00 53.72           O  
ANISOU 2278  O   ALA B  72     7107   8361   4944   -875   1611  -1257       O  
ATOM   2279  CB  ALA B  72      53.895  -0.118 -10.065  1.00 33.75           C  
ANISOU 2279  CB  ALA B  72     4574   5699   2552   -833   1385  -1201       C  
ATOM   2280  N   ASN B  73      54.367  -2.552 -12.380  1.00 49.98           N  
ANISOU 2280  N   ASN B  73     6748   7804   4438   -734   1459  -1318       N  
ATOM   2281  CA  ASN B  73      55.218  -3.510 -13.067  1.00 53.13           C  
ANISOU 2281  CA  ASN B  73     7126   8242   4819   -682   1549  -1394       C  
ATOM   2282  C   ASN B  73      54.865  -3.620 -14.542  1.00 51.45           C  
ANISOU 2282  C   ASN B  73     7083   8059   4407   -744   1562  -1386       C  
ATOM   2283  O   ASN B  73      55.106  -4.660 -15.159  1.00 59.72           O  
ANISOU 2283  O   ASN B  73     8154   9115   5420   -680   1597  -1466       O  
ATOM   2284  CB  ASN B  73      55.122  -4.869 -12.384  1.00 53.27           C  
ANISOU 2284  CB  ASN B  73     7069   8205   4967   -534   1503  -1477       C  
ATOM   2285  CG  ASN B  73      55.782  -4.868 -11.030  1.00 60.60           C  
ANISOU 2285  CG  ASN B  73     7825   9123   6079   -471   1508  -1488       C  
ATOM   2286  OD1 ASN B  73      56.984  -5.095 -10.916  1.00 69.63           O  
ANISOU 2286  OD1 ASN B  73     8858  10309   7288   -444   1600  -1528       O  
ATOM   2287  ND2 ASN B  73      55.011  -4.578  -9.995  1.00 61.82           N  
ANISOU 2287  ND2 ASN B  73     7952   9223   6312   -449   1410  -1454       N  
ATOM   2288  N   ASN B  74      54.255  -2.576 -15.096  1.00 52.32           N  
ANISOU 2288  N   ASN B  74     5922   9074   4882  -1495   1783  -1259       N  
ATOM   2289  CA  ASN B  74      53.885  -2.496 -16.509  1.00 54.46           C  
ANISOU 2289  CA  ASN B  74     6338   9459   4897  -1499   1902  -1179       C  
ATOM   2290  C   ASN B  74      53.034  -3.670 -16.977  1.00 51.74           C  
ANISOU 2290  C   ASN B  74     6161   9117   4381  -1310   1836  -1324       C  
ATOM   2291  O   ASN B  74      53.066  -4.038 -18.147  1.00 57.85           O  
ANISOU 2291  O   ASN B  74     7010  10046   4923  -1255   1956  -1339       O  
ATOM   2292  CB  ASN B  74      55.125  -2.343 -17.381  1.00 62.57           C  
ANISOU 2292  CB  ASN B  74     7197  10735   5841  -1554   2156  -1123       C  
ATOM   2293  CG  ASN B  74      55.766  -1.008 -17.184  1.00 72.52           C  
ANISOU 2293  CG  ASN B  74     8334  11978   7244  -1786   2217   -930       C  
ATOM   2294  OD1 ASN B  74      55.200   0.019 -17.567  1.00 76.05           O  
ANISOU 2294  OD1 ASN B  74     8924  12332   7641  -1924   2200   -747       O  
ATOM   2295  ND2 ASN B  74      56.922  -0.994 -16.529  1.00 74.14           N  
ANISOU 2295  ND2 ASN B  74     8275  12250   7645  -1833   2267   -965       N  
ATOM   2296  N   ILE B  75      52.237  -4.243 -16.094  1.00 46.28           N  
ANISOU 2296  N   ILE B  75     5539   8253   3792  -1217   1642  -1425       N  
ATOM   2297  CA  ILE B  75      51.284  -5.273 -16.490  1.00 51.21           C  
ANISOU 2297  CA  ILE B  75     6334   8841   4284  -1071   1546  -1542       C  
ATOM   2298  C   ILE B  75      49.989  -4.593 -16.917  1.00 48.79           C  
ANISOU 2298  C   ILE B  75     6234   8424   3879  -1143   1436  -1404       C  
ATOM   2299  O   ILE B  75      49.451  -3.745 -16.199  1.00 51.17           O  
ANISOU 2299  O   ILE B  75     6560   8566   4315  -1230   1332  -1290       O  
ATOM   2300  CB  ILE B  75      51.050  -6.270 -15.346  1.00 47.59           C  
ANISOU 2300  CB  ILE B  75     5838   8252   3993   -940   1397  -1699       C  
ATOM   2301  CG1 ILE B  75      52.378  -6.928 -14.946  1.00 46.47           C  
ANISOU 2301  CG1 ILE B  75     5482   8226   3950   -856   1500  -1825       C  
ATOM   2302  CG2 ILE B  75      50.046  -7.322 -15.755  1.00 44.75           C  
ANISOU 2302  CG2 ILE B  75     5651   7834   3519   -814   1286  -1809       C  
ATOM   2303  CD1 ILE B  75      52.283  -7.755 -13.649  1.00 43.12           C  
ANISOU 2303  CD1 ILE B  75     5002   7666   3717   -742   1351  -1945       C  
ATOM   2304  N   GLN B  76      49.509  -4.925 -18.105  1.00 52.36           N  
ANISOU 2304  N   GLN B  76     6839   8966   4091  -1101   1459  -1412       N  
ATOM   2305  CA  GLN B  76      48.262  -4.357 -18.596  1.00 51.18           C  
ANISOU 2305  CA  GLN B  76     6880   8730   3836  -1154   1340  -1279       C  
ATOM   2306  C   GLN B  76      47.093  -5.132 -17.999  1.00 47.63           C  
ANISOU 2306  C   GLN B  76     6516   8114   3467  -1060   1123  -1373       C  
ATOM   2307  O   GLN B  76      47.091  -6.364 -17.998  1.00 50.82           O  
ANISOU 2307  O   GLN B  76     6928   8532   3850   -935   1084  -1556       O  
ATOM   2308  CB  GLN B  76      48.222  -4.387 -20.128  1.00 47.99           C  
ANISOU 2308  CB  GLN B  76     6609   8503   3123  -1150   1437  -1245       C  
ATOM   2309  N   ILE B  77      46.114  -4.408 -17.452  1.00 42.07           N  
ANISOU 2309  N   ILE B  77     5869   7245   2870  -1117    985  -1243       N  
ATOM   2310  CA  ILE B  77      45.028  -5.012 -16.692  1.00 42.62           C  
ANISOU 2310  CA  ILE B  77     5980   7154   3061  -1043    794  -1299       C  
ATOM   2311  C   ILE B  77      43.705  -4.378 -17.102  1.00 46.54           C  
ANISOU 2311  C   ILE B  77     6615   7570   3499  -1084    665  -1146       C  
ATOM   2312  O   ILE B  77      43.659  -3.292 -17.684  1.00 46.04           O  
ANISOU 2312  O   ILE B  77     6606   7534   3352  -1175    714   -978       O  
ATOM   2313  CB  ILE B  77      45.208  -4.849 -15.169  1.00 39.38           C  
ANISOU 2313  CB  ILE B  77     5449   6606   2907  -1037    754  -1311       C  
ATOM   2314  CG1 ILE B  77      44.935  -3.384 -14.773  1.00 37.90           C  
ANISOU 2314  CG1 ILE B  77     5276   6319   2807  -1147    745  -1124       C  
ATOM   2315  CG2 ILE B  77      46.595  -5.332 -14.744  1.00 45.83           C  
ANISOU 2315  CG2 ILE B  77     6108   7512   3793  -1005    874  -1438       C  
ATOM   2316  CD1 ILE B  77      45.217  -3.039 -13.295  1.00 37.94           C  
ANISOU 2316  CD1 ILE B  77     5181   6197   3036  -1152    714  -1137       C  
ATOM   2317  N   ILE B  78      42.624  -5.077 -16.782  1.00 40.35           N  
ANISOU 2317  N   ILE B  78     5876   6683   2771  -1016    497  -1194       N  
ATOM   2318  CA  ILE B  78      41.288  -4.494 -16.716  1.00 38.35           C  
ANISOU 2318  CA  ILE B  78     5697   6318   2557  -1037    351  -1045       C  
ATOM   2319  C   ILE B  78      41.012  -4.167 -15.253  1.00 39.17           C  
ANISOU 2319  C   ILE B  78     5714   6262   2908  -1020    308  -1010       C  
ATOM   2320  O   ILE B  78      41.376  -4.941 -14.359  1.00 43.67           O  
ANISOU 2320  O   ILE B  78     6198   6793   3602   -960    308  -1137       O  
ATOM   2321  CB  ILE B  78      40.245  -5.470 -17.288  1.00 40.89           C  
ANISOU 2321  CB  ILE B  78     6105   6636   2795   -983    188  -1111       C  
ATOM   2322  CG1 ILE B  78      40.512  -5.695 -18.779  1.00 46.06           C  
ANISOU 2322  CG1 ILE B  78     6876   7456   3167   -995    226  -1149       C  
ATOM   2323  CG2 ILE B  78      38.813  -5.004 -16.988  1.00 38.20           C  
ANISOU 2323  CG2 ILE B  78     5791   6174   2551   -988     24   -962       C  
ATOM   2324  CD1 ILE B  78      39.558  -6.613 -19.419  1.00 52.23           C  
ANISOU 2324  CD1 ILE B  78     7758   8236   3851   -955     50  -1228       C  
ATOM   2325  N   HIS B  79      40.398  -3.017 -14.996  1.00 38.24           N  
ANISOU 2325  N   HIS B  79     5625   6050   2853  -1062    275   -840       N  
ATOM   2326  CA  HIS B  79      40.206  -2.569 -13.616  1.00 37.75           C  
ANISOU 2326  CA  HIS B  79     5499   5842   3001  -1037    253   -810       C  
ATOM   2327  C   HIS B  79      39.012  -1.631 -13.556  1.00 41.16           C  
ANISOU 2327  C   HIS B  79     5995   6164   3479  -1035    165   -634       C  
ATOM   2328  O   HIS B  79      39.011  -0.605 -14.246  1.00 47.17           O  
ANISOU 2328  O   HIS B  79     6827   6932   4162  -1100    197   -497       O  
ATOM   2329  CB  HIS B  79      41.462  -1.866 -13.104  1.00 39.61           C  
ANISOU 2329  CB  HIS B  79     5670   6080   3300  -1102    382   -822       C  
ATOM   2330  CG  HIS B  79      41.462  -1.633 -11.628  1.00 47.93           C  
ANISOU 2330  CG  HIS B  79     6663   7002   4545  -1064    357   -847       C  
ATOM   2331  ND1 HIS B  79      42.271  -0.695 -11.023  1.00 51.26           N  
ANISOU 2331  ND1 HIS B  79     7052   7373   5052  -1132    422   -824       N  
ATOM   2332  CD2 HIS B  79      40.750  -2.214 -10.631  1.00 49.06           C  
ANISOU 2332  CD2 HIS B  79     6781   7058   4801   -967    270   -890       C  
ATOM   2333  CE1 HIS B  79      42.062  -0.710  -9.717  1.00 49.52           C  
ANISOU 2333  CE1 HIS B  79     6801   7043   4972  -1068    371   -867       C  
ATOM   2334  NE2 HIS B  79      41.143  -1.623  -9.453  1.00 49.65           N  
ANISOU 2334  NE2 HIS B  79     6819   7042   5003   -963    290   -900       N  
ATOM   2335  N   ASN B  80      38.005  -1.966 -12.738  1.00 38.22           N  
ANISOU 2335  N   ASN B  80     5593   5693   3235   -954     64   -626       N  
ATOM   2336  CA  ASN B  80      36.848  -1.103 -12.558  1.00 37.05           C  
ANISOU 2336  CA  ASN B  80     5481   5441   3154   -923    -11   -462       C  
ATOM   2337  C   ASN B  80      37.049  -0.237 -11.318  1.00 37.98           C  
ANISOU 2337  C   ASN B  80     5578   5429   3424   -898     43   -436       C  
ATOM   2338  O   ASN B  80      38.138  -0.171 -10.754  1.00 46.68           O  
ANISOU 2338  O   ASN B  80     6646   6531   4561   -931    128   -529       O  
ATOM   2339  CB  ASN B  80      35.560  -1.928 -12.506  1.00 37.64           C  
ANISOU 2339  CB  ASN B  80     5525   5502   3275   -852   -148   -448       C  
ATOM   2340  CG  ASN B  80      35.468  -2.811 -11.267  1.00 39.79           C  
ANISOU 2340  CG  ASN B  80     5705   5720   3695   -780   -156   -549       C  
ATOM   2341  OD1 ASN B  80      36.474  -3.217 -10.722  1.00 30.90           O  
ANISOU 2341  OD1 ASN B  80     4543   4607   2589   -782    -80   -674       O  
ATOM   2342  ND2 ASN B  80      34.252  -3.108 -10.831  1.00 32.13           N  
ANISOU 2342  ND2 ASN B  80     4687   4694   2828   -716   -250   -480       N  
ATOM   2343  N   ASN B  81      35.998   0.449 -10.880  1.00 48.87           N  
ANISOU 2343  N   ASN B  81     6978   6698   4893   -833    -12   -314       N  
ATOM   2344  CA  ASN B  81      36.126   1.382  -9.765  1.00 52.61           C  
ANISOU 2344  CA  ASN B  81     7465   7036   5490   -797     35   -295       C  
ATOM   2345  C   ASN B  81      34.902   1.322  -8.864  1.00 47.26           C  
ANISOU 2345  C   ASN B  81     6752   6273   4930   -663    -21   -244       C  
ATOM   2346  O   ASN B  81      33.899   0.669  -9.167  1.00 43.93           O  
ANISOU 2346  O   ASN B  81     6285   5894   4513   -615   -101   -196       O  
ATOM   2347  CB  ASN B  81      36.337   2.824 -10.244  1.00 59.08           C  
ANISOU 2347  CB  ASN B  81     8382   7776   6289   -862     70   -168       C  
ATOM   2348  CG  ASN B  81      35.178   3.328 -11.063  1.00 65.49           C  
ANISOU 2348  CG  ASN B  81     9251   8568   7065   -826     -7      8       C  
ATOM   2349  OD1 ASN B  81      34.317   4.049 -10.563  1.00 67.08           O  
ANISOU 2349  OD1 ASN B  81     9476   8646   7364   -734    -39    104       O  
ATOM   2350  ND2 ASN B  81      35.127   2.917 -12.325  1.00 69.51           N  
ANISOU 2350  ND2 ASN B  81     9779   9204   7426   -884    -43     46       N  
ATOM   2351  N   GLU B  82      34.997   2.052  -7.750  1.00 47.10           N  
ANISOU 2351  N   GLU B  82     6755   6133   5006   -606     24   -254       N  
ATOM   2352  CA  GLU B  82      33.994   1.978  -6.697  1.00 54.28           C  
ANISOU 2352  CA  GLU B  82     7628   6974   6021   -462      7   -226       C  
ATOM   2353  C   GLU B  82      32.605   2.388  -7.169  1.00 53.26           C  
ANISOU 2353  C   GLU B  82     7496   6817   5923   -385    -55    -57       C  
ATOM   2354  O   GLU B  82      31.616   1.988  -6.549  1.00 59.50           O  
ANISOU 2354  O   GLU B  82     8210   7603   6793   -272    -76    -16       O  
ATOM   2355  CB  GLU B  82      34.415   2.851  -5.505  1.00 56.88           C  
ANISOU 2355  CB  GLU B  82     8018   7177   6417   -410     67   -277       C  
ATOM   2356  CG  GLU B  82      34.796   4.280  -5.873  1.00 61.40           C  
ANISOU 2356  CG  GLU B  82     8708   7632   6988   -470     87   -215       C  
ATOM   2357  CD  GLU B  82      35.375   5.044  -4.692  1.00 76.22           C  
ANISOU 2357  CD  GLU B  82    10657   9377   8927   -442    127   -305       C  
ATOM   2358  OE1 GLU B  82      34.977   4.755  -3.540  1.00 80.53           O  
ANISOU 2358  OE1 GLU B  82    11184   9897   9515   -313    138   -363       O  
ATOM   2359  OE2 GLU B  82      36.239   5.925  -4.908  1.00 81.64           O  
ANISOU 2359  OE2 GLU B  82    11422   9985   9614   -553    144   -317       O  
ATOM   2360  N   GLY B  83      32.502   3.175  -8.234  1.00 50.01           N  
ANISOU 2360  N   GLY B  83     7156   6392   5453   -441    -84     55       N  
ATOM   2361  CA  GLY B  83      31.213   3.548  -8.781  1.00 48.23           C  
ANISOU 2361  CA  GLY B  83     6919   6154   5253   -367   -162    226       C  
ATOM   2362  C   GLY B  83      30.681   2.603  -9.841  1.00 52.56           C  
ANISOU 2362  C   GLY B  83     7404   6841   5726   -416   -268    262       C  
ATOM   2363  O   GLY B  83      29.682   2.926 -10.498  1.00 53.26           O  
ANISOU 2363  O   GLY B  83     7482   6938   5817   -377   -358    412       O  
ATOM   2364  N   ALA B  84      31.311   1.431 -10.016  1.00 44.40           N  
ANISOU 2364  N   ALA B  84     6330   5911   4628   -494   -272    124       N  
ATOM   2365  CA  ALA B  84      31.017   0.567 -11.147  1.00 40.62           C  
ANISOU 2365  CA  ALA B  84     5832   5555   4048   -560   -377    125       C  
ATOM   2366  C   ALA B  84      31.226  -0.892 -10.768  1.00 41.00           C  
ANISOU 2366  C   ALA B  84     5799   5663   4118   -574   -393    -25       C  
ATOM   2367  O   ALA B  84      31.793  -1.673 -11.540  1.00 42.76           O  
ANISOU 2367  O   ALA B  84     6046   5975   4224   -654   -419   -126       O  
ATOM   2368  CB  ALA B  84      31.873   0.935 -12.364  1.00 43.32           C  
ANISOU 2368  CB  ALA B  84     6284   5965   4211   -673   -359    123       C  
ATOM   2369  N   ASN B  85      30.765  -1.285  -9.577  1.00 33.46           N  
ANISOU 2369  N   ASN B  85     4753   4655   3307   -489   -373    -38       N  
ATOM   2370  CA  ASN B  85      31.007  -2.637  -9.090  1.00 33.25           C  
ANISOU 2370  CA  ASN B  85     4656   4659   3317   -498   -380   -165       C  
ATOM   2371  C   ASN B  85      29.728  -3.475  -9.078  1.00 35.40           C  
ANISOU 2371  C   ASN B  85     4817   4945   3688   -471   -496    -92       C  
ATOM   2372  O   ASN B  85      29.641  -4.479  -8.377  1.00 30.67           O  
ANISOU 2372  O   ASN B  85     4144   4336   3174   -455   -496   -149       O  
ATOM   2373  CB  ASN B  85      31.688  -2.608  -7.718  1.00 33.72           C  
ANISOU 2373  CB  ASN B  85     4703   4660   3448   -440   -264   -249       C  
ATOM   2374  CG  ASN B  85      30.794  -2.052  -6.612  1.00 38.26           C  
ANISOU 2374  CG  ASN B  85     5230   5159   4148   -315   -227   -144       C  
ATOM   2375  OD1 ASN B  85      29.585  -1.971  -6.754  1.00 40.00           O  
ANISOU 2375  OD1 ASN B  85     5385   5378   4437   -265   -287    -11       O  
ATOM   2376  ND2 ASN B  85      31.402  -1.705  -5.486  1.00 37.93           N  
ANISOU 2376  ND2 ASN B  85     5216   5062   4133   -258   -129   -209       N  
ATOM   2377  N   MET B  86      28.740  -3.095  -9.855  1.00 35.54           N  
ANISOU 2377  N   MET B  86     4816   4985   3701   -473   -601     43       N  
ATOM   2378  CA  MET B  86      27.606  -3.973 -10.044  1.00 39.24           C  
ANISOU 2378  CA  MET B  86     5168   5481   4259   -483   -738    104       C  
ATOM   2379  C   MET B  86      27.682  -4.525 -11.460  1.00 39.96           C  
ANISOU 2379  C   MET B  86     5322   5650   4210   -593   -880     49       C  
ATOM   2380  O   MET B  86      28.636  -4.259 -12.198  1.00 36.41           O  
ANISOU 2380  O   MET B  86     5001   5243   3592   -646   -844    -34       O  
ATOM   2381  CB  MET B  86      26.311  -3.234  -9.733  1.00 45.29           C  
ANISOU 2381  CB  MET B  86     5833   6224   5153   -388   -766    302       C  
ATOM   2382  CG  MET B  86      26.372  -2.575  -8.346  1.00 49.63           C  
ANISOU 2382  CG  MET B  86     6361   6697   5801   -260   -603    331       C  
ATOM   2383  SD  MET B  86      24.769  -2.339  -7.596  1.00 55.03           S  
ANISOU 2383  SD  MET B  86     6861   7367   6679   -123   -607    531       S  
ATOM   2384  CE  MET B  86      25.191  -2.240  -5.859  1.00 47.39           C  
ANISOU 2384  CE  MET B  86     5894   6335   5776      0   -407    473       C  
ATOM   2385  N   ALA B  87      26.681  -5.320 -11.824  1.00 42.88           N  
ANISOU 2385  N   ALA B  87     5601   6044   4649   -629  -1042     93       N  
ATOM   2386  CA  ALA B  87      26.743  -6.053 -13.080  1.00 41.45           C  
ANISOU 2386  CA  ALA B  87     5491   5928   4331   -733  -1197      5       C  
ATOM   2387  C   ALA B  87      26.977  -5.114 -14.252  1.00 42.25           C  
ANISOU 2387  C   ALA B  87     5722   6100   4232   -755  -1226     52       C  
ATOM   2388  O   ALA B  87      27.902  -5.310 -15.051  1.00 37.62           O  
ANISOU 2388  O   ALA B  87     5270   5571   3453   -812  -1206    -75       O  
ATOM   2389  CB  ALA B  87      25.455  -6.853 -13.270  1.00 43.92           C  
ANISOU 2389  CB  ALA B  87     5673   6243   4773   -775  -1395     77       C  
ATOM   2390  N   ALA B  88      26.150  -4.076 -14.361  1.00 38.88           N  
ANISOU 2390  N   ALA B  88     5255   5671   3847   -700  -1262    245       N  
ATOM   2391  CA  ALA B  88      26.232  -3.191 -15.513  1.00 43.31           C  
ANISOU 2391  CA  ALA B  88     5939   6294   4224   -720  -1311    325       C  
ATOM   2392  C   ALA B  88      27.588  -2.515 -15.594  1.00 44.09           C  
ANISOU 2392  C   ALA B  88     6182   6389   4180   -732  -1130    256       C  
ATOM   2393  O   ALA B  88      28.191  -2.448 -16.671  1.00 44.63           O  
ANISOU 2393  O   ALA B  88     6383   6541   4033   -797  -1143    213       O  
ATOM   2394  CB  ALA B  88      25.115  -2.152 -15.459  1.00 46.11           C  
ANISOU 2394  CB  ALA B  88     6216   6624   4681   -634  -1371    556       C  
ATOM   2395  N   GLY B  89      28.097  -2.024 -14.463  1.00 43.73           N  
ANISOU 2395  N   GLY B  89     6112   6256   4249   -675   -959    245       N  
ATOM   2396  CA  GLY B  89      29.373  -1.332 -14.491  1.00 36.79           C  
ANISOU 2396  CA  GLY B  89     5348   5366   3264   -703   -798    191       C  
ATOM   2397  C   GLY B  89      30.540  -2.250 -14.769  1.00 39.09           C  
ANISOU 2397  C   GLY B  89     5692   5727   3435   -777   -738    -11       C  
ATOM   2398  O   GLY B  89      31.541  -1.833 -15.356  1.00 41.01           O  
ANISOU 2398  O   GLY B  89     6035   6020   3527   -831   -645    -46       O  
ATOM   2399  N   ILE B  90      30.441  -3.505 -14.338  1.00 38.03           N  
ANISOU 2399  N   ILE B  90     5483   5592   3374   -776   -782   -138       N  
ATOM   2400  CA  ILE B  90      31.515  -4.454 -14.584  1.00 40.38           C  
ANISOU 2400  CA  ILE B  90     5826   5945   3571   -823   -730   -338       C  
ATOM   2401  C   ILE B  90      31.556  -4.819 -16.060  1.00 44.97           C  
ANISOU 2401  C   ILE B  90     6515   6639   3933   -885   -828   -383       C  
ATOM   2402  O   ILE B  90      32.628  -4.884 -16.676  1.00 52.47           O  
ANISOU 2402  O   ILE B  90     7555   7669   4712   -920   -734   -485       O  
ATOM   2403  CB  ILE B  90      31.319  -5.694 -13.690  1.00 42.10           C  
ANISOU 2403  CB  ILE B  90     5946   6105   3945   -796   -762   -444       C  
ATOM   2404  CG1 ILE B  90      31.615  -5.347 -12.236  1.00 36.74           C  
ANISOU 2404  CG1 ILE B  90     5193   5341   3426   -729   -631   -430       C  
ATOM   2405  CG2 ILE B  90      32.179  -6.853 -14.151  1.00 34.62           C  
ANISOU 2405  CG2 ILE B  90     5052   5207   2895   -831   -759   -650       C  
ATOM   2406  CD1 ILE B  90      31.142  -6.437 -11.286  1.00 32.10           C  
ANISOU 2406  CD1 ILE B  90     4500   4691   3005   -693   -671   -470       C  
ATOM   2407  N   THR B  91      30.387  -5.072 -16.644  1.00 48.49           N  
ANISOU 2407  N   THR B  91     6948   7102   4374   -897  -1019   -307       N  
ATOM   2408  CA  THR B  91      30.295  -5.325 -18.075  1.00 48.85           C  
ANISOU 2408  CA  THR B  91     7113   7259   4189   -951  -1140   -338       C  
ATOM   2409  C   THR B  91      30.898  -4.177 -18.870  1.00 50.57           C  
ANISOU 2409  C   THR B  91     7451   7555   4207   -968  -1042   -243       C  
ATOM   2410  O   THR B  91      31.689  -4.392 -19.793  1.00 50.76           O  
ANISOU 2410  O   THR B  91     7596   7688   4002  -1004   -995   -339       O  
ATOM   2411  CB  THR B  91      28.838  -5.534 -18.447  1.00 49.90           C  
ANISOU 2411  CB  THR B  91     7190   7389   4381   -961  -1378   -230       C  
ATOM   2412  OG1 THR B  91      28.331  -6.638 -17.694  1.00 51.45           O  
ANISOU 2412  OG1 THR B  91     7267   7506   4776   -964  -1457   -309       O  
ATOM   2413  CG2 THR B  91      28.689  -5.794 -19.946  1.00 43.70           C  
ANISOU 2413  CG2 THR B  91     6545   6724   3335  -1015  -1534   -268       C  
ATOM   2414  N   SER B  92      30.556  -2.946 -18.496  1.00 47.44           N  
ANISOU 2414  N   SER B  92     7026   7099   3899   -937   -998    -51       N  
ATOM   2415  CA  SER B  92      31.118  -1.781 -19.169  1.00 54.98           C  
ANISOU 2415  CA  SER B  92     8095   8099   4696   -962   -901     67       C  
ATOM   2416  C   SER B  92      32.637  -1.727 -19.030  1.00 52.48           C  
ANISOU 2416  C   SER B  92     7820   7814   4307  -1000   -685    -52       C  
ATOM   2417  O   SER B  92      33.338  -1.334 -19.966  1.00 56.42           O  
ANISOU 2417  O   SER B  92     8429   8414   4593  -1050   -607    -28       O  
ATOM   2418  CB  SER B  92      30.484  -0.508 -18.615  1.00 56.91           C  
ANISOU 2418  CB  SER B  92     8299   8231   5093   -909   -891    280       C  
ATOM   2419  OG  SER B  92      31.230   0.624 -19.014  1.00 63.22           O  
ANISOU 2419  OG  SER B  92     9203   9031   5787   -943   -763    382       O  
ATOM   2420  N   ALA B  93      33.167  -2.114 -17.872  1.00 48.86           N  
ANISOU 2420  N   ALA B  93     7266   7279   4019   -977   -584   -168       N  
ATOM   2421  CA  ALA B  93      34.616  -2.076 -17.696  1.00 44.08           C  
ANISOU 2421  CA  ALA B  93     6672   6710   3366  -1012   -392   -277       C  
ATOM   2422  C   ALA B  93      35.312  -3.049 -18.639  1.00 40.05           C  
ANISOU 2422  C   ALA B  93     6226   6344   2646  -1038   -371   -442       C  
ATOM   2423  O   ALA B  93      36.362  -2.731 -19.202  1.00 45.55           O  
ANISOU 2423  O   ALA B  93     6976   7138   3193  -1081   -226   -460       O  
ATOM   2424  CB  ALA B  93      34.980  -2.388 -16.247  1.00 45.79           C  
ANISOU 2424  CB  ALA B  93     6773   6823   3802   -971   -319   -374       C  
ATOM   2425  N   PHE B  94      34.736  -4.233 -18.831  1.00 45.06           N  
ANISOU 2425  N   PHE B  94     6858   6993   3270  -1012   -512   -562       N  
ATOM   2426  CA  PHE B  94      35.341  -5.208 -19.734  1.00 47.90           C  
ANISOU 2426  CA  PHE B  94     7300   7474   3424  -1017   -503   -742       C  
ATOM   2427  C   PHE B  94      35.283  -4.738 -21.186  1.00 52.21           C  
ANISOU 2427  C   PHE B  94     7995   8160   3681  -1054   -529   -663       C  
ATOM   2428  O   PHE B  94      36.228  -4.956 -21.949  1.00 50.74           O  
ANISOU 2428  O   PHE B  94     7890   8107   3283  -1062   -409   -759       O  
ATOM   2429  CB  PHE B  94      34.661  -6.573 -19.571  1.00 43.51           C  
ANISOU 2429  CB  PHE B  94     6721   6864   2945   -988   -673   -889       C  
ATOM   2430  CG  PHE B  94      35.320  -7.459 -18.547  1.00 44.88           C  
ANISOU 2430  CG  PHE B  94     6803   6965   3284   -945   -592  -1053       C  
ATOM   2431  CD1 PHE B  94      36.351  -8.315 -18.913  1.00 42.68           C  
ANISOU 2431  CD1 PHE B  94     6570   6757   2891   -917   -503  -1256       C  
ATOM   2432  CD2 PHE B  94      34.929  -7.419 -17.217  1.00 42.94           C  
ANISOU 2432  CD2 PHE B  94     6429   6587   3301   -919   -598   -998       C  
ATOM   2433  CE1 PHE B  94      36.966  -9.123 -17.969  1.00 39.22           C  
ANISOU 2433  CE1 PHE B  94     6045   6246   2609   -865   -438  -1394       C  
ATOM   2434  CE2 PHE B  94      35.538  -8.229 -16.278  1.00 42.23           C  
ANISOU 2434  CE2 PHE B  94     6264   6434   3348   -874   -532  -1133       C  
ATOM   2435  CZ  PHE B  94      36.556  -9.080 -16.656  1.00 37.35           C  
ANISOU 2435  CZ  PHE B  94     5687   5877   2627   -849   -459  -1327       C  
ATOM   2436  N   ILE B  95      34.190  -4.090 -21.590  1.00 55.70           N  
ANISOU 2436  N   ILE B  95     8474   8587   4104  -1068   -680   -482       N  
ATOM   2437  CA  ILE B  95      34.106  -3.597 -22.962  1.00 60.53           C  
ANISOU 2437  CA  ILE B  95     9238   9336   4426  -1098   -716   -384       C  
ATOM   2438  C   ILE B  95      35.081  -2.447 -23.174  1.00 59.23           C  
ANISOU 2438  C   ILE B  95     9112   9222   4172  -1138   -498   -254       C  
ATOM   2439  O   ILE B  95      35.822  -2.416 -24.162  1.00 60.81           O  
ANISOU 2439  O   ILE B  95     9421   9575   4108  -1162   -394   -276       O  
ATOM   2440  CB  ILE B  95      32.665  -3.184 -23.307  1.00 61.54           C  
ANISOU 2440  CB  ILE B  95     9380   9431   4570  -1094   -950   -208       C  
ATOM   2441  CG1 ILE B  95      31.732  -4.389 -23.193  1.00 58.03           C  
ANISOU 2441  CG1 ILE B  95     8888   8948   4214  -1080  -1174   -337       C  
ATOM   2442  CG2 ILE B  95      32.600  -2.634 -24.721  1.00 50.48           C  
ANISOU 2442  CG2 ILE B  95     8149   8178   2854  -1120   -994    -91       C  
ATOM   2443  CD1 ILE B  95      30.275  -4.023 -23.030  1.00 57.99           C  
ANISOU 2443  CD1 ILE B  95     8804   8872   4357  -1069  -1390   -159       C  
ATOM   2444  N   MET B  96      35.108  -1.496 -22.238  1.00 61.07           N  
ANISOU 2444  N   MET B  96     9255   9323   4624  -1146   -422   -119       N  
ATOM   2445  CA  MET B  96      35.908  -0.290 -22.424  1.00 60.63           C  
ANISOU 2445  CA  MET B  96     9237   9281   4517  -1204   -244     34       C  
ATOM   2446  C   MET B  96      37.400  -0.584 -22.421  1.00 58.85           C  
ANISOU 2446  C   MET B  96     8984   9150   4225  -1241    -21   -102       C  
ATOM   2447  O   MET B  96      38.164   0.109 -23.101  1.00 60.17           O  
ANISOU 2447  O   MET B  96     9213   9411   4238  -1304    127      0       O  
ATOM   2448  CB  MET B  96      35.594   0.736 -21.333  1.00 61.34           C  
ANISOU 2448  CB  MET B  96     9249   9182   4877  -1200   -230    176       C  
ATOM   2449  CG  MET B  96      34.259   1.433 -21.481  1.00 71.72           C  
ANISOU 2449  CG  MET B  96    10595  10413   6241  -1160   -403    377       C  
ATOM   2450  SD  MET B  96      34.096   2.189 -23.102  1.00 88.21           S  
ANISOU 2450  SD  MET B  96    12864  12632   8020  -1203   -442    586       S  
ATOM   2451  CE  MET B  96      32.869   3.460 -22.785  1.00 91.68           C  
ANISOU 2451  CE  MET B  96    13303  12897   8635  -1147   -572    859       C  
ATOM   2452  N   GLN B  97      37.841  -1.594 -21.673  1.00 52.65           N  
ANISOU 2452  N   GLN B  97     8099   8345   3560  -1201     11   -317       N  
ATOM   2453  CA  GLN B  97      39.251  -1.707 -21.341  1.00 53.67           C  
ANISOU 2453  CA  GLN B  97     8152   8529   3713  -1226    223   -422       C  
ATOM   2454  C   GLN B  97      39.947  -2.928 -21.922  1.00 57.08           C  
ANISOU 2454  C   GLN B  97     8602   9112   3974  -1181    286   -643       C  
ATOM   2455  O   GLN B  97      41.180  -2.994 -21.855  1.00 63.49           O  
ANISOU 2455  O   GLN B  97     9347  10008   4770  -1195    478   -715       O  
ATOM   2456  CB  GLN B  97      39.431  -1.714 -19.818  1.00 51.73           C  
ANISOU 2456  CB  GLN B  97     7760   8126   3770  -1208    241   -479       C  
ATOM   2457  CG  GLN B  97      38.764  -0.533 -19.111  1.00 45.80           C  
ANISOU 2457  CG  GLN B  97     6996   7207   3200  -1230    188   -291       C  
ATOM   2458  CD  GLN B  97      39.120  -0.497 -17.655  1.00 46.89           C  
ANISOU 2458  CD  GLN B  97     7011   7214   3592  -1211    229   -361       C  
ATOM   2459  OE1 GLN B  97      40.224  -0.888 -17.282  1.00 53.88           O  
ANISOU 2459  OE1 GLN B  97     7816   8148   4509  -1225    348   -489       O  
ATOM   2460  NE2 GLN B  97      38.183  -0.057 -16.811  1.00 42.51           N  
ANISOU 2460  NE2 GLN B  97     6437   6502   3214  -1168    129   -280       N  
ATOM   2461  N   SER B  98      39.209  -3.897 -22.461  1.00 47.56           N  
ANISOU 2461  N   SER B  98     7478   7937   2654  -1124    126   -756       N  
ATOM   2462  CA  SER B  98      39.844  -5.059 -23.073  1.00 59.39           C  
ANISOU 2462  CA  SER B  98     9024   9564   3977  -1065    179   -982       C  
ATOM   2463  C   SER B  98      40.697  -4.645 -24.262  1.00 62.96           C  
ANISOU 2463  C   SER B  98     9566  10214   4142  -1084    356   -934       C  
ATOM   2464  O   SER B  98      40.252  -3.878 -25.124  1.00 57.51           O  
ANISOU 2464  O   SER B  98     8991   9588   3273  -1128    321   -758       O  
ATOM   2465  CB  SER B  98      38.797  -6.072 -23.530  1.00 54.02           C  
ANISOU 2465  CB  SER B  98     8444   8861   3219  -1017    -55  -1101       C  
ATOM   2466  OG  SER B  98      38.071  -6.546 -22.420  1.00 51.64           O  
ANISOU 2466  OG  SER B  98     8039   8380   3201   -997   -198  -1138       O  
ATOM   2467  N   THR B  99      41.937  -5.138 -24.288  1.00 63.57           N  
ANISOU 2467  N   THR B  99     9564  10360   4228  -1021    546  -1063       N  
ATOM   2468  CA  THR B  99      42.836  -5.032 -25.429  1.00 67.42           C  
ANISOU 2468  CA  THR B  99    10104  11013   4500   -980    724  -1042       C  
ATOM   2469  C   THR B  99      43.492  -6.401 -25.585  1.00 69.26           C  
ANISOU 2469  C   THR B  99    10318  11255   4742   -823    766  -1288       C  
ATOM   2470  O   THR B  99      43.358  -7.242 -24.688  1.00 69.06           O  
ANISOU 2470  O   THR B  99    10218  11103   4918   -774    678  -1439       O  
ATOM   2471  CB  THR B  99      43.891  -3.933 -25.232  1.00 72.60           C  
ANISOU 2471  CB  THR B  99    10654  11756   5176  -1092    967   -886       C  
ATOM   2472  OG1 THR B  99      44.957  -4.433 -24.422  1.00 77.60           O  
ANISOU 2472  OG1 THR B  99    11111  12390   5984  -1059   1106  -1029       O  
ATOM   2473  CG2 THR B  99      43.300  -2.691 -24.570  1.00 74.05           C  
ANISOU 2473  CG2 THR B  99    10831  11850   5456  -1248    916   -674       C  
ATOM   2474  N   PRO B 100      44.187  -6.683 -26.692  1.00 70.46           N  
ANISOU 2474  N   PRO B 100    10548  11542   4681   -733    897  -1328       N  
ATOM   2475  CA  PRO B 100      44.859  -7.991 -26.812  1.00 71.72           C  
ANISOU 2475  CA  PRO B 100    10707  11693   4852   -573    945  -1560       C  
ATOM   2476  C   PRO B 100      45.969  -8.222 -25.792  1.00 70.03           C  
ANISOU 2476  C   PRO B 100    10279  11468   4861   -561   1106  -1636       C  
ATOM   2477  O   PRO B 100      46.376  -9.374 -25.602  1.00 67.77           O  
ANISOU 2477  O   PRO B 100     9977  11124   4649   -430   1104  -1827       O  
ATOM   2478  CB  PRO B 100      45.415  -7.976 -28.246  1.00 73.60           C  
ANISOU 2478  CB  PRO B 100    11081  12097   4785   -492   1088  -1544       C  
ATOM   2479  CG  PRO B 100      44.579  -6.984 -28.974  1.00 73.22           C  
ANISOU 2479  CG  PRO B 100    11161  12107   4554   -583   1004  -1341       C  
ATOM   2480  CD  PRO B 100      44.201  -5.938 -27.966  1.00 71.27           C  
ANISOU 2480  CD  PRO B 100    10785  11792   4503   -753    970  -1167       C  
ATOM   2481  N   LYS B 101      46.471  -7.175 -25.131  1.00 70.47           N  
ANISOU 2481  N   LYS B 101    10178  11570   5029   -693   1234  -1491       N  
ATOM   2482  CA  LYS B 101      47.572  -7.329 -24.188  1.00 71.88           C  
ANISOU 2482  CA  LYS B 101    10141  11759   5412   -688   1378  -1559       C  
ATOM   2483  C   LYS B 101      47.106  -7.594 -22.763  1.00 68.81           C  
ANISOU 2483  C   LYS B 101     9656  11198   5292   -714   1232  -1626       C  
ATOM   2484  O   LYS B 101      47.817  -8.262 -22.001  1.00 66.43           O  
ANISOU 2484  O   LYS B 101     9217  10863   5160   -641   1277  -1753       O  
ATOM   2485  CB  LYS B 101      48.457  -6.079 -24.205  1.00 76.45           C  
ANISOU 2485  CB  LYS B 101    10592  12476   5981   -828   1596  -1374       C  
ATOM   2486  N   THR B 102      45.932  -7.090 -22.388  1.00 67.55           N  
ANISOU 2486  N   THR B 102     9566  10930   5169   -807   1061  -1535       N  
ATOM   2487  CA  THR B 102      45.436  -7.205 -21.021  1.00 62.84           C  
ANISOU 2487  CA  THR B 102     8887  10176   4814   -836    936  -1572       C  
ATOM   2488  C   THR B 102      45.149  -8.664 -20.701  1.00 60.41           C  
ANISOU 2488  C   THR B 102     8595   9741   4616   -690    800  -1762       C  
ATOM   2489  O   THR B 102      44.182  -9.238 -21.213  1.00 57.76           O  
ANISOU 2489  O   THR B 102     8400   9334   4211   -648    632  -1800       O  
ATOM   2490  CB  THR B 102      44.177  -6.357 -20.843  1.00 61.82           C  
ANISOU 2490  CB  THR B 102     8848   9969   4673   -952    787  -1420       C  
ATOM   2491  OG1 THR B 102      43.205  -6.730 -21.827  1.00 64.31           O  
ANISOU 2491  OG1 THR B 102     9331  10277   4827   -909    635  -1416       O  
ATOM   2492  CG2 THR B 102      44.498  -4.864 -20.972  1.00 59.29           C  
ANISOU 2492  CG2 THR B 102     8500   9683   4346  -1080    901  -1185       C  
ATOM   2493  N   LYS B 103      45.961  -9.262 -19.829  1.00 63.90           N  
ANISOU 2493  N   LYS B 103     8894  10147   5238   -622    861  -1873       N  
ATOM   2494  CA  LYS B 103      45.792 -10.664 -19.460  1.00 68.89           C  
ANISOU 2494  CA  LYS B 103     9542  10643   5989   -486    746  -2036       C  
ATOM   2495  C   LYS B 103      45.352 -10.867 -18.006  1.00 63.76           C  
ANISOU 2495  C   LYS B 103     8801   9836   5590   -499    631  -2046       C  
ATOM   2496  O   LYS B 103      45.268 -12.015 -17.547  1.00 58.73           O  
ANISOU 2496  O   LYS B 103     8163   9075   5077   -396    543  -2159       O  
ATOM   2497  CB  LYS B 103      47.084 -11.435 -19.738  1.00 72.81           C  
ANISOU 2497  CB  LYS B 103     9974  11217   6475   -355    898  -2163       C  
ATOM   2498  N   ILE B 104      45.067  -9.792 -17.271  1.00 57.20           N  
ANISOU 2498  N   ILE B 104     7908   8999   4828   -620    631  -1926       N  
ATOM   2499  CA  ILE B 104      44.503  -9.876 -15.929  1.00 49.96           C  
ANISOU 2499  CA  ILE B 104     6929   7935   4119   -630    519  -1919       C  
ATOM   2500  C   ILE B 104      43.364  -8.879 -15.817  1.00 48.73           C  
ANISOU 2500  C   ILE B 104     6831   7705   3980   -731    417  -1735       C  
ATOM   2501  O   ILE B 104      43.483  -7.734 -16.266  1.00 48.04           O  
ANISOU 2501  O   ILE B 104     6759   7683   3811   -819    491  -1596       O  
ATOM   2502  CB  ILE B 104      45.546  -9.586 -14.829  1.00 51.94           C  
ANISOU 2502  CB  ILE B 104     7008   8193   4534   -626    621  -1926       C  
ATOM   2503  CG1 ILE B 104      46.737 -10.524 -14.946  1.00 60.08           C  
ANISOU 2503  CG1 ILE B 104     7954   9294   5579   -508    721  -2072       C  
ATOM   2504  CG2 ILE B 104      44.916  -9.705 -13.426  1.00 48.21           C  
ANISOU 2504  CG2 ILE B 104     6490   7545   4284   -609    492  -1887       C  
ATOM   2505  CD1 ILE B 104      47.731 -10.358 -13.816  1.00 63.59           C  
ANISOU 2505  CD1 ILE B 104     8219   9764   6180   -500    795  -2107       C  
ATOM   2506  N   ALA B 105      42.270  -9.298 -15.188  1.00 41.14           N  
ANISOU 2506  N   ALA B 105     5890   6594   3146   -711    253  -1717       N  
ATOM   2507  CA  ALA B 105      41.228  -8.378 -14.766  1.00 37.14           C  
ANISOU 2507  CA  ALA B 105     5395   5994   2721   -773    165  -1535       C  
ATOM   2508  C   ALA B 105      41.200  -8.311 -13.246  1.00 36.67           C  
ANISOU 2508  C   ALA B 105     5230   5813   2890   -743    149  -1508       C  
ATOM   2509  O   ALA B 105      41.319  -9.333 -12.559  1.00 37.19           O  
ANISOU 2509  O   ALA B 105     5249   5819   3062   -669    113  -1615       O  
ATOM   2510  CB  ALA B 105      39.856  -8.792 -15.306  1.00 37.48           C  
ANISOU 2510  CB  ALA B 105     5534   5983   2723   -779    -13  -1503       C  
ATOM   2511  N   VAL B 106      41.052  -7.102 -12.726  1.00 33.13           N  
ANISOU 2511  N   VAL B 106     4757   5323   2506   -795    176  -1364       N  
ATOM   2512  CA  VAL B 106      40.994  -6.855 -11.298  1.00 38.06           C  
ANISOU 2512  CA  VAL B 106     5306   5840   3314   -765    165  -1331       C  
ATOM   2513  C   VAL B 106      39.651  -6.186 -11.059  1.00 38.58           C  
ANISOU 2513  C   VAL B 106     5415   5808   3435   -776     72  -1176       C  
ATOM   2514  O   VAL B 106      39.459  -5.023 -11.438  1.00 37.64           O  
ANISOU 2514  O   VAL B 106     5340   5689   3271   -835     96  -1051       O  
ATOM   2515  CB  VAL B 106      42.147  -5.964 -10.824  1.00 35.26           C  
ANISOU 2515  CB  VAL B 106     4885   5517   2994   -810    284  -1322       C  
ATOM   2516  CG1 VAL B 106      42.045  -5.689  -9.322  1.00 32.07           C  
ANISOU 2516  CG1 VAL B 106     4428   5001   2757   -772    254  -1301       C  
ATOM   2517  CG2 VAL B 106      43.484  -6.575 -11.217  1.00 37.83           C  
ANISOU 2517  CG2 VAL B 106     5144   5968   3261   -799    388  -1459       C  
ATOM   2518  N   ILE B 107      38.714  -6.914 -10.469  1.00 30.35           N  
ANISOU 2518  N   ILE B 107     4355   4682   2495   -718    -31  -1171       N  
ATOM   2519  CA  ILE B 107      37.311  -6.507 -10.478  1.00 30.24           C  
ANISOU 2519  CA  ILE B 107     4364   4601   2523   -718   -128  -1026       C  
ATOM   2520  C   ILE B 107      36.795  -6.471  -9.056  1.00 35.52           C  
ANISOU 2520  C   ILE B 107     4969   5167   3360   -650   -140   -974       C  
ATOM   2521  O   ILE B 107      36.701  -7.518  -8.404  1.00 31.81           O  
ANISOU 2521  O   ILE B 107     4452   4660   2975   -600   -173  -1037       O  
ATOM   2522  CB  ILE B 107      36.442  -7.449 -11.329  1.00 37.11           C  
ANISOU 2522  CB  ILE B 107     5268   5485   3347   -725   -258  -1046       C  
ATOM   2523  CG1 ILE B 107      36.910  -7.461 -12.792  1.00 40.71           C  
ANISOU 2523  CG1 ILE B 107     5813   6058   3597   -779   -248  -1103       C  
ATOM   2524  CG2 ILE B 107      34.942  -7.083 -11.210  1.00 31.00           C  
ANISOU 2524  CG2 ILE B 107     4477   4649   2654   -720   -370   -883       C  
ATOM   2525  CD1 ILE B 107      36.818  -6.109 -13.491  1.00 41.11           C  
ANISOU 2525  CD1 ILE B 107     5923   6157   3540   -836   -211   -961       C  
ATOM   2526  N   GLU B 108      36.432  -5.280  -8.580  1.00 28.81           N  
ANISOU 2526  N   GLU B 108     4129   4265   2553   -642   -111   -854       N  
ATOM   2527  CA  GLU B 108      35.681  -5.201  -7.331  1.00 28.03           C  
ANISOU 2527  CA  GLU B 108     3984   4077   2589   -561   -123   -786       C  
ATOM   2528  C   GLU B 108      34.203  -5.362  -7.656  1.00 31.82           C  
ANISOU 2528  C   GLU B 108     4443   4535   3114   -543   -222   -662       C  
ATOM   2529  O   GLU B 108      33.724  -4.880  -8.689  1.00 35.39           O  
ANISOU 2529  O   GLU B 108     4935   5016   3495   -587   -274   -585       O  
ATOM   2530  CB  GLU B 108      35.957  -3.899  -6.559  1.00 30.85           C  
ANISOU 2530  CB  GLU B 108     4369   4375   2977   -539    -48   -737       C  
ATOM   2531  CG  GLU B 108      35.494  -2.579  -7.153  1.00 39.95           C  
ANISOU 2531  CG  GLU B 108     5587   5495   4096   -567    -47   -609       C  
ATOM   2532  CD  GLU B 108      35.439  -1.443  -6.092  1.00 46.90           C  
ANISOU 2532  CD  GLU B 108     6501   6270   5049   -509      5   -563       C  
ATOM   2533  OE1 GLU B 108      36.347  -0.572  -6.076  1.00 54.80           O  
ANISOU 2533  OE1 GLU B 108     7554   7243   6024   -567     60   -593       O  
ATOM   2534  OE2 GLU B 108      34.493  -1.433  -5.259  1.00 42.66           O  
ANISOU 2534  OE2 GLU B 108     5937   5676   4595   -404     -6   -500       O  
ATOM   2535  N   ILE B 109      33.495  -6.107  -6.813  1.00 28.02           N  
ANISOU 2535  N   ILE B 109     3888   4008   2749   -482   -256   -634       N  
ATOM   2536  CA  ILE B 109      32.122  -6.487  -7.110  1.00 32.07           C  
ANISOU 2536  CA  ILE B 109     4346   4510   3331   -479   -360   -521       C  
ATOM   2537  C   ILE B 109      31.286  -6.397  -5.839  1.00 34.98           C  
ANISOU 2537  C   ILE B 109     4632   4821   3837   -383   -325   -413       C  
ATOM   2538  O   ILE B 109      31.641  -6.962  -4.798  1.00 27.62           O  
ANISOU 2538  O   ILE B 109     3672   3862   2960   -333   -272   -461       O  
ATOM   2539  CB  ILE B 109      32.053  -7.902  -7.732  1.00 33.14           C  
ANISOU 2539  CB  ILE B 109     4465   4662   3463   -535   -463   -608       C  
ATOM   2540  CG1 ILE B 109      30.606  -8.294  -8.098  1.00 33.29           C  
ANISOU 2540  CG1 ILE B 109     4413   4668   3568   -558   -599   -487       C  
ATOM   2541  CG2 ILE B 109      32.696  -8.945  -6.810  1.00 32.02           C  
ANISOU 2541  CG2 ILE B 109     4295   4483   3389   -499   -423   -713       C  
ATOM   2542  CD1 ILE B 109      30.530  -9.514  -8.970  1.00 30.85           C  
ANISOU 2542  CD1 ILE B 109     4122   4365   3234   -636   -731   -584       C  
ATOM   2543  N   ASP B 110      30.171  -5.691  -5.929  1.00 38.02           N  
ANISOU 2543  N   ASP B 110     4977   5195   4272   -346   -352   -259       N  
ATOM   2544  CA  ASP B 110      29.212  -5.672  -4.842  1.00 28.93           C  
ANISOU 2544  CA  ASP B 110     3731   4010   3251   -246   -313   -139       C  
ATOM   2545  C   ASP B 110      28.804  -7.099  -4.475  1.00 37.82           C  
ANISOU 2545  C   ASP B 110     4760   5133   4477   -268   -363   -138       C  
ATOM   2546  O   ASP B 110      28.559  -7.935  -5.345  1.00 39.20           O  
ANISOU 2546  O   ASP B 110     4912   5322   4660   -360   -485   -161       O  
ATOM   2547  CB  ASP B 110      27.999  -4.857  -5.265  1.00 31.32           C  
ANISOU 2547  CB  ASP B 110     3982   4318   3602   -208   -357     30       C  
ATOM   2548  CG  ASP B 110      26.982  -4.719  -4.154  1.00 44.77           C  
ANISOU 2548  CG  ASP B 110     5574   6002   5436    -84   -290    166       C  
ATOM   2549  OD1 ASP B 110      27.187  -3.830  -3.297  1.00 55.28           O  
ANISOU 2549  OD1 ASP B 110     6957   7293   6754     26   -171    169       O  
ATOM   2550  OD2 ASP B 110      26.002  -5.499  -4.132  1.00 46.28           O  
ANISOU 2550  OD2 ASP B 110     5628   6216   5741    -97   -354    265       O  
ATOM   2551  N   GLU B 111      28.738  -7.378  -3.175  1.00 37.14           N  
ANISOU 2551  N   GLU B 111     4628   5020   4462   -182   -274   -110       N  
ATOM   2552  CA  GLU B 111      28.482  -8.747  -2.734  1.00 45.33           C  
ANISOU 2552  CA  GLU B 111     5588   6039   5598   -206   -309   -100       C  
ATOM   2553  C   GLU B 111      27.110  -9.229  -3.190  1.00 41.29           C  
ANISOU 2553  C   GLU B 111     4942   5533   5214   -257   -414     47       C  
ATOM   2554  O   GLU B 111      26.939 -10.413  -3.501  1.00 37.52           O  
ANISOU 2554  O   GLU B 111     4423   5027   4806   -345   -515     26       O  
ATOM   2555  CB  GLU B 111      28.629  -8.848  -1.209  1.00 46.61           C  
ANISOU 2555  CB  GLU B 111     5733   6184   5793    -94   -181    -70       C  
ATOM   2556  CG  GLU B 111      27.895  -7.762  -0.427  1.00 52.19           C  
ANISOU 2556  CG  GLU B 111     6409   6904   6517     35    -74     57       C  
ATOM   2557  CD  GLU B 111      28.686  -6.438  -0.301  1.00 63.48           C  
ANISOU 2557  CD  GLU B 111     7970   8323   7826     92     -3    -31       C  
ATOM   2558  OE1 GLU B 111      29.367  -5.986  -1.267  1.00 52.66           O  
ANISOU 2558  OE1 GLU B 111     6680   6951   6376     12    -54   -124       O  
ATOM   2559  OE2 GLU B 111      28.618  -5.843   0.798  1.00 70.41           O  
ANISOU 2559  OE2 GLU B 111     8874   9190   8687    219    108     -5       O  
ATOM   2560  N   GLY B 112      26.137  -8.321  -3.280  1.00 37.86           N  
ANISOU 2560  N   GLY B 112     4439   5127   4820   -204   -405    192       N  
ATOM   2561  CA  GLY B 112      24.833  -8.676  -3.796  1.00 32.07           C  
ANISOU 2561  CA  GLY B 112     3557   4414   4214   -257   -522    339       C  
ATOM   2562  C   GLY B 112      24.814  -8.995  -5.277  1.00 45.32           C  
ANISOU 2562  C   GLY B 112     5272   6105   5841   -392   -707    275       C  
ATOM   2563  O   GLY B 112      23.856  -9.612  -5.750  1.00 45.34           O  
ANISOU 2563  O   GLY B 112     5157   6115   5955   -471   -846    363       O  
ATOM   2564  N   SER B 113      25.840  -8.585  -6.020  1.00 38.76           N  
ANISOU 2564  N   SER B 113     4600   5286   4841   -423   -714    129       N  
ATOM   2565  CA  SER B 113      25.880  -8.749  -7.470  1.00 34.33           C  
ANISOU 2565  CA  SER B 113     4103   4756   4184   -533   -872     64       C  
ATOM   2566  C   SER B 113      26.564 -10.040  -7.889  1.00 36.68           C  
ANISOU 2566  C   SER B 113     4467   5024   4446   -628   -950   -108       C  
ATOM   2567  O   SER B 113      26.565 -10.375  -9.074  1.00 39.35           O  
ANISOU 2567  O   SER B 113     4868   5387   4698   -717  -1091   -181       O  
ATOM   2568  CB  SER B 113      26.591  -7.548  -8.108  1.00 36.77           C  
ANISOU 2568  CB  SER B 113     4548   5103   4320   -511   -821     21       C  
ATOM   2569  OG  SER B 113      25.762  -6.383  -8.009  1.00 38.93           O  
ANISOU 2569  OG  SER B 113     4767   5389   4635   -431   -799    191       O  
ATOM   2570  N   ILE B 114      27.115 -10.778  -6.932  1.00 37.61           N  
ANISOU 2570  N   ILE B 114     4580   5087   4624   -599   -865   -172       N  
ATOM   2571  CA  ILE B 114      27.903 -11.960  -7.258  1.00 33.49           C  
ANISOU 2571  CA  ILE B 114     4137   4520   4069   -661   -921   -348       C  
ATOM   2572  C   ILE B 114      27.095 -13.006  -8.030  1.00 44.34           C  
ANISOU 2572  C   ILE B 114     5471   5853   5522   -776  -1122   -349       C  
ATOM   2573  O   ILE B 114      27.595 -13.513  -9.048  1.00 43.86           O  
ANISOU 2573  O   ILE B 114     5524   5792   5350   -840  -1221   -509       O  
ATOM   2574  CB  ILE B 114      28.552 -12.512  -5.978  1.00 33.48           C  
ANISOU 2574  CB  ILE B 114     4125   4461   4133   -592   -798   -383       C  
ATOM   2575  CG1 ILE B 114      29.640 -11.551  -5.486  1.00 29.74           C  
ANISOU 2575  CG1 ILE B 114     3729   4031   3540   -504   -639   -447       C  
ATOM   2576  CG2 ILE B 114      29.151 -13.863  -6.220  1.00 31.44           C  
ANISOU 2576  CG2 ILE B 114     3925   4132   3890   -642   -870   -534       C  
ATOM   2577  CD1 ILE B 114      30.288 -11.951  -4.181  1.00 29.29           C  
ANISOU 2577  CD1 ILE B 114     3666   3936   3528   -424   -529   -474       C  
ATOM   2578  N   PRO B 115      25.853 -13.347  -7.647  1.00 45.42           N  
ANISOU 2578  N   PRO B 115     5452   5958   5846   -810  -1196   -182       N  
ATOM   2579  CA  PRO B 115      25.113 -14.337  -8.451  1.00 49.53           C  
ANISOU 2579  CA  PRO B 115     5939   6430   6451   -944  -1416   -195       C  
ATOM   2580  C   PRO B 115      24.852 -13.879  -9.874  1.00 51.27           C  
ANISOU 2580  C   PRO B 115     6226   6724   6530  -1007  -1572   -237       C  
ATOM   2581  O   PRO B 115      25.144 -14.619 -10.819  1.00 54.92           O  
ANISOU 2581  O   PRO B 115     6801   7158   6907  -1089  -1715   -398       O  
ATOM   2582  CB  PRO B 115      23.812 -14.526  -7.660  1.00 48.15           C  
ANISOU 2582  CB  PRO B 115     5548   6233   6514   -960  -1433     34       C  
ATOM   2583  CG  PRO B 115      24.139 -14.058  -6.270  1.00 47.55           C  
ANISOU 2583  CG  PRO B 115     5433   6167   6468   -825  -1200    116       C  
ATOM   2584  CD  PRO B 115      25.048 -12.895  -6.495  1.00 37.80           C  
ANISOU 2584  CD  PRO B 115     4331   5003   5027   -733  -1086     24       C  
ATOM   2585  N   ARG B 116      24.312 -12.675 -10.062  1.00 48.72           N  
ANISOU 2585  N   ARG B 116     5849   6493   6169   -960  -1549    -97       N  
ATOM   2586  CA  ARG B 116      24.032 -12.211 -11.418  1.00 50.95           C  
ANISOU 2586  CA  ARG B 116     6199   6853   6307  -1014  -1705   -112       C  
ATOM   2587  C   ARG B 116      25.290 -12.213 -12.284  1.00 50.21           C  
ANISOU 2587  C   ARG B 116     6325   6790   5962  -1020  -1681   -328       C  
ATOM   2588  O   ARG B 116      25.244 -12.609 -13.452  1.00 55.08           O  
ANISOU 2588  O   ARG B 116     7039   7433   6455  -1099  -1850   -429       O  
ATOM   2589  CB  ARG B 116      23.390 -10.818 -11.387  1.00 47.34           C  
ANISOU 2589  CB  ARG B 116     5664   6477   5847   -934  -1657     80       C  
ATOM   2590  N   VAL B 117      26.427 -11.790 -11.732  1.00 49.81           N  
ANISOU 2590  N   VAL B 117     6353   6744   5829   -936  -1475   -403       N  
ATOM   2591  CA  VAL B 117      27.636 -11.705 -12.552  1.00 47.64           C  
ANISOU 2591  CA  VAL B 117     6258   6520   5322   -937  -1427   -585       C  
ATOM   2592  C   VAL B 117      28.219 -13.091 -12.839  1.00 43.03           C  
ANISOU 2592  C   VAL B 117     5759   5872   4717   -981  -1493   -794       C  
ATOM   2593  O   VAL B 117      28.721 -13.352 -13.940  1.00 43.14           O  
ANISOU 2593  O   VAL B 117     5915   5933   4543  -1013  -1556   -945       O  
ATOM   2594  CB  VAL B 117      28.664 -10.784 -11.881  1.00 42.79           C  
ANISOU 2594  CB  VAL B 117     5680   5933   4647   -846  -1198   -590       C  
ATOM   2595  CG1 VAL B 117      29.996 -10.877 -12.588  1.00 43.36           C  
ANISOU 2595  CG1 VAL B 117     5902   6058   4514   -850  -1128   -778       C  
ATOM   2596  CG2 VAL B 117      28.163  -9.342 -11.879  1.00 44.00           C  
ANISOU 2596  CG2 VAL B 117     5799   6135   4783   -804  -1153   -411       C  
ATOM   2597  N   LEU B 118      28.175 -13.996 -11.864  1.00 45.07           N  
ANISOU 2597  N   LEU B 118     5942   6021   5160   -973  -1474   -804       N  
ATOM   2598  CA  LEU B 118      28.774 -15.312 -12.059  1.00 46.93           C  
ANISOU 2598  CA  LEU B 118     6267   6170   5395   -998  -1529  -1002       C  
ATOM   2599  C   LEU B 118      27.954 -16.218 -12.960  1.00 50.15           C  
ANISOU 2599  C   LEU B 118     6705   6520   5831  -1112  -1779  -1056       C  
ATOM   2600  O   LEU B 118      28.386 -17.346 -13.202  1.00 58.30           O  
ANISOU 2600  O   LEU B 118     7831   7457   6865  -1132  -1847  -1234       O  
ATOM   2601  CB  LEU B 118      29.005 -16.006 -10.716  1.00 45.85           C  
ANISOU 2601  CB  LEU B 118     6052   5921   5448   -951  -1436   -981       C  
ATOM   2602  CG  LEU B 118      30.448 -15.868 -10.246  1.00 48.16           C  
ANISOU 2602  CG  LEU B 118     6414   6237   5646   -849  -1245  -1103       C  
ATOM   2603  CD1 LEU B 118      30.771 -14.411  -9.933  1.00 48.67           C  
ANISOU 2603  CD1 LEU B 118     6454   6415   5623   -788  -1087  -1008       C  
ATOM   2604  CD2 LEU B 118      30.701 -16.739  -9.059  1.00 48.40           C  
ANISOU 2604  CD2 LEU B 118     6393   6153   5845   -803  -1191  -1100       C  
ATOM   2605  N   LYS B 119      26.801 -15.772 -13.458  1.00 50.50           N  
ANISOU 2605  N   LYS B 119     6674   6611   5901  -1182  -1928   -915       N  
ATOM   2606  CA  LYS B 119      26.191 -16.456 -14.589  1.00 57.81           C  
ANISOU 2606  CA  LYS B 119     7667   7516   6781  -1294  -2187  -1002       C  
ATOM   2607  C   LYS B 119      26.920 -16.179 -15.899  1.00 61.48           C  
ANISOU 2607  C   LYS B 119     8339   8087   6933  -1279  -2210  -1175       C  
ATOM   2608  O   LYS B 119      26.633 -16.847 -16.896  1.00 62.93           O  
ANISOU 2608  O   LYS B 119     8630   8253   7029  -1356  -2419  -1303       O  
ATOM   2609  CB  LYS B 119      24.711 -16.066 -14.717  1.00 60.52           C  
ANISOU 2609  CB  LYS B 119     7845   7890   7258  -1373  -2357   -786       C  
ATOM   2610  CG  LYS B 119      23.798 -16.782 -13.710  1.00 61.28           C  
ANISOU 2610  CG  LYS B 119     7742   7866   7676  -1434  -2409   -643       C  
ATOM   2611  CD  LYS B 119      22.367 -16.277 -13.769  1.00 60.96           C  
ANISOU 2611  CD  LYS B 119     7500   7883   7780  -1494  -2544   -406       C  
ATOM   2612  N   GLU B 120      27.861 -15.232 -15.919  1.00 62.86           N  
ANISOU 2612  N   GLU B 120     8576   8371   6936  -1186  -2002  -1183       N  
ATOM   2613  CA  GLU B 120      28.555 -14.825 -17.136  1.00 64.92           C  
ANISOU 2613  CA  GLU B 120     9017   8759   6890  -1168  -1987  -1307       C  
ATOM   2614  C   GLU B 120      30.063 -14.976 -17.060  1.00 66.03           C  
ANISOU 2614  C   GLU B 120     9265   8925   6900  -1081  -1776  -1483       C  
ATOM   2615  O   GLU B 120      30.700 -15.193 -18.093  1.00 72.15           O  
ANISOU 2615  O   GLU B 120    10203   9773   7436  -1069  -1782  -1652       O  
ATOM   2616  CB  GLU B 120      28.241 -13.357 -17.475  1.00 68.18           C  
ANISOU 2616  CB  GLU B 120     9405   9307   7194  -1153  -1942  -1117       C  
ATOM   2617  CG  GLU B 120      26.765 -13.021 -17.531  1.00 77.31           C  
ANISOU 2617  CG  GLU B 120    10430  10463   8483  -1214  -2133   -914       C  
ATOM   2618  CD  GLU B 120      26.075 -13.629 -18.735  1.00 89.60           C  
ANISOU 2618  CD  GLU B 120    12070  12041   9933  -1309  -2416   -990       C  
ATOM   2619  OE1 GLU B 120      26.521 -13.378 -19.878  1.00 95.09           O  
ANISOU 2619  OE1 GLU B 120    12943  12846  10341  -1306  -2447  -1085       O  
ATOM   2620  OE2 GLU B 120      25.088 -14.366 -18.538  1.00 94.17           O  
ANISOU 2620  OE2 GLU B 120    12539  12530  10711  -1392  -2611   -952       O  
ATOM   2621  N   VAL B 121      30.650 -14.838 -15.877  1.00 57.89           N  
ANISOU 2621  N   VAL B 121     8140   7848   6008  -1014  -1589  -1445       N  
ATOM   2622  CA  VAL B 121      32.092 -14.839 -15.694  1.00 55.50           C  
ANISOU 2622  CA  VAL B 121     7898   7584   5606   -928  -1382  -1581       C  
ATOM   2623  C   VAL B 121      32.424 -15.766 -14.538  1.00 53.04           C  
ANISOU 2623  C   VAL B 121     7515   7134   5505   -883  -1332  -1636       C  
ATOM   2624  O   VAL B 121      31.833 -15.650 -13.459  1.00 54.14           O  
ANISOU 2624  O   VAL B 121     7519   7201   5849   -886  -1323  -1482       O  
ATOM   2625  CB  VAL B 121      32.643 -13.433 -15.391  1.00 60.27           C  
ANISOU 2625  CB  VAL B 121     8461   8297   6143   -888  -1187  -1456       C  
ATOM   2626  CG1 VAL B 121      34.147 -13.494 -15.152  1.00 61.08           C  
ANISOU 2626  CG1 VAL B 121     8594   8442   6173   -812   -986  -1593       C  
ATOM   2627  CG2 VAL B 121      32.337 -12.481 -16.508  1.00 62.99           C  
ANISOU 2627  CG2 VAL B 121     8881   8768   6284   -928  -1229  -1377       C  
ATOM   2628  N   THR B 122      33.387 -16.656 -14.752  1.00 49.27           N  
ANISOU 2628  N   THR B 122     7129   6625   4966   -828  -1290  -1846       N  
ATOM   2629  CA  THR B 122      33.984 -17.418 -13.670  1.00 53.95           C  
ANISOU 2629  CA  THR B 122     7667   7106   5726   -758  -1210  -1900       C  
ATOM   2630  C   THR B 122      35.361 -16.845 -13.352  1.00 45.91           C  
ANISOU 2630  C   THR B 122     6635   6191   4617   -662   -985  -1950       C  
ATOM   2631  O   THR B 122      36.281 -16.968 -14.178  1.00 48.55           O  
ANISOU 2631  O   THR B 122     7065   6612   4769   -616   -915  -2113       O  
ATOM   2632  CB  THR B 122      34.086 -18.896 -14.048  1.00 56.64           C  
ANISOU 2632  CB  THR B 122     8111   7311   6100   -749  -1334  -2099       C  
ATOM   2633  OG1 THR B 122      32.790 -19.360 -14.414  1.00 60.86           O  
ANISOU 2633  OG1 THR B 122     8652   7752   6721   -864  -1564  -2049       O  
ATOM   2634  CG2 THR B 122      34.565 -19.718 -12.857  1.00 57.96           C  
ANISOU 2634  CG2 THR B 122     8216   7340   6468   -677  -1272  -2118       C  
ATOM   2635  N   PRO B 123      35.550 -16.201 -12.206  1.00 48.56           N  
ANISOU 2635  N   PRO B 123     6853   6531   5065   -630   -867  -1818       N  
ATOM   2636  CA  PRO B 123      36.895 -15.735 -11.838  1.00 43.15           C  
ANISOU 2636  CA  PRO B 123     6141   5933   4320   -552   -677  -1874       C  
ATOM   2637  C   PRO B 123      37.824 -16.915 -11.657  1.00 44.67           C  
ANISOU 2637  C   PRO B 123     6359   6064   4548   -461   -649  -2056       C  
ATOM   2638  O   PRO B 123      37.393 -18.006 -11.294  1.00 41.83           O  
ANISOU 2638  O   PRO B 123     6011   5556   4328   -450   -757  -2090       O  
ATOM   2639  CB  PRO B 123      36.680 -15.012 -10.499  1.00 44.08           C  
ANISOU 2639  CB  PRO B 123     6140   6027   4583   -539   -609  -1701       C  
ATOM   2640  CG  PRO B 123      35.210 -14.866 -10.329  1.00 44.37           C  
ANISOU 2640  CG  PRO B 123     6138   5998   4722   -606   -733  -1538       C  
ATOM   2641  CD  PRO B 123      34.548 -15.924 -11.162  1.00 47.92           C  
ANISOU 2641  CD  PRO B 123     6657   6376   5176   -659   -906  -1619       C  
ATOM   2642  N   SER B 124      39.117 -16.677 -11.862  1.00 43.69           N  
ANISOU 2642  N   SER B 124     6234   6052   4316   -392   -499  -2161       N  
ATOM   2643  CA  SER B 124      40.089 -17.673 -11.445  1.00 45.97           C  
ANISOU 2643  CA  SER B 124     6510   6285   4673   -278   -449  -2296       C  
ATOM   2644  C   SER B 124      40.370 -17.593  -9.947  1.00 44.07           C  
ANISOU 2644  C   SER B 124     6148   5993   4604   -231   -401  -2210       C  
ATOM   2645  O   SER B 124      40.682 -18.609  -9.325  1.00 46.93           O  
ANISOU 2645  O   SER B 124     6498   6247   5088   -148   -428  -2273       O  
ATOM   2646  CB  SER B 124      41.378 -17.529 -12.263  1.00 47.36           C  
ANISOU 2646  CB  SER B 124     6709   6581   4706   -206   -298  -2364       C  
ATOM   2647  OG  SER B 124      41.991 -16.282 -12.063  1.00 50.32           O  
ANISOU 2647  OG  SER B 124     6993   7102   5023   -232   -162  -2287       O  
ATOM   2648  N   MET B 125      40.265 -16.415  -9.339  1.00 43.51           N  
ANISOU 2648  N   MET B 125     5999   5988   4543   -274   -337  -2059       N  
ATOM   2649  CA  MET B 125      40.355 -16.349  -7.893  1.00 40.19           C  
ANISOU 2649  CA  MET B 125     5488   5512   4272   -229   -314  -1964       C  
ATOM   2650  C   MET B 125      39.438 -15.250  -7.381  1.00 38.40           C  
ANISOU 2650  C   MET B 125     5226   5291   4073   -300   -320  -1775       C  
ATOM   2651  O   MET B 125      39.085 -14.304  -8.091  1.00 30.21           O  
ANISOU 2651  O   MET B 125     4215   4328   2935   -372   -306  -1719       O  
ATOM   2652  CB  MET B 125      41.803 -16.143  -7.377  1.00 44.71           C  
ANISOU 2652  CB  MET B 125     5984   6170   4834   -148   -192  -2036       C  
ATOM   2653  CG  MET B 125      42.484 -14.864  -7.773  1.00 46.35           C  
ANISOU 2653  CG  MET B 125     6155   6533   4924   -198    -76  -2020       C  
ATOM   2654  SD  MET B 125      44.024 -14.563  -6.833  1.00 45.11           S  
ANISOU 2654  SD  MET B 125     5868   6459   4814   -126     31  -2064       S  
ATOM   2655  CE  MET B 125      45.183 -15.576  -7.751  1.00 39.85           C  
ANISOU 2655  CE  MET B 125     5193   5862   4086    -29     94  -2263       C  
ATOM   2656  N   MET B 126      39.039 -15.404  -6.133  1.00 32.47           N  
ANISOU 2656  N   MET B 126     4423   4459   3456   -265   -336  -1672       N  
ATOM   2657  CA  MET B 126      38.161 -14.448  -5.498  1.00 33.05           C  
ANISOU 2657  CA  MET B 126     4462   4531   3566   -300   -329  -1499       C  
ATOM   2658  C   MET B 126      38.688 -14.219  -4.091  1.00 32.96           C  
ANISOU 2658  C   MET B 126     4395   4514   3615   -223   -264  -1459       C  
ATOM   2659  O   MET B 126      38.904 -15.176  -3.338  1.00 30.90           O  
ANISOU 2659  O   MET B 126     4116   4184   3441   -154   -286  -1476       O  
ATOM   2660  CB  MET B 126      36.712 -14.954  -5.497  1.00 39.68           C  
ANISOU 2660  CB  MET B 126     5298   5273   4504   -344   -439  -1385       C  
ATOM   2661  CG  MET B 126      35.668 -13.834  -5.512  1.00 53.69           C  
ANISOU 2661  CG  MET B 126     7047   7079   6272   -394   -440  -1224       C  
ATOM   2662  SD  MET B 126      33.980 -14.325  -5.992  1.00 58.59           S  
ANISOU 2662  SD  MET B 126     7642   7628   6990   -474   -587  -1101       S  
ATOM   2663  CE  MET B 126      34.322 -15.882  -6.748  1.00 30.54           C  
ANISOU 2663  CE  MET B 126     4157   3995   3451   -499   -697  -1273       C  
ATOM   2664  N   VAL B 127      38.937 -12.957  -3.748  1.00 26.96           N  
ANISOU 2664  N   VAL B 127     3619   3821   2803   -234   -191  -1409       N  
ATOM   2665  CA  VAL B 127      39.330 -12.599  -2.398  1.00 26.34           C  
ANISOU 2665  CA  VAL B 127     3507   3740   2762   -167   -147  -1372       C  
ATOM   2666  C   VAL B 127      38.137 -11.934  -1.711  1.00 28.45           C  
ANISOU 2666  C   VAL B 127     3776   3967   3067   -162   -145  -1210       C  
ATOM   2667  O   VAL B 127      37.452 -11.082  -2.291  1.00 32.09           O  
ANISOU 2667  O   VAL B 127     4256   4442   3495   -218   -142  -1141       O  
ATOM   2668  CB  VAL B 127      40.583 -11.704  -2.376  1.00 29.68           C  
ANISOU 2668  CB  VAL B 127     3912   4253   3112   -177    -76  -1452       C  
ATOM   2669  CG1 VAL B 127      40.361 -10.386  -3.135  1.00 30.20           C  
ANISOU 2669  CG1 VAL B 127     4010   4365   3101   -267    -38  -1407       C  
ATOM   2670  CG2 VAL B 127      40.988 -11.419  -0.944  1.00 25.88           C  
ANISOU 2670  CG2 VAL B 127     3406   3764   2662   -107    -60  -1430       C  
ATOM   2671  N   PHE B 128      37.887 -12.337  -0.482  1.00 27.53           N  
ANISOU 2671  N   PHE B 128     3640   3806   3016    -85   -142  -1144       N  
ATOM   2672  CA  PHE B 128      36.829 -11.775   0.332  1.00 26.80           C  
ANISOU 2672  CA  PHE B 128     3542   3687   2952    -50   -115   -993       C  
ATOM   2673  C   PHE B 128      37.482 -11.118   1.531  1.00 30.19           C  
ANISOU 2673  C   PHE B 128     3991   4144   3335     27    -59  -1008       C  
ATOM   2674  O   PHE B 128      38.325 -11.745   2.187  1.00 29.77           O  
ANISOU 2674  O   PHE B 128     3931   4097   3284     83    -69  -1072       O  
ATOM   2675  CB  PHE B 128      35.856 -12.861   0.775  1.00 25.90           C  
ANISOU 2675  CB  PHE B 128     3391   3503   2947    -26   -152   -881       C  
ATOM   2676  CG  PHE B 128      34.982 -13.346  -0.309  1.00 26.40           C  
ANISOU 2676  CG  PHE B 128     3434   3530   3067   -113   -227   -846       C  
ATOM   2677  CD1 PHE B 128      33.783 -12.727  -0.557  1.00 26.56           C  
ANISOU 2677  CD1 PHE B 128     3421   3556   3114   -146   -231   -715       C  
ATOM   2678  CD2 PHE B 128      35.371 -14.409  -1.113  1.00 26.92           C  
ANISOU 2678  CD2 PHE B 128     3517   3557   3156   -157   -303   -954       C  
ATOM   2679  CE1 PHE B 128      32.961 -13.174  -1.568  1.00 27.24           C  
ANISOU 2679  CE1 PHE B 128     3481   3615   3253   -234   -326   -683       C  
ATOM   2680  CE2 PHE B 128      34.546 -14.864  -2.120  1.00 33.75           C  
ANISOU 2680  CE2 PHE B 128     4378   4383   4063   -244   -395   -937       C  
ATOM   2681  CZ  PHE B 128      33.338 -14.245  -2.346  1.00 27.78           C  
ANISOU 2681  CZ  PHE B 128     3580   3640   3336   -290   -415   -798       C  
