CNRS Nantes University US2B US2B
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***  Fhb7  ***

elNémo ID: 2501180908401208128

Job options:

ID        	=	 2501180908401208128
JOBID     	=	 Fhb7
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER Fhb7

HEADER    TRANSFERASE                             13-JUL-23   8K2O              
TITLE     CRYSTAL STRUCTURE OF FHB7-M10                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FHB7-M10;                                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THINOPYRUM ELONGATUM;                           
SOURCE   3 ORGANISM_TAXID: 4588;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FHB7, TRANSFERASE, DETOXIFICATION, DEOXYNIVALENOL                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YANG,X.G.LEI,J.Y.XIAO                                               
REVDAT   1   13-MAR-24 8K2O    0                                                
JRNL        AUTH   J.YANG,K.LIANG,H.KE,Y.ZHANG,Q.MENG,L.GAO,J.FAN,G.LI,H.ZHOU,  
JRNL        AUTH 2 J.XIAO,X.LEI                                                 
JRNL        TITL   ENZYMATIC DEGRADATION OF DEOXYNIVALENOL WITH THE ENGINEERED  
JRNL        TITL 2 DETOXIFICATION ENZYME FHB7.                                  
JRNL        REF    JACS AU                       V.   4   619 2024              
JRNL        REFN                   ESSN 2691-3704                               
JRNL        PMID   38425922                                                     
JRNL        DOI    10.1021/JACSAU.3C00696                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.20.1                                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 79493                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.510                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 51.8000 -  4.8400    1.00     5824   150  0.1810 0.1791        
REMARK   3     2  4.8300 -  3.8400    1.00     5628   146  0.1654 0.1974        
REMARK   3     3  3.8400 -  3.3500    1.00     5600   144  0.1896 0.2266        
REMARK   3     4  3.3500 -  3.0500    1.00     5533   143  0.2037 0.2292        
REMARK   3     5  3.0500 -  2.8300    1.00     5535   143  0.2137 0.2501        
REMARK   3     6  2.8300 -  2.6600    1.00     5511   142  0.2203 0.2730        
REMARK   3     7  2.6600 -  2.5300    1.00     5516   142  0.2228 0.2864        
REMARK   3     8  2.5300 -  2.4200    1.00     5499   143  0.2170 0.2559        
REMARK   3     9  2.4200 -  2.3200    1.00     5508   142  0.2185 0.3017        
REMARK   3    10  2.3200 -  2.2400    1.00     5462   141  0.2219 0.2560        
REMARK   3    11  2.2400 -  2.1700    1.00     5501   141  0.2238 0.2690        
REMARK   3    12  2.1700 -  2.1100    1.00     5446   139  0.2302 0.2457        
REMARK   3    13  2.1100 -  2.0600    1.00     5475   142  0.2400 0.3027        
REMARK   3    14  2.0600 -  2.0100    1.00     5457   140  0.2595 0.3036        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :  0.050           1263                                  
REMARK   3   PLANARITY :  0.010           1523                                  
REMARK   3   DIHEDRAL  :  6.023           1179                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2642 -13.5486 -37.0535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2075 T22:   0.1674                                     
REMARK   3      T33:   0.2141 T12:   0.0289                                     
REMARK   3      T13:  -0.0119 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3697 L22:   0.0750                                     
REMARK   3      L33:   0.2329 L12:   0.1125                                     
REMARK   3      L13:  -0.1229 L23:  -0.0277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0005 S12:  -0.0393 S13:  -0.0307                       
REMARK   3      S21:   0.0010 S22:   0.0044 S23:   0.0055                       
REMARK   3      S31:   0.0060 S32:   0.0187 S33:   0.0000                       