ATOM   2682  N   THR B 129      37.109  -9.855   1.797  1.00 26.95           N  
ANISOU 2682  N   THR B 129     3613   3745   2882     35    -13   -956       N  
ATOM   2683  CA  THR B 129      37.680  -9.056   2.880  1.00 25.01           C  
ANISOU 2683  CA  THR B 129     3411   3515   2578    101     26   -988       C  
ATOM   2684  C   THR B 129      36.987  -9.315   4.222  1.00 25.26           C  
ANISOU 2684  C   THR B 129     3453   3527   2617    218     59   -884       C  
ATOM   2685  O   THR B 129      37.642  -9.697   5.196  1.00 25.45           O  
ANISOU 2685  O   THR B 129     3493   3568   2610    288     52   -922       O  
ATOM   2686  CB  THR B 129      37.597  -7.558   2.537  1.00 27.56           C  
ANISOU 2686  CB  THR B 129     3785   3834   2853     60     58   -989       C  
ATOM   2687  OG1 THR B 129      36.225  -7.234   2.317  1.00 28.97           O  
ANISOU 2687  OG1 THR B 129     3960   3980   3066     78     79   -854       O  
ATOM   2688  CG2 THR B 129      38.394  -7.218   1.262  1.00 25.01           C  
ANISOU 2688  CG2 THR B 129     3456   3543   2504    -60     42  -1078       C  
ATOM   2689  N   ASN B 130      35.681  -9.062   4.302  1.00 25.46           N  
ANISOU 2689  N   ASN B 130     3466   3530   2677    247     99   -745       N  
ATOM   2690  CA  ASN B 130      34.907  -9.261   5.531  1.00 29.07           C  
ANISOU 2690  CA  ASN B 130     3924   3987   3136    365    160   -622       C  
ATOM   2691  C   ASN B 130      33.416  -9.173   5.212  1.00 26.33           C  
ANISOU 2691  C   ASN B 130     3512   3625   2866    366    196   -459       C  
ATOM   2692  O   ASN B 130      33.025  -8.703   4.142  1.00 37.33           O  
ANISOU 2692  O   ASN B 130     4884   5009   4292    290    168   -451       O  
ATOM   2693  CB  ASN B 130      35.295  -8.248   6.608  1.00 35.49           C  
ANISOU 2693  CB  ASN B 130     4831   4817   3838    462    209   -670       C  
ATOM   2694  CG  ASN B 130      35.312  -6.858   6.076  1.00 46.13           C  
ANISOU 2694  CG  ASN B 130     6233   6142   5153    427    220   -722       C  
ATOM   2695  OD1 ASN B 130      34.275  -6.339   5.663  1.00 46.75           O  
ANISOU 2695  OD1 ASN B 130     6292   6199   5270    435    258   -623       O  
ATOM   2696  ND2 ASN B 130      36.491  -6.247   6.037  1.00 43.29           N  
ANISOU 2696  ND2 ASN B 130     5931   5781   4735    381    181   -867       N  
ATOM   2697  N   PHE B 131      32.586  -9.652   6.147  1.00 29.04           N  
ANISOU 2697  N   PHE B 131     3816   3977   3240    455    259   -316       N  
ATOM   2698  CA  PHE B 131      31.139  -9.443   6.092  1.00 33.34           C  
ANISOU 2698  CA  PHE B 131     4279   4528   3862    483    316   -142       C  
ATOM   2699  C   PHE B 131      30.683  -8.836   7.415  1.00 43.22           C  
ANISOU 2699  C   PHE B 131     5569   5816   5036    647    444    -64       C  
ATOM   2700  O   PHE B 131      30.751  -9.492   8.457  1.00 45.05           O  
ANISOU 2700  O   PHE B 131     5810   6073   5235    723    493     -9       O  
ATOM   2701  CB  PHE B 131      30.373 -10.743   5.818  1.00 31.12           C  
ANISOU 2701  CB  PHE B 131     3877   4226   3723    415    277     -9       C  
ATOM   2702  CG  PHE B 131      30.669 -11.367   4.478  1.00 27.76           C  
ANISOU 2702  CG  PHE B 131     3425   3757   3365    265    146    -92       C  
ATOM   2703  CD1 PHE B 131      30.385 -10.701   3.312  1.00 37.96           C  
ANISOU 2703  CD1 PHE B 131     4706   5052   4665    189     94   -120       C  
ATOM   2704  CD2 PHE B 131      31.195 -12.645   4.400  1.00 29.98           C  
ANISOU 2704  CD2 PHE B 131     3703   3991   3698    211     76   -135       C  
ATOM   2705  CE1 PHE B 131      30.643 -11.280   2.076  1.00 38.08           C  
ANISOU 2705  CE1 PHE B 131     4715   5039   4713     62    -24   -202       C  
ATOM   2706  CE2 PHE B 131      31.461 -13.234   3.163  1.00 33.22           C  
ANISOU 2706  CE2 PHE B 131     4108   4358   4156     89    -41   -230       C  
ATOM   2707  CZ  PHE B 131      31.182 -12.544   2.001  1.00 32.99           C  
ANISOU 2707  CZ  PHE B 131     4075   4349   4111     15    -88   -266       C  
ATOM   2708  N   PHE B 132      30.190  -7.604   7.381  1.00 46.89           N  
ANISOU 2708  N   PHE B 132     6065   6284   5467    713    503    -53       N  
ATOM   2709  CA  PHE B 132      29.662  -6.955   8.574  1.00 45.67           C  
ANISOU 2709  CA  PHE B 132     5959   6163   5231    889    636     11       C  
ATOM   2710  C   PHE B 132      28.174  -6.685   8.389  1.00 49.25           C  
ANISOU 2710  C   PHE B 132     6288   6640   5785    945    717    197       C  
ATOM   2711  O   PHE B 132      27.733  -6.307   7.302  1.00 43.03           O  
ANISOU 2711  O   PHE B 132     5437   5826   5085    869    660    220       O  
ATOM   2712  CB  PHE B 132      30.426  -5.662   8.891  1.00 43.59           C  
ANISOU 2712  CB  PHE B 132     5860   5868   4834    953    642   -154       C  
ATOM   2713  CG  PHE B 132      31.851  -5.899   9.354  1.00 49.63           C  
ANISOU 2713  CG  PHE B 132     6730   6632   5497    923    571   -320       C  
ATOM   2714  CD1 PHE B 132      32.110  -6.464  10.601  1.00 56.37           C  
ANISOU 2714  CD1 PHE B 132     7630   7534   6255   1025    611   -307       C  
ATOM   2715  CD2 PHE B 132      32.927  -5.538   8.558  1.00 42.84           C  
ANISOU 2715  CD2 PHE B 132     5915   5731   4633    797    467   -477       C  
ATOM   2716  CE1 PHE B 132      33.427  -6.682  11.034  1.00 54.98           C  
ANISOU 2716  CE1 PHE B 132     7537   7363   5989   1004    527   -454       C  
ATOM   2717  CE2 PHE B 132      34.250  -5.753   8.981  1.00 44.73           C  
ANISOU 2717  CE2 PHE B 132     6221   5981   4795    770    397   -622       C  
ATOM   2718  CZ  PHE B 132      34.494  -6.331  10.216  1.00 48.68           C  
ANISOU 2718  CZ  PHE B 132     6761   6528   5209    875    418   -613       C  
ATOM   2719  N   ARG B 133      27.398  -6.907   9.455  1.00 60.53           N  
ANISOU 2719  N   ARG B 133     7671   8129   7197   1083    853    341       N  
ATOM   2720  CA  ARG B 133      25.945  -6.781   9.376  1.00 64.85           C  
ANISOU 2720  CA  ARG B 133     8061   8721   7859   1145    945    543       C  
ATOM   2721  C   ARG B 133      25.483  -5.333   9.272  1.00 67.13           C  
ANISOU 2721  C   ARG B 133     8398   8995   8114   1270   1009    520       C  
ATOM   2722  O   ARG B 133      24.342  -5.096   8.856  1.00 71.20           O  
ANISOU 2722  O   ARG B 133     8768   9536   8750   1300   1048    670       O  
ATOM   2723  CB  ARG B 133      25.297  -7.451  10.595  1.00 65.05           C  
ANISOU 2723  CB  ARG B 133     8018   8829   7870   1262   1096    716       C  
ATOM   2724  N   ASP B 134      26.343  -4.374   9.622  1.00 66.01           N  
ANISOU 2724  N   ASP B 134     8454   8803   7824   1338   1009    338       N  
ATOM   2725  CA  ASP B 134      26.027  -2.933   9.665  1.00 66.98           C  
ANISOU 2725  CA  ASP B 134     8669   8879   7902   1474   1069    292       C  
ATOM   2726  C   ASP B 134      24.934  -2.653  10.685  1.00 71.69           C  
ANISOU 2726  C   ASP B 134     9221   9547   8471   1702   1262    429       C  
ATOM   2727  O   ASP B 134      25.155  -2.816  11.888  1.00 74.54           O  
ANISOU 2727  O   ASP B 134     9673   9957   8691   1827   1362    405       O  
ATOM   2728  CB  ASP B 134      25.622  -2.389   8.285  1.00 48.32           C  
ANISOU 2728  CB  ASP B 134     6234   6460   5667   1378    977    324       C  
ATOM   2729  N   GLY B 140      19.371 -12.207  11.455  1.00 50.26           N  
ANISOU 2729  N   GLY B 140     4939   7233   6926   1018   1440   2112       N  
ATOM   2730  CA  GLY B 140      20.529 -12.983  11.022  1.00 55.71           C  
ANISOU 2730  CA  GLY B 140     5781   7793   7592    862   1251   1939       C  
ATOM   2731  C   GLY B 140      20.855 -12.791   9.537  1.00 66.50           C  
ANISOU 2731  C   GLY B 140     7166   9066   9036    704   1021   1761       C  
ATOM   2732  O   GLY B 140      20.952 -13.769   8.779  1.00 66.91           O  
ANISOU 2732  O   GLY B 140     7168   9022   9231    506    849   1753       O  
ATOM   2733  N   GLU B 141      21.061 -11.527   9.128  1.00 66.25           N  
ANISOU 2733  N   GLU B 141     6193   8279  10699   -937   1551   -704       N  
ATOM   2734  CA  GLU B 141      21.105 -11.161   7.710  1.00 65.25           C  
ANISOU 2734  CA  GLU B 141     5988   8099  10705   -832   1297   -657       C  
ATOM   2735  C   GLU B 141      22.423 -11.526   7.025  1.00 57.22           C  
ANISOU 2735  C   GLU B 141     5244   7009   9489   -798   1100   -600       C  
ATOM   2736  O   GLU B 141      22.417 -11.867   5.834  1.00 56.93           O  
ANISOU 2736  O   GLU B 141     5197   6946   9488   -809    885   -541       O  
ATOM   2737  CB  GLU B 141      20.837  -9.665   7.549  1.00 66.21           C  
ANISOU 2737  CB  GLU B 141     5918   8207  11030   -647   1311   -725       C  
ATOM   2738  N   ILE B 142      23.553 -11.455   7.733  1.00 50.70           N  
ANISOU 2738  N   ILE B 142     4651   6160   8453   -762   1166   -622       N  
ATOM   2739  CA  ILE B 142      24.816 -11.875   7.130  1.00 56.04           C  
ANISOU 2739  CA  ILE B 142     5562   6778   8952   -730    996   -576       C  
ATOM   2740  C   ILE B 142      24.751 -13.346   6.737  1.00 63.87           C  
ANISOU 2740  C   ILE B 142     6650   7735   9882   -868    899   -515       C  
ATOM   2741  O   ILE B 142      25.157 -13.731   5.633  1.00 61.64           O  
ANISOU 2741  O   ILE B 142     6430   7415   9577   -855    709   -490       O  
ATOM   2742  CB  ILE B 142      25.996 -11.598   8.079  1.00 55.80           C  
ANISOU 2742  CB  ILE B 142     5745   6736   8719   -681   1087   -603       C  
ATOM   2743  CG1 ILE B 142      26.263 -10.098   8.174  1.00 63.55           C  
ANISOU 2743  CG1 ILE B 142     6665   7724   9758   -534   1124   -667       C  
ATOM   2744  CG2 ILE B 142      27.264 -12.304   7.589  1.00 55.72           C  
ANISOU 2744  CG2 ILE B 142     5963   6673   8534   -667    931   -555       C  
ATOM   2745  CD1 ILE B 142      26.577  -9.469   6.847  1.00 67.62           C  
ANISOU 2745  CD1 ILE B 142     7133   8210  10351   -428    917   -638       C  
ATOM   2746  N   ASP B 143      24.223 -14.182   7.638  1.00 69.93           N  
ANISOU 2746  N   ASP B 143     7436   8514  10619  -1016   1033   -495       N  
ATOM   2747  CA  ASP B 143      24.150 -15.628   7.420  1.00 78.99           C  
ANISOU 2747  CA  ASP B 143     8696   9601  11715  -1164    949   -433       C  
ATOM   2748  C   ASP B 143      23.500 -15.988   6.085  1.00 71.50           C  
ANISOU 2748  C   ASP B 143     7627   8638  10903  -1203    769   -418       C  
ATOM   2749  O   ASP B 143      24.008 -16.841   5.348  1.00 71.00           O  
ANISOU 2749  O   ASP B 143     7709   8496  10772  -1233    612   -403       O  
ATOM   2750  CB  ASP B 143      23.377 -16.283   8.567  1.00 92.18           C  
ANISOU 2750  CB  ASP B 143    10346  11307  13373  -1345   1128   -401       C  
ATOM   2751  CG  ASP B 143      24.203 -16.423   9.826  1.00 99.70           C  
ANISOU 2751  CG  ASP B 143    11509  12251  14121  -1369   1251   -382       C  
ATOM   2752  OD1 ASP B 143      24.908 -17.449   9.945  1.00100.77           O  
ANISOU 2752  OD1 ASP B 143    11865  12290  14132  -1430   1161   -313       O  
ATOM   2753  OD2 ASP B 143      24.147 -15.515  10.688  1.00103.44           O  
ANISOU 2753  OD2 ASP B 143    11930  12808  14564  -1329   1427   -439       O  
ATOM   2754  N   ILE B 144      22.367 -15.360   5.763  1.00 64.42           N  
ANISOU 2754  N   ILE B 144     6459   7814  10202  -1207    785   -428       N  
ATOM   2755  CA  ILE B 144      21.678 -15.685   4.518  1.00 63.08           C  
ANISOU 2755  CA  ILE B 144     6164   7646  10159  -1267    598   -401       C  
ATOM   2756  C   ILE B 144      22.524 -15.301   3.316  1.00 60.29           C  
ANISOU 2756  C   ILE B 144     5900   7264   9743  -1153    395   -409       C  
ATOM   2757  O   ILE B 144      22.687 -16.091   2.382  1.00 65.34           O  
ANISOU 2757  O   ILE B 144     6632   7864  10331  -1224    230   -402       O  
ATOM   2758  CB  ILE B 144      20.303 -15.003   4.459  1.00 69.95           C  
ANISOU 2758  CB  ILE B 144     6697   8605  11275  -1280    645   -398       C  
ATOM   2759  CG1 ILE B 144      19.394 -15.547   5.551  1.00 71.94           C  
ANISOU 2759  CG1 ILE B 144     6846   8909  11579  -1433    852   -395       C  
ATOM   2760  CG2 ILE B 144      19.664 -15.217   3.087  1.00 69.72           C  
ANISOU 2760  CG2 ILE B 144     6538   8585  11367  -1340    411   -354       C  
ATOM   2761  CD1 ILE B 144      17.930 -15.366   5.244  1.00 77.85           C  
ANISOU 2761  CD1 ILE B 144     7252   9743  12584  -1505    851   -380       C  
ATOM   2762  N   MET B 145      23.062 -14.080   3.314  1.00 58.49           N  
ANISOU 2762  N   MET B 145     5650   7060   9513   -988    408   -431       N  
ATOM   2763  CA  MET B 145      23.795 -13.585   2.151  1.00 54.98           C  
ANISOU 2763  CA  MET B 145     5266   6612   9010   -899    220   -426       C  
ATOM   2764  C   MET B 145      25.042 -14.420   1.895  1.00 47.98           C  
ANISOU 2764  C   MET B 145     4652   5672   7908   -903    160   -451       C  
ATOM   2765  O   MET B 145      25.402 -14.698   0.742  1.00 43.23           O  
ANISOU 2765  O   MET B 145     4113   5071   7241   -920     -8   -459       O  
ATOM   2766  CB  MET B 145      24.165 -12.118   2.360  1.00 56.06           C  
ANISOU 2766  CB  MET B 145     5344   6769   9189   -737    260   -437       C  
ATOM   2767  CG  MET B 145      24.819 -11.455   1.165  1.00 63.95           C  
ANISOU 2767  CG  MET B 145     6380   7779  10138   -665     66   -409       C  
ATOM   2768  SD  MET B 145      25.979 -10.161   1.669  1.00 69.02           S  
ANISOU 2768  SD  MET B 145     7119   8408  10699   -498    133   -433       S  
ATOM   2769  CE  MET B 145      27.082 -11.087   2.715  1.00 72.34           C  
ANISOU 2769  CE  MET B 145     7793   8800  10893   -514    277   -484       C  
ATOM   2770  N   VAL B 146      25.710 -14.837   2.962  1.00 39.74           N  
ANISOU 2770  N   VAL B 146     3765   4583   6750   -891    294   -468       N  
ATOM   2771  CA  VAL B 146      26.895 -15.664   2.804  1.00 39.75           C  
ANISOU 2771  CA  VAL B 146     4003   4518   6581   -877    237   -492       C  
ATOM   2772  C   VAL B 146      26.521 -17.004   2.192  1.00 42.02           C  
ANISOU 2772  C   VAL B 146     4349   4739   6877  -1011    137   -499       C  
ATOM   2773  O   VAL B 146      27.240 -17.534   1.337  1.00 42.69           O  
ANISOU 2773  O   VAL B 146     4561   4787   6874   -996     18   -546       O  
ATOM   2774  CB  VAL B 146      27.592 -15.813   4.166  1.00 42.69           C  
ANISOU 2774  CB  VAL B 146     4516   4854   6851   -847    385   -483       C  
ATOM   2775  CG1 VAL B 146      28.695 -16.846   4.100  1.00 47.29           C  
ANISOU 2775  CG1 VAL B 146     5321   5345   7302   -837    319   -496       C  
ATOM   2776  CG2 VAL B 146      28.139 -14.457   4.602  1.00 43.62           C  
ANISOU 2776  CG2 VAL B 146     4605   5031   6936   -715    457   -498       C  
ATOM   2777  N   ASN B 147      25.373 -17.559   2.600  1.00 36.95           N  
ANISOU 2777  N   ASN B 147     3609   4086   6345  -1152    188   -462       N  
ATOM   2778  CA  ASN B 147      24.909 -18.827   2.035  1.00 37.24           C  
ANISOU 2778  CA  ASN B 147     3697   4048   6405  -1304     85   -467       C  
ATOM   2779  C   ASN B 147      24.648 -18.703   0.540  1.00 42.44           C  
ANISOU 2779  C   ASN B 147     4287   4750   7090  -1326    -99   -500       C  
ATOM   2780  O   ASN B 147      25.043 -19.574  -0.244  1.00 44.04           O  
ANISOU 2780  O   ASN B 147     4629   4884   7220  -1376   -216   -558       O  
ATOM   2781  CB  ASN B 147      23.648 -19.292   2.763  1.00 45.41           C  
ANISOU 2781  CB  ASN B 147     4605   5088   7559  -1470    180   -409       C  
ATOM   2782  CG  ASN B 147      23.955 -20.023   4.051  1.00 57.41           C  
ANISOU 2782  CG  ASN B 147     6279   6530   9005  -1530    312   -369       C  
ATOM   2783  OD1 ASN B 147      25.015 -20.626   4.194  1.00 63.14           O  
ANISOU 2783  OD1 ASN B 147     7228   7148   9613  -1482    275   -380       O  
ATOM   2784  ND2 ASN B 147      23.028 -19.976   4.999  1.00 60.73           N  
ANISOU 2784  ND2 ASN B 147     6573   7008   9493  -1641    464   -318       N  
ATOM   2785  N   ASN B 148      24.003 -17.610   0.123  1.00 49.67           N  
ANISOU 2785  N   ASN B 148     4991   5775   8108  -1292   -134   -468       N  
ATOM   2786  CA  ASN B 148      23.732 -17.401  -1.296  1.00 52.99           C  
ANISOU 2786  CA  ASN B 148     5342   6252   8538  -1330   -330   -473       C  
ATOM   2787  C   ASN B 148      25.021 -17.298  -2.096  1.00 49.78           C  
ANISOU 2787  C   ASN B 148     5116   5849   7950  -1242   -415   -538       C  
ATOM   2788  O   ASN B 148      25.112 -17.824  -3.212  1.00 48.90           O  
ANISOU 2788  O   ASN B 148     5073   5744   7761  -1323   -560   -587       O  
ATOM   2789  CB  ASN B 148      22.891 -16.141  -1.480  1.00 66.17           C  
ANISOU 2789  CB  ASN B 148     6750   8022  10370  -1286   -359   -404       C  
ATOM   2790  CG  ASN B 148      21.582 -16.202  -0.725  1.00 73.20           C  
ANISOU 2790  CG  ASN B 148     7422   8931  11460  -1366   -258   -358       C  
ATOM   2791  OD1 ASN B 148      21.074 -17.283  -0.437  1.00 76.55           O  
ANISOU 2791  OD1 ASN B 148     7871   9314  11902  -1516   -229   -359       O  
ATOM   2792  ND2 ASN B 148      21.029 -15.042  -0.399  1.00 76.35           N  
ANISOU 2792  ND2 ASN B 148     7601   9389  12020  -1271   -201   -321       N  
ATOM   2793  N   ILE B 149      26.027 -16.620  -1.541  1.00 39.06           N  
ANISOU 2793  N   ILE B 149     3832   4497   6512  -1088   -321   -546       N  
ATOM   2794  CA  ILE B 149      27.319 -16.524  -2.211  1.00 39.80           C  
ANISOU 2794  CA  ILE B 149     4082   4609   6433  -1006   -379   -610       C  
ATOM   2795  C   ILE B 149      27.967 -17.899  -2.302  1.00 44.95           C  
ANISOU 2795  C   ILE B 149     4934   5158   6988  -1043   -383   -703       C  
ATOM   2796  O   ILE B 149      28.543 -18.264  -3.336  1.00 45.51           O  
ANISOU 2796  O   ILE B 149     5100   5245   6945  -1057   -478   -789       O  
ATOM   2797  CB  ILE B 149      28.224 -15.524  -1.468  1.00 36.28           C  
ANISOU 2797  CB  ILE B 149     3660   4187   5937   -848   -273   -591       C  
ATOM   2798  CG1 ILE B 149      27.628 -14.114  -1.551  1.00 39.47           C  
ANISOU 2798  CG1 ILE B 149     3875   4668   6452   -802   -294   -515       C  
ATOM   2799  CG2 ILE B 149      29.706 -15.603  -1.966  1.00 31.36           C  
ANISOU 2799  CG2 ILE B 149     3203   3581   5130   -765   -302   -664       C  
ATOM   2800  CD1 ILE B 149      28.462 -13.047  -0.860  1.00 37.69           C  
ANISOU 2800  CD1 ILE B 149     3677   4457   6186   -661   -201   -504       C  
ATOM   2801  N   ALA B 150      27.904 -18.671  -1.213  1.00 40.62           N  
ANISOU 2801  N   ALA B 150     4455   4498   6482  -1060   -278   -690       N  
ATOM   2802  CA  ALA B 150      28.489 -20.011  -1.223  1.00 41.66           C  
ANISOU 2802  CA  ALA B 150     4778   4492   6560  -1086   -296   -766       C  
ATOM   2803  C   ALA B 150      27.865 -20.872  -2.310  1.00 42.96           C  
ANISOU 2803  C   ALA B 150     4959   4622   6741  -1234   -428   -833       C  
ATOM   2804  O   ALA B 150      28.575 -21.565  -3.047  1.00 53.29           O  
ANISOU 2804  O   ALA B 150     6409   5875   7963  -1223   -491   -953       O  
ATOM   2805  CB  ALA B 150      28.323 -20.677   0.140  1.00 36.66           C  
ANISOU 2805  CB  ALA B 150     4206   3740   5982  -1119   -187   -702       C  
ATOM   2806  N   GLU B 151      26.538 -20.826  -2.442  1.00 51.70           N  
ANISOU 2806  N   GLU B 151     5915   5767   7961  -1376   -469   -769       N  
ATOM   2807  CA  GLU B 151      25.875 -21.638  -3.462  1.00 55.45           C  
ANISOU 2807  CA  GLU B 151     6404   6216   8449  -1544   -610   -826       C  
ATOM   2808  C   GLU B 151      26.306 -21.224  -4.857  1.00 54.93           C  
ANISOU 2808  C   GLU B 151     6355   6259   8255  -1534   -736   -908       C  
ATOM   2809  O   GLU B 151      26.489 -22.065  -5.740  1.00 59.13           O  
ANISOU 2809  O   GLU B 151     7012   6746   8710  -1619   -827  -1028       O  
ATOM   2810  CB  GLU B 151      24.364 -21.522  -3.315  1.00 62.45           C  
ANISOU 2810  CB  GLU B 151     7085   7151   9491  -1697   -636   -724       C  
ATOM   2811  CG  GLU B 151      23.819 -22.432  -2.247  1.00 69.30           C  
ANISOU 2811  CG  GLU B 151     7980   7896  10455  -1800   -544   -675       C  
ATOM   2812  CD  GLU B 151      22.398 -22.096  -1.892  1.00 75.40           C  
ANISOU 2812  CD  GLU B 151     8505   8754  11390  -1923   -519   -568       C  
ATOM   2813  OE1 GLU B 151      22.037 -20.898  -2.005  1.00 77.60           O  
ANISOU 2813  OE1 GLU B 151     8584   9172  11729  -1847   -513   -516       O  
ATOM   2814  OE2 GLU B 151      21.649 -23.027  -1.514  1.00 68.34           O  
ANISOU 2814  OE2 GLU B 151     7610   7783  10574  -2096   -510   -537       O  
ATOM   2815  N   THR B 152      26.511 -19.929  -5.053  1.00 48.98           N  
ANISOU 2815  N   THR B 152     5491   5648   7471  -1439   -739   -848       N  
ATOM   2816  CA  THR B 152      26.869 -19.401  -6.356  1.00 50.50           C  
ANISOU 2816  CA  THR B 152     5690   5970   7528  -1454   -863   -891       C  
ATOM   2817  C   THR B 152      28.257 -19.845  -6.797  1.00 49.93           C  
ANISOU 2817  C   THR B 152     5815   5879   7277  -1374   -834  -1042       C  
ATOM   2818  O   THR B 152      28.469 -20.126  -7.979  1.00 51.71           O  
ANISOU 2818  O   THR B 152     6112   6168   7369  -1458   -933  -1147       O  
ATOM   2819  CB  THR B 152      26.788 -17.882  -6.297  1.00 48.34           C  
ANISOU 2819  CB  THR B 152     5257   5823   7287  -1366   -870   -768       C  
ATOM   2820  OG1 THR B 152      25.458 -17.521  -5.918  1.00 61.76           O  
ANISOU 2820  OG1 THR B 152     6750   7533   9182  -1429   -893   -649       O  
ATOM   2821  CG2 THR B 152      27.123 -17.272  -7.626  1.00 44.09           C  
ANISOU 2821  CG2 THR B 152     4727   5426   6600  -1407  -1013   -778       C  
ATOM   2822  N   ILE B 153      29.233 -19.882  -5.884  1.00 47.96           N  
ANISOU 2822  N   ILE B 153     5646   5558   7017  -1215   -699  -1061       N  
ATOM   2823  CA  ILE B 153      30.610 -20.135  -6.309  1.00 48.91           C  
ANISOU 2823  CA  ILE B 153     5910   5687   6988  -1115   -667  -1200       C  
ATOM   2824  C   ILE B 153      31.034 -21.584  -6.125  1.00 49.03           C  
ANISOU 2824  C   ILE B 153     6089   5516   7023  -1107   -637  -1336       C  
ATOM   2825  O   ILE B 153      32.168 -21.931  -6.474  1.00 54.18           O  
ANISOU 2825  O   ILE B 153     6848   6156   7581  -1012   -604  -1475       O  
ATOM   2826  CB  ILE B 153      31.612 -19.186  -5.614  1.00 49.42           C  
ANISOU 2826  CB  ILE B 153     5956   5808   7015   -939   -566  -1144       C  
ATOM   2827  CG1 ILE B 153      31.748 -19.474  -4.120  1.00 45.44           C  
ANISOU 2827  CG1 ILE B 153     5479   5167   6619   -849   -451  -1079       C  
ATOM   2828  CG2 ILE B 153      31.206 -17.735  -5.827  1.00 42.95           C  
ANISOU 2828  CG2 ILE B 153     4986   5140   6193   -945   -608  -1014       C  
ATOM   2829  CD1 ILE B 153      32.353 -18.256  -3.348  1.00 43.11           C  
ANISOU 2829  CD1 ILE B 153     5124   4950   6304   -718   -369   -986       C  
ATOM   2830  N   SER B 154      30.150 -22.448  -5.634  1.00 45.55           N  
ANISOU 2830  N   SER B 154     5666   4928   6713  -1209   -652  -1304       N  
ATOM   2831  CA  SER B 154      30.536 -23.819  -5.330  1.00 52.51           C  
ANISOU 2831  CA  SER B 154     6713   5593   7644  -1198   -635  -1409       C  
ATOM   2832  C   SER B 154      30.911 -24.611  -6.580  1.00 53.42           C  
ANISOU 2832  C   SER B 154     6949   5680   7668  -1249   -706  -1624       C  
ATOM   2833  O   SER B 154      30.278 -24.484  -7.628  1.00 53.40           O  
ANISOU 2833  O   SER B 154     6911   5787   7593  -1397   -802  -1668       O  
ATOM   2834  CB  SER B 154      29.402 -24.535  -4.610  1.00 56.65           C  
ANISOU 2834  CB  SER B 154     7228   5976   8320  -1338   -650  -1311       C  
ATOM   2835  OG  SER B 154      29.511 -25.927  -4.810  1.00 67.56           O  
ANISOU 2835  OG  SER B 154     8776   7149   9744  -1397   -696  -1434       O  
ATOM   2836  N   ASN B 155      31.934 -25.461  -6.438  1.00 54.51           N  
ANISOU 2836  N   ASN B 155     7230   5664   7816  -1128   -660  -1763       N  
ATOM   2837  CA  ASN B 155      32.330 -26.440  -7.455  1.00 57.30           C  
ANISOU 2837  CA  ASN B 155     7721   5934   8118  -1159   -701  -2006       C  
ATOM   2838  C   ASN B 155      32.589 -25.790  -8.805  1.00 56.29           C  
ANISOU 2838  C   ASN B 155     7557   6046   7786  -1207   -727  -2127       C  
ATOM   2839  O   ASN B 155      32.330 -26.373  -9.854  1.00 57.72           O  
ANISOU 2839  O   ASN B 155     7814   6229   7888  -1340   -793  -2296       O  
ATOM   2840  CB  ASN B 155      31.300 -27.561  -7.592  1.00 64.19           C  
ANISOU 2840  CB  ASN B 155     8677   6621   9093  -1347   -792  -2041       C  
ATOM   2841  CG  ASN B 155      31.586 -28.707  -6.656  1.00 72.36           C  
ANISOU 2841  CG  ASN B 155     9843   7352  10297  -1280   -773  -2046       C  
ATOM   2842  OD1 ASN B 155      31.025 -28.782  -5.562  1.00 80.46           O  
ANISOU 2842  OD1 ASN B 155    10841   8288  11441  -1317   -764  -1854       O  
ATOM   2843  ND2 ASN B 155      32.500 -29.587  -7.058  1.00 64.24           N  
ANISOU 2843  ND2 ASN B 155     8957   6166   9285  -1176   -763  -2265       N  
ATOM   2844  N   LYS B 156      33.117 -24.576  -8.790  1.00 48.08           N  
ANISOU 2844  N   LYS B 156     6411   5210   6646  -1116   -679  -2040       N  
ATOM   2845  CA  LYS B 156      33.511 -23.926 -10.020  1.00 50.81           C  
ANISOU 2845  CA  LYS B 156     6734   5792   6781  -1164   -698  -2137       C  
ATOM   2846  C   LYS B 156      35.018 -23.882 -10.210  1.00 48.84           C  
ANISOU 2846  C   LYS B 156     6523   5598   6435   -991   -586  -2291       C  
ATOM   2847  O   LYS B 156      35.478 -23.313 -11.200  1.00 55.17           O  
ANISOU 2847  O   LYS B 156     7306   6617   7040  -1034   -580  -2373       O  
ATOM   2848  CB  LYS B 156      32.910 -22.520 -10.067  1.00 51.97           C  
ANISOU 2848  CB  LYS B 156     6725   6143   6878  -1227   -753  -1920       C  
ATOM   2849  CG  LYS B 156      31.401 -22.572 -10.086  1.00 51.12           C  
ANISOU 2849  CG  LYS B 156     6549   6009   6867  -1408   -872  -1794       C  
ATOM   2850  CD  LYS B 156      30.786 -21.208 -10.199  1.00 54.49           C  
ANISOU 2850  CD  LYS B 156     6809   6616   7278  -1455   -941  -1592       C  
ATOM   2851  CE  LYS B 156      29.661 -21.244 -11.197  1.00 61.42           C  
ANISOU 2851  CE  LYS B 156     7642   7579   8116  -1682  -1110  -1568       C  
ATOM   2852  NZ  LYS B 156      28.662 -20.175 -10.950  1.00 66.50           N  
ANISOU 2852  NZ  LYS B 156     8091   8307   8869  -1723  -1194  -1335       N  
ATOM   2853  N   GLY B 157      35.794 -24.490  -9.310  1.00 50.17           N  
ANISOU 2853  N   GLY B 157     6741   5585   6738   -808   -505  -2328       N  
ATOM   2854  CA  GLY B 157      37.241 -24.444  -9.413  1.00 46.18           C  
ANISOU 2854  CA  GLY B 157     6240   5133   6174   -629   -400  -2465       C  
ATOM   2855  C   GLY B 157      37.869 -23.107  -9.063  1.00 46.98           C  
ANISOU 2855  C   GLY B 157     6220   5437   6194   -542   -349  -2314       C  
ATOM   2856  O   GLY B 157      39.042 -22.879  -9.375  1.00 49.19           O  
ANISOU 2856  O   GLY B 157     6475   5832   6383   -433   -267  -2424       O  
ATOM   2857  N   ILE B 158      37.127 -22.213  -8.423  1.00 41.91           N  
ANISOU 2857  N   ILE B 158     5496   4840   5589   -590   -389  -2074       N  
ATOM   2858  CA  ILE B 158      37.645 -20.884  -8.108  1.00 37.31           C  
ANISOU 2858  CA  ILE B 158     4809   4433   4934   -525   -353  -1932       C  
ATOM   2859  C   ILE B 158      38.554 -20.985  -6.897  1.00 39.44           C  
ANISOU 2859  C   ILE B 158     5079   4594   5311   -333   -274  -1885       C  
ATOM   2860  O   ILE B 158      38.195 -21.602  -5.888  1.00 44.94           O  
ANISOU 2860  O   ILE B 158     5819   5091   6165   -295   -278  -1812       O  
ATOM   2861  CB  ILE B 158      36.505 -19.897  -7.834  1.00 34.91           C  
ANISOU 2861  CB  ILE B 158     4415   4192   4659   -631   -423  -1712       C  
ATOM   2862  CG1 ILE B 158      35.575 -19.802  -9.042  1.00 48.11           C  
ANISOU 2862  CG1 ILE B 158     6074   5970   6235   -829   -533  -1734       C  
ATOM   2863  CG2 ILE B 158      37.087 -18.504  -7.390  1.00 33.12           C  
ANISOU 2863  CG2 ILE B 158     4095   4107   4383   -551   -385  -1568       C  
ATOM   2864  CD1 ILE B 158      34.229 -19.181  -8.724  1.00 43.11           C  
ANISOU 2864  CD1 ILE B 158     5341   5335   5703   -930   -620  -1535       C  
ATOM   2865  N   LYS B 159      39.737 -20.395  -6.994  1.00 34.76           N  
ANISOU 2865  N   LYS B 159     4439   4142   4628   -229   -210  -1917       N  
ATOM   2866  CA  LYS B 159      40.589 -20.285  -5.829  1.00 33.61           C  
ANISOU 2866  CA  LYS B 159     4274   3928   4569    -64   -158  -1839       C  
ATOM   2867  C   LYS B 159      40.032 -19.178  -4.935  1.00 37.05           C  
ANISOU 2867  C   LYS B 159     4651   4402   5025    -95   -172  -1606       C  
ATOM   2868  O   LYS B 159      39.874 -18.038  -5.375  1.00 41.18           O  
ANISOU 2868  O   LYS B 159     5104   5100   5444   -164   -188  -1532       O  
ATOM   2869  CB  LYS B 159      42.028 -19.996  -6.251  1.00 36.43           C  
ANISOU 2869  CB  LYS B 159     4579   4437   4827     44    -87  -1951       C  
ATOM   2870  CG  LYS B 159      42.986 -19.877  -5.066  1.00 33.64           C  
ANISOU 2870  CG  LYS B 159     4194   4026   4563    209    -52  -1865       C  
ATOM   2871  CD  LYS B 159      44.391 -19.475  -5.498  1.00 36.50           C  
ANISOU 2871  CD  LYS B 159     4469   4569   4829    302     16  -1962       C  
ATOM   2872  CE  LYS B 159      45.227 -20.651  -5.991  1.00 38.55           C  
ANISOU 2872  CE  LYS B 159     4739   4757   5152    423     66  -2203       C  
ATOM   2873  NZ  LYS B 159      46.469 -20.115  -6.632  1.00 44.04           N  
ANISOU 2873  NZ  LYS B 159     5320   5692   5721    473    151  -2311       N  
ATOM   2874  N   LEU B 160      39.702 -19.509  -3.692  1.00 31.90           N  
ANISOU 2874  N   LEU B 160     4032   3582   4507    -55   -168  -1494       N  
ATOM   2875  CA  LEU B 160      39.151 -18.540  -2.746  1.00 29.78           C  
ANISOU 2875  CA  LEU B 160     3714   3338   4264    -82   -158  -1303       C  
ATOM   2876  C   LEU B 160      40.224 -18.088  -1.771  1.00 28.89           C  
ANISOU 2876  C   LEU B 160     3592   3242   4141     43   -112  -1235       C  
ATOM   2877  O   LEU B 160      40.913 -18.923  -1.172  1.00 29.93           O  
ANISOU 2877  O   LEU B 160     3782   3252   4339    141   -105  -1262       O  
ATOM   2878  CB  LEU B 160      37.987 -19.121  -1.955  1.00 30.07           C  
ANISOU 2878  CB  LEU B 160     3788   3210   4426   -155   -170  -1216       C  
ATOM   2879  CG  LEU B 160      36.809 -19.602  -2.788  1.00 37.13           C  
ANISOU 2879  CG  LEU B 160     4681   4077   5350   -298   -229  -1262       C  
ATOM   2880  CD1 LEU B 160      35.668 -20.077  -1.862  1.00 32.86           C  
ANISOU 2880  CD1 LEU B 160     4153   3393   4938   -382   -226  -1154       C  
ATOM   2881  CD2 LEU B 160      36.367 -18.503  -3.721  1.00 36.00           C  
ANISOU 2881  CD2 LEU B 160     4439   4122   5117   -378   -269  -1238       C  
ATOM   2882  N   LEU B 161      40.362 -16.764  -1.602  1.00 27.64           N  
ANISOU 2882  N   LEU B 161     3365   3225   3913     34    -95  -1141       N  
ATOM   2883  CA  LEU B 161      41.272 -16.226  -0.599  1.00 26.82           C  
ANISOU 2883  CA  LEU B 161     3256   3143   3793    123    -60  -1063       C  
ATOM   2884  C   LEU B 161      40.397 -15.663   0.511  1.00 30.57           C  
ANISOU 2884  C   LEU B 161     3734   3562   4318     72    -35   -923       C  
ATOM   2885  O   LEU B 161      39.718 -14.646   0.328  1.00 29.10           O  
ANISOU 2885  O   LEU B 161     3486   3451   4118      8    -33   -867       O  
ATOM   2886  CB  LEU B 161      42.231 -15.191  -1.191  1.00 27.21           C  
ANISOU 2886  CB  LEU B 161     3236   3384   3720    145    -54  -1079       C  
ATOM   2887  CG  LEU B 161      42.834 -15.458  -2.588  1.00 33.87           C  
ANISOU 2887  CG  LEU B 161     4048   4349   4471    141    -59  -1229       C  
ATOM   2888  CD1 LEU B 161      44.056 -14.582  -2.839  1.00 28.20           C  
ANISOU 2888  CD1 LEU B 161     3263   3813   3639    175    -35  -1230       C  
ATOM   2889  CD2 LEU B 161      43.169 -16.919  -2.906  1.00 37.08           C  
ANISOU 2889  CD2 LEU B 161     4504   4645   4938    210    -50  -1386       C  
ATOM   2890  N   LEU B 162      40.390 -16.344   1.651  1.00 36.20           N  
ANISOU 2890  N   LEU B 162     4518   4142   5094     97    -18   -868       N  
ATOM   2891  CA  LEU B 162      39.478 -16.030   2.733  1.00 26.07           C  
ANISOU 2891  CA  LEU B 162     3248   2806   3850     28     28   -758       C  
ATOM   2892  C   LEU B 162      40.232 -15.473   3.940  1.00 25.54           C  
ANISOU 2892  C   LEU B 162     3215   2761   3729     72     62   -676       C  
ATOM   2893  O   LEU B 162      41.331 -15.932   4.278  1.00 25.92           O  
ANISOU 2893  O   LEU B 162     3308   2784   3755    152     30   -675       O  
ATOM   2894  CB  LEU B 162      38.681 -17.272   3.141  1.00 27.16           C  
ANISOU 2894  CB  LEU B 162     3456   2782   4081    -33     23   -742       C  
ATOM   2895  CG  LEU B 162      37.968 -18.037   2.027  1.00 30.47           C  
ANISOU 2895  CG  LEU B 162     3866   3154   4558    -91    -24   -831       C  
ATOM   2896  CD1 LEU B 162      37.251 -19.221   2.661  1.00 29.20           C  
ANISOU 2896  CD1 LEU B 162     3786   2817   4490   -166    -31   -791       C  
ATOM   2897  CD2 LEU B 162      36.989 -17.158   1.218  1.00 27.61           C  
ANISOU 2897  CD2 LEU B 162     3394   2905   4192   -173    -28   -835       C  
ATOM   2898  N   ASN B 163      39.637 -14.463   4.566  1.00 24.97           N  
ANISOU 2898  N   ASN B 163     3112   2735   3641     18    122   -613       N  
ATOM   2899  CA  ASN B 163      40.091 -13.901   5.837  1.00 24.72           C  
ANISOU 2899  CA  ASN B 163     3128   2718   3545     21    167   -541       C  
ATOM   2900  C   ASN B 163      39.801 -14.916   6.938  1.00 30.50           C  
ANISOU 2900  C   ASN B 163     3960   3333   4295    -28    186   -474       C  
ATOM   2901  O   ASN B 163      38.667 -15.042   7.390  1.00 26.48           O  
ANISOU 2901  O   ASN B 163     3452   2784   3826   -122    252   -447       O  
ATOM   2902  CB  ASN B 163      39.350 -12.598   6.107  1.00 24.21           C  
ANISOU 2902  CB  ASN B 163     3003   2716   3481    -28    239   -526       C  
ATOM   2903  CG  ASN B 163      39.799 -11.894   7.380  1.00 24.94           C  
ANISOU 2903  CG  ASN B 163     3153   2833   3490    -40    295   -478       C  
ATOM   2904  OD1 ASN B 163      40.526 -12.442   8.219  1.00 24.50           O  
ANISOU 2904  OD1 ASN B 163     3189   2751   3368    -36    277   -430       O  
ATOM   2905  ND2 ASN B 163      39.390 -10.630   7.502  1.00 24.06           N  
ANISOU 2905  ND2 ASN B 163     2989   2770   3384    -58    351   -492       N  
ATOM   2906  N   ALA B 164      40.827 -15.604   7.415  1.00 27.81           N  
ANISOU 2906  N   ALA B 164     3698   2942   3926     26    124   -438       N  
ATOM   2907  CA  ALA B 164      40.602 -16.605   8.451  1.00 33.00           C  
ANISOU 2907  CA  ALA B 164     4467   3477   4596    -35    114   -347       C  
ATOM   2908  C   ALA B 164      39.999 -15.998   9.716  1.00 27.49           C  
ANISOU 2908  C   ALA B 164     3812   2819   3815   -151    211   -270       C  
ATOM   2909  O   ALA B 164      39.224 -16.664  10.394  1.00 28.52           O  
ANISOU 2909  O   ALA B 164     4007   2875   3956   -259    248   -207       O  
ATOM   2910  CB  ALA B 164      41.913 -17.314   8.777  1.00 31.62           C  
ANISOU 2910  CB  ALA B 164     4357   3241   4417     57      6   -303       C  
ATOM   2911  N   ASP B 165      40.328 -14.737  10.036  1.00 26.69           N  
ANISOU 2911  N   ASP B 165     3680   2835   3627   -142    261   -282       N  
ATOM   2912  CA  ASP B 165      39.856 -14.070  11.248  1.00 31.50           C  
ANISOU 2912  CA  ASP B 165     4335   3490   4142   -248    369   -243       C  
ATOM   2913  C   ASP B 165      38.371 -13.694  11.215  1.00 31.88           C  
ANISOU 2913  C   ASP B 165     4307   3551   4254   -329    501   -290       C  
ATOM   2914  O   ASP B 165      37.827 -13.339  12.260  1.00 32.80           O  
ANISOU 2914  O   ASP B 165     4459   3699   4303   -429    618   -275       O  
ATOM   2915  CB  ASP B 165      40.675 -12.785  11.514  1.00 26.32           C  
ANISOU 2915  CB  ASP B 165     3669   2941   3389   -212    377   -265       C  
ATOM   2916  CG  ASP B 165      42.178 -13.048  11.742  1.00 28.55           C  
ANISOU 2916  CG  ASP B 165     4009   3238   3601   -148    251   -207       C  
ATOM   2917  OD1 ASP B 165      42.583 -14.173  12.124  1.00 31.46           O  
ANISOU 2917  OD1 ASP B 165     4453   3526   3975   -146    167   -126       O  
ATOM   2918  OD2 ASP B 165      42.957 -12.093  11.568  1.00 31.57           O  
ANISOU 2918  OD2 ASP B 165     4355   3709   3933   -104    228   -235       O  
ATOM   2919  N   ASP B 166      37.711 -13.730  10.058  1.00 30.06           N  
ANISOU 2919  N   ASP B 166     3966   3307   4149   -294    489   -352       N  
ATOM   2920  CA  ASP B 166      36.284 -13.439   9.983  1.00 28.91           C  
ANISOU 2920  CA  ASP B 166     3720   3171   4094   -365    595   -387       C  
ATOM   2921  C   ASP B 166      35.518 -14.753   9.832  1.00 28.28           C  
ANISOU 2921  C   ASP B 166     3654   3003   4089   -445    577   -353       C  
ATOM   2922  O   ASP B 166      35.655 -15.417   8.807  1.00 33.23           O  
ANISOU 2922  O   ASP B 166     4266   3575   4783   -401    473   -375       O  
ATOM   2923  CB  ASP B 166      35.992 -12.501   8.805  1.00 26.41           C  
ANISOU 2923  CB  ASP B 166     3263   2902   3871   -291    569   -458       C  
ATOM   2924  CG  ASP B 166      34.534 -12.055   8.737  1.00 39.21           C  
ANISOU 2924  CG  ASP B 166     4747   4535   5616   -345    665   -491       C  
ATOM   2925  OD1 ASP B 166      33.625 -12.827   9.140  1.00 40.23           O  
ANISOU 2925  OD1 ASP B 166     4865   4631   5790   -442    728   -470       O  
ATOM   2926  OD2 ASP B 166      34.287 -10.910   8.281  1.00 34.25           O  
ANISOU 2926  OD2 ASP B 166     4013   3945   5054   -292    672   -534       O  
ATOM   2927  N   PRO B 167      34.726 -15.174  10.819  1.00 29.56           N  
ANISOU 2927  N   PRO B 167     3850   3149   4231   -577    679   -304       N  
ATOM   2928  CA  PRO B 167      34.029 -16.462  10.686  1.00 33.10           C  
ANISOU 2928  CA  PRO B 167     4323   3503   4751   -675    649   -257       C  
ATOM   2929  C   PRO B 167      33.009 -16.480   9.562  1.00 36.97           C  
ANISOU 2929  C   PRO B 167     4662   3992   5392   -681    637   -319       C  
ATOM   2930  O   PRO B 167      32.738 -17.556   9.026  1.00 32.42           O  
ANISOU 2930  O   PRO B 167     4112   3322   4883   -726    556   -305       O  
ATOM   2931  CB  PRO B 167      33.361 -16.663  12.061  1.00 32.21           C  
ANISOU 2931  CB  PRO B 167     4264   3415   4560   -842    787   -188       C  
ATOM   2932  CG  PRO B 167      33.201 -15.236  12.622  1.00 31.90           C  
ANISOU 2932  CG  PRO B 167     4151   3504   4464   -822    933   -259       C  
ATOM   2933  CD  PRO B 167      34.416 -14.475  12.084  1.00 30.25           C  
ANISOU 2933  CD  PRO B 167     3958   3313   4222   -660    832   -298       C  
ATOM   2934  N   PHE B 168      32.428 -15.343   9.171  1.00 30.19           N  
ANISOU 2934  N   PHE B 168     3649   3224   4599   -642    700   -385       N  
ATOM   2935  CA  PHE B 168      31.464 -15.436   8.083  1.00 36.18           C  
ANISOU 2935  CA  PHE B 168     4262   3981   5503   -660    655   -422       C  
ATOM   2936  C   PHE B 168      32.144 -15.507   6.721  1.00 32.65           C  
ANISOU 2936  C   PHE B 168     3819   3517   5068   -562    497   -464       C  
ATOM   2937  O   PHE B 168      31.623 -16.160   5.806  1.00 39.04           O  
ANISOU 2937  O   PHE B 168     4588   4290   5954   -605    415   -482       O  
ATOM   2938  CB  PHE B 168      30.463 -14.291   8.162  1.00 47.13           C  
ANISOU 2938  CB  PHE B 168     5464   5454   6991   -659    764   -463       C  
ATOM   2939  CG  PHE B 168      29.506 -14.430   9.313  1.00 59.54           C  
ANISOU 2939  CG  PHE B 168     6993   7055   8576   -786    939   -447       C  
ATOM   2940  CD1 PHE B 168      28.673 -15.543   9.398  1.00 66.08           C  
ANISOU 2940  CD1 PHE B 168     7809   7846   9454   -931    949   -400       C  
ATOM   2941  CD2 PHE B 168      29.450 -13.476  10.313  1.00 61.90           C  
ANISOU 2941  CD2 PHE B 168     7269   7422   8828   -775   1097   -486       C  
ATOM   2942  CE1 PHE B 168      27.797 -15.692  10.456  1.00 68.82           C  
ANISOU 2942  CE1 PHE B 168     8110   8242   9797  -1071   1123   -382       C  
ATOM   2943  CE2 PHE B 168      28.577 -13.617  11.371  1.00 69.32           C  
ANISOU 2943  CE2 PHE B 168     8167   8412   9759   -906   1281   -489       C  
ATOM   2944  CZ  PHE B 168      27.748 -14.729  11.444  1.00 72.09           C  
ANISOU 2944  CZ  PHE B 168     8495   8744  10153  -1058   1297   -431       C  
ATOM   2945  N   VAL B 169      33.309 -14.891   6.571  1.00 28.23           N  
ANISOU 2945  N   VAL B 169     3312   2994   4422   -448    455   -483       N  
ATOM   2946  CA  VAL B 169      34.085 -15.094   5.356  1.00 31.53           C  
ANISOU 2946  CA  VAL B 169     3749   3411   4820   -371    324   -529       C  
ATOM   2947  C   VAL B 169      34.578 -16.535   5.286  1.00 28.88           C  
ANISOU 2947  C   VAL B 169     3540   2963   4469   -382    256   -531       C  
ATOM   2948  O   VAL B 169      34.506 -17.181   4.233  1.00 33.98           O  
ANISOU 2948  O   VAL B 169     4184   3574   5154   -387    170   -588       O  
ATOM   2949  CB  VAL B 169      35.261 -14.104   5.289  1.00 27.66           C  
ANISOU 2949  CB  VAL B 169     3277   2997   4237   -263    307   -543       C  
ATOM   2950  CG1 VAL B 169      36.214 -14.459   4.088  1.00 25.95           C  
ANISOU 2950  CG1 VAL B 169     3086   2799   3976   -194    191   -600       C  
ATOM   2951  CG2 VAL B 169      34.756 -12.681   5.186  1.00 26.45           C  
ANISOU 2951  CG2 VAL B 169     3004   2921   4126   -249    348   -547       C  
ATOM   2952  N   SER B 170      35.071 -17.061   6.410  1.00 30.00           N  
ANISOU 2952  N   SER B 170     3800   3041   4559   -393    287   -469       N  
ATOM   2953  CA  SER B 170      35.643 -18.409   6.429  1.00 32.97           C  
ANISOU 2953  CA  SER B 170     4302   3279   4945   -383    203   -457       C  
ATOM   2954  C   SER B 170      34.613 -19.481   6.123  1.00 36.64           C  
ANISOU 2954  C   SER B 170     4778   3635   5509   -500    178   -457       C  
ATOM   2955  O   SER B 170      34.989 -20.570   5.677  1.00 33.38           O  
ANISOU 2955  O   SER B 170     4451   3093   5140   -481     86   -491       O  
ATOM   2956  CB  SER B 170      36.284 -18.702   7.779  1.00 29.86           C  
ANISOU 2956  CB  SER B 170     4031   2835   4478   -392    220   -356       C  
ATOM   2957  OG  SER B 170      37.566 -18.085   7.857  1.00 38.46           O  
ANISOU 2957  OG  SER B 170     5135   3991   5488   -267    189   -367       O  
ATOM   2958  N   ARG B 171      33.334 -19.190   6.357  1.00 31.15           N  
ANISOU 2958  N   ARG B 171     3989   2985   4860   -621    258   -428       N  
ATOM   2959  CA  ARG B 171      32.271 -20.138   6.046  1.00 39.36           C  
ANISOU 2959  CA  ARG B 171     5017   3940   5998   -757    232   -422       C  
ATOM   2960  C   ARG B 171      32.294 -20.518   4.573  1.00 44.12           C  
ANISOU 2960  C   ARG B 171     5596   4515   6652   -726    117   -527       C  
ATOM   2961  O   ARG B 171      31.851 -21.615   4.204  1.00 43.88           O  
ANISOU 2961  O   ARG B 171     5620   4364   6690   -815     52   -545       O  
ATOM   2962  CB  ARG B 171      30.920 -19.529   6.451  1.00 42.08           C  
ANISOU 2962  CB  ARG B 171     5213   4382   6395   -874    349   -387       C  
ATOM   2963  CG  ARG B 171      29.681 -20.369   6.169  1.00 50.18           C  
ANISOU 2963  CG  ARG B 171     6186   5353   7529  -1039    332   -370       C  
ATOM   2964  CD  ARG B 171      29.810 -21.760   6.738  1.00 57.82           C  
ANISOU 2964  CD  ARG B 171     7324   6153   8491  -1141    292   -302       C  
ATOM   2965  NE  ARG B 171      28.552 -22.497   6.652  1.00 68.05           N  
ANISOU 2965  NE  ARG B 171     8565   7406   9883  -1333    294   -269       N  
ATOM   2966  CZ  ARG B 171      28.379 -23.724   7.125  1.00 63.74           C  
ANISOU 2966  CZ  ARG B 171     8153   6708   9357  -1470    257   -192       C  
ATOM   2967  NH1 ARG B 171      29.390 -24.355   7.709  1.00 60.76           N  
ANISOU 2967  NH1 ARG B 171     7971   6196   8920  -1422    203   -137       N  
ATOM   2968  NH2 ARG B 171      27.198 -24.317   7.011  1.00 75.97           N  
ANISOU 2968  NH2 ARG B 171     9638   8234  10995  -1662    259   -161       N  
ATOM   2969  N   LEU B 172      32.842 -19.648   3.725  1.00 31.31           N  
ANISOU 2969  N   LEU B 172     3908   3003   4986   -615     87   -600       N  
ATOM   2970  CA  LEU B 172      32.927 -19.921   2.300  1.00 31.47           C  
ANISOU 2970  CA  LEU B 172     3914   3030   5015   -602    -15   -708       C  
ATOM   2971  C   LEU B 172      33.894 -21.061   1.975  1.00 43.52           C  
ANISOU 2971  C   LEU B 172     5584   4420   6530   -538    -86   -788       C  
ATOM   2972  O   LEU B 172      34.025 -21.405   0.797  1.00 43.88           O  
ANISOU 2972  O   LEU B 172     5637   4467   6568   -533   -157   -907       O  
ATOM   2973  CB  LEU B 172      33.335 -18.656   1.535  1.00 30.21           C  
ANISOU 2973  CB  LEU B 172     3657   3034   4789   -518    -27   -747       C  
ATOM   2974  CG  LEU B 172      32.423 -17.426   1.637  1.00 33.56           C  
ANISOU 2974  CG  LEU B 172     3923   3574   5256   -553     17   -685       C  
ATOM   2975  CD1 LEU B 172      32.984 -16.246   0.830  1.00 33.49           C  
ANISOU 2975  CD1 LEU B 172     3850   3697   5179   -474    -25   -708       C  
ATOM   2976  CD2 LEU B 172      31.030 -17.775   1.173  1.00 35.37           C  
ANISOU 2976  CD2 LEU B 172     4054   3793   5592   -690    -20   -674       C  
ATOM   2977  N   LYS B 173      34.560 -21.664   2.971  1.00 39.37           N  
ANISOU 2977  N   LYS B 173     5174   3776   6009   -491    -74   -731       N  
ATOM   2978  CA  LYS B 173      35.433 -22.798   2.673  1.00 43.20           C  
ANISOU 2978  CA  LYS B 173     5784   4101   6530   -414   -152   -810       C  
ATOM   2979  C   LYS B 173      34.652 -23.978   2.085  1.00 40.14           C  
ANISOU 2979  C   LYS B 173     5456   3559   6238   -530   -219   -871       C  
ATOM   2980  O   LYS B 173      35.216 -24.764   1.319  1.00 37.91           O  
ANISOU 2980  O   LYS B 173     5245   3172   5988   -468   -285  -1006       O  
ATOM   2981  CB  LYS B 173      36.206 -23.228   3.930  1.00 40.14           C  
ANISOU 2981  CB  LYS B 173     5503   3600   6150   -354   -154   -702       C  
ATOM   2982  CG  LYS B 173      35.333 -23.678   5.103  1.00 35.31           C  
ANISOU 2982  CG  LYS B 173     4950   2897   5568   -509   -125   -546       C  
ATOM   2983  CD  LYS B 173      36.077 -24.624   6.055  1.00 44.61           C  
ANISOU 2983  CD  LYS B 173     6282   3888   6781   -477   -192   -447       C  
ATOM   2984  CE  LYS B 173      35.120 -25.141   7.123  1.00 48.27           C  
ANISOU 2984  CE  LYS B 173     6815   4271   7256   -673   -166   -287       C  
ATOM   2985  NZ  LYS B 173      35.732 -26.021   8.169  1.00 50.31           N  
ANISOU 2985  NZ  LYS B 173     7234   4348   7532   -681   -248   -143       N  
ATOM   2986  N   ILE B 174      33.350 -24.074   2.368  1.00 35.75           N  
ANISOU 2986  N   ILE B 174     4860   2997   5727   -702   -199   -791       N  
ATOM   2987  CA  ILE B 174      32.531 -25.142   1.814  1.00 43.44           C  
ANISOU 2987  CA  ILE B 174     5883   3833   6789   -841   -271   -840       C  
ATOM   2988  C   ILE B 174      32.305 -25.009   0.319  1.00 37.59           C  
ANISOU 2988  C   ILE B 174     5084   3175   6024   -859   -329   -995       C  
ATOM   2989  O   ILE B 174      31.793 -25.939  -0.301  1.00 39.17           O  
ANISOU 2989  O   ILE B 174     5344   3257   6283   -967   -404  -1072       O  
ATOM   2990  CB  ILE B 174      31.162 -25.180   2.517  1.00 48.90           C  
ANISOU 2990  CB  ILE B 174     6512   4534   7532  -1037   -225   -705       C  
ATOM   2991  CG1 ILE B 174      30.385 -23.903   2.185  1.00 52.84           C  
ANISOU 2991  CG1 ILE B 174     6811   5262   8002  -1068   -165   -692       C  
ATOM   2992  CG2 ILE B 174      31.347 -25.316   4.020  1.00 51.63           C  
ANISOU 2992  CG2 ILE B 174     6930   4820   7867  -1054   -159   -548       C  
ATOM   2993  CD1 ILE B 174      29.052 -23.753   2.936  1.00 51.87           C  
ANISOU 2993  CD1 ILE B 174     6577   5188   7942  -1238    -87   -572       C  
ATOM   2994  N   ALA B 175      32.669 -23.882  -0.279  1.00 41.55           N  
ANISOU 2994  N   ALA B 175     5481   3877   6431   -775   -305  -1038       N  
ATOM   2995  CA  ALA B 175      32.325 -23.602  -1.666  1.00 39.25           C  
ANISOU 2995  CA  ALA B 175     5125   3701   6088   -830   -367  -1150       C  
ATOM   2996  C   ALA B 175      33.438 -23.954  -2.642  1.00 39.97           C  
ANISOU 2996  C   ALA B 175     5297   3787   6102   -725   -400  -1335       C  
ATOM   2997  O   ALA B 175      33.242 -23.838  -3.855  1.00 44.44           O  
ANISOU 2997  O   ALA B 175     5838   4452   6595   -789   -454  -1445       O  
ATOM   2998  CB  ALA B 175      31.965 -22.120  -1.822  1.00 34.98           C  
ANISOU 2998  CB  ALA B 175     4417   3382   5491   -827   -337  -1072       C  
ATOM   2999  N   SER B 176      34.605 -24.356  -2.156  1.00 38.73           N  
ANISOU 2999  N   SER B 176     5227   3532   5958   -571   -370  -1372       N  
ATOM   3000  CA  SER B 176      35.676 -24.712  -3.071  1.00 42.26           C  
ANISOU 3000  CA  SER B 176     5726   3981   6349   -461   -380  -1570       C  
ATOM   3001  C   SER B 176      36.642 -25.646  -2.376  1.00 38.23           C  
ANISOU 3001  C   SER B 176     5324   3260   5941   -317   -377  -1600       C  
ATOM   3002  O   SER B 176      36.758 -25.654  -1.149  1.00 45.39           O  
ANISOU 3002  O   SER B 176     6251   4085   6910   -278   -363  -1441       O  
ATOM   3003  CB  SER B 176      36.426 -23.482  -3.583  1.00 40.94           C  
ANISOU 3003  CB  SER B 176     5457   4061   6036   -377   -334  -1592       C  
ATOM   3004  OG  SER B 176      37.600 -23.886  -4.271  1.00 48.71           O  
ANISOU 3004  OG  SER B 176     6483   5050   6975   -257   -316  -1783       O  
ATOM   3005  N   ASP B 177      37.359 -26.408  -3.190  1.00 39.73           N  
ANISOU 3005  N   ASP B 177     5579   3370   6146   -237   -393  -1812       N  
ATOM   3006  CA  ASP B 177      38.444 -27.248  -2.715  1.00 54.16           C  
ANISOU 3006  CA  ASP B 177     7483   5002   8093    -61   -400  -1872       C  
ATOM   3007  C   ASP B 177      39.799 -26.547  -2.752  1.00 50.02           C  
ANISOU 3007  C   ASP B 177     6871   4636   7499    126   -336  -1916       C  
ATOM   3008  O   ASP B 177      40.786 -27.122  -2.294  1.00 49.17           O  
ANISOU 3008  O   ASP B 177     6793   4388   7501    293   -347  -1947       O  
ATOM   3009  CB  ASP B 177      38.482 -28.539  -3.541  1.00 63.74           C  
ANISOU 3009  CB  ASP B 177     8810   6009   9398    -63   -445  -2102       C  
ATOM   3010  CG  ASP B 177      38.159 -28.293  -5.000  1.00 79.88           C  
ANISOU 3010  CG  ASP B 177    10827   8229  11296   -166   -427  -2299       C  
ATOM   3011  OD1 ASP B 177      37.871 -27.118  -5.346  1.00 82.61           O  
ANISOU 3011  OD1 ASP B 177    11062   8846  11480   -238   -396  -2227       O  
ATOM   3012  OD2 ASP B 177      38.197 -29.258  -5.797  1.00 86.98           O  
ANISOU 3012  OD2 ASP B 177    11821   8991  12237   -182   -450  -2524       O  
ATOM   3013  N   THR B 178      39.873 -25.314  -3.247  1.00 48.53           N  
ANISOU 3013  N   THR B 178     6569   4729   7143     99   -282  -1904       N  
ATOM   3014  CA  THR B 178      41.131 -24.565  -3.306  1.00 50.45           C  
ANISOU 3014  CA  THR B 178     6718   5145   7306    246   -222  -1935       C  
ATOM   3015  C   THR B 178      41.014 -23.296  -2.445  1.00 37.31           C  
ANISOU 3015  C   THR B 178     4976   3632   5569    224   -200  -1710       C  
ATOM   3016  O   THR B 178      40.564 -22.259  -2.929  1.00 36.63           O  
ANISOU 3016  O   THR B 178     4817   3744   5356    129   -181  -1670       O  
ATOM   3017  CB  THR B 178      41.478 -24.219  -4.767  1.00 55.91           C  
ANISOU 3017  CB  THR B 178     7355   6044   7844    222   -174  -2140       C  
ATOM   3018  OG1 THR B 178      41.183 -25.341  -5.617  1.00 66.62           O  
ANISOU 3018  OG1 THR B 178     8803   7265   9244    179   -195  -2353       O  
ATOM   3019  CG2 THR B 178      42.944 -23.880  -4.886  1.00 57.54           C  
ANISOU 3019  CG2 THR B 178     7475   6377   8009    390   -105  -2227       C  
ATOM   3020  N   ILE B 179      41.444 -23.371  -1.185  1.00 35.74           N  
ANISOU 3020  N   ILE B 179     4798   3332   5449    308   -211  -1566       N  
ATOM   3021  CA  ILE B 179      41.292 -22.287  -0.215  1.00 37.44           C  
ANISOU 3021  CA  ILE B 179     4965   3656   5603    277   -187  -1366       C  
ATOM   3022  C   ILE B 179      42.674 -21.773   0.174  1.00 37.86           C  
ANISOU 3022  C   ILE B 179     4959   3805   5621    424   -168  -1349       C  
ATOM   3023  O   ILE B 179      43.561 -22.557   0.528  1.00 36.64           O  
ANISOU 3023  O   ILE B 179     4832   3523   5566    555   -202  -1381       O  
ATOM   3024  CB  ILE B 179      40.512 -22.747   1.039  1.00 38.53           C  
ANISOU 3024  CB  ILE B 179     5188   3622   5830    201   -215  -1194       C  
ATOM   3025  CG1 ILE B 179      39.219 -23.489   0.645  1.00 35.53           C  
ANISOU 3025  CG1 ILE B 179     4864   3123   5513     53   -244  -1221       C  
ATOM   3026  CG2 ILE B 179      40.134 -21.555   1.896  1.00 35.80           C  
ANISOU 3026  CG2 ILE B 179     4790   3411   5401    139   -166  -1027       C  
ATOM   3027  CD1 ILE B 179      38.220 -22.548  -0.063  1.00 42.83           C  
ANISOU 3027  CD1 ILE B 179     5695   4230   6347    -77   -214  -1221       C  
ATOM   3028  N   VAL B 180      42.842 -20.454   0.159  1.00 37.41           N  
ANISOU 3028  N   VAL B 180     4817   3960   5438    399   -126  -1286       N  
ATOM   3029  CA  VAL B 180      44.030 -19.813   0.700  1.00 30.41           C  
ANISOU 3029  CA  VAL B 180     3872   3175   4509    502   -115  -1232       C  
ATOM   3030  C   VAL B 180      43.578 -18.915   1.843  1.00 32.07           C  
ANISOU 3030  C   VAL B 180     4094   3418   4673    430   -104  -1042       C  
ATOM   3031  O   VAL B 180      42.694 -18.069   1.662  1.00 30.37           O  
ANISOU 3031  O   VAL B 180     3852   3291   4398    323    -72  -1000       O  
ATOM   3032  CB  VAL B 180      44.793 -19.021  -0.384  1.00 33.77           C  
ANISOU 3032  CB  VAL B 180     4189   3829   4813    526    -72  -1343       C  
ATOM   3033  CG1 VAL B 180      45.920 -18.142   0.225  1.00 29.84           C  
ANISOU 3033  CG1 VAL B 180     3617   3462   4257    595    -62  -1261       C  
ATOM   3034  CG2 VAL B 180      45.366 -19.940  -1.416  1.00 31.84           C  
ANISOU 3034  CG2 VAL B 180     3929   3565   4603    604    -58  -1556       C  
ATOM   3035  N   TYR B 181      44.172 -19.104   3.017  1.00 30.49           N  
ANISOU 3035  N   TYR B 181     3935   3144   4507    487   -134   -934       N  
ATOM   3036  CA  TYR B 181      43.820 -18.333   4.202  1.00 29.15           C  
ANISOU 3036  CA  TYR B 181     3796   3003   4278    411   -114   -773       C  
ATOM   3037  C   TYR B 181      44.848 -17.249   4.480  1.00 27.45           C  
ANISOU 3037  C   TYR B 181     3514   2951   3965    457   -107   -735       C  
ATOM   3038  O   TYR B 181      46.058 -17.511   4.488  1.00 28.77           O  
ANISOU 3038  O   TYR B 181     3643   3137   4151    568   -150   -760       O  
ATOM   3039  CB  TYR B 181      43.714 -19.227   5.442  1.00 29.29           C  
ANISOU 3039  CB  TYR B 181     3926   2840   4362    398   -163   -651       C  
ATOM   3040  CG  TYR B 181      42.503 -20.115   5.442  1.00 33.62           C  
ANISOU 3040  CG  TYR B 181     4552   3233   4990    300   -164   -642       C  
ATOM   3041  CD1 TYR B 181      41.247 -19.578   5.678  1.00 34.04           C  
ANISOU 3041  CD1 TYR B 181     4602   3329   5004    159    -93   -591       C  
ATOM   3042  CD2 TYR B 181      42.611 -21.484   5.191  1.00 36.31           C  
ANISOU 3042  CD2 TYR B 181     4958   3378   5460    349   -235   -691       C  
ATOM   3043  CE1 TYR B 181      40.139 -20.360   5.667  1.00 30.80           C  
ANISOU 3043  CE1 TYR B 181     4241   2794   4666     55    -92   -579       C  
ATOM   3044  CE2 TYR B 181      41.487 -22.299   5.184  1.00 37.68           C  
ANISOU 3044  CE2 TYR B 181     5207   3403   5705    237   -243   -678       C  
ATOM   3045  CZ  TYR B 181      40.258 -21.729   5.425  1.00 31.76           C  
ANISOU 3045  CZ  TYR B 181     4442   2724   4901     83   -170   -617       C  
ATOM   3046  OH  TYR B 181      39.136 -22.492   5.418  1.00 42.74           O  
ANISOU 3046  OH  TYR B 181     5887   3990   6362    -44   -175   -598       O  
ATOM   3047  N   TYR B 182      44.352 -16.049   4.774  1.00 26.24           N  
ANISOU 3047  N   TYR B 182     3343   2902   3725    370    -56   -674       N  
ATOM   3048  CA  TYR B 182      45.162 -14.968   5.314  1.00 25.56           C  
ANISOU 3048  CA  TYR B 182     3225   2941   3544    377    -53   -614       C  
ATOM   3049  C   TYR B 182      44.522 -14.451   6.605  1.00 25.22           C  
ANISOU 3049  C   TYR B 182     3258   2867   3456    283    -16   -501       C  
ATOM   3050  O   TYR B 182      43.358 -14.718   6.899  1.00 29.79           O  
ANISOU 3050  O   TYR B 182     3882   3365   4072    206     28   -479       O  
ATOM   3051  CB  TYR B 182      45.325 -13.820   4.297  1.00 24.67           C  
ANISOU 3051  CB  TYR B 182     3018   2997   3360    358    -26   -673       C  
ATOM   3052  CG  TYR B 182      44.066 -13.041   4.045  1.00 23.93           C  
ANISOU 3052  CG  TYR B 182     2916   2916   3260    259     19   -659       C  
ATOM   3053  CD1 TYR B 182      43.769 -11.900   4.788  1.00 25.01           C  
ANISOU 3053  CD1 TYR B 182     3063   3085   3354    202     54   -588       C  
ATOM   3054  CD2 TYR B 182      43.188 -13.416   3.039  1.00 24.12           C  
ANISOU 3054  CD2 TYR B 182     2915   2919   3331    225     20   -725       C  
ATOM   3055  CE1 TYR B 182      42.619 -11.152   4.558  1.00 22.86           C  
ANISOU 3055  CE1 TYR B 182     2762   2812   3113    133     92   -582       C  
ATOM   3056  CE2 TYR B 182      42.016 -12.685   2.798  1.00 23.67           C  
ANISOU 3056  CE2 TYR B 182     2828   2873   3294    142     42   -699       C  
ATOM   3057  CZ  TYR B 182      41.749 -11.539   3.561  1.00 23.07           C  
ANISOU 3057  CZ  TYR B 182     2746   2819   3201    107     80   -628       C  
ATOM   3058  OH  TYR B 182      40.607 -10.814   3.344  1.00 22.92           O  
ANISOU 3058  OH  TYR B 182     2676   2794   3237     47     99   -609       O  
ATOM   3059  N   GLY B 183      45.296 -13.711   7.388  1.00 24.99           N  
ANISOU 3059  N   GLY B 183     3240   2913   3343    279    -28   -437       N  
ATOM   3060  CA  GLY B 183      44.820 -13.276   8.678  1.00 30.32           C  
ANISOU 3060  CA  GLY B 183     4002   3567   3953    184     14   -349       C  
ATOM   3061  C   GLY B 183      45.928 -12.615   9.473  1.00 29.97           C  
ANISOU 3061  C   GLY B 183     3976   3606   3805    183    -29   -288       C  
ATOM   3062  O   GLY B 183      47.037 -12.424   8.982  1.00 32.33           O  
ANISOU 3062  O   GLY B 183     4201   3988   4096    256    -90   -309       O  
ATOM   3063  N   MET B 184      45.601 -12.290  10.721  1.00 25.42           N  
ANISOU 3063  N   MET B 184     3497   3018   3144     84      6   -217       N  
ATOM   3064  CA  MET B 184      46.478 -11.527  11.601  1.00 25.61           C  
ANISOU 3064  CA  MET B 184     3561   3125   3045     43    -29   -162       C  
ATOM   3065  C   MET B 184      46.691 -12.280  12.913  1.00 26.94           C  
ANISOU 3065  C   MET B 184     3854   3235   3146    -20    -86    -41       C  
ATOM   3066  O   MET B 184      45.725 -12.751  13.528  1.00 27.51           O  
ANISOU 3066  O   MET B 184     4015   3234   3205   -107    -24     -8       O  
ATOM   3067  CB  MET B 184      45.850 -10.147  11.843  1.00 24.97           C  
ANISOU 3067  CB  MET B 184     3491   3101   2897    -43     78   -212       C  
ATOM   3068  CG  MET B 184      46.654  -9.196  12.664  1.00 41.72           C  
ANISOU 3068  CG  MET B 184     5662   5304   4886   -105     52   -183       C  
ATOM   3069  SD  MET B 184      45.812  -7.582  12.693  1.00 39.52           S  
ANISOU 3069  SD  MET B 184     5384   5047   4586   -176    182   -279       S  
ATOM   3070  CE  MET B 184      46.029  -7.116  10.993  1.00 25.90           C  
ANISOU 3070  CE  MET B 184     3508   3361   2971    -81    140   -331       C  
ATOM   3071  N   LYS B 185      47.952 -12.401  13.332  1.00 23.68           N  
ANISOU 3071  N   LYS B 185     2746   3363   2889    425   -270   -128       N  
ATOM   3072  CA  LYS B 185      48.283 -13.072  14.592  1.00 24.22           C  
ANISOU 3072  CA  LYS B 185     2836   3340   3027    422   -323    -25       C  
ATOM   3073  C   LYS B 185      47.646 -12.352  15.769  1.00 30.25           C  
ANISOU 3073  C   LYS B 185     3705   4146   3644    382   -361     34       C  
ATOM   3074  O   LYS B 185      47.464 -11.138  15.747  1.00 25.75           O  
ANISOU 3074  O   LYS B 185     3172   3634   2976    383   -359      5       O  
ATOM   3075  CB  LYS B 185      49.803 -13.110  14.812  1.00 24.28           C  
ANISOU 3075  CB  LYS B 185     2787   3283   3156    437   -392     55       C  
ATOM   3076  CG  LYS B 185      50.562 -14.055  13.857  1.00 28.84           C  
ANISOU 3076  CG  LYS B 185     3228   3772   3959    467   -318    -24       C  
ATOM   3077  CD  LYS B 185      51.959 -14.365  14.358  1.00 31.49           C  
ANISOU 3077  CD  LYS B 185     3467   3991   4508    488   -398     92       C  
ATOM   3078  CE  LYS B 185      52.776 -15.136  13.312  1.00 34.47           C  
ANISOU 3078  CE  LYS B 185     3678   4264   5156    518   -276    -39       C  
ATOM   3079  NZ  LYS B 185      52.104 -16.426  13.017  1.00 46.27           N  
ANISOU 3079  NZ  LYS B 185     5120   5654   6806    516   -176   -131       N  
ATOM   3080  N   ALA B 186      47.313 -13.107  16.815  1.00 31.92           N  
ANISOU 3080  N   ALA B 186     3958   4321   3851    326   -385    110       N  
ATOM   3081  CA  ALA B 186      46.845 -12.477  18.043  1.00 27.83           C  
ANISOU 3081  CA  ALA B 186     3548   3858   3168    235   -394    142       C  
ATOM   3082  C   ALA B 186      47.902 -11.505  18.559  1.00 32.94           C  
ANISOU 3082  C   ALA B 186     4238   4534   3742    197   -474    198       C  
ATOM   3083  O   ALA B 186      49.104 -11.769  18.466  1.00 29.77           O  
ANISOU 3083  O   ALA B 186     3785   4090   3438    213   -570    295       O  
ATOM   3084  CB  ALA B 186      46.535 -13.521  19.112  1.00 27.58           C  
ANISOU 3084  CB  ALA B 186     3561   3804   3116    131   -429    251       C  
ATOM   3085  N   HIS B 187      47.437 -10.376  19.101  1.00 28.48           N  
ANISOU 3085  N   HIS B 187     3753   4030   3039    141   -423    122       N  
ATOM   3086  CA  HIS B 187      48.279  -9.300  19.635  1.00 32.38           C  
ANISOU 3086  CA  HIS B 187     4303   4556   3445     80   -475    137       C  
ATOM   3087  C   HIS B 187      49.148  -8.647  18.576  1.00 28.37           C  
ANISOU 3087  C   HIS B 187     3719   4026   3034    187   -513    131       C  
ATOM   3088  O   HIS B 187      50.207  -8.095  18.879  1.00 34.50           O  
ANISOU 3088  O   HIS B 187     4512   4812   3783    149   -596    189       O  
ATOM   3089  CB  HIS B 187      49.165  -9.794  20.762  1.00 28.61           C  
ANISOU 3089  CB  HIS B 187     3883   4102   2887    -63   -608    300       C  
ATOM   3090  CG  HIS B 187      48.426 -10.561  21.799  1.00 36.39           C  
ANISOU 3090  CG  HIS B 187     4946   5127   3755   -212   -596    349       C  
ATOM   3091  ND1 HIS B 187      47.698  -9.947  22.794  1.00 38.91           N  
ANISOU 3091  ND1 HIS B 187     5386   5535   3864   -378   -496    247       N  
ATOM   3092  CD2 HIS B 187      48.312 -11.893  22.007  1.00 37.44           C  
ANISOU 3092  CD2 HIS B 187     5048   5220   3957   -239   -660    487       C  
ATOM   3093  CE1 HIS B 187      47.155 -10.869  23.564  1.00 40.52           C  
ANISOU 3093  CE1 HIS B 187     5641   5777   3976   -516   -501    325       C  
ATOM   3094  NE2 HIS B 187      47.511 -12.059  23.108  1.00 42.50           N  
ANISOU 3094  NE2 HIS B 187     5801   5945   4401   -428   -615    488       N  
ATOM   3095  N   ALA B 188      48.763  -8.748  17.324  1.00 25.74           N  
ANISOU 3095  N   ALA B 188     3304   3678   2799    295   -463     72       N  
ATOM   3096  CA  ALA B 188      49.485  -8.006  16.311  1.00 31.99           C  
ANISOU 3096  CA  ALA B 188     4038   4477   3641    354   -487     62       C  
ATOM   3097  C   ALA B 188      49.285  -6.495  16.478  1.00 31.34           C  
ANISOU 3097  C   ALA B 188     3993   4402   3514    339   -472     15       C  
ATOM   3098  O   ALA B 188      50.176  -5.720  16.125  1.00 31.71           O  
ANISOU 3098  O   ALA B 188     4022   4452   3573    346   -523     42       O  
ATOM   3099  CB  ALA B 188      49.050  -8.471  14.924  1.00 28.51           C  
ANISOU 3099  CB  ALA B 188     3514   4051   3269    412   -438     12       C  
ATOM   3100  N   HIS B 189      48.143  -6.072  17.024  1.00 32.75           N  
ANISOU 3100  N   HIS B 189     4207   4565   3672    314   -391    -64       N  
ATOM   3101  CA  HIS B 189      47.798  -4.665  17.205  1.00 32.43           C  
ANISOU 3101  CA  HIS B 189     4170   4483   3668    304   -345   -138       C  
ATOM   3102  C   HIS B 189      46.667  -4.603  18.214  1.00 37.25           C  
ANISOU 3102  C   HIS B 189     4823   5070   4259    240   -218   -253       C  
ATOM   3103  O   HIS B 189      45.823  -5.490  18.254  1.00 36.73           O  
ANISOU 3103  O   HIS B 189     4744   5019   4191    244   -170   -265       O  
ATOM   3104  CB  HIS B 189      47.352  -4.006  15.891  1.00 25.23           C  
ANISOU 3104  CB  HIS B 189     3152   3544   2892    388   -361   -119       C  
ATOM   3105  CG  HIS B 189      47.273  -2.505  15.950  1.00 32.26           C  
ANISOU 3105  CG  HIS B 189     4014   4351   3892    390   -348   -153       C  
ATOM   3106  ND1 HIS B 189      48.384  -1.696  15.870  1.00 34.95           N  
ANISOU 3106  ND1 HIS B 189     4374   4684   4221    371   -414   -114       N  
ATOM   3107  CD2 HIS B 189      46.212  -1.667  16.066  1.00 33.38           C  
ANISOU 3107  CD2 HIS B 189     4089   4389   4206    408   -270   -224       C  
ATOM   3108  CE1 HIS B 189      48.009  -0.426  15.930  1.00 33.85           C  
ANISOU 3108  CE1 HIS B 189     4191   4436   4233    376   -382   -159       C  
ATOM   3109  NE2 HIS B 189      46.694  -0.381  16.046  1.00 37.40           N  
ANISOU 3109  NE2 HIS B 189     4577   4814   4818    403   -291   -227       N  
ATOM   3110  N   GLU B 190      46.630  -3.545  19.010  1.00 38.97           N  
ANISOU 3110  N   GLU B 190     5086   5248   4473    165   -143   -360       N  
ATOM   3111  CA  GLU B 190      45.501  -3.330  19.910  1.00 38.09           C  
ANISOU 3111  CA  GLU B 190     4994   5104   4373     86     31   -523       C  
ATOM   3112  C   GLU B 190      44.530  -2.381  19.224  1.00 35.13           C  
ANISOU 3112  C   GLU B 190     4475   4598   4274    192    110   -598       C  
ATOM   3113  O   GLU B 190      44.741  -1.165  19.208  1.00 35.19           O  
ANISOU 3113  O   GLU B 190     4447   4509   4415    198    137   -658       O  
ATOM   3114  CB  GLU B 190      45.956  -2.792  21.261  1.00 39.65           C  
ANISOU 3114  CB  GLU B 190     5323   5336   4408   -105    103   -638       C  
ATOM   3115  CG  GLU B 190      46.648  -3.835  22.119  1.00 45.18           C  
ANISOU 3115  CG  GLU B 190     6153   6172   4843   -256     10   -529       C  
ATOM   3116  N   PHE B 191      43.451  -2.940  18.679  1.00 27.83           N  
ANISOU 3116  N   PHE B 191     3454   3657   3462    265    137   -580       N  
ATOM   3117  CA  PHE B 191      42.478  -2.155  17.946  1.00 33.51           C  
ANISOU 3117  CA  PHE B 191     4001   4248   4484    361    167   -591       C  
ATOM   3118  C   PHE B 191      41.595  -1.384  18.919  1.00 44.55           C  
ANISOU 3118  C   PHE B 191     5352   5522   6054    305    390   -811       C  
ATOM   3119  O   PHE B 191      41.498  -1.720  20.105  1.00 49.94           O  
ANISOU 3119  O   PHE B 191     6149   6262   6564    170    538   -963       O  
ATOM   3120  CB  PHE B 191      41.597  -3.032  17.063  1.00 30.62           C  
ANISOU 3120  CB  PHE B 191     3538   3917   4178    429    112   -493       C  
ATOM   3121  CG  PHE B 191      42.307  -3.683  15.912  1.00 30.08           C  
ANISOU 3121  CG  PHE B 191     3482   3954   3993    467    -68   -321       C  
ATOM   3122  CD1 PHE B 191      42.930  -4.916  16.073  1.00 29.56           C  
ANISOU 3122  CD1 PHE B 191     3525   3998   3708    432    -99   -293       C  
ATOM   3123  CD2 PHE B 191      42.292  -3.099  14.651  1.00 32.74           C  
ANISOU 3123  CD2 PHE B 191     3708   4274   4459    514   -197   -188       C  
ATOM   3124  CE1 PHE B 191      43.544  -5.555  14.994  1.00 28.10           C  
ANISOU 3124  CE1 PHE B 191     3331   3891   3453    454   -214   -186       C  
ATOM   3125  CE2 PHE B 191      42.916  -3.714  13.579  1.00 34.94           C  
ANISOU 3125  CE2 PHE B 191     4003   4671   4600    504   -323    -70       C  
ATOM   3126  CZ  PHE B 191      43.537  -4.955  13.754  1.00 32.35           C  
ANISOU 3126  CZ  PHE B 191     3779   4440   4073    478   -310    -96       C  
ATOM   3127  N   GLU B 192      40.913  -0.360  18.381  1.00 45.88           N  
ANISOU 3127  N   GLU B 192     5335   5514   6585    393    415   -822       N  
ATOM   3128  CA  GLU B 192      40.204   0.613  19.210  1.00 55.06           C  
ANISOU 3128  CA  GLU B 192     6409   6499   8011    352    650  -1060       C  
ATOM   3129  C   GLU B 192      39.184  -0.039  20.141  1.00 62.70           C  
ANISOU 3129  C   GLU B 192     7387   7497   8940    263    877  -1254       C  
ATOM   3130  O   GLU B 192      38.932   0.485  21.233  1.00 78.16           O  
ANISOU 3130  O   GLU B 192     9372   9392  10933    138   1126  -1523       O  
ATOM   3131  CB  GLU B 192      39.530   1.660  18.321  1.00 56.90           C  
ANISOU 3131  CB  GLU B 192     6385   6505   8729    483    602   -980       C  
ATOM   3132  N   GLN B 193      38.570  -1.145  19.715  1.00 68.03           N  
ANISOU 3132  N   GLN B 193     8036   8266   9545    303    811  -1139       N  
ATOM   3133  CA  GLN B 193      37.710  -2.016  20.526  1.00 83.15           C  
ANISOU 3133  CA  GLN B 193     9987  10255  11353    205    989  -1274       C  
ATOM   3134  C   GLN B 193      36.284  -1.485  20.675  1.00 78.27           C  
ANISOU 3134  C   GLN B 193     9139   9455  11145    238   1203  -1441       C  
ATOM   3135  O   GLN B 193      36.065  -0.275  20.821  1.00 78.91           O  
ANISOU 3135  O   GLN B 193     9083   9335  11563    263   1332  -1583       O  
ATOM   3136  CB  GLN B 193      38.348  -2.299  21.904  1.00 94.01           C  
ANISOU 3136  CB  GLN B 193    11597  11767  12356    -13   1119  -1430       C  
ATOM   3137  CG  GLN B 193      37.854  -1.497  23.113  1.00103.05           C  
ANISOU 3137  CG  GLN B 193    12741  12836  13577   -180   1443  -1765       C  
ATOM   3138  CD  GLN B 193      38.717  -1.745  24.348  1.00104.18           C  
ANISOU 3138  CD  GLN B 193    13147  13163  13273   -445   1500  -1859       C  
ATOM   3139  OE1 GLN B 193      38.908  -2.890  24.764  1.00103.79           O  
ANISOU 3139  OE1 GLN B 193    13245  13302  12889   -561   1425  -1749       O  
ATOM   3140  NE2 GLN B 193      39.253  -0.675  24.926  1.00103.20           N  
ANISOU 3140  NE2 GLN B 193    13076  12984  13153   -558   1615  -2045       N  
ATOM   3141  N   SER B 194      35.312  -2.398  20.617  1.00 75.04           N  
ANISOU 3141  N   SER B 194     8667   9096  10747    239   1244  -1423       N  
ATOM   3142  CA  SER B 194      33.888  -2.045  20.647  1.00 81.47           C  
ANISOU 3142  CA  SER B 194     9227   9741  11987    282   1428  -1549       C  
ATOM   3143  C   SER B 194      33.044  -3.173  21.242  1.00 86.25           C  
ANISOU 3143  C   SER B 194     9870  10466  12436    179   1573  -1634       C  
ATOM   3144  O   SER B 194      31.924  -2.946  21.714  1.00 89.10           O  
ANISOU 3144  O   SER B 194    10062  10715  13078    148   1822  -1830       O  
ATOM   3145  CB  SER B 194      33.380  -1.707  19.239  1.00 74.85           C  
ANISOU 3145  CB  SER B 194     8137   8773  11530    467   1201  -1300       C  
ATOM   3146  N   ASN B 197      30.063  -5.530  20.860  1.00 89.29           N  
ANISOU 3146  N   ASN B 197     9965  10939  13023    177   1671  -1557       N  
ATOM   3147  CA  ASN B 197      30.391  -6.574  21.828  1.00 90.11           C  
ANISOU 3147  CA  ASN B 197    10328  11243  12665     -8   1764  -1627       C  
ATOM   3148  C   ASN B 197      29.193  -7.491  22.069  1.00 93.76           C  
ANISOU 3148  C   ASN B 197    10706  11749  13169    -75   1889  -1669       C  
ATOM   3149  O   ASN B 197      28.418  -7.280  23.004  1.00103.16           O  
ANISOU 3149  O   ASN B 197    11831  12906  14458   -201   2200  -1919       O  
ATOM   3150  CB  ASN B 197      30.855  -5.958  23.151  1.00 88.23           C  
ANISOU 3150  CB  ASN B 197    10237  11028  12259   -193   2022  -1892       C  
ATOM   3151  N   GLU B 198      29.043  -8.507  21.222  1.00 85.73           N  
ANISOU 3151  N   GLU B 198     9688  10808  12078     -9   1664  -1444       N  
ATOM   3152  CA  GLU B 198      27.917  -9.424  21.303  1.00 82.33           C  
ANISOU 3152  CA  GLU B 198     9168  10414  11698    -64   1744  -1452       C  
ATOM   3153  C   GLU B 198      28.409 -10.835  21.026  1.00 77.45           C  
ANISOU 3153  C   GLU B 198     8744   9955  10728   -107   1546  -1263       C  
ATOM   3154  O   GLU B 198      29.570 -11.052  20.672  1.00 77.23           O  
ANISOU 3154  O   GLU B 198     8880   9987  10476    -74   1350  -1129       O  
ATOM   3155  CB  GLU B 198      26.796  -9.036  20.325  1.00 79.25           C  
ANISOU 3155  CB  GLU B 198     8450   9877  11783     80   1682  -1379       C  
ATOM   3156  N   SER B 199      27.511 -11.799  21.209  1.00 76.71           N  
ANISOU 3156  N   SER B 199     8613   9911  10621   -185   1614  -1265       N  
ATOM   3157  CA  SER B 199      27.777 -13.204  20.916  1.00 71.42           C  
ANISOU 3157  CA  SER B 199     8083   9350   9704   -227   1449  -1100       C  
ATOM   3158  C   SER B 199      27.187 -13.563  19.555  1.00 57.66           C  
ANISOU 3158  C   SER B 199     6172   7573   8165   -107   1258   -957       C  
ATOM   3159  O   SER B 199      26.052 -13.186  19.237  1.00 56.89           O  
ANISOU 3159  O   SER B 199     5835   7399   8381    -66   1317   -990       O  
ATOM   3160  CB  SER B 199      27.197 -14.113  22.007  1.00 74.51           C  
ANISOU 3160  CB  SER B 199     8558   9827   9924   -425   1632  -1176       C  
ATOM   3161  N   ARG B 200      27.963 -14.278  18.756  1.00 47.38           N  
ANISOU 3161  N   ARG B 200     4982   6325   6696    -70   1034   -802       N  
ATOM   3162  CA  ARG B 200      27.587 -14.658  17.409  1.00 46.67           C  
ANISOU 3162  CA  ARG B 200     4776   6240   6718     -9    842   -676       C  
ATOM   3163  C   ARG B 200      27.521 -16.180  17.319  1.00 49.54           C  
ANISOU 3163  C   ARG B 200     5241   6667   6914    -95    797   -627       C  
ATOM   3164  O   ARG B 200      28.119 -16.907  18.122  1.00 43.06           O  
ANISOU 3164  O   ARG B 200     4599   5875   5886   -171    847   -634       O  
ATOM   3165  CB  ARG B 200      28.587 -14.099  16.381  1.00 54.48           C  
ANISOU 3165  CB  ARG B 200     5794   7235   7671     81    639   -572       C  
ATOM   3166  N   TYR B 201      26.794 -16.659  16.323  1.00 47.28           N  
ANISOU 3166  N   TYR B 201     4832   6396   6735    -99    689   -563       N  
ATOM   3167  CA  TYR B 201      26.483 -18.074  16.204  1.00 41.13           C  
ANISOU 3167  CA  TYR B 201     4109   5652   5865   -191    671   -542       C  
ATOM   3168  C   TYR B 201      27.447 -18.721  15.232  1.00 39.35           C  
ANISOU 3168  C   TYR B 201     3995   5458   5499   -187    505   -484       C  
ATOM   3169  O   TYR B 201      27.879 -18.093  14.261  1.00 41.32           O  
ANISOU 3169  O   TYR B 201     4208   5734   5758   -138    375   -440       O  
ATOM   3170  CB  TYR B 201      25.051 -18.279  15.731  1.00 38.64           C  
ANISOU 3170  CB  TYR B 201     3589   5341   5753   -232    668   -530       C  
ATOM   3171  CG  TYR B 201      24.018 -18.300  16.820  1.00 40.87           C  
ANISOU 3171  CG  TYR B 201     3783   5594   6151   -289    884   -619       C  
ATOM   3172  CD1 TYR B 201      23.724 -19.476  17.482  1.00 45.08           C  
ANISOU 3172  CD1 TYR B 201     4409   6152   6567   -406    977   -642       C  
ATOM   3173  CD2 TYR B 201      23.299 -17.157  17.155  1.00 48.74           C  
ANISOU 3173  CD2 TYR B 201     4585   6528   7407   -239   1004   -686       C  
ATOM   3174  CE1 TYR B 201      22.765 -19.529  18.462  1.00 50.47           C  
ANISOU 3174  CE1 TYR B 201     5016   6831   7330   -493   1190   -731       C  
ATOM   3175  CE2 TYR B 201      22.324 -17.195  18.150  1.00 57.95           C  
ANISOU 3175  CE2 TYR B 201     5655   7670   8693   -314   1246   -808       C  
ATOM   3176  CZ  TYR B 201      22.059 -18.398  18.798  1.00 61.03           C  
ANISOU 3176  CZ  TYR B 201     6162   8119   8907   -452   1340   -830       C  
ATOM   3177  OH  TYR B 201      21.094 -18.489  19.787  1.00 62.69           O  
ANISOU 3177  OH  TYR B 201     6287   8329   9202   -562   1594   -956       O  
ATOM   3178  N   CYS B 202      27.825 -19.954  15.536  1.00 38.96           N  
ANISOU 3178  N   CYS B 202     4073   5394   5335   -252    523   -486       N  
ATOM   3179  CA  CYS B 202      28.683 -20.718  14.651  1.00 35.01           C  
ANISOU 3179  CA  CYS B 202     3653   4890   4758   -262    415   -476       C  
ATOM   3180  C   CYS B 202      27.930 -20.943  13.351  1.00 33.41           C  
ANISOU 3180  C   CYS B 202     3334   4747   4612   -323    322   -482       C  
ATOM   3181  O   CYS B 202      26.831 -21.511  13.383  1.00 40.40           O  
ANISOU 3181  O   CYS B 202     4138   5639   5575   -398    353   -489       O  
ATOM   3182  CB  CYS B 202      29.066 -22.060  15.282  1.00 31.15           C  
ANISOU 3182  CB  CYS B 202     3279   4328   4228   -325    460   -468       C  
ATOM   3183  SG  CYS B 202      29.991 -23.161  14.168  1.00 37.15           S  
ANISOU 3183  SG  CYS B 202     4090   5030   4994   -349    383   -512       S  
ATOM   3184  N   PRO B 203      28.471 -20.543  12.198  1.00 40.20           N  
ANISOU 3184  N   PRO B 203     4187   5668   5419   -325    204   -475       N  
ATOM   3185  CA  PRO B 203      27.756 -20.777  10.935  1.00 45.36           C  
ANISOU 3185  CA  PRO B 203     4743   6415   6075   -445     96   -467       C  
ATOM   3186  C   PRO B 203      27.584 -22.241  10.588  1.00 51.99           C  
ANISOU 3186  C   PRO B 203     5632   7241   6882   -569    131   -557       C  
ATOM   3187  O   PRO B 203      26.811 -22.544   9.675  1.00 59.51           O  
ANISOU 3187  O   PRO B 203     6505   8280   7827   -706     54   -561       O  
ATOM   3188  CB  PRO B 203      28.623 -20.052   9.901  1.00 46.81           C  
ANISOU 3188  CB  PRO B 203     4951   6682   6151   -456    -21   -443       C  
ATOM   3189  CG  PRO B 203      29.971 -19.980  10.525  1.00 43.39           C  
ANISOU 3189  CG  PRO B 203     4656   6172   5658   -347     52   -486       C  
ATOM   3190  CD  PRO B 203      29.726 -19.803  11.989  1.00 38.79           C  
ANISOU 3190  CD  PRO B 203     4085   5496   5157   -249    160   -464       C  
ATOM   3191  N   ASN B 204      28.243 -23.158  11.294  1.00 51.92           N  
ANISOU 3191  N   ASN B 204     5738   7116   6873   -542    233   -616       N  
ATOM   3192  CA  ASN B 204      28.186 -24.569  10.940  1.00 43.47           C  
ANISOU 3192  CA  ASN B 204     4703   5988   5827   -655    276   -713       C  
ATOM   3193  C   ASN B 204      27.272 -25.393  11.829  1.00 46.85           C  
ANISOU 3193  C   ASN B 204     5108   6340   6354   -690    350   -687       C  
ATOM   3194  O   ASN B 204      26.704 -26.382  11.351  1.00 54.98           O  
ANISOU 3194  O   ASN B 204     6112   7354   7424   -814    362   -755       O  
ATOM   3195  CB  ASN B 204      29.584 -25.197  10.976  1.00 50.05           C  
ANISOU 3195  CB  ASN B 204     5645   6702   6671   -618    328   -787       C  
ATOM   3196  CG  ASN B 204      29.569 -26.671  10.564  1.00 56.33           C  
ANISOU 3196  CG  ASN B 204     6453   7390   7560   -734    395   -915       C  
ATOM   3197  OD1 ASN B 204      29.197 -27.007   9.438  1.00 55.26           O  
ANISOU 3197  OD1 ASN B 204     6286   7335   7374   -881    385  -1036       O  
ATOM   3198  ND2 ASN B 204      29.967 -27.554  11.483  1.00 51.77           N  
ANISOU 3198  ND2 ASN B 204     5915   6628   7127   -691    456   -881       N  
ATOM   3199  N   CYS B 205      27.128 -25.050  13.111  1.00 38.49           N  
ANISOU 3199  N   CYS B 205     4063   5241   5320   -614    412   -603       N  
ATOM   3200  CA  CYS B 205      26.373 -25.903  14.011  1.00 43.77           C  
ANISOU 3200  CA  CYS B 205     4729   5846   6055   -680    494   -573       C  
ATOM   3201  C   CYS B 205      25.357 -25.179  14.879  1.00 43.00           C  
ANISOU 3201  C   CYS B 205     4549   5808   5981   -673    566   -526       C  
ATOM   3202  O   CYS B 205      24.620 -25.848  15.610  1.00 41.43           O  
ANISOU 3202  O   CYS B 205     4338   5582   5822   -756    649   -507       O  
ATOM   3203  CB  CYS B 205      27.321 -26.691  14.925  1.00 39.10           C  
ANISOU 3203  CB  CYS B 205     4263   5119   5475   -671    530   -520       C  
ATOM   3204  SG  CYS B 205      28.029 -25.665  16.202  1.00 40.95           S  
ANISOU 3204  SG  CYS B 205     4580   5377   5602   -589    555   -421       S  
ATOM   3205  N   GLY B 206      25.305 -23.855  14.861  1.00 45.23           N  
ANISOU 3205  N   GLY B 206     4768   6156   6263   -588    556   -516       N  
ATOM   3206  CA  GLY B 206      24.287 -23.199  15.657  1.00 46.36           C  
ANISOU 3206  CA  GLY B 206     4799   6324   6491   -590    667   -516       C  
ATOM   3207  C   GLY B 206      24.607 -23.047  17.127  1.00 50.62           C  
ANISOU 3207  C   GLY B 206     5444   6843   6946   -604    810   -517       C  
ATOM   3208  O   GLY B 206      23.741 -22.597  17.887  1.00 52.31           O  
ANISOU 3208  O   GLY B 206     5571   7080   7224   -643    954   -560       O  
ATOM   3209  N   ARG B 207      25.803 -23.429  17.563  1.00 34.68           N  
ANISOU 3209  N   ARG B 207     3597   4785   4793   -601    779   -472       N  
ATOM   3210  CA  ARG B 207      26.248 -23.057  18.897  1.00 38.66           C  
ANISOU 3210  CA  ARG B 207     4211   5304   5173   -643    877   -451       C  
ATOM   3211  C   ARG B 207      26.705 -21.610  18.890  1.00 34.27           C  
ANISOU 3211  C   ARG B 207     3637   4780   4604   -538    889   -503       C  
ATOM   3212  O   ARG B 207      27.058 -21.063  17.847  1.00 34.01           O  
ANISOU 3212  O   ARG B 207     3550   4741   4632   -424    779   -508       O  
ATOM   3213  CB  ARG B 207      27.395 -23.959  19.361  1.00 43.64           C  
ANISOU 3213  CB  ARG B 207     5008   5873   5699   -690    797   -338       C  
ATOM   3214  CG  ARG B 207      26.927 -25.206  20.092  1.00 52.50           C  
ANISOU 3214  CG  ARG B 207     6174   6963   6812   -849    834   -254       C  
ATOM   3215  CD  ARG B 207      28.069 -26.132  20.385  1.00 57.72           C  
ANISOU 3215  CD  ARG B 207     6952   7519   7461   -881    714   -103       C  
ATOM   3216  NE  ARG B 207      28.439 -26.861  19.184  1.00 68.46           N  
ANISOU 3216  NE  ARG B 207     8264   8760   8989   -793    620   -134       N  
ATOM   3217  CZ  ARG B 207      28.059 -28.104  18.922  1.00 69.19           C  
ANISOU 3217  CZ  ARG B 207     8326   8748   9216   -861    607   -113       C  
ATOM   3218  NH1 ARG B 207      27.307 -28.768  19.788  1.00 71.88           N  
ANISOU 3218  NH1 ARG B 207     8680   9089   9541  -1010    659    -26       N  
ATOM   3219  NH2 ARG B 207      28.443 -28.684  17.796  1.00 68.80           N  
ANISOU 3219  NH2 ARG B 207     8233   8592   9314   -800    555   -192       N  
ATOM   3220  N   LEU B 208      26.679 -20.981  20.064  1.00 38.07           N  
ANISOU 3220  N   LEU B 208     4167   5300   4999   -605   1033   -549       N  
ATOM   3221  CA  LEU B 208      27.453 -19.755  20.247  1.00 34.47           C  
ANISOU 3221  CA  LEU B 208     3747   4853   4496   -529   1040   -591       C  
ATOM   3222  C   LEU B 208      28.927 -20.025  19.955  1.00 44.84           C  
ANISOU 3222  C   LEU B 208     5202   6142   5695   -473    869   -485       C  
ATOM   3223  O   LEU B 208      29.480 -21.034  20.402  1.00 40.94           O  
ANISOU 3223  O   LEU B 208     4824   5629   5102   -556    812   -380       O  
ATOM   3224  CB  LEU B 208      27.283 -19.221  21.664  1.00 39.07           C  
ANISOU 3224  CB  LEU B 208     4394   5494   4958   -670   1241   -681       C  
ATOM   3225  CG  LEU B 208      25.866 -18.757  22.010  1.00 43.09           C  
ANISOU 3225  CG  LEU B 208     4732   6009   5630   -722   1466   -837       C  
ATOM   3226  CD1 LEU B 208      25.823 -18.121  23.391  1.00 49.11           C  
ANISOU 3226  CD1 LEU B 208     5570   6838   6252   -892   1706   -982       C  
ATOM   3227  CD2 LEU B 208      25.306 -17.808  20.931  1.00 40.28           C  
ANISOU 3227  CD2 LEU B 208     4146   5576   5582   -539   1432   -890       C  
ATOM   3228  N   LEU B 209      29.556 -19.131  19.180  1.00 31.91           N  
ANISOU 3228  N   LEU B 209     3533   4491   4102   -337    783   -501       N  
ATOM   3229  CA  LEU B 209      30.944 -19.302  18.748  1.00 31.62           C  
ANISOU 3229  CA  LEU B 209     3594   4425   3994   -273    636   -422       C  
ATOM   3230  C   LEU B 209      31.893 -18.920  19.873  1.00 31.13           C  
ANISOU 3230  C   LEU B 209     3672   4384   3771   -332    651   -383       C  
ATOM   3231  O   LEU B 209      31.855 -17.793  20.358  1.00 33.04           O  
ANISOU 3231  O   LEU B 209     3913   4661   3979   -334    738   -463       O  
ATOM   3232  CB  LEU B 209      31.235 -18.415  17.539  1.00 34.48           C  
ANISOU 3232  CB  LEU B 209     3874   4789   4439   -141    545   -447       C  
ATOM   3233  CG  LEU B 209      31.767 -18.945  16.227  1.00 39.86           C  
ANISOU 3233  CG  LEU B 209     4541   5459   5146    -95    414   -421       C  
ATOM   3234  CD1 LEU B 209      32.505 -17.816  15.495  1.00 33.39           C  
ANISOU 3234  CD1 LEU B 209     3702   4664   4321     -5    333   -419       C  
ATOM   3235  CD2 LEU B 209      32.620 -20.205  16.395  1.00 30.88           C  
ANISOU 3235  CD2 LEU B 209     3503   4256   3973   -132    376   -374       C  
ATOM   3236  N   GLN B 210      32.769 -19.821  20.275  1.00 34.10           N  
ANISOU 3236  N   GLN B 210     4156   4729   4072   -390    560   -257       N  
ATOM   3237  CA  GLN B 210      33.754 -19.447  21.277  1.00 37.03           C  
ANISOU 3237  CA  GLN B 210     4653   5134   4284   -469    528   -182       C  
ATOM   3238  C   GLN B 210      34.923 -18.728  20.612  1.00 32.98           C  
ANISOU 3238  C   GLN B 210     4142   4593   3797   -331    422   -176       C  
ATOM   3239  O   GLN B 210      35.357 -19.105  19.525  1.00 33.74           O  
ANISOU 3239  O   GLN B 210     4182   4624   4015   -216    334   -164       O  
ATOM   3240  CB  GLN B 210      34.257 -20.676  22.019  1.00 45.52           C  
ANISOU 3240  CB  GLN B 210     5816   6173   5305   -603    433      7       C  
ATOM   3241  CG  GLN B 210      35.405 -20.373  22.943  1.00 56.40           C  
ANISOU 3241  CG  GLN B 210     7313   7590   6527   -703    340    137       C  
ATOM   3242  CD  GLN B 210      35.122 -20.840  24.351  1.00 76.45           C  
ANISOU 3242  CD  GLN B 210     9962  10218   8866   -973    362    257       C  
ATOM   3243  OE1 GLN B 210      34.208 -21.640  24.583  1.00 80.45           O  
ANISOU 3243  OE1 GLN B 210    10453  10727   9388  -1070    424    276       O  
ATOM   3244  NE2 GLN B 210      35.901 -20.343  25.304  1.00 86.33           N  
ANISOU 3244  NE2 GLN B 210    11331  11561   9910  -1127    306    343       N  
ATOM   3245  N   TYR B 211      35.428 -17.686  21.266  1.00 30.11           N  
ANISOU 3245  N   TYR B 211     3845   4285   3312   -365    447   -203       N  
ATOM   3246  CA  TYR B 211      36.613 -16.986  20.799  1.00 39.16           C  
ANISOU 3246  CA  TYR B 211     5003   5410   4465   -260    345   -181       C  
ATOM   3247  C   TYR B 211      37.743 -17.152  21.807  1.00 37.76           C  
ANISOU 3247  C   TYR B 211     4949   5255   4144   -379    247    -37       C  
ATOM   3248  O   TYR B 211      37.523 -17.061  23.014  1.00 39.42           O  
ANISOU 3248  O   TYR B 211     5255   5548   4176   -569    305    -20       O  
ATOM   3249  CB  TYR B 211      36.330 -15.503  20.578  1.00 37.22           C  
ANISOU 3249  CB  TYR B 211     4710   5192   4241   -192    432   -324       C  
ATOM   3250  CG  TYR B 211      35.636 -15.140  19.278  1.00 27.92           C  
ANISOU 3250  CG  TYR B 211     3385   3979   3243    -50    435   -394       C  
ATOM   3251  CD1 TYR B 211      34.250 -15.293  19.128  1.00 31.10           C  
ANISOU 3251  CD1 TYR B 211     3684   4382   3751    -62    535   -464       C  
ATOM   3252  CD2 TYR B 211      36.351 -14.581  18.231  1.00 26.82           C  
ANISOU 3252  CD2 TYR B 211     3205   3822   3163     68    331   -375       C  
ATOM   3253  CE1 TYR B 211      33.607 -14.940  17.944  1.00 31.04           C  
ANISOU 3253  CE1 TYR B 211     3530   4355   3909     36    497   -484       C  
ATOM   3254  CE2 TYR B 211      35.713 -14.216  17.043  1.00 26.51           C  
ANISOU 3254  CE2 TYR B 211     3036   3778   3257    148    303   -400       C  
ATOM   3255  CZ  TYR B 211      34.353 -14.394  16.912  1.00 27.26           C  
ANISOU 3255  CZ  TYR B 211     3025   3872   3459    129    372   -442       C  
ATOM   3256  OH  TYR B 211      33.736 -14.033  15.742  1.00 36.48           O  
ANISOU 3256  OH  TYR B 211     4056   5046   4760    178    304   -424       O  
ATOM   3257  N   ASP B 212      38.946 -17.419  21.298  1.00 40.96           N  
ANISOU 3257  N   ASP B 212     5342   5591   4630   -292     99     68       N  
ATOM   3258  CA  ASP B 212      40.152 -17.422  22.114  1.00 42.53           C  
ANISOU 3258  CA  ASP B 212     5622   5799   4737   -387    -32    230       C  
ATOM   3259  C   ASP B 212      40.772 -16.038  22.217  1.00 37.69           C  
ANISOU 3259  C   ASP B 212     5050   5248   4024   -366    -25    155       C  
ATOM   3260  O   ASP B 212      41.456 -15.750  23.196  1.00 37.59           O  
ANISOU 3260  O   ASP B 212     5133   5298   3852   -514    -92    248       O  
ATOM   3261  CB  ASP B 212      41.204 -18.384  21.537  1.00 50.65           C  
ANISOU 3261  CB  ASP B 212     6580   6692   5973   -298   -187    378       C  
ATOM   3262  CG  ASP B 212      40.681 -19.816  21.349  1.00 61.45           C  
ANISOU 3262  CG  ASP B 212     7891   7956   7503   -309   -194    443       C  
ATOM   3263  OD1 ASP B 212      39.804 -20.253  22.128  1.00 58.45           O  
ANISOU 3263  OD1 ASP B 212     7563   7624   7020   -453   -149    485       O  
ATOM   3264  OD2 ASP B 212      41.168 -20.513  20.418  1.00 60.80           O  
ANISOU 3264  OD2 ASP B 212     7705   7736   7659   -189   -230    439       O  
ATOM   3265  N   TYR B 213      40.559 -15.186  21.219  1.00 33.44           N  
ANISOU 3265  N   TYR B 213     4438   4694   3575   -208     40      6       N  
ATOM   3266  CA  TYR B 213      41.159 -13.862  21.135  1.00 31.66           C  
ANISOU 3266  CA  TYR B 213     4228   4495   3307   -166     41    -62       C  
ATOM   3267  C   TYR B 213      40.358 -13.055  20.127  1.00 28.98           C  
ANISOU 3267  C   TYR B 213     3787   4135   3089    -30    133   -211       C  
ATOM   3268  O   TYR B 213      40.004 -13.570  19.072  1.00 35.21           O  
ANISOU 3268  O   TYR B 213     4488   4889   4002     68    113   -213       O  
ATOM   3269  CB  TYR B 213      42.630 -13.918  20.679  1.00 26.91           C  
ANISOU 3269  CB  TYR B 213     3612   3849   2765    -92   -116     53       C  
ATOM   3270  CG  TYR B 213      43.254 -12.545  20.511  1.00 37.10           C  
ANISOU 3270  CG  TYR B 213     4914   5163   4020    -49   -119    -12       C  
ATOM   3271  CD1 TYR B 213      43.839 -11.890  21.592  1.00 37.34           C  
ANISOU 3271  CD1 TYR B 213     5046   5253   3887   -188   -143     13       C  
ATOM   3272  CD2 TYR B 213      43.225 -11.886  19.286  1.00 36.85           C  
ANISOU 3272  CD2 TYR B 213     4794   5103   4104    100   -104    -91       C  
ATOM   3273  CE1 TYR B 213      44.387 -10.654  21.455  1.00 31.37           C  
ANISOU 3273  CE1 TYR B 213     4300   4505   3116   -157   -140    -55       C  
ATOM   3274  CE2 TYR B 213      43.768 -10.628  19.142  1.00 34.10           C  
ANISOU 3274  CE2 TYR B 213     4451   4763   3743    131   -114   -133       C  
ATOM   3275  CZ  TYR B 213      44.350 -10.023  20.227  1.00 34.33           C  
ANISOU 3275  CZ  TYR B 213     4577   4828   3640     14   -125   -124       C  
ATOM   3276  OH  TYR B 213      44.917  -8.777  20.075  1.00 35.19           O  
ANISOU 3276  OH  TYR B 213     4687   4930   3753     40   -133   -172       O  
ATOM   3277  N   ILE B 214      40.119 -11.786  20.427  1.00 30.06           N  
ANISOU 3277  N   ILE B 214     3927   4287   3209    -42    223   -326       N  
ATOM   3278  CA  ILE B 214      39.328 -10.923  19.560  1.00 35.27           C  
ANISOU 3278  CA  ILE B 214     4462   4902   4037     74    286   -427       C  
ATOM   3279  C   ILE B 214      40.216  -9.789  19.081  1.00 31.42           C  
ANISOU 3279  C   ILE B 214     3961   4389   3588    148    218   -422       C  
ATOM   3280  O   ILE B 214      40.810  -9.081  19.895  1.00 30.83           O  
ANISOU 3280  O   ILE B 214     3967   4325   3423     74    244   -461       O  
ATOM   3281  CB  ILE B 214      38.097 -10.374  20.294  1.00 43.08           C  
ANISOU 3281  CB  ILE B 214     5414   5880   5076      3    480   -581       C  
ATOM   3282  CG1 ILE B 214      37.116 -11.503  20.586  1.00 38.93           C  
ANISOU 3282  CG1 ILE B 214     4878   5382   4532    -65    547   -580       C  
ATOM   3283  CG2 ILE B 214      37.468  -9.196  19.526  1.00 37.68           C  
ANISOU 3283  CG2 ILE B 214     4571   5108   4638    123    522   -658       C  
ATOM   3284  CD1 ILE B 214      36.058 -11.105  21.552  1.00 38.37           C  
ANISOU 3284  CD1 ILE B 214     4789   5318   4470   -182    768   -746       C  
ATOM   3285  N   HIS B 215      40.329  -9.631  17.767  1.00 28.60           N  
ANISOU 3285  N   HIS B 215     3510   4011   3344    264    128   -372       N  
ATOM   3286  CA  HIS B 215      40.900  -8.397  17.239  1.00 27.57           C  
ANISOU 3286  CA  HIS B 215     3342   3851   3281    324     76   -366       C  
ATOM   3287  C   HIS B 215      39.955  -7.231  17.498  1.00 29.78           C  
ANISOU 3287  C   HIS B 215     3533   4052   3729    336    185   -467       C  
ATOM   3288  O   HIS B 215      40.299  -6.277  18.196  1.00 34.68           O  
ANISOU 3288  O   HIS B 215     4190   4630   4355    301    250   -547       O  
ATOM   3289  CB  HIS B 215      41.189  -8.543  15.741  1.00 24.02           C  
ANISOU 3289  CB  HIS B 215     2818   3426   2882    395    -46   -277       C  
ATOM   3290  CG  HIS B 215      42.258  -9.544  15.430  1.00 28.08           C  
ANISOU 3290  CG  HIS B 215     3391   3983   3296    387   -117   -221       C  
ATOM   3291  ND1 HIS B 215      43.556  -9.404  15.871  1.00 23.11           N  
ANISOU 3291  ND1 HIS B 215     2831   3353   2596    376   -164   -184       N  
ATOM   3292  CD2 HIS B 215      42.224 -10.697  14.711  1.00 23.17           C  
ANISOU 3292  CD2 HIS B 215     2744   3386   2672    384   -136   -207       C  
ATOM   3293  CE1 HIS B 215      44.280 -10.416  15.426  1.00 25.41           C  
ANISOU 3293  CE1 HIS B 215     3119   3651   2885    382   -208   -144       C  
ATOM   3294  NE2 HIS B 215      43.491 -11.226  14.736  1.00 25.14           N  
ANISOU 3294  NE2 HIS B 215     3033   3627   2891    384   -179   -173       N  
ATOM   3295  N   TYR B 216      38.739  -7.322  16.967  1.00 34.43           N  
ANISOU 3295  N   TYR B 216     3990   4608   4485    375    215   -473       N  
ATOM   3296  CA  TYR B 216      37.675  -6.363  17.201  1.00 36.75           C  
ANISOU 3296  CA  TYR B 216     4146   4790   5029    396    333   -567       C  
ATOM   3297  C   TYR B 216      36.369  -6.998  16.757  1.00 33.97           C  
ANISOU 3297  C   TYR B 216     3663   4433   4810    411    350   -547       C  
ATOM   3298  O   TYR B 216      36.304  -7.616  15.688  1.00 29.33           O  
ANISOU 3298  O   TYR B 216     3039   3909   4197    435    206   -420       O  
ATOM   3299  CB  TYR B 216      37.885  -5.039  16.455  1.00 36.02           C  
ANISOU 3299  CB  TYR B 216     3935   4599   5151    473    246   -505       C  
ATOM   3300  CG  TYR B 216      38.073  -5.158  14.963  1.00 40.35           C  
ANISOU 3300  CG  TYR B 216     4415   5202   5716    517     35   -311       C  
ATOM   3301  CD1 TYR B 216      39.330  -5.434  14.417  1.00 43.83           C  
ANISOU 3301  CD1 TYR B 216     4968   5742   5943    505    -87   -228       C  
ATOM   3302  CD2 TYR B 216      37.009  -4.950  14.086  1.00 47.71           C  
ANISOU 3302  CD2 TYR B 216     5158   6091   6878    544    -43   -209       C  
ATOM   3303  CE1 TYR B 216      39.522  -5.521  13.027  1.00 45.46           C  
ANISOU 3303  CE1 TYR B 216     5121   6024   6126    496   -252    -79       C  
ATOM   3304  CE2 TYR B 216      37.186  -5.042  12.694  1.00 51.76           C  
ANISOU 3304  CE2 TYR B 216     5624   6691   7351    523   -249    -21       C  
ATOM   3305  CZ  TYR B 216      38.445  -5.338  12.175  1.00 50.53           C  
ANISOU 3305  CZ  TYR B 216     5604   6655   6941    488   -336     25       C  
ATOM   3306  OH  TYR B 216      38.634  -5.425  10.809  1.00 52.12           O  
ANISOU 3306  OH  TYR B 216     5770   6968   7065    420   -506    178       O  
ATOM   3307  N   ASN B 217      35.333  -6.806  17.572  1.00 31.01           N  
ANISOU 3307  N   ASN B 217     3213   3989   4581    378    539   -689       N  
ATOM   3308  CA  ASN B 217      34.003  -7.306  17.253  1.00 38.82           C  
ANISOU 3308  CA  ASN B 217     4049   4958   5742    388    572   -680       C  
ATOM   3309  C   ASN B 217      34.061  -8.785  16.879  1.00 36.97           C  
ANISOU 3309  C   ASN B 217     3909   4854   5283    350    480   -591       C  
ATOM   3310  O   ASN B 217      34.590  -9.589  17.644  1.00 42.03           O  
ANISOU 3310  O   ASN B 217     4719   5567   5682    274    529   -627       O  
ATOM   3311  CB  ASN B 217      33.391  -6.459  16.138  1.00 45.06           C  
ANISOU 3311  CB  ASN B 217     4607   5646   6869    481    446   -557       C  
ATOM   3312  CG  ASN B 217      33.001  -5.054  16.616  1.00 58.48           C  
ANISOU 3312  CG  ASN B 217     6148   7151   8922    525    581   -668       C  
ATOM   3313  OD1 ASN B 217      32.856  -4.801  17.816  1.00 63.28           O  
ANISOU 3313  OD1 ASN B 217     6797   7706   9539    468    827   -893       O  
ATOM   3314  ND2 ASN B 217      32.823  -4.145  15.676  1.00 61.57           N  
ANISOU 3314  ND2 ASN B 217     6352   7431   9612    602    426   -514       N  
ATOM   3315  N   GLN B 218      33.552  -9.156  15.708  1.00 32.74           N  
ANISOU 3315  N   GLN B 218     3263   4345   4832    381    338   -467       N  
ATOM   3316  CA  GLN B 218      33.518 -10.561  15.311  1.00 36.83           C  
ANISOU 3316  CA  GLN B 218     3853   4964   5176    331    277   -419       C  
ATOM   3317  C   GLN B 218      34.849 -11.071  14.778  1.00 36.82           C  
ANISOU 3317  C   GLN B 218     3996   5040   4955    326    157   -356       C  
ATOM   3318  O   GLN B 218      34.965 -12.275  14.519  1.00 35.72           O  
ANISOU 3318  O   GLN B 218     3919   4954   4699    282    133   -346       O  
ATOM   3319  CB  GLN B 218      32.454 -10.779  14.230  1.00 39.73           C  
ANISOU 3319  CB  GLN B 218     4049   5348   5699    324    174   -327       C  
ATOM   3320  CG  GLN B 218      32.951 -10.432  12.823  1.00 48.21           C  
ANISOU 3320  CG  GLN B 218     5088   6483   6747    321    -37   -181       C  
ATOM   3321  CD  GLN B 218      31.814 -10.165  11.850  1.00 58.40           C  
ANISOU 3321  CD  GLN B 218     6169   7779   8243    288   -169    -50       C  
ATOM   3322  OE1 GLN B 218      30.794  -9.574  12.215  1.00 59.13           O  
ANISOU 3322  OE1 GLN B 218     6081   7759   8626    328   -115    -48       O  
ATOM   3323  NE2 GLN B 218      31.976 -10.619  10.606  1.00 59.66           N  
ANISOU 3323  NE2 GLN B 218     6339   8067   8261    191   -339     58       N  
ATOM   3324  N   ILE B 219      35.836 -10.192  14.596  1.00 33.22           N  
ANISOU 3324  N   ILE B 219     3576   4572   4473    366     96   -325       N  
ATOM   3325  CA  ILE B 219      37.094 -10.526  13.935  1.00 28.47           C  
ANISOU 3325  CA  ILE B 219     3070   4035   3712    362    -10   -271       C  
ATOM   3326  C   ILE B 219      38.079 -11.029  14.995  1.00 28.79           C  
ANISOU 3326  C   ILE B 219     3262   4069   3606    346     48   -312       C  
ATOM   3327  O   ILE B 219      38.454 -10.287  15.912  1.00 25.76           O  
ANISOU 3327  O   ILE B 219     2931   3651   3206    345    102   -349       O  
ATOM   3328  CB  ILE B 219      37.657  -9.301  13.185  1.00 25.65           C  
ANISOU 3328  CB  ILE B 219     2663   3674   3407    395   -116   -195       C  
ATOM   3329  CG1 ILE B 219      36.636  -8.708  12.213  1.00 28.48           C  
ANISOU 3329  CG1 ILE B 219     2849   4029   3942    386   -214    -95       C  
ATOM   3330  CG2 ILE B 219      38.893  -9.642  12.422  1.00 26.67           C  
ANISOU 3330  CG2 ILE B 219     2871   3881   3380    372   -200   -158       C  
ATOM   3331  CD1 ILE B 219      36.209  -9.704  11.099  1.00 35.44           C  
ANISOU 3331  CD1 ILE B 219     3704   5027   4734    295   -302    -43       C  
ATOM   3332  N   GLY B 220      38.515 -12.279  14.877  1.00 24.44           N  
ANISOU 3332  N   GLY B 220     2773   3543   2969    316     29   -300       N  
ATOM   3333  CA  GLY B 220      39.360 -12.816  15.931  1.00 24.37           C  
ANISOU 3333  CA  GLY B 220     2878   3513   2868    284     48   -285       C  
ATOM   3334  C   GLY B 220      39.704 -14.277  15.722  1.00 29.21           C  
ANISOU 3334  C   GLY B 220     3512   4106   3481    260     25   -257       C  
ATOM   3335  O   GLY B 220      39.504 -14.845  14.645  1.00 29.68           O  
ANISOU 3335  O   GLY B 220     3513   4177   3586    264      9   -284       O  
ATOM   3336  N   HIS B 221      40.221 -14.883  16.781  1.00 24.83           N  
ANISOU 3336  N   HIS B 221     3034   3517   2884    211     19   -198       N  
ATOM   3337  CA  HIS B 221      40.637 -16.286  16.763  1.00 30.38           C  
ANISOU 3337  CA  HIS B 221     3736   4150   3656    189    -13   -142       C  
ATOM   3338  C   HIS B 221      39.553 -17.094  17.465  1.00 29.48           C  
ANISOU 3338  C   HIS B 221     3639   4028   3535    109     44   -129       C  
ATOM   3339  O   HIS B 221      39.498 -17.152  18.695  1.00 40.34           O  
ANISOU 3339  O   HIS B 221     5090   5419   4820     14     50    -58       O  
ATOM   3340  CB  HIS B 221      42.010 -16.442  17.409  1.00 27.03           C  
ANISOU 3340  CB  HIS B 221     3355   3676   3241    177   -102    -27       C  
ATOM   3341  CG  HIS B 221      43.124 -15.913  16.556  1.00 34.56           C  
ANISOU 3341  CG  HIS B 221     4266   4622   4243    255   -145    -50       C  
ATOM   3342  ND1 HIS B 221      44.190 -16.688  16.154  1.00 37.56           N  
ANISOU 3342  ND1 HIS B 221     4586   4906   4778    286   -185    -17       N  
ATOM   3343  CD2 HIS B 221      43.317 -14.689  15.998  1.00 34.08           C  
ANISOU 3343  CD2 HIS B 221     4200   4628   4119    300   -145   -104       C  
ATOM   3344  CE1 HIS B 221      45.000 -15.966  15.401  1.00 35.64           C  
ANISOU 3344  CE1 HIS B 221     4312   4693   4538    337   -193    -64       C  
ATOM   3345  NE2 HIS B 221      44.488 -14.752  15.283  1.00 33.63           N  
ANISOU 3345  NE2 HIS B 221     4098   4542   4139    342   -181   -104       N  
ATOM   3346  N   TYR B 222      38.657 -17.664  16.673  1.00 26.53           N  
ANISOU 3346  N   TYR B 222     3198   3650   3232    117     88   -199       N  
ATOM   3347  CA  TYR B 222      37.477 -18.366  17.144  1.00 27.18           C  
ANISOU 3347  CA  TYR B 222     3275   3732   3322     44    153   -204       C  
ATOM   3348  C   TYR B 222      37.671 -19.872  16.950  1.00 27.33           C  
ANISOU 3348  C   TYR B 222     3277   3647   3461     15    130   -165       C  
ATOM   3349  O   TYR B 222      38.456 -20.316  16.104  1.00 30.10           O  
ANISOU 3349  O   TYR B 222     3586   3931   3920     62    100   -195       O  
ATOM   3350  CB  TYR B 222      36.230 -17.879  16.385  1.00 27.98           C  
ANISOU 3350  CB  TYR B 222     3289   3894   3450     62    208   -301       C  
ATOM   3351  CG  TYR B 222      36.408 -17.986  14.875  1.00 35.11           C  
ANISOU 3351  CG  TYR B 222     4124   4813   4405    100    158   -353       C  
ATOM   3352  CD1 TYR B 222      36.121 -19.167  14.185  1.00 31.81           C  
ANISOU 3352  CD1 TYR B 222     3672   4363   4050     52    168   -398       C  
ATOM   3353  CD2 TYR B 222      36.884 -16.908  14.145  1.00 34.40           C  
ANISOU 3353  CD2 TYR B 222     4008   4775   4286    150    106   -362       C  
ATOM   3354  CE1 TYR B 222      36.305 -19.249  12.808  1.00 31.78           C  
ANISOU 3354  CE1 TYR B 222     3623   4405   4048     31    142   -475       C  
ATOM   3355  CE2 TYR B 222      37.080 -16.988  12.784  1.00 34.03           C  
ANISOU 3355  CE2 TYR B 222     3915   4778   4235    130     62   -404       C  
ATOM   3356  CZ  TYR B 222      36.819 -18.158  12.127  1.00 31.10           C  
ANISOU 3356  CZ  TYR B 222     3524   4397   3895     60     88   -472       C  
ATOM   3357  OH  TYR B 222      37.026 -18.184  10.781  1.00 34.07           O  
ANISOU 3357  OH  TYR B 222     3869   4852   4224    -10     63   -539       O  
ATOM   3358  N   HIS B 223      36.947 -20.666  17.735  1.00 31.79           N  
ANISOU 3358  N   HIS B 223     4391   3605   4082   -299    129    697       N  
ATOM   3359  CA  HIS B 223      37.102 -22.124  17.648  1.00 35.49           C  
ANISOU 3359  CA  HIS B 223     4826   3924   4735   -329     93    778       C  
ATOM   3360  C   HIS B 223      35.858 -22.764  18.239  1.00 40.68           C  
ANISOU 3360  C   HIS B 223     5494   4572   5389   -427    198    845       C  
ATOM   3361  O   HIS B 223      35.547 -22.516  19.409  1.00 47.02           O  
ANISOU 3361  O   HIS B 223     6394   5438   6035   -487    239    951       O  
ATOM   3362  CB  HIS B 223      38.373 -22.554  18.399  1.00 41.66           C  
ANISOU 3362  CB  HIS B 223     5674   4631   5523   -318    -32    931       C  
ATOM   3363  CG  HIS B 223      38.725 -24.002  18.267  1.00 60.73           C  
ANISOU 3363  CG  HIS B 223     8052   6868   8156   -324    -78   1020       C  
ATOM   3364  ND1 HIS B 223      39.877 -24.531  18.811  1.00 71.36           N  
ANISOU 3364  ND1 HIS B 223     9427   8123   9562   -299   -200   1169       N  
ATOM   3365  CD2 HIS B 223      38.080 -25.039  17.675  1.00 72.64           C  
ANISOU 3365  CD2 HIS B 223     9494   8261   9846   -354    -19    984       C  
ATOM   3366  CE1 HIS B 223      39.927 -25.829  18.560  1.00 74.62           C  
ANISOU 3366  CE1 HIS B 223     9795   8362  10196   -302   -206   1225       C  
ATOM   3367  NE2 HIS B 223      38.852 -26.162  17.868  1.00 73.22           N  
ANISOU 3367  NE2 HIS B 223     9566   8162  10092   -341    -94   1106       N  
ATOM   3368  N   CYS B 224      35.126 -23.543  17.436  1.00 37.04           N  
ANISOU 3368  N   CYS B 224     4938   4044   5092   -454    249    777       N  
ATOM   3369  CA  CYS B 224      33.892 -24.185  17.881  1.00 35.42           C  
ANISOU 3369  CA  CYS B 224     4721   3828   4910   -556    355    830       C  
ATOM   3370  C   CYS B 224      34.156 -25.657  18.156  1.00 36.92           C  
ANISOU 3370  C   CYS B 224     4929   3838   5262   -611    321    954       C  
ATOM   3371  O   CYS B 224      34.995 -26.277  17.504  1.00 37.74           O  
ANISOU 3371  O   CYS B 224     4999   3813   5526   -561    241    931       O  
ATOM   3372  CB  CYS B 224      32.764 -24.063  16.847  1.00 34.92           C  
ANISOU 3372  CB  CYS B 224     4532   3817   4920   -571    435    675       C  
ATOM   3373  SG  CYS B 224      31.125 -24.715  17.438  1.00 36.55           S  
ANISOU 3373  SG  CYS B 224     4699   4037   5151   -709    580    735       S  
ATOM   3374  N   GLN B 225      33.423 -26.221  19.118  1.00 39.79           N  
ANISOU 3374  N   GLN B 225     5342   4184   5592   -714    393   1088       N  
ATOM   3375  CA  GLN B 225      33.625 -27.642  19.385  1.00 42.44           C  
ANISOU 3375  CA  GLN B 225     5699   4332   6096   -770    365   1220       C  
ATOM   3376  C   GLN B 225      33.191 -28.518  18.211  1.00 41.62           C  
ANISOU 3376  C   GLN B 225     5482   4106   6227   -790    392   1095       C  
ATOM   3377  O   GLN B 225      33.541 -29.683  18.201  1.00 41.41           O  
ANISOU 3377  O   GLN B 225     5464   3892   6379   -814    361   1172       O  
ATOM   3378  CB  GLN B 225      32.931 -28.071  20.701  1.00 44.41           C  
ANISOU 3378  CB  GLN B 225     6038   4589   6248   -891    441   1405       C  
ATOM   3379  CG  GLN B 225      31.456 -27.688  20.853  1.00 57.04           C  
ANISOU 3379  CG  GLN B 225     7594   6314   7763   -976    601   1344       C  
ATOM   3380  CD  GLN B 225      30.992 -27.508  22.326  1.00 73.14           C  
ANISOU 3380  CD  GLN B 225     9753   8439   9596  -1072    686   1507       C  
ATOM   3381  OE1 GLN B 225      30.371 -28.398  22.909  1.00 70.21           O  
ANISOU 3381  OE1 GLN B 225     9408   8000   9268  -1186    758   1631       O  
ATOM   3382  NE2 GLN B 225      31.260 -26.331  22.901  1.00 82.68           N  
ANISOU 3382  NE2 GLN B 225    11040   9799  10577  -1034    690   1495       N  
ATOM   3383  N   CYS B 226      32.510 -27.980  17.189  1.00 43.79           N  
ANISOU 3383  N   CYS B 226     5654   4476   6510   -779    440    903       N  
ATOM   3384  CA  CYS B 226      32.159 -28.786  16.013  1.00 42.76           C  
ANISOU 3384  CA  CYS B 226     5424   4241   6582   -812    453    768       C  
ATOM   3385  C   CYS B 226      33.303 -28.927  15.018  1.00 45.69           C  
ANISOU 3385  C   CYS B 226     5772   4519   7068   -715    364    662       C  
ATOM   3386  O   CYS B 226      33.136 -29.614  14.009  1.00 44.85           O  
ANISOU 3386  O   CYS B 226     5600   4317   7124   -744    375    535       O  
ATOM   3387  CB  CYS B 226      30.969 -28.166  15.263  1.00 40.28           C  
ANISOU 3387  CB  CYS B 226     5000   4078   6225   -848    523    612       C  
ATOM   3388  SG  CYS B 226      31.399 -26.659  14.299  1.00 38.10           S  
ANISOU 3388  SG  CYS B 226     4679   3975   5824   -718    469    444       S  
ATOM   3389  N   GLY B 227      34.426 -28.235  15.232  1.00 41.15           N  
ANISOU 3389  N   GLY B 227     5246   3982   6407   -608    284    695       N  
ATOM   3390  CA  GLY B 227      35.535 -28.214  14.303  1.00 38.43           C  
ANISOU 3390  CA  GLY B 227     4870   3574   6158   -511    213    590       C  
ATOM   3391  C   GLY B 227      35.716 -26.886  13.584  1.00 38.60           C  
ANISOU 3391  C   GLY B 227     4858   3768   6041   -437    195    448       C  
ATOM   3392  O   GLY B 227      36.831 -26.575  13.170  1.00 40.52           O  
ANISOU 3392  O   GLY B 227     5099   3993   6303   -347    130    407       O  
ATOM   3393  N   PHE B 228      34.643 -26.115  13.396  1.00 39.19           N  
ANISOU 3393  N   PHE B 228     4897   4001   5994   -472    254    375       N  
ATOM   3394  CA  PHE B 228      34.778 -24.825  12.716  1.00 32.69           C  
ANISOU 3394  CA  PHE B 228     4044   3332   5046   -399    237    255       C  
ATOM   3395  C   PHE B 228      35.665 -23.894  13.538  1.00 32.00           C  
ANISOU 3395  C   PHE B 228     4038   3308   4811   -327    187    345       C  
ATOM   3396  O   PHE B 228      35.453 -23.720  14.740  1.00 32.52           O  
ANISOU 3396  O   PHE B 228     4178   3409   4771   -358    206    477       O  
ATOM   3397  CB  PHE B 228      33.407 -24.193  12.490  1.00 32.42           C  
ANISOU 3397  CB  PHE B 228     3948   3446   4926   -445    308    191       C  
ATOM   3398  CG  PHE B 228      33.442 -22.933  11.659  1.00 35.59           C  
ANISOU 3398  CG  PHE B 228     4310   3990   5223   -372    290     73       C  
ATOM   3399  CD1 PHE B 228      33.671 -22.990  10.297  1.00 38.39           C  
ANISOU 3399  CD1 PHE B 228     4603   4343   5642   -354    254    -73       C  
ATOM   3400  CD2 PHE B 228      33.239 -21.692  12.246  1.00 30.31           C  
ANISOU 3400  CD2 PHE B 228     3674   3452   4391   -327    315    107       C  
ATOM   3401  CE1 PHE B 228      33.702 -21.826   9.534  1.00 40.64           C  
ANISOU 3401  CE1 PHE B 228     4858   4758   5824   -292    233   -163       C  
ATOM   3402  CE2 PHE B 228      33.241 -20.549  11.496  1.00 29.19           C  
ANISOU 3402  CE2 PHE B 228     3498   3423   4169   -260    301     13       C  
ATOM   3403  CZ  PHE B 228      33.496 -20.604  10.144  1.00 28.69           C  
ANISOU 3403  CZ  PHE B 228     3374   3362   4166   -241    254   -113       C  
ATOM   3404  N   LYS B 229      36.674 -23.310  12.894  1.00 30.97           N  
ANISOU 3404  N   LYS B 229     3901   3196   4670   -242    125    269       N  
ATOM   3405  CA  LYS B 229      37.656 -22.540  13.654  1.00 30.52           C  
ANISOU 3405  CA  LYS B 229     3918   3183   4496   -185     63    354       C  
ATOM   3406  C   LYS B 229      38.427 -21.585  12.751  1.00 35.26           C  
ANISOU 3406  C   LYS B 229     4490   3849   5057   -104     24    235       C  
ATOM   3407  O   LYS B 229      38.401 -21.690  11.520  1.00 32.44           O  
ANISOU 3407  O   LYS B 229     4064   3484   4779    -87     35     98       O  
ATOM   3408  CB  LYS B 229      38.627 -23.476  14.380  1.00 31.67           C  
ANISOU 3408  CB  LYS B 229     4104   3187   4741   -181     -9    499       C  
ATOM   3409  CG  LYS B 229      39.514 -24.295  13.440  1.00 37.64           C  
ANISOU 3409  CG  LYS B 229     4794   3799   5707   -130    -47    433       C  
ATOM   3410  CD  LYS B 229      40.598 -25.021  14.233  1.00 50.23           C  
ANISOU 3410  CD  LYS B 229     6418   5264   7403   -102   -133    598       C  
ATOM   3411  CE  LYS B 229      41.590 -25.724  13.318  1.00 60.53           C  
ANISOU 3411  CE  LYS B 229     7646   6423   8929    -32   -158    526       C  
ATOM   3412  NZ  LYS B 229      40.893 -26.594  12.321  1.00 62.54           N  
ANISOU 3412  NZ  LYS B 229     7849   6578   9337    -72    -73    390       N  
ATOM   3413  N   ARG B 230      39.090 -20.618  13.390  1.00 33.39           N  
ANISOU 3413  N   ARG B 230     4317   3687   4684    -67    -20    287       N  
ATOM   3414  CA  ARG B 230      40.041 -19.751  12.699  1.00 27.86           C  
ANISOU 3414  CA  ARG B 230     3600   3032   3954      3    -66    202       C  
ATOM   3415  C   ARG B 230      41.208 -20.603  12.193  1.00 28.06           C  
ANISOU 3415  C   ARG B 230     3577   2930   4155     43   -126    197       C  
ATOM   3416  O   ARG B 230      41.995 -21.113  12.995  1.00 30.40           O  
ANISOU 3416  O   ARG B 230     3899   3150   4502     50   -193    325       O  
ATOM   3417  CB  ARG B 230      40.524 -18.644  13.638  1.00 31.32           C  
ANISOU 3417  CB  ARG B 230     4124   3558   4217     15   -102    270       C  
ATOM   3418  CG  ARG B 230      41.299 -17.453  12.932  1.00 30.71           C  
ANISOU 3418  CG  ARG B 230     4037   3553   4080     75   -131    172       C  
ATOM   3419  CD  ARG B 230      42.771 -17.785  12.618  1.00 26.29           C  
ANISOU 3419  CD  ARG B 230     3438   2921   3629    118   -218    182       C  
ATOM   3420  NE  ARG B 230      43.515 -16.586  12.238  1.00 32.50           N  
ANISOU 3420  NE  ARG B 230     4232   3783   4333    155   -243    119       N  
ATOM   3421  CZ  ARG B 230      44.810 -16.575  11.948  1.00 31.74           C  
ANISOU 3421  CZ  ARG B 230     4094   3653   4311    192   -309    117       C  
ATOM   3422  NH1 ARG B 230      45.493 -17.708  11.982  1.00 31.19           N  
ANISOU 3422  NH1 ARG B 230     3969   3471   4411    210   -355    173       N  
ATOM   3423  NH2 ARG B 230      45.422 -15.434  11.640  1.00 36.49           N  
ANISOU 3423  NH2 ARG B 230     4707   4327   4831    212   -324     62       N  
ATOM   3424  N   GLU B 231      41.318 -20.792  10.875  1.00 31.58           N  
ANISOU 3424  N   GLU B 231     3951   3351   4698     68   -100     53       N  
ATOM   3425  CA  GLU B 231      42.326 -21.701  10.353  1.00 33.98           C  
ANISOU 3425  CA  GLU B 231     4201   3517   5191    105   -125     30       C  
ATOM   3426  C   GLU B 231      43.701 -21.038  10.303  1.00 37.82           C  
ANISOU 3426  C   GLU B 231     4676   4026   5666    173   -189     36       C  
ATOM   3427  O   GLU B 231      43.838 -19.804  10.322  1.00 32.62           O  
ANISOU 3427  O   GLU B 231     4048   3494   4853    186   -203     14       O  
ATOM   3428  CB  GLU B 231      41.947 -22.202   8.958  1.00 28.35           C  
ANISOU 3428  CB  GLU B 231     3426   2769   4576     90    -61   -141       C  
ATOM   3429  CG  GLU B 231      40.648 -23.001   8.921  1.00 39.66           C  
ANISOU 3429  CG  GLU B 231     4852   4166   6051     10     -5   -157       C  
ATOM   3430  CD  GLU B 231      40.810 -24.413   9.496  1.00 41.37           C  
ANISOU 3430  CD  GLU B 231     5071   4196   6453    -12     -7    -62       C  
ATOM   3431  OE1 GLU B 231      41.955 -24.903   9.580  1.00 43.21           O  
ANISOU 3431  OE1 GLU B 231     5288   4311   6820     46    -44    -21       O  
ATOM   3432  OE2 GLU B 231      39.794 -25.016   9.876  1.00 38.30           O  
ANISOU 3432  OE2 GLU B 231     4694   3775   6084    -87     29    -20       O  
ATOM   3433  N   GLN B 232      44.726 -21.892  10.234  1.00 33.31           N  
ANISOU 3433  N   GLN B 232     4054   3321   5280    215   -222     69       N  
ATOM   3434  CA  GLN B 232      46.098 -21.432  10.098  1.00 33.75           C  
ANISOU 3434  CA  GLN B 232     4069   3384   5371    280   -278     72       C  
ATOM   3435  C   GLN B 232      46.258 -20.666   8.796  1.00 35.10           C  
ANISOU 3435  C   GLN B 232     4205   3635   5495    298   -221   -106       C  
ATOM   3436  O   GLN B 232      45.721 -21.067   7.762  1.00 37.28           O  
ANISOU 3436  O   GLN B 232     4456   3889   5820    280   -143   -242       O  
ATOM   3437  CB  GLN B 232      47.037 -22.621  10.135  1.00 34.49           C  
ANISOU 3437  CB  GLN B 232     4091   3302   5712    330   -305    130       C  
ATOM   3438  CG  GLN B 232      48.452 -22.368   9.653  1.00 58.37           C  
ANISOU 3438  CG  GLN B 232     7030   6310   8838    403   -332     94       C  
ATOM   3439  CD  GLN B 232      49.301 -23.651   9.640  1.00 75.41           C  
ANISOU 3439  CD  GLN B 232     9100   8271  11283    465   -342    148       C  
ATOM   3440  OE1 GLN B 232      48.804 -24.740   9.322  1.00 79.10           O  
ANISOU 3440  OE1 GLN B 232     9560   8600  11896    456   -275    109       O  
ATOM   3441  NE2 GLN B 232      50.582 -23.522   9.991  1.00 78.46           N  
ANISOU 3441  NE2 GLN B 232     9413   8639  11760    528   -424    238       N  
ATOM   3442  N   ALA B 233      46.997 -19.551   8.842  1.00 33.32           N  
ANISOU 3442  N   ALA B 233     3984   3508   5167    323   -261   -105       N  
ATOM   3443  CA  ALA B 233      47.049 -18.633   7.707  1.00 32.12           C  
ANISOU 3443  CA  ALA B 233     3820   3452   4931    329   -209   -251       C  
ATOM   3444  C   ALA B 233      48.345 -18.789   6.932  1.00 32.81           C  
ANISOU 3444  C   ALA B 233     3823   3489   5154    379   -196   -320       C  
ATOM   3445  O   ALA B 233      49.431 -18.845   7.513  1.00 37.72           O  
ANISOU 3445  O   ALA B 233     4403   4071   5858    415   -263   -230       O  
ATOM   3446  CB  ALA B 233      46.883 -17.171   8.141  1.00 24.98           C  
ANISOU 3446  CB  ALA B 233     2986   2690   3817    315   -238   -223       C  
ATOM   3447  N   LYS B 234      48.216 -18.833   5.611  1.00 31.37           N  
ANISOU 3447  N   LYS B 234     3613   3318   4988    374   -110   -481       N  
ATOM   3448  CA  LYS B 234      49.388 -18.868   4.744  1.00 31.20           C  
ANISOU 3448  CA  LYS B 234     3515   3266   5075    412    -67   -571       C  
ATOM   3449  C   LYS B 234      50.104 -17.519   4.720  1.00 28.37           C  
ANISOU 3449  C   LYS B 234     3162   3025   4594    420    -98   -560       C  
ATOM   3450  O   LYS B 234      51.333 -17.467   4.683  1.00 29.92           O  
ANISOU 3450  O   LYS B 234     3284   3192   4892    458   -111   -548       O  
ATOM   3451  CB  LYS B 234      48.955 -19.274   3.342  1.00 33.45           C  
ANISOU 3451  CB  LYS B 234     3790   3544   5376    384     41   -753       C  
ATOM   3452  CG  LYS B 234      50.068 -19.630   2.414  1.00 35.00           C  
ANISOU 3452  CG  LYS B 234     3907   3678   5712    417    119   -866       C  
ATOM   3453  CD  LYS B 234      49.491 -19.815   1.016  1.00 42.65           C  
ANISOU 3453  CD  LYS B 234     4899   4680   6625    362    224  -1054       C  
ATOM   3454  CE  LYS B 234      50.537 -20.343   0.010  1.00 46.85           C  
ANISOU 3454  CE  LYS B 234     5360   5136   7304    385    336  -1197       C  
ATOM   3455  NZ  LYS B 234      49.921 -20.466  -1.359  1.00 47.70           N  
ANISOU 3455  NZ  LYS B 234     5511   5298   7313    309    434  -1387       N  
ATOM   3456  N   TYR B 235      49.356 -16.418   4.730  1.00 31.02           N  
ANISOU 3456  N   TYR B 235     3576   3485   4724    385   -107   -562       N  
ATOM   3457  CA  TYR B 235      49.935 -15.082   4.777  1.00 32.45           C  
ANISOU 3457  CA  TYR B 235     3779   3765   4784    383   -135   -546       C  
ATOM   3458  C   TYR B 235      49.376 -14.392   6.006  1.00 28.90           C  
ANISOU 3458  C   TYR B 235     3415   3368   4197    362   -207   -430       C  
ATOM   3459  O   TYR B 235      48.156 -14.287   6.166  1.00 27.69           O  
ANISOU 3459  O   TYR B 235     3323   3251   3948    340   -189   -427       O  
ATOM   3460  CB  TYR B 235      49.638 -14.289   3.503  1.00 30.92           C  
ANISOU 3460  CB  TYR B 235     3608   3664   4477    361    -62   -668       C  
ATOM   3461  CG  TYR B 235      49.956 -15.059   2.225  1.00 30.75           C  
ANISOU 3461  CG  TYR B 235     3525   3599   4559    361     29   -805       C  
ATOM   3462  CD1 TYR B 235      51.265 -15.222   1.781  1.00 26.76           C  
ANISOU 3462  CD1 TYR B 235     2939   3053   4175    387     67   -850       C  
ATOM   3463  CD2 TYR B 235      48.941 -15.633   1.476  1.00 33.43           C  
ANISOU 3463  CD2 TYR B 235     3886   3941   4875    328     81   -895       C  
ATOM   3464  CE1 TYR B 235      51.554 -15.934   0.617  1.00 28.84           C  
ANISOU 3464  CE1 TYR B 235     3154   3273   4529    384    172   -992       C  
ATOM   3465  CE2 TYR B 235      49.204 -16.325   0.320  1.00 30.76           C  
ANISOU 3465  CE2 TYR B 235     3509   3567   4611    312    170  -1036       C  
ATOM   3466  CZ  TYR B 235      50.518 -16.479  -0.109  1.00 36.00           C  
ANISOU 3466  CZ  TYR B 235     4103   4184   5392    342    224  -1089       C  
ATOM   3467  OH  TYR B 235      50.758 -17.167  -1.270  1.00 36.16           O  
ANISOU 3467  OH  TYR B 235     4094   4167   5479    321    334  -1246       O  
ATOM   3468  N   GLU B 236      50.263 -13.961   6.884  1.00 28.85           N  
ANISOU 3468  N   GLU B 236     3407   3368   4186    364   -285   -338       N  
ATOM   3469  CA  GLU B 236      49.842 -13.426   8.159  1.00 27.75           C  
ANISOU 3469  CA  GLU B 236     3356   3270   3917    333   -350   -232       C  
ATOM   3470  C   GLU B 236      50.602 -12.149   8.491  1.00 30.21           C  
ANISOU 3470  C   GLU B 236     3701   3653   4124    310   -395   -214       C  
ATOM   3471  O   GLU B 236      51.830 -12.060   8.330  1.00 30.89           O  
ANISOU 3471  O   GLU B 236     3713   3728   4294    318   -432   -210       O  
ATOM   3472  CB  GLU B 236      50.051 -14.454   9.272  1.00 32.95           C  
ANISOU 3472  CB  GLU B 236     4001   3852   4668    334   -428   -102       C  
ATOM   3473  CG  GLU B 236      49.151 -14.277  10.470  1.00 34.78           C  
ANISOU 3473  CG  GLU B 236     4340   4117   4758    290   -459     -9       C  
ATOM   3474  CD  GLU B 236      49.004 -15.594  11.247  1.00 39.03           C  
ANISOU 3474  CD  GLU B 236     4863   4563   5402    289   -503    106       C  
ATOM   3475  OE1 GLU B 236      47.966 -15.805  11.915  1.00 35.81           O  
ANISOU 3475  OE1 GLU B 236     4531   4164   4913    254   -484    157       O  
ATOM   3476  OE2 GLU B 236      49.938 -16.416  11.181  1.00 33.13           O  
ANISOU 3476  OE2 GLU B 236     4027   3730   4832    326   -550    151       O  
ATOM   3477  N   ILE B 237      49.856 -11.178   8.988  1.00 27.13           N  
ANISOU 3477  N   ILE B 237     3418   3327   3562    278   -388   -204       N  
ATOM   3478  CA  ILE B 237      50.435 -10.028   9.666  1.00 28.94           C  
ANISOU 3478  CA  ILE B 237     3709   3609   3679    237   -439   -172       C  
ATOM   3479  C   ILE B 237      50.755 -10.447  11.090  1.00 28.45           C  
ANISOU 3479  C   ILE B 237     3676   3533   3599    201   -542    -47       C  
ATOM   3480  O   ILE B 237      49.863 -10.839  11.857  1.00 30.78           O  
ANISOU 3480  O   ILE B 237     4038   3823   3833    185   -538      7       O  
ATOM   3481  CB  ILE B 237      49.484  -8.826   9.644  1.00 24.77           C  
ANISOU 3481  CB  ILE B 237     3288   3137   2985    221   -375   -217       C  
ATOM   3482  CG1 ILE B 237      49.403  -8.244   8.240  1.00 26.88           C  
ANISOU 3482  CG1 ILE B 237     3528   3428   3258    248   -299   -316       C  
ATOM   3483  CG2 ILE B 237      49.904  -7.748  10.691  1.00 22.44           C  
ANISOU 3483  CG2 ILE B 237     3090   2878   2559    163   -426   -179       C  
ATOM   3484  CD1 ILE B 237      48.336  -7.139   8.108  1.00 25.90           C  
ANISOU 3484  CD1 ILE B 237     3494   3345   3001    251   -234   -348       C  
ATOM   3485  N  ASER B 238      52.035 -10.387  11.438  0.47 25.65           N  
ANISOU 3485  N  ASER B 238     3267   3179   3299    183   -636      5       N  
ATOM   3486  N  BSER B 238      52.032 -10.391  11.447  0.53 24.54           N  
ANISOU 3486  N  BSER B 238     3127   3038   3158    182   -637      5       N  
ATOM   3487  CA ASER B 238      52.479 -10.640  12.799  0.47 25.63           C  
ANISOU 3487  CA ASER B 238     3295   3184   3258    134   -760    135       C  
ATOM   3488  CA BSER B 238      52.430 -10.643  12.824  0.53 25.62           C  
ANISOU 3488  CA BSER B 238     3298   3183   3252    133   -758    136       C  
ATOM   3489  C  ASER B 238      52.452  -9.389  13.660  0.47 27.22           C  