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 8K2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300039414.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-23                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
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 PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79602                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.90                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.05700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 7YOC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M BIS        
REMARK 280  -TRIS, PH 5.5, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.75300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.59150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.07800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.59150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.75300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.07800            
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, 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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     PHE A    69                                                      
REMARK 465     GLY A    70                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     ALA C    68                                                      
REMARK 465     PHE C    69                                                      
REMARK 465     GLY C    70                                                      
REMARK 465     LEU C    71                                                      
REMARK 465     LEU C   136                                                      
REMARK 465     SER C   137                                                      
REMARK 465     GLU C   138                                                      
REMARK 465     ILE C   139                                                      
REMARK 465     ARG C   140                                                      
REMARK 465     ALA C   141                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     SER D    67                                                      
REMARK 465     ALA D    68                                                      
REMARK 465     PHE D    69                                                      
REMARK 465     GLY D    70                                                      
REMARK 465     LEU D   136                                                      
REMARK 465     SER D   137                                                      
REMARK 465     GLU D   138                                                      
REMARK 465     TRP D   193                                                      
REMARK 465     ASP D   194                                                      
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     GLU A  65    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  71    CG   CD1  CD2                                       
REMARK 470     LEU A  72    CG   CD1  CD2                                       
REMARK 470     LYS A  73    CG   CD   CE   NZ                                   
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 470     LEU A 136    CG   CD1  CD2                                       
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 139    CG1  CG2  CD1                                       
REMARK 470     ARG A 140    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  65    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  69    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B  71    CG   CD1  CD2                                       
REMARK 470     LEU B  72    CG   CD1  CD2                                       
REMARK 470     LEU B 136    CG   CD1  CD2                                       
REMARK 470     ARG B 140    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 195    CG   OD1  OD2                                       