ANISOU 3489  C  ASER B 238     3627   3462   3255     51   -792    139       C  
ATOM   3490  C  BSER B 238      52.418  -9.381  13.670  0.53 25.68           C  
ANISOU 3490  C  BSER B 238     3434   3267   3055     50   -790    138       C  
ATOM   3491  O  ASER B 238      52.380  -9.491  14.889  0.47 31.10           O  
ANISOU 3491  O  ASER B 238     4197   3978   3643     -9   -870    233       O  
ATOM   3492  O  BSER B 238      52.324  -9.468  14.898  0.53 31.45           O  
ANISOU 3492  O  BSER B 238     4246   4022   3680    -10   -865    231       O  
ATOM   3493  CB ASER B 238      53.894 -11.220  12.788  0.47 26.70           C  
ANISOU 3493  CB ASER B 238     3291   3287   3567    152   -863    202       C  
ATOM   3494  CB BSER B 238      53.824 -11.270  12.870  0.53 26.73           C  
ANISOU 3494  CB BSER B 238     3301   3289   3565    150   -865    210       C  
ATOM   3495  OG ASER B 238      54.347 -11.463  14.104  0.47 27.96           O  
ANISOU 3495  OG ASER B 238     3475   3465   3684     99  -1005    347       O  
ATOM   3496  OG BSER B 238      54.803 -10.313  12.527  0.53 31.91           O  
ANISOU 3496  OG BSER B 238     3918   3993   4214    123   -888    162       O  
ATOM   3497  N   SER B 239      52.509  -8.217  13.046  1.00 27.20           N  
ANISOU 3497  N   SER B 239     3656   3493   3187     40   -730     37       N  
ATOM   3498  CA  SER B 239      52.568  -6.978  13.793  1.00 26.91           C  
ANISOU 3498  CA  SER B 239     3743   3508   2973    -42   -748     22       C  
ATOM   3499  C   SER B 239      52.331  -5.859  12.811  1.00 30.96           C  
ANISOU 3499  C   SER B 239     4284   4027   3454    -25   -642    -94       C  
ATOM   3500  O   SER B 239      52.706  -5.974  11.640  1.00 26.59           O  
ANISOU 3500  O   SER B 239     3629   3456   3017     25   -602   -144       O  
ATOM   3501  CB  SER B 239      53.936  -6.792  14.458  1.00 33.91           C  
ANISOU 3501  CB  SER B 239     4593   4427   3866   -115   -893     89       C  
ATOM   3502  OG  SER B 239      53.900  -5.740  15.407  1.00 44.47           O  
ANISOU 3502  OG  SER B 239     6074   5814   5010   -216   -921     78       O  
ATOM   3503  N   PHE B 240      51.739  -4.769  13.300  1.00 27.62           N  
ANISOU 3503  N   PHE B 240     4000   3624   2872    -69   -592   -136       N  
ATOM   3504  CA  PHE B 240      51.746  -3.561  12.505  1.00 25.06           C  
ANISOU 3504  CA  PHE B 240     3707   3294   2520    -65   -513   -225       C  
ATOM   3505  C   PHE B 240      51.549  -2.361  13.420  1.00 31.45           C  
ANISOU 3505  C   PHE B 240     4673   4111   3165   -143   -497   -255       C  
ATOM   3506  O   PHE B 240      51.086  -2.485  14.559  1.00 33.04           O  
ANISOU 3506  O   PHE B 240     4970   4328   3257   -188   -512   -223       O  
ATOM   3507  CB  PHE B 240      50.687  -3.623  11.390  1.00 28.29           C  
ANISOU 3507  CB  PHE B 240     4094   3685   2971     24   -395   -278       C  
ATOM   3508  CG  PHE B 240      49.293  -3.262  11.820  1.00 26.87           C  
ANISOU 3508  CG  PHE B 240     4018   3500   2690     45   -308   -294       C  
ATOM   3509  CD1 PHE B 240      48.862  -1.933  11.814  1.00 26.42           C  
ANISOU 3509  CD1 PHE B 240     4063   3431   2546     37   -231   -348       C  
ATOM   3510  CD2 PHE B 240      48.398  -4.244  12.214  1.00 26.93           C  
ANISOU 3510  CD2 PHE B 240     4016   3510   2708     73   -294   -254       C  
ATOM   3511  CE1 PHE B 240      47.554  -1.594  12.210  1.00 27.94           C  
ANISOU 3511  CE1 PHE B 240     4335   3612   2668     68   -137   -365       C  
ATOM   3512  CE2 PHE B 240      47.072  -3.934  12.590  1.00 27.44           C  
ANISOU 3512  CE2 PHE B 240     4157   3575   2695     94   -200   -270       C  
ATOM   3513  CZ  PHE B 240      46.653  -2.587  12.595  1.00 31.92           C  
ANISOU 3513  CZ  PHE B 240     4817   4131   3182     96   -119   -327       C  
ATOM   3514  N  AASP B 241      51.910  -1.193  12.909  0.38 27.67           N  
ANISOU 3514  N  AASP B 241     4228   3618   2668   -166   -456   -319       N  
ATOM   3515  N  BASP B 241      51.931  -1.196  12.905  0.62 26.37           N  
ANISOU 3515  N  BASP B 241     4062   3454   2505   -167   -457   -319       N  
ATOM   3516  CA AASP B 241      51.527   0.046  13.563  0.38 32.43           C  
ANISOU 3516  CA AASP B 241     4989   4201   3133   -224   -400   -374       C  
ATOM   3517  CA BASP B 241      51.664   0.077  13.554  0.62 32.49           C  
ANISOU 3517  CA BASP B 241     4992   4210   3144   -231   -409   -373       C  
ATOM   3518  C  AASP B 241      51.277   1.103  12.494  0.38 30.99           C  
ANISOU 3518  C  AASP B 241     4823   3972   2979   -181   -295   -439       C  
ATOM   3519  C  BASP B 241      51.276   1.098  12.487  0.62 31.25           C  
ANISOU 3519  C  BASP B 241     4856   4006   3013   -180   -295   -439       C  
ATOM   3520  O  AASP B 241      51.474   0.871  11.295  0.38 28.99           O  
ANISOU 3520  O  AASP B 241     4465   3719   2830   -122   -278   -439       O  
ATOM   3521  O  BASP B 241      51.373   0.838  11.280  0.62 28.67           O  
ANISOU 3521  O  BASP B 241     4425   3678   2789   -115   -272   -438       O  
ATOM   3522  CB AASP B 241      52.575   0.495  14.590  0.38 41.55           C  
ANISOU 3522  CB AASP B 241     6205   5382   4202   -358   -507   -366       C  
ATOM   3523  CB BASP B 241      52.875   0.574  14.357  0.62 41.38           C  
ANISOU 3523  CB BASP B 241     6155   5360   4209   -361   -519   -368       C  
ATOM   3524  CG AASP B 241      53.965   0.623  14.005  0.38 43.77           C  
ANISOU 3524  CG AASP B 241     6372   5676   4582   -398   -591   -357       C  
ATOM   3525  CG BASP B 241      52.473   1.317  15.618  0.62 48.50           C  
ANISOU 3525  CG BASP B 241     7237   6258   4932   -453   -499   -406       C  
ATOM   3526  OD1AASP B 241      54.151   1.382  13.037  0.38 45.90           O  
ANISOU 3526  OD1AASP B 241     6625   5913   4903   -380   -522   -409       O  
ATOM   3527  OD1BASP B 241      51.265   1.326  15.942  0.62 53.28           O  
ANISOU 3527  OD1BASP B 241     7928   6845   5472   -407   -397   -426       O  
ATOM   3528  OD2AASP B 241      54.889  -0.024  14.533  0.38 48.84           O  
ANISOU 3528  OD2AASP B 241     6939   6364   5254   -453   -727   -289       O  
ATOM   3529  OD2BASP B 241      53.365   1.876  16.298  0.62 54.73           O  
ANISOU 3529  OD2BASP B 241     8082   7068   5645   -578   -584   -418       O  
ATOM   3530  N   VAL B 242      50.829   2.267  12.953  1.00 29.78           N  
ANISOU 3530  N   VAL B 242     4811   3775   2729   -213   -221   -495       N  
ATOM   3531  CA  VAL B 242      50.409   3.373  12.108  1.00 29.77           C  
ANISOU 3531  CA  VAL B 242     4852   3712   2748   -167   -113   -543       C  
ATOM   3532  C   VAL B 242      51.092   4.602  12.699  1.00 36.09           C  
ANISOU 3532  C   VAL B 242     5773   4467   3474   -279   -114   -598       C  
ATOM   3533  O   VAL B 242      50.642   5.130  13.721  1.00 39.34           O  
ANISOU 3533  O   VAL B 242     6320   4848   3778   -326    -70   -642       O  
ATOM   3534  CB  VAL B 242      48.888   3.556  12.095  1.00 37.90           C  
ANISOU 3534  CB  VAL B 242     5934   4708   3759    -73      8   -556       C  
ATOM   3535  CG1 VAL B 242      48.528   4.766  11.250  1.00 42.83           C  
ANISOU 3535  CG1 VAL B 242     6599   5259   4416    -24    105   -587       C  
ATOM   3536  CG2 VAL B 242      48.178   2.322  11.579  1.00 34.09           C  
ANISOU 3536  CG2 VAL B 242     5334   4273   3344     17      2   -508       C  
ATOM   3537  N   ALA B 243      52.166   5.067  12.074  1.00 34.09           N  
ANISOU 3537  N   ALA B 243     5474   4206   3273   -331   -154   -603       N  
ATOM   3538  CA  ALA B 243      52.887   6.122  12.775  1.00 34.63           C  
ANISOU 3538  CA  ALA B 243     5654   4236   3268   -462   -173   -657       C  
ATOM   3539  C   ALA B 243      53.741   6.959  11.836  1.00 28.96           C  
ANISOU 3539  C   ALA B 243     4904   3478   2622   -500   -160   -671       C  
ATOM   3540  O   ALA B 243      54.965   6.958  11.958  1.00 39.98           O  
ANISOU 3540  O   ALA B 243     6244   4910   4037   -604   -256   -666       O  
ATOM   3541  CB  ALA B 243      53.750   5.520  13.893  1.00 36.96           C  
ANISOU 3541  CB  ALA B 243     5937   4607   3499   -578   -316   -635       C  
ATOM   3542  N   PRO B 244      53.133   7.768  10.950  1.00 33.05           N  
ANISOU 3542  N   PRO B 244     5463   3917   3178   -428    -44   -685       N  
ATOM   3543  CA  PRO B 244      51.675   7.923  10.888  1.00 34.82           C  
ANISOU 3543  CA  PRO B 244     5750   4092   3388   -310     67   -689       C  
ATOM   3544  C   PRO B 244      51.035   7.101   9.779  1.00 31.74           C  
ANISOU 3544  C   PRO B 244     5234   3750   3075   -179     83   -628       C  
ATOM   3545  O   PRO B 244      49.820   7.109   9.631  1.00 36.00           O  
ANISOU 3545  O   PRO B 244     5794   4266   3620    -77    159   -618       O  
ATOM   3546  CB  PRO B 244      51.510   9.420  10.628  1.00 33.45           C  
ANISOU 3546  CB  PRO B 244     5698   3793   3220   -323    170   -730       C  
ATOM   3547  CG  PRO B 244      52.624   9.710   9.730  1.00 35.00           C  
ANISOU 3547  CG  PRO B 244     5826   3996   3477   -381    130   -707       C  
ATOM   3548  CD  PRO B 244      53.802   8.891  10.277  1.00 27.85           C  
ANISOU 3548  CD  PRO B 244     4834   3191   2558   -486     -6   -704       C  
ATOM   3549  N   PHE B 245      51.846   6.403   9.001  1.00 31.64           N  
ANISOU 3549  N   PHE B 245     5090   3804   3126   -186     16   -593       N  
ATOM   3550  CA  PHE B 245      51.324   5.520   7.971  1.00 29.87           C  
ANISOU 3550  CA  PHE B 245     4753   3633   2964    -84     26   -551       C  
ATOM   3551  C   PHE B 245      51.444   4.061   8.406  1.00 30.33           C  
ANISOU 3551  C   PHE B 245     4715   3768   3042    -74    -54   -531       C  
ATOM   3552  O   PHE B 245      52.119   3.730   9.386  1.00 27.56           O  
ANISOU 3552  O   PHE B 245     4367   3439   2667   -149   -133   -531       O  
ATOM   3553  CB  PHE B 245      52.053   5.742   6.645  1.00 33.19           C  
ANISOU 3553  CB  PHE B 245     5101   4067   3443    -92     36   -535       C  
ATOM   3554  CG  PHE B 245      51.926   7.128   6.114  1.00 28.84           C  
ANISOU 3554  CG  PHE B 245     4643   3435   2881    -99    113   -534       C  
ATOM   3555  CD1 PHE B 245      50.781   7.520   5.442  1.00 28.14           C  
ANISOU 3555  CD1 PHE B 245     4585   3314   2793      0    184   -501       C  
ATOM   3556  CD2 PHE B 245      52.967   8.039   6.274  1.00 29.95           C  
ANISOU 3556  CD2 PHE B 245     4833   3528   3020   -208    108   -557       C  
ATOM   3557  CE1 PHE B 245      50.665   8.791   4.946  1.00 31.02           C  
ANISOU 3557  CE1 PHE B 245     5034   3591   3161      1    251   -481       C  
ATOM   3558  CE2 PHE B 245      52.862   9.338   5.777  1.00 29.40           C  
ANISOU 3558  CE2 PHE B 245     4856   3363   2950   -219    185   -549       C  
ATOM   3559  CZ  PHE B 245      51.715   9.711   5.117  1.00 31.83           C  
ANISOU 3559  CZ  PHE B 245     5199   3631   3264   -109    256   -506       C  
ATOM   3560  N   LEU B 246      50.763   3.190   7.663  1.00 29.00           N  
ANISOU 3560  N   LEU B 246     4461   3637   2919     14    -37   -508       N  
ATOM   3561  CA  LEU B 246      50.801   1.764   7.960  1.00 34.93           C  
ANISOU 3561  CA  LEU B 246     5120   4442   3710     31   -100   -486       C  
ATOM   3562  C   LEU B 246      52.216   1.226   7.782  1.00 30.05           C  
ANISOU 3562  C   LEU B 246     4399   3854   3164    -24   -176   -479       C  
ATOM   3563  O   LEU B 246      52.884   1.510   6.785  1.00 33.08           O  
ANISOU 3563  O   LEU B 246     4729   4245   3595    -35   -155   -493       O  
ATOM   3564  CB  LEU B 246      49.849   1.001   7.047  1.00 33.63           C  
ANISOU 3564  CB  LEU B 246     4885   4305   3587    123    -61   -476       C  
ATOM   3565  CG  LEU B 246      48.400   0.757   7.407  1.00 34.55           C  
ANISOU 3565  CG  LEU B 246     5034   4418   3674    187    -17   -464       C  
ATOM   3566  CD1 LEU B 246      47.815  -0.138   6.303  1.00 31.42           C  
ANISOU 3566  CD1 LEU B 246     4537   4065   3335    249     -7   -460       C  
ATOM   3567  CD2 LEU B 246      48.282   0.089   8.763  1.00 30.42           C  
ANISOU 3567  CD2 LEU B 246     4538   3899   3121    157    -58   -448       C  
ATOM   3568  N   TYR B 247      52.678   0.488   8.774  1.00 30.57           N  
ANISOU 3568  N   TYR B 247     4437   3939   3238    -61   -264   -451       N  
ATOM   3569  CA  TYR B 247      53.940  -0.237   8.721  1.00 31.01           C  
ANISOU 3569  CA  TYR B 247     4368   4023   3391    -95   -347   -428       C  
ATOM   3570  C   TYR B 247      53.615  -1.671   9.120  1.00 26.09           C  
ANISOU 3570  C   TYR B 247     3677   3412   2823    -47   -395   -383       C  
ATOM   3571  O   TYR B 247      53.230  -1.922  10.269  1.00 28.28           O  
ANISOU 3571  O   TYR B 247     4019   3692   3034    -69   -443   -344       O  
ATOM   3572  CB  TYR B 247      54.962   0.403   9.662  1.00 25.28           C  
ANISOU 3572  CB  TYR B 247     3676   3302   2626   -206   -432   -417       C  
ATOM   3573  CG  TYR B 247      56.341  -0.138   9.540  1.00 44.16           C  
ANISOU 3573  CG  TYR B 247     5920   5724   5134   -243   -518   -387       C  
ATOM   3574  CD1 TYR B 247      57.178   0.277   8.515  1.00 55.79           C  
ANISOU 3574  CD1 TYR B 247     7311   7200   6686   -260   -476   -418       C  
ATOM   3575  CD2 TYR B 247      56.829  -1.058  10.459  1.00 51.05           C  
ANISOU 3575  CD2 TYR B 247     6728   6623   6047   -262   -639   -319       C  
ATOM   3576  CE1 TYR B 247      58.465  -0.223   8.393  1.00 55.21           C  
ANISOU 3576  CE1 TYR B 247     7081   7154   6742   -289   -542   -393       C  
ATOM   3577  CE2 TYR B 247      58.117  -1.564  10.348  1.00 53.32           C  
ANISOU 3577  CE2 TYR B 247     6857   6933   6469   -285   -721   -281       C  
ATOM   3578  CZ  TYR B 247      58.928  -1.140   9.312  1.00 55.73           C  
ANISOU 3578  CZ  TYR B 247     7069   7240   6864   -296   -667   -324       C  
ATOM   3579  OH  TYR B 247      60.205  -1.628   9.194  1.00 62.30           O  
ANISOU 3579  OH  TYR B 247     7727   8096   7848   -314   -734   -290       O  
ATOM   3580  N   LEU B 248      53.776  -2.613   8.191  1.00 25.52           N  
ANISOU 3580  N   LEU B 248     3484   3343   2869     12   -375   -389       N  
ATOM   3581  CA  LEU B 248      53.269  -3.976   8.364  1.00 26.28           C  
ANISOU 3581  CA  LEU B 248     3524   3430   3031     67   -393   -358       C  
ATOM   3582  C   LEU B 248      54.400  -5.001   8.386  1.00 32.34           C  
ANISOU 3582  C   LEU B 248     4149   4187   3950     71   -465   -321       C  
ATOM   3583  O   LEU B 248      55.357  -4.902   7.613  1.00 31.09           O  
ANISOU 3583  O   LEU B 248     3897   4034   3881     66   -448   -353       O  
ATOM   3584  CB  LEU B 248      52.323  -4.341   7.228  1.00 27.18           C  
ANISOU 3584  CB  LEU B 248     3619   3542   3165    136   -299   -407       C  
ATOM   3585  CG  LEU B 248      51.219  -3.358   6.841  1.00 33.23           C  
ANISOU 3585  CG  LEU B 248     4486   4318   3821    153   -222   -438       C  
ATOM   3586  CD1 LEU B 248      50.621  -3.819   5.513  1.00 39.13           C  
ANISOU 3586  CD1 LEU B 248     5180   5082   4605    205   -155   -482       C  
ATOM   3587  CD2 LEU B 248      50.141  -3.302   7.897  1.00 33.04           C  
ANISOU 3587  CD2 LEU B 248     4554   4285   3713    159   -221   -406       C  
ATOM   3588  N   ASN B 249      54.268  -6.005   9.245  1.00 27.62           N  
ANISOU 3588  N   ASN B 249     3531   3571   3391     84   -536   -250       N  
ATOM   3589  CA  ASN B 249      55.151  -7.166   9.258  1.00 24.23           C  
ANISOU 3589  CA  ASN B 249     2959   3111   3136    113   -598   -201       C  
ATOM   3590  C   ASN B 249      54.336  -8.363   8.737  1.00 27.60           C  
ANISOU 3590  C   ASN B 249     3350   3489   3648    186   -537   -218       C  
ATOM   3591  O   ASN B 249      53.499  -8.913   9.461  1.00 27.37           O  
ANISOU 3591  O   ASN B 249     3378   3442   3578    193   -558   -166       O  
ATOM   3592  CB  ASN B 249      55.685  -7.372  10.675  1.00 34.53           C  
ANISOU 3592  CB  ASN B 249     4272   4426   4421     62   -741    -86       C  
ATOM   3593  CG  ASN B 249      56.701  -8.509  10.779  1.00 41.30           C  
ANISOU 3593  CG  ASN B 249     4968   5246   5480     97   -825     -9       C  
ATOM   3594  OD1 ASN B 249      57.064  -9.130   9.776  1.00 38.80           O  
ANISOU 3594  OD1 ASN B 249     4530   4886   5327    162   -759    -58       O  
ATOM   3595  ND2 ASN B 249      57.188  -8.766  12.006  1.00 36.64           N  
ANISOU 3595  ND2 ASN B 249     4374   4671   4876     52   -971    114       N  
ATOM   3596  N   ILE B 250      54.551  -8.744   7.474  1.00 25.11           N  
ANISOU 3596  N   ILE B 250     2948   3154   3440    230   -452   -300       N  
ATOM   3597  CA  ILE B 250      53.808  -9.828   6.809  1.00 29.04           C  
ANISOU 3597  CA  ILE B 250     3414   3604   4015    284   -382   -344       C  
ATOM   3598  C   ILE B 250      54.786 -10.936   6.462  1.00 27.84           C  
ANISOU 3598  C   ILE B 250     3115   3384   4080    327   -384   -346       C  
ATOM   3599  O   ILE B 250      55.669 -10.738   5.616  1.00 33.79           O  
ANISOU 3599  O   ILE B 250     3784   4144   4910    332   -333   -410       O  
ATOM   3600  CB  ILE B 250      53.114  -9.351   5.518  1.00 28.84           C  
ANISOU 3600  CB  ILE B 250     3426   3615   3917    289   -269   -456       C  
ATOM   3601  CG1 ILE B 250      52.296  -8.082   5.770  1.00 27.26           C  
ANISOU 3601  CG1 ILE B 250     3355   3474   3530    259   -261   -451       C  
ATOM   3602  CG2 ILE B 250      52.283 -10.515   4.852  1.00 25.58           C  
ANISOU 3602  CG2 ILE B 250     2986   3159   3573    325   -206   -512       C  
ATOM   3603  CD1 ILE B 250      51.528  -7.611   4.549  1.00 31.17           C  
ANISOU 3603  CD1 ILE B 250     3883   4008   3951    268   -170   -531       C  
ATOM   3604  N   ASN B 251      54.608 -12.110   7.064  1.00 36.41           N  
ANISOU 3604  N   ASN B 251     4168   4395   5273    359   -429   -277       N  
ATOM   3605  CA  ASN B 251      55.516 -13.231   6.824  1.00 32.52           C  
ANISOU 3605  CA  ASN B 251     3530   3812   5016    414   -429   -266       C  
ATOM   3606  C   ASN B 251      56.968 -12.778   6.927  1.00 30.72           C  
ANISOU 3606  C   ASN B 251     3192   3606   4873    409   -483   -233       C  
ATOM   3607  O   ASN B 251      57.791 -13.051   6.059  1.00 34.10           O  
ANISOU 3607  O   ASN B 251     3500   4004   5452    442   -411   -303       O  
ATOM   3608  CB  ASN B 251      55.243 -13.872   5.464  1.00 28.40           C  
ANISOU 3608  CB  ASN B 251     2966   3243   4582    449   -289   -408       C  
ATOM   3609  CG  ASN B 251      53.976 -14.685   5.464  1.00 37.26           C  
ANISOU 3609  CG  ASN B 251     4154   4316   5686    455   -256   -424       C  
ATOM   3610  OD1 ASN B 251      53.132 -14.547   6.364  1.00 33.20           O  
ANISOU 3610  OD1 ASN B 251     3732   3824   5057    429   -317   -342       O  
ATOM   3611  ND2 ASN B 251      53.824 -15.543   4.451  1.00 35.13           N  
ANISOU 3611  ND2 ASN B 251     3838   3980   5528    479   -152   -537       N  
ATOM   3612  N   ASP B 252      57.252 -12.014   7.980  1.00 35.69           N  
ANISOU 3612  N   ASP B 252     3869   4298   5395    354   -602   -134       N  
ATOM   3613  CA  ASP B 252      58.613 -11.620   8.337  1.00 44.09           C  
ANISOU 3613  CA  ASP B 252     4825   5390   6536    332   -691    -74       C  
ATOM   3614  C   ASP B 252      59.261 -10.745   7.266  1.00 40.59           C  
ANISOU 3614  C   ASP B 252     4333   4997   6093    310   -596   -187       C  
ATOM   3615  O   ASP B 252      60.466 -10.793   7.042  1.00 49.91           O  
ANISOU 3615  O   ASP B 252     5364   6173   7426    319   -609   -179       O  
ATOM   3616  CB  ASP B 252      59.471 -12.846   8.653  1.00 54.83           C  
ANISOU 3616  CB  ASP B 252     6021   6663   8150    399   -758     20       C  
ATOM   3617  CG  ASP B 252      59.327 -13.286  10.103  1.00 74.19           C  
ANISOU 3617  CG  ASP B 252     8512   9104  10572    381   -922    194       C  
ATOM   3618  OD1 ASP B 252      59.182 -12.400  10.985  1.00 79.58           O  
ANISOU 3618  OD1 ASP B 252     9305   9876  11056    295  -1017    250       O  
ATOM   3619  OD2 ASP B 252      59.350 -14.509  10.364  1.00 84.17           O  
ANISOU 3619  OD2 ASP B 252     9708  10269  12005    446   -952    275       O  
ATOM   3620  N   GLU B 253      58.461  -9.931   6.602  1.00 33.16           N  
ANISOU 3620  N   GLU B 253     3513   4102   4984    280   -501   -284       N  
ATOM   3621  CA  GLU B 253      58.982  -8.848   5.780  1.00 31.40           C  
ANISOU 3621  CA  GLU B 253     3284   3938   4707    235   -429   -364       C  
ATOM   3622  C   GLU B 253      58.248  -7.587   6.179  1.00 32.48           C  
ANISOU 3622  C   GLU B 253     3591   4136   4615    169   -449   -361       C  
ATOM   3623  O   GLU B 253      57.088  -7.643   6.597  1.00 30.00           O  
ANISOU 3623  O   GLU B 253     3396   3817   4186    177   -454   -346       O  
ATOM   3624  CB  GLU B 253      58.796  -9.095   4.297  1.00 31.96           C  
ANISOU 3624  CB  GLU B 253     3328   3998   4816    268   -269   -493       C  
ATOM   3625  CG  GLU B 253      59.652 -10.210   3.760  1.00 57.60           C  
ANISOU 3625  CG  GLU B 253     6405   7179   8301    329   -214   -527       C  
ATOM   3626  CD  GLU B 253      61.100  -9.796   3.622  1.00 72.21           C  
ANISOU 3626  CD  GLU B 253     8112   9053  10270    306   -217   -519       C  
ATOM   3627  OE1 GLU B 253      61.839  -9.843   4.628  1.00 78.71           O  
ANISOU 3627  OE1 GLU B 253     8855   9874  11177    299   -351   -406       O  
ATOM   3628  OE2 GLU B 253      61.492  -9.401   2.503  1.00 77.95           O  
ANISOU 3628  OE2 GLU B 253     8806   9811  10999    287    -88   -620       O  
ATOM   3629  N   LYS B 254      58.931  -6.457   6.050  1.00 30.06           N  
ANISOU 3629  N   LYS B 254     3291   3877   4255    103   -450   -376       N  
ATOM   3630  CA  LYS B 254      58.405  -5.176   6.492  1.00 28.96           C  
ANISOU 3630  CA  LYS B 254     3307   3775   3921     36   -466   -374       C  
ATOM   3631  C   LYS B 254      57.876  -4.411   5.289  1.00 32.65           C  
ANISOU 3631  C   LYS B 254     3844   4260   4302     36   -335   -462       C  
ATOM   3632  O   LYS B 254      58.548  -4.319   4.260  1.00 32.70           O  
ANISOU 3632  O   LYS B 254     3769   4277   4377     32   -256   -517       O  
ATOM   3633  CB  LYS B 254      59.491  -4.372   7.208  1.00 37.52           C  
ANISOU 3633  CB  LYS B 254     4366   4891   4999    -54   -562   -330       C  
ATOM   3634  CG  LYS B 254      60.190  -5.160   8.324  1.00 44.48           C  
ANISOU 3634  CG  LYS B 254     5153   5771   5978    -60   -713   -225       C  
ATOM   3635  CD  LYS B 254      59.226  -5.642   9.403  1.00 51.16           C  
ANISOU 3635  CD  LYS B 254     6109   6604   6727    -48   -785   -157       C  
ATOM   3636  CE  LYS B 254      59.895  -6.670  10.342  1.00 58.27           C  
ANISOU 3636  CE  LYS B 254     6900   7493   7747    -37   -932    -34       C  
ATOM   3637  NZ  LYS B 254      60.100  -8.030   9.725  1.00 49.87           N  
ANISOU 3637  NZ  LYS B 254     5684   6362   6901     70   -893    -23       N  
ATOM   3638  N   TYR B 255      56.670  -3.875   5.413  1.00 26.00           N  
ANISOU 3638  N   TYR B 255     3147   3420   3312     41   -309   -470       N  
ATOM   3639  CA  TYR B 255      56.036  -3.148   4.323  1.00 26.46           C  
ANISOU 3639  CA  TYR B 255     3276   3496   3283     47   -203   -529       C  
ATOM   3640  C   TYR B 255      55.734  -1.753   4.837  1.00 24.57           C  
ANISOU 3640  C   TYR B 255     3172   3255   2908     -5   -213   -512       C  
ATOM   3641  O   TYR B 255      54.878  -1.580   5.712  1.00 31.07           O  
ANISOU 3641  O   TYR B 255     4094   4065   3648      3   -244   -485       O  
ATOM   3642  CB  TYR B 255      54.784  -3.857   3.821  1.00 24.48           C  
ANISOU 3642  CB  TYR B 255     3054   3242   3007    114   -153   -554       C  
ATOM   3643  CG  TYR B 255      55.159  -5.160   3.152  1.00 28.03           C  
ANISOU 3643  CG  TYR B 255     3379   3678   3595    154   -120   -595       C  
ATOM   3644  CD1 TYR B 255      55.370  -6.311   3.911  1.00 28.20           C  
ANISOU 3644  CD1 TYR B 255     3327   3655   3731    185   -185   -555       C  
ATOM   3645  CD2 TYR B 255      55.362  -5.235   1.766  1.00 24.56           C  
ANISOU 3645  CD2 TYR B 255     2897   3262   3172    155    -20   -673       C  
ATOM   3646  CE1 TYR B 255      55.749  -7.523   3.304  1.00 30.77           C  
ANISOU 3646  CE1 TYR B 255     3537   3944   4209    227   -143   -599       C  
ATOM   3647  CE2 TYR B 255      55.749  -6.445   1.160  1.00 29.64           C  
ANISOU 3647  CE2 TYR B 255     3431   3881   3950    188     28   -730       C  
ATOM   3648  CZ  TYR B 255      55.943  -7.587   1.937  1.00 32.94           C  
ANISOU 3648  CZ  TYR B 255     3773   4238   4504    229    -30   -696       C  
ATOM   3649  OH  TYR B 255      56.349  -8.811   1.360  1.00 32.74           O  
ANISOU 3649  OH  TYR B 255     3638   4163   4637    268     28   -757       O  
ATOM   3650  N   ASP B 256      56.534  -0.797   4.386  1.00 27.65           N  
ANISOU 3650  N   ASP B 256     3564   3654   3288    -63   -178   -531       N  
ATOM   3651  CA  ASP B 256      56.462   0.606   4.773  1.00 26.44           C  
ANISOU 3651  CA  ASP B 256     3530   3481   3035   -129   -182   -523       C  
ATOM   3652  C   ASP B 256      55.525   1.315   3.824  1.00 28.37           C  
ANISOU 3652  C   ASP B 256     3871   3716   3194    -94    -86   -539       C  
ATOM   3653  O   ASP B 256      55.923   1.776   2.776  1.00 32.17           O  
ANISOU 3653  O   ASP B 256     4333   4211   3681   -112    -18   -557       O  
ATOM   3654  CB  ASP B 256      57.856   1.217   4.689  1.00 29.72           C  
ANISOU 3654  CB  ASP B 256     3881   3906   3507   -220   -200   -527       C  
ATOM   3655  CG  ASP B 256      57.930   2.605   5.281  1.00 45.08           C  
ANISOU 3655  CG  ASP B 256     5952   5817   5360   -308   -212   -525       C  
ATOM   3656  OD1 ASP B 256      56.910   3.115   5.768  1.00 47.87           O  
ANISOU 3656  OD1 ASP B 256     6445   6133   5610   -290   -202   -524       O  
ATOM   3657  OD2 ASP B 256      59.020   3.192   5.251  1.00 46.61           O  
ANISOU 3657  OD2 ASP B 256     6101   6015   5592   -398   -226   -530       O  
ATOM   3658  N   MET B 257      54.275   1.429   4.217  1.00 23.18           N  
ANISOU 3658  N   MET B 257     3311   3037   2460    -46    -80   -526       N  
ATOM   3659  CA  MET B 257      53.288   2.001   3.332  1.00 21.79           C  
ANISOU 3659  CA  MET B 257     3195   2859   2226      6     -4   -525       C  
ATOM   3660  C   MET B 257      53.035   3.496   3.408  1.00 25.01           C  
ANISOU 3660  C   MET B 257     3728   3210   2564    -23     33   -511       C  
ATOM   3661  O   MET B 257      53.622   4.192   4.215  1.00 26.37           O  
ANISOU 3661  O   MET B 257     3952   3342   2725    -93      7   -517       O  
ATOM   3662  CB  MET B 257      52.027   1.187   3.445  1.00 24.80           C  
ANISOU 3662  CB  MET B 257     3580   3251   2591     84     -9   -517       C  
ATOM   3663  CG  MET B 257      52.373  -0.278   3.262  1.00 33.32           C  
ANISOU 3663  CG  MET B 257     4530   4370   3759    101    -30   -540       C  
ATOM   3664  SD  MET B 257      50.997  -1.364   3.015  1.00 37.94           S  
ANISOU 3664  SD  MET B 257     5096   4973   4345    175    -26   -542       S  
ATOM   3665  CE  MET B 257      50.206  -0.682   1.574  1.00 28.40           C  
ANISOU 3665  CE  MET B 257     3914   3807   3070    207     41   -550       C  
ATOM   3666  N   LYS B 258      52.185   3.974   2.513  1.00 23.99           N  
ANISOU 3666  N   LYS B 258     3642   3077   2395     26     93   -489       N  
ATOM   3667  CA  LYS B 258      51.858   5.383   2.446  1.00 28.26           C  
ANISOU 3667  CA  LYS B 258     4300   3547   2891     20    141   -462       C  
ATOM   3668  C   LYS B 258      50.376   5.696   2.613  1.00 26.53           C  
ANISOU 3668  C   LYS B 258     4138   3303   2641    115    169   -431       C  
ATOM   3669  O   LYS B 258      49.909   6.739   2.211  1.00 28.75           O  
ANISOU 3669  O   LYS B 258     4489   3533   2903    143    216   -389       O  
ATOM   3670  CB  LYS B 258      52.465   6.033   1.207  1.00 32.84           C  
ANISOU 3670  CB  LYS B 258     4875   4136   3467    -21    187   -441       C  
ATOM   3671  CG  LYS B 258      53.962   6.227   1.315  1.00 29.88           C  
ANISOU 3671  CG  LYS B 258     4456   3763   3133   -127    176   -470       C  
ATOM   3672  CD  LYS B 258      54.327   7.010   2.563  1.00 33.92           C  
ANISOU 3672  CD  LYS B 258     5061   4190   3637   -191    154   -484       C  
ATOM   3673  CE  LYS B 258      55.791   7.403   2.580  1.00 42.38           C  
ANISOU 3673  CE  LYS B 258     6091   5261   4751   -315    136   -505       C  
ATOM   3674  NZ  LYS B 258      56.667   6.392   3.224  1.00 41.97           N  
ANISOU 3674  NZ  LYS B 258     5902   5280   4765   -346     62   -531       N  
ATOM   3675  N   ILE B 259      49.641   4.735   3.148  1.00 23.07           N  
ANISOU 3675  N   ILE B 259     3662   2896   2208    166    142   -442       N  
ATOM   3676  CA  ILE B 259      48.253   4.942   3.543  1.00 27.98           C  
ANISOU 3676  CA  ILE B 259     4327   3489   2814    247    172   -420       C  
ATOM   3677  C   ILE B 259      48.180   4.691   5.046  1.00 30.07           C  
ANISOU 3677  C   ILE B 259     4635   3726   3065    226    157   -453       C  
ATOM   3678  O   ILE B 259      49.100   4.134   5.646  1.00 27.45           O  
ANISOU 3678  O   ILE B 259     4278   3415   2737    159    102   -479       O  
ATOM   3679  CB  ILE B 259      47.279   4.018   2.803  1.00 29.43           C  
ANISOU 3679  CB  ILE B 259     4426   3748   3009    318    161   -398       C  
ATOM   3680  CG1 ILE B 259      47.655   2.549   3.126  1.00 27.72           C  
ANISOU 3680  CG1 ILE B 259     4123   3589   2822    294    110   -436       C  
ATOM   3681  CG2 ILE B 259      47.323   4.304   1.319  1.00 31.63           C  
ANISOU 3681  CG2 ILE B 259     4679   4067   3272    323    171   -363       C  
ATOM   3682  CD1 ILE B 259      46.868   1.533   2.390  1.00 27.27           C  
ANISOU 3682  CD1 ILE B 259     3981   3600   2780    338     98   -434       C  
ATOM   3683  N   ALA B 260      47.070   5.119   5.647  1.00 25.70           N  
ANISOU 3683  N   ALA B 260     4142   3127   2496    284    208   -447       N  
ATOM   3684  CA  ALA B 260      46.889   5.047   7.090  1.00 28.92           C  
ANISOU 3684  CA  ALA B 260     4616   3506   2867    257    217   -482       C  
ATOM   3685  C   ALA B 260      45.603   4.308   7.390  1.00 28.69           C  
ANISOU 3685  C   ALA B 260     4545   3508   2846    332    242   -467       C  
ATOM   3686  O   ALA B 260      44.940   3.848   6.467  1.00 32.52           O  
ANISOU 3686  O   ALA B 260     4944   4040   3371    397    239   -432       O  
ATOM   3687  CB  ALA B 260      46.845   6.451   7.711  1.00 29.92           C  
ANISOU 3687  CB  ALA B 260     4881   3526   2963    235    288   -513       C  
ATOM   3688  N   GLY B 261      45.214   4.255   8.660  1.00 29.23           N  
ANISOU 3688  N   GLY B 261     4680   3556   2871    315    272   -494       N  
ATOM   3689  CA  GLY B 261      43.984   3.629   9.095  1.00 30.81           C  
ANISOU 3689  CA  GLY B 261     4847   3781   3077    374    314   -481       C  
ATOM   3690  C   GLY B 261      44.236   2.197   9.521  1.00 36.54           C  
ANISOU 3690  C   GLY B 261     5509   4578   3797    335    240   -469       C  
ATOM   3691  O   GLY B 261      44.733   1.384   8.721  1.00 30.64           O  
ANISOU 3691  O   GLY B 261     4666   3878   3096    331    170   -450       O  
ATOM   3692  N   ASP B 262      43.881   1.885  10.776  1.00 31.35           N  
ANISOU 3692  N   ASP B 262     4909   3921   3083    303    264   -478       N  
ATOM   3693  CA  ASP B 262      44.077   0.535  11.313  1.00 31.05           C  
ANISOU 3693  CA  ASP B 262     4822   3936   3038    263    195   -448       C  
ATOM   3694  C   ASP B 262      43.349  -0.497  10.471  1.00 35.00           C  
ANISOU 3694  C   ASP B 262     5194   4480   3624    326    185   -416       C  
ATOM   3695  O   ASP B 262      43.890  -1.564  10.169  1.00 37.68           O  
ANISOU 3695  O   ASP B 262     5458   4850   4010    306    108   -395       O  
ATOM   3696  CB  ASP B 262      43.577   0.470  12.759  1.00 29.32           C  
ANISOU 3696  CB  ASP B 262     4698   3714   2727    220    244   -455       C  
ATOM   3697  CG  ASP B 262      44.493   1.148  13.724  1.00 37.74           C  
ANISOU 3697  CG  ASP B 262     5892   4758   3689    121    218   -488       C  
ATOM   3698  OD1 ASP B 262      45.584   1.578  13.312  1.00 45.61           O  
ANISOU 3698  OD1 ASP B 262     6889   5744   4698     82    150   -500       O  
ATOM   3699  OD2 ASP B 262      44.120   1.262  14.905  1.00 52.04           O  
ANISOU 3699  OD2 ASP B 262     7805   6568   5398     72    268   -507       O  
ATOM   3700  N   PHE B 263      42.124  -0.166  10.060  1.00 35.39           N  
ANISOU 3700  N   PHE B 263     5215   4528   3705    401    265   -414       N  
ATOM   3701  CA  PHE B 263      41.279  -1.037   9.251  1.00 41.08           C  
ANISOU 3701  CA  PHE B 263     5814   5295   4499    451    257   -389       C  
ATOM   3702  C   PHE B 263      41.947  -1.428   7.934  1.00 39.84           C  
ANISOU 3702  C   PHE B 263     5578   5169   4392    451    183   -390       C  
ATOM   3703  O   PHE B 263      41.700  -2.520   7.406  1.00 44.78           O  
ANISOU 3703  O   PHE B 263     6113   5833   5067    452    147   -385       O  
ATOM   3704  CB  PHE B 263      39.964  -0.297   8.998  1.00 51.92           C  
ANISOU 3704  CB  PHE B 263     7167   6661   5900    532    347   -381       C  
ATOM   3705  CG  PHE B 263      40.141   1.212   8.883  1.00 53.39           C  
ANISOU 3705  CG  PHE B 263     7435   6783   6067    564    399   -396       C  
ATOM   3706  CD1 PHE B 263      40.104   2.020  10.011  1.00 58.24           C  
ANISOU 3706  CD1 PHE B 263     8168   7335   6627    547    482   -431       C  
ATOM   3707  CD2 PHE B 263      40.382   1.809   7.652  1.00 56.44           C  
ANISOU 3707  CD2 PHE B 263     7791   7167   6485    599    369   -377       C  
ATOM   3708  CE1 PHE B 263      40.284   3.400   9.912  1.00 61.94           C  
ANISOU 3708  CE1 PHE B 263     8719   7723   7091    571    537   -452       C  
ATOM   3709  CE2 PHE B 263      40.553   3.183   7.546  1.00 62.15           C  
ANISOU 3709  CE2 PHE B 263     8594   7816   7203    625    419   -380       C  
ATOM   3710  CZ  PHE B 263      40.507   3.977   8.679  1.00 59.62           C  
ANISOU 3710  CZ  PHE B 263     8389   7417   6846    613    504   -421       C  
ATOM   3711  N   ASN B 264      42.800  -0.555   7.398  1.00 25.75           N  
ANISOU 3711  N   ASN B 264     3831   3362   2589    442    168   -404       N  
ATOM   3712  CA  ASN B 264      43.476  -0.804   6.135  1.00 27.42           C  
ANISOU 3712  CA  ASN B 264     3979   3605   2833    435    119   -412       C  
ATOM   3713  C   ASN B 264      44.567  -1.866   6.213  1.00 24.33           C  
ANISOU 3713  C   ASN B 264     3546   3226   2474    380     52   -427       C  
ATOM   3714  O   ASN B 264      45.012  -2.318   5.160  1.00 28.98           O  
ANISOU 3714  O   ASN B 264     4068   3843   3100    375     29   -447       O  
ATOM   3715  CB  ASN B 264      44.090   0.491   5.596  1.00 25.66           C  
ANISOU 3715  CB  ASN B 264     3815   3352   2584    432    134   -414       C  
ATOM   3716  CG  ASN B 264      43.146   1.255   4.709  1.00 30.91           C  
ANISOU 3716  CG  ASN B 264     4468   4022   3253    500    173   -381       C  
ATOM   3717  OD1 ASN B 264      42.250   0.665   4.089  1.00 28.75           O  
ANISOU 3717  OD1 ASN B 264     4114   3803   3006    537    163   -363       O  
ATOM   3718  ND2 ASN B 264      43.353   2.586   4.615  1.00 25.28           N  
ANISOU 3718  ND2 ASN B 264     3834   3250   2522    511    211   -368       N  
ATOM   3719  N   ALA B 265      45.034  -2.259   7.402  1.00 22.54           N  
ANISOU 3719  N   ALA B 265     3354   2977   2235    338     24   -418       N  
ATOM   3720  CA  ALA B 265      45.966  -3.392   7.468  1.00 23.55           C  
ANISOU 3720  CA  ALA B 265     3418   3108   2422    302    -45   -414       C  
ATOM   3721  C   ALA B 265      45.373  -4.644   6.822  1.00 25.00           C  
ANISOU 3721  C   ALA B 265     3508   3311   2680    328    -46   -420       C  
ATOM   3722  O   ALA B 265      46.039  -5.327   6.038  1.00 26.35           O  
ANISOU 3722  O   ALA B 265     3607   3485   2920    322    -70   -447       O  
ATOM   3723  CB  ALA B 265      46.357  -3.704   8.910  1.00 20.55           C  
ANISOU 3723  CB  ALA B 265     3089   2709   2011    254    -88   -377       C  
ATOM   3724  N   TYR B 266      44.125  -4.967   7.144  1.00 22.36           N  
ANISOU 3724  N   TYR B 266     3172   2987   2338    351    -12   -403       N  
ATOM   3725  CA  TYR B 266      43.506  -6.157   6.547  1.00 24.10           C  
ANISOU 3725  CA  TYR B 266     3305   3222   2629    361    -14   -415       C  
ATOM   3726  C   TYR B 266      43.338  -6.008   5.043  1.00 24.60           C  
ANISOU 3726  C   TYR B 266     3315   3327   2703    379     -5   -461       C  
ATOM   3727  O   TYR B 266      43.476  -6.987   4.298  1.00 24.14           O  
ANISOU 3727  O   TYR B 266     3190   3275   2706    364    -19   -500       O  
ATOM   3728  CB  TYR B 266      42.152  -6.430   7.188  1.00 20.21           C  
ANISOU 3728  CB  TYR B 266     2814   2738   2125    373     26   -385       C  
ATOM   3729  CG  TYR B 266      42.226  -7.292   8.413  1.00 26.73           C  
ANISOU 3729  CG  TYR B 266     3662   3531   2965    337     10   -340       C  
ATOM   3730  CD1 TYR B 266      42.506  -8.671   8.308  1.00 23.36           C  
ANISOU 3730  CD1 TYR B 266     3173   3073   2629    315    -29   -333       C  
ATOM   3731  CD2 TYR B 266      42.006  -6.742   9.679  1.00 22.54           C  
ANISOU 3731  CD2 TYR B 266     3220   2993   2352    321     38   -303       C  
ATOM   3732  CE1 TYR B 266      42.547  -9.471   9.436  1.00 26.67           C  
ANISOU 3732  CE1 TYR B 266     3615   3456   3062    282    -50   -269       C  
ATOM   3733  CE2 TYR B 266      42.057  -7.531  10.812  1.00 32.30           C  
ANISOU 3733  CE2 TYR B 266     4486   4208   3578    277     19   -248       C  
ATOM   3734  CZ  TYR B 266      42.320  -8.899  10.682  1.00 31.69           C  
ANISOU 3734  CZ  TYR B 266     4343   4101   3598    260    -30   -221       C  
ATOM   3735  OH  TYR B 266      42.356  -9.671  11.807  1.00 33.02           O  
ANISOU 3735  OH  TYR B 266     4546   4244   3757    217    -54   -146       O  
ATOM   3736  N   ASN B 267      43.043  -4.790   4.566  1.00 23.55           N  
ANISOU 3736  N   ASN B 267     3218   3220   2511    406     22   -456       N  
ATOM   3737  CA  ASN B 267      42.922  -4.600   3.122  1.00 28.40           C  
ANISOU 3737  CA  ASN B 267     3793   3885   3114    413     20   -483       C  
ATOM   3738  C   ASN B 267      44.265  -4.776   2.431  1.00 27.67           C  
ANISOU 3738  C   ASN B 267     3688   3789   3036    377      6   -528       C  
ATOM   3739  O   ASN B 267      44.338  -5.352   1.337  1.00 24.52           O  
ANISOU 3739  O   ASN B 267     3239   3428   2650    358      5   -576       O  
ATOM   3740  CB  ASN B 267      42.339  -3.223   2.814  1.00 24.53           C  
ANISOU 3740  CB  ASN B 267     3344   3411   2565    454     46   -446       C  
ATOM   3741  CG  ASN B 267      40.964  -3.028   3.430  1.00 31.08           C  
ANISOU 3741  CG  ASN B 267     4165   4243   3400    500     77   -405       C  
ATOM   3742  OD1 ASN B 267      40.179  -3.969   3.538  1.00 28.89           O  
ANISOU 3742  OD1 ASN B 267     3823   3991   3161    495     72   -408       O  
ATOM   3743  ND2 ASN B 267      40.682  -1.803   3.865  1.00 35.44           N  
ANISOU 3743  ND2 ASN B 267     4779   4761   3925    543    120   -371       N  
ATOM   3744  N   ALA B 268      45.337  -4.278   3.052  1.00 21.53           N  
ANISOU 3744  N   ALA B 268     2954   2970   2257    360     -1   -518       N  
ATOM   3745  CA  ALA B 268      46.660  -4.463   2.483  1.00 22.17           C  
ANISOU 3745  CA  ALA B 268     3004   3046   2372    327     -8   -557       C  
ATOM   3746  C   ALA B 268      47.012  -5.941   2.422  1.00 23.75           C  
ANISOU 3746  C   ALA B 268     3126   3227   2671    316    -22   -595       C  
ATOM   3747  O   ALA B 268      47.556  -6.411   1.426  1.00 22.40           O  
ANISOU 3747  O   ALA B 268     2904   3071   2536    299      0   -655       O  
ATOM   3748  CB  ALA B 268      47.711  -3.718   3.298  1.00 21.35           C  
ANISOU 3748  CB  ALA B 268     2946   2904   2261    302    -26   -533       C  
ATOM   3749  N   LEU B 269      46.689  -6.693   3.471  1.00 24.11           N  
ANISOU 3749  N   LEU B 269     3165   3234   2762    322    -50   -562       N  
ATOM   3750  CA  LEU B 269      47.035  -8.117   3.465  1.00 22.25           C  
ANISOU 3750  CA  LEU B 269     2857   2957   2641    316    -62   -586       C  
ATOM   3751  C   LEU B 269      46.195  -8.887   2.445  1.00 22.33           C  
ANISOU 3751  C   LEU B 269     2825   2991   2669    313    -30   -649       C  
ATOM   3752  O   LEU B 269      46.673  -9.867   1.855  1.00 26.48           O  
ANISOU 3752  O   LEU B 269     3292   3485   3283    301    -12   -711       O  
ATOM   3753  CB  LEU B 269      46.863  -8.685   4.871  1.00 24.93           C  
ANISOU 3753  CB  LEU B 269     3211   3247   3013    317   -104   -515       C  
ATOM   3754  CG  LEU B 269      47.090 -10.188   5.104  1.00 28.34           C  
ANISOU 3754  CG  LEU B 269     3578   3612   3577    317   -123   -510       C  
ATOM   3755  CD1 LEU B 269      48.525 -10.626   4.805  1.00 21.35           C  
ANISOU 3755  CD1 LEU B 269     2623   2683   2806    321   -138   -532       C  
ATOM   3756  CD2 LEU B 269      46.702 -10.517   6.531  1.00 21.09           C  
ANISOU 3756  CD2 LEU B 269     2701   2663   2649    308   -164   -417       C  
ATOM   3757  N   ALA B 270      44.935  -8.477   2.260  1.00 26.18           N  
ANISOU 3757  N   ALA B 270     3337   3530   3081    320    -21   -635       N  
ATOM   3758  CA  ALA B 270      44.078  -9.111   1.273  1.00 24.27           C  
ANISOU 3758  CA  ALA B 270     3053   3329   2839    301     -7   -691       C  
ATOM   3759  C   ALA B 270      44.660  -8.907  -0.117  1.00 30.36           C  
ANISOU 3759  C   ALA B 270     3814   4147   3574    276     18   -765       C  
ATOM   3760  O   ALA B 270      44.773  -9.857  -0.907  1.00 24.19           O  
ANISOU 3760  O   ALA B 270     2993   3362   2835    242     40   -850       O  
ATOM   3761  CB  ALA B 270      42.661  -8.546   1.363  1.00 21.89           C  
ANISOU 3761  CB  ALA B 270     2763   3084   2469    318    -12   -645       C  
ATOM   3762  N   ALA B 271      45.096  -7.676  -0.394  1.00 22.05           N  
ANISOU 3762  N   ALA B 271     2806   3130   2442    286     23   -738       N  
ATOM   3763  CA  ALA B 271      45.790  -7.353  -1.637  1.00 22.10           C  
ANISOU 3763  CA  ALA B 271     2815   3183   2400    254     56   -795       C  
ATOM   3764  C   ALA B 271      47.114  -8.104  -1.757  1.00 24.25           C  
ANISOU 3764  C   ALA B 271     3042   3400   2770    237     92   -863       C  
ATOM   3765  O   ALA B 271      47.432  -8.667  -2.812  1.00 23.62           O  
ANISOU 3765  O   ALA B 271     2937   3343   2695    200    139   -955       O  
ATOM   3766  CB  ALA B 271      46.001  -5.829  -1.704  1.00 24.90           C  
ANISOU 3766  CB  ALA B 271     3230   3565   2664    268     56   -731       C  
ATOM   3767  N   TYR B 272      47.903  -8.131  -0.684  1.00 27.60           N  
ANISOU 3767  N   TYR B 272     3454   3755   3276    260     72   -820       N  
ATOM   3768  CA  TYR B 272      49.147  -8.907  -0.688  1.00 27.84           C  
ANISOU 3768  CA  TYR B 272     3419   3726   3434    257     98   -868       C  
ATOM   3769  C   TYR B 272      48.902 -10.362  -1.089  1.00 29.26           C  
ANISOU 3769  C   TYR B 272     3544   3861   3712    250    128   -948       C  
ATOM   3770  O   TYR B 272      49.644 -10.941  -1.895  1.00 28.46           O  
ANISOU 3770  O   TYR B 272     3395   3741   3678    235    193  -1040       O  
ATOM   3771  CB  TYR B 272      49.772  -8.823   0.696  1.00 25.51           C  
ANISOU 3771  CB  TYR B 272     3114   3369   3208    281     41   -784       C  
ATOM   3772  CG  TYR B 272      50.975  -9.696   0.924  1.00 28.63           C  
ANISOU 3772  CG  TYR B 272     3421   3693   3765    292     43   -801       C  
ATOM   3773  CD1 TYR B 272      50.841 -11.039   1.310  1.00 29.15           C  
ANISOU 3773  CD1 TYR B 272     3435   3680   3961    314     32   -804       C  
ATOM   3774  CD2 TYR B 272      52.246  -9.180   0.780  1.00 35.18           C  
ANISOU 3774  CD2 TYR B 272     4209   4526   4631    282     56   -804       C  
ATOM   3775  CE1 TYR B 272      51.937 -11.814   1.541  1.00 32.40           C  
ANISOU 3775  CE1 TYR B 272     3756   4014   4542    338     32   -803       C  
ATOM   3776  CE2 TYR B 272      53.341  -9.939   1.009  1.00 33.76           C  
ANISOU 3776  CE2 TYR B 272     3927   4282   4617    301     54   -808       C  
ATOM   3777  CZ  TYR B 272      53.190 -11.257   1.386  1.00 36.45           C  
ANISOU 3777  CZ  TYR B 272     4215   4540   5094    335     41   -804       C  
ATOM   3778  OH  TYR B 272      54.317 -11.997   1.601  1.00 33.37           O  
ANISOU 3778  OH  TYR B 272     3712   4075   4892    367     39   -796       O  
ATOM   3779  N   THR B 273      47.863 -10.965  -0.524  1.00 27.35           N  
ANISOU 3779  N   THR B 273     3310   3595   3485    258     93   -918       N  
ATOM   3780  CA  THR B 273      47.573 -12.381  -0.769  1.00 27.68           C  
ANISOU 3780  CA  THR B 273     3307   3575   3634    245    119   -988       C  
ATOM   3781  C   THR B 273      47.241 -12.627  -2.230  1.00 26.47           C  
ANISOU 3781  C   THR B 273     3157   3481   3420    192    177  -1111       C  
ATOM   3782  O   THR B 273      47.724 -13.591  -2.830  1.00 27.25           O  
ANISOU 3782  O   THR B 273     3217   3524   3612    173    240  -1217       O  
ATOM   3783  CB  THR B 273      46.415 -12.821   0.118  1.00 26.41           C  
ANISOU 3783  CB  THR B 273     3161   3391   3482    249     71   -921       C  
ATOM   3784  OG1 THR B 273      46.781 -12.625   1.479  1.00 26.68           O  
ANISOU 3784  OG1 THR B 273     3206   3377   3554    284     21   -810       O  
ATOM   3785  CG2 THR B 273      46.074 -14.292  -0.087  1.00 31.65           C  
ANISOU 3785  CG2 THR B 273     3785   3975   4266    225     98   -989       C  
ATOM   3786  N   VAL B 274      46.394 -11.778  -2.815  1.00 29.24           N  
ANISOU 3786  N   VAL B 274     3555   3943   3612    166    157  -1099       N  
ATOM   3787  CA  VAL B 274      46.117 -11.885  -4.246  1.00 34.50           C  
ANISOU 3787  CA  VAL B 274     4235   4690   4185    102    198  -1204       C  
ATOM   3788  C   VAL B 274      47.418 -11.853  -5.024  1.00 32.42           C  
ANISOU 3788  C   VAL B 274     3962   4421   3937     85    281  -1289       C  
ATOM   3789  O   VAL B 274      47.648 -12.674  -5.910  1.00 36.50           O  
ANISOU 3789  O   VAL B 274     4464   4927   4476     36    352  -1420       O  
ATOM   3790  CB  VAL B 274      45.164 -10.765  -4.716  1.00 31.82           C  
ANISOU 3790  CB  VAL B 274     3942   4476   3671     87    147  -1141       C  
ATOM   3791  CG1 VAL B 274      45.180 -10.643  -6.242  1.00 24.21           C  
ANISOU 3791  CG1 VAL B 274     3005   3613   2579     13    182  -1230       C  
ATOM   3792  CG2 VAL B 274      43.762 -11.017  -4.244  1.00 26.30           C  
ANISOU 3792  CG2 VAL B 274     3229   3794   2968     90     86  -1090       C  
ATOM   3793  N   LEU B 275      48.304 -10.916  -4.689  1.00 31.41           N  
ANISOU 3793  N   LEU B 275     3839   4295   3802    118    282  -1224       N  
ATOM   3794  CA  LEU B 275      49.469 -10.708  -5.545  1.00 30.45           C  
ANISOU 3794  CA  LEU B 275     3704   4190   3674     91    370  -1299       C  
ATOM   3795  C   LEU B 275      50.461 -11.867  -5.453  1.00 32.23           C  
ANISOU 3795  C   LEU B 275     3849   4305   4091    109    444  -1388       C  
ATOM   3796  O   LEU B 275      51.039 -12.282  -6.465  1.00 36.86           O  
ANISOU 3796  O   LEU B 275     4419   4899   4688     69    549  -1513       O  
ATOM   3797  CB  LEU B 275      50.114  -9.383  -5.191  1.00 27.66           C  
ANISOU 3797  CB  LEU B 275     3373   3866   3272    111    350  -1203       C  
ATOM   3798  CG  LEU B 275      49.235  -8.193  -5.575  1.00 24.22           C  
ANISOU 3798  CG  LEU B 275     3019   3531   2654     92    304  -1129       C  
ATOM   3799  CD1 LEU B 275      49.647  -6.926  -4.777  1.00 22.71           C  
ANISOU 3799  CD1 LEU B 275     2858   3326   2446    125    266  -1014       C  
ATOM   3800  CD2 LEU B 275      49.208  -7.950  -7.099  1.00 24.31           C  
ANISOU 3800  CD2 LEU B 275     3071   3645   2521     19    363  -1199       C  
ATOM   3801  N   ARG B 276      50.667 -12.398  -4.252  1.00 29.53           N  
ANISOU 3801  N   ARG B 276     3456   3859   3904    169    394  -1321       N  
ATOM   3802  CA  ARG B 276      51.451 -13.618  -4.093  1.00 32.75           C  
ANISOU 3802  CA  ARG B 276     3779   4142   4522    200    451  -1385       C  
ATOM   3803  C   ARG B 276      50.843 -14.764  -4.883  1.00 38.21           C  
ANISOU 3803  C   ARG B 276     4478   4799   5240    158    517  -1522       C  
ATOM   3804  O   ARG B 276      51.553 -15.506  -5.570  1.00 36.23           O  
ANISOU 3804  O   ARG B 276     4183   4490   5093    149    628  -1649       O  
ATOM   3805  CB  ARG B 276      51.540 -14.002  -2.622  1.00 30.47           C  
ANISOU 3805  CB  ARG B 276     3451   3757   4371    263    361  -1261       C  
ATOM   3806  CG  ARG B 276      52.348 -13.071  -1.801  1.00 29.30           C  
ANISOU 3806  CG  ARG B 276     3283   3624   4224    294    300  -1147       C  
ATOM   3807  CD  ARG B 276      53.791 -12.982  -2.315  1.00 28.39           C  
ANISOU 3807  CD  ARG B 276     3083   3495   4209    301    378  -1201       C  
ATOM   3808  NE  ARG B 276      54.442 -14.280  -2.386  1.00 41.60           N  
ANISOU 3808  NE  ARG B 276     4655   5046   6104    342    440  -1265       N  
ATOM   3809  CZ  ARG B 276      54.922 -14.929  -1.340  1.00 45.12           C  
ANISOU 3809  CZ  ARG B 276     5024   5387   6731    402    375  -1174       C  
ATOM   3810  NH1 ARG B 276      54.818 -14.392  -0.133  1.00 39.70           N  
ANISOU 3810  NH1 ARG B 276     4362   4719   6005    415    245  -1024       N  
ATOM   3811  NH2 ARG B 276      55.501 -16.122  -1.505  1.00 47.16           N  
ANISOU 3811  NH2 ARG B 276     5187   5520   7213    447    443  -1233       N  
ATOM   3812  N   GLU B 277      49.520 -14.922  -4.791  1.00 33.93           N  
ANISOU 3812  N   GLU B 277     3989   4291   4610    126    455  -1503       N  
ATOM   3813  CA  GLU B 277      48.864 -16.000  -5.504  1.00 35.86           C  
ANISOU 3813  CA  GLU B 277     4246   4507   4874     68    505  -1634       C  
ATOM   3814  C   GLU B 277      48.917 -15.805  -7.013  1.00 37.69           C  
ANISOU 3814  C   GLU B 277     4521   4841   4959    -17    591  -1778       C  
ATOM   3815  O   GLU B 277      48.833 -16.788  -7.756  1.00 36.35           O  
ANISOU 3815  O   GLU B 277     4355   4628   4829    -72    672  -1932       O  
ATOM   3816  CB  GLU B 277      47.425 -16.150  -5.003  1.00 32.54           C  
ANISOU 3816  CB  GLU B 277     3857   4111   4396     47    412  -1568       C  
ATOM   3817  CG  GLU B 277      47.353 -16.776  -3.608  1.00 32.48           C  
ANISOU 3817  CG  GLU B 277     3812   3976   4552    109    358  -1460       C  
ATOM   3818  CD  GLU B 277      47.996 -18.186  -3.549  1.00 40.90           C  
ANISOU 3818  CD  GLU B 277     4823   4871   5846    127    431  -1541       C  
ATOM   3819  OE1 GLU B 277      47.683 -19.015  -4.431  1.00 41.74           O  
ANISOU 3819  OE1 GLU B 277     4940   4948   5973     63    502  -1690       O  
ATOM   3820  OE2 GLU B 277      48.800 -18.463  -2.623  1.00 36.46           O  
ANISOU 3820  OE2 GLU B 277     4208   4202   5444    201    413  -1454       O  
ATOM   3821  N   LEU B 278      49.066 -14.578  -7.489  1.00 30.88           N  
ANISOU 3821  N   LEU B 278     4040   3731   3961     84   1356   -974       N  
ATOM   3822  CA  LEU B 278      49.358 -14.397  -8.903  1.00 33.89           C  
ANISOU 3822  CA  LEU B 278     4398   4150   4329    -50   1465  -1050       C  
ATOM   3823  C   LEU B 278      50.826 -14.631  -9.225  1.00 42.44           C  
ANISOU 3823  C   LEU B 278     5362   5223   5542    -50   1520  -1183       C  
ATOM   3824  O   LEU B 278      51.203 -14.530 -10.395  1.00 48.84           O  
ANISOU 3824  O   LEU B 278     6154   6056   6348   -170   1632  -1264       O  
ATOM   3825  CB  LEU B 278      48.962 -12.986  -9.352  1.00 30.03           C  
ANISOU 3825  CB  LEU B 278     3954   3722   3734   -151   1458  -1007       C  
ATOM   3826  CG  LEU B 278      47.477 -12.617  -9.294  1.00 33.71           C  
ANISOU 3826  CG  LEU B 278     4525   4197   4087   -178   1412   -896       C  
ATOM   3827  CD1 LEU B 278      47.212 -11.103  -9.429  1.00 27.21           C  
ANISOU 3827  CD1 LEU B 278     3732   3421   3185   -246   1368   -849       C  
ATOM   3828  CD2 LEU B 278      46.749 -13.382 -10.393  1.00 37.81           C  
ANISOU 3828  CD2 LEU B 278     5103   4703   4559   -263   1484   -908       C  
ATOM   3829  N   GLY B 279      51.667 -14.912  -8.224  1.00 35.27           N  
ANISOU 3829  N   GLY B 279     4376   4272   4753     76   1443  -1214       N  
ATOM   3830  CA  GLY B 279      53.064 -15.228  -8.470  1.00 37.46           C  
ANISOU 3830  CA  GLY B 279     4518   4522   5192     89   1485  -1356       C  
ATOM   3831  C   GLY B 279      54.081 -14.127  -8.239  1.00 42.92           C  
ANISOU 3831  C   GLY B 279     5119   5240   5948     85   1458  -1415       C  
ATOM   3832  O   GLY B 279      55.287 -14.381  -8.400  1.00 41.24           O  
ANISOU 3832  O   GLY B 279     4775   4996   5897    100   1492  -1549       O  
ATOM   3833  N   LEU B 280      53.651 -12.916  -7.888  1.00 39.39           N  
ANISOU 3833  N   LEU B 280     4726   4845   5395     64   1402  -1330       N  
ATOM   3834  CA  LEU B 280      54.605 -11.846  -7.623  1.00 39.89           C  
ANISOU 3834  CA  LEU B 280     4703   4932   5521     63   1374  -1385       C  
ATOM   3835  C   LEU B 280      55.385 -12.139  -6.349  1.00 40.75           C  
ANISOU 3835  C   LEU B 280     4733   4983   5766    224   1236  -1407       C  
ATOM   3836  O   LEU B 280      54.838 -12.666  -5.375  1.00 45.44           O  
ANISOU 3836  O   LEU B 280     5398   5538   6331    334   1127  -1317       O  
ATOM   3837  CB  LEU B 280      53.890 -10.504  -7.480  1.00 39.25           C  
ANISOU 3837  CB  LEU B 280     4706   4914   5295     10   1336  -1280       C  
ATOM   3838  CG  LEU B 280      53.463  -9.760  -8.744  1.00 43.05           C  
ANISOU 3838  CG  LEU B 280     5250   5449   5657   -161   1447  -1277       C  
ATOM   3839  CD1 LEU B 280      52.308 -10.463  -9.436  1.00 37.02           C  
ANISOU 3839  CD1 LEU B 280     4598   4682   4787   -218   1494  -1218       C  
ATOM   3840  CD2 LEU B 280      53.082  -8.324  -8.390  1.00 40.47           C  
ANISOU 3840  CD2 LEU B 280     4971   5171   5236   -186   1380  -1195       C  
ATOM   3841  N   ASN B 281      56.665 -11.798  -6.349  1.00 37.45           N  
ANISOU 3841  N   ASN B 281     4177   4553   5501    234   1239  -1532       N  
ATOM   3842  CA  ASN B 281      57.438 -12.056  -5.146  1.00 38.30           C  
ANISOU 3842  CA  ASN B 281     4212   4595   5747    390   1084  -1560       C  
ATOM   3843  C   ASN B 281      57.380 -10.859  -4.200  1.00 38.18           C  
ANISOU 3843  C   ASN B 281     4226   4612   5668    433    965  -1483       C  
ATOM   3844  O   ASN B 281      56.850  -9.789  -4.522  1.00 34.14           O  
ANISOU 3844  O   ASN B 281     3771   4174   5028    340   1011  -1423       O  
ATOM   3845  CB  ASN B 281      58.886 -12.459  -5.485  1.00 35.63           C  
ANISOU 3845  CB  ASN B 281     3688   4204   5647    405   1121  -1748       C  
ATOM   3846  CG  ASN B 281      59.707 -11.338  -6.114  1.00 56.96           C  
ANISOU 3846  CG  ASN B 281     6284   6953   8407    298   1219  -1857       C  
ATOM   3847  OD1 ASN B 281      59.419 -10.141  -5.959  1.00 54.39           O  
ANISOU 3847  OD1 ASN B 281     6008   6689   7968    253   1203  -1788       O  
ATOM   3848  ND2 ASN B 281      60.764 -11.731  -6.813  1.00 53.11           N  
ANISOU 3848  ND2 ASN B 281     5646   6427   8108    255   1326  -2036       N  
ATOM   3849  N   GLU B 282      57.944 -11.058  -3.010  1.00 40.04           N  
ANISOU 3849  N   GLU B 282     4431   4784   5999    578    800  -1487       N  
ATOM   3850  CA  GLU B 282      57.807 -10.075  -1.941  1.00 38.99           C  
ANISOU 3850  CA  GLU B 282     4350   4669   5796    636    668  -1404       C  
ATOM   3851  C   GLU B 282      58.386  -8.721  -2.331  1.00 43.97           C  
ANISOU 3851  C   GLU B 282     4892   5365   6448    552    719  -1464       C  
ATOM   3852  O   GLU B 282      57.823  -7.674  -1.980  1.00 40.27           O  
ANISOU 3852  O   GLU B 282     4497   4952   5852    524    690  -1371       O  
ATOM   3853  CB  GLU B 282      58.470 -10.607  -0.670  1.00 43.65           C  
ANISOU 3853  CB  GLU B 282     4925   5164   6497    802    475  -1417       C  
ATOM   3854  CG  GLU B 282      57.657 -11.722  -0.007  1.00 54.27           C  
ANISOU 3854  CG  GLU B 282     6418   6443   7761    885    403  -1313       C  
ATOM   3855  CD  GLU B 282      58.502 -12.750   0.730  1.00 68.91           C  
ANISOU 3855  CD  GLU B 282     8234   8175   9773   1029    251  -1373       C  
ATOM   3856  OE1 GLU B 282      59.362 -13.402   0.090  1.00 78.25           O  
ANISOU 3856  OE1 GLU B 282     9273   9317  11141   1033    292  -1509       O  
ATOM   3857  OE2 GLU B 282      58.290 -12.920   1.951  1.00 71.47           O  
ANISOU 3857  OE2 GLU B 282     8682   8436  10037   1134     90  -1287       O  
ATOM   3858  N   GLN B 283      59.506  -8.707  -3.054  1.00 39.03           N  
ANISOU 3858  N   GLN B 283     4109   4730   5991    505    802  -1623       N  
ATOM   3859  CA  GLN B 283      60.111  -7.417  -3.386  1.00 43.61           C  
ANISOU 3859  CA  GLN B 283     4607   5363   6599    422    856  -1688       C  
ATOM   3860  C   GLN B 283      59.256  -6.638  -4.376  1.00 40.08           C  
ANISOU 3860  C   GLN B 283     4256   5001   5970    260   1001  -1621       C  
ATOM   3861  O   GLN B 283      59.105  -5.422  -4.249  1.00 41.14           O  
ANISOU 3861  O   GLN B 283     4417   5189   6025    214    990  -1576       O  
ATOM   3862  CB  GLN B 283      61.520  -7.601  -3.939  1.00 42.37           C  
ANISOU 3862  CB  GLN B 283     4255   5166   6679    400    930  -1891       C  
ATOM   3863  CG  GLN B 283      62.239  -6.285  -4.223  1.00 53.46           C  
ANISOU 3863  CG  GLN B 283     5568   6614   8131    316    991  -1973       C  
ATOM   3864  CD  GLN B 283      62.365  -5.400  -2.982  1.00 60.83           C  
ANISOU 3864  CD  GLN B 283     6507   7553   9054    416    810  -1911       C  
ATOM   3865  OE1 GLN B 283      62.936  -5.804  -1.965  1.00 67.18           O  
ANISOU 3865  OE1 GLN B 283     7252   8288   9987    564    639  -1940       O  
ATOM   3866  NE2 GLN B 283      61.819  -4.188  -3.062  1.00 56.91           N  
ANISOU 3866  NE2 GLN B 283     6089   7132   8402    336    841  -1824       N  
ATOM   3867  N   THR B 284      58.702  -7.317  -5.377  1.00 37.78           N  
ANISOU 3867  N   THR B 284     4022   4718   5614    172   1129  -1618       N  
ATOM   3868  CA  THR B 284      57.833  -6.641  -6.331  1.00 34.90           C  
ANISOU 3868  CA  THR B 284     3769   4421   5072     21   1242  -1549       C  
ATOM   3869  C   THR B 284      56.602  -6.062  -5.643  1.00 41.29           C  
ANISOU 3869  C   THR B 284     4715   5264   5708     53   1139  -1376       C  
ATOM   3870  O   THR B 284      56.174  -4.943  -5.952  1.00 38.99           O  
ANISOU 3870  O   THR B 284     4481   5025   5307    -36   1162  -1322       O  
ATOM   3871  CB  THR B 284      57.407  -7.616  -7.414  1.00 40.18           C  
ANISOU 3871  CB  THR B 284     4485   5079   5702    -62   1372  -1572       C  
ATOM   3872  OG1 THR B 284      58.567  -8.153  -8.071  1.00 44.74           O  
ANISOU 3872  OG1 THR B 284     4929   5619   6452   -101   1485  -1747       O  
ATOM   3873  CG2 THR B 284      56.538  -6.909  -8.401  1.00 41.77           C  
ANISOU 3873  CG2 THR B 284     4812   5336   5721   -216   1464  -1504       C  
ATOM   3874  N  AILE B 285      56.009  -6.809  -4.713  0.75 30.91           N  
ANISOU 3874  N  AILE B 285     3459   3913   4371    173   1030  -1292       N  
ATOM   3875  N  BILE B 285      56.010  -6.823  -4.717  0.25 34.83           N  
ANISOU 3875  N  BILE B 285     3956   4410   4868    173   1030  -1292       N  
ATOM   3876  CA AILE B 285      54.882  -6.266  -3.968  0.75 31.14           C  
ANISOU 3876  CA AILE B 285     3609   3966   4257    203    943  -1145       C  
ATOM   3877  CA BILE B 285      54.907  -6.305  -3.910  0.25 32.66           C  
ANISOU 3877  CA BILE B 285     3800   4155   4455    211    937  -1145       C  
ATOM   3878  C  AILE B 285      55.333  -5.082  -3.107  0.75 37.54           C  
ANISOU 3878  C  AILE B 285     4385   4797   5082    245    847  -1134       C  
ATOM   3879  C  BILE B 285      55.359  -5.077  -3.142  0.25 36.30           C  
ANISOU 3879  C  BILE B 285     4225   4641   4928    242    851  -1137       C  
ATOM   3880  O  AILE B 285      54.628  -4.069  -2.996  0.75 34.03           O  
ANISOU 3880  O  AILE B 285     4008   4396   4526    199    832  -1050       O  
ATOM   3881  O  BILE B 285      54.679  -4.044  -3.114  0.25 34.66           O  
ANISOU 3881  O  BILE B 285     4082   4480   4609    188    843  -1058       O  
ATOM   3882  CB AILE B 285      54.222  -7.376  -3.134  0.75 31.36           C  
ANISOU 3882  CB AILE B 285     3715   3937   4262    314    865  -1071       C  
ATOM   3883  CB BILE B 285      54.388  -7.386  -2.945  0.25 31.64           C  
ANISOU 3883  CB BILE B 285     3739   3966   4317    336    844  -1078       C  
ATOM   3884  CG1AILE B 285      53.789  -8.518  -4.052  0.75 31.89           C  
ANISOU 3884  CG1AILE B 285     3809   3987   4321    266    967  -1089       C  
ATOM   3885  CG1BILE B 285      54.020  -8.637  -3.716  0.25 31.66           C  
ANISOU 3885  CG1BILE B 285     3765   3941   4324    307    932  -1097       C  
ATOM   3886  CG2AILE B 285      53.029  -6.830  -2.341  0.75 31.44           C  
ANISOU 3886  CG2AILE B 285     3850   3963   4134    336    796   -933       C  
ATOM   3887  CG2BILE B 285      53.181  -6.868  -2.162  0.25 30.95           C  
ANISOU 3887  CG2BILE B 285     3779   3893   4088    357    778   -939       C  
ATOM   3888  CD1AILE B 285      53.294  -9.751  -3.305  0.75 29.67           C  
ANISOU 3888  CD1AILE B 285     3595   3639   4040    373    905  -1036       C  
ATOM   3889  CD1BILE B 285      53.214  -8.315  -4.898  0.25 29.24           C  
ANISOU 3889  CD1BILE B 285     3516   3686   3908    166   1049  -1069       C  
ATOM   3890  N   LYS B 286      56.518  -5.185  -2.495  1.00 42.37           N  
ANISOU 3890  N   LYS B 286     4886   5371   5842    333    775  -1224       N  
ATOM   3891  CA  LYS B 286      57.001  -4.108  -1.646  1.00 44.85           C  
ANISOU 3891  CA  LYS B 286     5162   5699   6179    379    676  -1222       C  
ATOM   3892  C   LYS B 286      57.151  -2.815  -2.434  1.00 40.72           C  
ANISOU 3892  C   LYS B 286     4608   5243   5622    248    768  -1248       C  
ATOM   3893  O   LYS B 286      56.779  -1.742  -1.945  1.00 40.53           O  
ANISOU 3893  O   LYS B 286     4627   5255   5519    242    714  -1177       O  
ATOM   3894  CB  LYS B 286      58.318  -4.518  -0.989  1.00 45.13           C  
ANISOU 3894  CB  LYS B 286     5072   5672   6404    492    578  -1334       C  
ATOM   3895  CG  LYS B 286      58.755  -3.574   0.125  1.00 52.79           C  
ANISOU 3895  CG  LYS B 286     6021   6641   7394    567    437  -1322       C  
ATOM   3896  CD  LYS B 286      60.033  -4.074   0.785  1.00 57.56           C  
ANISOU 3896  CD  LYS B 286     6504   7167   8199    688    314  -1437       C  
ATOM   3897  CE  LYS B 286      59.871  -5.504   1.266  1.00 60.52           C  
ANISOU 3897  CE  LYS B 286     6936   7458   8599    795    232  -1413       C  
ATOM   3898  NZ  LYS B 286      60.776  -5.831   2.414  1.00 62.53           N  
ANISOU 3898  NZ  LYS B 286     7148   7623   8989    947     29  -1463       N  
ATOM   3899  N   ASN B 287      57.627  -2.912  -3.679  1.00 42.62           N  
ANISOU 3899  N   ASN B 287     4789   5495   5909    135    915  -1345       N  
ATOM   3900  CA  ASN B 287      57.764  -1.732  -4.533  1.00 48.41           C  
ANISOU 3900  CA  ASN B 287     5518   6280   6595     -7   1017  -1371       C  
ATOM   3901  C   ASN B 287      56.424  -1.032  -4.757  1.00 43.19           C  
ANISOU 3901  C   ASN B 287     5006   5665   5740    -78   1015  -1228       C  
ATOM   3902  O   ASN B 287      56.329   0.191  -4.623  1.00 44.81           O  
ANISOU 3902  O   ASN B 287     5228   5904   5893   -119    991  -1191       O  
ATOM   3903  CB  ASN B 287      58.399  -2.123  -5.868  1.00 55.65           C  
ANISOU 3903  CB  ASN B 287     6381   7189   7574   -130   1191  -1498       C  
ATOM   3904  CG  ASN B 287      59.829  -2.635  -5.712  1.00 62.72           C  
ANISOU 3904  CG  ASN B 287     7099   8034   8696    -73   1205  -1668       C  
ATOM   3905  OD1 ASN B 287      60.517  -2.316  -4.738  1.00 66.94           O  
ANISOU 3905  OD1 ASN B 287     7542   8549   9344     32   1088  -1703       O  
ATOM   3906  ND2 ASN B 287      60.278  -3.444  -6.675  1.00 60.20           N  
ANISOU 3906  ND2 ASN B 287     6731   7687   8454   -144   1344  -1780       N  
ATOM   3907  N   GLY B 288      55.380  -1.788  -5.113  1.00 35.41           N  
ANISOU 3907  N   GLY B 288     4122   4672   4659    -94   1035  -1152       N  
ATOM   3908  CA  GLY B 288      54.060  -1.187  -5.294  1.00 32.35           C  
ANISOU 3908  CA  GLY B 288     3864   4314   4115   -152   1017  -1026       C  
ATOM   3909  C   GLY B 288      53.456  -0.669  -3.997  1.00 34.79           C  
ANISOU 3909  C   GLY B 288     4208   4625   4385    -53    885   -927       C  
ATOM   3910  O   GLY B 288      52.950   0.461  -3.930  1.00 29.19           O  
ANISOU 3910  O   GLY B 288     3542   3946   3603    -98    856   -865       O  
ATOM   3911  N   PHE B 289      53.500  -1.484  -2.947  1.00 29.33           N  
ANISOU 3911  N   PHE B 289     3509   3896   3740     79    804   -913       N  
ATOM   3912  CA  PHE B 289      52.921  -1.081  -1.670  1.00 28.72           C  
ANISOU 3912  CA  PHE B 289     3486   3811   3616    166    690   -824       C  
ATOM   3913  C   PHE B 289      53.582   0.185  -1.137  1.00 30.92           C  
ANISOU 3913  C   PHE B 289     3707   4117   3923    175    633   -844       C  
ATOM   3914  O   PHE B 289      52.920   1.008  -0.503  1.00 29.56           O  
ANISOU 3914  O   PHE B 289     3590   3961   3682    183    577   -767       O  
ATOM   3915  CB  PHE B 289      53.045  -2.206  -0.632  1.00 27.10           C  
ANISOU 3915  CB  PHE B 289     3298   3546   3453    300    611   -817       C  
ATOM   3916  CG  PHE B 289      51.965  -3.264  -0.735  1.00 33.14           C  
ANISOU 3916  CG  PHE B 289     4159   4280   4154    307    642   -753       C  
ATOM   3917  CD1 PHE B 289      51.318  -3.501  -1.936  1.00 32.33           C  
ANISOU 3917  CD1 PHE B 289     4082   4197   4004    204    744   -747       C  
ATOM   3918  CD2 PHE B 289      51.602  -4.014   0.378  1.00 26.76           C  
ANISOU 3918  CD2 PHE B 289     3425   3415   3328    412    568   -703       C  
ATOM   3919  CE1 PHE B 289      50.328  -4.463  -2.044  1.00 26.10           C  
ANISOU 3919  CE1 PHE B 289     3372   3377   3166    209    772   -696       C  
ATOM   3920  CE2 PHE B 289      50.610  -4.996   0.287  1.00 27.75           C  
ANISOU 3920  CE2 PHE B 289     3637   3506   3399    413    608   -650       C  
ATOM   3921  CZ  PHE B 289      49.979  -5.228  -0.926  1.00 31.86           C  
ANISOU 3921  CZ  PHE B 289     4163   4051   3890    315    710   -650       C  
ATOM   3922  N   GLU B 290      54.872   0.374  -1.403  1.00 27.81           N  
ANISOU 3922  N   GLU B 290     3198   3727   3642    167    655   -956       N  
ATOM   3923  CA  GLU B 290      55.552   1.531  -0.848  1.00 30.60           C  
ANISOU 3923  CA  GLU B 290     3488   4101   4037    182    598   -984       C  
ATOM   3924  C   GLU B 290      55.157   2.834  -1.521  1.00 32.11           C  
ANISOU 3924  C   GLU B 290     3708   4344   4149     59    654   -951       C  
ATOM   3925  O   GLU B 290      55.476   3.904  -0.993  1.00 33.59           O  
ANISOU 3925  O   GLU B 290     3864   4552   4348     68    602   -951       O  
ATOM   3926  CB  GLU B 290      57.055   1.333  -0.931  1.00 35.14           C  
ANISOU 3926  CB  GLU B 290     3919   4655   4779    210    605  -1127       C  
ATOM   3927  CG  GLU B 290      57.637   0.692   0.328  1.00 50.65           C  
ANISOU 3927  CG  GLU B 290     5847   6563   6836    368    462  -1151       C  
ATOM   3928  CD  GLU B 290      59.070   0.187   0.150  1.00 62.63           C  
ANISOU 3928  CD  GLU B 290     7208   8038   8552    406    464  -1308       C  
ATOM   3929  OE1 GLU B 290      59.655   0.337  -0.952  1.00 64.42           O  
ANISOU 3929  OE1 GLU B 290     7347   8282   8849    302    599  -1409       O  
ATOM   3930  OE2 GLU B 290      59.609  -0.370   1.127  1.00 65.30           O  
ANISOU 3930  OE2 GLU B 290     7514   8316   8980    537    327  -1335       O  
ATOM   3931  N   THR B 291      54.462   2.781  -2.651  1.00 27.02           N  
ANISOU 3931  N   THR B 291     3130   3713   3422    -53    748   -921       N  
ATOM   3932  CA  THR B 291      54.114   3.992  -3.383  1.00 37.57           C  
ANISOU 3932  CA  THR B 291     4510   5084   4682   -176    790   -890       C  
ATOM   3933  C   THR B 291      52.621   4.185  -3.544  1.00 40.19           C  
ANISOU 3933  C   THR B 291     4963   5418   4890   -212    764   -770       C  
ATOM   3934  O   THR B 291      52.219   5.191  -4.123  1.00 39.97           O  
ANISOU 3934  O   THR B 291     4983   5406   4796   -308    775   -735       O  
ATOM   3935  CB  THR B 291      54.726   3.993  -4.785  1.00 36.04           C  
ANISOU 3935  CB  THR B 291     4302   4895   4497   -311    927   -976       C  
ATOM   3936  OG1 THR B 291      54.210   2.865  -5.495  1.00 33.36           O  
ANISOU 3936  OG1 THR B 291     4019   4536   4121   -339    985   -968       O  
ATOM   3937  CG2 THR B 291      56.231   3.905  -4.722  1.00 38.94           C  
ANISOU 3937  CG2 THR B 291     4531   5254   5012   -293    971  -1116       C  
ATOM   3938  N   TYR B 292      51.788   3.248  -3.096  1.00 25.36           N  
ANISOU 3938  N   TYR B 292     3135   3515   2987   -143    729   -714       N  
ATOM   3939  CA  TYR B 292      50.361   3.488  -3.188  1.00 29.79           C  
ANISOU 3939  CA  TYR B 292     3792   4069   3458   -174    701   -615       C  
ATOM   3940  C   TYR B 292      49.944   4.555  -2.168  1.00 34.69           C  
ANISOU 3940  C   TYR B 292     4419   4698   4064   -132    615   -557       C  
ATOM   3941  O   TYR B 292      50.470   4.603  -1.052  1.00 28.47           O  
ANISOU 3941  O   TYR B 292     3589   3908   3320    -37    560   -571       O  
ATOM   3942  CB  TYR B 292      49.583   2.193  -2.969  1.00 24.38           C  
ANISOU 3942  CB  TYR B 292     3154   3349   2759   -117    703   -581       C  
ATOM   3943  CG  TYR B 292      48.103   2.444  -2.964  1.00 26.97           C  
ANISOU 3943  CG  TYR B 292     3563   3661   3022   -143    672   -493       C  
ATOM   3944  CD1 TYR B 292      47.433   2.764  -4.144  1.00 26.89           C  
ANISOU 3944  CD1 TYR B 292     3607   3651   2959   -255    697   -471       C  
ATOM   3945  CD2 TYR B 292      47.382   2.426  -1.784  1.00 23.26           C  
ANISOU 3945  CD2 TYR B 292     3119   3168   2549    -62    616   -440       C  
ATOM   3946  CE1 TYR B 292      46.065   3.029  -4.141  1.00 30.00           C  
ANISOU 3946  CE1 TYR B 292     4061   4019   3320   -274    653   -402       C  
ATOM   3947  CE2 TYR B 292      46.010   2.702  -1.773  1.00 33.27           C  
ANISOU 3947  CE2 TYR B 292     4444   4413   3783    -90    596   -377       C  
ATOM   3948  CZ  TYR B 292      45.362   3.001  -2.956  1.00 33.53           C  
ANISOU 3948  CZ  TYR B 292     4511   4444   3786   -191    608   -361       C  
ATOM   3949  OH  TYR B 292      44.003   3.275  -2.957  1.00 37.07           O  
ANISOU 3949  OH  TYR B 292     5000   4858   4227   -214    574   -309       O  
ATOM   3950  N   THR B 293      49.016   5.436  -2.566  1.00 28.68           N  
ANISOU 3950  N   THR B 293     3713   3940   3245   -204    597   -497       N  
ATOM   3951  CA  THR B 293      48.497   6.478  -1.677  1.00 28.62           C  
ANISOU 3951  CA  THR B 293     3710   3934   3230   -175    523   -446       C  
ATOM   3952  C   THR B 293      47.011   6.658  -1.928  1.00 22.63           C  
ANISOU 3952  C   THR B 293     3021   3147   2431   -215    498   -374       C  
ATOM   3953  O   THR B 293      46.506   6.334  -3.000  1.00 35.20           O  
ANISOU 3953  O   THR B 293     4660   4724   3991   -289    526   -364       O  
ATOM   3954  CB  THR B 293      49.160   7.851  -1.902  1.00 41.32           C  
ANISOU 3954  CB  THR B 293     5281   5572   4845   -234    512   -467       C  
ATOM   3955  OG1 THR B 293      48.768   8.357  -3.184  1.00 40.14           O  
ANISOU 3955  OG1 THR B 293     5188   5420   4645   -358    539   -449       O  
ATOM   3956  CG2 THR B 293      50.666   7.766  -1.851  1.00 45.21           C  
ANISOU 3956  CG2 THR B 293     5690   6088   5399   -214    546   -556       C  
ATOM   3957  N   SER B 294      46.317   7.232  -0.952  1.00 24.09           N  
ANISOU 3957  N   SER B 294     3212   3319   2624   -170    444   -333       N  
ATOM   3958  CA  SER B 294      44.908   7.574  -1.149  1.00 25.69           C  
ANISOU 3958  CA  SER B 294     3458   3484   2818   -209    414   -280       C  
ATOM   3959  C   SER B 294      44.774   8.752  -2.111  1.00 28.40           C  
ANISOU 3959  C   SER B 294     3815   3831   3144   -310    380   -264       C  
ATOM   3960  O   SER B 294      45.751   9.380  -2.504  1.00 29.94           O  
ANISOU 3960  O   SER B 294     3990   4059   3327   -352    391   -292       O  
ATOM   3961  CB  SER B 294      44.226   7.893   0.177  1.00 32.69           C  
ANISOU 3961  CB  SER B 294     4343   4347   3729   -143    381   -254       C  
ATOM   3962  OG  SER B 294      44.725   9.081   0.773  1.00 42.23           O  
ANISOU 3962  OG  SER B 294     5515   5580   4949   -134    340   -258       O  
ATOM   3963  N   ASP B 295      43.537   9.035  -2.517  1.00 33.09           N  
ANISOU 3963  N   ASP B 295     4448   4382   3744   -354    336   -224       N  
ATOM   3964  CA  ASP B 295      43.298  10.129  -3.454  1.00 37.15           C  
ANISOU 3964  CA  ASP B 295     4996   4880   4239   -450    280   -202       C  
ATOM   3965  C   ASP B 295      42.205  11.094  -3.002  1.00 40.60           C  
ANISOU 3965  C   ASP B 295     5423   5274   4729   -447    197   -167       C  
ATOM   3966  O   ASP B 295      41.751  11.919  -3.806  1.00 49.12           O  
ANISOU 3966  O   ASP B 295     6542   6319   5804   -523    127   -141       O  
ATOM   3967  CB  ASP B 295      42.978   9.574  -4.854  1.00 42.03           C  
ANISOU 3967  CB  ASP B 295     5690   5472   4808   -535    287   -197       C  
ATOM   3968  CG  ASP B 295      41.679   8.784  -4.901  0.74 50.57           C  
ANISOU 3968  CG  ASP B 295     6791   6501   5921   -515    262   -177       C  
ATOM   3969  OD1 ASP B 295      40.958   8.702  -3.876  0.77 53.46           O  
ANISOU 3969  OD1 ASP B 295     7114   6845   6352   -444    250   -169       O  
ATOM   3970  OD2 ASP B 295      41.376   8.235  -5.985  0.74 55.01           O  
ANISOU 3970  OD2 ASP B 295     7417   7038   6445   -577    261   -175       O  
ATOM   3971  N   ASN B 296      41.781  11.031  -1.743  1.00 39.10           N  
ANISOU 3971  N   ASN B 296     5188   5075   4592   -367    202   -168       N  
ATOM   3972  CA  ASN B 296      40.700  11.873  -1.252  1.00 38.57           C  
ANISOU 3972  CA  ASN B 296     5099   4960   4596   -365    141   -151       C  
ATOM   3973  C   ASN B 296      41.196  12.958  -0.289  1.00 39.94           C  
ANISOU 3973  C   ASN B 296     5228   5160   4789   -335    125   -156       C  
ATOM   3974  O   ASN B 296      40.405  13.488   0.487  1.00 39.37           O  
ANISOU 3974  O   ASN B 296     5126   5052   4782   -312    102   -156       O  
ATOM   3975  CB  ASN B 296      39.638  11.006  -0.566  1.00 36.21           C  
ANISOU 3975  CB  ASN B 296     4793   4614   4352   -314    174   -158       C  
ATOM   3976  CG  ASN B 296      40.223  10.160   0.556  1.00 49.46           C  
ANISOU 3976  CG  ASN B 296     6469   6323   6002   -231    253   -177       C  
ATOM   3977  OD1 ASN B 296      41.376  10.360   0.967  1.00 50.04           O  
ANISOU 3977  OD1 ASN B 296     6530   6449   6033   -201    265   -187       O  
ATOM   3978  ND2 ASN B 296      39.442   9.201   1.050  1.00 55.24           N  
ANISOU 3978  ND2 ASN B 296     7216   7013   6759   -196    303   -185       N  
ATOM   3979  N   GLY B 297      42.493  13.262  -0.276  1.00 35.93           N  
ANISOU 3979  N   GLY B 297     4707   4711   4233   -334    145   -171       N  
ATOM   3980  CA  GLY B 297      42.965  14.219   0.712  1.00 33.75           C  
ANISOU 3980  CA  GLY B 297     4386   4459   3978   -299    129   -181       C  
ATOM   3981  C   GLY B 297      42.813  13.806   2.165  1.00 34.65           C  
ANISOU 3981  C   GLY B 297     4485   4571   4110   -210    160   -195       C  
ATOM   3982  O   GLY B 297      42.811  14.668   3.046  1.00 29.95           O  
ANISOU 3982  O   GLY B 297     3862   3976   3540   -188    139   -201       O  
ATOM   3983  N   ARG B 298      42.686  12.520   2.469  1.00 31.60           N  
ANISOU 3983  N   ARG B 298     4126   4175   3704   -163    210   -202       N  
ATOM   3984  CA  ARG B 298      42.754  12.075   3.862  1.00 32.49           C  
ANISOU 3984  CA  ARG B 298     4255   4281   3808    -83    240   -215       C  
ATOM   3985  C   ARG B 298      44.018  11.242   4.023  1.00 32.03           C  
ANISOU 3985  C   ARG B 298     4204   4262   3703    -30    258   -236       C  
ATOM   3986  O   ARG B 298      44.154  10.179   3.396  1.00 26.97           O  
ANISOU 3986  O   ARG B 298     3581   3621   3045    -29    290   -240       O  
ATOM   3987  CB  ARG B 298      41.519  11.272   4.272  1.00 36.70           C  
ANISOU 3987  CB  ARG B 298     4827   4753   4363    -69    285   -209       C  
ATOM   3988  N   MET B 299      44.954  11.743   4.826  1.00 29.07           N  
ANISOU 3988  N   MET B 299     3809   3917   3319     14    230   -257       N  
ATOM   3989  CA  MET B 299      46.273  11.131   4.952  1.00 32.72           C  
ANISOU 3989  CA  MET B 299     4256   4410   3765     66    223   -291       C  
ATOM   3990  C   MET B 299      46.872  10.798   3.583  1.00 29.02           C  
ANISOU 3990  C   MET B 299     3753   3970   3304     14    250   -312       C  
ATOM   3991  O   MET B 299      47.436   9.734   3.373  1.00 29.10           O  
ANISOU 3991  O   MET B 299     3765   3981   3312     46    274   -337       O  
ATOM   3992  CB  MET B 299      46.201   9.875   5.837  1.00 35.90           C  
ANISOU 3992  CB  MET B 299     4726   4776   4137    145    237   -290       C  
ATOM   3993  CG  MET B 299      45.745  10.146   7.283  1.00 27.50           C  
ANISOU 3993  CG  MET B 299     3724   3678   3047    190    222   -277       C  
ATOM   3994  SD  MET B 299      46.814  11.355   8.156  1.00 30.64           S  
ANISOU 3994  SD  MET B 299     4083   4110   3449    224    146   -305       S  
ATOM   3995  CE  MET B 299      48.407  10.551   8.024  1.00 27.86           C  
ANISOU 3995  CE  MET B 299     3696   3780   3111    291     99   -352       C  
ATOM   3996  N   GLN B 300      46.742  11.704   2.629  1.00 27.34           N  
ANISOU 3996  N   GLN B 300     3517   3771   3099    -72    247   -304       N  
ATOM   3997  CA  GLN B 300      47.270  11.454   1.298  1.00 26.34           C  
ANISOU 3997  CA  GLN B 300     3382   3663   2964   -140    285   -325       C  
ATOM   3998  C   GLN B 300      48.693  11.986   1.170  1.00 33.71           C  
ANISOU 3998  C   GLN B 300     4252   4637   3920   -150    291   -383       C  
ATOM   3999  O   GLN B 300      48.970  13.150   1.488  1.00 23.19           O  
ANISOU 3999  O   GLN B 300     2888   3321   2603   -164    258   -386       O  
ATOM   4000  CB  GLN B 300      46.368  12.081   0.251  1.00 24.63           C  
ANISOU 4000  CB  GLN B 300     3202   3426   2731   -239    274   -286       C  
ATOM   4001  CG  GLN B 300      46.883  11.977  -1.164  1.00 29.73           C  
ANISOU 4001  CG  GLN B 300     3867   4082   3346   -330    315   -306       C  
ATOM   4002  CD  GLN B 300      45.872  12.501  -2.155  1.00 28.70           C  
ANISOU 4002  CD  GLN B 300     3801   3914   3189   -423    279   -259       C  
ATOM   4003  OE1 GLN B 300      44.746  12.823  -1.780  1.00 36.03           O  
ANISOU 4003  OE1 GLN B 300     4741   4805   4143   -408    224   -218       O  
ATOM   4004  NE2 GLN B 300      46.279  12.636  -3.412  1.00 27.66           N  
ANISOU 4004  NE2 GLN B 300     3715   3782   3011   -522    307   -270       N  
ATOM   4005  N   TYR B 301      49.570  11.143   0.645  1.00 31.44           N  
ANISOU 4005  N   TYR B 301     3939   4361   3645   -149    340   -435       N  
ATOM   4006  CA  TYR B 301      51.005  11.357   0.586  1.00 26.51           C  
ANISOU 4006  CA  TYR B 301     3238   3765   3071   -146    359   -514       C  
ATOM   4007  C   TYR B 301      51.419  11.781  -0.819  1.00 27.82           C  
ANISOU 4007  C   TYR B 301     3405   3941   3224   -271    430   -545       C  
ATOM   4008  O   TYR B 301      50.807  11.381  -1.810  1.00 29.64           O  
ANISOU 4008  O   TYR B 301     3701   4156   3404   -342    470   -518       O  
ATOM   4009  CB  TYR B 301      51.732  10.065   0.983  1.00 25.70           C  
ANISOU 4009  CB  TYR B 301     3101   3653   3012    -59    367   -567       C  
ATOM   4010  CG  TYR B 301      53.249  10.095   0.860  1.00 27.64           C  
ANISOU 4010  CG  TYR B 301     3246   3914   3343    -51    388   -670       C  
ATOM   4011  CD1 TYR B 301      54.015  10.796   1.786  1.00 27.92           C  
ANISOU 4011  CD1 TYR B 301     3216   3959   3433      7    323   -708       C  
ATOM   4012  CD2 TYR B 301      53.916   9.402  -0.165  1.00 25.21           C  
ANISOU 4012  CD2 TYR B 301     2904   3604   3072   -103    476   -740       C  
ATOM   4013  CE1 TYR B 301      55.395  10.833   1.703  1.00 26.66           C  
ANISOU 4013  CE1 TYR B 301     2949   3805   3375     18    337   -815       C  
ATOM   4014  CE2 TYR B 301      55.291   9.425  -0.252  1.00 36.87           C  
ANISOU 4014  CE2 TYR B 301     4273   5084   4651    -97    503   -852       C  
ATOM   4015  CZ  TYR B 301      56.027  10.151   0.688  1.00 31.19           C  
ANISOU 4015  CZ  TYR B 301     3480   4373   3999    -34    430   -890       C  
ATOM   4016  OH  TYR B 301      57.388  10.195   0.622  1.00 36.11           O  
ANISOU 4016  OH  TYR B 301     3982   4993   4747    -25    451  -1012       O  
ATOM   4017  N   PHE B 302      52.470  12.600  -0.897  1.00 27.05           N  
ANISOU 4017  N   PHE B 302     3242   3865   3169   -302    448   -606       N  
ATOM   4018  CA  PHE B 302      52.998  13.080  -2.169  1.00 24.78           C  
ANISOU 4018  CA  PHE B 302     2967   3582   2867   -433    533   -648       C  
ATOM   4019  C   PHE B 302      54.505  13.052  -2.092  1.00 25.60           C  
ANISOU 4019  C   PHE B 302     2961   3701   3066   -422    586   -765       C  
ATOM   4020  O   PHE B 302      55.080  13.312  -1.032  1.00 27.75           O  
ANISOU 4020  O   PHE B 302     3151   3984   3409   -331    525   -797       O  
ATOM   4021  CB  PHE B 302      52.608  14.538  -2.500  1.00 24.63           C  
ANISOU 4021  CB  PHE B 302     2994   3560   2803   -520    508   -601       C  
ATOM   4022  CG  PHE B 302      51.139  14.783  -2.607  1.00 23.98           C  
ANISOU 4022  CG  PHE B 302     3005   3452   2654   -537    441   -497       C  
ATOM   4023  CD1 PHE B 302      50.382  15.014  -1.474  1.00 25.90           C  
ANISOU 4023  CD1 PHE B 302     3234   3691   2914   -447    356   -446       C  
ATOM   4024  CD2 PHE B 302      50.519  14.835  -3.841  1.00 31.23           C  
ANISOU 4024  CD2 PHE B 302     4027   4340   3499   -648    461   -459       C  
ATOM   4025  CE1 PHE B 302      49.020  15.272  -1.580  1.00 28.20           C  
ANISOU 4025  CE1 PHE B 302     3594   3949   3173   -466    299   -368       C  
ATOM   4026  CE2 PHE B 302      49.157  15.092  -3.944  1.00 31.31           C  
ANISOU 4026  CE2 PHE B 302     4111   4315   3472   -659    382   -374       C  
ATOM   4027  CZ  PHE B 302      48.424  15.320  -2.808  1.00 25.33           C  
ANISOU 4027  CZ  PHE B 302     3317   3554   2755   -567    305   -334       C  
ATOM   4028  N   LYS B 303      55.149  12.806  -3.231  1.00 29.10           N  
ANISOU 4028  N   LYS B 303     3405   4138   3515   -523    699   -835       N  
ATOM   4029  CA  LYS B 303      56.602  12.846  -3.230  1.00 34.44           C  
ANISOU 4029  CA  LYS B 303     3961   4819   4306   -527    765   -966       C  
ATOM   4030  C   LYS B 303      57.107  13.139  -4.628  1.00 35.64           C  
ANISOU 4030  C   LYS B 303     4150   4958   4432   -691    909  -1029       C  
ATOM   4031  O   LYS B 303      56.600  12.595  -5.621  1.00 33.11           O  
ANISOU 4031  O   LYS B 303     3930   4621   4028   -774    974  -1004       O  
ATOM   4032  CB  LYS B 303      57.223  11.539  -2.720  1.00 40.83           C  
ANISOU 4032  CB  LYS B 303     4680   5618   5217   -416    756  -1038       C  
ATOM   4033  CG  LYS B 303      58.757  11.543  -2.808  1.00 44.43           C  
ANISOU 4033  CG  LYS B 303     4992   6065   5823   -423    824  -1195       C  
ATOM   4034  CD  LYS B 303      59.404  10.520  -1.886  1.00 53.21           C  
ANISOU 4034  CD  LYS B 303     5997   7158   7064   -274    750  -1261       C  
ATOM   4035  CE  LYS B 303      59.683   9.235  -2.608  1.00 58.04           C  
ANISOU 4035  CE  LYS B 303     6589   7742   7720   -291    838  -1328       C  
ATOM   4036  NZ  LYS B 303      60.813   9.408  -3.567  1.00 68.63           N  
ANISOU 4036  NZ  LYS B 303     7842   9070   9163   -403    991  -1477       N  
ATOM   4037  N   LYS B 304      58.112  14.004  -4.672  1.00 37.40           N  
ANISOU 4037  N   LYS B 304     4299   5185   4726   -741    962  -1115       N  
ATOM   4038  CA  LYS B 304      58.821  14.402  -5.886  1.00 39.47           C  
ANISOU 4038  CA  LYS B 304     4587   5428   4980   -906   1121  -1201       C  
ATOM   4039  C   LYS B 304      60.278  14.567  -5.472  1.00 34.03           C  
ANISOU 4039  C   LYS B 304     3724   4739   4467   -878   1173  -1355       C  
ATOM   4040  O   LYS B 304      60.631  15.549  -4.807  1.00 38.37           O  
ANISOU 4040  O   LYS B 304     4211   5302   5067   -849   1119  -1365       O  
ATOM   4041  CB  LYS B 304      58.262  15.687  -6.490  1.00 41.36           C  
ANISOU 4041  CB  LYS B 304     4960   5659   5095  -1032   1125  -1121       C  
ATOM   4042  CG  LYS B 304      59.138  16.277  -7.595  1.00 50.49           C  
ANISOU 4042  CG  LYS B 304     6151   6788   6245  -1209   1293  -1219       C  
ATOM   4043  CD  LYS B 304      58.311  16.824  -8.753  1.00 57.90           C  
ANISOU 4043  CD  LYS B 304     7305   7693   7002  -1366   1321  -1126       C  
ATOM   4044  CE  LYS B 304      58.326  18.349  -8.787  1.00 60.55           C  
ANISOU 4044  CE  LYS B 304     7696   8016   7295  -1443   1299  -1090       C  
ATOM   4045  NZ  LYS B 304      58.804  18.846 -10.113  1.00 64.10           N  
ANISOU 4045  NZ  LYS B 304     8280   8416   7658  -1652   1460  -1143       N  
ATOM   4046  N   GLU B 305      61.108  13.591  -5.849  1.00 35.54           N  
ANISOU 4046  N   GLU B 305     3829   4910   4763   -884   1275  -1482       N  
ATOM   4047  CA  GLU B 305      62.534  13.569  -5.513  1.00 40.48           C  
ANISOU 4047  CA  GLU B 305     4267   5521   5592   -852   1325  -1653       C  
ATOM   4048  C   GLU B 305      62.643  13.581  -3.990  1.00 44.51           C  
ANISOU 4048  C   GLU B 305     4668   6048   6197   -664   1139  -1633       C  
ATOM   4049  O   GLU B 305      62.076  12.683  -3.345  1.00 46.60           O  
ANISOU 4049  O   GLU B 305     4948   6314   6442   -539   1026  -1564       O  
ATOM   4050  CB  GLU B 305      63.243  14.706  -6.261  1.00 50.17           C  
ANISOU 4050  CB  GLU B 305     5496   6735   6831  -1015   1470  -1737       C  
ATOM   4051  CG  GLU B 305      63.462  14.435  -7.759  1.00 60.33           C  
ANISOU 4051  CG  GLU B 305     6876   7987   8058  -1205   1682  -1806       C  
ATOM   4052  N   ARG B 306      63.328  14.543  -3.372  1.00 45.49           N  
ANISOU 4052  N   ARG B 306     4695   6178   6413   -640   1099  -1688       N  
ATOM   4053  CA  ARG B 306      63.481  14.542  -1.928  1.00 49.91           C  
ANISOU 4053  CA  ARG B 306     5164   6744   7054   -466    917  -1676       C  
ATOM   4054  C   ARG B 306      62.379  15.320  -1.215  1.00 47.08           C  
ANISOU 4054  C   ARG B 306     4917   6419   6551   -423    789  -1512       C  
ATOM   4055  O   ARG B 306      62.375  15.370   0.016  1.00 42.45           O  
ANISOU 4055  O   ARG B 306     4288   5838   6002   -288    639  -1487       O  
ATOM   4056  CB  ARG B 306      64.842  15.119  -1.542  1.00 54.60           C  
ANISOU 4056  CB  ARG B 306     5580   7321   7845   -449    925  -1835       C  
ATOM   4057  CG  ARG B 306      66.040  14.254  -1.906  1.00 56.74           C  
ANISOU 4057  CG  ARG B 306     5694   7546   8320   -447   1013  -2022       C  
ATOM   4058  CD  ARG B 306      67.338  14.956  -1.507  1.00 57.17           C  
ANISOU 4058  CD  ARG B 306     5563   7576   8582   -434   1014  -2185       C  
ATOM   4059  N   LYS B 307      61.465  15.939  -1.952  1.00 45.94           N  
ANISOU 4059  N   LYS B 307     4916   6290   6250   -537    842  -1408       N  
ATOM   4060  CA  LYS B 307      60.392  16.712  -1.351  1.00 40.60           C  
ANISOU 4060  CA  LYS B 307     4334   5636   5457   -507    730  -1266       C  
ATOM   4061  C   LYS B 307      59.185  15.822  -1.078  1.00 36.15           C  
ANISOU 4061  C   LYS B 307     3871   5074   4792   -436    655  -1146       C  
ATOM   4062  O   LYS B 307      58.680  15.161  -1.988  1.00 32.91           O  
ANISOU 4062  O   LYS B 307     3543   4652   4309   -502    726  -1116       O  
ATOM   4063  CB  LYS B 307      59.994  17.875  -2.259  1.00 33.93           C  
ANISOU 4063  CB  LYS B 307     3591   4792   4509   -661    805  -1216       C  
ATOM   4064  CG  LYS B 307      58.815  18.664  -1.730  1.00 36.72           C  
ANISOU 4064  CG  LYS B 307     4037   5159   4756   -635    691  -1074       C  
ATOM   4065  CD  LYS B 307      59.189  19.367  -0.403  1.00 38.21           C  
ANISOU 4065  CD  LYS B 307     4128   5366   5024   -528    582  -1091       C  
ATOM   4066  CE  LYS B 307      58.124  20.402  -0.020  1.00 37.76           C  
ANISOU 4066  CE  LYS B 307     4156   5316   4876   -535    498   -971       C  
ATOM   4067  NZ  LYS B 307      58.161  20.822   1.421  1.00 34.23           N  
ANISOU 4067  NZ  LYS B 307     3645   4885   4476   -412    376   -962       N  
ATOM   4068  N   GLU B 308      58.702  15.846   0.166  1.00 37.35           N  
ANISOU 4068  N   GLU B 308     4024   5234   4933   -310    517  -1080       N  
ATOM   4069  CA  GLU B 308      57.534  15.092   0.605  1.00 28.57           C  
ANISOU 4069  CA  GLU B 308     3006   4117   3733   -240    446   -972       C  
ATOM   4070  C   GLU B 308      56.439  16.019   1.127  1.00 30.47           C  
ANISOU 4070  C   GLU B 308     3326   4368   3885   -238    373   -859       C  
ATOM   4071  O   GLU B 308      56.715  17.111   1.644  1.00 34.93           O  
ANISOU 4071  O   GLU B 308     3852   4945   4475   -236    332   -868       O  
ATOM   4072  CB  GLU B 308      57.913  14.090   1.715  1.00 34.75           C  
ANISOU 4072  CB  GLU B 308     3735   4883   4584    -89    354  -1003       C  
ATOM   4073  CG  GLU B 308      58.966  13.035   1.300  1.00 37.80           C  
ANISOU 4073  CG  GLU B 308     4031   5248   5085    -70    407  -1121       C  
ATOM   4074  CD  GLU B 308      59.322  12.121   2.438  1.00 43.24           C  
ANISOU 4074  CD  GLU B 308     4682   5907   5842     84    288  -1144       C  
ATOM   4075  OE1 GLU B 308      60.075  12.552   3.343  1.00 49.06           O  
ANISOU 4075  OE1 GLU B 308     5341   6636   6664    159    194  -1199       O  
ATOM   4076  OE2 GLU B 308      58.811  10.980   2.447  1.00 45.76           O  
ANISOU 4076  OE2 GLU B 308     5059   6204   6123    128    279  -1104       O  
ATOM   4077  N   ALA B 309      55.188  15.558   1.006  1.00 25.15           N  
ANISOU 4077  N   ALA B 309     2753   3682   3119   -238    356   -762       N  
ATOM   4078  CA  ALA B 309      54.045  16.274   1.543  1.00 32.74           C  
ANISOU 4078  CA  ALA B 309     3781   4641   4016   -228    288   -665       C  
ATOM   4079  C   ALA B 309      52.977  15.278   1.951  1.00 31.22           C  
ANISOU 4079  C   ALA B 309     3660   4428   3775   -165    257   -597       C  
ATOM   4080  O   ALA B 309      52.906  14.155   1.437  1.00 30.60           O  
ANISOU 4080  O   ALA B 309     3603   4338   3685   -164    299   -604       O  
ATOM   4081  CB  ALA B 309      53.458  17.294   0.535  1.00 24.19           C  
ANISOU 4081  CB  ALA B 309     2761   3553   2878   -357    321   -617       C  
ATOM   4082  N   MET B 310      52.147  15.687   2.897  1.00 27.74           N  
ANISOU 4082  N   MET B 310     3253   3979   3309   -117    190   -538       N  
ATOM   4083  CA  MET B 310      50.916  14.954   3.119  1.00 29.39           C  
ANISOU 4083  CA  MET B 310     3539   4159   3469    -89    181   -471       C  
ATOM   4084  C   MET B 310      49.819  15.936   3.479  1.00 24.24           C  
ANISOU 4084  C   MET B 310     2922   3491   2797   -112    143   -410       C  
ATOM   4085  O   MET B 310      50.078  16.997   4.062  1.00 26.91           O  
ANISOU 4085  O   MET B 310     3227   3842   3157   -107    105   -419       O  
ATOM   4086  CB  MET B 310      51.058  13.870   4.189  1.00 30.00           C  
ANISOU 4086  CB  MET B 310     3630   4219   3548     25    149   -481       C  
ATOM   4087  CG  MET B 310      51.506  14.334   5.526  1.00 51.31           C  
ANISOU 4087  CG  MET B 310     6312   6920   6265    104     77   -499       C  
ATOM   4088  SD  MET B 310      50.548  13.374   6.695  1.00 77.96           S  
ANISOU 4088  SD  MET B 310     9792  10249   9582    188     51   -448       S  
ATOM   4089  CE  MET B 310      48.945  14.161   6.528  1.00 68.50           C  
ANISOU 4089  CE  MET B 310     8640   9034   8354    115     81   -379       C  
ATOM   4090  N   ILE B 311      48.602  15.596   3.077  1.00 27.62           N  
ANISOU 4090  N   ILE B 311     3410   3887   3197   -142    153   -356       N  
ATOM   4091  CA  ILE B 311      47.436  16.439   3.324  1.00 21.55           C  
ANISOU 4091  CA  ILE B 311     2665   3089   2433   -167    118   -308       C  
ATOM   4092  C   ILE B 311      46.430  15.649   4.149  1.00 26.56           C  
ANISOU 4092  C   ILE B 311     3342   3687   3062   -108    122   -283       C  
ATOM   4093  O   ILE B 311      46.226  14.442   3.926  1.00 23.23           O  
ANISOU 4093  O   ILE B 311     2955   3252   2620    -87    156   -279       O  
ATOM   4094  CB  ILE B 311      46.823  16.955   2.002  1.00 24.18           C  
ANISOU 4094  CB  ILE B 311     3028   3401   2760   -271    113   -275       C  
ATOM   4095  CG1 ILE B 311      45.664  17.914   2.290  1.00 23.53           C  
ANISOU 4095  CG1 ILE B 311     2952   3276   2712   -291     59   -236       C  
ATOM   4096  CG2 ILE B 311      46.359  15.784   1.075  1.00 24.47           C  
ANISOU 4096  CG2 ILE B 311     3116   3417   2766   -298    149   -260       C  
ATOM   4097  CD1 ILE B 311      45.160  18.659   1.033  1.00 24.65           C  
ANISOU 4097  CD1 ILE B 311     3129   3384   2853   -393     20   -202       C  
ATOM   4098  N   ASN B 312      45.848  16.315   5.149  1.00 21.38           N  
ANISOU 4098  N   ASN B 312     2688   3011   2425    -83     98   -273       N  
ATOM   4099  CA  ASN B 312      44.793  15.718   5.960  1.00 24.30           C  
ANISOU 4099  CA  ASN B 312     3106   3334   2794    -46    120   -258       C  
ATOM   4100  C   ASN B 312      43.752  16.759   6.343  1.00 30.78           C  
ANISOU 4100  C   ASN B 312     3913   4116   3665    -77    104   -248       C  
ATOM   4101  O   ASN B 312      44.048  17.675   7.122  1.00 28.12           O  
ANISOU 4101  O   ASN B 312     3554   3791   3340    -63     81   -262       O  
ATOM   4102  CB  ASN B 312      45.338  15.069   7.232  1.00 24.97           C  
ANISOU 4102  CB  ASN B 312     3230   3420   2838     40    126   -278       C  
ATOM   4103  CG  ASN B 312      44.337  14.118   7.830  1.00 28.17           C  
ANISOU 4103  CG  ASN B 312     3709   3771   3224     65    174   -264       C  
ATOM   4104  OD1 ASN B 312      43.890  13.198   7.138  1.00 29.29           O  
ANISOU 4104  OD1 ASN B 312     3868   3895   3364     51    208   -251       O  
ATOM   4105  ND2 ASN B 312      43.910  14.371   9.077  1.00 24.35           N  
ANISOU 4105  ND2 ASN B 312     3272   3255   2726     91    186   -270       N  
ATOM   4106  N   LEU B 313      42.525  16.554   5.870  1.00 27.42           N  
ANISOU 4106  N   LEU B 313     3497   3640   3281   -114    117   -230       N  
ATOM   4107  CA  LEU B 313      41.403  17.425   6.202  1.00 25.59           C  
ANISOU 4107  CA  LEU B 313     3240   3354   3128   -142    103   -233       C  
ATOM   4108  C   LEU B 313      41.178  17.496   7.704  1.00 32.71           C  
ANISOU 4108  C   LEU B 313     4165   4237   4028    -97    146   -260       C  
ATOM   4109  O   LEU B 313      41.172  16.472   8.391  1.00 26.18           O  
ANISOU 4109  O   LEU B 313     3400   3399   3150    -54    201   -267       O  
ATOM   4110  CB  LEU B 313      40.123  16.927   5.516  1.00 28.73           C  
ANISOU 4110  CB  LEU B 313     3642   3689   3585   -178    110   -224       C  
ATOM   4111  CG  LEU B 313      39.005  17.863   5.987  1.00 40.78           C  
ANISOU 4111  CG  LEU B 313     5124   5150   5220   -201     96   -245       C  
ATOM   4112  CD1 LEU B 313      38.421  18.719   4.893  1.00 40.62           C  
ANISOU 4112  CD1 LEU B 313     5063   5090   5281   -262      6   -229       C  
ATOM   4113  CD2 LEU B 313      37.959  17.136   6.736  1.00 45.87           C  
ANISOU 4113  CD2 LEU B 313     5786   5733   5910   -184    174   -276       C  
ATOM   4114  N   ALA B 314      40.990  18.718   8.215  1.00 21.01           N  
ANISOU 4114  N   ALA B 314     2643   2743   2595   -114    123   -275       N  
ATOM   4115  CA  ALA B 314      40.624  18.942   9.607  1.00 26.28           C  
ANISOU 4115  CA  ALA B 314     3338   3381   3267    -90    171   -307       C  
ATOM   4116  C   ALA B 314      39.667  20.117   9.662  1.00 26.00           C  
ANISOU 4116  C   ALA B 314     3236   3294   3347   -136    157   -329       C  
ATOM   4117  O   ALA B 314      39.990  21.198   9.172  1.00 25.90           O  
ANISOU 4117  O   ALA B 314     3166   3302   3372   -163     88   -319       O  
ATOM   4118  CB  ALA B 314      41.842  19.242  10.488  1.00 25.07           C  
ANISOU 4118  CB  ALA B 314     3210   3280   3035    -44    150   -317       C  
ATOM   4119  N   LYS B 315      38.513  19.920  10.278  1.00 24.35           N  
ANISOU 4119  N   LYS B 315     3037   3013   3203   -149    227   -364       N  
ATOM   4120  CA  LYS B 315      37.505  20.970  10.323  1.00 27.41           C  
ANISOU 4120  CA  LYS B 315     3347   3336   3732   -193    217   -399       C  
ATOM   4121  C   LYS B 315      36.905  21.158  11.710  1.00 28.31           C  
ANISOU 4121  C   LYS B 315     3484   3398   3873   -195    315   -460       C  
ATOM   4122  O   LYS B 315      35.884  21.844  11.832  1.00 33.25           O  
ANISOU 4122  O   LYS B 315     4041   3953   4641   -234    332   -508       O  
ATOM   4123  CB  LYS B 315      36.375  20.663   9.338  1.00 28.73           C  
ANISOU 4123  CB  LYS B 315     3466   3437   4014   -228    196   -402       C  
ATOM   4124  CG  LYS B 315      35.743  19.317   9.613  1.00 29.13           C  
ANISOU 4124  CG  LYS B 315     3570   3448   4050   -217    294   -421       C  
ATOM   4125  CD  LYS B 315      34.533  19.089   8.739  1.00 45.01           C  
ANISOU 4125  CD  LYS B 315     5520   5381   6199   -252    271   -440       C  
ATOM   4126  CE  LYS B 315      33.313  19.806   9.327  1.00 51.76           C  
ANISOU 4126  CE  LYS B 315     6298   6138   7230   -284    310   -518       C  
ATOM   4127  NZ  LYS B 315      32.108  19.716   8.433  1.00 50.74           N  
ANISOU 4127  NZ  LYS B 315     6088   5919   7270   -315    259   -547       N  
ATOM   4128  N   ASN B 316      37.462  20.526  12.742  1.00 23.87           N  
ANISOU 4128  N   ASN B 316     3026   2858   3185   -161    382   -464       N  
ATOM   4129  CA  ASN B 316      36.958  20.666  14.100  1.00 24.70           C  
ANISOU 4129  CA  ASN B 316     3188   2909   3287   -174    486   -521       C  
ATOM   4130  C   ASN B 316      38.105  20.370  15.060  1.00 24.81           C  
ANISOU 4130  C   ASN B 316     3321   2973   3132   -128    485   -504       C  
ATOM   4131  O   ASN B 316      39.177  19.936  14.633  1.00 23.89           O  
ANISOU 4131  O   ASN B 316     3226   2925   2927    -82    410   -456       O  
ATOM   4132  CB  ASN B 316      35.760  19.736  14.338  1.00 30.41           C  
ANISOU 4132  CB  ASN B 316     3948   3547   4061   -203    607   -563       C  
ATOM   4133  CG  ASN B 316      36.080  18.268  14.049  1.00 31.53           C  
ANISOU 4133  CG  ASN B 316     4179   3706   4094   -168    626   -520       C  
ATOM   4134  OD1 ASN B 316      37.177  17.773  14.313  1.00 32.04           O  
ANISOU 4134  OD1 ASN B 316     4330   3829   4014   -119    591   -478       O  
ATOM   4135  ND2 ASN B 316      35.116  17.581  13.478  1.00 28.50           N  
ANISOU 4135  ND2 ASN B 316     3766   3267   3795   -192    672   -535       N  
ATOM   4136  N   PRO B 317      37.910  20.570  16.370  1.00 28.01           N  
ANISOU 4136  N   PRO B 317     3810   3338   3493   -141    565   -549       N  
ATOM   4137  CA  PRO B 317      39.064  20.426  17.277  1.00 33.17           C  
ANISOU 4137  CA  PRO B 317     4582   4033   3987    -94    531   -532       C  
ATOM   4138  C   PRO B 317      39.695  19.032  17.279  1.00 32.46           C  
ANISOU 4138  C   PRO B 317     4607   3959   3767    -41    516   -488       C  
ATOM   4139  O   PRO B 317      40.923  18.924  17.245  1.00 31.72           O  
ANISOU 4139  O   PRO B 317     4534   3927   3593     16    416   -456       O  
ATOM   4140  CB  PRO B 317      38.482  20.822  18.646  1.00 24.81           C  
ANISOU 4140  CB  PRO B 317     3614   2906   2907   -135    638   -594       C  
ATOM   4141  CG  PRO B 317      37.385  21.738  18.327  1.00 27.86           C  
ANISOU 4141  CG  PRO B 317     3866   3247   3474   -196    686   -647       C  
ATOM   4142  CD  PRO B 317      36.780  21.236  17.039  1.00 26.91           C  
ANISOU 4142  CD  PRO B 317     3646   3118   3461   -202    667   -624       C  
ATOM   4143  N   ALA B 318      38.901  17.965  17.302  1.00 29.91           N  
ANISOU 4143  N   ALA B 318     4352   3576   3435    -58    610   -492       N  
ATOM   4144  CA  ALA B 318      39.464  16.616  17.314  1.00 28.04           C  
ANISOU 4144  CA  ALA B 318     4228   3345   3080     -7    596   -451       C  
ATOM   4145  C   ALA B 318      40.264  16.346  16.046  1.00 26.89           C  
ANISOU 4145  C   ALA B 318     3984   3276   2957     36    488   -404       C  
ATOM   4146  O   ALA B 318      41.405  15.871  16.103  1.00 28.31           O  
ANISOU 4146  O   ALA B 318     4210   3498   3049     96    407   -376       O  
ATOM   4147  CB  ALA B 318      38.344  15.578  17.491  1.00 24.85           C  
ANISOU 4147  CB  ALA B 318     3904   2856   2681    -44    730   -470       C  
ATOM   4148  N   GLY B 319      39.691  16.663  14.886  1.00 25.59           N  
ANISOU 4148  N   GLY B 319     3685   3123   2914      1    482   -401       N  
ATOM   4149  CA  GLY B 319      40.419  16.466  13.641  1.00 23.38           C  
ANISOU 4149  CA  GLY B 319     3325   2910   2648     25    394   -362       C  
ATOM   4150  C   GLY B 319      41.698  17.286  13.557  1.00 25.53           C  
ANISOU 4150  C   GLY B 319     3548   3257   2896     55    291   -353       C  
ATOM   4151  O   GLY B 319      42.708  16.816  13.033  1.00 27.06           O  
ANISOU 4151  O   GLY B 319     3730   3501   3049     94    231   -332       O  
ATOM   4152  N   MET B 320      41.678  18.522  14.085  1.00 23.23           N  
ANISOU 4152  N   MET B 320     3219   2968   2638     34    276   -378       N  
ATOM   4153  CA  MET B 320      42.880  19.367  14.055  1.00 22.40           C  
ANISOU 4153  CA  MET B 320     3063   2929   2520     58    184   -377       C  
ATOM   4154  C   MET B 320      43.966  18.816  14.974  1.00 22.87           C  
ANISOU 4154  C   MET B 320     3219   3004   2467    126    141   -381       C  
ATOM   4155  O   MET B 320      45.138  18.743  14.592  1.00 24.32           O  
ANISOU 4155  O   MET B 320     3364   3241   2636    166     62   -377       O  
ATOM   4156  CB  MET B 320      42.530  20.809  14.449  1.00 24.46           C  
ANISOU 4156  CB  MET B 320     3265   3182   2848     19    181   -406       C  
ATOM   4157  CG  MET B 320      43.716  21.803  14.405  1.00 25.49           C  
ANISOU 4157  CG  MET B 320     3332   3376   2977     36     91   -411       C  
ATOM   4158  SD  MET B 320      44.471  21.992  12.769  1.00 25.82           S  
ANISOU 4158  SD  MET B 320     3265   3481   3065     21     25   -382       S  
ATOM   4159  CE  MET B 320      43.174  22.855  11.884  1.00 21.54           C  
ANISOU 4159  CE  MET B 320     2645   2896   2645    -59     38   -371       C  
ATOM   4160  N   ASN B 321      43.589  18.432  16.193  1.00 23.46           N  
ANISOU 4160  N   ASN B 321     3425   3022   2465    136    190   -395       N  
ATOM   4161  CA  ASN B 321      44.538  17.802  17.108  1.00 30.98           C  
ANISOU 4161  CA  ASN B 321     4500   3970   3302    202    131   -394       C  
ATOM   4162  C   ASN B 321      45.173  16.562  16.486  1.00 26.60           C  
ANISOU 4162  C   ASN B 321     3957   3430   2720    254     90   -368       C  
ATOM   4163  O   ASN B 321      46.386  16.369  16.592  1.00 27.37           O  
ANISOU 4163  O   ASN B 321     4053   3556   2789    316    -10   -373       O  
ATOM   4164  CB  ASN B 321      43.855  17.427  18.421  1.00 26.05           C  
ANISOU 4164  CB  ASN B 321     4050   3264   2584    188    207   -407       C  
ATOM   4165  CG  ASN B 321      43.511  18.616  19.254  1.00 34.87           C  
ANISOU 4165  CG  ASN B 321     5174   4364   3710    146    237   -445       C  
ATOM   4166  OD1 ASN B 321      43.996  19.723  19.018  1.00 38.02           O  
ANISOU 4166  OD1 ASN B 321     5459   4815   4170    144    176   -459       O  
ATOM   4167  ND2 ASN B 321      42.690  18.393  20.273  1.00 30.01           N  
ANISOU 4167  ND2 ASN B 321     4702   3669   3030    107    340   -468       N  
ATOM   4168  N   ALA B 322      44.378  15.733  15.799  1.00 27.97           N  
ANISOU 4168  N   ALA B 322     4130   3580   2917    230    164   -347       N  
ATOM   4169  CA  ALA B 322      44.946  14.571  15.106  1.00 30.85           C  
ANISOU 4169  CA  ALA B 322     4494   3960   3268    274    132   -326       C  
ATOM   4170  C   ALA B 322      45.899  14.998  13.995  1.00 28.45           C  
ANISOU 4170  C   ALA B 322     4044   3732   3033    281     62   -332       C  
ATOM   4171  O   ALA B 322      46.989  14.428  13.849  1.00 33.97           O  
ANISOU 4171  O   ALA B 322     4735   4453   3718    338     -6   -340       O  
ATOM   4172  CB  ALA B 322      43.835  13.679  14.538  1.00 23.48           C  
ANISOU 4172  CB  ALA B 322     3580   2987   2353    238    230   -308       C  
ATOM   4173  N   SER B 323      45.514  15.995  13.195  1.00 26.72           N  
ANISOU 4173  N   SER B 323     3713   3546   2895    221     79   -333       N  
ATOM   4174  CA  SER B 323      46.390  16.385  12.091  1.00 25.09           C  
ANISOU 4174  CA  SER B 323     3389   3402   2743    211     30   -339       C  
ATOM   4175  C   SER B 323      47.693  16.985  12.604  1.00 25.59           C  
ANISOU 4175  C   SER B 323     3420   3502   2802    255    -54   -373       C  
ATOM   4176  O   SER B 323      48.753  16.782  12.007  1.00 29.74           O  
ANISOU 4176  O   SER B 323     3881   4065   3355    277    -95   -395       O  
ATOM   4177  CB  SER B 323      45.685  17.364  11.161  1.00 29.57           C  
ANISOU 4177  CB  SER B 323     3869   3981   3385    133     54   -329       C  
ATOM   4178  OG  SER B 323      44.516  16.796  10.635  1.00 28.83           O  
ANISOU 4178  OG  SER B 323     3795   3848   3311     96    115   -306       O  
ATOM   4179  N   LEU B 324      47.629  17.743  13.699  1.00 28.09           N  
ANISOU 4179  N   LEU B 324     3775   3803   3094    265    -75   -387       N  
ATOM   4180  CA  LEU B 324      48.834  18.356  14.248  1.00 25.41           C  
ANISOU 4180  CA  LEU B 324     3404   3493   2756    308   -165   -425       C  
ATOM   4181  C   LEU B 324      49.744  17.312  14.862  1.00 33.01           C  
ANISOU 4181  C   LEU B 324     4439   4435   3667    393   -238   -440       C  
ATOM   4182  O   LEU B 324      50.964  17.497  14.881  1.00 37.46           O  
ANISOU 4182  O   LEU B 324     4940   5025   4267    437   -323   -481       O  
ATOM   4183  CB  LEU B 324      48.464  19.398  15.293  1.00 25.52           C  
ANISOU 4183  CB  LEU B 324     3456   3491   2751    292   -168   -437       C  
ATOM   4184  CG  LEU B 324      47.667  20.610  14.803  1.00 28.23           C  
ANISOU 4184  CG  LEU B 324     3714   3846   3165    215   -118   -431       C  
ATOM   4185  CD1 LEU B 324      47.424  21.621  15.940  1.00 32.22           C  
ANISOU 4185  CD1 LEU B 324     4254   4332   3656    205   -122   -455       C  
ATOM   4186  CD2 LEU B 324      48.366  21.309  13.683  1.00 27.43           C  
ANISOU 4186  CD2 LEU B 324     3482   3801   3140    186   -149   -440       C  
ATOM   4187  N   SER B 325      49.180  16.204  15.358  1.00 29.63           N  
ANISOU 4187  N   SER B 325     4142   3952   3165    418   -210   -413       N  
ATOM   4188  CA  SER B 325      50.025  15.165  15.928  1.00 40.39           C  
ANISOU 4188  CA  SER B 325     5587   5280   4479    502   -296   -423       C  
ATOM   4189  C   SER B 325      50.669  14.277  14.860  1.00 44.14           C  
ANISOU 4189  C   SER B 325     5978   5777   5016    527   -307   -434       C  
ATOM   4190  O   SER B 325      51.608  13.549  15.175  1.00 44.11           O  
ANISOU 4190  O   SER B 325     5998   5750   5012    603   -399   -459       O  
ATOM   4191  CB  SER B 325      49.219  14.320  16.915  1.00 38.90           C  
ANISOU 4191  CB  SER B 325     5591   5011   4177    514   -261   -390       C  
ATOM   4192  N   VAL B 326      50.194  14.328  13.610  1.00 36.32           N  
ANISOU 4192  N   VAL B 326     4896   4824   4081    464   -221   -421       N  
ATOM   4193  CA  VAL B 326      50.851  13.597  12.529  1.00 36.64           C  
ANISOU 4193  CA  VAL B 326     4852   4888   4181    473   -219   -441       C  
ATOM   4194  C   VAL B 326      52.260  14.117  12.319  1.00 41.55           C  
ANISOU 4194  C   VAL B 326     5355   5548   4884    500   -295   -507       C  
ATOM   4195  O   VAL B 326      53.217  13.341  12.179  1.00 38.68           O  
ANISOU 4195  O   VAL B 326     4958   5175   4565    557   -348   -549       O  
ATOM   4196  CB  VAL B 326      50.043  13.704  11.228  1.00 41.23           C  
ANISOU 4196  CB  VAL B 326     5374   5498   4794    387   -118   -415       C  
ATOM   4197  CG1 VAL B 326      50.905  13.182  10.065  1.00 43.08           C  
ANISOU 4197  CG1 VAL B 326     5513   5763   5091    381   -110   -450       C  
ATOM   4198  CG2 VAL B 326      48.741  12.923  11.337  1.00 36.95           C  
ANISOU 4198  CG2 VAL B 326     4933   4909   4197    369    -45   -365       C  
ATOM   4199  N   GLY B 327      52.411  15.440  12.318  1.00 37.02           N  
ANISOU 4199  N   GLY B 327     4712   5012   4342    460   -300   -523       N  
ATOM   4200  CA  GLY B 327      53.714  16.030  12.094  1.00 32.32           C  
ANISOU 4200  CA  GLY B 327     3995   4451   3835    475   -358   -595       C  
ATOM   4201  C   GLY B 327      54.768  15.521  13.044  1.00 35.93           C  
ANISOU 4201  C   GLY B 327     4471   4872   4307    578   -484   -644       C  
ATOM   4202  O   GLY B 327      55.916  15.309  12.653  1.00 44.90           O  
ANISOU 4202  O   GLY B 327     5503   6016   5542    609   -527   -717       O  
ATOM   4203  N   GLU B 328      54.402  15.300  14.306  1.00 45.59           N  
ANISOU 4203  N   GLU B 328     5835   6046   5440    630   -547   -613       N  
ATOM   4204  CA  GLU B 328      55.437  14.888  15.246  1.00 43.64           C  
ANISOU 4204  CA  GLU B 328     5623   5754   5205    730   -697   -660       C  
ATOM   4205  C   GLU B 328      55.860  13.437  15.049  1.00 39.30           C  
ANISOU 4205  C   GLU B 328     5098   5158   4677    795   -738   -672       C  
ATOM   4206  O   GLU B 328      56.952  13.060  15.485  1.00 38.37           O  
ANISOU 4206  O   GLU B 328     4955   5002   4621    879   -872   -732       O  
ATOM   4207  CB  GLU B 328      55.000  15.157  16.693  1.00 57.00           C  
ANISOU 4207  CB  GLU B 328     7481   7398   6778    759   -762   -626       C  
ATOM   4208  CG  GLU B 328      53.858  14.337  17.234  1.00 75.28           C  
ANISOU 4208  CG  GLU B 328     9985   9657   8961    751   -707   -553       C  
ATOM   4209  CD  GLU B 328      53.508  14.730  18.665  1.00 88.07           C  
ANISOU 4209  CD  GLU B 328    11776  11226  10462    763   -757   -534       C  
ATOM   4210  OE1 GLU B 328      52.857  15.781  18.865  1.00 92.69           O  
ANISOU 4210  OE1 GLU B 328    12356  11838  11025    698   -686   -524       O  
ATOM   4211  OE2 GLU B 328      53.907  14.001  19.597  1.00 93.15           O  
ANISOU 4211  OE2 GLU B 328    12565  11795  11032    834   -871   -532       O  
ATOM   4212  N   GLN B 329      55.062  12.618  14.368  1.00 38.85           N  
ANISOU 4212  N   GLN B 329     5077   5099   4586    759   -634   -624       N  
ATOM   4213  CA  GLN B 329      55.545  11.280  14.048  1.00 39.50           C  
ANISOU 4213  CA  GLN B 329     5158   5141   4709    817   -667   -645       C  
ATOM   4214  C   GLN B 329      56.402  11.264  12.796  1.00 38.77           C  
ANISOU 4214  C   GLN B 329     4877   5093   4760    793   -626   -719       C  
ATOM   4215  O   GLN B 329      56.860  10.198  12.388  1.00 41.95           O  
ANISOU 4215  O   GLN B 329     5252   5466   5221    832   -639   -751       O  
ATOM   4216  CB  GLN B 329      54.372  10.310  13.886  1.00 43.61           C  
ANISOU 4216  CB  GLN B 329     5801   5632   5135    792   -573   -569       C  
ATOM   4217  CG  GLN B 329      53.577  10.107  15.163  1.00 48.47           C  
ANISOU 4217  CG  GLN B 329     6623   6185   5610    813   -600   -507       C  
ATOM   4218  CD  GLN B 329      52.431   9.132  14.970  1.00 57.71           C  
ANISOU 4218  CD  GLN B 329     7904   7320   6703    783   -494   -444       C  
ATOM   4219  OE1 GLN B 329      52.459   8.015  15.490  1.00 67.14           O  
ANISOU 4219  OE1 GLN B 329     9225   8441   7844    840   -542   -426       O  
ATOM   4220  NE2 GLN B 329      51.418   9.548  14.219  1.00 52.67           N  
ANISOU 4220  NE2 GLN B 329     7222   6727   6064    693   -357   -414       N  
ATOM   4221  N   LEU B 330      56.608  12.414  12.173  1.00 40.51           N  
ANISOU 4221  N   LEU B 330     4860   5788   4743   1362   -434   -905       N  
ATOM   4222  CA  LEU B 330      57.331  12.530  10.914  1.00 40.50           C  
ANISOU 4222  CA  LEU B 330     4647   5898   4843   1285   -357  -1031       C  
ATOM   4223  C   LEU B 330      58.755  12.983  11.204  1.00 46.48           C  
ANISOU 4223  C   LEU B 330     5140   6855   5667   1387   -459  -1219       C  
ATOM   4224  O   LEU B 330      58.964  13.935  11.959  1.00 56.27           O  
ANISOU 4224  O   LEU B 330     6291   8181   6908   1350   -533  -1252       O  
ATOM   4225  CB  LEU B 330      56.619  13.532  10.007  1.00 38.32           C  
ANISOU 4225  CB  LEU B 330     4324   5633   4601    996   -217   -981       C  
ATOM   4226  CG  LEU B 330      55.894  13.153   8.708  1.00 42.93           C  
ANISOU 4226  CG  LEU B 330     4987   6135   5190    857    -79   -926       C  
ATOM   4227  CD1 LEU B 330      55.496  11.667   8.579  1.00 32.69           C  
ANISOU 4227  CD1 LEU B 330     3880   4686   3856    985    -73   -881       C  
ATOM   4228  CD2 LEU B 330      54.697  14.068   8.545  1.00 36.96           C  
ANISOU 4228  CD2 LEU B 330     4303   5324   4416    647    -18   -807       C  
ATOM   4229  N   GLU B 331      59.732  12.309  10.614  1.00 50.00           N  
ANISOU 4229  N   GLU B 331     5447   7375   6174   1513   -463  -1361       N  
ATOM   4230  CA  GLU B 331      61.124  12.607  10.915  1.00 51.68           C  
ANISOU 4230  CA  GLU B 331     5376   7791   6470   1634   -569  -1572       C  
ATOM   4231  C   GLU B 331      61.576  13.878  10.204  1.00 48.40           C  
ANISOU 4231  C   GLU B 331     4697   7534   6158   1369   -445  -1681       C  
ATOM   4232  O   GLU B 331      61.161  14.162   9.077  1.00 48.13           O  
ANISOU 4232  O   GLU B 331     4675   7470   6141   1153   -262  -1635       O  
ATOM   4233  CB  GLU B 331      62.019  11.431  10.518  1.00 57.29           C  
ANISOU 4233  CB  GLU B 331     6011   8532   7224   1876   -608  -1705       C  
ATOM   4234  N   GLY B 332      62.420  14.647  10.874  1.00 43.21           N  
ANISOU 4234  N   GLY B 332     3818   7037   5562   1383   -548  -1827       N  
ATOM   4235  CA  GLY B 332      62.985  15.828  10.262  1.00 46.80           C  
ANISOU 4235  CA  GLY B 332     4018   7635   6128   1128   -422  -1953       C  
ATOM   4236  C   GLY B 332      62.094  17.034  10.412  1.00 42.72           C  
ANISOU 4236  C   GLY B 332     3614   7041   5575    877   -357  -1818       C  
ATOM   4237  O   GLY B 332      61.029  16.995  11.033  1.00 45.61           O  
ANISOU 4237  O   GLY B 332     4229   7264   5837    902   -411  -1640       O  
ATOM   4238  N   GLU B 333      62.528  18.142   9.820  1.00 42.35           N  
ANISOU 4238  N   GLU B 333     3388   7084   5619    626   -224  -1909       N  
ATOM   4239  CA  GLU B 333      61.739  19.337  10.031  1.00 44.05           C  
ANISOU 4239  CA  GLU B 333     3718   7215   5805    412   -180  -1793       C  
ATOM   4240  C   GLU B 333      60.550  19.361   9.077  1.00 41.74           C  
ANISOU 4240  C   GLU B 333     3661   6761   5437    265    -28  -1590       C  
ATOM   4241  O   GLU B 333      60.528  18.665   8.061  1.00 41.05           O  
ANISOU 4241  O   GLU B 333     3603   6656   5337    264     79  -1573       O  
ATOM   4242  CB  GLU B 333      62.601  20.600   9.913  1.00 52.46           C  
ANISOU 4242  CB  GLU B 333     4541   8403   6989    194   -108  -1960       C  
ATOM   4243  CG  GLU B 333      63.279  20.872   8.606  1.00 65.18           C  
ANISOU 4243  CG  GLU B 333     5992  10089   8685     -7    115  -2061       C  
ATOM   4244  CD  GLU B 333      64.320  21.994   8.737  1.00 81.33           C  
ANISOU 4244  CD  GLU B 333     7761  12270  10869   -201    169  -2271       C  
ATOM   4245  OE1 GLU B 333      64.604  22.421   9.883  1.00 86.85           O  
ANISOU 4245  OE1 GLU B 333     8392  13011  11596   -137     -3  -2352       O  
ATOM   4246  OE2 GLU B 333      64.859  22.446   7.701  1.00 84.21           O  
ANISOU 4246  OE2 GLU B 333     8061  12650  11284   -418    383  -2326       O  
ATOM   4247  N   LYS B 334      59.536  20.152   9.447  1.00 33.32           N  
ANISOU 4247  N   LYS B 334     2763   5580   4318    159    -34  -1446       N  
ATOM   4248  CA  LYS B 334      58.259  20.231   8.755  1.00 33.99           C  
ANISOU 4248  CA  LYS B 334     3073   5512   4329     53     59  -1256       C  
ATOM   4249  C   LYS B 334      58.012  21.654   8.272  1.00 40.30           C  
ANISOU 4249  C   LYS B 334     3889   6273   5150   -196    167  -1222       C  
ATOM   4250  O   LYS B 334      58.498  22.622   8.856  1.00 39.97           O  
ANISOU 4250  O   LYS B 334     3745   6277   5166   -276    141  -1307       O  
ATOM   4251  CB  LYS B 334      57.089  19.831   9.668  1.00 30.37           C  
ANISOU 4251  CB  LYS B 334     2823   4931   3787    175    -46  -1107       C  
ATOM   4252  CG  LYS B 334      56.707  18.345   9.679  1.00 28.02           C  
ANISOU 4252  CG  LYS B 334     2649   4567   3431    357    -83  -1045       C  
ATOM   4253  CD  LYS B 334      57.711  17.524  10.407  1.00 35.55           C  
ANISOU 4253  CD  LYS B 334     3507   5605   4394    581   -204  -1162       C  
ATOM   4254  CE  LYS B 334      57.668  17.750  11.896  1.00 36.07           C  
ANISOU 4254  CE  LYS B 334     3620   5674   4412    704   -357  -1158       C  
ATOM   4255  NZ  LYS B 334      58.442  16.667  12.552  1.00 43.26           N  
ANISOU 4255  NZ  LYS B 334     4514   6629   5295    974   -496  -1237       N  
ATOM   4256  N   VAL B 335      57.202  21.785   7.230  1.00 34.06           N  
ANISOU 4256  N   VAL B 335     3251   5385   4307   -310    276  -1096       N  
ATOM   4257  CA  VAL B 335      56.599  23.067   6.914  1.00 37.72           C  
ANISOU 4257  CA  VAL B 335     3819   5755   4756   -494    340  -1010       C  
ATOM   4258  C   VAL B 335      55.100  22.847   6.849  1.00 34.15           C  
ANISOU 4258  C   VAL B 335     3581   5169   4226   -447    296   -836       C  
ATOM   4259  O   VAL B 335      54.637  21.855   6.275  1.00 29.32           O  
ANISOU 4259  O   VAL B 335     3043   4533   3566   -379    305   -783       O  
ATOM   4260  CB  VAL B 335      57.132  23.688   5.611  1.00 37.03           C  
ANISOU 4260  CB  VAL B 335     3717   5681   4673   -699    520  -1039       C  
ATOM   4261  CG1 VAL B 335      56.907  22.747   4.394  1.00 28.53           C  
ANISOU 4261  CG1 VAL B 335     2721   4598   3520   -677    602   -993       C  
ATOM   4262  CG2 VAL B 335      56.444  25.013   5.392  1.00 29.91           C  
ANISOU 4262  CG2 VAL B 335     2971   4650   3745   -858    563   -932       C  
ATOM   4263  N   TYR B 336      54.347  23.740   7.480  1.00 25.95           N  
ANISOU 4263  N   TYR B 336     2627   4047   3185   -478    246   -767       N  
ATOM   4264  CA  TYR B 336      52.900  23.616   7.561  1.00 23.59           C  
ANISOU 4264  CA  TYR B 336     2491   3637   2835   -429    200   -629       C  
ATOM   4265  C   TYR B 336      52.223  24.599   6.625  1.00 24.38           C  
ANISOU 4265  C   TYR B 336     2716   3642   2907   -562    258   -540       C  
ATOM   4266  O   TYR B 336      52.689  25.732   6.441  1.00 25.63           O  
ANISOU 4266  O   TYR B 336     2872   3777   3088   -690    313   -564       O  
ATOM   4267  CB  TYR B 336      52.388  23.855   8.990  1.00 25.52           C  
ANISOU 4267  CB  TYR B 336     2755   3853   3087   -339    100   -616       C  
ATOM   4268  CG  TYR B 336      52.466  22.647   9.923  1.00 27.43           C  
ANISOU 4268  CG  TYR B 336     2982   4135   3305   -164     24   -636       C  
ATOM   4269  CD1 TYR B 336      53.665  22.276  10.499  1.00 25.94           C  
ANISOU 4269  CD1 TYR B 336     2668   4052   3136    -82    -27   -755       C  
ATOM   4270  CD2 TYR B 336      51.334  21.912  10.251  1.00 21.75           C  
ANISOU 4270  CD2 TYR B 336     2380   3341   2544    -82      4   -541       C  
ATOM   4271  CE1 TYR B 336      53.750  21.204  11.372  1.00 26.33           C  
ANISOU 4271  CE1 TYR B 336     2745   4118   3143    100   -111   -762       C  
ATOM   4272  CE2 TYR B 336      51.418  20.795  11.111  1.00 25.05           C  
ANISOU 4272  CE2 TYR B 336     2829   3765   2922     71    -48   -545       C  
ATOM   4273  CZ  TYR B 336      52.631  20.465  11.671  1.00 28.02           C  
ANISOU 4273  CZ  TYR B 336     3116   4233   3299    172   -112   -647       C  
ATOM   4274  OH  TYR B 336      52.758  19.402  12.544  1.00 30.69           O  
ANISOU 4274  OH  TYR B 336     3520   4562   3578    347   -179   -643       O  
ATOM   4275  N   VAL B 337      51.128  24.156   6.022  1.00 25.72           N  
ANISOU 4275  N   VAL B 337     3001   3748   3025   -528    242   -443       N  
ATOM   4276  CA  VAL B 337      50.193  25.066   5.383  1.00 25.09           C  
ANISOU 4276  CA  VAL B 337     3058   3565   2910   -592    240   -348       C  
ATOM   4277  C   VAL B 337      48.820  24.736   5.948  1.00 27.21           C  
ANISOU 4277  C   VAL B 337     3371   3781   3185   -488    150   -287       C  
ATOM   4278  O   VAL B 337      48.359  23.588   5.877  1.00 26.22           O  
ANISOU 4278  O   VAL B 337     3240   3675   3049   -418    129   -279       O  
ATOM   4279  CB  VAL B 337      50.238  24.984   3.845  1.00 31.95           C  
ANISOU 4279  CB  VAL B 337     4021   4422   3698   -670    310   -311       C  
ATOM   4280  CG1 VAL B 337      49.930  23.584   3.359  1.00 26.18           C  
ANISOU 4280  CG1 VAL B 337     3284   3732   2931   -593    294   -316       C  
ATOM   4281  CG2 VAL B 337      49.285  26.021   3.192  1.00 23.83           C  
ANISOU 4281  CG2 VAL B 337     3164   3276   2615   -709    280   -208       C  
ATOM   4282  N   ILE B 338      48.203  25.709   6.593  1.00 25.48           N  
ANISOU 4282  N   ILE B 338     3188   3496   2996   -480    107   -259       N  
ATOM   4283  CA  ILE B 338      46.951  25.475   7.298  1.00 23.17           C  
ANISOU 4283  CA  ILE B 338     2907   3169   2727   -387     43   -226       C  
ATOM   4284  C   ILE B 338      45.931  26.453   6.764  1.00 20.36           C  
ANISOU 4284  C   ILE B 338     2644   2723   2370   -394      2   -166       C  
ATOM   4285  O   ILE B 338      46.217  27.656   6.650  1.00 25.20           O  
ANISOU 4285  O   ILE B 338     3319   3271   2983   -448     10   -155       O  
ATOM   4286  CB  ILE B 338      47.120  25.634   8.816  1.00 20.33           C  
ANISOU 4286  CB  ILE B 338     2493   2827   2404   -331     25   -272       C  
ATOM   4287  CG1 ILE B 338      48.303  24.797   9.298  1.00 26.33           C  
ANISOU 4287  CG1 ILE B 338     3172   3677   3154   -303     39   -340       C  
ATOM   4288  CG2 ILE B 338      45.823  25.264   9.533  1.00 21.43           C  
ANISOU 4288  CG2 ILE B 338     2645   2937   2560   -248     -2   -244       C  
ATOM   4289  CD1 ILE B 338      48.537  24.913  10.830  1.00 25.77           C  
ANISOU 4289  CD1 ILE B 338     3072   3633   3088   -229     -1   -391       C  
ATOM   4290  N   SER B 339      44.758  25.945   6.401  1.00 19.67           N  
ANISOU 4290  N   SER B 339     2568   2623   2283   -338    -48   -135       N  
ATOM   4291  CA  SER B 339      43.767  26.762   5.720  1.00 23.80           C  
ANISOU 4291  CA  SER B 339     3172   3073   2798   -314   -117    -88       C  
ATOM   4292  C   SER B 339      42.449  26.759   6.464  1.00 25.34           C  
ANISOU 4292  C   SER B 339     3305   3256   3066   -224   -171   -104       C  
ATOM   4293  O   SER B 339      41.903  25.700   6.780  1.00 22.21           O  
ANISOU 4293  O   SER B 339     2828   2908   2701   -199   -161   -132       O  
ATOM   4294  CB  SER B 339      43.511  26.282   4.306  1.00 24.81           C  
ANISOU 4294  CB  SER B 339     3364   3209   2852   -329   -149    -58       C  
ATOM   4295  OG  SER B 339      42.552  27.131   3.707  1.00 27.04           O  
ANISOU 4295  OG  SER B 339     3735   3422   3116   -276   -246    -15       O  
ATOM   4296  N   LEU B 340      41.904  27.947   6.661  1.00 21.11           N  
ANISOU 4296  N   LEU B 340     2814   2646   2559   -180   -220    -92       N  