REMARK 470     LYS C 120    CG   CD   CE   NZ                                   
REMARK 470     GLN C 131    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 190    CG   CD1  CD2                                       
REMARK 470     GLU C 201    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 120    CG   CD   CE   NZ                                   
REMARK 470     ILE D 139    CG1  CG2  CD1                                       
REMARK 470     ARG D 140    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 178    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 190    CG   CD1  CD2                                       
REMARK 470     GLU D 197    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   305     O    HOH A   426              1.83            
REMARK 500   O    SER A    67     O    HOH A   301              1.91            
REMARK 500   O    HOH A   432     O    HOH A   452              1.92            
REMARK 500   O    HOH D   417     O    HOH D   426              1.93            
REMARK 500   O    HOH A   337     O    HOH A   467              1.93            
REMARK 500   O    HOH C   473     O    HOH D   424              1.94            
REMARK 500   OD2  ASP B   122     O    HOH B   301              2.01            
REMARK 500   O    ASP B    54     O    HOH B   302              2.02            
REMARK 500   NZ   LYS C   223     O    HOH C   301              2.02            
REMARK 500   O    THR D    25     O    HOH D   301              2.03            
REMARK 500   O    HOH C   328     O    HOH C   471              2.04            
REMARK 500   NH2  ARG B   186     O    HOH B   303              2.04            
REMARK 500   O    HOH C   334     O    HOH C   463              2.08            
REMARK 500   O    ASP A    54     O    HOH A   302              2.08            
REMARK 500   O    THR B     9     O    HOH B   304              2.10            
REMARK 500   O    HOH D   307     O    HOH D   378              2.10            
REMARK 500   O    HOH B   462     O    HOH B   465              2.12            
REMARK 500   O    HOH C   309     O    HOH C   315              2.12            
REMARK 500   OD2  ASP D    98     O    HOH D   302              2.13            
REMARK 500   NZ   LYS D    41     OE1  GLN D   104              2.14            
REMARK 500   OD2  ASP A   147     O    HOH A   303              2.14            
REMARK 500   O    ASP C    54     O    HOH C   302              2.17            
REMARK 500   O    HOH A   310     O    HOH C   464              2.18            
REMARK 500   N    ILE D   139     O    HOH D   303              2.18            
REMARK 500   O    ALA B   261     O    HOH B   305              2.19            
REMARK 500   O    HOH B   342     O    HOH B   398              2.19            
REMARK 500   N    LEU C    72     O    HOH C   303              2.19            
REMARK 500   OG   SER B   256     O    HOH B   306              2.19            
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    LEU A  52   CA  -  CB  -  CG  ANGL. DEV. =  22.6 DEGREES          
REMARK 500    GLY A  63   C   -  N   -  CA  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    GLY B  63   C   -  N   -  CA  ANGL. DEV. = -18.3 DEGREES          
REMARK 500    LEU C  52   CA  -  CB  -  CG  ANGL. DEV. =  14.0 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    GLN A  18     -132.13   -102.64                                   
REMARK 500    CYS A  27       -1.68   -143.96                                   
REMARK 500    ASP A  54      156.60    -49.91                                   
REMARK 500    ILE A  55      -62.33     82.87                                   
REMARK 500    ASP A  95      112.05     77.62                                   
REMARK 500    ARG A 140     -127.12     56.73                                   
REMARK 500    SER A 142      108.28    -48.41                                   
REMARK 500    GLU A 144      -38.99     78.67                                   
REMARK 500    ARG A 186      -59.23    105.00                                   
REMARK 500    LEU A 196      -65.82     99.33                                   
REMARK 500    MET A 198      107.92     74.41                                   
REMARK 500    LEU A 231       39.84    -99.78                                   
REMARK 500    GLN B  18     -131.93   -100.63                                   
REMARK 500    CYS B  27       -0.19   -143.47                                   
REMARK 500    ILE B  55      -60.14     81.91                                   
REMARK 500    SER B  67     -147.62   -111.59                                   
REMARK 500    PHE B  69      -47.88   -136.95                                   
REMARK 500    LEU B  71     -115.18    -82.83                                   
REMARK 500    LEU B  72       70.61   -169.80                                   
REMARK 500    LYS B  73      -64.04     59.61                                   
REMARK 500    ASP B  95      119.43     71.83                                   
REMARK 500    LEU B 121       72.44   -109.16                                   
REMARK 500    GLU B 144      -37.03     75.50                                   
REMARK 500    LEU B 172       21.99   -140.61                                   
REMARK 500    ASP B 173      102.40     56.73                                   
REMARK 500    PRO B 174       37.54    -72.19                                   
REMARK 500    ALA B 175      -31.83   -131.80                                   
REMARK 500    ARG B 186      -53.11     92.96                                   
REMARK 500    LEU B 196      -38.22    123.25                                   
REMARK 500    MET B 198      110.42     77.99                                   
REMARK 500    LEU B 231       41.44    -99.64                                   
REMARK 500    VAL C  22     -169.25    -67.02                                   
REMARK 500    ALA C  23      -41.95     65.77                                   
REMARK 500    CYS C  27       -6.28   -146.82                                   
REMARK 500    ILE C  55      -64.02     75.34                                   
REMARK 500    ASP C  95      116.47     73.50                                   
REMARK 500    GLU C 144      -37.28     67.19                                   
REMARK 500    LEU C 190      116.94    -24.96                                   
REMARK 500    CYS D  27        0.04   -152.39                                   
REMARK 500    ILE D  55      -63.95     83.52                                   
REMARK 500    ILE D  62     -167.15   -125.43                                   
REMARK 500    ASP D  95      115.34     65.92                                   
REMARK 500    ASP D 122       48.60    -84.49                                   
REMARK 500    ALA D 141      118.89     63.32                                   
REMARK 500    SER D 142      108.73    -11.56                                   
REMARK 500    ARG D 186      -49.32    161.70                                   
REMARK 500    SER D 191      -30.96   -147.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU C  190     SER C  191                 -149.31                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG C  19         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  8K2O A   -1   283  PDB    8K2O     8K2O            -1    283             
DBREF  8K2O B   -1   283  PDB    8K2O     8K2O            -1    283             
DBREF  8K2O C   -1   283  PDB    8K2O     8K2O            -1    283             
DBREF  8K2O D   -1   283  PDB    8K2O     8K2O            -1    283             
SEQRES   1 A  285  GLY SER MET ALA THR SER THR SER THR SER THR PRO ILE          
SEQRES   2 A  285  ILE PHE TYR ASP ILE ALA GLN ARG PRO PRO VAL ALA GLU          
SEQRES   3 A  285  THR CYS CYS ALA PRO ASN PRO TRP LYS SER ARG LEU ALA          
SEQRES   4 A  285  LEU ASN PHE LYS ALA VAL PRO TYR THR THR THR TRP VAL          
SEQRES   5 A  285  LYS LEU PRO ASP ILE GLU ARG VAL CYS LYS GLU ILE GLY          