ATOM   4297  CA  LEU B 340      40.672  28.127   7.401  1.00 19.77           C  
ANISOU 4297  CA  LEU B 340     2572   2469   2471    -88   -258   -127       C  
ATOM   4298  C   LEU B 340      39.788  29.037   6.569  1.00 23.03           C  
ANISOU 4298  C   LEU B 340     3054   2810   2886    -13   -371   -101       C  
ATOM   4299  O   LEU B 340      39.934  30.268   6.618  1.00 25.16           O  
ANISOU 4299  O   LEU B 340     3426   2981   3151     11   -395    -76       O  
ATOM   4300  CB  LEU B 340      40.969  28.717   8.773  1.00 19.60           C  
ANISOU 4300  CB  LEU B 340     2531   2429   2487    -75   -206   -164       C  
ATOM   4301  CG  LEU B 340      39.808  28.918   9.738  1.00 31.62           C  
ANISOU 4301  CG  LEU B 340     3975   3951   4088     14   -207   -216       C  
ATOM   4302  CD1 LEU B 340      39.182  27.551  10.173  1.00 19.52           C  
ANISOU 4302  CD1 LEU B 340     2330   2503   2585     12   -148   -248       C  
ATOM   4303  CD2 LEU B 340      40.283  29.797  10.936  1.00 24.22           C  
ANISOU 4303  CD2 LEU B 340     3070   2976   3158     24   -167   -254       C  
ATOM   4304  N   ASN B 341      38.896  28.427   5.797  1.00 23.44           N  
ANISOU 4304  N   ASN B 341     3060   2903   2943     29   -448   -112       N  
ATOM   4305  CA  ASN B 341      37.817  29.144   5.137  1.00 25.18           C  
ANISOU 4305  CA  ASN B 341     3309   3079   3179    145   -589   -113       C  
ATOM   4306  C   ASN B 341      36.629  29.242   6.095  1.00 27.50           C  
ANISOU 4306  C   ASN B 341     3439   3402   3608    239   -603   -200       C  
ATOM   4307  O   ASN B 341      36.512  28.478   7.055  1.00 29.74           O  
ANISOU 4307  O   ASN B 341     3593   3751   3954    195   -498   -254       O  
ATOM   4308  CB  ASN B 341      37.370  28.433   3.852  1.00 23.24           C  
ANISOU 4308  CB  ASN B 341     3071   2882   2876    154   -688   -113       C  
ATOM   4309  CG  ASN B 341      38.227  28.756   2.656  1.00 33.91           C  
ANISOU 4309  CG  ASN B 341     4632   4180   4072    108   -707    -23       C  
ATOM   4310  OD1 ASN B 341      39.038  29.675   2.696  1.00 31.98           O  
ANISOU 4310  OD1 ASN B 341     4532   3843   3776     71   -656     42       O  
ATOM   4311  ND2 ASN B 341      38.037  27.992   1.555  1.00 27.05           N  
ANISOU 4311  ND2 ASN B 341     3787   3365   3124     98   -773    -29       N  
ATOM   4312  N   ASP B 342      35.744  30.194   5.824  1.00 29.18           N  
ANISOU 4312  N   ASP B 342     3668   3559   3859    375   -728   -217       N  
ATOM   4313  CA  ASP B 342      34.520  30.358   6.609  1.00 27.72           C  
ANISOU 4313  CA  ASP B 342     3306   3413   3815    481   -746   -322       C  
ATOM   4314  C   ASP B 342      33.323  30.490   5.670  1.00 27.92           C  
ANISOU 4314  C   ASP B 342     3265   3464   3880    619   -934   -374       C  
ATOM   4315  O   ASP B 342      32.397  31.288   5.879  1.00 28.43           O  
ANISOU 4315  O   ASP B 342     3265   3505   4032    775  -1025   -439       O  
ATOM   4316  CB  ASP B 342      34.650  31.526   7.605  1.00 28.78           C  
ANISOU 4316  CB  ASP B 342     3493   3455   3986    541   -701   -330       C  
ATOM   4317  CG  ASP B 342      34.653  32.921   6.948  1.00 31.01           C  
ANISOU 4317  CG  ASP B 342     3969   3588   4225    658   -832   -272       C  
ATOM   4318  OD1 ASP B 342      34.881  33.040   5.724  1.00 31.09           O  
ANISOU 4318  OD1 ASP B 342     4128   3552   4134    665   -934   -192       O  
ATOM   4319  OD2 ASP B 342      34.444  33.912   7.696  1.00 35.58           O  
ANISOU 4319  OD2 ASP B 342     4574   4082   4861    743   -823   -307       O  
ATOM   4320  N   ASN B 343      33.329  29.685   4.606  1.00 27.04           N  
ANISOU 4320  N   ASN B 343     3163   3409   3702    575  -1005   -361       N  
ATOM   4321  CA  ASN B 343      32.189  29.605   3.717  1.00 29.68           C  
ANISOU 4321  CA  ASN B 343     3407   3799   4070    698  -1200   -437       C  
ATOM   4322  C   ASN B 343      31.052  28.834   4.383  1.00 30.00           C  
ANISOU 4322  C   ASN B 343     3139   3967   4292    692  -1160   -598       C  
ATOM   4323  O   ASN B 343      31.216  28.235   5.453  1.00 31.71           O  
ANISOU 4323  O   ASN B 343     3252   4219   4579    576   -966   -629       O  
ATOM   4324  CB  ASN B 343      32.616  28.988   2.386  1.00 35.20           C  
ANISOU 4324  CB  ASN B 343     4233   4518   4623    642  -1283   -382       C  
ATOM   4325  CG  ASN B 343      33.660  29.849   1.688  1.00 40.43           C  
ANISOU 4325  CG  ASN B 343     5208   5049   5103    642  -1301   -229       C  
ATOM   4326  OD1 ASN B 343      33.511  31.068   1.630  1.00 42.65           O  
ANISOU 4326  OD1 ASN B 343     5624   5218   5363    770  -1386   -181       O  
ATOM   4327  ND2 ASN B 343      34.730  29.234   1.193  1.00 36.64           N  
ANISOU 4327  ND2 ASN B 343     4848   4574   4500    496  -1204   -158       N  
ATOM   4328  N   ALA B 344      29.871  28.902   3.749  1.00 34.39           N  
ANISOU 4328  N   ALA B 344     3554   4590   4924    825  -1349   -709       N  
ATOM   4329  CA  ALA B 344      28.651  28.333   4.327  1.00 37.24           C  
ANISOU 4329  CA  ALA B 344     3589   5076   5485    826  -1318   -893       C  
ATOM   4330  C   ALA B 344      28.857  26.897   4.802  1.00 39.53           C  
ANISOU 4330  C   ALA B 344     3768   5436   5817    602  -1114   -929       C  
ATOM   4331  O   ALA B 344      28.404  26.525   5.893  1.00 34.55           O  
ANISOU 4331  O   ALA B 344     2960   4849   5317    531   -938  -1014       O  
ATOM   4332  CB  ALA B 344      27.515  28.379   3.307  1.00 42.24           C  
ANISOU 4332  CB  ALA B 344     4082   5793   6173    976  -1579  -1019       C  
ATOM   4333  N   ALA B 345      29.546  26.077   4.004  1.00 39.18           N  
ANISOU 4333  N   ALA B 345     3845   5389   5653    490  -1124   -865       N  
ATOM   4334  CA  ALA B 345      29.719  24.671   4.367  1.00 36.66           C  
ANISOU 4334  CA  ALA B 345     3446   5113   5372    292   -947   -901       C  
ATOM   4335  C   ALA B 345      30.735  24.460   5.492  1.00 32.44           C  
ANISOU 4335  C   ALA B 345     3023   4513   4791    185   -712   -797       C  
ATOM   4336  O   ALA B 345      30.698  23.413   6.139  1.00 33.36           O  
ANISOU 4336  O   ALA B 345     3066   4647   4961     48   -541   -834       O  
ATOM   4337  CB  ALA B 345      30.124  23.869   3.139  1.00 35.77           C  
ANISOU 4337  CB  ALA B 345     3432   5012   5146    226  -1040   -881       C  
ATOM   4338  N   ASP B 346      31.651  25.416   5.717  1.00 26.39           N  
ANISOU 4338  N   ASP B 346     2443   3664   3920    243   -708   -674       N  
ATOM   4339  CA  ASP B 346      32.558  25.401   6.862  1.00 34.42           C  
ANISOU 4339  CA  ASP B 346     3547   4632   4899    174   -521   -600       C  
ATOM   4340  C   ASP B 346      31.880  25.830   8.158  1.00 36.60           C  
ANISOU 4340  C   ASP B 346     3699   4920   5287    212   -412   -670       C  
ATOM   4341  O   ASP B 346      32.323  25.419   9.233  1.00 38.19           O  
ANISOU 4341  O   ASP B 346     3928   5110   5472    135   -236   -648       O  
ATOM   4342  CB  ASP B 346      33.754  26.340   6.624  1.00 26.60           C  
ANISOU 4342  CB  ASP B 346     2778   3555   3774    209   -558   -472       C  
ATOM   4343  CG  ASP B 346      34.465  26.058   5.308  1.00 31.54           C  
ANISOU 4343  CG  ASP B 346     3544   4168   4272    173   -645   -402       C  
ATOM   4344  OD1 ASP B 346      34.884  24.879   5.120  1.00 23.98           O  
ANISOU 4344  OD1 ASP B 346     2582   3244   3284     65   -573   -403       O  
ATOM   4345  OD2 ASP B 346      34.564  26.994   4.457  1.00 29.97           O  
ANISOU 4345  OD2 ASP B 346     3473   3916   3997    257   -779   -350       O  
ATOM   4346  N   GLY B 347      30.820  26.644   8.068  1.00 32.71           N  
ANISOU 4346  N   GLY B 347     3079   4451   4897    345   -518   -761       N  
ATOM   4347  CA  GLY B 347      30.346  27.455   9.173  1.00 37.61           C  
ANISOU 4347  CA  GLY B 347     3628   5063   5598    425   -440   -817       C  
ATOM   4348  C   GLY B 347      31.100  28.780   9.282  1.00 34.85           C  
ANISOU 4348  C   GLY B 347     3475   4604   5162    527   -503   -725       C  
ATOM   4349  O   GLY B 347      32.292  28.856   8.968  1.00 33.77           O  
ANISOU 4349  O   GLY B 347     3536   4401   4893    469   -508   -603       O  
ATOM   4350  N  AARG B 348      30.405  29.823   9.726  0.58 32.86           N  
ANISOU 4350  N  AARG B 348     3164   4329   4994    672   -542   -797       N  
ATOM   4351  N  BARG B 348      30.431  29.839   9.719  0.42 33.81           N  
ANISOU 4351  N  BARG B 348     3289   4447   5111    673   -543   -794       N  
ATOM   4352  CA AARG B 348      31.005  31.141   9.869  0.58 39.50           C  
ANISOU 4352  CA AARG B 348     4194   5043   5771    769   -597   -728       C  
ATOM   4353  CA BARG B 348      31.125  31.113   9.841  0.42 38.84           C  
ANISOU 4353  CA BARG B 348     4129   4955   5675    757   -594   -715       C  
ATOM   4354  C  AARG B 348      31.724  31.334  11.195  0.58 38.67           C  
ANISOU 4354  C  AARG B 348     4164   4902   5625    700   -418   -711       C  
ATOM   4355  C  BARG B 348      31.798  31.298  11.192  0.42 38.44           C  
ANISOU 4355  C  BARG B 348     4144   4873   5589    691   -414   -704       C  
ATOM   4356  O  AARG B 348      32.518  32.271  11.317  0.58 41.67           O  
ANISOU 4356  O  AARG B 348     4726   5172   5935    725   -443   -646       O  
ATOM   4357  O  BARG B 348      32.638  32.192  11.329  0.42 41.34           O  
ANISOU 4357  O  BARG B 348     4694   5131   5882    707   -434   -637       O  
ATOM   4358  CB AARG B 348      29.935  32.233   9.722  0.58 41.44           C  
ANISOU 4358  CB AARG B 348     4364   5259   6123    985   -737   -820       C  
ATOM   4359  CB BARG B 348      30.169  32.288   9.594  0.42 42.21           C  
ANISOU 4359  CB BARG B 348     4512   5334   6190    975   -749   -789       C  
ATOM   4360  CG AARG B 348      29.629  32.637   8.282  0.58 45.06           C  
ANISOU 4360  CG AARG B 348     4893   5679   6550   1114   -986   -785       C  
ATOM   4361  CG BARG B 348      30.906  33.588   9.254  0.42 44.78           C  
ANISOU 4361  CG BARG B 348     5106   5486   6421   1059   -847   -684       C  
ATOM   4362  CD AARG B 348      30.839  33.301   7.578  0.58 46.52           C  
ANISOU 4362  CD AARG B 348     5403   5710   6563   1090  -1051   -613       C  
ATOM   4363  CD BARG B 348      30.509  34.093   7.889  0.42 48.79           C  
ANISOU 4363  CD BARG B 348     5704   5938   6897   1204  -1084   -646       C  
ATOM   4364  NE AARG B 348      30.411  34.190   6.494  0.58 52.31           N  
ANISOU 4364  NE AARG B 348     6266   6351   7260   1280  -1284   -581       N  
ATOM   4365  NE BARG B 348      29.087  34.424   7.878  0.42 51.25           N  
ANISOU 4365  NE BARG B 348     5811   6306   7357   1409  -1207   -792       N  
ATOM   4366  CZ AARG B 348      31.110  34.451   5.394  0.58 52.13           C  
ANISOU 4366  CZ AARG B 348     6498   6231   7078   1265  -1382   -443       C  
ATOM   4367  CZ BARG B 348      28.595  35.582   8.290  0.42 41.22           C  
ANISOU 4367  CZ BARG B 348     4563   4943   6157   1599  -1265   -849       C  
ATOM   4368  NH1AARG B 348      32.285  33.875   5.200  0.58 60.14           N  
ANISOU 4368  NH1AARG B 348     7632   7243   7974   1063  -1262   -341       N  
ATOM   4369  NH1BARG B 348      29.416  36.521   8.730  0.42 35.35           N  
ANISOU 4369  NH1BARG B 348     4056   4032   5343   1592  -1207   -766       N  
ATOM   4370  NH2AARG B 348      30.623  35.277   4.478  0.58 44.83           N  
ANISOU 4370  NH2AARG B 348     5715   5211   6107   1460  -1598   -413       N  
ATOM   4371  NH2BARG B 348      27.287  35.792   8.260  0.42 41.68           N  
ANISOU 4371  NH2BARG B 348     4397   5075   6363   1796  -1380  -1004       N  
ATOM   4372  N   ASP B 349      31.457  30.493  12.190  1.00 33.70           N  
ANISOU 4372  N   ASP B 349     3414   4359   5032    613   -239   -772       N  
ATOM   4373  CA  ASP B 349      32.031  30.650  13.525  1.00 37.62           C  
ANISOU 4373  CA  ASP B 349     3988   4833   5471    570    -80   -771       C  
ATOM   4374  C   ASP B 349      33.349  29.879  13.589  1.00 35.36           C  
ANISOU 4374  C   ASP B 349     3844   4541   5050    429    -23   -660       C  
ATOM   4375  O   ASP B 349      33.353  28.648  13.615  1.00 30.13           O  
ANISOU 4375  O   ASP B 349     3134   3942   4373    327     61   -647       O  
ATOM   4376  CB  ASP B 349      31.049  30.182  14.600  1.00 34.80           C  
ANISOU 4376  CB  ASP B 349     3462   4563   5199    558     96   -890       C  
ATOM   4377  CG  ASP B 349      31.553  30.469  16.016  1.00 41.64           C  
ANISOU 4377  CG  ASP B 349     4433   5406   5981    542    248   -898       C  
ATOM   4378  OD1 ASP B 349      32.657  31.024  16.143  1.00 42.99           O  
ANISOU 4378  OD1 ASP B 349     4785   5501   6048    539    198   -825       O  
ATOM   4379  OD2 ASP B 349      30.843  30.165  17.000  1.00 47.54           O  
ANISOU 4379  OD2 ASP B 349     5086   6213   6765    528    421   -989       O  
ATOM   4380  N   THR B 350      34.464  30.600  13.603  1.00 31.93           N  
ANISOU 4380  N   THR B 350     3579   4026   4526    424    -69   -592       N  
ATOM   4381  CA  THR B 350      35.788  29.982  13.655  1.00 27.50           C  
ANISOU 4381  CA  THR B 350     3129   3469   3850    312    -33   -510       C  
ATOM   4382  C   THR B 350      36.292  29.768  15.078  1.00 28.98           C  
ANISOU 4382  C   THR B 350     3362   3680   3969    282     94   -534       C  
ATOM   4383  O   THR B 350      37.467  29.407  15.261  1.00 28.70           O  
ANISOU 4383  O   THR B 350     3417   3650   3839    218    103   -485       O  
ATOM   4384  CB  THR B 350      36.797  30.833  12.882  1.00 32.47           C  
ANISOU 4384  CB  THR B 350     3902   4012   4425    299   -138   -441       C  
ATOM   4385  OG1 THR B 350      36.738  32.188  13.358  1.00 38.12           O  
ANISOU 4385  OG1 THR B 350     4684   4634   5164    375   -165   -481       O  
ATOM   4386  CG2 THR B 350      36.478  30.809  11.399  1.00 33.18           C  
ANISOU 4386  CG2 THR B 350     3995   4083   4528    316   -257   -393       C  
ATOM   4387  N   SER B 351      35.423  29.917  16.079  1.00 28.40           N  
ANISOU 4387  N   SER B 351     3225   3630   3936    333    192   -617       N  
ATOM   4388  CA  SER B 351      35.880  29.918  17.465  1.00 30.96           C  
ANISOU 4388  CA  SER B 351     3631   3967   4167    327    299   -645       C  
ATOM   4389  C   SER B 351      36.528  28.596  17.850  1.00 32.16           C  
ANISOU 4389  C   SER B 351     3839   4168   4213    244    378   -586       C  
ATOM   4390  O   SER B 351      37.433  28.577  18.687  1.00 30.78           O  
ANISOU 4390  O   SER B 351     3778   3995   3921    242    395   -577       O  
ATOM   4391  CB  SER B 351      34.720  30.226  18.410  1.00 30.70           C  
ANISOU 4391  CB  SER B 351     3520   3958   4188    392    419   -751       C  
ATOM   4392  OG  SER B 351      34.207  31.533  18.162  1.00 44.34           O  
ANISOU 4392  OG  SER B 351     5214   5625   6009    500    334   -816       O  
ATOM   4393  N   TRP B 352      36.114  27.494  17.221  1.00 29.63           N  
ANISOU 4393  N   TRP B 352     3450   3879   3929    185    410   -551       N  
ATOM   4394  CA  TRP B 352      36.632  26.180  17.589  1.00 24.83           C  
ANISOU 4394  CA  TRP B 352     2917   3292   3226    119    492   -494       C  
ATOM   4395  C   TRP B 352      38.150  26.093  17.530  1.00 21.10           C  
ANISOU 4395  C   TRP B 352     2562   2810   2644    116    404   -434       C  
ATOM   4396  O   TRP B 352      38.740  25.243  18.205  1.00 30.37           O  
ANISOU 4396  O   TRP B 352     3835   3996   3710    109    457   -400       O  
ATOM   4397  CB  TRP B 352      36.023  25.106  16.692  1.00 24.45           C  
ANISOU 4397  CB  TRP B 352     2781   3257   3253     47    516   -475       C  
ATOM   4398  CG  TRP B 352      36.413  25.223  15.244  1.00 21.21           C  
ANISOU 4398  CG  TRP B 352     2338   2839   2883     36    362   -438       C  
ATOM   4399  CD1 TRP B 352      35.724  25.900  14.266  1.00 25.05           C  
ANISOU 4399  CD1 TRP B 352     2723   3324   3470     70    258   -471       C  
ATOM   4400  CD2 TRP B 352      37.546  24.627  14.598  1.00 21.73           C  
ANISOU 4400  CD2 TRP B 352     2482   2897   2877     -1    301   -368       C  
ATOM   4401  NE1 TRP B 352      36.344  25.733  13.046  1.00 23.02           N  
ANISOU 4401  NE1 TRP B 352     2499   3057   3191     45    145   -416       N  
ATOM   4402  CE2 TRP B 352      37.463  24.958  13.218  1.00 21.90           C  
ANISOU 4402  CE2 TRP B 352     2455   2915   2952     -6    180   -358       C  
ATOM   4403  CE3 TRP B 352      38.606  23.807  15.037  1.00 21.53           C  
ANISOU 4403  CE3 TRP B 352     2565   2870   2744    -17    333   -319       C  
ATOM   4404  CZ2 TRP B 352      38.416  24.530  12.288  1.00 19.19           C  
ANISOU 4404  CZ2 TRP B 352     2166   2570   2556    -43    117   -305       C  
ATOM   4405  CZ3 TRP B 352      39.545  23.357  14.098  1.00 19.80           C  
ANISOU 4405  CZ3 TRP B 352     2374   2654   2495    -42    258   -277       C  
ATOM   4406  CH2 TRP B 352      39.452  23.737  12.752  1.00 25.39           C  
ANISOU 4406  CH2 TRP B 352     3029   3362   3256    -64    164   -273       C  
ATOM   4407  N   ILE B 353      38.810  26.920  16.715  1.00 24.23           N  
ANISOU 4407  N   ILE B 353     2955   3186   3067    121    275   -424       N  
ATOM   4408  CA  ILE B 353      40.262  26.833  16.670  1.00 24.68           C  
ANISOU 4408  CA  ILE B 353     3086   3251   3040    104    208   -395       C  
ATOM   4409  C   ILE B 353      40.899  27.130  18.019  1.00 25.57           C  
ANISOU 4409  C   ILE B 353     3284   3381   3052    148    224   -437       C  
ATOM   4410  O   ILE B 353      42.042  26.734  18.238  1.00 23.99           O  
ANISOU 4410  O   ILE B 353     3132   3211   2771    151    178   -429       O  
ATOM   4411  CB  ILE B 353      40.860  27.753  15.593  1.00 26.34           C  
ANISOU 4411  CB  ILE B 353     3286   3428   3295     75    101   -385       C  
ATOM   4412  CG1 ILE B 353      40.676  29.228  15.987  1.00 20.18           C  
ANISOU 4412  CG1 ILE B 353     2529   2590   2549    111     69   -440       C  
ATOM   4413  CG2 ILE B 353      40.329  27.340  14.202  1.00 22.07           C  
ANISOU 4413  CG2 ILE B 353     2690   2879   2816     43     69   -339       C  
ATOM   4414  CD1 ILE B 353      41.308  30.220  14.984  1.00 21.91           C  
ANISOU 4414  CD1 ILE B 353     2783   2741   2800     68    -16   -423       C  
ATOM   4415  N   TYR B 354      40.187  27.802  18.943  1.00 21.19           N  
ANISOU 4415  N   TYR B 354     2745   2813   2494    194    280   -496       N  
ATOM   4416  CA  TYR B 354      40.737  28.023  20.279  1.00 25.78           C  
ANISOU 4416  CA  TYR B 354     3428   3416   2953    242    293   -545       C  
ATOM   4417  C   TYR B 354      40.589  26.789  21.164  1.00 26.95           C  
ANISOU 4417  C   TYR B 354     3668   3595   2978    265    397   -508       C  
ATOM   4418  O   TYR B 354      41.262  26.694  22.196  1.00 24.04           O  
ANISOU 4418  O   TYR B 354     3416   3251   2467    319    381   -530       O  
ATOM   4419  CB  TYR B 354      40.115  29.306  20.936  1.00 25.63           C  
ANISOU 4419  CB  TYR B 354     3413   3362   2963    288    315   -636       C  
ATOM   4420  CG  TYR B 354      40.802  30.540  20.344  1.00 23.19           C  
ANISOU 4420  CG  TYR B 354     3091   2999   2720    268    192   -672       C  
ATOM   4421  CD1 TYR B 354      41.974  31.049  20.911  1.00 22.94           C  
ANISOU 4421  CD1 TYR B 354     3122   2976   2617    261    116   -732       C  
ATOM   4422  CD2 TYR B 354      40.353  31.105  19.149  1.00 22.40           C  
ANISOU 4422  CD2 TYR B 354     2927   2836   2747    247    148   -645       C  
ATOM   4423  CE1 TYR B 354      42.644  32.115  20.334  1.00 29.63           C  
ANISOU 4423  CE1 TYR B 354     3963   3761   3534    207     29   -768       C  
ATOM   4424  CE2 TYR B 354      41.024  32.181  18.565  1.00 22.39           C  
ANISOU 4424  CE2 TYR B 354     2956   2761   2792    211     57   -660       C  
ATOM   4425  CZ  TYR B 354      42.173  32.658  19.150  1.00 22.72           C  
ANISOU 4425  CZ  TYR B 354     3053   2804   2776    176     12   -721       C  
ATOM   4426  OH  TYR B 354      42.851  33.687  18.562  1.00 25.22           O  
ANISOU 4426  OH  TYR B 354     3401   3035   3146    108    -51   -742       O  
ATOM   4427  N   ASP B 355      39.803  25.807  20.747  1.00 23.64           N  
ANISOU 4427  N   ASP B 355     3215   3165   2601    223    493   -453       N  
ATOM   4428  CA  ASP B 355      39.789  24.524  21.434  1.00 28.31           C  
ANISOU 4428  CA  ASP B 355     3929   3754   3074    226    597   -398       C  
ATOM   4429  C   ASP B 355      40.766  23.516  20.839  1.00 35.73           C  
ANISOU 4429  C   ASP B 355     4908   4691   3976    223    519   -328       C  
ATOM   4430  O   ASP B 355      40.962  22.442  21.420  1.00 35.03           O  
ANISOU 4430  O   ASP B 355     4959   4579   3770    250    578   -274       O  
ATOM   4431  CB  ASP B 355      38.378  23.944  21.423  1.00 39.45           C  
ANISOU 4431  CB  ASP B 355     5291   5143   4557    161    775   -393       C  
ATOM   4432  N   ALA B 356      41.341  23.799  19.677  1.00 29.96           N  
ANISOU 4432  N   ALA B 356     4073   3973   3338    195    400   -328       N  
ATOM   4433  CA  ALA B 356      42.401  22.956  19.161  1.00 27.03           C  
ANISOU 4433  CA  ALA B 356     3728   3612   2930    208    324   -287       C  
ATOM   4434  C   ALA B 356      43.703  23.248  19.898  1.00 29.53           C  
ANISOU 4434  C   ALA B 356     4105   3977   3137    292    214   -326       C  
ATOM   4435  O   ALA B 356      43.951  24.373  20.342  1.00 31.06           O  
ANISOU 4435  O   ALA B 356     4278   4197   3328    305    160   -396       O  
ATOM   4436  CB  ALA B 356      42.589  23.194  17.667  1.00 25.38           C  
ANISOU 4436  CB  ALA B 356     3391   3409   2842    143    254   -283       C  
ATOM   4437  N   ASP B 357      44.572  22.249  19.948  1.00 24.76           N  
ANISOU 4437  N   ASP B 357     3566   3384   2456    353    165   -297       N  
ATOM   4438  CA  ASP B 357      45.831  22.329  20.711  1.00 27.78           C  
ANISOU 4438  CA  ASP B 357     3999   3828   2727    460     40   -350       C  
ATOM   4439  C   ASP B 357      46.988  22.794  19.814  1.00 27.44           C  
ANISOU 4439  C   ASP B 357     3800   3851   2774    433    -82   -416       C  
ATOM   4440  O   ASP B 357      47.943  22.071  19.533  1.00 28.99           O  
ANISOU 4440  O   ASP B 357     3976   4085   2952    492   -154   -426       O  
ATOM   4441  CB  ASP B 357      46.114  20.972  21.351  1.00 37.44           C  
ANISOU 4441  CB  ASP B 357     5396   5021   3809    573     46   -288       C  
ATOM   4442  CG  ASP B 357      47.269  20.996  22.330  1.00 53.97           C  
ANISOU 4442  CG  ASP B 357     7565   7181   5759    723   -102   -348       C  
ATOM   4443  OD1 ASP B 357      47.806  22.081  22.640  1.00 58.26           O  
ANISOU 4443  OD1 ASP B 357     8023   7801   6314    724   -199   -451       O  
ATOM   4444  OD2 ASP B 357      47.652  19.897  22.791  1.00 62.69           O  
ANISOU 4444  OD2 ASP B 357     8825   8255   6738    847   -130   -297       O  
ATOM   4445  N   PHE B 358      46.907  24.054  19.376  1.00 24.81           N  
ANISOU 4445  N   PHE B 358     3360   3526   2540    341    -95   -469       N  
ATOM   4446  CA  PHE B 358      47.962  24.607  18.526  1.00 23.01           C  
ANISOU 4446  CA  PHE B 358     2996   3348   2397    280   -173   -534       C  
ATOM   4447  C   PHE B 358      49.270  24.787  19.291  1.00 26.93           C  
ANISOU 4447  C   PHE B 358     3461   3936   2835    352   -298   -645       C  
ATOM   4448  O   PHE B 358      50.335  24.775  18.677  1.00 25.20           O  
ANISOU 4448  O   PHE B 358     3119   3781   2673    326   -356   -709       O  
ATOM   4449  CB  PHE B 358      47.511  25.937  17.904  1.00 25.96           C  
ANISOU 4449  CB  PHE B 358     3310   3677   2878    162   -145   -552       C  
ATOM   4450  CG  PHE B 358      46.576  25.764  16.703  1.00 27.02           C  
ANISOU 4450  CG  PHE B 358     3426   3749   3093     92    -71   -465       C  
ATOM   4451  CD1 PHE B 358      47.084  25.480  15.452  1.00 26.74           C  
ANISOU 4451  CD1 PHE B 358     3327   3726   3108     29    -75   -446       C  
ATOM   4452  CD2 PHE B 358      45.215  25.875  16.837  1.00 21.82           C  
ANISOU 4452  CD2 PHE B 358     2807   3031   2453     95     -3   -420       C  
ATOM   4453  CE1 PHE B 358      46.240  25.318  14.357  1.00 32.86           C  
ANISOU 4453  CE1 PHE B 358     4099   4451   3934    -24    -30   -377       C  
ATOM   4454  CE2 PHE B 358      44.367  25.726  15.744  1.00 25.72           C  
ANISOU 4454  CE2 PHE B 358     3267   3483   3021     44     34   -363       C  
ATOM   4455  CZ  PHE B 358      44.885  25.433  14.508  1.00 30.19           C  
ANISOU 4455  CZ  PHE B 358     3792   4060   3620    -11     11   -339       C  
ATOM   4456  N   GLU B 359      49.203  24.895  20.620  1.00 22.95           N  
ANISOU 4456  N   GLU B 359     3062   3447   2212    448   -339   -680       N  
ATOM   4457  CA  GLU B 359      50.401  24.998  21.443  1.00 26.03           C  
ANISOU 4457  CA  GLU B 359     3428   3935   2527    543   -488   -801       C  
ATOM   4458  C   GLU B 359      51.358  23.829  21.225  1.00 29.19           C  
ANISOU 4458  C   GLU B 359     3795   4400   2896    653   -572   -805       C  
ATOM   4459  O   GLU B 359      52.578  24.015  21.279  1.00 30.83           O  
ANISOU 4459  O   GLU B 359     3871   4713   3130    687   -700   -936       O  
ATOM   4460  CB  GLU B 359      49.994  25.103  22.929  1.00 29.24           C  
ANISOU 4460  CB  GLU B 359     4008   4337   2766    652   -511   -815       C  
ATOM   4461  CG  GLU B 359      49.317  26.475  23.343  1.00 29.54           C  
ANISOU 4461  CG  GLU B 359     4058   4333   2833    567   -462   -870       C  
ATOM   4462  CD  GLU B 359      47.845  26.654  22.880  1.00 39.20           C  
ANISOU 4462  CD  GLU B 359     5319   5450   4125    485   -290   -765       C  
ATOM   4463  OE1 GLU B 359      47.189  25.682  22.410  1.00 41.93           O  
ANISOU 4463  OE1 GLU B 359     5701   5753   4476    486   -195   -647       O  
ATOM   4464  OE2 GLU B 359      47.342  27.799  22.988  1.00 40.68           O  
ANISOU 4464  OE2 GLU B 359     5492   5596   4370    423   -256   -816       O  
ATOM   4465  N   LYS B 360      50.840  22.629  20.932  1.00 28.73           N  
ANISOU 4465  N   LYS B 360     3840   4276   2799    706   -499   -681       N  
ATOM   4466  CA  LYS B 360      51.716  21.460  20.804  1.00 32.18           C  
ANISOU 4466  CA  LYS B 360     4277   4754   3197    843   -582   -686       C  
ATOM   4467  C   LYS B 360      52.712  21.624  19.666  1.00 31.04           C  
ANISOU 4467  C   LYS B 360     3902   4690   3200    774   -618   -777       C  
ATOM   4468  O   LYS B 360      53.727  20.925  19.635  1.00 33.07           O  
ANISOU 4468  O   LYS B 360     4097   5020   3447    899   -720   -842       O  
ATOM   4469  CB  LYS B 360      50.889  20.175  20.593  1.00 25.95           C  
ANISOU 4469  CB  LYS B 360     3656   3847   2356    882   -472   -535       C  
ATOM   4470  CG  LYS B 360      50.569  19.928  19.118  1.00 35.98           C  
ANISOU 4470  CG  LYS B 360     4819   5079   3772    749   -370   -491       C  
ATOM   4471  CD  LYS B 360      49.227  19.179  18.875  1.00 46.56           C  
ANISOU 4471  CD  LYS B 360     6299   6287   5104    692   -217   -357       C  
ATOM   4472  CE  LYS B 360      49.098  17.894  19.668  1.00 50.16           C  
ANISOU 4472  CE  LYS B 360     6980   6658   5420    832   -202   -279       C  
ATOM   4473  NZ  LYS B 360      47.855  17.132  19.291  1.00 48.61           N  
ANISOU 4473  NZ  LYS B 360     6890   6332   5248    738    -35   -172       N  
ATOM   4474  N   LEU B 361      52.462  22.553  18.744  1.00 25.36           N  
ANISOU 4474  N   LEU B 361     3064   3959   2612    585   -533   -788       N  
ATOM   4475  CA  LEU B 361      53.392  22.767  17.641  1.00 29.93           C  
ANISOU 4475  CA  LEU B 361     3445   4610   3318    493   -531   -872       C  
ATOM   4476  C   LEU B 361      54.768  23.204  18.136  1.00 35.87           C  
ANISOU 4476  C   LEU B 361     4034   5501   4094    537   -668  -1056       C  
ATOM   4477  O   LEU B 361      55.765  22.983  17.445  1.00 36.12           O  
ANISOU 4477  O   LEU B 361     3892   5622   4211    522   -684  -1150       O  
ATOM   4478  CB  LEU B 361      52.807  23.806  16.676  1.00 31.11           C  
ANISOU 4478  CB  LEU B 361     3553   4698   3571    285   -414   -836       C  
ATOM   4479  CG  LEU B 361      52.107  23.460  15.336  1.00 32.07           C  
ANISOU 4479  CG  LEU B 361     3696   4746   3744    190   -293   -727       C  
ATOM   4480  CD1 LEU B 361      51.885  21.992  15.053  1.00 29.29           C  
ANISOU 4480  CD1 LEU B 361     3413   4369   3348    292   -274   -653       C  
ATOM   4481  CD2 LEU B 361      50.849  24.301  15.034  1.00 24.66           C  
ANISOU 4481  CD2 LEU B 361     2837   3701   2831     81   -214   -639       C  
ATOM   4482  N   SER B 362      54.851  23.803  19.327  1.00 30.68           N  
ANISOU 4482  N   SER B 362     3418   4874   3365    591   -768  -1126       N  
ATOM   4483  CA  SER B 362      56.146  24.174  19.868  1.00 39.81           C  
ANISOU 4483  CA  SER B 362     4408   6175   4544    642   -924  -1326       C  
ATOM   4484  C   SER B 362      57.039  22.968  20.116  1.00 41.67           C  
ANISOU 4484  C   SER B 362     4601   6507   4726    864  -1060  -1381       C  
ATOM   4485  O   SER B 362      58.251  23.137  20.271  1.00 48.10           O  
ANISOU 4485  O   SER B 362     5209   7468   5600    908  -1190  -1572       O  
ATOM   4486  CB  SER B 362      55.963  24.974  21.157  1.00 43.84           C  
ANISOU 4486  CB  SER B 362     5006   6692   4961    675  -1017  -1391       C  
ATOM   4487  OG  SER B 362      55.432  26.258  20.860  1.00 47.08           O  
ANISOU 4487  OG  SER B 362     5403   7027   5458    468   -911  -1394       O  
ATOM   4488  N   LYS B 363      56.484  21.759  20.149  1.00 36.80           N  
ANISOU 4488  N   LYS B 363     4168   5807   4008   1006  -1035  -1232       N  
ATOM   4489  CA  LYS B 363      57.309  20.579  20.392  1.00 41.15           C  
ANISOU 4489  CA  LYS B 363     4715   6421   4501   1245  -1171  -1276       C  
ATOM   4490  C   LYS B 363      57.849  19.955  19.116  1.00 34.33           C  
ANISOU 4490  C   LYS B 363     3690   5586   3768   1217  -1103  -1301       C  
ATOM   4491  O   LYS B 363      58.509  18.917  19.184  1.00 45.99           O  
ANISOU 4491  O   LYS B 363     5160   7101   5214   1425  -1205  -1339       O  
ATOM   4492  CB  LYS B 363      56.514  19.543  21.178  1.00 44.12           C  
ANISOU 4492  CB  LYS B 363     5411   6669   4685   1425  -1179  -1108       C  
ATOM   4493  CG  LYS B 363      55.965  20.112  22.466  1.00 51.00           C  
ANISOU 4493  CG  LYS B 363     6463   7514   5402   1459  -1225  -1084       C  
ATOM   4494  CD  LYS B 363      55.043  19.136  23.161  1.00 58.67           C  
ANISOU 4494  CD  LYS B 363     7773   8337   6181   1586  -1169   -901       C  
ATOM   4495  CE  LYS B 363      54.551  19.728  24.472  1.00 66.27           C  
ANISOU 4495  CE  LYS B 363     8919   9288   6972   1621  -1201   -893       C  
ATOM   4496  NZ  LYS B 363      53.823  18.699  25.264  1.00 71.20           N  
ANISOU 4496  NZ  LYS B 363     9896   9775   7383   1762  -1147   -726       N  
ATOM   4497  N   GLN B 364      57.577  20.545  17.964  1.00 35.60           N  
ANISOU 4497  N   GLN B 364     3743   5722   4060    980   -936  -1281       N  
ATOM   4498  CA  GLN B 364      58.000  20.002  16.684  1.00 36.86           C  
ANISOU 4498  CA  GLN B 364     3775   5905   4326    933   -843  -1301       C  
ATOM   4499  C   GLN B 364      59.051  20.899  16.045  1.00 39.00           C  
ANISOU 4499  C   GLN B 364     3750   6316   4751    775   -816  -1487       C  
ATOM   4500  O   GLN B 364      59.186  22.077  16.359  1.00 36.21           O  
ANISOU 4500  O   GLN B 364     3317   5999   4443    635   -823  -1564       O  
ATOM   4501  CB  GLN B 364      56.816  19.850  15.721  1.00 35.13           C  
ANISOU 4501  CB  GLN B 364     3694   5539   4114    785   -657  -1123       C  
ATOM   4502  CG  GLN B 364      55.665  18.998  16.251  1.00 36.53           C  
ANISOU 4502  CG  GLN B 364     4147   5567   4164    887   -639   -947       C  
ATOM   4503  CD  GLN B 364      54.565  18.805  15.216  1.00 32.85           C  
ANISOU 4503  CD  GLN B 364     3770   4982   3731    740   -474   -811       C  
ATOM   4504  OE1 GLN B 364      54.797  18.972  14.025  1.00 30.72           O  
ANISOU 4504  OE1 GLN B 364     3384   4739   3550    618   -390   -840       O  
ATOM   4505  NE2 GLN B 364      53.362  18.471  15.670  1.00 27.66           N  
ANISOU 4505  NE2 GLN B 364     3316   4197   2995    747   -423   -674       N  
ATOM   4506  N   GLN B 365      59.771  20.307  15.110  1.00 41.29           N  
ANISOU 4506  N   GLN B 365     3890   6675   5125    787   -765  -1560       N  
ATOM   4507  CA  GLN B 365      60.837  20.949  14.354  1.00 42.95           C  
ANISOU 4507  CA  GLN B 365     3809   7023   5488    631   -696  -1745       C  
ATOM   4508  C   GLN B 365      60.196  21.534  13.098  1.00 38.29           C  
ANISOU 4508  C   GLN B 365     3272   6336   4940    365   -470  -1635       C  
ATOM   4509  O   GLN B 365      59.928  20.813  12.131  1.00 35.22           O  
ANISOU 4509  O   GLN B 365     2941   5898   4542    363   -362  -1556       O  
ATOM   4510  CB  GLN B 365      61.888  19.885  14.054  1.00 48.52           C  
ANISOU 4510  CB  GLN B 365     4343   7851   6243    818   -756  -1882       C  
ATOM   4511  CG  GLN B 365      63.217  20.286  13.516  1.00 52.21           C  
ANISOU 4511  CG  GLN B 365     4460   8505   6872    727   -718  -2127       C  
ATOM   4512  CD  GLN B 365      64.110  19.045  13.232  1.00 60.61           C  
ANISOU 4512  CD  GLN B 365     5379   9675   7976    966   -782  -2252       C  
ATOM   4513  OE1 GLN B 365      63.680  17.887  13.372  1.00 59.09           O  
ANISOU 4513  OE1 GLN B 365     5384   9386   7682   1190   -846  -2133       O  
ATOM   4514  NE2 GLN B 365      65.347  19.298  12.831  1.00 59.34           N  
ANISOU 4514  NE2 GLN B 365     4969   9640   7938    889   -730  -2455       N  
ATOM   4515  N   ILE B 366      59.894  22.831  13.112  1.00 39.06           N  
ANISOU 4515  N   ILE B 366     3379   6391   5070    153   -405  -1625       N  
ATOM   4516  CA  ILE B 366      59.070  23.430  12.066  1.00 36.98           C  
ANISOU 4516  CA  ILE B 366     3241   6002   4809    -62   -223  -1485       C  
ATOM   4517  C   ILE B 366      59.781  24.628  11.458  1.00 36.64           C  
ANISOU 4517  C   ILE B 366     3045   6001   4876   -316   -100  -1602       C  
ATOM   4518  O   ILE B 366      60.111  25.582  12.171  1.00 46.40           O  
ANISOU 4518  O   ILE B 366     4208   7260   6160   -394   -153  -1702       O  
ATOM   4519  CB  ILE B 366      57.698  23.867  12.605  1.00 37.47           C  
ANISOU 4519  CB  ILE B 366     3542   5910   4784    -69   -244  -1313       C  
ATOM   4520  CG1 ILE B 366      56.919  22.666  13.131  1.00 39.69           C  
ANISOU 4520  CG1 ILE B 366     3991   6132   4959    143   -320  -1190       C  
ATOM   4521  CG2 ILE B 366      56.916  24.660  11.533  1.00 27.55           C  
ANISOU 4521  CG2 ILE B 366     2399   4531   3539   -278    -86  -1192       C  
ATOM   4522  CD1 ILE B 366      55.579  23.043  13.801  1.00 34.81           C  
ANISOU 4522  CD1 ILE B 366     3580   5383   4262    145   -330  -1047       C  
ATOM   4523  N   GLU B 367      59.937  24.620  10.129  1.00 36.59           N  
ANISOU 4523  N   GLU B 367     3021   5983   4897   -461     79  -1580       N  
ATOM   4524  CA  GLU B 367      60.622  25.720   9.442  1.00 39.79           C  
ANISOU 4524  CA  GLU B 367     3315   6408   5396   -729    240  -1677       C  
ATOM   4525  C   GLU B 367      59.760  26.967   9.358  1.00 37.43           C  
ANISOU 4525  C   GLU B 367     3216   5937   5069   -904    302  -1549       C  
ATOM   4526  O   GLU B 367      60.276  28.085   9.388  1.00 47.48           O  
ANISOU 4526  O   GLU B 367     4421   7199   6422  -1102    373  -1645       O  
ATOM   4527  CB  GLU B 367      60.988  25.341   8.014  1.00 49.11           C  
ANISOU 4527  CB  GLU B 367     4464   7615   6581   -832    434  -1677       C  
ATOM   4528  CG  GLU B 367      61.582  24.004   7.785  1.00 62.83           C  
ANISOU 4528  CG  GLU B 367     6067   9480   8327   -650    406  -1762       C  
ATOM   4529  CD  GLU B 367      62.088  23.911   6.372  1.00 65.36           C  
ANISOU 4529  CD  GLU B 367     6335   9838   8661   -803    633  -1801       C  
ATOM   4530  OE1 GLU B 367      62.663  24.911   5.902  1.00 66.94           O  
ANISOU 4530  OE1 GLU B 367     6454  10054   8926  -1051    796  -1881       O  
ATOM   4531  OE2 GLU B 367      61.890  22.869   5.724  1.00 65.49           O  
ANISOU 4531  OE2 GLU B 367     6413   9855   8617   -689    661  -1751       O  
ATOM   4532  N   ALA B 368      58.464  26.795   9.141  1.00 37.70           N  
ANISOU 4532  N   ALA B 368     3495   5830   4999   -845    291  -1343       N  
ATOM   4533  CA  ALA B 368      57.558  27.892   8.833  1.00 36.12           C  
ANISOU 4533  CA  ALA B 368     3501   5457   4766   -982    353  -1209       C  
ATOM   4534  C   ALA B 368      56.150  27.331   8.839  1.00 34.21           C  
ANISOU 4534  C   ALA B 368     3462   5114   4423   -838    286  -1023       C  
ATOM   4535  O   ALA B 368      55.960  26.138   8.598  1.00 31.88           O  
ANISOU 4535  O   ALA B 368     3168   4863   4083   -706    261   -984       O  
ATOM   4536  CB  ALA B 368      57.877  28.516   7.473  1.00 36.83           C  
ANISOU 4536  CB  ALA B 368     3641   5492   4861  -1209    557  -1187       C  
ATOM   4537  N   ILE B 369      55.175  28.187   9.145  1.00 26.78           N  
ANISOU 4537  N   ILE B 369     2680   4036   3458   -862    258   -924       N  
ATOM   4538  CA  ILE B 369      53.764  27.861   9.012  1.00 24.90           C  
ANISOU 4538  CA  ILE B 369     2617   3698   3145   -761    216   -762       C  
ATOM   4539  C   ILE B 369      53.157  28.886   8.077  1.00 26.48           C  
ANISOU 4539  C   ILE B 369     2985   3753   3322   -892    295   -659       C  
ATOM   4540  O   ILE B 369      53.221  30.087   8.353  1.00 28.45           O  
ANISOU 4540  O   ILE B 369     3283   3917   3610   -991    312   -679       O  
ATOM   4541  CB  ILE B 369      53.039  27.853  10.364  1.00 29.25           C  
ANISOU 4541  CB  ILE B 369     3203   4227   3684   -623     94   -749       C  
ATOM   4542  CG1 ILE B 369      53.724  26.885  11.320  1.00 27.09           C  
ANISOU 4542  CG1 ILE B 369     2803   4084   3406   -482      5   -846       C  
ATOM   4543  CG2 ILE B 369      51.564  27.495  10.195  1.00 22.92           C  
ANISOU 4543  CG2 ILE B 369     2546   3335   2827   -537     72   -604       C  
ATOM   4544  CD1 ILE B 369      53.233  27.017  12.731  1.00 27.90           C  
ANISOU 4544  CD1 ILE B 369     2952   4173   3475   -366    -99   -854       C  
ATOM   4545  N   ILE B 370      52.597  28.423   6.964  1.00 24.41           N  
ANISOU 4545  N   ILE B 370     2826   3456   2993   -888    337   -555       N  
ATOM   4546  CA  ILE B 370      51.829  29.263   6.048  1.00 28.72           C  
ANISOU 4546  CA  ILE B 370     3570   3859   3485   -959    375   -436       C  
ATOM   4547  C   ILE B 370      50.359  29.123   6.412  1.00 27.60           C  
ANISOU 4547  C   ILE B 370     3518   3648   3319   -815    259   -341       C  
ATOM   4548  O   ILE B 370      49.851  27.998   6.512  1.00 27.91           O  
ANISOU 4548  O   ILE B 370     3515   3748   3340   -701    208   -324       O  
ATOM   4549  CB  ILE B 370      52.065  28.847   4.589  1.00 31.32           C  
ANISOU 4549  CB  ILE B 370     3967   4200   3733  -1030    475   -391       C  
ATOM   4550  CG1 ILE B 370      53.570  28.818   4.312  1.00 36.55           C  
ANISOU 4550  CG1 ILE B 370     4492   4962   4435  -1168    612   -515       C  
ATOM   4551  CG2 ILE B 370      51.293  29.783   3.641  1.00 29.45           C  
ANISOU 4551  CG2 ILE B 370     3973   3805   3413  -1086    494   -261       C  
ATOM   4552  CD1 ILE B 370      53.937  28.383   2.956  1.00 38.85           C  
ANISOU 4552  CD1 ILE B 370     4838   5283   4642  -1243    738   -495       C  
ATOM   4553  N   VAL B 371      49.683  30.242   6.659  1.00 28.66           N  
ANISOU 4553  N   VAL B 371     3767   3656   3467   -819    224   -295       N  
ATOM   4554  CA  VAL B 371      48.259  30.230   7.001  1.00 21.50           C  
ANISOU 4554  CA  VAL B 371     2921   2691   2557   -682    124   -228       C  
ATOM   4555  C   VAL B 371      47.500  30.823   5.826  1.00 28.49           C  
ANISOU 4555  C   VAL B 371     3987   3458   3380   -690    110   -121       C  
ATOM   4556  O   VAL B 371      47.985  31.753   5.174  1.00 24.19           O  
ANISOU 4556  O   VAL B 371     3570   2817   2804   -803    175    -92       O  
ATOM   4557  CB  VAL B 371      47.960  30.964   8.324  1.00 28.84           C  
ANISOU 4557  CB  VAL B 371     3831   3577   3549   -633     73   -276       C  
ATOM   4558  CG1 VAL B 371      48.605  30.195   9.481  1.00 29.11           C  
ANISOU 4558  CG1 VAL B 371     3710   3740   3609   -589     59   -374       C  
ATOM   4559  CG2 VAL B 371      48.449  32.442   8.323  1.00 22.84           C  
ANISOU 4559  CG2 VAL B 371     3167   2692   2818   -750    114   -298       C  
ATOM   4560  N   THR B 372      46.341  30.243   5.511  1.00 21.53           N  
ANISOU 4560  N   THR B 372     3123   2584   2474   -574     28    -69       N  
ATOM   4561  CA  THR B 372      45.656  30.594   4.291  1.00 22.33           C  
ANISOU 4561  CA  THR B 372     3386   2602   2495   -555    -15     21       C  
ATOM   4562  C   THR B 372      44.152  30.406   4.473  1.00 25.57           C  
ANISOU 4562  C   THR B 372     3776   3003   2936   -401   -144     39       C  
ATOM   4563  O   THR B 372      43.668  30.127   5.572  1.00 24.69           O  
ANISOU 4563  O   THR B 372     3539   2933   2908   -331   -169    -13       O  
ATOM   4564  CB  THR B 372      46.228  29.799   3.105  1.00 23.39           C  
ANISOU 4564  CB  THR B 372     3551   2802   2533   -624     46     39       C  
ATOM   4565  OG1 THR B 372      45.655  30.299   1.898  1.00 32.16           O  
ANISOU 4565  OG1 THR B 372     4863   3821   3535   -608      0    130       O  
ATOM   4566  CG2 THR B 372      45.949  28.324   3.194  1.00 22.53           C  
ANISOU 4566  CG2 THR B 372     3306   2818   2438   -558     18     -2       C  
ATOM   4567  N   GLY B 373      43.412  30.611   3.380  1.00 25.78           N  
ANISOU 4567  N   GLY B 373     3931   2974   2889   -347   -224    105       N  
ATOM   4568  CA  GLY B 373      41.960  30.652   3.416  1.00 24.67           C  
ANISOU 4568  CA  GLY B 373     3766   2820   2787   -197   -363    104       C  
ATOM   4569  C   GLY B 373      41.453  32.028   3.800  1.00 30.37           C  
ANISOU 4569  C   GLY B 373     4585   3404   3549   -120   -422    125       C  
ATOM   4570  O   GLY B 373      42.224  32.946   4.096  1.00 25.50           O  
ANISOU 4570  O   GLY B 373     4066   2691   2932   -197   -350    141       O  
ATOM   4571  N   THR B 374      40.122  32.170   3.797  1.00 24.58           N  
ANISOU 4571  N   THR B 374     3816   2662   2863     36   -556    110       N  
ATOM   4572  CA  THR B 374      39.503  33.479   4.012  1.00 28.90           C  
ANISOU 4572  CA  THR B 374     4470   3067   3445    151   -637    125       C  
ATOM   4573  C   THR B 374      39.686  33.984   5.435  1.00 32.87           C  
ANISOU 4573  C   THR B 374     4890   3544   4056    142   -563     59       C  
ATOM   4574  O   THR B 374      39.587  35.194   5.664  1.00 33.49           O  
ANISOU 4574  O   THR B 374     5096   3475   4154    193   -587     71       O  
ATOM   4575  CB  THR B 374      38.000  33.459   3.704  1.00 26.86           C  
ANISOU 4575  CB  THR B 374     4149   2829   3229    344   -810     93       C  
ATOM   4576  OG1 THR B 374      37.361  32.415   4.434  1.00 28.34           O  
ANISOU 4576  OG1 THR B 374     4074   3169   3526    361   -793     -7       O  
ATOM   4577  CG2 THR B 374      37.733  33.249   2.218  1.00 38.01           C  
ANISOU 4577  CG2 THR B 374     5696   4237   4509    387   -929    157       C  
ATOM   4578  N   ARG B 375      39.943  33.100   6.397  1.00 26.44           N  
ANISOU 4578  N   ARG B 375     3888   2858   3301     88   -477    -12       N  
ATOM   4579  CA  ARG B 375      40.209  33.519   7.765  1.00 24.91           C  
ANISOU 4579  CA  ARG B 375     3634   2653   3179     77   -408    -79       C  
ATOM   4580  C   ARG B 375      41.646  33.182   8.160  1.00 22.69           C  
ANISOU 4580  C   ARG B 375     3336   2420   2864    -79   -294    -93       C  
ATOM   4581  O   ARG B 375      41.925  32.810   9.298  1.00 24.18           O  
ANISOU 4581  O   ARG B 375     3416   2682   3088    -92   -241   -162       O  
ATOM   4582  CB  ARG B 375      39.182  32.897   8.717  1.00 25.21           C  
ANISOU 4582  CB  ARG B 375     3485   2791   3304    173   -410   -160       C  
ATOM   4583  CG  ARG B 375      37.784  33.222   8.305  1.00 26.20           C  
ANISOU 4583  CG  ARG B 375     3581   2891   3484    328   -527   -177       C  
ATOM   4584  CD  ARG B 375      37.603  34.753   8.333  1.00 33.02           C  
ANISOU 4584  CD  ARG B 375     4597   3584   4365    420   -588   -167       C  
ATOM   4585  NE  ARG B 375      37.773  35.283   9.690  1.00 31.78           N  
ANISOU 4585  NE  ARG B 375     4407   3401   4266    421   -508   -243       N  
ATOM   4586  CZ  ARG B 375      36.822  35.217  10.616  1.00 34.93           C  
ANISOU 4586  CZ  ARG B 375     4662   3857   4754    525   -493   -339       C  
ATOM   4587  NH1 ARG B 375      35.649  34.648  10.329  1.00 36.04           N  
ANISOU 4587  NH1 ARG B 375     4653   4085   4956    624   -549   -378       N  
ATOM   4588  NH2 ARG B 375      37.031  35.712  11.821  1.00 36.09           N  
ANISOU 4588  NH2 ARG B 375     4807   3977   4927    525   -417   -410       N  
ATOM   4589  N   ALA B 376      42.571  33.304   7.206  1.00 23.04           N  
ANISOU 4589  N   ALA B 376     3491   2429   2834   -194   -257    -36       N  
ATOM   4590  CA  ALA B 376      43.987  33.059   7.481  1.00 24.13           C  
ANISOU 4590  CA  ALA B 376     3589   2622   2957   -341   -152    -72       C  
ATOM   4591  C   ALA B 376      44.502  33.892   8.657  1.00 31.27           C  
ANISOU 4591  C   ALA B 376     4481   3479   3921   -377   -119   -150       C  
ATOM   4592  O   ALA B 376      45.300  33.405   9.465  1.00 27.86           O  
ANISOU 4592  O   ALA B 376     3931   3149   3506   -427    -75   -226       O  
ATOM   4593  CB  ALA B 376      44.810  33.363   6.234  1.00 25.71           C  
ANISOU 4593  CB  ALA B 376     3928   2763   3076   -467    -95     -9       C  
ATOM   4594  N   GLU B 377      44.053  35.155   8.762  1.00 24.11           N  
ANISOU 4594  N   GLU B 377     3705   2413   3042   -340   -152   -141       N  
ATOM   4595  CA  GLU B 377      44.456  36.013   9.873  1.00 24.64           C  
ANISOU 4595  CA  GLU B 377     3776   2420   3166   -370   -127   -230       C  
ATOM   4596  C   GLU B 377      43.979  35.489  11.227  1.00 23.74           C  
ANISOU 4596  C   GLU B 377     3514   2417   3090   -267   -147   -316       C  
ATOM   4597  O   GLU B 377      44.663  35.708  12.231  1.00 28.03           O  
ANISOU 4597  O   GLU B 377     4013   2989   3650   -315   -121   -411       O  
ATOM   4598  CB  GLU B 377      43.942  37.453   9.655  1.00 26.26           C  
ANISOU 4598  CB  GLU B 377     4179   2406   3393   -329   -163   -201       C  
ATOM   4599  CG  GLU B 377      44.510  38.164   8.394  1.00 29.89           C  
ANISOU 4599  CG  GLU B 377     4852   2709   3794   -451   -119   -107       C  
ATOM   4600  CD  GLU B 377      43.834  37.694   7.080  1.00 47.21           C  
ANISOU 4600  CD  GLU B 377     7129   4907   5903   -372   -179     15       C  
ATOM   4601  OE1 GLU B 377      42.947  36.788   7.102  1.00 41.94           O  
ANISOU 4601  OE1 GLU B 377     6327   4368   5240   -237   -258     15       O  
ATOM   4602  OE2 GLU B 377      44.183  38.246   6.020  1.00 48.72           O  
ANISOU 4602  OE2 GLU B 377     7531   4967   6015   -451   -145    107       O  
ATOM   4603  N   GLU B 378      42.804  34.835  11.298  1.00 23.93           N  
ANISOU 4603  N   GLU B 378     3466   2502   3123   -132   -190   -296       N  
ATOM   4604  CA  GLU B 378      42.395  34.218  12.564  1.00 26.62           C  
ANISOU 4604  CA  GLU B 378     3684   2951   3481    -58   -171   -369       C  
ATOM   4605  C   GLU B 378      43.411  33.163  13.005  1.00 29.36           C  
ANISOU 4605  C   GLU B 378     3941   3435   3780   -131   -126   -396       C  
ATOM   4606  O   GLU B 378      43.670  33.000  14.203  1.00 25.52           O  
ANISOU 4606  O   GLU B 378     3412   3008   3277   -109   -108   -470       O  
ATOM   4607  CB  GLU B 378      41.014  33.560  12.463  1.00 22.83           C  
ANISOU 4607  CB  GLU B 378     3122   2522   3029     62   -194   -351       C  
ATOM   4608  CG  GLU B 378      39.843  34.442  12.487  1.00 33.30           C  
ANISOU 4608  CG  GLU B 378     4475   3757   4419    188   -245   -371       C  
ATOM   4609  CD  GLU B 378      39.766  35.351  13.720  1.00 44.31           C  
ANISOU 4609  CD  GLU B 378     5897   5093   5844    236   -217   -465       C  
ATOM   4610  OE1 GLU B 378      40.098  34.908  14.855  1.00 45.22           O  
ANISOU 4610  OE1 GLU B 378     5956   5295   5930    215   -152   -529       O  
ATOM   4611  OE2 GLU B 378      39.361  36.522  13.528  1.00 38.60           O  
ANISOU 4611  OE2 GLU B 378     5274   4228   5166    307   -268   -475       O  
ATOM   4612  N   LEU B 379      43.988  32.443  12.039  1.00 27.13           N  
ANISOU 4612  N   LEU B 379     3641   3204   3465   -203   -115   -341       N  
ATOM   4613  CA  LEU B 379      44.997  31.433  12.324  1.00 29.39           C  
ANISOU 4613  CA  LEU B 379     3842   3612   3712   -250    -85   -370       C  
ATOM   4614  C   LEU B 379      46.300  32.071  12.756  1.00 26.75           C  
ANISOU 4614  C   LEU B 379     3502   3280   3383   -345    -73   -452       C  
ATOM   4615  O   LEU B 379      46.963  31.582  13.674  1.00 25.81           O  
ANISOU 4615  O   LEU B 379     3308   3256   3241   -328    -82   -526       O  
ATOM   4616  CB  LEU B 379      45.247  30.567  11.094  1.00 23.88           C  
ANISOU 4616  CB  LEU B 379     3130   2958   2985   -296    -70   -306       C  
ATOM   4617  CG  LEU B 379      44.149  29.600  10.671  1.00 31.54           C  
ANISOU 4617  CG  LEU B 379     4073   3961   3951   -222    -85   -252       C  
ATOM   4618  CD1 LEU B 379      44.561  28.989   9.355  1.00 25.56           C  
ANISOU 4618  CD1 LEU B 379     3329   3228   3153   -282    -75   -204       C  
ATOM   4619  CD2 LEU B 379      43.901  28.526  11.741  1.00 25.73           C  
ANISOU 4619  CD2 LEU B 379     3263   3308   3206   -157    -61   -283       C  
ATOM   4620  N   GLN B 380      46.715  33.132  12.070  1.00 22.51           N  
ANISOU 4620  N   GLN B 380     3045   2635   2871   -449    -54   -445       N  
ATOM   4621  CA  GLN B 380      47.907  33.826  12.522  1.00 23.01           C  
ANISOU 4621  CA  GLN B 380     3087   2693   2962   -564    -33   -548       C  
ATOM   4622  C   GLN B 380      47.747  34.220  13.976  1.00 24.09           C  
ANISOU 4622  C   GLN B 380     3207   2838   3108   -493    -78   -647       C  
ATOM   4623  O   GLN B 380      48.634  33.991  14.802  1.00 23.59           O  
ANISOU 4623  O   GLN B 380     3054   2874   3036   -511   -101   -755       O  
ATOM   4624  CB  GLN B 380      48.175  35.053  11.665  1.00 25.40           C  
ANISOU 4624  CB  GLN B 380     3522   2834   3295   -695     15   -522       C  
ATOM   4625  CG  GLN B 380      49.299  35.888  12.253  1.00 26.53           C  
ANISOU 4625  CG  GLN B 380     3636   2954   3490   -834     44   -654       C  
ATOM   4626  CD  GLN B 380      49.726  36.961  11.328  1.00 34.41           C  
ANISOU 4626  CD  GLN B 380     4774   3786   4514  -1004    129   -625       C  
ATOM   4627  OE1 GLN B 380      50.851  36.954  10.844  1.00 33.40           O  
ANISOU 4627  OE1 GLN B 380     4587   3698   4405  -1173    214   -674       O  
ATOM   4628  NE2 GLN B 380      48.821  37.902  11.053  1.00 34.88           N  
ANISOU 4628  NE2 GLN B 380     5029   3650   4572   -958    113   -546       N  
ATOM   4629  N   LEU B 381      46.591  34.795  14.315  1.00 26.83           N  
ANISOU 4629  N   LEU B 381     3639   3088   3468   -397    -98   -623       N  
ATOM   4630  CA  LEU B 381      46.403  35.282  15.671  1.00 24.82           C  
ANISOU 4630  CA  LEU B 381     3392   2829   3211   -332   -125   -725       C  
ATOM   4631  C   LEU B 381      46.334  34.115  16.657  1.00 23.14           C  
ANISOU 4631  C   LEU B 381     3094   2772   2926   -231   -139   -753       C  
ATOM   4632  O   LEU B 381      46.910  34.187  17.742  1.00 23.93           O  
ANISOU 4632  O   LEU B 381     3174   2933   2987   -218   -172   -860       O  
ATOM   4633  CB  LEU B 381      45.158  36.176  15.720  1.00 24.41           C  
ANISOU 4633  CB  LEU B 381     3444   2633   3197   -241   -130   -702       C  
ATOM   4634  CG  LEU B 381      44.668  36.600  17.092  1.00 24.97           C  
ANISOU 4634  CG  LEU B 381     3530   2701   3257   -144   -140   -804       C  
ATOM   4635  CD1 LEU B 381      45.765  37.377  17.825  1.00 26.11           C  
ANISOU 4635  CD1 LEU B 381     3695   2821   3403   -240   -159   -940       C  
ATOM   4636  CD2 LEU B 381      43.361  37.395  17.007  1.00 25.60           C  
ANISOU 4636  CD2 LEU B 381     3688   2649   3390    -31   -141   -786       C  
ATOM   4637  N   ARG B 382      45.661  33.018  16.284  1.00 22.09           N  
ANISOU 4637  N   ARG B 382     2926   2699   2767   -164   -119   -660       N  
ATOM   4638  CA  ARG B 382      45.624  31.826  17.145  1.00 21.59           C  
ANISOU 4638  CA  ARG B 382     2821   2758   2625    -80   -115   -667       C  
ATOM   4639  C   ARG B 382      47.032  31.307  17.456  1.00 21.82           C  
ANISOU 4639  C   ARG B 382     2790   2892   2607   -112   -159   -731       C  
ATOM   4640  O   ARG B 382      47.351  30.990  18.606  1.00 22.27           O  
ANISOU 4640  O   ARG B 382     2855   3021   2587    -40   -195   -797       O  
ATOM   4641  CB  ARG B 382      44.788  30.720  16.479  1.00 20.64           C  
ANISOU 4641  CB  ARG B 382     2676   2663   2503    -41    -75   -561       C  
ATOM   4642  CG  ARG B 382      44.826  29.369  17.213  1.00 22.09           C  
ANISOU 4642  CG  ARG B 382     2849   2943   2603     27    -52   -549       C  
ATOM   4643  CD  ARG B 382      44.099  29.429  18.555  1.00 20.89           C  
ANISOU 4643  CD  ARG B 382     2752   2794   2391    112    -12   -587       C  
ATOM   4644  NE  ARG B 382      44.189  28.186  19.314  1.00 22.96           N  
ANISOU 4644  NE  ARG B 382     3055   3121   2546    174     19   -563       N  
ATOM   4645  CZ  ARG B 382      44.979  27.994  20.359  1.00 26.62           C  
ANISOU 4645  CZ  ARG B 382     3576   3641   2898    232    -26   -617       C  
ATOM   4646  NH1 ARG B 382      45.809  28.955  20.754  1.00 22.30           N  
ANISOU 4646  NH1 ARG B 382     3019   3108   2346    219   -109   -718       N  
ATOM   4647  NH2 ARG B 382      44.966  26.823  20.992  1.00 24.11           N  
ANISOU 4647  NH2 ARG B 382     3336   3357   2467    304      5   -574       N  
ATOM   4648  N   LEU B 383      47.891  31.239  16.442  1.00 23.84           N  
ANISOU 4648  N   LEU B 383     2989   3164   2907   -211   -159   -721       N  
ATOM   4649  CA  LEU B 383      49.279  30.833  16.632  1.00 27.41           C  
ANISOU 4649  CA  LEU B 383     3345   3726   3344   -242   -204   -809       C  
ATOM   4650  C   LEU B 383      50.071  31.831  17.478  1.00 27.38           C  
ANISOU 4650  C   LEU B 383     3318   3729   3357   -290   -259   -959       C  
ATOM   4651  O   LEU B 383      50.925  31.418  18.273  1.00 30.17           O  
ANISOU 4651  O   LEU B 383     3602   4198   3664   -239   -337  -1061       O  
ATOM   4652  CB  LEU B 383      49.948  30.664  15.271  1.00 27.71           C  
ANISOU 4652  CB  LEU B 383     3319   3773   3436   -355   -159   -779       C  
ATOM   4653  CG  LEU B 383      49.365  29.476  14.499  1.00 33.50           C  
ANISOU 4653  CG  LEU B 383     4062   4526   4140   -299   -125   -661       C  
ATOM   4654  CD1 LEU B 383      49.684  29.561  12.997  1.00 23.25           C  
ANISOU 4654  CD1 LEU B 383     2754   3200   2880   -416    -63   -613       C  
ATOM   4655  CD2 LEU B 383      49.887  28.161  15.145  1.00 25.82           C  
ANISOU 4655  CD2 LEU B 383     3034   3673   3105   -186   -170   -689       C  
ATOM   4656  N   LYS B 384      49.862  33.145  17.281  1.00 24.26           N  
ANISOU 4656  N   LYS B 384     2982   3207   3027   -386   -230   -985       N  
ATOM   4657  CA  LYS B 384      50.457  34.122  18.208  1.00 25.70           C  
ANISOU 4657  CA  LYS B 384     3161   3377   3226   -432   -283  -1143       C  
ATOM   4658  C   LYS B 384      50.050  33.826  19.646  1.00 25.86           C  
ANISOU 4658  C   LYS B 384     3226   3459   3140   -276   -349  -1195       C  
ATOM   4659  O   LYS B 384      50.888  33.802  20.554  1.00 26.93           O  
ANISOU 4659  O   LYS B 384     3310   3693   3229   -252   -439  -1333       O  
ATOM   4660  CB  LYS B 384      50.049  35.551  17.839  1.00 28.52           C  
ANISOU 4660  CB  LYS B 384     3627   3548   3663   -534   -233  -1145       C  
ATOM   4661  CG  LYS B 384      50.528  36.634  18.850  1.00 33.34           C  
ANISOU 4661  CG  LYS B 384     4256   4117   4294   -585   -283  -1321       C  
ATOM   4662  CD  LYS B 384      50.199  38.046  18.368  1.00 29.04           C  
ANISOU 4662  CD  LYS B 384     3844   3353   3837   -696   -223  -1318       C  
ATOM   4663  CE  LYS B 384      50.724  39.119  19.345  1.00 30.89           C  
ANISOU 4663  CE  LYS B 384     4101   3532   4102   -766   -268  -1511       C  
ATOM   4664  NZ  LYS B 384      50.403  40.487  18.853  1.00 38.88           N  
ANISOU 4664  NZ  LYS B 384     5273   4296   5202   -871   -204  -1502       N  
ATOM   4665  N   LEU B 385      48.751  33.615  19.878  1.00 25.06           N  
ANISOU 4665  N   LEU B 385     3222   3305   2993   -169   -302  -1097       N  
ATOM   4666  CA  LEU B 385      48.280  33.366  21.236  1.00 26.36           C  
ANISOU 4666  CA  LEU B 385     3458   3518   3041    -34   -327  -1140       C  
ATOM   4667  C   LEU B 385      48.741  32.011  21.771  1.00 32.31           C  
ANISOU 4667  C   LEU B 385     4190   4412   3675     70   -376  -1124       C  
ATOM   4668  O   LEU B 385      48.826  31.841  22.993  1.00 36.31           O  
ANISOU 4668  O   LEU B 385     4764   4978   4055    172   -428  -1192       O  
ATOM   4669  CB  LEU B 385      46.758  33.474  21.288  1.00 25.80           C  
ANISOU 4669  CB  LEU B 385     3472   3361   2970     38   -237  -1053       C  
ATOM   4670  CG  LEU B 385      46.287  34.888  21.711  1.00 30.17           C  
ANISOU 4670  CG  LEU B 385     4100   3794   3571     28   -227  -1141       C  
ATOM   4671  CD1 LEU B 385      46.973  35.968  20.894  1.00 33.95           C  
ANISOU 4671  CD1 LEU B 385     4566   4166   4167   -117   -250  -1183       C  
ATOM   4672  CD2 LEU B 385      44.814  35.031  21.580  1.00 25.60           C  
ANISOU 4672  CD2 LEU B 385     3565   3137   3024    105   -143  -1070       C  
ATOM   4673  N   ALA B 386      49.043  31.061  20.882  1.00 28.04           N  
ANISOU 4673  N   ALA B 386     3579   3915   3160     56   -363  -1038       N  
ATOM   4674  CA  ALA B 386      49.596  29.759  21.241  1.00 30.33           C  
ANISOU 4674  CA  ALA B 386     3856   4317   3351    161   -417  -1021       C  
ATOM   4675  C   ALA B 386      51.074  29.821  21.567  1.00 35.88           C  
ANISOU 4675  C   ALA B 386     4451   5133   4048    162   -549  -1169       C  
ATOM   4676  O   ALA B 386      51.632  28.800  21.972  1.00 33.19           O  
ANISOU 4676  O   ALA B 386     4105   4888   3617    283   -627  -1176       O  
ATOM   4677  CB  ALA B 386      49.383  28.755  20.092  1.00 23.23           C  
ANISOU 4677  CB  ALA B 386     2918   3412   2496    145   -353   -892       C  
ATOM   4678  N   GLU B 387      51.718  30.985  21.369  1.00 28.52           N  
ANISOU 4678  N   GLU B 387     3432   4185   3218     29   -575  -1294       N  
ATOM   4679  CA  GLU B 387      53.144  31.157  21.594  1.00 28.06           C  
ANISOU 4679  CA  GLU B 387     3225   4244   3192     -5   -693  -1470       C  
ATOM   4680  C   GLU B 387      53.964  30.203  20.725  1.00 33.54           C  
ANISOU 4680  C   GLU B 387     3776   5032   3937     -6   -700  -1453       C  
ATOM   4681  O   GLU B 387      54.957  29.627  21.171  1.00 31.98           O  
ANISOU 4681  O   GLU B 387     3475   4973   3704     88   -825  -1563       O  
ATOM   4682  CB  GLU B 387      53.492  30.985  23.074  1.00 35.44           C  
ANISOU 4682  CB  GLU B 387     4210   5276   3980    149   -842  -1587       C  
ATOM   4683  CG  GLU B 387      52.691  31.904  23.990  1.00 38.61           C  
ANISOU 4683  CG  GLU B 387     4762   5592   4316    159   -826  -1620       C  
ATOM   4684  CD  GLU B 387      53.127  31.812  25.444  1.00 49.30           C  
ANISOU 4684  CD  GLU B 387     6181   7049   5502    305   -983  -1755       C  
ATOM   4685  OE1 GLU B 387      52.550  31.010  26.205  1.00 52.88           O  
ANISOU 4685  OE1 GLU B 387     6797   7518   5777    472   -985  -1667       O  
ATOM   4686  OE2 GLU B 387      54.058  32.537  25.828  1.00 49.53           O  
ANISOU 4686  OE2 GLU B 387     6108   7141   5572    248  -1102  -1955       O  
ATOM   4687  N   VAL B 388      53.530  30.000  19.485  1.00 29.68           N  
ANISOU 4687  N   VAL B 388     3285   4471   3520    -92   -573  -1322       N  
ATOM   4688  CA  VAL B 388      54.274  29.178  18.543  1.00 34.43           C  
ANISOU 4688  CA  VAL B 388     3757   5150   4175   -108   -554  -1314       C  
ATOM   4689  C   VAL B 388      55.246  30.082  17.793  1.00 44.65           C  
ANISOU 4689  C   VAL B 388     4894   6461   5610   -313   -509  -1437       C  
ATOM   4690  O   VAL B 388      54.843  30.836  16.909  1.00 41.83           O  
ANISOU 4690  O   VAL B 388     4588   5984   5322   -471   -387  -1370       O  
ATOM   4691  CB  VAL B 388      53.331  28.435  17.593  1.00 33.67           C  
ANISOU 4691  CB  VAL B 388     3750   4976   4068    -97   -444  -1124       C  
ATOM   4692  CG1 VAL B 388      54.135  27.695  16.549  1.00 30.19           C  
ANISOU 4692  CG1 VAL B 388     3181   4608   3682   -128   -410  -1134       C  
ATOM   4693  CG2 VAL B 388      52.433  27.475  18.394  1.00 25.81           C  
ANISOU 4693  CG2 VAL B 388     2901   3964   2942     82   -467  -1021       C  
ATOM   4694  N   GLU B 389      56.535  29.987  18.131  1.00 45.79           N  
ANISOU 4694  N   GLU B 389     4850   6752   5797   -309   -604  -1623       N  
ATOM   4695  CA  GLU B 389      57.540  30.982  17.736  1.00 47.57           C  
ANISOU 4695  CA  GLU B 389     4906   7004   6164   -524   -563  -1793       C  
ATOM   4696  C   GLU B 389      58.318  30.495  16.516  1.00 51.12           C  
ANISOU 4696  C   GLU B 389     5193   7525   6704   -618   -461  -1811       C  
ATOM   4697  O   GLU B 389      59.481  30.100  16.590  1.00 53.37           O  
ANISOU 4697  O   GLU B 389     5254   7976   7050   -597   -524  -1982       O  
ATOM   4698  CB  GLU B 389      58.496  31.260  18.892  1.00 50.80           C  
ANISOU 4698  CB  GLU B 389     5171   7549   6580   -476   -736  -2030       C  
ATOM   4699  CG  GLU B 389      57.818  31.519  20.197  1.00 62.31           C  
ANISOU 4699  CG  GLU B 389     6796   8969   7910   -341   -853  -2026       C  
ATOM   4700  CD  GLU B 389      57.512  32.977  20.385  1.00 73.51           C  