SEQRES   6 A  285  ALA GLU PRO SER ALA PHE GLY LEU LEU LYS GLU GLY LYS          
SEQRES   7 A  285  PRO TYR TYR THR LEU PRO ILE ILE HIS ASP PRO ALA THR          
SEQRES   8 A  285  ASP SER LEU ILE GLY ASP SER PHE ASP ILE ALA ALA TYR          
SEQRES   9 A  285  LEU GLN ARG THR TYR PRO ALA SER GLY ALA GLY ASP LEU          
SEQRES  10 A  285  PHE PRO PRO GLN LYS LEU ASP TYR ALA VAL GLY ARG ASP          
SEQRES  11 A  285  MET GLN GLN LEU LEU PHE PRO LEU SER GLU ILE ARG ALA          
SEQRES  12 A  285  SER PRO GLU LEU ALA ASP TYR ALA ARG PHE ASN SER ASN          
SEQRES  13 A  285  VAL ASP ALA ALA PHE THR ALA HIS VAL GLY LEU MET VAL          
SEQRES  14 A  285  HIS GLY LEU PRO LEU ASP PRO ALA THR ALA GLU VAL THR          
SEQRES  15 A  285  LYS ALA GLU PHE VAL ARG ARG ALA GLY LEU SER SER TRP          
SEQRES  16 A  285  ASP ASP LEU GLU MET VAL GLY GLU ALA ARG ASP LYS MET          
SEQRES  17 A  285  MET GLN SER PHE ARG ASN MET LEU GLY ASP LEU ALA ALA          
SEQRES  18 A  285  LEU PHE ARG LYS ASP ALA SER GLY PRO PHE LEU LEU GLY          
SEQRES  19 A  285  GLN ARG ALA THR TYR ALA ASP MET ILE VAL GLY GLY TRP          
SEQRES  20 A  285  LEU ARG MET MET ARG ALA THR LEU PRO VAL SER GLU TRP          
SEQRES  21 A  285  GLN GLU ALA ARG ALA TRP HIS GLY GLY ILE PHE GLY ARG          
SEQRES  22 A  285  LEU HIS ASP ALA LEU ASP LYS TYR ALA GLU VAL LYS              
SEQRES   1 B  285  GLY SER MET ALA THR SER THR SER THR SER THR PRO ILE          
SEQRES   2 B  285  ILE PHE TYR ASP ILE ALA GLN ARG PRO PRO VAL ALA GLU          
SEQRES   3 B  285  THR CYS CYS ALA PRO ASN PRO TRP LYS SER ARG LEU ALA          
SEQRES   4 B  285  LEU ASN PHE LYS ALA VAL PRO TYR THR THR THR TRP VAL          
SEQRES   5 B  285  LYS LEU PRO ASP ILE GLU ARG VAL CYS LYS GLU ILE GLY          
SEQRES   6 B  285  ALA GLU PRO SER ALA PHE GLY LEU LEU LYS GLU GLY LYS          
SEQRES   7 B  285  PRO TYR TYR THR LEU PRO ILE ILE HIS ASP PRO ALA THR          
SEQRES   8 B  285  ASP SER LEU ILE GLY ASP SER PHE ASP ILE ALA ALA TYR          
SEQRES   9 B  285  LEU GLN ARG THR TYR PRO ALA SER GLY ALA GLY ASP LEU          
SEQRES  10 B  285  PHE PRO PRO GLN LYS LEU ASP TYR ALA VAL GLY ARG ASP          
SEQRES  11 B  285  MET GLN GLN LEU LEU PHE PRO LEU SER GLU ILE ARG ALA          
SEQRES  12 B  285  SER PRO GLU LEU ALA ASP TYR ALA ARG PHE ASN SER ASN          
SEQRES  13 B  285  VAL ASP ALA ALA PHE THR ALA HIS VAL GLY LEU MET VAL          
SEQRES  14 B  285  HIS GLY LEU PRO LEU ASP PRO ALA THR ALA GLU VAL THR          
SEQRES  15 B  285  LYS ALA GLU PHE VAL ARG ARG ALA GLY LEU SER SER TRP          
SEQRES  16 B  285  ASP ASP LEU GLU MET VAL GLY GLU ALA ARG ASP LYS MET          
SEQRES  17 B  285  MET GLN SER PHE ARG ASN MET LEU GLY ASP LEU ALA ALA          
SEQRES  18 B  285  LEU PHE ARG LYS ASP ALA SER GLY PRO PHE LEU LEU GLY          
SEQRES  19 B  285  GLN ARG ALA THR TYR ALA ASP MET ILE VAL GLY GLY TRP          
SEQRES  20 B  285  LEU ARG MET MET ARG ALA THR LEU PRO VAL SER GLU TRP          
SEQRES  21 B  285  GLN GLU ALA ARG ALA TRP HIS GLY GLY ILE PHE GLY ARG          
SEQRES  22 B  285  LEU HIS ASP ALA LEU ASP LYS TYR ALA GLU VAL LYS              
SEQRES   1 C  285  GLY SER MET ALA THR SER THR SER THR SER THR PRO ILE          
SEQRES   2 C  285  ILE PHE TYR ASP ILE ALA GLN ARG PRO PRO VAL ALA GLU          
SEQRES   3 C  285  THR CYS CYS ALA PRO ASN PRO TRP LYS SER ARG LEU ALA          
SEQRES   4 C  285  LEU ASN PHE LYS ALA VAL PRO TYR THR THR THR TRP VAL          
SEQRES   5 C  285  LYS LEU PRO ASP ILE GLU ARG VAL CYS LYS GLU ILE GLY          
SEQRES   6 C  285  ALA GLU PRO SER ALA PHE GLY LEU LEU LYS GLU GLY LYS          
SEQRES   7 C  285  PRO TYR TYR THR LEU PRO ILE ILE HIS ASP PRO ALA THR          
SEQRES   8 C  285  ASP SER LEU ILE GLY ASP SER PHE ASP ILE ALA ALA TYR          
SEQRES   9 C  285  LEU GLN ARG THR TYR PRO ALA SER GLY ALA GLY ASP LEU          
SEQRES  10 C  285  PHE PRO PRO GLN LYS LEU ASP TYR ALA VAL GLY ARG ASP          
SEQRES  11 C  285  MET GLN GLN LEU LEU PHE PRO LEU SER GLU ILE ARG ALA          
SEQRES  12 C  285  SER PRO GLU LEU ALA ASP TYR ALA ARG PHE ASN SER ASN          
SEQRES  13 C  285  VAL ASP ALA ALA PHE THR ALA HIS VAL GLY LEU MET VAL          
SEQRES  14 C  285  HIS GLY LEU PRO LEU ASP PRO ALA THR ALA GLU VAL THR          
SEQRES  15 C  285  LYS ALA GLU PHE VAL ARG ARG ALA GLY LEU SER SER TRP          
SEQRES  16 C  285  ASP ASP LEU GLU MET VAL GLY GLU ALA ARG ASP LYS MET          
SEQRES  17 C  285  MET GLN SER PHE ARG ASN MET LEU GLY ASP LEU ALA ALA          
SEQRES  18 C  285  LEU PHE ARG LYS ASP ALA SER GLY PRO PHE LEU LEU GLY          
SEQRES  19 C  285  GLN ARG ALA THR TYR ALA ASP MET ILE VAL GLY GLY TRP          
SEQRES  20 C  285  LEU ARG MET MET ARG ALA THR LEU PRO VAL SER GLU TRP          
SEQRES  21 C  285  GLN GLU ALA ARG ALA TRP HIS GLY GLY ILE PHE GLY ARG          
SEQRES  22 C  285  LEU HIS ASP ALA LEU ASP LYS TYR ALA GLU VAL LYS              
SEQRES   1 D  285  GLY SER MET ALA THR SER THR SER THR SER THR PRO ILE          
SEQRES   2 D  285  ILE PHE TYR ASP ILE ALA GLN ARG PRO PRO VAL ALA GLU          
SEQRES   3 D  285  THR CYS CYS ALA PRO ASN PRO TRP LYS SER ARG LEU ALA          
SEQRES   4 D  285  LEU ASN PHE LYS ALA VAL PRO TYR THR THR THR TRP VAL          
SEQRES   5 D  285  LYS LEU PRO ASP ILE GLU ARG VAL CYS LYS GLU ILE GLY          
SEQRES   6 D  285  ALA GLU PRO SER ALA PHE GLY LEU LEU LYS GLU GLY LYS          
SEQRES   7 D  285  PRO TYR TYR THR LEU PRO ILE ILE HIS ASP PRO ALA THR          
SEQRES   8 D  285  ASP SER LEU ILE GLY ASP SER PHE ASP ILE ALA ALA TYR          
SEQRES   9 D  285  LEU GLN ARG THR TYR PRO ALA SER GLY ALA GLY ASP LEU          
SEQRES  10 D  285  PHE PRO PRO GLN LYS LEU ASP TYR ALA VAL GLY ARG ASP          
SEQRES  11 D  285  MET GLN GLN LEU LEU PHE PRO LEU SER GLU ILE ARG ALA          
SEQRES  12 D  285  SER PRO GLU LEU ALA ASP TYR ALA ARG PHE ASN SER ASN          
SEQRES  13 D  285  VAL ASP ALA ALA PHE THR ALA HIS VAL GLY LEU MET VAL          
SEQRES  14 D  285  HIS GLY LEU PRO LEU ASP PRO ALA THR ALA GLU VAL THR          
SEQRES  15 D  285  LYS ALA GLU PHE VAL ARG ARG ALA GLY LEU SER SER TRP          
SEQRES  16 D  285  ASP ASP LEU GLU MET VAL GLY GLU ALA ARG ASP LYS MET          
SEQRES  17 D  285  MET GLN SER PHE ARG ASN MET LEU GLY ASP LEU ALA ALA          
SEQRES  18 D  285  LEU PHE ARG LYS ASP ALA SER GLY PRO PHE LEU LEU GLY          
SEQRES  19 D  285  GLN ARG ALA THR TYR ALA ASP MET ILE VAL GLY GLY TRP          
SEQRES  20 D  285  LEU ARG MET MET ARG ALA THR LEU PRO VAL SER GLU TRP          
SEQRES  21 D  285  GLN GLU ALA ARG ALA TRP HIS GLY GLY ILE PHE GLY ARG          
SEQRES  22 D  285  LEU HIS ASP ALA LEU ASP LYS TYR ALA GLU VAL LYS              
FORMUL   5  HOH   *688(H2 O)                                                    
HELIX    1 AA1 PRO A   21  CYS A   26  1                                   6    
HELIX    2 AA2 ALA A   28  ALA A   42  1                                  15    
HELIX    3 AA3 ILE A   55  ILE A   62  1                                   8    
HELIX    4 AA4 LEU A   72  LYS A   76  5                                   5    
HELIX    5 AA5 ASP A   95  TYR A  107  1                                  13    
HELIX    6 AA6 ASP A  128  PHE A  134  1                                   7    
HELIX    7 AA7 LEU A  145  ALA A  161  1                                  17    
HELIX    8 AA8 VAL A  163  HIS A  168  1                                   6    
HELIX    9 AA9 THR A  176  ALA A  188  1                                  13    
HELIX   10 AB1 TRP A  193  MET A  198  1                                   6    
HELIX   11 AB2 GLY A  200  LYS A  223  1                                  24    
HELIX   12 AB3 THR A  236  LEU A  253  1                                  18    
HELIX   13 AB4 PRO A  254  TRP A  264  1                                  11    
HELIX   14 AB5 GLY A  267  LEU A  276  1                                  10    
HELIX   15 AB6 ASP A  277  ALA A  280  5                                   4    
HELIX   16 AB7 PRO B   21  CYS B   26  1                                   6    