ANISOU 4700  CD  GLU B 389     8289  10252   9388   -518   -799  -2084       C  
ATOM   4701  OE1 GLU B 389      58.474  33.756  20.564  1.00 80.35           O  
ANISOU 4701  OE1 GLU B 389     8999  11170  10360   -663   -838  -2297       O  
ATOM   4702  OE2 GLU B 389      56.319  33.343  20.336  1.00 72.81           O  
ANISOU 4702  OE2 GLU B 389     8407  10004   9253   -514   -715  -1928       O  
ATOM   4703  N   VAL B 390      57.634  30.514  15.379  1.00 38.51           N  
ANISOU 4703  N   VAL B 390     3715   5807   5111   -710   -304  -1639       N  
ATOM   4704  CA  VAL B 390      58.248  30.168  14.104  1.00 41.91           C  
ANISOU 4704  CA  VAL B 390     4036   6279   5607   -822   -171  -1640       C  
ATOM   4705  C   VAL B 390      57.724  31.121  13.053  1.00 36.31           C  
ANISOU 4705  C   VAL B 390     3475   5397   4926  -1034      3  -1525       C  
ATOM   4706  O   VAL B 390      56.655  31.720  13.217  1.00 40.10           O  
ANISOU 4706  O   VAL B 390     4155   5721   5359  -1027      3  -1401       O  
ATOM   4707  CB  VAL B 390      57.945  28.696  13.692  1.00 43.62           C  
ANISOU 4707  CB  VAL B 390     4277   6548   5747   -640   -184  -1525       C  
ATOM   4708  CG1 VAL B 390      58.218  27.720  14.845  1.00 45.62           C  
ANISOU 4708  CG1 VAL B 390     4475   6923   5935   -388   -371  -1592       C  
ATOM   4709  CG2 VAL B 390      56.537  28.546  13.220  1.00 32.53           C  
ANISOU 4709  CG2 VAL B 390     3109   4991   4261   -610   -124  -1300       C  
ATOM   4710  N   PRO B 391      58.493  31.347  11.997  1.00 32.42           N  
ANISOU 4710  N   PRO B 391     2889   4922   4506  -1223    156  -1575       N  
ATOM   4711  CA  PRO B 391      58.012  32.221  10.919  1.00 35.26           C  
ANISOU 4711  CA  PRO B 391     3436   5101   4862  -1415    326  -1447       C  
ATOM   4712  C   PRO B 391      56.591  31.853  10.503  1.00 35.19           C  
ANISOU 4712  C   PRO B 391     3664   4969   4737  -1285    311  -1214       C  
ATOM   4713  O   PRO B 391      56.289  30.694  10.213  1.00 33.04           O  
ANISOU 4713  O   PRO B 391     3384   4767   4403  -1141    282  -1141       O  
ATOM   4714  CB  PRO B 391      59.019  31.968   9.790  1.00 39.24           C  
ANISOU 4714  CB  PRO B 391     3805   5689   5417  -1572    496  -1515       C  
ATOM   4715  CG  PRO B 391      60.301  31.554  10.510  1.00 40.73           C  
ANISOU 4715  CG  PRO B 391     3672   6095   5708  -1543    418  -1765       C  
ATOM   4716  CD  PRO B 391      59.840  30.800  11.730  1.00 39.39           C  
ANISOU 4716  CD  PRO B 391     3499   5995   5474  -1260    186  -1757       C  
ATOM   4717  N   ILE B 392      55.699  32.841  10.512  1.00 33.51           N  
ANISOU 4717  N   ILE B 392     3657   4571   4503  -1328    321  -1112       N  
ATOM   4718  CA  ILE B 392      54.312  32.648  10.093  1.00 37.07           C  
ANISOU 4718  CA  ILE B 392     4313   4907   4864  -1213    299   -916       C  
ATOM   4719  C   ILE B 392      54.054  33.538   8.890  1.00 34.36           C  
ANISOU 4719  C   ILE B 392     4163   4394   4500  -1369    427   -808       C  
ATOM   4720  O   ILE B 392      54.338  34.741   8.931  1.00 38.94           O  
ANISOU 4720  O   ILE B 392     4819   4848   5130  -1523    488   -847       O  
ATOM   4721  CB  ILE B 392      53.327  32.944  11.237  1.00 36.81           C  
ANISOU 4721  CB  ILE B 392     4360   4812   4813  -1068    174   -891       C  
ATOM   4722  CG1 ILE B 392      53.461  31.857  12.297  1.00 40.28           C  
ANISOU 4722  CG1 ILE B 392     4666   5412   5227   -892     57   -957       C  
ATOM   4723  CG2 ILE B 392      51.884  33.040  10.718  1.00 28.71           C  
ANISOU 4723  CG2 ILE B 392     3530   3653   3727   -982    165   -714       C  
ATOM   4724  CD1 ILE B 392      52.936  32.273  13.619  1.00 49.06           C  
ANISOU 4724  CD1 ILE B 392     5822   6495   6323   -792    -42   -997       C  
ATOM   4725  N   ILE B 393      53.542  32.946   7.816  1.00 31.91           N  
ANISOU 4725  N   ILE B 393     3949   4069   4107  -1331    467   -676       N  
ATOM   4726  CA  ILE B 393      53.357  33.632   6.539  1.00 34.87           C  
ANISOU 4726  CA  ILE B 393     4533   4295   4422  -1461    585   -563       C  
ATOM   4727  C   ILE B 393      51.880  33.610   6.177  1.00 36.29           C  
ANISOU 4727  C   ILE B 393     4907   4364   4516  -1307    492   -397       C  
ATOM   4728  O   ILE B 393      51.286  32.534   6.034  1.00 35.44           O  
ANISOU 4728  O   ILE B 393     4757   4346   4363  -1164    421   -350       O  
ATOM   4729  CB  ILE B 393      54.198  32.986   5.432  1.00 37.87           C  
ANISOU 4729  CB  ILE B 393     4854   4771   4762  -1567    725   -578       C  
ATOM   4730  CG1 ILE B 393      55.675  33.285   5.694  1.00 37.74           C  
ANISOU 4730  CG1 ILE B 393     4641   4847   4853  -1753    841   -762       C  
ATOM   4731  CG2 ILE B 393      53.754  33.484   4.046  1.00 35.11           C  
ANISOU 4731  CG2 ILE B 393     4778   4270   4294  -1650    826   -425       C  
ATOM   4732  CD1 ILE B 393      56.598  32.229   5.174  1.00 41.47           C  
ANISOU 4732  CD1 ILE B 393     4918   5507   5330  -1771    924   -853       C  
ATOM   4733  N   VAL B 394      51.296  34.792   6.004  1.00 28.64           N  
ANISOU 4733  N   VAL B 394     4150   3198   3534  -1337    489   -320       N  
ATOM   4734  CA  VAL B 394      49.883  34.930   5.668  1.00 30.35           C  
ANISOU 4734  CA  VAL B 394     4541   3306   3685  -1178    383   -184       C  
ATOM   4735  C   VAL B 394      49.772  35.017   4.157  1.00 39.57           C  
ANISOU 4735  C   VAL B 394     5912   4392   4729  -1234    450    -61       C  
ATOM   4736  O   VAL B 394      50.283  35.957   3.535  1.00 34.58           O  
ANISOU 4736  O   VAL B 394     5459   3618   4063  -1393    568    -25       O  
ATOM   4737  CB  VAL B 394      49.260  36.173   6.324  1.00 35.10           C  
ANISOU 4737  CB  VAL B 394     5274   3729   4335  -1138    323   -176       C  
ATOM   4738  CG1 VAL B 394      47.822  36.369   5.824  1.00 30.11           C  
ANISOU 4738  CG1 VAL B 394     4814   2987   3641   -962    209    -46       C  
ATOM   4739  CG2 VAL B 394      49.315  36.056   7.853  1.00 30.15           C  
ANISOU 4739  CG2 VAL B 394     4463   3191   3803  -1070    254   -304       C  
ATOM   4740  N   GLU B 395      49.083  34.056   3.560  1.00 27.15           N  
ANISOU 4740  N   GLU B 395     4336   2900   3081  -1109    379      4       N  
ATOM   4741  CA  GLU B 395      48.872  34.066   2.117  1.00 33.51           C  
ANISOU 4741  CA  GLU B 395     5351   3641   3741  -1133    415    118       C  
ATOM   4742  C   GLU B 395      47.443  33.568   1.920  1.00 30.34           C  
ANISOU 4742  C   GLU B 395     4982   3250   3297   -919    236    186       C  
ATOM   4743  O   GLU B 395      47.205  32.361   1.943  1.00 26.53           O  
ANISOU 4743  O   GLU B 395     4345   2917   2818   -844    190    151       O  
ATOM   4744  CB  GLU B 395      49.906  33.190   1.406  1.00 31.33           C  
ANISOU 4744  CB  GLU B 395     4987   3504   3414  -1254    555     73       C  
ATOM   4745  CG  GLU B 395      49.665  32.983  -0.080  1.00 34.29           C  
ANISOU 4745  CG  GLU B 395     5573   3844   3612  -1263    589    178       C  
ATOM   4746  CD  GLU B 395      49.335  34.305  -0.789  1.00 40.24           C  
ANISOU 4746  CD  GLU B 395     6664   4367   4257  -1308    610    307       C  
ATOM   4747  OE1 GLU B 395      50.270  35.021  -1.215  1.00 42.21           O  
ANISOU 4747  OE1 GLU B 395     7039   4527   4470  -1512    799    315       O  
ATOM   4748  OE2 GLU B 395      48.137  34.628  -0.898  1.00 41.97           O  
ANISOU 4748  OE2 GLU B 395     7023   4490   4433  -1138    439    395       O  
ATOM   4749  N   ARG B 396      46.495  34.495   1.740  1.00 28.12           N  
ANISOU 4749  N   ARG B 396     4893   2805   2985   -820    134    270       N  
ATOM   4750  CA  ARG B 396      45.078  34.117   1.732  1.00 35.54           C  
ANISOU 4750  CA  ARG B 396     5810   3768   3924   -608    -51    297       C  
ATOM   4751  C   ARG B 396      44.697  33.234   0.533  1.00 34.86           C  
ANISOU 4751  C   ARG B 396     5776   3759   3710   -560   -102    346       C  
ATOM   4752  O   ARG B 396      43.708  32.503   0.605  1.00 26.72           O  
ANISOU 4752  O   ARG B 396     4632   2814   2706   -420   -234    321       O  
ATOM   4753  CB  ARG B 396      44.195  35.379   1.762  1.00 32.50           C  
ANISOU 4753  CB  ARG B 396     5620   3189   3540   -491   -159    361       C  
ATOM   4754  CG  ARG B 396      44.274  36.175   3.078  1.00 34.06           C  
ANISOU 4754  CG  ARG B 396     5749   3316   3878   -493   -144    291       C  
ATOM   4755  CD  ARG B 396      43.593  37.568   2.931  1.00 39.34           C  
ANISOU 4755  CD  ARG B 396     6667   3748   4533   -392   -226    359       C  
ATOM   4756  NE  ARG B 396      42.210  37.426   2.497  1.00 35.79           N  
ANISOU 4756  NE  ARG B 396     6245   3299   4054   -162   -415    399       N  
ATOM   4757  CZ  ARG B 396      41.201  37.134   3.313  1.00 39.49           C  
ANISOU 4757  CZ  ARG B 396     6516   3851   4637      3   -526    320       C  
ATOM   4758  NH1 ARG B 396      41.424  36.965   4.613  1.00 33.71           N  
ANISOU 4758  NH1 ARG B 396     5584   3196   4030    -33   -461    216       N  
ATOM   4759  NH2 ARG B 396      39.967  37.003   2.832  1.00 39.21           N  
ANISOU 4759  NH2 ARG B 396     6480   3830   4587    203   -699    335       N  
ATOM   4760  N   ASP B 397      45.422  33.323  -0.584  1.00 35.65           N  
ANISOU 4760  N   ASP B 397     6054   3824   3666   -680      4    405       N  
ATOM   4761  CA  ASP B 397      45.114  32.528  -1.770  1.00 29.18           C  
ANISOU 4761  CA  ASP B 397     5313   3075   2700   -639    -42    442       C  
ATOM   4762  C   ASP B 397      45.614  31.100  -1.539  1.00 27.54           C  
ANISOU 4762  C   ASP B 397     4854   3065   2546   -682     21    341       C  
ATOM   4763  O   ASP B 397      46.819  30.864  -1.462  1.00 36.12           O  
ANISOU 4763  O   ASP B 397     5867   4208   3648   -830    191    291       O  
ATOM   4764  CB  ASP B 397      45.760  33.152  -3.006  1.00 39.73           C  
ANISOU 4764  CB  ASP B 397     6954   4297   3843   -759     77    540       C  
ATOM   4765  CG  ASP B 397      45.439  32.387  -4.308  1.00 41.10           C  
ANISOU 4765  CG  ASP B 397     7249   4538   3828   -709     23    577       C  
ATOM   4766  OD1 ASP B 397      45.510  31.146  -4.340  1.00 37.02           O  
ANISOU 4766  OD1 ASP B 397     6539   4191   3337   -702     23    493       O  
ATOM   4767  OD2 ASP B 397      45.123  33.036  -5.324  1.00 47.14           O  
ANISOU 4767  OD2 ASP B 397     8330   5176   4405   -672    -22    689       O  
ATOM   4768  N   ILE B 398      44.692  30.143  -1.477  1.00 31.64           N  
ANISOU 4768  N   ILE B 398     5245   3681   3096   -553   -114    302       N  
ATOM   4769  CA  ILE B 398      45.061  28.776  -1.111  1.00 30.37           C  
ANISOU 4769  CA  ILE B 398     4862   3676   3002   -575    -65    207       C  
ATOM   4770  C   ILE B 398      46.003  28.163  -2.145  1.00 31.37           C  
ANISOU 4770  C   ILE B 398     5052   3865   3004   -681     63    197       C  
ATOM   4771  O   ILE B 398      46.934  27.437  -1.788  1.00 27.02           O  
ANISOU 4771  O   ILE B 398     4346   3410   2509   -750    179    118       O  
ATOM   4772  CB  ILE B 398      43.798  27.924  -0.911  1.00 29.71           C  
ANISOU 4772  CB  ILE B 398     4656   3656   2975   -437   -222    167       C  
ATOM   4773  CG1 ILE B 398      42.967  28.516   0.221  1.00 24.95           C  
ANISOU 4773  CG1 ILE B 398     3963   3009   2509   -344   -307    157       C  
ATOM   4774  CG2 ILE B 398      44.178  26.458  -0.593  1.00 27.67           C  
ANISOU 4774  CG2 ILE B 398     4215   3527   2773   -462   -162     80       C  
ATOM   4775  CD1 ILE B 398      41.575  27.934   0.343  1.00 26.24           C  
ANISOU 4775  CD1 ILE B 398     4015   3220   2736   -217   -455    113       C  
ATOM   4776  N   TYR B 399      45.799  28.459  -3.436  1.00 27.29           N  
ANISOU 4776  N   TYR B 399     4770   3294   2306   -685     44    269       N  
ATOM   4777  CA  TYR B 399      46.712  27.930  -4.447  1.00 32.75           C  
ANISOU 4777  CA  TYR B 399     5540   4044   2861   -793    191    253       C  
ATOM   4778  C   TYR B 399      48.126  28.491  -4.259  1.00 37.34           C  
ANISOU 4778  C   TYR B 399     6111   4611   3466   -971    418    236       C  
ATOM   4779  O   TYR B 399      49.116  27.750  -4.302  1.00 36.71           O  
ANISOU 4779  O   TYR B 399     5895   4642   3410  -1054    561    146       O  
ATOM   4780  CB  TYR B 399      46.209  28.238  -5.855  1.00 32.18           C  
ANISOU 4780  CB  TYR B 399     5763   3907   2558   -760    127    341       C  
ATOM   4781  CG  TYR B 399      44.831  27.727  -6.220  1.00 39.47           C  
ANISOU 4781  CG  TYR B 399     6696   4857   3443   -588   -114    335       C  
ATOM   4782  CD1 TYR B 399      44.621  26.401  -6.584  1.00 37.00           C  
ANISOU 4782  CD1 TYR B 399     6273   4668   3117   -558   -154    243       C  
ATOM   4783  CD2 TYR B 399      43.747  28.593  -6.260  1.00 45.09           C  
ANISOU 4783  CD2 TYR B 399     7533   5466   4133   -456   -303    407       C  
ATOM   4784  CE1 TYR B 399      43.358  25.950  -6.952  1.00 34.33           C  
ANISOU 4784  CE1 TYR B 399     5931   4358   2755   -422   -375    214       C  
ATOM   4785  CE2 TYR B 399      42.488  28.154  -6.616  1.00 41.01           C  
ANISOU 4785  CE2 TYR B 399     6995   4992   3596   -299   -534    376       C  
ATOM   4786  CZ  TYR B 399      42.294  26.834  -6.959  1.00 44.63           C  
ANISOU 4786  CZ  TYR B 399     7326   5582   4051   -293   -568    275       C  
ATOM   4787  OH  TYR B 399      41.026  26.414  -7.319  1.00 51.27           O  
ANISOU 4787  OH  TYR B 399     8126   6468   4886   -155   -800    220       O  
ATOM   4788  N   LYS B 400      48.244  29.802  -4.026  1.00 38.09           N  
ANISOU 4788  N   LYS B 400     6338   4567   3569  -1032    454    306       N  
ATOM   4789  CA  LYS B 400      49.576  30.374  -3.840  1.00 37.95           C  
ANISOU 4789  CA  LYS B 400     6294   4532   3592  -1228    677    268       C  
ATOM   4790  C   LYS B 400      50.209  29.888  -2.540  1.00 29.07           C  
ANISOU 4790  C   LYS B 400     4841   3526   2678  -1241    703    135       C  
ATOM   4791  O   LYS B 400      51.396  29.539  -2.513  1.00 31.43           O  
ANISOU 4791  O   LYS B 400     4997   3925   3021  -1362    866     36       O  
ATOM   4792  CB  LYS B 400      49.512  31.899  -3.895  1.00 41.65           C  
ANISOU 4792  CB  LYS B 400     7005   4797   4024  -1300    710    370       C  
ATOM   4793  CG  LYS B 400      49.076  32.411  -5.250  1.00 51.15           C  
ANISOU 4793  CG  LYS B 400     8580   5869   4985  -1291    705    510       C  
ATOM   4794  CD  LYS B 400      49.878  33.634  -5.670  1.00 65.10           C  
ANISOU 4794  CD  LYS B 400    10598   7464   6674  -1494    915    580       C  
ATOM   4795  CE  LYS B 400      49.061  34.910  -5.568  1.00 71.81           C  
ANISOU 4795  CE  LYS B 400    11718   8077   7490  -1411    791    709       C  
ATOM   4796  NZ  LYS B 400      48.078  35.021  -6.675  1.00 78.56           N  
ANISOU 4796  NZ  LYS B 400    12895   8842   8112  -1251    635    845       N  
ATOM   4797  N   ALA B 401      49.416  29.788  -1.469  1.00 28.95           N  
ANISOU 4797  N   ALA B 401     4700   3514   2786  -1105    538    122       N  
ATOM   4798  CA  ALA B 401      49.946  29.296  -0.202  1.00 30.95           C  
ANISOU 4798  CA  ALA B 401     4679   3874   3206  -1091    541      6       C  
ATOM   4799  C   ALA B 401      50.517  27.890  -0.342  1.00 35.17           C  
ANISOU 4799  C   ALA B 401     5043   4570   3749  -1069    585    -86       C  
ATOM   4800  O   ALA B 401      51.602  27.598   0.179  1.00 25.55           O  
ANISOU 4800  O   ALA B 401     3642   3448   2618  -1126    675   -195       O  
ATOM   4801  CB  ALA B 401      48.855  29.302   0.861  1.00 24.68           C  
ANISOU 4801  CB  ALA B 401     3816   3056   2506   -938    368     17       C  
ATOM   4802  N   THR B 402      49.799  27.018  -1.053  1.00 25.96           N  
ANISOU 4802  N   THR B 402     3935   3433   2497   -979    514    -55       N  
ATOM   4803  CA  THR B 402      50.173  25.609  -1.147  1.00 26.87           C  
ANISOU 4803  CA  THR B 402     3910   3675   2626   -932    535   -142       C  
ATOM   4804  C   THR B 402      51.421  25.426  -2.004  1.00 30.03           C  
ANISOU 4804  C   THR B 402     4306   4143   2960  -1055    724   -205       C  
ATOM   4805  O   THR B 402      52.327  24.660  -1.648  1.00 32.98           O  
ANISOU 4805  O   THR B 402     4491   4629   3410  -1050    792   -321       O  
ATOM   4806  CB  THR B 402      48.995  24.810  -1.720  1.00 30.44           C  
ANISOU 4806  CB  THR B 402     4439   4121   3006   -822    407   -104       C  
ATOM   4807  OG1 THR B 402      47.841  24.971  -0.876  1.00 30.62           O  
ANISOU 4807  OG1 THR B 402     4428   4094   3111   -718    254    -68       O  
ATOM   4808  CG2 THR B 402      49.339  23.364  -1.785  1.00 28.63           C  
ANISOU 4808  CG2 THR B 402     4090   3991   2796   -775    431   -195       C  
ATOM   4809  N   ALA B 403      51.461  26.093  -3.162  1.00 31.94           N  
ANISOU 4809  N   ALA B 403     4766   4318   3050  -1155    812   -134       N  
ATOM   4810  CA  ALA B 403      52.662  26.120  -3.998  1.00 32.22           C  
ANISOU 4810  CA  ALA B 403     4819   4409   3014  -1306   1036   -193       C  
ATOM   4811  C   ALA B 403      53.883  26.550  -3.202  1.00 35.87           C  
ANISOU 4811  C   ALA B 403     5075   4927   3628  -1421   1166   -301       C  
ATOM   4812  O   ALA B 403      54.982  26.025  -3.404  1.00 36.20           O  
ANISOU 4812  O   ALA B 403     4960   5090   3704  -1484   1315   -427       O  
ATOM   4813  CB  ALA B 403      52.458  27.076  -5.175  1.00 31.17           C  
ANISOU 4813  CB  ALA B 403     5003   4155   2685  -1411   1117    -72       C  
ATOM   4814  N   LYS B 404      53.704  27.511  -2.296  1.00 37.72           N  
ANISOU 4814  N   LYS B 404     5295   5078   3959  -1443   1106   -269       N  
ATOM   4815  CA  LYS B 404      54.825  28.058  -1.543  1.00 39.88           C  
ANISOU 4815  CA  LYS B 404     5380   5396   4375  -1568   1214   -384       C  
ATOM   4816  C   LYS B 404      55.528  26.990  -0.725  1.00 39.17           C  
ANISOU 4816  C   LYS B 404     4982   5480   4421  -1472   1178   -542       C  
ATOM   4817  O   LYS B 404      56.736  27.094  -0.493  1.00 39.58           O  
ANISOU 4817  O   LYS B 404     4839   5629   4570  -1576   1301   -686       O  
ATOM   4818  CB  LYS B 404      54.344  29.174  -0.624  1.00 39.07           C  
ANISOU 4818  CB  LYS B 404     5328   5168   4350  -1576   1118   -331       C  
ATOM   4819  CG  LYS B 404      55.348  30.250  -0.360  1.00 52.77           C  
ANISOU 4819  CG  LYS B 404     7016   6866   6168  -1783   1271   -406       C  
ATOM   4820  CD  LYS B 404      54.653  31.420   0.332  1.00 63.62           C  
ANISOU 4820  CD  LYS B 404     8523   8070   7581  -1780   1171   -327       C  
ATOM   4821  N   THR B 405      54.797  25.965  -0.266  1.00 37.88           N  
ANISOU 4821  N   THR B 405     4772   5351   4270  -1274   1009   -526       N  
ATOM   4822  CA  THR B 405      55.450  24.941   0.544  1.00 34.28           C  
ANISOU 4822  CA  THR B 405     4067   5034   3925  -1159    963   -662       C  
ATOM   4823  C   THR B 405      56.524  24.203  -0.233  1.00 37.96           C  
ANISOU 4823  C   THR B 405     4417   5625   4380  -1197   1115   -786       C  
ATOM   4824  O   THR B 405      57.388  23.569   0.377  1.00 36.06           O  
ANISOU 4824  O   THR B 405     3945   5509   4247  -1123   1105   -930       O  
ATOM   4825  CB  THR B 405      54.444  23.912   1.065  1.00 31.36           C  
ANISOU 4825  CB  THR B 405     3714   4650   3551   -958    786   -610       C  
ATOM   4826  OG1 THR B 405      53.783  23.294  -0.055  1.00 35.26           O  
ANISOU 4826  OG1 THR B 405     4362   5113   3923   -934    796   -544       O  
ATOM   4827  CG2 THR B 405      53.437  24.581   2.031  1.00 24.01           C  
ANISOU 4827  CG2 THR B 405     2847   3619   2655   -907    646   -519       C  
ATOM   4828  N   MET B 406      56.465  24.234  -1.566  1.00 31.91           N  
ANISOU 4828  N   MET B 406     3816   4832   3477  -1290   1247   -738       N  
ATOM   4829  CA  MET B 406      57.459  23.539  -2.351  1.00 32.51           C  
ANISOU 4829  CA  MET B 406     3789   5030   3533  -1327   1414   -866       C  
ATOM   4830  C   MET B 406      58.819  24.197  -2.238  1.00 41.52           C  
ANISOU 4830  C   MET B 406     4736   6261   4778  -1496   1597  -1012       C  
ATOM   4831  O   MET B 406      59.807  23.587  -2.645  1.00 44.18           O  
ANISOU 4831  O   MET B 406     4904   6734   5148  -1510   1734  -1165       O  
ATOM   4832  CB  MET B 406      57.045  23.487  -3.822  1.00 36.54           C  
ANISOU 4832  CB  MET B 406     4554   5486   3842  -1395   1520   -780       C  
ATOM   4833  CG  MET B 406      55.668  22.926  -4.049  1.00 38.57           C  
ANISOU 4833  CG  MET B 406     4997   5660   3999  -1252   1336   -656       C  
ATOM   4834  SD  MET B 406      55.602  21.166  -3.658  1.00 39.06           S  
ANISOU 4834  SD  MET B 406     4903   5807   4130  -1035   1220   -758       S  
ATOM   4835  CE  MET B 406      56.722  20.446  -4.850  1.00 34.51           C  
ANISOU 4835  CE  MET B 406     4282   5351   3480  -1085   1444   -904       C  
ATOM   4836  N   ASP B 407      58.883  25.422  -1.705  1.00 35.33           N  
ANISOU 4836  N   ASP B 407     3964   5405   4054  -1629   1608   -982       N  
ATOM   4837  CA  ASP B 407      60.151  26.122  -1.541  1.00 46.76           C  
ANISOU 4837  CA  ASP B 407     5213   6931   5621  -1820   1783  -1139       C  
ATOM   4838  C   ASP B 407      60.918  25.670  -0.313  1.00 47.66           C  
ANISOU 4838  C   ASP B 407     4983   7197   5928  -1704   1667  -1325       C  
ATOM   4839  O   ASP B 407      62.028  26.147  -0.085  1.00 53.87           O  
ANISOU 4839  O   ASP B 407     5560   8068   6841  -1830   1768  -1489       O  
ATOM   4840  CB  ASP B 407      59.916  27.634  -1.455  1.00 43.59           C  
ANISOU 4840  CB  ASP B 407     4982   6369   5211  -2017   1840  -1043       C  
ATOM   4841  CG  ASP B 407      59.298  28.193  -2.716  1.00 54.14           C  
ANISOU 4841  CG  ASP B 407     6681   7548   6342  -2134   1965   -865       C  
ATOM   4842  OD1 ASP B 407      59.529  27.591  -3.791  1.00 56.75           O  
ANISOU 4842  OD1 ASP B 407     7079   7929   6556  -2142   2088   -872       O  
ATOM   4843  OD2 ASP B 407      58.590  29.220  -2.645  1.00 60.81           O  
ANISOU 4843  OD2 ASP B 407     7759   8211   7134  -2191   1919   -719       O  
ATOM   4844  N   TYR B 408      60.358  24.793   0.502  1.00 40.68           N  
ANISOU 4844  N   TYR B 408     4061   6331   5066  -1455   1437  -1301       N  
ATOM   4845  CA  TYR B 408      61.023  24.375   1.721  1.00 38.57           C  
ANISOU 4845  CA  TYR B 408     3514   6191   4949  -1315   1297  -1459       C  
ATOM   4846  C   TYR B 408      61.404  22.907   1.590  1.00 46.10           C  
ANISOU 4846  C   TYR B 408     4339   7264   5911  -1108   1256  -1554       C  
ATOM   4847  O   TYR B 408      60.676  22.117   0.984  1.00 48.94           O  
ANISOU 4847  O   TYR B 408     4872   7563   6159  -1011   1238  -1447       O  
ATOM   4848  CB  TYR B 408      60.123  24.598   2.945  1.00 38.19           C  
ANISOU 4848  CB  TYR B 408     3547   6052   4911  -1188   1067  -1357       C  
ATOM   4849  CG  TYR B 408      59.698  26.042   3.174  1.00 43.61           C  
ANISOU 4849  CG  TYR B 408     4367   6606   5598  -1361   1087  -1273       C  
ATOM   4850  CD1 TYR B 408      58.661  26.613   2.442  1.00 39.24           C  
ANISOU 4850  CD1 TYR B 408     4107   5882   4920  -1439   1129  -1079       C  
ATOM   4851  CD2 TYR B 408      60.330  26.831   4.145  1.00 48.00           C  
ANISOU 4851  CD2 TYR B 408     4759   7201   6278  -1432   1046  -1398       C  
ATOM   4852  CE1 TYR B 408      58.274  27.933   2.655  1.00 44.27           C  
ANISOU 4852  CE1 TYR B 408     4884   6377   5559  -1574   1140  -1004       C  
ATOM   4853  CE2 TYR B 408      59.948  28.157   4.368  1.00 45.10           C  
ANISOU 4853  CE2 TYR B 408     4529   6691   5916  -1589   1068  -1330       C  
ATOM   4854  CZ  TYR B 408      58.920  28.698   3.623  1.00 49.37           C  
ANISOU 4854  CZ  TYR B 408     5374   7049   6334  -1653   1118  -1129       C  
ATOM   4855  OH  TYR B 408      58.545  30.006   3.839  1.00 53.28           O  
ANISOU 4855  OH  TYR B 408     6022   7386   6837  -1786   1133  -1063       O  
ATOM   4856  N   LYS B 409      62.542  22.549   2.161  1.00 45.85           N  
ANISOU 4856  N   LYS B 409     4004   7400   6018  -1032   1231  -1767       N  
ATOM   4857  CA  LYS B 409      63.017  21.182   2.102  1.00 42.92           C  
ANISOU 4857  CA  LYS B 409     3499   7137   5670   -810   1182  -1879       C  
ATOM   4858  C   LYS B 409      62.353  20.290   3.144  1.00 44.37           C  
ANISOU 4858  C   LYS B 409     3755   7268   5835   -529    922  -1803       C  
ATOM   4859  O   LYS B 409      62.472  19.061   3.053  1.00 43.64           O  
ANISOU 4859  O   LYS B 409     3645   7206   5732   -325    868  -1845       O  
ATOM   4860  CB  LYS B 409      64.538  21.187   2.250  1.00 46.61           C  
ANISOU 4860  CB  LYS B 409     3659   7767   6283   -816   1220  -2122       C  
ATOM   4861  CG  LYS B 409      65.217  21.993   1.151  1.00 50.61           C  
ANISOU 4861  CG  LYS B 409     4191   8253   6784  -1085   1459  -2154       C  
ATOM   4862  CD  LYS B 409      66.730  21.772   1.109  1.00 48.83           C  
ANISOU 4862  CD  LYS B 409     3707   8160   6686  -1064   1487  -2383       C  
ATOM   4863  N   GLY B 410      61.619  20.875   4.089  1.00 34.77           N  
ANISOU 4863  N   GLY B 410     2647   5958   4605   -521    778  -1688       N  
ATOM   4864  CA  GLY B 410      60.925  20.094   5.092  1.00 35.53           C  
ANISOU 4864  CA  GLY B 410     2845   5990   4665   -282    564  -1602       C  
ATOM   4865  C   GLY B 410      59.733  19.323   4.546  1.00 38.32           C  
ANISOU 4865  C   GLY B 410     3458   6201   4899   -220    559  -1424       C  
ATOM   4866  O   GLY B 410      59.249  19.514   3.431  1.00 36.87           O  
ANISOU 4866  O   GLY B 410     3409   5956   4643   -358    690  -1342       O  
ATOM   4867  N   PHE B 411      59.264  18.409   5.375  1.00 36.71           N  
ANISOU 4867  N   PHE B 411     3333   5943   4671     -6    402  -1373       N  
ATOM   4868  CA  PHE B 411      58.073  17.639   5.068  1.00 28.99           C  
ANISOU 4868  CA  PHE B 411     2589   4823   3602     50    382  -1219       C  
ATOM   4869  C   PHE B 411      56.857  18.553   5.163  1.00 32.60           C  
ANISOU 4869  C   PHE B 411     3213   5165   4008    -84    374  -1056       C  
ATOM   4870  O   PHE B 411      56.560  19.079   6.233  1.00 24.64           O  
ANISOU 4870  O   PHE B 411     2215   4132   3015    -59    277  -1019       O  
ATOM   4871  CB  PHE B 411      57.974  16.491   6.060  1.00 29.98           C  
ANISOU 4871  CB  PHE B 411     2761   4908   3721    298    232  -1213       C  
ATOM   4872  CG  PHE B 411      57.203  15.321   5.573  1.00 31.04           C  
ANISOU 4872  CG  PHE B 411     3076   4923   3794    375    243  -1132       C  
ATOM   4873  CD1 PHE B 411      55.894  15.449   5.173  1.00 33.23           C  
ANISOU 4873  CD1 PHE B 411     3538   5077   4009    264    272   -986       C  
ATOM   4874  CD2 PHE B 411      57.789  14.073   5.549  1.00 32.04           C  
ANISOU 4874  CD2 PHE B 411     3184   5056   3934    567    213  -1217       C  
ATOM   4875  CE1 PHE B 411      55.171  14.333   4.734  1.00 32.27           C  
ANISOU 4875  CE1 PHE B 411     3571   4845   3845    319    279   -934       C  
ATOM   4876  CE2 PHE B 411      57.087  12.975   5.122  1.00 36.22           C  
ANISOU 4876  CE2 PHE B 411     3893   5456   4414    627    227  -1154       C  
ATOM   4877  CZ  PHE B 411      55.769  13.113   4.708  1.00 32.43           C  
ANISOU 4877  CZ  PHE B 411     3588   4857   3877    488    264  -1015       C  
ATOM   4878  N   THR B 412      56.152  18.751   4.054  1.00 29.88           N  
ANISOU 4878  N   THR B 412     3002   4753   3597   -211    466   -969       N  
ATOM   4879  CA  THR B 412      54.974  19.599   4.087  1.00 27.08           C  
ANISOU 4879  CA  THR B 412     2798   4292   3199   -309    442   -826       C  
ATOM   4880  C   THR B 412      53.848  18.875   4.813  1.00 26.16           C  
ANISOU 4880  C   THR B 412     2799   4079   3063   -186    330   -731       C  
ATOM   4881  O   THR B 412      53.538  17.724   4.495  1.00 27.15           O  
ANISOU 4881  O   THR B 412     2988   4167   3162   -104    323   -724       O  
ATOM   4882  CB  THR B 412      54.511  19.960   2.670  1.00 28.64           C  
ANISOU 4882  CB  THR B 412     3121   4445   3314   -451    545   -763       C  
ATOM   4883  OG1 THR B 412      55.547  20.635   1.975  1.00 27.95           O  
ANISOU 4883  OG1 THR B 412     2953   4436   3232   -588    685   -844       O  
ATOM   4884  CG2 THR B 412      53.250  20.871   2.722  1.00 28.01           C  
ANISOU 4884  CG2 THR B 412     3193   4253   3195   -518    491   -623       C  
ATOM   4885  N   VAL B 413      53.244  19.535   5.785  1.00 24.85           N  
ANISOU 4885  N   VAL B 413     2665   3866   2912   -184    257   -669       N  
ATOM   4886  CA  VAL B 413      52.004  19.067   6.402  1.00 22.23           C  
ANISOU 4886  CA  VAL B 413     2452   3435   2558   -114    189   -572       C  
ATOM   4887  C   VAL B 413      50.927  20.069   6.022  1.00 28.56           C  
ANISOU 4887  C   VAL B 413     3338   4169   3344   -227    195   -481       C  
ATOM   4888  O   VAL B 413      50.962  21.228   6.459  1.00 26.37           O  
ANISOU 4888  O   VAL B 413     3042   3890   3088   -284    184   -472       O  
ATOM   4889  CB  VAL B 413      52.101  18.917   7.930  1.00 22.74           C  
ANISOU 4889  CB  VAL B 413     2502   3500   2637      8    104   -580       C  
ATOM   4890  CG1 VAL B 413      50.776  18.405   8.475  1.00 19.48           C  
ANISOU 4890  CG1 VAL B 413     2223   2979   2198     50     79   -480       C  
ATOM   4891  CG2 VAL B 413      53.218  17.947   8.312  1.00 27.56           C  
ANISOU 4891  CG2 VAL B 413     3039   4177   3256    156     68   -675       C  
ATOM   4892  N   ALA B 414      49.968  19.618   5.213  1.00 25.75           N  
ANISOU 4892  N   ALA B 414     3076   3754   2953   -250    201   -425       N  
ATOM   4893  CA  ALA B 414      48.931  20.473   4.657  1.00 21.32           C  
ANISOU 4893  CA  ALA B 414     2593   3137   2370   -329    185   -351       C  
ATOM   4894  C   ALA B 414      47.604  20.130   5.332  1.00 26.65           C  
ANISOU 4894  C   ALA B 414     3306   3746   3074   -278    126   -301       C  
ATOM   4895  O   ALA B 414      47.173  18.971   5.349  1.00 18.63           O  
ANISOU 4895  O   ALA B 414     2313   2704   2061   -235    125   -308       O  
ATOM   4896  CB  ALA B 414      48.866  20.307   3.141  1.00 25.40           C  
ANISOU 4896  CB  ALA B 414     3178   3656   2816   -394    223   -348       C  
ATOM   4897  N   ILE B 415      46.986  21.120   5.946  1.00 19.32           N  
ANISOU 4897  N   ILE B 415     2382   2785   2172   -288     92   -263       N  
ATOM   4898  CA  ILE B 415      45.810  20.870   6.762  1.00 23.22           C  
ANISOU 4898  CA  ILE B 415     2884   3232   2705   -243     62   -236       C  
ATOM   4899  C   ILE B 415      44.717  21.848   6.356  1.00 27.15           C  
ANISOU 4899  C   ILE B 415     3406   3691   3220   -274     16   -199       C  
ATOM   4900  O   ILE B 415      44.692  22.982   6.854  1.00 23.64           O  
ANISOU 4900  O   ILE B 415     2962   3229   2793   -274     -1   -186       O  
ATOM   4901  CB  ILE B 415      46.130  20.996   8.262  1.00 20.16           C  
ANISOU 4901  CB  ILE B 415     2473   2852   2335   -182     65   -247       C  
ATOM   4902  CG1 ILE B 415      47.328  20.133   8.651  1.00 24.74           C  
ANISOU 4902  CG1 ILE B 415     3033   3476   2891   -119     78   -292       C  
ATOM   4903  CG2 ILE B 415      44.936  20.597   9.086  1.00 17.28           C  
ANISOU 4903  CG2 ILE B 415     2131   2438   1996   -149     74   -222       C  
ATOM   4904  CD1 ILE B 415      47.696  20.298  10.137  1.00 23.91           C  
ANISOU 4904  CD1 ILE B 415     2923   3385   2776    -40     52   -308       C  
ATOM   4905  N   PRO B 416      43.806  21.460   5.485  1.00 21.99           N  
ANISOU 4905  N   PRO B 416     2771   3021   2562   -287    -18   -193       N  
ATOM   4906  CA  PRO B 416      42.683  22.344   5.130  1.00 23.91           C  
ANISOU 4906  CA  PRO B 416     3025   3233   2826   -280    -92   -171       C  
ATOM   4907  C   PRO B 416      41.384  22.028   5.891  1.00 26.64           C  
ANISOU 4907  C   PRO B 416     3299   3566   3258   -246   -105   -195       C  
ATOM   4908  O   PRO B 416      41.193  20.892   6.319  1.00 23.48           O  
ANISOU 4908  O   PRO B 416     2869   3167   2885   -255    -52   -221       O  
ATOM   4909  CB  PRO B 416      42.527  22.059   3.626  1.00 18.75           C  
ANISOU 4909  CB  PRO B 416     2431   2589   2104   -308   -138   -171       C  
ATOM   4910  CG  PRO B 416      42.742  20.500   3.593  1.00 26.61           C  
ANISOU 4910  CG  PRO B 416     3400   3607   3105   -321    -87   -218       C  
ATOM   4911  CD  PRO B 416      43.829  20.240   4.663  1.00 21.98           C  
ANISOU 4911  CD  PRO B 416     2788   3032   2533   -302     -6   -221       C  
ATOM   4912  N   ASN B 417      40.465  22.985   6.062  1.00 18.57           N  
ANISOU 4912  N   ASN B 417     2250   2524   2283   -209   -162   -193       N  
ATOM   4913  CA  ASN B 417      39.106  22.626   6.450  1.00 20.75           C  
ANISOU 4913  CA  ASN B 417     2428   2806   2650   -190   -172   -242       C  
ATOM   4914  C   ASN B 417      38.309  22.363   5.172  1.00 19.85           C  
ANISOU 4914  C   ASN B 417     2294   2711   2538   -192   -275   -276       C  
ATOM   4915  O   ASN B 417      38.881  22.293   4.081  1.00 23.88           O  
ANISOU 4915  O   ASN B 417     2892   3225   2957   -210   -320   -252       O  
ATOM   4916  CB  ASN B 417      38.525  23.679   7.413  1.00 27.29           C  
ANISOU 4916  CB  ASN B 417     3213   3616   3540   -131   -172   -251       C  
ATOM   4917  CG  ASN B 417      38.188  25.007   6.742  1.00 27.07           C  
ANISOU 4917  CG  ASN B 417     3223   3555   3506    -69   -289   -234       C  
ATOM   4918  OD1 ASN B 417      38.691  25.326   5.667  1.00 24.25           O  
ANISOU 4918  OD1 ASN B 417     2965   3179   3068    -79   -351   -190       O  
ATOM   4919  ND2 ASN B 417      37.325  25.791   7.398  1.00 22.42           N  
ANISOU 4919  ND2 ASN B 417     2573   2951   2996      2   -309   -269       N  
ATOM   4920  N   TYR B 418      36.989  22.175   5.267  1.00 22.49           N  
ANISOU 4920  N   TYR B 418     2509   3067   2971   -177   -313   -347       N  
ATOM   4921  CA  TYR B 418      36.293  21.485   4.175  1.00 24.92           C  
ANISOU 4921  CA  TYR B 418     2774   3408   3288   -199   -402   -411       C  
ATOM   4922  C   TYR B 418      36.362  22.235   2.842  1.00 29.11           C  
ANISOU 4922  C   TYR B 418     3401   3942   3717   -141   -558   -382       C  
ATOM   4923  O   TYR B 418      36.729  21.650   1.819  1.00 26.57           O  
ANISOU 4923  O   TYR B 418     3155   3634   3306   -176   -594   -386       O  
ATOM   4924  CB  TYR B 418      34.835  21.180   4.510  1.00 24.14           C  
ANISOU 4924  CB  TYR B 418     2492   3345   3334   -203   -417   -521       C  
ATOM   4925  CG  TYR B 418      34.196  20.568   3.289  1.00 26.60           C  
ANISOU 4925  CG  TYR B 418     2758   3700   3649   -225   -540   -605       C  
ATOM   4926  CD1 TYR B 418      34.601  19.317   2.816  1.00 26.65           C  
ANISOU 4926  CD1 TYR B 418     2812   3696   3617   -320   -490   -629       C  
ATOM   4927  CD2 TYR B 418      33.250  21.266   2.556  1.00 29.63           C  
ANISOU 4927  CD2 TYR B 418     3069   4130   4059   -132   -725   -667       C  
ATOM   4928  CE1 TYR B 418      34.062  18.779   1.669  1.00 28.47           C  
ANISOU 4928  CE1 TYR B 418     3014   3966   3837   -342   -612   -719       C  
ATOM   4929  CE2 TYR B 418      32.697  20.728   1.419  1.00 30.68           C  
ANISOU 4929  CE2 TYR B 418     3168   4313   4177   -140   -864   -756       C  
ATOM   4930  CZ  TYR B 418      33.103  19.498   0.972  1.00 33.11           C  
ANISOU 4930  CZ  TYR B 418     3522   4614   4446   -253   -806   -785       C  
ATOM   4931  OH  TYR B 418      32.527  18.984  -0.167  1.00 42.09           O  
ANISOU 4931  OH  TYR B 418     4627   5803   5562   -262   -955   -892       O  
ATOM   4932  N   THR B 419      35.939  23.502   2.792  1.00 25.15           N  
ANISOU 4932  N   THR B 419     2915   3420   3219    -43   -658   -359       N  
ATOM   4933  CA  THR B 419      35.971  24.085   1.448  1.00 25.15           C  
ANISOU 4933  CA  THR B 419     3052   3407   3096     16   -808   -322       C  
ATOM   4934  C   THR B 419      37.373  24.499   1.028  1.00 23.24           C  
ANISOU 4934  C   THR B 419     3011   3113   2707    -30   -740   -213       C  
ATOM   4935  O   THR B 419      37.552  24.879  -0.121  1.00 37.62           O  
ANISOU 4935  O   THR B 419     4986   4915   4394     -5   -826   -170       O  
ATOM   4936  CB  THR B 419      35.018  25.293   1.271  1.00 27.65           C  
ANISOU 4936  CB  THR B 419     3363   3701   3443    162   -971   -330       C  
ATOM   4937  OG1 THR B 419      35.418  26.388   2.106  1.00 26.28           O  
ANISOU 4937  OG1 THR B 419     3246   3451   3288    199   -910   -264       O  
ATOM   4938  CG2 THR B 419      33.569  24.917   1.554  1.00 26.38           C  
ANISOU 4938  CG2 THR B 419     2966   3615   3442    213  -1050   -470       C  
ATOM   4939  N   SER B 420      38.370  24.430   1.921  1.00 21.95           N  
ANISOU 4939  N   SER B 420     2849   2932   2559    -97   -586   -178       N  
ATOM   4940  CA  SER B 420      39.754  24.597   1.509  1.00 21.55           C  
ANISOU 4940  CA  SER B 420     2937   2858   2393   -165   -501   -111       C  
ATOM   4941  C   SER B 420      40.312  23.357   0.813  1.00 26.07           C  
ANISOU 4941  C   SER B 420     3524   3482   2901   -233   -450   -142       C  
ATOM   4942  O   SER B 420      41.328  23.458   0.123  1.00 24.82           O  
ANISOU 4942  O   SER B 420     3481   3320   2630   -284   -392   -105       O  
ATOM   4943  CB  SER B 420      40.654  24.914   2.715  1.00 24.43           C  
ANISOU 4943  CB  SER B 420     3271   3205   2808   -202   -376    -92       C  
ATOM   4944  OG  SER B 420      40.185  26.027   3.467  1.00 28.98           O  
ANISOU 4944  OG  SER B 420     3836   3727   3448   -142   -408    -79       O  
ATOM   4945  N   LEU B 421      39.692  22.192   0.992  1.00 23.05           N  
ANISOU 4945  N   LEU B 421     3029   3140   2590   -243   -453   -217       N  
ATOM   4946  CA  LEU B 421      40.346  20.950   0.572  1.00 22.23           C  
ANISOU 4946  CA  LEU B 421     2941   3064   2443   -304   -380   -254       C  
ATOM   4947  C   LEU B 421      40.554  20.892  -0.944  1.00 23.82           C  
ANISOU 4947  C   LEU B 421     3273   3282   2495   -316   -440   -254       C  
ATOM   4948  O   LEU B 421      41.661  20.616  -1.413  1.00 27.58           O  
ANISOU 4948  O   LEU B 421     3829   3770   2881   -361   -348   -242       O  
ATOM   4949  CB  LEU B 421      39.540  19.744   1.055  1.00 23.12           C  
ANISOU 4949  CB  LEU B 421     2934   3186   2666   -325   -367   -336       C  
ATOM   4950  CG  LEU B 421      40.026  18.381   0.521  1.00 24.94           C  
ANISOU 4950  CG  LEU B 421     3198   3420   2858   -377   -312   -388       C  
ATOM   4951  CD1 LEU B 421      41.491  18.076   0.981  1.00 20.24           C  
ANISOU 4951  CD1 LEU B 421     2648   2816   2226   -384   -181   -352       C  
ATOM   4952  CD2 LEU B 421      39.023  17.250   0.936  1.00 23.84           C  
ANISOU 4952  CD2 LEU B 421     2959   3262   2838   -418   -300   -475       C  
ATOM   4953  N   ALA B 422      39.498  21.111  -1.721  1.00 24.31           N  
ANISOU 4953  N   ALA B 422     3355   3356   2527   -268   -594   -282       N  
ATOM   4954  CA  ALA B 422      39.609  20.979  -3.175  1.00 30.09           C  
ANISOU 4954  CA  ALA B 422     4234   4107   3090   -269   -665   -290       C  
ATOM   4955  C   ALA B 422      40.680  21.886  -3.778  1.00 25.73           C  
ANISOU 4955  C   ALA B 422     3875   3523   2378   -288   -597   -190       C  
ATOM   4956  O   ALA B 422      41.495  21.391  -4.571  1.00 28.49           O  
ANISOU 4956  O   ALA B 422     4324   3896   2605   -343   -517   -200       O  
ATOM   4957  CB  ALA B 422      38.233  21.210  -3.833  1.00 25.90           C  
ANISOU 4957  CB  ALA B 422     3690   3600   2550   -186   -880   -342       C  
ATOM   4958  N   PRO B 423      40.740  23.194  -3.487  1.00 30.04           N  
ANISOU 4958  N   PRO B 423     4490   4009   2916   -256   -610   -100       N  
ATOM   4959  CA  PRO B 423      41.855  23.974  -4.049  1.00 25.41           C  
ANISOU 4959  CA  PRO B 423     4093   3377   2185   -315   -503    -13       C  
ATOM   4960  C   PRO B 423      43.227  23.522  -3.550  1.00 27.07           C  
ANISOU 4960  C   PRO B 423     4236   3618   2432   -419   -299    -31       C  
ATOM   4961  O   PRO B 423      44.196  23.475  -4.324  1.00 27.58           O  
ANISOU 4961  O   PRO B 423     4412   3695   2371   -494   -184    -21       O  
ATOM   4962  CB  PRO B 423      41.527  25.423  -3.621  1.00 32.95           C  
ANISOU 4962  CB  PRO B 423     5119   4238   3164   -261   -559     72       C  
ATOM   4963  CG  PRO B 423      40.580  25.304  -2.483  1.00 29.77           C  
ANISOU 4963  CG  PRO B 423     4509   3851   2953   -189   -635     19       C  
ATOM   4964  CD  PRO B 423      39.748  24.064  -2.813  1.00 26.02           C  
ANISOU 4964  CD  PRO B 423     3916   3460   2512   -164   -724    -83       C  
ATOM   4965  N   MET B 424      43.352  23.189  -2.269  1.00 22.98           N  
ANISOU 4965  N   MET B 424     3537   3115   2078   -419   -249    -67       N  
ATOM   4966  CA  MET B 424      44.667  22.799  -1.769  1.00 22.29           C  
ANISOU 4966  CA  MET B 424     3379   3065   2026   -488    -88    -96       C  
ATOM   4967  C   MET B 424      45.112  21.475  -2.381  1.00 28.21           C  
ANISOU 4967  C   MET B 424     4112   3876   2730   -507    -32   -170       C  
ATOM   4968  O   MET B 424      46.273  21.329  -2.770  1.00 26.39           O  
ANISOU 4968  O   MET B 424     3903   3682   2442   -566     97   -193       O  
ATOM   4969  CB  MET B 424      44.641  22.721  -0.247  1.00 23.78           C  
ANISOU 4969  CB  MET B 424     3409   3254   2374   -458    -74   -116       C  
ATOM   4970  CG  MET B 424      45.973  22.282   0.369  1.00 22.40           C  
ANISOU 4970  CG  MET B 424     3145   3127   2240   -496     54   -161       C  
ATOM   4971  SD  MET B 424      45.852  22.194   2.148  1.00 26.53           S  
ANISOU 4971  SD  MET B 424     3528   3646   2906   -438     44   -178       S  
ATOM   4972  CE  MET B 424      45.744  23.951   2.588  1.00 19.62           C  
ANISOU 4972  CE  MET B 424     2698   2707   2048   -461     21   -121       C  
ATOM   4973  N   LEU B 425      44.186  20.511  -2.519  1.00 23.56           N  
ANISOU 4973  N   LEU B 425     3482   3298   2170   -463   -122   -223       N  
ATOM   4974  CA  LEU B 425      44.521  19.219  -3.124  1.00 22.67           C  
ANISOU 4974  CA  LEU B 425     3372   3223   2017   -476    -78   -305       C  
ATOM   4975  C   LEU B 425      44.846  19.368  -4.605  1.00 26.20           C  
ANISOU 4975  C   LEU B 425     3988   3693   2274   -510    -63   -306       C  
ATOM   4976  O   LEU B 425      45.770  18.725  -5.129  1.00 26.76           O  
ANISOU 4976  O   LEU B 425     4083   3803   2281   -543     52   -361       O  
ATOM   4977  CB  LEU B 425      43.345  18.252  -2.925  1.00 24.44           C  
ANISOU 4977  CB  LEU B 425     3526   3435   2326   -445   -177   -369       C  
ATOM   4978  CG  LEU B 425      43.537  16.838  -3.445  1.00 30.19           C  
ANISOU 4978  CG  LEU B 425     4263   4173   3035   -458   -141   -466       C  
ATOM   4979  CD1 LEU B 425      44.715  16.169  -2.709  1.00 26.28           C  
ANISOU 4979  CD1 LEU B 425     3710   3676   2600   -448     -1   -488       C  
ATOM   4980  CD2 LEU B 425      42.212  16.047  -3.294  1.00 31.77           C  
ANISOU 4980  CD2 LEU B 425     4397   4346   3329   -458   -243   -535       C  
ATOM   4981  N   GLU B 426      44.090  20.213  -5.302  1.00 27.54           N  
ANISOU 4981  N   GLU B 426     4285   3837   2341   -491   -179   -248       N  
ATOM   4982  CA  GLU B 426      44.383  20.502  -6.701  1.00 31.56           C  
ANISOU 4982  CA  GLU B 426     5004   4355   2631   -518   -166   -228       C  
ATOM   4983  C   GLU B 426      45.792  21.066  -6.878  1.00 31.48           C  
ANISOU 4983  C   GLU B 426     5063   4349   2549   -608     38   -188       C  
ATOM   4984  O   GLU B 426      46.541  20.637  -7.762  1.00 31.19           O  
ANISOU 4984  O   GLU B 426     5114   4355   2383   -658    154   -230       O  
ATOM   4985  CB  GLU B 426      43.338  21.478  -7.230  1.00 37.35           C  
ANISOU 4985  CB  GLU B 426     5879   5042   3270   -453   -344   -154       C  
ATOM   4986  CG  GLU B 426      43.680  22.080  -8.559  1.00 47.61           C  
ANISOU 4986  CG  GLU B 426     7453   6322   4313   -474   -325    -92       C  
ATOM   4987  CD  GLU B 426      42.575  22.976  -9.070  1.00 54.40           C  
ANISOU 4987  CD  GLU B 426     8471   7128   5071   -369   -540    -22       C  
ATOM   4988  OE1 GLU B 426      41.413  22.799  -8.642  1.00 62.32           O  
ANISOU 4988  OE1 GLU B 426     9336   8144   6198   -275   -728    -70       O  
ATOM   4989  OE2 GLU B 426      42.867  23.856  -9.894  1.00 61.74           O  
ANISOU 4989  OE2 GLU B 426     9664   7997   5796   -377   -518     77       O  
ATOM   4990  N   GLN B 427      46.178  22.039  -6.047  1.00 29.90           N  
ANISOU 4990  N   GLN B 427     4817   4107   2435   -638     94   -122       N  
ATOM   4991  CA  GLN B 427      47.521  22.593  -6.178  1.00 32.01           C  
ANISOU 4991  CA  GLN B 427     5121   4382   2660   -748    296   -107       C  
ATOM   4992  C   GLN B 427      48.594  21.555  -5.858  1.00 35.14           C  
ANISOU 4992  C   GLN B 427     5343   4869   3139   -775    438   -222       C  
ATOM   4993  O   GLN B 427      49.652  21.524  -6.502  1.00 33.43           O  
ANISOU 4993  O   GLN B 427     5163   4699   2839   -859    611   -263       O  
ATOM   4994  CB  GLN B 427      47.693  23.804  -5.272  1.00 29.66           C  
ANISOU 4994  CB  GLN B 427     4793   4017   2461   -782    315    -38       C  
ATOM   4995  CG  GLN B 427      49.045  24.439  -5.441  1.00 30.78           C  
ANISOU 4995  CG  GLN B 427     4962   4163   2571   -924    529    -40       C  
ATOM   4996  CD  GLN B 427      49.271  24.955  -6.856  1.00 38.69           C  
ANISOU 4996  CD  GLN B 427     6238   5123   3341  -1006    623     23       C  
ATOM   4997  OE1 GLN B 427      48.424  25.635  -7.434  1.00 35.98           O  
ANISOU 4997  OE1 GLN B 427     6119   4685   2868   -962    508    127       O  
ATOM   4998  NE2 GLN B 427      50.421  24.633  -7.414  1.00 40.72           N  
ANISOU 4998  NE2 GLN B 427     6484   5450   3538  -1116    833    -45       N  
ATOM   4999  N   LEU B 428      48.370  20.730  -4.834  1.00 25.17           N  
ANISOU 4999  N   LEU B 428     3894   3628   2040   -701    376   -279       N  
ATOM   5000  CA  LEU B 428      49.374  19.723  -4.501  1.00 29.27           C  
ANISOU 5000  CA  LEU B 428     4267   4220   2636   -689    485   -387       C  
ATOM   5001  C   LEU B 428      49.565  18.760  -5.665  1.00 28.84           C  
ANISOU 5001  C   LEU B 428     4293   4206   2458   -688    536   -464       C  
ATOM   5002  O   LEU B 428      50.701  18.433  -6.021  1.00 29.20           O  
ANISOU 5002  O   LEU B 428     4296   4318   2480   -723    692   -544       O  
ATOM   5003  CB  LEU B 428      48.989  18.971  -3.213  1.00 26.38           C  
ANISOU 5003  CB  LEU B 428     3745   3842   2437   -595    399   -416       C  
ATOM   5004  CG  LEU B 428      49.210  19.806  -1.941  1.00 31.51           C  
ANISOU 5004  CG  LEU B 428     4291   4478   3205   -594    390   -376       C  
ATOM   5005  CD1 LEU B 428      48.652  19.151  -0.707  1.00 27.50           C  
ANISOU 5005  CD1 LEU B 428     3683   3945   2822   -502    304   -383       C  
ATOM   5006  CD2 LEU B 428      50.703  20.102  -1.756  1.00 25.21           C  
ANISOU 5006  CD2 LEU B 428     3392   3749   2436   -647    532   -438       C  
ATOM   5007  N   ASN B 429      48.463  18.333  -6.302  1.00 26.85           N  
ANISOU 5007  N   ASN B 429     4152   3922   2128   -650    406   -457       N  
ATOM   5008  CA  ASN B 429      48.577  17.460  -7.466  1.00 30.55           C  
ANISOU 5008  CA  ASN B 429     4722   4425   2461   -650    442   -540       C  
ATOM   5009  C   ASN B 429      49.361  18.133  -8.573  1.00 43.56           C  
ANISOU 5009  C   ASN B 429     6526   6108   3918   -739    590   -522       C  
ATOM   5010  O   ASN B 429      50.240  17.517  -9.193  1.00 39.10           O  
ANISOU 5010  O   ASN B 429     5966   5604   3287   -763    738   -618       O  
ATOM   5011  CB  ASN B 429      47.196  17.042  -7.972  1.00 36.42           C  
ANISOU 5011  CB  ASN B 429     5555   5133   3149   -605    254   -546       C  
ATOM   5012  CG  ASN B 429      46.651  15.856  -7.210  1.00 41.97           C  
ANISOU 5012  CG  ASN B 429     6121   5808   4016   -548    180   -622       C  
ATOM   5013  OD1 ASN B 429      47.385  14.907  -6.919  1.00 45.19           O  
ANISOU 5013  OD1 ASN B 429     6452   6225   4493   -524    277   -703       O  
ATOM   5014  ND2 ASN B 429      45.374  15.908  -6.861  1.00 35.25           N  
ANISOU 5014  ND2 ASN B 429     5242   4917   3235   -523     18   -599       N  
ATOM   5015  N   ARG B 430      49.074  19.413  -8.815  1.00 44.52           N  
ANISOU 5015  N   ARG B 430     6786   6182   3948   -789    566   -402       N  
ATOM   5016  CA  ARG B 430      49.795  20.149  -9.843  1.00 39.74           C  
ANISOU 5016  CA  ARG B 430     6371   5583   3144   -893    730   -364       C  
ATOM   5017  C   ARG B 430      51.275  20.268  -9.483  1.00 34.81           C  
ANISOU 5017  C   ARG B 430     5599   5021   2608   -988    972   -427       C  
ATOM   5018  O   ARG B 430      52.150  20.005 -10.320  1.00 38.09           O  
ANISOU 5018  O   ARG B 430     6065   5499   2908  -1058   1163   -500       O  
ATOM   5019  CB  ARG B 430      49.134  21.515 -10.008  1.00 44.85           C  
ANISOU 5019  CB  ARG B 430     7211   6132   3697   -912    641   -210       C  
ATOM   5020  CG  ARG B 430      49.550  22.359 -11.159  1.00 52.81           C  
ANISOU 5020  CG  ARG B 430     8506   7104   4457  -1009    773   -133       C  
ATOM   5021  CD  ARG B 430      48.870  23.717 -10.994  1.00 60.11           C  
ANISOU 5021  CD  ARG B 430     9596   7899   5344   -997    660     24       C  
ATOM   5022  NE  ARG B 430      47.437  23.644 -11.265  1.00 64.99           N  
ANISOU 5022  NE  ARG B 430    10314   8481   5898   -848    376     64       N  
ATOM   5023  CZ  ARG B 430      46.497  24.247 -10.546  1.00 66.94           C  
ANISOU 5023  CZ  ARG B 430    10516   8658   6260   -756    185    128       C  
ATOM   5024  NH1 ARG B 430      46.823  24.961  -9.477  1.00 67.47           N  
ANISOU 5024  NH1 ARG B 430    10459   8674   6503   -798    245    167       N  
ATOM   5025  NH2 ARG B 430      45.223  24.123 -10.894  1.00 69.23           N  
ANISOU 5025  NH2 ARG B 430    10872   8938   6493   -618    -71    135       N  
ATOM   5026  N   SER B 431      51.570  20.599  -8.225  1.00 30.59           N  
ANISOU 5026  N   SER B 431     4862   4481   2279   -986    965   -424       N  
ATOM   5027  CA  SER B 431      52.952  20.846  -7.823  1.00 40.56           C  
ANISOU 5027  CA  SER B 431     5959   5812   3640  -1077   1168   -499       C  
ATOM   5028  C   SER B 431      53.788  19.576  -7.846  1.00 39.33           C  
ANISOU 5028  C   SER B 431     5627   5766   3549  -1020   1260   -664       C  
ATOM   5029  O   SER B 431      55.007  19.647  -8.007  1.00 40.06           O  
ANISOU 5029  O   SER B 431     5611   5944   3667  -1101   1462   -762       O  
ATOM   5030  CB  SER B 431      53.010  21.463  -6.417  1.00 40.00           C  
ANISOU 5030  CB  SER B 431     5716   5715   3768  -1068   1102   -472       C  
ATOM   5031  OG  SER B 431      52.685  22.854  -6.402  1.00 37.58           O  
ANISOU 5031  OG  SER B 431     5553   5309   3416  -1155   1095   -347       O  
ATOM   5032  N   PHE B 432      53.168  18.413  -7.680  1.00 33.26           N  
ANISOU 5032  N   PHE B 432     4825   4992   2819   -885   1121   -708       N  
ATOM   5033  CA  PHE B 432      53.905  17.169  -7.556  1.00 39.40           C  
ANISOU 5033  CA  PHE B 432     5448   5845   3679   -799   1183   -861       C  
ATOM   5034  C   PHE B 432      53.908  16.340  -8.835  1.00 43.41           C  
ANISOU 5034  C   PHE B 432     6094   6379   4022   -790   1250   -940       C  
ATOM   5035  O   PHE B 432      54.474  15.243  -8.842  1.00 38.50           O  
ANISOU 5035  O   PHE B 432     5367   5803   3457   -704   1301  -1077       O  
ATOM   5036  CB  PHE B 432      53.375  16.351  -6.357  1.00 28.87           C  
ANISOU 5036  CB  PHE B 432     3987   4467   2515   -655   1010   -869       C  
ATOM   5037  CG  PHE B 432      53.932  16.822  -5.030  1.00 34.83           C  
ANISOU 5037  CG  PHE B 432     4548   5244   3442   -633    997   -866       C  
ATOM   5038  CD1 PHE B 432      55.162  16.365  -4.578  1.00 28.74           C  
ANISOU 5038  CD1 PHE B 432     3576   4564   2779   -577   1085   -998       C  
ATOM   5039  CD2 PHE B 432      53.264  17.776  -4.285  1.00 28.18           C  
ANISOU 5039  CD2 PHE B 432     3723   4341   2645   -665    894   -747       C  
ATOM   5040  CE1 PHE B 432      55.685  16.829  -3.374  1.00 31.66           C  
ANISOU 5040  CE1 PHE B 432     3771   4967   3293   -552   1051  -1010       C  
ATOM   5041  CE2 PHE B 432      53.773  18.241  -3.081  1.00 30.01           C  
ANISOU 5041  CE2 PHE B 432     3792   4595   3017   -648    877   -756       C  
ATOM   5042  CZ  PHE B 432      54.983  17.772  -2.621  1.00 33.81           C  
ANISOU 5042  CZ  PHE B 432     4078   5171   3596   -594    948   -887       C  
ATOM   5043  N   GLU B 433      53.323  16.845  -9.917  1.00 53.68           N  
ANISOU 5043  N   GLU B 433     7638   7646   5111   -864   1248   -864       N  
ATOM   5044  CA  GLU B 433      53.519  16.262 -11.245  1.00 56.00           C  
ANISOU 5044  CA  GLU B 433     8090   7981   5208   -880   1351   -947       C  
ATOM   5045  C   GLU B 433      54.942  16.512 -11.743  1.00 55.37           C  
ANISOU 5045  C   GLU B 433     7954   8001   5083   -982   1642  -1040       C  
ATOM   5046  O   GLU B 433      55.822  15.662 -11.602  1.00 59.27           O  
ANISOU 5046  O   GLU B 433     8267   8575   5678   -924   1750  -1197       O  
ATOM   5047  CB  GLU B 433      52.514  16.837 -12.245  1.00 63.23           C  
ANISOU 5047  CB  GLU B 433     9305   8837   5883   -921   1253   -835       C  
ATOM   5048  CG  GLU B 433      51.195  16.078 -12.311  1.00 67.97           C  
ANISOU 5048  CG  GLU B 433     9968   9383   6475   -814   1001   -840       C  
TER    5049      GLU B 433                                                      
HETATM 9898  C1 A144 A 301      29.525  54.741  28.906  0.48 36.27           C  
HETATM 9899  C1 B144 A 301      31.148  54.358  27.263  0.52 38.22           C  
HETATM 9900  N  A144 A 301      29.553  54.406  27.474  0.48 37.79           N  
HETATM 9901  N  B144 A 301      29.686  54.559  27.316  0.52 37.50           N  
HETATM 9902  C2 A144 A 301      28.863  53.145  27.210  0.48 34.22           C  
HETATM 9903  C2 B144 A 301      29.177  54.855  28.649  0.52 36.27           C  
HETATM 9904  O2 A144 A 301      29.160  52.215  28.252  0.48 27.79           O  
HETATM 9905  O2 B144 A 301      30.150  54.727  29.661  0.52 38.12           O  
HETATM 9906  C3 A144 A 301      28.819  55.426  26.765  0.48 36.67           C  
HETATM 9907  C3 B144 A 301      29.287  55.710  26.510  0.52 34.72           C  
HETATM 9908  O3 A144 A 301      27.514  55.411  27.335  0.48 28.51           O  
HETATM 9909  O3 B144 A 301      30.131  55.901  25.383  0.52 27.08           O  
HETATM 9910  C4 A144 A 301      30.894  54.286  26.909  0.48 36.59           C  
HETATM 9911  C4 B144 A 301      28.989  53.335  26.922  0.52 34.69           C  
HETATM 9912  O4 A144 A 301      31.909  54.717  27.799  0.48 34.56           O  
HETATM 9913  O4 B144 A 301      28.560  53.365  25.569  0.52 31.71           O  
HETATM 9914  C1  PEG A 302      51.637  52.116  44.310  1.00 56.02           C  
HETATM 9915  O1  PEG A 302      51.358  51.371  45.463  1.00 57.01           O  
HETATM 9916  C2  PEG A 302      50.314  52.638  43.748  1.00 67.35           C  
HETATM 9917  O2  PEG A 302      50.080  52.085  42.481  1.00 71.75           O  
HETATM 9918  C3  PEG A 302      50.809  52.683  41.442  1.00 71.80           C  
HETATM 9919  C4  PEG A 302      51.571  51.593  40.688  1.00 70.09           C  
HETATM 9920  O4  PEG A 302      50.940  50.371  40.943  1.00 63.64           O  
HETATM 9921 ZN    ZN B 501      30.142 -25.016  15.405  1.00 40.05          ZN  
HETATM 9922 MG    MG B 502      45.511   1.393  16.316  1.00 43.60          MG  
CONECT 3183 9921                                                                
CONECT 3204 9921                                                                
CONECT 3373 9921                                                                
CONECT 3388 9921                                                                
CONECT 3699 9922                                                                
CONECT 8077 9923                                                                
CONECT 8098 9923                                                                
CONECT 8264 9923                                                                
CONECT 8275 9923                                                                
CONECT 9898 9900                                                                
CONECT 9899 9901                                                                
CONECT 9900 9898 9902 9906 9910                                                 
CONECT 9901 9899 9903 9907 9911                                                 
CONECT 9902 9900 9904                                                           
CONECT 9903 9901 9905                                                           
CONECT 9904 9902                                                                
CONECT 9905 9903                                                                
CONECT 9906 9900 9908                                                           
CONECT 9907 9901 9909                                                           
CONECT 9908 9906                                                                
CONECT 9909 9907                                                                
CONECT 9910 9900 9912                                                           
CONECT 9911 9901 9913                                                           
CONECT 9912 9910                                                                
CONECT 9913 9911                                                                
CONECT 9914 9915 9916                                                           
CONECT 9915 9914                                                                
CONECT 9916 9914 9917                                                           
CONECT 9917 9916 9918                                                           
CONECT 9918 9917 9919                                                           
CONECT 9919 9918 9920                                                           
CONECT 9920 9919                                                                
CONECT 9921 3183 3204 3373 3388                                                 
CONECT 9922 3699100621008610141                                                 
CONECT 9923 8077 8098 8264 8275                                                 
CONECT10062 9922                                                                
CONECT10086 9922                                                                
CONECT10141 9922                                                                
MASTER      514    0    5   47   64    0    9    610355    4   38  108          
END                                                                             


A second structure was input as follows:


HEADER    LIGASE                                  13-FEB-18   6FQB              
TITLE     MURT/GATD PEPTIDOGLYCAN AMIDOTRANSFERASE COMPLEX FROM STREPTOCOCCUS   
TITLE    2 PNEUMONIAE R6                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MUR LIGASE FAMILY PROTEIN;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: UDP-N-ACETYLMURAMYL PEPTIDE SYNTHASE,UDP-N-ACETYLMURAMYL    
COMPND   5 TRIPEPTIDE SYNTHETASE,MUR LIGASE;                                    
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COBYRIC ACID SYNTHASE;                                     
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 SYNONYM: GLUTAMINE AMIDOTRANSFERASE;                                 
COMPND  12 EC: 6.3.5.10;                                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 GENE: A4260_05845, ERS019420_00606, ERS020535_00125,                 
SOURCE   5 ERS021368_00525, ERS022199_00743, ERS043879_01366;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;                                  
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30-HAT;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE  13 ORGANISM_TAXID: 1313;                                                
SOURCE  14 GENE: A4260_05840, AWW74_09320, CHL72_09035, CIT24_04835,            
SOURCE  15 CS877_04020, CSH34_00860, ERS003549_02292, ERS019166_00428,          
SOURCE  16 ERS019416_00232, ERS019420_00605, ERS019499_01955, ERS019595_01427,  
SOURCE  17 ERS020136_01107, ERS020137_00292, ERS020140_00887, ERS020142_00808,  
SOURCE  18 ERS020143_01959, ERS020147_00746, ERS020148_00821, ERS020178_04008,  
SOURCE  19 ERS020408_00223, ERS020474_01302, ERS020521_00204, ERS020522_00778,  
SOURCE  20 ERS020523_00656, ERS020524_01042, ERS020526_00540, ERS020526_04035,  
SOURCE  21 ERS020527_01973, ERS020528_00148, ERS020541_00600, ERS020692_00332,  
SOURCE  22 ERS020827_01405, ERS020831_02169, ERS021300_01369, ERS021447_05442,  
SOURCE  23 ERS021629_07046, ERS021762_02260, ERS021858_02776, ERS022045_06260,  
SOURCE  24 ERS022071_00358, ERS022199_00742, ERS022232_05365, ERS022363_01901,  
SOURCE  25 ERS022390_00924, ERS044004_01668, ERS068943_01580, ERS232497_02277,  
SOURCE  26 ERS232498_04930, ERS232508_01880, ERS409064_00176, ERS558328_00424,  
SOURCE  27 SAMEA1026345_00620, SAMEA2626854_01213, SAMEA2626872_01126;          
SOURCE  28 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  30 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE  31 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;                                  
SOURCE  32 EXPRESSION_SYSTEM_PLASMID: PET30-HAT                                 
KEYWDS    MUR FAMILY, AMIDOTRANSFERASE, CYTOSOLIC, LIGASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.MORLOT,C.CONTRERAS-MARTEL,F.LEISICO,D.STRAUME,K.PETERS,O.A.HEGNAR,  
AUTHOR   2 N.SIMON,A.M.VILLARD,E.BREUKINK,C.GRAVIER-PELLETIER,L.LE CORRE,       
AUTHOR   3 W.VOLLMER,N.PIETRANCOSTA,L.S.HAVARSTEIN,A.ZAPUN                      
REVDAT   2   07-NOV-18 6FQB    1       REMARK                                   
REVDAT   1 2 22-AUG-18 6FQB    0                                                
JRNL        AUTH   C.MORLOT,D.STRAUME,K.PETERS,O.A.HEGNAR,N.SIMON,A.M.VILLARD,  
JRNL        AUTH 2 C.CONTRERAS-MARTEL,F.LEISICO,E.BREUKINK,C.GRAVIER-PELLETIER, 
JRNL        AUTH 3 L.LE CORRE,W.VOLLMER,N.PIETRANCOSTA,L.S.HAVARSTEIN,A.ZAPUN   
JRNL        TITL   STRUCTURE OF THE ESSENTIAL PEPTIDOGLYCAN AMIDOTRANSFERASE    
JRNL        TITL 2 MURT/GATD COMPLEX FROM STREPTOCOCCUS PNEUMONIAE.             