HELIX   17 AB8 ALA B   28  ALA B   42  1                                  15    
HELIX   18 AB9 ILE B   55  ILE B   62  1                                   8    
HELIX   19 AC1 ASP B   95  TYR B  107  1                                  13    
HELIX   20 AC2 ASP B  128  PHE B  134  1                                   7    
HELIX   21 AC3 LEU B  145  ALA B  161  1                                  17    
HELIX   22 AC4 HIS B  162  LEU B  170  5                                   9    
HELIX   23 AC5 THR B  176  ALA B  188  1                                  13    
HELIX   24 AC6 TRP B  193  MET B  198  1                                   6    
HELIX   25 AC7 VAL B  199  LYS B  223  1                                  25    
HELIX   26 AC8 THR B  236  LEU B  253  1                                  18    
HELIX   27 AC9 PRO B  254  ASP B  277  1                                  24    
HELIX   28 AD1 LYS B  278  ALA B  280  5                                   3    
HELIX   29 AD2 ALA C   28  ALA C   42  1                                  15    
HELIX   30 AD3 ILE C   55  ILE C   62  1                                   8    
HELIX   31 AD4 LEU C   72  LYS C   76  5                                   5    
HELIX   32 AD5 ASP C   95  TYR C  107  1                                  13    
HELIX   33 AD6 ASP C  128  PHE C  134  1                                   7    
HELIX   34 AD7 LEU C  145  HIS C  162  1                                  18    
HELIX   35 AD8 VAL C  163  HIS C  168  1                                   6    
HELIX   36 AD9 THR C  176  GLY C  189  1                                  14    
HELIX   37 AE1 SER C  192  MET C  198  5                                   7    
HELIX   38 AE2 GLY C  200  ARG C  222  1                                  23    
HELIX   39 AE3 THR C  236  LEU C  253  1                                  18    
HELIX   40 AE4 PRO C  254  ASP C  277  1                                  24    
HELIX   41 AE5 LYS C  278  ALA C  280  5                                   3    
HELIX   42 AE6 PRO D   21  CYS D   26  1                                   6    
HELIX   43 AE7 ALA D   28  ALA D   42  1                                  15    
HELIX   44 AE8 ILE D   55  ILE D   62  1                                   8    
HELIX   45 AE9 ASP D   95  TYR D  107  1                                  13    
HELIX   46 AF1 ASP D  128  PHE D  134  1                                   7    
HELIX   47 AF2 LEU D  145  ALA D  161  1                                  17    
HELIX   48 AF3 VAL D  163  HIS D  168  1                                   6    
HELIX   49 AF4 THR D  176  ALA D  188  1                                  13    
HELIX   50 AF5 VAL D  199  ARG D  222  1                                  24    
HELIX   51 AF6 THR D  236  LEU D  253  1                                  18    
HELIX   52 AF7 PRO D  254  ASP D  277  1                                  24    
HELIX   53 AF8 LYS D  278  ALA D  280  5                                   3    
SHEET    1 AA1 4 TYR A  45  VAL A  50  0                                        
SHEET    2 AA1 4 ILE A  11  ILE A  16  1  N  PHE A  13   O  THR A  46           
SHEET    3 AA1 4 ILE A  83  ASP A  86 -1  O  ILE A  83   N  TYR A  14           
SHEET    4 AA1 4 SER A  91  GLY A  94 -1  O  ILE A  93   N  ILE A  84           
SHEET    1 AA2 2 TYR A  78  THR A  80  0                                        
SHEET    2 AA2 2 TYR C  78  THR C  80 -1  O  TYR C  79   N  TYR A  79           
SHEET    1 AA3 4 TYR B  45  VAL B  50  0                                        
SHEET    2 AA3 4 ILE B  11  ILE B  16  1  N  ASP B  15   O  VAL B  50           
SHEET    3 AA3 4 ILE B  83  ASP B  86 -1  O  ILE B  83   N  TYR B  14           
SHEET    4 AA3 4 SER B  91  GLY B  94 -1  O  ILE B  93   N  ILE B  84           
SHEET    1 AA4 2 TYR B  78  THR B  80  0                                        
SHEET    2 AA4 2 TYR D  78  THR D  80 -1  O  TYR D  79   N  TYR B  79           
SHEET    1 AA5 4 TYR C  45  VAL C  50  0                                        