JRNL        REF    NAT COMMUN                    V.   9  3180 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30093673                                                     
JRNL        DOI    10.1038/S41467-018-05602-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 61871                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6854                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4588                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 497                          
REMARK   3   BIN FREE R VALUE                    : 0.5750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19687                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.67000                                             
REMARK   3    B22 (A**2) : -2.67000                                             
REMARK   3    B33 (A**2) : 8.66000                                              
REMARK   3    B12 (A**2) : -1.33000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.405         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.362         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.948        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20115 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 18262 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27279 ; 1.544 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 42415 ; 0.994 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2483 ; 6.833 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   986 ;34.534 ;25.152       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3307 ;16.330 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    81 ;19.381 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3043 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 22558 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3991 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 10004 ; 5.719 ; 8.604       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 10003 ; 5.718 ; 8.604       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12463 ; 8.676 ;12.894       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 12464 ; 8.676 ;12.894       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 10111 ; 5.784 ; 9.048       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 10108 ; 5.779 ; 9.047       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 14817 ; 8.916 ;13.409       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 21684 ;11.634 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 21685 ;11.634 ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 12                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    43    438       B    43    438   23046  0.08  0.05     
REMARK   3    2     A    43    438       C    43    438   23118  0.06  0.05     
REMARK   3    3     A    43    439       D    43    439   23208  0.07  0.05     
REMARK   3    4     E     1    247       F     1    247   16116  0.06  0.05     
REMARK   3    5     E     1    247       G     1    247   16102  0.07  0.05     
REMARK   3    6     E     1    247       H     1    247   16022  0.07  0.05     
REMARK   3    7     B    43    438       C    43    438   22926  0.07  0.05     
REMARK   3    8     B    43    438       D    43    438   22850  0.08  0.05     
REMARK   3    9     F     1    247       G     1    247   16062  0.06  0.05     
REMARK   3   10     F     1    247       H     1    247   16002  0.07  0.05     
REMARK   3   11     C    43    437       D    43    437   22968  0.08  0.05     
REMARK   3   12     G     1    247       H     1    247   16008  0.08  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6FQB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008721.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 193.15                             
REMARK 200  PH                             : 6.0-6.2                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96500                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68725                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200   FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.44700                            
REMARK 200   FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M TRI-SODIUM CITRATE PH 6.1 14%      
REMARK 280  PEG 3350 4 MM NISO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      144.21500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       83.26257            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       38.36667            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000      144.21500            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       83.26257            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.36667            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000      144.21500            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       83.26257            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.36667            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      166.52514            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       76.73333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      166.52514            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       76.73333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      166.52514            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       76.73333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 2290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
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   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ASN A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     TYR A    -5                                                      
REMARK 465     PHE A    -4                                                      
REMARK 465     GLN A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     PHE A    17                                                      
REMARK 465     VAL A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     VAL A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     LEU A    34                                                      
REMARK 465     GLN A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     ASP A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     ILE A    40                                                      
REMARK 465     LEU A    41                                                      
REMARK 465     GLN A    42                                                      
REMARK 465     PHE A    94                                                      
REMARK 465     LEU A    95                                                      
REMARK 465     THR A    96                                                      
REMARK 465     ALA A    97                                                      
REMARK 465     LYS A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     SER A   100                                                      
REMARK 465     LYS A   101                                                      
REMARK 465     THR A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     MET A   138                                                      
REMARK 465     ASP A   139                                                      
REMARK 465     ARG A   140                                                      
REMARK 465     PHE A   141                                                      
REMARK 465     GLN A   440                                                      
REMARK 465     ILE A   441                                                      
REMARK 465     VAL A   442                                                      
REMARK 465     ARG A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     MET A   446                                                      
REMARK 465     ASN A   447                                                      
REMARK 465     GLU E   248                                                      
REMARK 465     GLU E   249                                                      
REMARK 465     TYR E   250                                                      
REMARK 465     SER E   251                                                      
REMARK 465     ASP E   252                                                      
REMARK 465     VAL E   253                                                      
REMARK 465     LYS E   254                                                      
REMARK 465     SER E   255                                                      
REMARK 465     LYS E   256                                                      
REMARK 465     ALA E   257                                                      
REMARK 465     ASP E   258                                                      
REMARK 465     PHE E   259                                                      
REMARK 465     SER E   260                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ASN B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     PHE B    -4                                                      
REMARK 465     GLN B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     PHE B    17                                                      
REMARK 465     VAL B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ARG B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     VAL B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     PHE B    36                                                      
REMARK 465     ASP B    37                                                      
REMARK 465     LYS B    38                                                      
REMARK 465     ASP B    39                                                      
REMARK 465     ILE B    40                                                      
REMARK 465     LEU B    41                                                      
REMARK 465     GLN B    42                                                      
REMARK 465     SER B    82                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     THR B    92                                                      
REMARK 465     THR B    93                                                      
REMARK 465     PHE B    94                                                      
REMARK 465     LEU B    95                                                      
REMARK 465     THR B    96                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     LYS B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     LYS B   101                                                      
REMARK 465     THR B   102                                                      
REMARK 465     GLY B   103                                                      
REMARK 465     MET B   138                                                      
REMARK 465     ASP B   139                                                      
REMARK 465     ARG B   140                                                      
REMARK 465     PHE B   141                                                      
REMARK 465     ARG B   439                                                      
REMARK 465     GLN B   440                                                      
REMARK 465     ILE B   441                                                      
REMARK 465     VAL B   442                                                      
REMARK 465     ARG B   443                                                      
REMARK 465     LYS B   444                                                      
REMARK 465     GLU B   445                                                      
REMARK 465     MET B   446                                                      
REMARK 465     ASN B   447                                                      
REMARK 465     GLU F   248                                                      
REMARK 465     GLU F   249                                                      
REMARK 465     TYR F   250                                                      
REMARK 465     SER F   251                                                      
REMARK 465     ASP F   252                                                      
REMARK 465     VAL F   253                                                      
REMARK 465     LYS F   254                                                      
REMARK 465     SER F   255                                                      
REMARK 465     LYS F   256                                                      
REMARK 465     ALA F   257                                                      
REMARK 465     ASP F   258                                                      
REMARK 465     PHE F   259                                                      
REMARK 465     SER F   260                                                      
REMARK 465     MET C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     GLU C    -8                                                      
REMARK 465     ASN C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     TYR C    -5                                                      
REMARK 465     PHE C    -4                                                      
REMARK 465     GLN C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     LEU C     9                                                      
REMARK 465     LEU C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     SER C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     PHE C    17                                                      
REMARK 465     VAL C    18                                                      
REMARK 465     LEU C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ARG C    21                                                      
REMARK 465     LEU C    22                                                      
REMARK 465     GLY C    23                                                      
REMARK 465     ARG C    24                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     SER C    26                                                      
REMARK 465     THR C    27                                                      
REMARK 465     LEU C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     GLY C    30                                                      
REMARK 465     LYS C    31                                                      
REMARK 465     VAL C    32                                                      
REMARK 465     ALA C    33                                                      
REMARK 465     LEU C    34                                                      
REMARK 465     GLN C    35                                                      
REMARK 465     PHE C    36                                                      
REMARK 465     ASP C    37                                                      
REMARK 465     LYS C    38                                                      
REMARK 465     ASP C    39                                                      
REMARK 465     ILE C    40                                                      
REMARK 465     LEU C    41                                                      
REMARK 465     GLN C    42                                                      
REMARK 465     GLY C    83                                                      
REMARK 465     ALA C    84                                                      
REMARK 465     ALA C    91                                                      
REMARK 465     THR C    92                                                      
REMARK 465     THR C    93                                                      
REMARK 465     PHE C    94                                                      
REMARK 465     LEU C    95                                                      
REMARK 465     THR C    96                                                      
REMARK 465     ALA C    97                                                      
REMARK 465     LYS C    98                                                      
REMARK 465     SER C    99                                                      
REMARK 465     SER C   100                                                      
REMARK 465     LYS C   101                                                      
REMARK 465     THR C   102                                                      
REMARK 465     GLY C   103                                                      
REMARK 465     LYS C   104                                                      
REMARK 465     MET C   138                                                      
REMARK 465     ASP C   139                                                      
REMARK 465     ARG C   140                                                      
REMARK 465     PHE C   141                                                      
REMARK 465     GLY C   142                                                      
REMARK 465     ARG C   439                                                      
REMARK 465     GLN C   440                                                      
REMARK 465     ILE C   441                                                      
REMARK 465     VAL C   442                                                      
REMARK 465     ARG C   443                                                      
REMARK 465     LYS C   444                                                      
REMARK 465     GLU C   445                                                      
REMARK 465     MET C   446                                                      
REMARK 465     ASN C   447                                                      
REMARK 465     GLU G   248                                                      
REMARK 465     GLU G   249                                                      
REMARK 465     TYR G   250                                                      
REMARK 465     SER G   251                                                      
REMARK 465     ASP G   252                                                      
REMARK 465     VAL G   253                                                      
REMARK 465     LYS G   254                                                      
REMARK 465     SER G   255                                                      
REMARK 465     LYS G   256                                                      
REMARK 465     ALA G   257                                                      
REMARK 465     ASP G   258                                                      
REMARK 465     PHE G   259                                                      
REMARK 465     SER G   260                                                      
REMARK 465     MET D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     GLU D    -8                                                      
REMARK 465     ASN D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     TYR D    -5                                                      
REMARK 465     PHE D    -4                                                      
REMARK 465     GLN D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     LEU D    10                                                      
REMARK 465     ALA D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     ARG D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     PHE D    17                                                      
REMARK 465     VAL D    18                                                      
REMARK 465     LEU D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     ARG D    21                                                      
REMARK 465     LEU D    22                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     ARG D    24                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     SER D    26                                                      
REMARK 465     THR D    27                                                      
REMARK 465     LEU D    28                                                      
REMARK 465     PRO D    29                                                      
REMARK 465     GLY D    30                                                      
REMARK 465     LYS D    31                                                      
REMARK 465     VAL D    32                                                      
REMARK 465     ALA D    33                                                      
REMARK 465     LEU D    34                                                      
REMARK 465     GLN D    35                                                      
REMARK 465     PHE D    36                                                      
REMARK 465     ASP D    37                                                      
REMARK 465     LYS D    38                                                      
REMARK 465     ASP D    39                                                      
REMARK 465     ILE D    40                                                      
REMARK 465     LEU D    41                                                      
REMARK 465     GLN D    42                                                      
REMARK 465     GLY D    83                                                      
REMARK 465     ALA D    84                                                      
REMARK 465     THR D    93                                                      
REMARK 465     PHE D    94                                                      
REMARK 465     LEU D    95                                                      
REMARK 465     THR D    96                                                      
REMARK 465     ALA D    97                                                      
REMARK 465     LYS D    98                                                      
REMARK 465     SER D    99                                                      
REMARK 465     SER D   100                                                      
REMARK 465     LYS D   101                                                      
REMARK 465     THR D   102                                                      
REMARK 465     GLY D   103                                                      
REMARK 465     LYS D   104                                                      
REMARK 465     MET D   138                                                      
REMARK 465     ASP D   139                                                      
REMARK 465     ARG D   140                                                      
REMARK 465     PHE D   141                                                      
REMARK 465     GLY D   142                                                      
REMARK 465     VAL D   442                                                      
REMARK 465     ARG D   443                                                      
REMARK 465     LYS D   444                                                      
REMARK 465     GLU D   445                                                      
REMARK 465     MET D   446                                                      
REMARK 465     ASN D   447                                                      
REMARK 465     GLU H   248                                                      
REMARK 465     GLU H   249                                                      
REMARK 465     TYR H   250                                                      
REMARK 465     SER H   251                                                      
REMARK 465     ASP H   252                                                      
REMARK 465     VAL H   253                                                      
REMARK 465     LYS H   254                                                      
REMARK 465     SER H   255                                                      
REMARK 465     LYS H   256                                                      
REMARK 465     ALA H   257                                                      
REMARK 465     ASP H   258                                                      
REMARK 465     PHE H   259                                                      
REMARK 465     SER H   260                                                      
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     SER B  43    OG                                                  
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   OH   TYR E   116     OH   TYR G   116              1.92            
REMARK 500   O    PRO B    81     N    GLY B    83              2.07            
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   OH   TYR F   116     OH   TYR H   116     2555     2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 205   CA  -  CB  -  SG  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    CYS A 227   CA  -  CB  -  SG  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    CYS B 205   CA  -  CB  -  SG  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    CYS B 227   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    CYS C 205   CA  -  CB  -  SG  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    CYS C 227   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    CYS D 205   CA  -  CB  -  SG  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    CYS D 227   CA  -  CB  -  SG  ANGL. DEV. =   8.5 DEGREES          
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    ASN A  47       33.12    -79.45                                   
REMARK 500    SER A  82     -134.60     47.34                                   
REMARK 500    ASN A  85     -109.32   -107.59                                   
REMARK 500    ILE A  87       37.70    -95.70                                   
REMARK 500    CYS A 120       -2.49    -51.51                                   
REMARK 500    TYR A 122      -70.53    -75.50                                   
REMARK 500    ASN A 132      165.76    172.90                                   
REMARK 500    TYR A 173      117.00   -163.67                                   
REMARK 500    LYS A 174       61.60     39.85                                   
REMARK 500    ASP A 207      -71.12    -99.28                                   
REMARK 500    THR A 218      -79.04    -74.30                                   
REMARK 500    ALA A 220     -128.37     52.19                                   
REMARK 500    LEU A 247      105.77   -163.62                                   
REMARK 500    GLN A 264       37.90    -93.50                                   
REMARK 500    ASN A 349     -168.43   -174.36                                   
REMARK 500    ARG A 381       35.26    -93.31                                   
REMARK 500    LEU A 436       26.83    -78.07                                   
REMARK 500    SER E  56     -139.16   -124.11                                   
REMARK 500    CYS E 107     -119.72     47.08                                   
REMARK 500    ASN E 141      144.43   -176.04                                   
REMARK 500    ASP E 155       62.40     38.07                                   
REMARK 500    ASN E 163       87.82   -161.84                                   
REMARK 500    VAL E 191      -63.86    -98.55                                   
REMARK 500    TYR E 197      -74.16    -91.15                                   
REMARK 500    LYS E 198       99.71   -162.53                                   
REMARK 500    ASN E 199       11.03     58.70                                   
REMARK 500    ILE E 233      153.16    -48.45                                   
REMARK 500    ASN B  47       54.72   -100.25                                   
REMARK 500    ASN B  85     -122.56   -115.78                                   
REMARK 500    TYR B 122      -70.25    -76.47                                   
REMARK 500    ASN B 132      165.25    173.49                                   
REMARK 500    ASP B 136     -148.73   -121.07                                   
REMARK 500    GLU B 143      -48.01   -135.31                                   
REMARK 500    TYR B 173      116.78   -164.22                                   
REMARK 500    ASP B 207      -71.25    -99.41                                   
REMARK 500    THR B 218      -76.97    -74.16                                   
REMARK 500    ALA B 220     -132.11     51.78                                   
REMARK 500    LEU B 247      105.54   -163.19                                   
REMARK 500    GLN B 264       39.52    -92.75                                   
REMARK 500    ASN B 349     -168.01   -173.43                                   
REMARK 500    ARG B 381       35.16    -92.68                                   
REMARK 500    HIS B 382      -36.78    -39.82                                   
REMARK 500    LEU B 436       37.10    -93.59                                   
REMARK 500    ALA B 437       57.55   -152.10                                   
REMARK 500    SER F  56     -132.54   -121.26                                   
REMARK 500    HIS F  58        5.55     49.20                                   
REMARK 500    CYS F 107     -119.22     46.66                                   
REMARK 500    ASN F 141      144.48   -176.96                                   
REMARK 500    ASP F 155       62.20     37.93                                   
REMARK 500    ASN F 163       95.53   -161.70                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLN E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLN F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLN G 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GLN H 301                 
CISPEP   1 GLY E  207    PRO E  208          0         0.55                     
CISPEP   2 GLY F  207    PRO F  208          0         2.43                     
CISPEP   3 GLY G  207    PRO G  208          0         3.96                     
CISPEP   4 GLY H  207    PRO H  208          0         3.10                     
DBREF1 6FQB A    1   447  UNP                  A0A0B7LND9_STREE                 
DBREF2 6FQB A     A0A0B7LND9                          1         447             
DBREF1 6FQB E    1   260  UNP                  A0A062WUX3_STREE                 
DBREF2 6FQB E     A0A062WUX3                          1         260             
DBREF1 6FQB B    1   447  UNP                  A0A0B7LND9_STREE                 
DBREF2 6FQB B     A0A0B7LND9                          1         447             
DBREF1 6FQB F    1   260  UNP                  A0A062WUX3_STREE                 
DBREF2 6FQB F     A0A062WUX3                          1         260             
DBREF1 6FQB C    1   447  UNP                  A0A0B7LND9_STREE                 
DBREF2 6FQB C     A0A0B7LND9                          1         447             
DBREF1 6FQB G    1   260  UNP                  A0A062WUX3_STREE                 
DBREF2 6FQB G     A0A062WUX3                          1         260             
DBREF1 6FQB D    1   447  UNP                  A0A0B7LND9_STREE                 
DBREF2 6FQB D     A0A0B7LND9                          1         447             
DBREF1 6FQB H    1   260  UNP                  A0A062WUX3_STREE                 
DBREF2 6FQB H     A0A062WUX3                          1         260             
SEQADV 6FQB MET A  -17  UNP  A0A0B7LND           INITIATING METHIONINE          
SEQADV 6FQB HIS A  -16  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A  -15  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A  -14  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A  -13  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A  -12  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A  -11  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A  -10  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A   -9  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLU A   -8  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB ASN A   -7  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB LEU A   -6  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB TYR A   -5  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB PHE A   -4  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLN A   -3  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLY A   -2  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB SER A   -1  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS A    0  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB MET B  -17  UNP  A0A0B7LND           INITIATING METHIONINE          
SEQADV 6FQB HIS B  -16  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B  -15  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B  -14  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B  -13  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B  -12  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B  -11  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B  -10  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B   -9  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLU B   -8  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB ASN B   -7  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB LEU B   -6  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB TYR B   -5  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB PHE B   -4  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLN B   -3  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLY B   -2  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB SER B   -1  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS B    0  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB MET C  -17  UNP  A0A0B7LND           INITIATING METHIONINE          
SEQADV 6FQB HIS C  -16  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C  -15  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C  -14  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C  -13  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C  -12  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C  -11  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C  -10  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C   -9  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLU C   -8  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB ASN C   -7  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB LEU C   -6  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB TYR C   -5  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB PHE C   -4  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLN C   -3  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLY C   -2  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB SER C   -1  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS C    0  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB MET D  -17  UNP  A0A0B7LND           INITIATING METHIONINE          
SEQADV 6FQB HIS D  -16  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D  -15  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D  -14  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D  -13  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D  -12  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D  -11  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D  -10  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D   -9  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLU D   -8  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB ASN D   -7  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB LEU D   -6  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB TYR D   -5  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB PHE D   -4  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLN D   -3  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB GLY D   -2  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB SER D   -1  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQADV 6FQB HIS D    0  UNP  A0A0B7LND           EXPRESSION TAG                 
SEQRES   1 A  465  MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR          
SEQRES   2 A  465  PHE GLN GLY SER HIS MET ASN LEU LYS THR THR LEU GLY          
SEQRES   3 A  465  LEU LEU ALA GLY ARG SER SER HIS PHE VAL LEU SER ARG          
SEQRES   4 A  465  LEU GLY ARG GLY SER THR LEU PRO GLY LYS VAL ALA LEU          
SEQRES   5 A  465  GLN PHE ASP LYS ASP ILE LEU GLN SER LEU ALA LYS ASN          
SEQRES   6 A  465  TYR GLU ILE VAL VAL VAL THR GLY THR ASN GLY LYS THR          
SEQRES   7 A  465  LEU THR THR ALA LEU THR VAL GLY ILE LEU LYS GLU VAL          
SEQRES   8 A  465  TYR GLY GLN VAL LEU THR ASN PRO SER GLY ALA ASN MET          
SEQRES   9 A  465  ILE THR GLY ILE ALA THR THR PHE LEU THR ALA LYS SER          
SEQRES  10 A  465  SER LYS THR GLY LYS ASN ILE ALA VAL LEU GLU ILE ASP          
SEQRES  11 A  465  GLU ALA SER LEU SER ARG ILE CYS ASP TYR ILE GLN PRO          
SEQRES  12 A  465  SER LEU PHE VAL ILE THR ASN ILE PHE ARG ASP GLN MET          
SEQRES  13 A  465  ASP ARG PHE GLY GLU ILE TYR THR THR TYR ASN MET ILE          
SEQRES  14 A  465  LEU ASP ALA ILE ARG LYS VAL PRO THR ALA THR VAL LEU          
SEQRES  15 A  465  LEU ASN GLY ASP SER PRO LEU PHE TYR LYS PRO THR ILE          
SEQRES  16 A  465  PRO ASN PRO ILE GLU TYR PHE GLY PHE ASP LEU GLU LYS          
SEQRES  17 A  465  GLY PRO ALA GLN LEU ALA HIS TYR ASN THR GLU GLY ILE          
SEQRES  18 A  465  LEU CYS PRO ASP CYS GLN GLY ILE LEU LYS TYR GLU HIS          
SEQRES  19 A  465  ASN THR TYR ALA ASN LEU GLY ALA TYR ILE CYS GLU GLY          
SEQRES  20 A  465  CYS GLY CYS LYS ARG PRO ASP LEU ASP TYR ARG LEU THR          
SEQRES  21 A  465  LYS LEU VAL GLU LEU THR ASN ASN ARG SER ARG PHE VAL          
SEQRES  22 A  465  ILE ASP GLY GLN GLU TYR GLY ILE GLN ILE GLY GLY LEU          
SEQRES  23 A  465  TYR ASN ILE TYR ASN ALA LEU ALA ALA VAL ALA ILE ALA          
SEQRES  24 A  465  ARG PHE LEU GLY ALA ASP SER GLN LEU ILE LYS GLN GLY          
SEQRES  25 A  465  PHE ASP LYS SER ARG ALA VAL PHE GLY ARG GLN GLU THR          
SEQRES  26 A  465  PHE HIS ILE GLY ASP LYS GLU CYS THR LEU VAL LEU ILE          
SEQRES  27 A  465  LYS ASN PRO VAL GLY ALA THR GLN ALA ILE GLU MET ILE          
SEQRES  28 A  465  LYS LEU ALA PRO TYR PRO PHE SER LEU SER VAL LEU LEU          
SEQRES  29 A  465  ASN ALA ASN TYR ALA ASP GLY ILE ASP THR SER TRP ILE          
SEQRES  30 A  465  TRP ASP ALA ASP PHE GLU GLN ILE THR ASP MET ASP ILE          
SEQRES  31 A  465  PRO GLU ILE ASN ALA GLY GLY VAL ARG HIS SER GLU ILE          
SEQRES  32 A  465  ALA ARG ARG LEU ARG VAL THR GLY TYR PRO ALA GLU LYS          
SEQRES  33 A  465  ILE THR GLU THR SER ASN LEU GLU GLN VAL LEU LYS THR          
SEQRES  34 A  465  ILE GLU ASN GLN ASP CYS LYS HIS ALA TYR ILE LEU ALA          
SEQRES  35 A  465  THR TYR THR ALA MET LEU GLU PHE ARG GLU LEU LEU ALA          
SEQRES  36 A  465  SER ARG GLN ILE VAL ARG LYS GLU MET ASN                      
SEQRES   1 E  260  MET VAL TYR THR SER LEU SER SER LYS ASP GLY ASN TYR          
SEQRES   2 E  260  PRO TYR GLN LEU ASN ILE ALA HIS LEU TYR GLY ASN LEU          
SEQRES   3 E  260  MET ASN THR TYR GLY ASP ASN GLY ASN ILE LEU MET LEU          
SEQRES   4 E  260  LYS TYR VAL ALA GLU LYS LEU GLY ALA HIS VAL THR VAL          
SEQRES   5 E  260  ASP ILE VAL SER LEU HIS ASP ASP PHE ASP GLU ASN HIS          
SEQRES   6 E  260  TYR ASP ILE ALA PHE PHE GLY GLY GLY GLN ASP PHE GLU          
SEQRES   7 E  260  GLN SER ILE ILE ALA ASP ASP LEU PRO ALA LYS LYS GLU          
SEQRES   8 E  260  SER ILE ASP ASN TYR ILE GLN ASN ASP GLY VAL VAL LEU          
SEQRES   9 E  260  ALA ILE CYS GLY GLY PHE GLN LEU LEU GLY GLN TYR TYR          
SEQRES  10 E  260  VAL GLU ALA SER GLY LYS ARG ILE GLU GLY LEU GLY VAL          
SEQRES  11 E  260  MET GLY HIS TYR THR LEU ASN GLN THR ASN ASN ARG PHE          
SEQRES  12 E  260  ILE GLY ASP ILE LYS ILE HIS ASN GLU ASP PHE ASP GLU          
SEQRES  13 E  260  THR TYR TYR GLY PHE GLU ASN HIS GLN GLY ARG THR PHE          
SEQRES  14 E  260  LEU SER ASP ASP GLN LYS PRO LEU GLY GLN VAL VAL TYR          
SEQRES  15 E  260  GLY ASN GLY ASN ASN GLU GLU LYS VAL GLY GLU GLY VAL          
SEQRES  16 E  260  HIS TYR LYS ASN VAL PHE GLY SER TYR PHE HIS GLY PRO          
SEQRES  17 E  260  ILE LEU SER ARG ASN ALA ASN LEU ALA TYR ARG LEU VAL          
SEQRES  18 E  260  THR THR ALA LEU LYS LYS LYS TYR GLY GLN ASP ILE GLN          
SEQRES  19 E  260  LEU PRO ALA TYR GLU ASP ILE LEU SER GLN GLU ILE ALA          
SEQRES  20 E  260  GLU GLU TYR SER ASP VAL LYS SER LYS ALA ASP PHE SER          
SEQRES   1 B  465  MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR          
SEQRES   2 B  465  PHE GLN GLY SER HIS MET ASN LEU LYS THR THR LEU GLY          
SEQRES   3 B  465  LEU LEU ALA GLY ARG SER SER HIS PHE VAL LEU SER ARG          
SEQRES   4 B  465  LEU GLY ARG GLY SER THR LEU PRO GLY LYS VAL ALA LEU          
SEQRES   5 B  465  GLN PHE ASP LYS ASP ILE LEU GLN SER LEU ALA LYS ASN          
SEQRES   6 B  465  TYR GLU ILE VAL VAL VAL THR GLY THR ASN GLY LYS THR          
SEQRES   7 B  465  LEU THR THR ALA LEU THR VAL GLY ILE LEU LYS GLU VAL          
SEQRES   8 B  465  TYR GLY GLN VAL LEU THR ASN PRO SER GLY ALA ASN MET          
SEQRES   9 B  465  ILE THR GLY ILE ALA THR THR PHE LEU THR ALA LYS SER          
SEQRES  10 B  465  SER LYS THR GLY LYS ASN ILE ALA VAL LEU GLU ILE ASP          
SEQRES  11 B  465  GLU ALA SER LEU SER ARG ILE CYS ASP TYR ILE GLN PRO          
SEQRES  12 B  465  SER LEU PHE VAL ILE THR ASN ILE PHE ARG ASP GLN MET          
SEQRES  13 B  465  ASP ARG PHE GLY GLU ILE TYR THR THR TYR ASN MET ILE          
SEQRES  14 B  465  LEU ASP ALA ILE ARG LYS VAL PRO THR ALA THR VAL LEU          
SEQRES  15 B  465  LEU ASN GLY ASP SER PRO LEU PHE TYR LYS PRO THR ILE          
SEQRES  16 B  465  PRO ASN PRO ILE GLU TYR PHE GLY PHE ASP LEU GLU LYS          
SEQRES  17 B  465  GLY PRO ALA GLN LEU ALA HIS TYR ASN THR GLU GLY ILE          
SEQRES  18 B  465  LEU CYS PRO ASP CYS GLN GLY ILE LEU LYS TYR GLU HIS          
SEQRES  19 B  465  ASN THR TYR ALA ASN LEU GLY ALA TYR ILE CYS GLU GLY          
SEQRES  20 B  465  CYS GLY CYS LYS ARG PRO ASP LEU ASP TYR ARG LEU THR          
SEQRES  21 B  465  LYS LEU VAL GLU LEU THR ASN ASN ARG SER ARG PHE VAL          
SEQRES  22 B  465  ILE ASP GLY GLN GLU TYR GLY ILE GLN ILE GLY GLY LEU          
SEQRES  23 B  465  TYR ASN ILE TYR ASN ALA LEU ALA ALA VAL ALA ILE ALA          
SEQRES  24 B  465  ARG PHE LEU GLY ALA ASP SER GLN LEU ILE LYS GLN GLY          
SEQRES  25 B  465  PHE ASP LYS SER ARG ALA VAL PHE GLY ARG GLN GLU THR          
SEQRES  26 B  465  PHE HIS ILE GLY ASP LYS GLU CYS THR LEU VAL LEU ILE          
SEQRES  27 B  465  LYS ASN PRO VAL GLY ALA THR GLN ALA ILE GLU MET ILE          
SEQRES  28 B  465  LYS LEU ALA PRO TYR PRO PHE SER LEU SER VAL LEU LEU          
SEQRES  29 B  465  ASN ALA ASN TYR ALA ASP GLY ILE ASP THR SER TRP ILE          
SEQRES  30 B  465  TRP ASP ALA ASP PHE GLU GLN ILE THR ASP MET ASP ILE          
SEQRES  31 B  465  PRO GLU ILE ASN ALA GLY GLY VAL ARG HIS SER GLU ILE          
SEQRES  32 B  465  ALA ARG ARG LEU ARG VAL THR GLY TYR PRO ALA GLU LYS          
SEQRES  33 B  465  ILE THR GLU THR SER ASN LEU GLU GLN VAL LEU LYS THR          
SEQRES  34 B  465  ILE GLU ASN GLN ASP CYS LYS HIS ALA TYR ILE LEU ALA          
SEQRES  35 B  465  THR TYR THR ALA MET LEU GLU PHE ARG GLU LEU LEU ALA          
SEQRES  36 B  465  SER ARG GLN ILE VAL ARG LYS GLU MET ASN                      
SEQRES   1 F  260  MET VAL TYR THR SER LEU SER SER LYS ASP GLY ASN TYR          
SEQRES   2 F  260  PRO TYR GLN LEU ASN ILE ALA HIS LEU TYR GLY ASN LEU          
SEQRES   3 F  260  MET ASN THR TYR GLY ASP ASN GLY ASN ILE LEU MET LEU          
SEQRES   4 F  260  LYS TYR VAL ALA GLU LYS LEU GLY ALA HIS VAL THR VAL          
SEQRES   5 F  260  ASP ILE VAL SER LEU HIS ASP ASP PHE ASP GLU ASN HIS          
SEQRES   6 F  260  TYR ASP ILE ALA PHE PHE GLY GLY GLY GLN ASP PHE GLU          
SEQRES   7 F  260  GLN SER ILE ILE ALA ASP ASP LEU PRO ALA LYS LYS GLU          
SEQRES   8 F  260  SER ILE ASP ASN TYR ILE GLN ASN ASP GLY VAL VAL LEU          
SEQRES   9 F  260  ALA ILE CYS GLY GLY PHE GLN LEU LEU GLY GLN TYR TYR          
SEQRES  10 F  260  VAL GLU ALA SER GLY LYS ARG ILE GLU GLY LEU GLY VAL          
SEQRES  11 F  260  MET GLY HIS TYR THR LEU ASN GLN THR ASN ASN ARG PHE          
SEQRES  12 F  260  ILE GLY ASP ILE LYS ILE HIS ASN GLU ASP PHE ASP GLU          
SEQRES  13 F  260  THR TYR TYR GLY PHE GLU ASN HIS GLN GLY ARG THR PHE          
SEQRES  14 F  260  LEU SER ASP ASP GLN LYS PRO LEU GLY GLN VAL VAL TYR          
SEQRES  15 F  260  GLY ASN GLY ASN ASN GLU GLU LYS VAL GLY GLU GLY VAL          
SEQRES  16 F  260  HIS TYR LYS ASN VAL PHE GLY SER TYR PHE HIS GLY PRO          
SEQRES  17 F  260  ILE LEU SER ARG ASN ALA ASN LEU ALA TYR ARG LEU VAL          
SEQRES  18 F  260  THR THR ALA LEU LYS LYS LYS TYR GLY GLN ASP ILE GLN          
SEQRES  19 F  260  LEU PRO ALA TYR GLU ASP ILE LEU SER GLN GLU ILE ALA          
SEQRES  20 F  260  GLU GLU TYR SER ASP VAL LYS SER LYS ALA ASP PHE SER          
SEQRES   1 C  465  MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR          
SEQRES   2 C  465  PHE GLN GLY SER HIS MET ASN LEU LYS THR THR LEU GLY          
SEQRES   3 C  465  LEU LEU ALA GLY ARG SER SER HIS PHE VAL LEU SER ARG          
SEQRES   4 C  465  LEU GLY ARG GLY SER THR LEU PRO GLY LYS VAL ALA LEU          
SEQRES   5 C  465  GLN PHE ASP LYS ASP ILE LEU GLN SER LEU ALA LYS ASN          
SEQRES   6 C  465  TYR GLU ILE VAL VAL VAL THR GLY THR ASN GLY LYS THR          
SEQRES   7 C  465  LEU THR THR ALA LEU THR VAL GLY ILE LEU LYS GLU VAL          
SEQRES   8 C  465  TYR GLY GLN VAL LEU THR ASN PRO SER GLY ALA ASN MET          
SEQRES   9 C  465  ILE THR GLY ILE ALA THR THR PHE LEU THR ALA LYS SER          
SEQRES  10 C  465  SER LYS THR GLY LYS ASN ILE ALA VAL LEU GLU ILE ASP          
SEQRES  11 C  465  GLU ALA SER LEU SER ARG ILE CYS ASP TYR ILE GLN PRO          
SEQRES  12 C  465  SER LEU PHE VAL ILE THR ASN ILE PHE ARG ASP GLN MET          
SEQRES  13 C  465  ASP ARG PHE GLY GLU ILE TYR THR THR TYR ASN MET ILE          
SEQRES  14 C  465  LEU ASP ALA ILE ARG LYS VAL PRO THR ALA THR VAL LEU          
SEQRES  15 C  465  LEU ASN GLY ASP SER PRO LEU PHE TYR LYS PRO THR ILE          
SEQRES  16 C  465  PRO ASN PRO ILE GLU TYR PHE GLY PHE ASP LEU GLU LYS          
SEQRES  17 C  465  GLY PRO ALA GLN LEU ALA HIS TYR ASN THR GLU GLY ILE          
SEQRES  18 C  465  LEU CYS PRO ASP CYS GLN GLY ILE LEU LYS TYR GLU HIS          
SEQRES  19 C  465  ASN THR TYR ALA ASN LEU GLY ALA TYR ILE CYS GLU GLY          
SEQRES  20 C  465  CYS GLY CYS LYS ARG PRO ASP LEU ASP TYR ARG LEU THR          
SEQRES  21 C  465  LYS LEU VAL GLU LEU THR ASN ASN ARG SER ARG PHE VAL          
SEQRES  22 C  465  ILE ASP GLY GLN GLU TYR GLY ILE GLN ILE GLY GLY LEU          
SEQRES  23 C  465  TYR ASN ILE TYR ASN ALA LEU ALA ALA VAL ALA ILE ALA          
SEQRES  24 C  465  ARG PHE LEU GLY ALA ASP SER GLN LEU ILE LYS GLN GLY          
SEQRES  25 C  465  PHE ASP LYS SER ARG ALA VAL PHE GLY ARG GLN GLU THR          
SEQRES  26 C  465  PHE HIS ILE GLY ASP LYS GLU CYS THR LEU VAL LEU ILE          
SEQRES  27 C  465  LYS ASN PRO VAL GLY ALA THR GLN ALA ILE GLU MET ILE          
SEQRES  28 C  465  LYS LEU ALA PRO TYR PRO PHE SER LEU SER VAL LEU LEU          
SEQRES  29 C  465  ASN ALA ASN TYR ALA ASP GLY ILE ASP THR SER TRP ILE          
SEQRES  30 C  465  TRP ASP ALA ASP PHE GLU GLN ILE THR ASP MET ASP ILE          
SEQRES  31 C  465  PRO GLU ILE ASN ALA GLY GLY VAL ARG HIS SER GLU ILE          
SEQRES  32 C  465  ALA ARG ARG LEU ARG VAL THR GLY TYR PRO ALA GLU LYS          
SEQRES  33 C  465  ILE THR GLU THR SER ASN LEU GLU GLN VAL LEU LYS THR          
SEQRES  34 C  465  ILE GLU ASN GLN ASP CYS LYS HIS ALA TYR ILE LEU ALA          
SEQRES  35 C  465  THR TYR THR ALA MET LEU GLU PHE ARG GLU LEU LEU ALA          
SEQRES  36 C  465  SER ARG GLN ILE VAL ARG LYS GLU MET ASN                      
SEQRES   1 G  260  MET VAL TYR THR SER LEU SER SER LYS ASP GLY ASN TYR          
SEQRES   2 G  260  PRO TYR GLN LEU ASN ILE ALA HIS LEU TYR GLY ASN LEU          
SEQRES   3 G  260  MET ASN THR TYR GLY ASP ASN GLY ASN ILE LEU MET LEU          
SEQRES   4 G  260  LYS TYR VAL ALA GLU LYS LEU GLY ALA HIS VAL THR VAL          
SEQRES   5 G  260  ASP ILE VAL SER LEU HIS ASP ASP PHE ASP GLU ASN HIS          
SEQRES   6 G  260  TYR ASP ILE ALA PHE PHE GLY GLY GLY GLN ASP PHE GLU          
SEQRES   7 G  260  GLN SER ILE ILE ALA ASP ASP LEU PRO ALA LYS LYS GLU          
SEQRES   8 G  260  SER ILE ASP ASN TYR ILE GLN ASN ASP GLY VAL VAL LEU          
SEQRES   9 G  260  ALA ILE CYS GLY GLY PHE GLN LEU LEU GLY GLN TYR TYR          
SEQRES  10 G  260  VAL GLU ALA SER GLY LYS ARG ILE GLU GLY LEU GLY VAL          
SEQRES  11 G  260  MET GLY HIS TYR THR LEU ASN GLN THR ASN ASN ARG PHE          
SEQRES  12 G  260  ILE GLY ASP ILE LYS ILE HIS ASN GLU ASP PHE ASP GLU          
SEQRES  13 G  260  THR TYR TYR GLY PHE GLU ASN HIS GLN GLY ARG THR PHE          
SEQRES  14 G  260  LEU SER ASP ASP GLN LYS PRO LEU GLY GLN VAL VAL TYR          
SEQRES  15 G  260  GLY ASN GLY ASN ASN GLU GLU LYS VAL GLY GLU GLY VAL          
SEQRES  16 G  260  HIS TYR LYS ASN VAL PHE GLY SER TYR PHE HIS GLY PRO          
SEQRES  17 G  260  ILE LEU SER ARG ASN ALA ASN LEU ALA TYR ARG LEU VAL          
SEQRES  18 G  260  THR THR ALA LEU LYS LYS LYS TYR GLY GLN ASP ILE GLN          
SEQRES  19 G  260  LEU PRO ALA TYR GLU ASP ILE LEU SER GLN GLU ILE ALA          
SEQRES  20 G  260  GLU GLU TYR SER ASP VAL LYS SER LYS ALA ASP PHE SER          
SEQRES   1 D  465  MET HIS HIS HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR          
SEQRES   2 D  465  PHE GLN GLY SER HIS MET ASN LEU LYS THR THR LEU GLY          
SEQRES   3 D  465  LEU LEU ALA GLY ARG SER SER HIS PHE VAL LEU SER ARG          
SEQRES   4 D  465  LEU GLY ARG GLY SER THR LEU PRO GLY LYS VAL ALA LEU          
SEQRES   5 D  465  GLN PHE ASP LYS ASP ILE LEU GLN SER LEU ALA LYS ASN          
SEQRES   6 D  465  TYR GLU ILE VAL VAL VAL THR GLY THR ASN GLY LYS THR          
SEQRES   7 D  465  LEU THR THR ALA LEU THR VAL GLY ILE LEU LYS GLU VAL          
SEQRES   8 D  465  TYR GLY GLN VAL LEU THR ASN PRO SER GLY ALA ASN MET          
SEQRES   9 D  465  ILE THR GLY ILE ALA THR THR PHE LEU THR ALA LYS SER          
SEQRES  10 D  465  SER LYS THR GLY LYS ASN ILE ALA VAL LEU GLU ILE ASP          
SEQRES  11 D  465  GLU ALA SER LEU SER ARG ILE CYS ASP TYR ILE GLN PRO          
SEQRES  12 D  465  SER LEU PHE VAL ILE THR ASN ILE PHE ARG ASP GLN MET          
SEQRES  13 D  465  ASP ARG PHE GLY GLU ILE TYR THR THR TYR ASN MET ILE          
SEQRES  14 D  465  LEU ASP ALA ILE ARG LYS VAL PRO THR ALA THR VAL LEU          
SEQRES  15 D  465  LEU ASN GLY ASP SER PRO LEU PHE TYR LYS PRO THR ILE          
SEQRES  16 D  465  PRO ASN PRO ILE GLU TYR PHE GLY PHE ASP LEU GLU LYS          
SEQRES  17 D  465  GLY PRO ALA GLN LEU ALA HIS TYR ASN THR GLU GLY ILE          
SEQRES  18 D  465  LEU CYS PRO ASP CYS GLN GLY ILE LEU LYS TYR GLU HIS          
SEQRES  19 D  465  ASN THR TYR ALA ASN LEU GLY ALA TYR ILE CYS GLU GLY          
SEQRES  20 D  465  CYS GLY CYS LYS ARG PRO ASP LEU ASP TYR ARG LEU THR          
SEQRES  21 D  465  LYS LEU VAL GLU LEU THR ASN ASN ARG SER ARG PHE VAL          
SEQRES  22 D  465  ILE ASP GLY GLN GLU TYR GLY ILE GLN ILE GLY GLY LEU          
SEQRES  23 D  465  TYR ASN ILE TYR ASN ALA LEU ALA ALA VAL ALA ILE ALA          
SEQRES  24 D  465  ARG PHE LEU GLY ALA ASP SER GLN LEU ILE LYS GLN GLY          
SEQRES  25 D  465  PHE ASP LYS SER ARG ALA VAL PHE GLY ARG GLN GLU THR          
SEQRES  26 D  465  PHE HIS ILE GLY ASP LYS GLU CYS THR LEU VAL LEU ILE          
SEQRES  27 D  465  LYS ASN PRO VAL GLY ALA THR GLN ALA ILE GLU MET ILE          
SEQRES  28 D  465  LYS LEU ALA PRO TYR PRO PHE SER LEU SER VAL LEU LEU          
SEQRES  29 D  465  ASN ALA ASN TYR ALA ASP GLY ILE ASP THR SER TRP ILE          
SEQRES  30 D  465  TRP ASP ALA ASP PHE GLU GLN ILE THR ASP MET ASP ILE          
SEQRES  31 D  465  PRO GLU ILE ASN ALA GLY GLY VAL ARG HIS SER GLU ILE          
SEQRES  32 D  465  ALA ARG ARG LEU ARG VAL THR GLY TYR PRO ALA GLU LYS          
SEQRES  33 D  465  ILE THR GLU THR SER ASN LEU GLU GLN VAL LEU LYS THR          
SEQRES  34 D  465  ILE GLU ASN GLN ASP CYS LYS HIS ALA TYR ILE LEU ALA          
SEQRES  35 D  465  THR TYR THR ALA MET LEU GLU PHE ARG GLU LEU LEU ALA          
SEQRES  36 D  465  SER ARG GLN ILE VAL ARG LYS GLU MET ASN                      
SEQRES   1 H  260  MET VAL TYR THR SER LEU SER SER LYS ASP GLY ASN TYR          
SEQRES   2 H  260  PRO TYR GLN LEU ASN ILE ALA HIS LEU TYR GLY ASN LEU          
SEQRES   3 H  260  MET ASN THR TYR GLY ASP ASN GLY ASN ILE LEU MET LEU          
SEQRES   4 H  260  LYS TYR VAL ALA GLU LYS LEU GLY ALA HIS VAL THR VAL          
SEQRES   5 H  260  ASP ILE VAL SER LEU HIS ASP ASP PHE ASP GLU ASN HIS          
SEQRES   6 H  260  TYR ASP ILE ALA PHE PHE GLY GLY GLY GLN ASP PHE GLU          
SEQRES   7 H  260  GLN SER ILE ILE ALA ASP ASP LEU PRO ALA LYS LYS GLU          
SEQRES   8 H  260  SER ILE ASP ASN TYR ILE GLN ASN ASP GLY VAL VAL LEU          
SEQRES   9 H  260  ALA ILE CYS GLY GLY PHE GLN LEU LEU GLY GLN TYR TYR          
SEQRES  10 H  260  VAL GLU ALA SER GLY LYS ARG ILE GLU GLY LEU GLY VAL          
SEQRES  11 H  260  MET GLY HIS TYR THR LEU ASN GLN THR ASN ASN ARG PHE          
SEQRES  12 H  260  ILE GLY ASP ILE LYS ILE HIS ASN GLU ASP PHE ASP GLU          
SEQRES  13 H  260  THR TYR TYR GLY PHE GLU ASN HIS GLN GLY ARG THR PHE          
SEQRES  14 H  260  LEU SER ASP ASP GLN LYS PRO LEU GLY GLN VAL VAL TYR          
SEQRES  15 H  260  GLY ASN GLY ASN ASN GLU GLU LYS VAL GLY GLU GLY VAL          
SEQRES  16 H  260  HIS TYR LYS ASN VAL PHE GLY SER TYR PHE HIS GLY PRO          
SEQRES  17 H  260  ILE LEU SER ARG ASN ALA ASN LEU ALA TYR ARG LEU VAL          
SEQRES  18 H  260  THR THR ALA LEU LYS LYS LYS TYR GLY GLN ASP ILE GLN          
SEQRES  19 H  260  LEU PRO ALA TYR GLU ASP ILE LEU SER GLN GLU ILE ALA          
SEQRES  20 H  260  GLU GLU TYR SER ASP VAL LYS SER LYS ALA ASP PHE SER          
HET    GLN  E 301      10                                                       
HET    GLN  F 301      10                                                       
HET    GLN  G 301      10                                                       
HET    GLN  H 301      10                                                       
HETNAM     GLN GLUTAMINE                                                        
FORMUL   9  GLN    4(C5 H10 N2 O3)                                              
HELIX    1 AA1 GLY A   58  GLY A   75  1                                  18    
HELIX    2 AA2 THR A   88  THR A   93  1                                   6    
HELIX    3 AA3 SER A  115  CYS A  120  1                                   6    
HELIX    4 AA4 GLU A  143  LYS A  157  1                                  15    
HELIX    5 AA5 LEU A  268  LEU A  284  1                                  17    
HELIX    6 AA6 ASP A  287  ARG A  299  1                                  13    
HELIX    7 AA7 ALA A  300  GLY A  303  5                                   4    
HELIX    8 AA8 ASN A  322  LYS A  334  1                                  13    
HELIX    9 AA9 ASP A  355  ASP A  361  5                                   7    
HELIX   10 AB1 ASP A  363  MET A  370  5                                   8    
HELIX   11 AB2 ARG A  381  THR A  392  1                                  12    
HELIX   12 AB3 PRO A  395  GLU A  397  5                                   3    
HELIX   13 AB4 ASN A  404  ASN A  414  1                                  11    
HELIX   14 AB5 THR A  425  ARG A  433  1                                   9    
HELIX   15 AB6 ASN E   33  LEU E   46  1                                  14    
HELIX   16 AB7 GLN E   75  LEU E   86  1                                  12    
HELIX   17 AB8 LYS E   89  ASN E   99  1                                  11    
HELIX   18 AB9 CYS E  107  GLY E  114  1                                   8    
HELIX   19 AC1 PRO E  208  ASN E  213  1                                   6    
HELIX   20 AC2 ASN E  213  GLY E  230  1                                  18    
HELIX   21 AC3 ALA E  237  LEU E  242  1                                   6    
HELIX   22 AC4 SER E  243  ILE E  246  5                                   4    
HELIX   23 AC5 GLY B   58  GLY B   75  1                                  18    
HELIX   24 AC6 ASN B   85  ILE B   90  5                                   6    
HELIX   25 AC7 SER B  115  ILE B  123  1                                   9    
HELIX   26 AC8 ILE B  144  LYS B  157  1                                  14    
HELIX   27 AC9 LEU B  268  LEU B  284  1                                  17    
HELIX   28 AD1 ASP B  287  ARG B  299  1                                  13    
HELIX   29 AD2 ALA B  300  GLY B  303  5                                   4    
HELIX   30 AD3 ASN B  322  LYS B  334  1                                  13    
HELIX   31 AD4 ASP B  355  ASP B  361  5                                   7    
HELIX   32 AD5 ASP B  363  MET B  370  5                                   8    
HELIX   33 AD6 ARG B  381  THR B  392  1                                  12    
HELIX   34 AD7 PRO B  395  GLU B  397  5                                   3    
HELIX   35 AD8 ASN B  404  ASN B  414  1                                  11    
HELIX   36 AD9 THR B  425  ARG B  433  1                                   9    
HELIX   37 AE1 ASN F   33  LEU F   46  1                                  14    
HELIX   38 AE2 GLN F   75  LEU F   86  1                                  12    
HELIX   39 AE3 LYS F   89  ASN F   99  1                                  11    
HELIX   40 AE4 CYS F  107  GLY F  114  1                                   8    
HELIX   41 AE5 PRO F  208  ASN F  213  1                                   6    
HELIX   42 AE6 ASN F  213  GLY F  230  1                                  18    
HELIX   43 AE7 ALA F  237  LEU F  242  1                                   6    
HELIX   44 AE8 SER F  243  ILE F  246  5                                   4    
HELIX   45 AE9 GLY C   58  GLY C   75  1                                  18    
HELIX   46 AF1 ASN C   85  ILE C   90  5                                   6    
HELIX   47 AF2 SER C  115  ILE C  123  1                                   9    
HELIX   48 AF3 ILE C  144  LYS C  157  1                                  14    
HELIX   49 AF4 LEU C  268  LEU C  284  1                                  17    
HELIX   50 AF5 ASP C  287  ARG C  299  1                                  13    
HELIX   51 AF6 ALA C  300  GLY C  303  5                                   4    
HELIX   52 AF7 ASN C  322  LYS C  334  1                                  13    
HELIX   53 AF8 ASP C  355  ASP C  361  5                                   7    
HELIX   54 AF9 ASP C  363  MET C  370  5                                   8    
HELIX   55 AG1 ARG C  381  THR C  392  1                                  12    
HELIX   56 AG2 PRO C  395  GLU C  397  5                                   3    
HELIX   57 AG3 ASN C  404  ASN C  414  1                                  11    
HELIX   58 AG4 THR C  425  PHE C  432  1                                   8    
HELIX   59 AG5 ASN G   33  LEU G   46  1                                  14    
HELIX   60 AG6 GLN G   75  LEU G   86  1                                  12    
HELIX   61 AG7 LYS G   89  ASN G   99  1                                  11    
HELIX   62 AG8 CYS G  107  GLY G  114  1                                   8    
HELIX   63 AG9 PRO G  208  ASN G  213  1                                   6    
HELIX   64 AH1 ASN G  213  GLY G  230  1                                  18    
HELIX   65 AH2 ALA G  237  LEU G  242  1                                   6    
HELIX   66 AH3 SER G  243  ILE G  246  5                                   4    
HELIX   67 AH4 GLY D   58  GLY D   75  1                                  18    
HELIX   68 AH5 ASN D   85  ILE D   90  5                                   6    
HELIX   69 AH6 SER D  115  ILE D  123  1                                   9    
HELIX   70 AH7 ILE D  144  LYS D  157  1                                  14    
HELIX   71 AH8 LEU D  268  LEU D  284  1                                  17    
HELIX   72 AH9 ASP D  287  ARG D  299  1                                  13    
HELIX   73 AI1 ALA D  300  GLY D  303  5                                   4    
HELIX   74 AI2 ASN D  322  LYS D  334  1                                  13    
HELIX   75 AI3 ASP D  355  ASP D  361  5                                   7    
HELIX   76 AI4 ASP D  363  MET D  370  5                                   8    
HELIX   77 AI5 ARG D  381  THR D  392  1                                  12    
HELIX   78 AI6 PRO D  395  GLU D  397  5                                   3    
HELIX   79 AI7 ASN D  404  ASN D  414  1                                  11    
HELIX   80 AI8 THR D  425  ARG D  433  1                                   9    
HELIX   81 AI9 ASN H   33  LEU H   46  1                                  14    
HELIX   82 AJ1 GLN H   75  LEU H   86  1                                  12    
HELIX   83 AJ2 LYS H   89  ASN H   99  1                                  11    
HELIX   84 AJ3 CYS H  107  GLY H  114  1                                   8    
HELIX   85 AJ4 PRO H  208  ASN H  213  1                                   6    
HELIX   86 AJ5 ASN H  213  GLY H  230  1                                  18    
HELIX   87 AJ6 ALA H  237  LEU H  242  1                                   6    
HELIX   88 AJ7 SER H  243  ILE H  246  5                                   4    
SHEET    1 AA1 9 VAL A  77  LEU A  78  0                                        
SHEET    2 AA1 9 ILE A 106  GLU A 110  1  O  VAL A 108   N  LEU A  78           
SHEET    3 AA1 9 GLU A  49  THR A  54  1  N  VAL A  51   O  LEU A 109           
SHEET    4 AA1 9 LEU A 127  ILE A 130  1  O  LEU A 127   N  VAL A  52           
SHEET    5 AA1 9 THR A 162  ASN A 166  1  O  LEU A 164   N  PHE A 128           
SHEET    6 AA1 9 ILE A 181  PHE A 186  1  O  GLU A 182   N  VAL A 163           
SHEET    7 AA1 9 TYR A 239  LEU A 247  1  O  LEU A 241   N  GLY A 185           
SHEET    8 AA1 9 SER A 252  ILE A 256 -1  O  VAL A 255   N  LYS A 243           
SHEET    9 AA1 9 GLN A 259  ILE A 263 -1  O  TYR A 261   N  PHE A 254           
SHEET    1 AA2 2 LYS A 213  ASN A 217  0                                        
SHEET    2 AA2 2 GLY A 223  ILE A 226 -1  O  ALA A 224   N  GLU A 215           
SHEET    1 AA3 6 THR A 307  ILE A 310  0                                        
SHEET    2 AA3 6 LYS A 313  LEU A 319 -1  O  CYS A 315   N  PHE A 308           
SHEET    3 AA3 6 HIS A 419  ALA A 424  1  O  ILE A 422   N  VAL A 318           
SHEET    4 AA3 6 PHE A 340  LEU A 345  1  N  LEU A 345   O  LEU A 423           
SHEET    5 AA3 6 ILE A 375  GLY A 378  1  O  ASN A 376   N  VAL A 344           
SHEET    6 AA3 6 ILE A 399  GLU A 401  1  O  THR A 400   N  ILE A 375           
SHEET    1 AA4 7 TYR E   3  SER E   7  0                                        
SHEET    2 AA4 7 ALA E  48  VAL E  55 -1  O  ILE E  54   N  TYR E   3           
SHEET    3 AA4 7 TYR E  15  LEU E  22  1  N  ILE E  19   O  ASP E  53           
SHEET    4 AA4 7 ILE E  68  PHE E  71  1  O  ILE E  68   N  ALA E  20           
SHEET    5 AA4 7 VAL E 102  ILE E 106  1  O  ILE E 106   N  PHE E  71           
SHEET    6 AA4 7 VAL E 200  SER E 203  1  O  PHE E 201   N  ALA E 105           
SHEET    7 AA4 7 VAL E 195  HIS E 196 -1  N  VAL E 195   O  GLY E 202           
SHEET    1 AA5 2 TYR E 116  VAL E 118  0                                        
SHEET    2 AA5 2 ARG E 124  GLU E 126 -1  O  ILE E 125   N  TYR E 117           
SHEET    1 AA6 2 TYR E 134  LEU E 136  0                                        
SHEET    2 AA6 2 ARG E 167  PHE E 169 -1  O  PHE E 169   N  TYR E 134           
SHEET    1 AA7 5 GLY E 192  GLU E 193  0                                        
SHEET    2 AA7 5 GLY E 178  TYR E 182 -1  N  GLY E 178   O  GLU E 193           
SHEET    3 AA7 5 PHE E 143  ASN E 151 -1  N  HIS E 150   O  GLN E 179           
SHEET    4 AA7 5 GLU E 156  HIS E 164 -1  O  GLU E 156   N  ASN E 151           
SHEET    5 AA7 5 PHE E 205  HIS E 206 -1  O  HIS E 206   N  PHE E 161           
SHEET    1 AA8 9 VAL B  77  LEU B  78  0                                        
SHEET    2 AA8 9 ILE B 106  GLU B 110  1  O  VAL B 108   N  LEU B  78           
SHEET    3 AA8 9 GLU B  49  THR B  54  1  N  VAL B  51   O  LEU B 109           
SHEET    4 AA8 9 LEU B 127  ILE B 130  1  O  LEU B 127   N  VAL B  52           
SHEET    5 AA8 9 THR B 162  ASN B 166  1  O  LEU B 164   N  PHE B 128           
SHEET    6 AA8 9 ILE B 181  PHE B 186  1  O  GLU B 182   N  VAL B 163           
SHEET    7 AA8 9 TYR B 239  LEU B 247  1  O  LEU B 241   N  GLY B 185           
SHEET    8 AA8 9 SER B 252  ILE B 256 -1  O  VAL B 255   N  LYS B 243           
SHEET    9 AA8 9 GLN B 259  ILE B 263 -1  O  TYR B 261   N  PHE B 254           
SHEET    1 AA9 2 LYS B 213  ASN B 217  0                                        
SHEET    2 AA9 2 GLY B 223  ILE B 226 -1  O  ALA B 224   N  GLU B 215           
SHEET    1 AB1 6 THR B 307  ILE B 310  0                                        
SHEET    2 AB1 6 LYS B 313  LEU B 319 -1  O  CYS B 315   N  PHE B 308           
SHEET    3 AB1 6 HIS B 419  ALA B 424  1  O  ILE B 422   N  VAL B 318           
SHEET    4 AB1 6 PHE B 340  LEU B 345  1  N  LEU B 345   O  LEU B 423           
SHEET    5 AB1 6 ILE B 375  GLY B 378  1  O  ASN B 376   N  VAL B 344           
SHEET    6 AB1 6 ILE B 399  GLU B 401  1  O  THR B 400   N  ILE B 375           
SHEET    1 AB2 7 TYR F   3  SER F   7  0                                        
SHEET    2 AB2 7 ALA F  48  VAL F  55 -1  O  ILE F  54   N  TYR F   3           
SHEET    3 AB2 7 TYR F  15  LEU F  22  1  N  ILE F  19   O  ASP F  53           
SHEET    4 AB2 7 ILE F  68  PHE F  71  1  O  ILE F  68   N  ALA F  20           
SHEET    5 AB2 7 VAL F 102  ILE F 106  1  O  ILE F 106   N  PHE F  71           
SHEET    6 AB2 7 VAL F 200  SER F 203  1  O  PHE F 201   N  ALA F 105           
SHEET    7 AB2 7 VAL F 195  HIS F 196 -1  N  VAL F 195   O  GLY F 202           
SHEET    1 AB3 2 TYR F 116  VAL F 118  0                                        
SHEET    2 AB3 2 ARG F 124  GLU F 126 -1  O  ILE F 125   N  TYR F 117           
SHEET    1 AB4 2 TYR F 134  LEU F 136  0                                        
SHEET    2 AB4 2 ARG F 167  PHE F 169 -1  O  PHE F 169   N  TYR F 134           
SHEET    1 AB5 5 GLY F 192  GLU F 193  0                                        
SHEET    2 AB5 5 GLY F 178  TYR F 182 -1  N  GLY F 178   O  GLU F 193           
SHEET    3 AB5 5 PHE F 143  ASN F 151 -1  N  HIS F 150   O  GLN F 179           
SHEET    4 AB5 5 GLU F 156  HIS F 164 -1  O  GLU F 156   N  ASN F 151           
SHEET    5 AB5 5 PHE F 205  HIS F 206 -1  O  HIS F 206   N  PHE F 161           
SHEET    1 AB6 9 VAL C  77  LEU C  78  0                                        
SHEET    2 AB6 9 ILE C 106  GLU C 110  1  O  VAL C 108   N  LEU C  78           
SHEET    3 AB6 9 GLU C  49  THR C  54  1  N  VAL C  51   O  LEU C 109           
SHEET    4 AB6 9 LEU C 127  ILE C 130  1  O  LEU C 127   N  VAL C  52           
SHEET    5 AB6 9 THR C 162  ASN C 166  1  O  LEU C 164   N  PHE C 128           
SHEET    6 AB6 9 ILE C 181  PHE C 186  1  O  GLU C 182   N  VAL C 163           
SHEET    7 AB6 9 TYR C 239  LEU C 247  1  O  LEU C 241   N  GLY C 185           
SHEET    8 AB6 9 SER C 252  ILE C 256 -1  O  VAL C 255   N  LYS C 243           
SHEET    9 AB6 9 GLN C 259  ILE C 263 -1  O  TYR C 261   N  PHE C 254           
SHEET    1 AB7 2 LYS C 213  ASN C 217  0                                        
SHEET    2 AB7 2 GLY C 223  ILE C 226 -1  O  ALA C 224   N  GLU C 215           
SHEET    1 AB8 6 THR C 307  ILE C 310  0                                        
SHEET    2 AB8 6 LYS C 313  LEU C 319 -1  O  CYS C 315   N  PHE C 308           
SHEET    3 AB8 6 HIS C 419  ALA C 424  1  O  ILE C 422   N  VAL C 318           
SHEET    4 AB8 6 PHE C 340  LEU C 345  1  N  LEU C 345   O  LEU C 423           
SHEET    5 AB8 6 ILE C 375  GLY C 378  1  O  ASN C 376   N  VAL C 344           
SHEET    6 AB8 6 ILE C 399  GLU C 401  1  O  THR C 400   N  ILE C 375           
SHEET    1 AB9 7 TYR G   3  SER G   7  0                                        
SHEET    2 AB9 7 ALA G  48  ILE G  54 -1  O  ILE G  54   N  TYR G   3           
SHEET    3 AB9 7 TYR G  15  LEU G  22  1  N  ILE G  19   O  ASP G  53           
SHEET    4 AB9 7 ILE G  68  PHE G  71  1  O  ILE G  68   N  ALA G  20           
SHEET    5 AB9 7 VAL G 102  ILE G 106  1  O  ILE G 106   N  PHE G  71           
SHEET    6 AB9 7 VAL G 200  SER G 203  1  O  PHE G 201   N  ALA G 105           
SHEET    7 AB9 7 VAL G 195  HIS G 196 -1  N  VAL G 195   O  GLY G 202           
SHEET    1 AC1 2 TYR G 116  VAL G 118  0                                        
SHEET    2 AC1 2 ARG G 124  GLU G 126 -1  O  ILE G 125   N  TYR G 117           
SHEET    1 AC2 2 TYR G 134  LEU G 136  0                                        
SHEET    2 AC2 2 ARG G 167  PHE G 169 -1  O  PHE G 169   N  TYR G 134           
SHEET    1 AC3 5 GLY G 192  GLU G 193  0                                        
SHEET    2 AC3 5 GLY G 178  TYR G 182 -1  N  GLY G 178   O  GLU G 193           
SHEET    3 AC3 5 PHE G 143  ASN G 151 -1  N  HIS G 150   O  GLN G 179           
SHEET    4 AC3 5 GLU G 156  HIS G 164 -1  O  GLU G 156   N  ASN G 151           
SHEET    5 AC3 5 PHE G 205  HIS G 206 -1  O  HIS G 206   N  PHE G 161           
SHEET    1 AC4 9 VAL D  77  LEU D  78  0                                        
SHEET    2 AC4 9 ILE D 106  GLU D 110  1  O  ILE D 106   N  LEU D  78           
SHEET    3 AC4 9 GLU D  49  THR D  54  1  N  VAL D  51   O  LEU D 109           
SHEET    4 AC4 9 LEU D 127  ILE D 130  1  O  LEU D 127   N  VAL D  52           
SHEET    5 AC4 9 THR D 162  ASN D 166  1  O  LEU D 164   N  PHE D 128           
SHEET    6 AC4 9 ILE D 181  PHE D 186  1  O  GLU D 182   N  VAL D 163           
SHEET    7 AC4 9 TYR D 239  LEU D 247  1  O  LEU D 241   N  GLY D 185           
SHEET    8 AC4 9 SER D 252  ILE D 256 -1  O  VAL D 255   N  LYS D 243           
SHEET    9 AC4 9 GLN D 259  ILE D 263 -1  O  TYR D 261   N  PHE D 254           
SHEET    1 AC5 2 LYS D 213  ASN D 217  0                                        
SHEET    2 AC5 2 GLY D 223  ILE D 226 -1  O  ALA D 224   N  GLU D 215           
SHEET    1 AC6 6 THR D 307  ILE D 310  0                                        
SHEET    2 AC6 6 LYS D 313  LEU D 319 -1  O  CYS D 315   N  PHE D 308           
SHEET    3 AC6 6 HIS D 419  ALA D 424  1  O  ILE D 422   N  VAL D 318           
SHEET    4 AC6 6 PHE D 340  LEU D 345  1  N  LEU D 345   O  LEU D 423           
SHEET    5 AC6 6 ILE D 375  GLY D 378  1  O  ASN D 376   N  VAL D 344           
SHEET    6 AC6 6 ILE D 399  GLU D 401  1  O  THR D 400   N  ILE D 375           
SHEET    1 AC7 7 TYR H   3  SER H   7  0                                        
SHEET    2 AC7 7 ALA H  48  ILE H  54 -1  O  ILE H  54   N  TYR H   3           
SHEET    3 AC7 7 TYR H  15  LEU H  22  1  N  ILE H  19   O  ASP H  53           
SHEET    4 AC7 7 ILE H  68  PHE H  71  1  O  ILE H  68   N  ALA H  20           
SHEET    5 AC7 7 VAL H 102  ILE H 106  1  O  ILE H 106   N  PHE H  71           
SHEET    6 AC7 7 VAL H 200  SER H 203  1  O  PHE H 201   N  VAL H 103           
SHEET    7 AC7 7 VAL H 195  HIS H 196 -1  N  VAL H 195   O  GLY H 202           
SHEET    1 AC8 2 TYR H 116  VAL H 118  0                                        
SHEET    2 AC8 2 ARG H 124  GLU H 126 -1  O  ILE H 125   N  TYR H 117           
SHEET    1 AC9 2 TYR H 134  LEU H 136  0                                        
SHEET    2 AC9 2 ARG H 167  PHE H 169 -1  O  PHE H 169   N  TYR H 134           
SHEET    1 AD1 5 GLY H 192  GLU H 193  0                                        
SHEET    2 AD1 5 GLY H 178  TYR H 182 -1  N  GLY H 178   O  GLU H 193           
SHEET    3 AD1 5 PHE H 143  ASN H 151 -1  N  HIS H 150   O  GLN H 179           
SHEET    4 AD1 5 GLU H 156  HIS H 164 -1  O  GLU H 156   N  ASN H 151           
SHEET    5 AD1 5 PHE H 205  HIS H 206 -1  O  HIS H 206   N  PHE H 161           
SSBOND   1 CYS A  205    CYS A  230                          1555   1555  2.06  
SSBOND   2 CYS A  205    CYS A  208                          1555   1555  2.05  
SSBOND   3 CYS A  208    CYS A  227                          1555   1555  2.05  
SSBOND   4 CYS A  208    CYS A  230                          1555   1555  2.02  
SSBOND   5 CYS A  227    CYS A  230                          1555   1555  2.03  
SSBOND   6 CYS B  205    CYS B  208                          1555   1555  2.05  
SSBOND   7 CYS B  205    CYS B  230                          1555   1555  2.06  
SSBOND   8 CYS B  208    CYS B  227                          1555   1555  2.06  
SSBOND   9 CYS B  208    CYS B  230                          1555   1555  2.02  
SSBOND  10 CYS B  227    CYS B  230                          1555   1555  2.03  
SSBOND  11 CYS C  205    CYS C  208                          1555   1555  2.05  
SSBOND  12 CYS C  205    CYS C  230                          1555   1555  2.07  
SSBOND  13 CYS C  208    CYS C  227                          1555   1555  2.05  
SSBOND  14 CYS C  208    CYS C  230                          1555   1555  2.01  
SSBOND  15 CYS C  227    CYS C  230                          1555   1555  2.06  
SSBOND  16 CYS D  205    CYS D  208                          1555   1555  2.06  
SSBOND  17 CYS D  205    CYS D  230                          1555   1555  2.05  
SSBOND  18 CYS D  208    CYS D  227                          1555   1555  2.05  
SSBOND  19 CYS D  208    CYS D  230                          1555   1555  2.02  
SSBOND  20 CYS D  227    CYS D  230                          1555   1555  2.05  
SITE     1 AC1  7 CYS E 107  GLN E 111  ARG E 142  ASN E 163                    
SITE     2 AC1  7 GLN E 165  GLY E 166  HIS E 206                               
SITE     1 AC2  8 CYS F 107  GLN F 111  ARG F 142  ASN F 163                    
SITE     2 AC2  8 HIS F 164  GLN F 165  GLY F 166  HIS F 206                    
SITE     1 AC3  7 CYS G 107  GLN G 111  ARG G 142  ASN G 163                    
SITE     2 AC3  7 GLN G 165  GLY G 166  HIS G 206                               
SITE     1 AC4  8 GLN H  79  CYS H 107  GLN H 111  ARG H 142                    
SITE     2 AC4  8 ASN H 163  GLN H 165  GLY H 166  HIS H 206                    
CRYST1  107.100  110.370  116.360  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      0.009337  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008594        0.00000                         
ATOM      1  N   SER A  43       6.826  -6.587   1.184  1.00115.48           N  
ATOM      2  CA  SER A  43       7.777  -6.102   0.190  1.00115.66           C  
ATOM      3  C   SER A  43       9.179  -6.162   0.749  1.00121.10           C  
ATOM      4  O   SER A  43      10.007  -5.312   0.452  1.00111.03           O  
ATOM      5  CB  SER A  43       7.454  -4.668  -0.235  1.00114.00           C  
ATOM      6  OG  SER A  43       6.211  -4.575  -0.907  1.00111.69           O  
ATOM      7  N   LEU A  44       9.438  -7.190   1.548  1.00134.95           N  
ATOM      8  CA  LEU A  44      10.729  -7.361   2.191  1.00133.75           C  
ATOM      9  C   LEU A  44      10.993  -8.809   2.555  1.00137.42           C  
ATOM     10  O   LEU A  44      10.069  -9.601   2.694  1.00139.46           O  
ATOM     11  CB  LEU A  44      10.733  -6.567   3.482  1.00124.47           C  
ATOM     12  CG  LEU A  44       9.635  -7.056   4.421  1.00123.11           C  
ATOM     13  CD1 LEU A  44      10.044  -8.296   5.191  1.00110.96           C  
ATOM     14  CD2 LEU A  44       9.207  -5.964   5.371  1.00119.98           C  
ATOM     15  N   ALA A  45      12.259  -9.143   2.750  1.00133.81           N  
ATOM     16  CA  ALA A  45      12.630 -10.489   3.139  1.00136.08           C  
ATOM     17  C   ALA A  45      13.122 -10.497   4.583  1.00147.29           C  
ATOM     18  O   ALA A  45      14.112  -9.855   4.926  1.00137.91           O  
ATOM     19  CB  ALA A  45      13.689 -11.036   2.209  1.00119.71           C  
ATOM     20  N   LYS A  46      12.422 -11.230   5.432  1.00143.54           N  
ATOM     21  CA  LYS A  46      12.780 -11.303   6.831  1.00126.86           C  
ATOM     22  C   LYS A  46      13.400 -12.626   7.162  1.00127.65           C  
ATOM     23  O   LYS A  46      13.245 -13.117   8.267  1.00113.10           O  
ATOM     24  CB  LYS A  46      11.539 -11.154   7.673  1.00129.18           C  
ATOM     25  CG  LYS A  46      11.838 -11.147   9.151  1.00127.40           C  
ATOM     26  CD  LYS A  46      10.570 -10.948   9.955  1.00131.46           C  
ATOM     27  CE  LYS A  46      10.860 -10.965  11.443  1.00131.42           C  
ATOM     28  NZ  LYS A  46       9.619 -10.769  12.238  1.00136.35           N  
ATOM     29  N   ASN A  47      14.072 -13.225   6.194  1.00148.73           N  
ATOM     30  CA  ASN A  47      14.756 -14.525   6.419  1.00154.67           C  
ATOM     31  C   ASN A  47      16.121 -14.370   7.148  1.00153.81           C  
ATOM     32  O   ASN A  47      17.073 -15.094   6.836  1.00144.99           O  
ATOM     33  CB  ASN A  47      14.993 -15.343   5.104  1.00150.86           C  
ATOM     34  CG  ASN A  47      15.421 -16.776   5.315  1.00144.23           C  
ATOM     35  OD1 ASN A  47      15.036 -17.381   6.303  1.00135.48           O  
ATOM     36  ND2 ASN A  47      16.144 -17.353   4.342  1.00137.34           N  
ATOM     37  N   TYR A  48      16.245 -13.383   8.048  1.00144.49           N  
ATOM     38  CA  TYR A  48      17.549 -12.900   8.495  1.00121.02           C  
ATOM     39  C   TYR A  48      17.561 -12.480   9.951  1.00116.82           C  
ATOM     40  O   TYR A  48      16.740 -11.661  10.358  1.00112.39           O  
ATOM     41  CB  TYR A  48      17.942 -11.674   7.688  1.00112.84           C  
ATOM     42  CG  TYR A  48      18.530 -11.946   6.344  1.00119.23           C  
ATOM     43  CD1 TYR A  48      18.045 -11.292   5.215  1.00122.22           C  
ATOM     44  CD2 TYR A  48      19.611 -12.814   6.197  1.00123.79           C  
ATOM     45  CE1 TYR A  48      18.598 -11.516   3.966  1.00114.62           C  
ATOM     46  CE2 TYR A  48      20.156 -13.066   4.963  1.00127.67           C  
ATOM     47  CZ  TYR A  48      19.653 -12.398   3.854  1.00123.09           C  
ATOM     48  OH  TYR A  48      20.204 -12.633   2.630  1.00133.86           O  
ATOM     49  N   GLU A  49      18.505 -13.023  10.725  1.00116.95           N  
ATOM     50  CA  GLU A  49      18.873 -12.405  11.998  1.00116.24           C  
ATOM     51  C   GLU A  49      19.602 -11.124  11.596  1.00117.16           C  
ATOM     52  O   GLU A  49      20.522 -11.151  10.772  1.00110.88           O  
ATOM     53  CB  GLU A  49      19.748 -13.322  12.860  1.00108.64           C  
ATOM     54  CG  GLU A  49      20.060 -12.754  14.237  1.00110.10           C  
ATOM     55  CD  GLU A  49      20.802 -13.726  15.139  1.00116.18           C  
ATOM     56  OE1 GLU A  49      21.351 -14.745  14.655  1.00118.44           O  
ATOM     57  OE2 GLU A  49      20.850 -13.496  16.364  1.00112.23           O  
ATOM     58  N   ILE A  50      19.165 -10.000  12.148  1.00111.11           N  
ATOM     59  CA  ILE A  50      19.563  -8.690  11.644  1.00108.41           C  
ATOM     60  C   ILE A  50      19.991  -7.736  12.778  1.00101.34           C  
ATOM     61  O   ILE A  50      19.279  -7.568  13.779  1.00 94.90           O  
ATOM     62  CB  ILE A  50      18.470  -8.105  10.707  1.00116.87           C  
ATOM     63  CG1 ILE A  50      18.739  -6.622  10.405  1.00125.63           C  
ATOM     64  CG2 ILE A  50      17.046  -8.339  11.246  1.00114.30           C  
ATOM     65  CD1 ILE A  50      18.115  -6.160   9.107  1.00128.62           C  
ATOM     66  N   VAL A  51      21.178  -7.146  12.586  1.00 95.31           N  
ATOM     67  CA  VAL A  51      21.822  -6.213  13.518  1.00 95.18           C  
ATOM     68  C   VAL A  51      21.831  -4.830  12.866  1.00101.27           C  
ATOM     69  O   VAL A  51      22.316  -4.693  11.736  1.00 94.08           O  
ATOM     70  CB  VAL A  51      23.295  -6.624  13.775  1.00 91.08           C  
ATOM     71  CG1 VAL A  51      24.019  -5.633  14.664  1.00 86.22           C  
ATOM     72  CG2 VAL A  51      23.377  -8.015  14.375  1.00 98.36           C  
ATOM     73  N   VAL A  52      21.305  -3.808  13.561  1.00 98.12           N  
ATOM     74  CA  VAL A  52      21.413  -2.403  13.084  1.00 91.24           C  
ATOM     75  C   VAL A  52      22.421  -1.619  13.936  1.00 86.70           C  
ATOM     76  O   VAL A  52      22.495  -1.808  15.157  1.00 77.79           O  
ATOM     77  CB  VAL A  52      20.054  -1.648  13.008  1.00 91.93           C  
ATOM     78  CG1 VAL A  52      19.025  -2.442  12.218  1.00 92.18           C  
ATOM     79  CG2 VAL A  52      19.493  -1.331  14.379  1.00 95.68           C  
ATOM     80  N   VAL A  53      23.176  -0.745  13.271  1.00 86.16           N  
ATOM     81  CA  VAL A  53      24.282   0.005  13.874  1.00 86.38           C  
ATOM     82  C   VAL A  53      24.038   1.490  13.592  1.00 89.18           C  
ATOM     83  O   VAL A  53      24.077   1.908  12.438  1.00 89.19           O  
ATOM     84  CB  VAL A  53      25.657  -0.429  13.289  1.00 79.83           C  
ATOM     85  CG1 VAL A  53      26.787   0.415  13.842  1.00 83.26           C  
ATOM     86  CG2 VAL A  53      25.940  -1.884  13.592  1.00 78.74           C  
ATOM     87  N   THR A  54      23.775   2.274  14.643  1.00 94.42           N  
ATOM     88  CA  THR A  54      23.544   3.728  14.535  1.00 92.63           C  
ATOM     89  C   THR A  54      24.521   4.445  15.462  1.00 88.35           C  
ATOM     90  O   THR A  54      25.421   3.815  16.032  1.00 82.99           O  
ATOM     91  CB  THR A  54      22.070   4.103  14.875  1.00 99.60           C  
ATOM     92  OG1 THR A  54      21.735   3.680  16.206  1.00103.15           O  
ATOM     93  CG2 THR A  54      21.111   3.452  13.897  1.00112.62           C  
ATOM     94  N   GLY A  55      24.350   5.759  15.589  1.00 90.17           N  
ATOM     95  CA  GLY A  55      25.204   6.611  16.415  1.00 87.49           C  
ATOM     96  C   GLY A  55      25.697   7.746  15.558  1.00 87.95           C  
ATOM     97  O   GLY A  55      25.560   7.710  14.343  1.00 89.15           O  
ATOM     98  N   THR A  56      26.302   8.750  16.178  1.00 94.11           N  
ATOM     99  CA  THR A  56      26.751   9.919  15.425  1.00 95.61           C  
ATOM    100  C   THR A  56      28.105   9.676  14.759  1.00 98.51           C  
ATOM    101  O   THR A  56      28.284  10.044  13.604  1.00103.26           O  
ATOM    102  CB  THR A  56      26.773  11.196  16.284  1.00 93.54           C  
ATOM    103  OG1 THR A  56      27.716  11.044  17.353  1.00 92.20           O  
ATOM    104  CG2 THR A  56      25.361  11.497  16.836  1.00 93.08           C  
ATOM    105  N   ASN A  57      29.042   9.053  15.474  1.00111.58           N  
ATOM    106  CA  ASN A  57      30.405   8.848  14.956  1.00118.37           C  
ATOM    107  C   ASN A  57      30.770   7.379  14.771  1.00108.50           C  
ATOM    108  O   ASN A  57      30.412   6.535  15.598  1.00 93.23           O  
ATOM    109  CB  ASN A  57      31.434   9.520  15.876  1.00130.97           C  
ATOM    110  CG  ASN A  57      31.294  11.032  15.905  1.00131.36           C  
ATOM    111  OD1 ASN A  57      30.190  11.559  15.887  1.00129.13           O  
ATOM    112  ND2 ASN A  57      32.418  11.733  15.989  1.00140.03           N  
ATOM    113  N   GLY A  58      31.463   7.103  13.658  1.00107.19           N  
ATOM    114  CA  GLY A  58      32.129   5.828  13.418  1.00101.27           C  
ATOM    115  C   GLY A  58      31.258   4.632  13.084  1.00 97.53           C  
ATOM    116  O   GLY A  58      31.624   3.505  13.402  1.00 94.95           O  
ATOM    117  N   LYS A  59      30.116   4.855  12.434  1.00101.53           N  
ATOM    118  CA  LYS A  59      29.241   3.751  12.057  1.00100.63           C  
ATOM    119  C   LYS A  59      29.850   2.893  10.956  1.00 96.76           C  
ATOM    120  O   LYS A  59      29.968   1.688  11.122  1.00100.70           O  
ATOM    121  CB  LYS A  59      27.898   4.252  11.569  1.00107.01           C  
ATOM    122  CG  LYS A  59      27.040   4.912  12.628  1.00115.59           C  
ATOM    123  CD  LYS A  59      25.799   5.532  11.993  1.00109.92           C  
ATOM    124  CE  LYS A  59      26.131   6.826  11.261  1.00 98.32           C  
ATOM    125  NZ  LYS A  59      24.923   7.654  11.101  1.00 98.51           N  
ATOM    126  N   THR A  60      30.237   3.508   9.840  1.00 95.41           N  
ATOM    127  CA  THR A  60      30.735   2.752   8.687  1.00 98.09           C  
ATOM    128  C   THR A  60      31.849   1.786   9.109  1.00 91.84           C  
ATOM    129  O   THR A  60      31.789   0.606   8.763  1.00 94.41           O  
ATOM    130  CB  THR A  60      31.272   3.637   7.528  1.00 96.25           C  
ATOM    131  OG1 THR A  60      32.263   4.540   8.018  1.00118.53           O  
ATOM    132  CG2 THR A  60      30.160   4.427   6.848  1.00 85.67           C  
ATOM    133  N   LEU A  61      32.829   2.280   9.873  1.00 85.58           N  
ATOM    134  CA  LEU A  61      33.956   1.448  10.343  1.00 92.17           C  
ATOM    135  C   LEU A  61      33.470   0.284  11.165  1.00 89.03           C  
ATOM    136  O   LEU A  61      33.775  -0.864  10.853  1.00 93.20           O  
ATOM    137  CB  LEU A  61      34.977   2.235  11.174  1.00 95.39           C  
ATOM    138  CG  LEU A  61      36.272   2.602  10.451  1.00100.26           C  
ATOM    139  CD1 LEU A  61      36.016   3.416   9.180  1.00101.85           C  
ATOM    140  CD2 LEU A  61      37.187   3.354  11.400  1.00105.12           C  
ATOM    141  N   THR A  62      32.710   0.597  12.208  1.00 82.02           N  
ATOM    142  CA  THR A  62      32.161  -0.428  13.084  1.00 76.39           C  
ATOM    143  C   THR A  62      31.386  -1.468  12.283  1.00 74.38           C  
ATOM    144  O   THR A  62      31.554  -2.666  12.495  1.00 85.80           O  
ATOM    145  CB  THR A  62      31.273   0.184  14.185  1.00 73.74           C  
ATOM    146  OG1 THR A  62      32.070   1.029  15.029  1.00 77.73           O  
ATOM    147  CG2 THR A  62      30.636  -0.901  15.046  1.00 75.46           C  
ATOM    148  N   THR A  63      30.570  -1.009  11.346  1.00 77.31           N  
ATOM    149  CA  THR A  63      29.766  -1.908  10.529  1.00 81.69           C  
ATOM    150  C   THR A  63      30.658  -2.734   9.609  1.00 82.31           C  
ATOM    151  O   THR A  63      30.545  -3.961   9.581  1.00 86.41           O  
ATOM    152  CB  THR A  63      28.703  -1.135   9.719  1.00 83.22           C  
ATOM    153  OG1 THR A  63      27.858  -0.418  10.630  1.00 82.92           O  
ATOM    154  CG2 THR A  63      27.839  -2.068   8.904  1.00 85.93           C  
ATOM    155  N   ALA A  64      31.551  -2.066   8.882  1.00 80.83           N  
ATOM    156  CA  ALA A  64      32.453  -2.745   7.945  1.00 83.40           C  
ATOM    157  C   ALA A  64      33.313  -3.793   8.634  1.00 84.81           C  
ATOM    158  O   ALA A  64      33.556  -4.865   8.086  1.00100.15           O  
ATOM    159  CB  ALA A  64      33.343  -1.741   7.244  1.00 83.51           C  
ATOM    160  N   LEU A  65      33.757  -3.470   9.840  1.00 83.32           N  
ATOM    161  CA  LEU A  65      34.574  -4.365  10.651  1.00 82.34           C  
ATOM    162  C   LEU A  65      33.757  -5.565  11.127  1.00 81.90           C  
ATOM    163  O   LEU A  65      34.176  -6.714  10.976  1.00 76.64           O  
ATOM    164  CB  LEU A  65      35.122  -3.588  11.841  1.00 82.16           C  
ATOM    165  CG  LEU A  65      36.359  -4.093  12.533  1.00 86.74           C  
ATOM    166  CD1 LEU A  65      37.514  -4.256  11.551  1.00 90.46           C  
ATOM    167  CD2 LEU A  65      36.704  -3.089  13.612  1.00 92.33           C  
ATOM    168  N   THR A  66      32.575  -5.285  11.673  1.00 83.76           N  
ATOM    169  CA  THR A  66      31.631  -6.324  12.098  1.00 80.09           C  
ATOM    170  C   THR A  66      31.300  -7.337  11.000  1.00 82.29           C  
ATOM    171  O   THR A  66      31.150  -8.517  11.301  1.00 89.14           O  
ATOM    172  CB  THR A  66      30.319  -5.703  12.624  1.00 77.37           C  
ATOM    173  OG1 THR A  66      30.616  -4.881  13.748  1.00 75.24           O  
ATOM    174  CG2 THR A  66      29.320  -6.754  13.058  1.00 82.47           C  
ATOM    175  N   VAL A  67      31.199  -6.883   9.745  1.00 79.70           N  
ATOM    176  CA  VAL A  67      30.948  -7.790   8.620  1.00 78.30           C  
ATOM    177  C   VAL A  67      32.113  -8.748   8.412  1.00 80.84           C  
ATOM    178  O   VAL A  67      31.914  -9.960   8.421  1.00 88.06           O  
ATOM    179  CB  VAL A  67      30.724  -7.048   7.292  1.00 80.60           C  
ATOM    180  CG1 VAL A  67      30.637  -8.022   6.118  1.00 76.54           C  
ATOM    181  CG2 VAL A  67      29.472  -6.204   7.351  1.00 91.37           C  
ATOM    182  N   GLY A  68      33.311  -8.195   8.214  1.00 76.98           N  
ATOM    183  CA  GLY A  68      34.529  -8.988   8.022  1.00 75.29           C  
ATOM    184  C   GLY A  68      34.726 -10.052   9.091  1.00 73.69           C  
ATOM    185  O   GLY A  68      35.113 -11.186   8.784  1.00 67.38           O  
ATOM    186  N   ILE A  69      34.444  -9.688  10.340  1.00 75.18           N  
ATOM    187  CA  ILE A  69      34.525 -10.625  11.449  1.00 77.35           C  
ATOM    188  C   ILE A  69      33.493 -11.735  11.248  1.00 81.13           C  
ATOM    189  O   ILE A  69      33.842 -12.904  11.176  1.00 88.06           O  
ATOM    190  CB  ILE A  69      34.306  -9.918  12.804  1.00 79.01           C  
ATOM    191  CG1 ILE A  69      35.497  -9.013  13.104  1.00 81.57           C  
ATOM    192  CG2 ILE A  69      34.113 -10.924  13.942  1.00 76.57           C  
ATOM    193  CD1 ILE A  69      35.261  -8.011  14.209  1.00 82.68           C  
ATOM    194  N   LEU A  70      32.228 -11.361  11.131  1.00 83.50           N  
ATOM    195  CA  LEU A  70      31.159 -12.341  10.983  1.00 78.39           C  
ATOM    196  C   LEU A  70      31.243 -13.198   9.716  1.00 82.22           C  
ATOM    197  O   LEU A  70      30.690 -14.292   9.708  1.00 87.19           O  
ATOM    198  CB  LEU A  70      29.790 -11.661  11.032  1.00 74.92           C  
ATOM    199  CG  LEU A  70      29.375 -10.996  12.337  1.00 72.87           C  
ATOM    200  CD1 LEU A  70      27.940 -10.520  12.211  1.00 74.67           C  
ATOM    201  CD2 LEU A  70      29.540 -11.926  13.521  1.00 72.77           C  
ATOM    202  N   LYS A  71      31.915 -12.732   8.655  1.00 81.91           N  
ATOM    203  CA  LYS A  71      32.122 -13.560   7.441  1.00 81.26           C  
ATOM    204  C   LYS A  71      32.950 -14.804   7.760  1.00 80.41           C  
ATOM    205  O   LYS A  71      32.709 -15.883   7.221  1.00 93.10           O  
ATOM    206  CB  LYS A  71      32.764 -12.768   6.286  1.00 88.55           C  
ATOM    207  CG  LYS A  71      31.759 -11.965   5.451  1.00 97.63           C  
ATOM    208  CD  LYS A  71      32.360 -11.225   4.268  1.00100.77           C  
ATOM    209  CE  LYS A  71      32.979 -12.113   3.214  1.00109.06           C  
ATOM    210  NZ  LYS A  71      33.828 -11.283   2.331  1.00113.92           N  
ATOM    211  N   GLU A  72      33.888 -14.654   8.677  1.00 82.52           N  
ATOM    212  CA  GLU A  72      34.704 -15.764   9.159  1.00 84.68           C  
ATOM    213  C   GLU A  72      33.916 -16.764  10.062  1.00 84.57           C  
ATOM    214  O   GLU A  72      34.466 -17.782  10.463  1.00 88.75           O  
ATOM    215  CB  GLU A  72      35.949 -15.178   9.859  1.00 86.89           C  
ATOM    216  CG  GLU A  72      37.250 -15.966   9.808  1.00 94.17           C  
ATOM    217  CD  GLU A  72      37.959 -15.893   8.463  1.00 98.43           C  
ATOM    218  OE1 GLU A  72      37.408 -15.285   7.519  1.00100.20           O  
ATOM    219  OE2 GLU A  72      39.064 -16.437   8.328  1.00105.06           O  
ATOM    220  N   VAL A  73      32.648 -16.479  10.368  1.00 84.38           N  
ATOM    221  CA  VAL A  73      31.761 -17.384  11.120  1.00 94.51           C  
ATOM    222  C   VAL A  73      30.570 -17.896  10.290  1.00 91.12           C  
ATOM    223  O   VAL A  73      30.261 -19.080  10.347  1.00102.92           O  
ATOM    224  CB  VAL A  73      31.219 -16.684  12.406  1.00 94.77           C  
ATOM    225  CG1 VAL A  73      30.224 -17.565  13.168  1.00 91.19           C  
ATOM    226  CG2 VAL A  73      32.381 -16.286  13.308  1.00 95.34           C  
ATOM    227  N   TYR A  74      29.892 -17.004   9.566  1.00 89.45           N  
ATOM    228  CA  TYR A  74      28.683 -17.317   8.777  1.00 86.36           C  
ATOM    229  C   TYR A  74      28.871 -17.303   7.250  1.00 80.65           C  
ATOM    230  O   TYR A  74      27.944 -17.673   6.527  1.00 75.20           O  
ATOM    231  CB  TYR A  74      27.556 -16.338   9.156  1.00 94.26           C  
ATOM    232  CG  TYR A  74      27.222 -16.364  10.630  1.00 96.86           C  
ATOM    233  CD1 TYR A  74      26.747 -17.530  11.226  1.00100.66           C  
ATOM    234  CD2 TYR A  74      27.388 -15.234  11.437  1.00 93.87           C  
ATOM    235  CE1 TYR A  74      26.446 -17.575  12.579  1.00 99.02           C  
ATOM    236  CE2 TYR A  74      27.096 -15.275  12.787  1.00 93.29           C  
ATOM    237  CZ  TYR A  74      26.619 -16.448  13.351  1.00 97.30           C  
ATOM    238  OH  TYR A  74      26.314 -16.520  14.689  1.00 97.47           O  
ATOM    239  N   GLY A  75      30.039 -16.861   6.768  1.00 77.61           N  
ATOM    240  CA  GLY A  75      30.374 -16.866   5.337  1.00 77.70           C  
ATOM    241  C   GLY A  75      29.789 -15.723   4.522  1.00 85.78           C  
ATOM    242  O   GLY A  75      30.522 -14.856   4.035  1.00 86.70           O  
ATOM    243  N   GLN A  76      28.475 -15.762   4.342  1.00 98.86           N  
ATOM    244  CA  GLN A  76      27.725 -14.730   3.625  1.00102.53           C  
ATOM    245  C   GLN A  76      27.108 -13.830   4.689  1.00105.10           C  
ATOM    246  O   GLN A  76      26.289 -14.296   5.488  1.00 97.12           O  
ATOM    247  CB  GLN A  76      26.636 -15.348   2.719  1.00105.42           C  
ATOM    248  CG  GLN A  76      27.082 -15.758   1.314  1.00112.28           C  
ATOM    249  CD  GLN A  76      27.341 -17.268   1.150  1.00127.80           C  
ATOM    250  OE1 GLN A  76      27.886 -17.936   2.037  1.00126.46           O  
ATOM    251  NE2 GLN A  76      26.950 -17.802   0.002  1.00133.04           N  
ATOM    252  N   VAL A  77      27.535 -12.560   4.718  1.00103.27           N  
ATOM    253  CA  VAL A  77      26.997 -11.545   5.639  1.00 96.21           C  
ATOM    254  C   VAL A  77      26.465 -10.371   4.817  1.00 93.60           C  
ATOM    255  O   VAL A  77      27.204  -9.755   4.053  1.00 92.72           O  
ATOM    256  CB  VAL A  77      28.062 -11.066   6.649  1.00 97.42           C  
ATOM    257  CG1 VAL A  77      27.702  -9.730   7.288  1.00102.72           C  
ATOM    258  CG2 VAL A  77      28.280 -12.109   7.725  1.00101.12           C  
ATOM    259  N   LEU A  78      25.188 -10.060   4.993  1.00 96.20           N  
ATOM    260  CA  LEU A  78      24.522  -9.064   4.165  1.00102.68           C  
ATOM    261  C   LEU A  78      24.632  -7.664   4.752  1.00101.52           C  
ATOM    262  O   LEU A  78      24.243  -7.437   5.893  1.00110.54           O  
ATOM    263  CB  LEU A  78      23.047  -9.434   3.999  1.00109.24           C  
ATOM    264  CG  LEU A  78      22.151  -8.452   3.237  1.00107.58           C  
ATOM    265  CD1 LEU A  78      22.722  -8.189   1.839  1.00104.09           C  
ATOM    266  CD2 LEU A  78      20.733  -8.993   3.193  1.00109.40           C  
ATOM    267  N   THR A  79      25.120  -6.718   3.958  1.00102.98           N  
ATOM    268  CA  THR A  79      25.315  -5.353   4.432  1.00105.74           C  
ATOM    269  C   THR A  79      24.995  -4.345   3.319  1.00113.63           C  
ATOM    270  O   THR A  79      24.531  -4.741   2.241  1.00118.62           O  
ATOM    271  CB  THR A  79      26.743  -5.185   4.987  1.00104.65           C  
ATOM    272  OG1 THR A  79      26.825  -3.989   5.765  1.00104.89           O  
ATOM    273  CG2 THR A  79      27.793  -5.163   3.864  1.00104.71           C  
ATOM    274  N   ASN A  80      25.172  -3.071   3.617  1.00119.65           N  
ATOM    275  CA  ASN A  80      24.883  -2.021   2.672  1.00122.01           C  
ATOM    276  C   ASN A  80      26.075  -1.110   2.604  1.00129.15           C  
ATOM    277  O   ASN A  80      26.590  -0.690   3.624  1.00127.57           O  
ATOM    278  CB  ASN A  80      23.703  -1.239   3.183  1.00120.41           C  
ATOM    279  CG  ASN A  80      23.825  -0.951   4.643  1.00110.02           C  
ATOM    280  OD1 ASN A  80      24.769  -1.385   5.272  1.00112.14           O  
ATOM    281  ND2 ASN A  80      22.884  -0.220   5.189  1.00 97.53           N  
ATOM    282  N   PRO A  81      26.484  -0.757   1.395  1.00134.74           N  
ATOM    283  CA  PRO A  81      27.649   0.077   1.110  1.00128.84           C  
ATOM    284  C   PRO A  81      27.454   1.524   1.508  1.00105.95           C  
ATOM    285  O   PRO A  81      26.334   1.996   1.497  1.00 83.72           O  
ATOM    286  CB  PRO A  81      27.736  -0.003  -0.404  1.00140.35           C  
ATOM    287  CG  PRO A  81      26.306  -0.081  -0.823  1.00143.31           C  
ATOM    288  CD  PRO A  81      25.605  -0.889   0.226  1.00136.78           C  
ATOM    289  N   SER A  82      28.540   2.213   1.832  1.00 30.00           N  
ATOM    290  CA  SER A  82      28.498   3.622   2.215  1.00 30.00           C  
ATOM    291  C   SER A  82      27.423   3.944   3.239  1.00 30.00           C  
ATOM    292  O   SER A  82      27.280   3.236   4.227  1.00 30.00           O  
ATOM    293  CB  SER A  82      28.318   4.503   0.985  1.00 30.00           C  
ATOM    294  OG  SER A  82      28.231   5.867   1.354  1.00 30.00           O  
ATOM    295  N   GLY A  83      26.693   5.021   3.001  1.00100.46           N  
ATOM    296  CA  GLY A  83      25.598   5.386   3.875  1.00116.81           C  
ATOM    297  C   GLY A  83      24.253   4.796   3.392  1.00133.75           C  
ATOM    298  O   GLY A  83      24.220   4.326   2.245  1.00129.24           O  
ATOM    299  N   ALA A  84      23.177   4.802   4.223  1.00148.75           N  
ATOM    300  CA  ALA A  84      21.807   4.271   3.836  1.00147.09           C  
ATOM    301  C   ALA A  84      20.607   4.708   4.801  1.00148.30           C  
ATOM    302  O   ALA A  84      20.818   4.625   6.007  1.00116.14           O  
ATOM    303  CB  ALA A  84      21.839   2.742   3.757  1.00137.55           C  
ATOM    304  N   ASN A  85      19.443   5.178   4.277  1.00161.74           N  
ATOM    305  CA  ASN A  85      18.232   5.595   5.023  1.00158.60           C  
ATOM    306  C   ASN A  85      17.149   4.447   4.761  1.00156.68           C  
ATOM    307  O   ASN A  85      17.441   3.298   5.135  1.00175.09           O  
ATOM    308  CB  ASN A  85      17.801   7.071   4.686  1.00155.07           C  
ATOM    309  CG  ASN A  85      18.816   8.139   5.129  1.00145.58           C  
ATOM    310  OD1 ASN A  85      18.639   9.340   4.895  1.00156.10           O  
ATOM    311  ND2 ASN A  85      19.863   7.700   5.798  1.00123.63           N  
ATOM    312  N   MET A  86      16.064   4.658   3.988  1.00148.58           N  
ATOM    313  CA  MET A  86      14.921   3.684   3.846  1.00143.72           C  
ATOM    314  C   MET A  86      15.053   2.913   2.543  1.00139.95           C  
ATOM    315  O   MET A  86      14.354   1.947   2.249  1.00121.73           O  
ATOM    316  CB  MET A  86      13.555   4.421   3.834  1.00153.30           C  
ATOM    317  CG  MET A  86      12.351   3.544   3.626  1.00161.17           C  
ATOM    318  SD  MET A  86      12.258   2.424   5.009  1.00166.80           S  
ATOM    319  CE  MET A  86      10.685   1.629   4.711  1.00152.26           C  
ATOM    320  N   ILE A  87      15.992   3.385   1.757  1.00156.49           N  
ATOM    321  CA  ILE A  87      16.215   2.879   0.430  1.00164.32           C  
ATOM    322  C   ILE A  87      17.313   1.855   0.540  1.00161.18           C  
ATOM    323  O   ILE A  87      18.167   1.747  -0.325  1.00170.78           O  
ATOM    324  CB  ILE A  87      16.627   3.963  -0.572  1.00167.38           C  
ATOM    325  CG1 ILE A  87      15.467   4.926  -0.816  1.00156.75           C  
ATOM    326  CG2 ILE A  87      17.033   3.325  -1.887  1.00170.51           C  
ATOM    327  CD1 ILE A  87      15.833   6.176  -1.580  1.00147.95           C  
ATOM    328  N   THR A  88      17.243   1.126   1.639  1.00146.70           N  
ATOM    329  CA  THR A  88      18.126  -0.018   1.833  1.00142.72           C  
ATOM    330  C   THR A  88      17.491  -1.369   1.338  1.00138.16           C  
ATOM    331  O   THR A  88      18.164  -2.396   1.418  1.00108.18           O  
ATOM    332  CB  THR A  88      18.621  -0.197   3.284  1.00145.24           C  
ATOM    333  OG1 THR A  88      19.135  -1.528   3.451  1.00137.66           O  
ATOM    334  CG2 THR A  88      17.479   0.091   4.276  1.00148.88           C  
ATOM    335  N   GLY A  89      16.230  -1.421   0.858  1.00133.90           N  
ATOM    336  CA  GLY A  89      15.679  -2.643   0.309  1.00125.67           C  
ATOM    337  C   GLY A  89      16.612  -3.077  -0.855  1.00133.56           C  
ATOM    338  O   GLY A  89      16.927  -4.274  -0.988  1.00122.02           O  
ATOM    339  N   ILE A  90      17.003  -2.136  -1.753  1.00146.52           N  
ATOM    340  CA  ILE A  90      18.030  -2.408  -2.809  1.00149.34           C  
ATOM    341  C   ILE A  90      19.244  -3.226  -2.199  1.00158.15           C  
ATOM    342  O   ILE A  90      19.686  -4.232  -2.782  1.00159.98           O  
ATOM    343  CB  ILE A  90      18.669  -1.128  -3.472  1.00139.65           C  
ATOM    344  CG1 ILE A  90      17.571  -0.210  -4.013  1.00130.46           C  
ATOM    345  CG2 ILE A  90      19.641  -1.522  -4.569  1.00129.85           C  
ATOM    346  CD1 ILE A  90      18.085   1.076  -4.621  1.00120.11           C  
ATOM    347  N   ALA A  91      19.814  -2.785  -1.055  1.00156.74           N  
ATOM    348  CA  ALA A  91      20.924  -3.577  -0.439  1.00148.78           C  
ATOM    349  C   ALA A  91      20.367  -5.022  -0.158  1.00154.66           C  
ATOM    350  O   ALA A  91      20.947  -6.030  -0.596  1.00149.14           O  
ATOM    351  CB  ALA A  91      21.501  -2.994   0.871  1.00135.96           C  
ATOM    352  N   THR A  92      19.235  -5.146   0.561  1.00156.50           N  
ATOM    353  CA  THR A  92      18.678  -6.524   0.835  1.00144.55           C  
ATOM    354  C   THR A  92      18.268  -7.425  -0.392  1.00141.60           C  
ATOM    355  O   THR A  92      17.966  -8.611  -0.170  1.00145.11           O  
ATOM    356  CB  THR A  92      17.418  -6.580   1.756  1.00129.49           C  
ATOM    357  OG1 THR A  92      16.238  -6.296   0.981  1.00135.12           O  
ATOM    358  CG2 THR A  92      17.572  -5.649   2.967  1.00111.57           C  
ATOM    359  N   THR A  93      18.113  -6.860  -1.607  1.00141.88           N  
ATOM    360  CA  THR A  93      17.760  -7.601  -2.858  1.00131.38           C  
ATOM    361  C   THR A  93      18.578  -7.166  -4.100  1.00110.18           C  
ATOM    362  O   THR A  93      19.789  -6.999  -4.032  1.00 84.04           O  
ATOM    363  CB  THR A  93      16.248  -7.424  -3.126  1.00133.75           C  
ATOM    364  OG1 THR A  93      15.939  -6.022  -3.143  1.00135.86           O  
ATOM    365  CG2 THR A  93      15.396  -8.153  -2.054  1.00127.13           C  
ATOM    366  N   LYS A 104      18.874 -19.283   9.183  1.00156.62           N  
ATOM    367  CA  LYS A 104      20.238 -19.608   8.772  1.00150.13           C  
ATOM    368  C   LYS A 104      21.175 -18.409   9.029  1.00128.38           C  
ATOM    369  O   LYS A 104      21.940 -18.410   9.999  1.00 95.11           O  
ATOM    370  CB  LYS A 104      20.254 -20.086   7.283  1.00151.49           C  
ATOM    371  CG  LYS A 104      19.573 -21.423   6.918  1.00139.86           C  
ATOM    372  CD  LYS A 104      19.639 -21.764   5.429  1.00136.30           C  
ATOM    373  CE  LYS A 104      18.980 -23.106   5.081  1.00137.54           C  
ATOM    3