SHEET    2 AA5 4 ILE C  11  ILE C  16  1  N  PHE C  13   O  THR C  46           
SHEET    3 AA5 4 ILE C  83  HIS C  85 -1  O  ILE C  83   N  TYR C  14           
SHEET    4 AA5 4 LEU C  92  GLY C  94 -1  O  ILE C  93   N  ILE C  84           
SHEET    1 AA6 4 TYR D  45  VAL D  50  0                                        
SHEET    2 AA6 4 ILE D  11  ILE D  16  1  N  PHE D  13   O  THR D  48           
SHEET    3 AA6 4 ILE D  83  ASP D  86 -1  O  ILE D  83   N  TYR D  14           
SHEET    4 AA6 4 SER D  91  ILE D  93 -1  O  ILE D  93   N  ILE D  84           
CISPEP   1 PRO A   20    PRO A   21          0        -0.15                     
CISPEP   2 LEU A   81    PRO A   82          0         2.89                     
CISPEP   3 PRO B   20    PRO B   21          0        -8.64                     
CISPEP   4 LEU B   81    PRO B   82          0         0.69                     
CISPEP   5 PRO C   20    PRO C   21          0        -1.96                     
CISPEP   6 LEU C   81    PRO C   82          0         5.27                     
CISPEP   7 PRO D   20    PRO D   21          0        -1.11                     
CISPEP   8 LEU D   81    PRO D   82          0        -0.78                     
CRYST1   77.506  112.156  135.183  90.00  90.00  90.00 P 21 21 21   16          
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      0.012902  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008916  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007397        0.00000                         
ATOM   2096  N   SER B   8      -9.862 -12.235   6.789  1.00 65.03           N  
ANISOU 2096  N   SER B   8     7813   9456   7438   -338     23   -305       N  
ATOM   2097  CA  SER B   8      -9.126 -11.435   5.820  1.00 61.08           C  
ANISOU 2097  CA  SER B   8     7333   8909   6965   -324     26   -340       C  
ATOM   2098  C   SER B   8      -9.389 -11.975   4.419  1.00 60.53           C  
ANISOU 2098  C   SER B   8     7292   8747   6959   -276     15   -316       C  
ATOM   2099  O   SER B   8      -9.531 -13.190   4.236  1.00 60.27           O  
ANISOU 2099  O   SER B   8     7258   8702   6941   -254     -4   -256       O  
ATOM   2100  CB  SER B   8      -7.625 -11.448   6.137  1.00 60.47           C  
ANISOU 2100  CB  SER B   8     7237   8886   6854   -340     12   -322       C  
ATOM   2101  OG  SER B   8      -6.947 -10.394   5.472  1.00 60.49           O  
ANISOU 2101  OG  SER B   8     7255   8858   6871   -340     22   -371       O  
ATOM   2102  N   THR B   9      -9.470 -11.076   3.430  1.00 57.75           N  
ANISOU 2102  N   THR B   9     6966   8332   6645   -261     28   -363       N  
ATOM   2103  CA  THR B   9      -9.625 -11.446   2.022  1.00 52.02           C  
ANISOU 2103  CA  THR B   9     6267   7521   5977   -218     18   -347       C  
ATOM   2104  C   THR B   9      -8.453 -10.867   1.238  1.00 45.57           C  
ANISOU 2104  C   THR B   9     5462   6681   5173   -209     14   -363       C  
ATOM   2105  O   THR B   9      -8.609  -9.865   0.527  1.00 44.16           O  
ANISOU 2105  O   THR B   9     5303   6455   5020   -203     30   -412       O  
ATOM   2106  CB  THR B   9     -10.947 -10.954   1.432  1.00 51.99           C  
ANISOU 2106  CB  THR B   9     6285   7458   6011   -203     37   -382       C  
ATOM   2107  OG1 THR B   9     -11.310  -9.702   2.033  1.00 58.94           O  
ANISOU 2107  OG1 THR B   9     7162   8361   6872   -232     64   -445       O  
ATOM   2108  CG2 THR B   9     -12.059 -11.984   1.634  1.00 54.74           C  
ANISOU 2108  CG2 THR B   9     6630   7801   6368   -193     31   -344       C  
ATOM   2109  N   PRO B  10      -7.277 -11.481   1.326  1.00 40.45           N  
ANISOU 2109  N   PRO B  10     4799   6062   4507   -208     -6   -322       N  
ATOM   2110  CA  PRO B  10      -6.122 -10.964   0.589  1.00 36.86           C  
ANISOU 2110  CA  PRO B  10     4354   5588   4064   -200    -10   -337       C  
ATOM   2111  C   PRO B  10      -6.250 -11.240  -0.901  1.00 33.22           C  
ANISOU 2111  C   PRO B  10     3921   5040   3661   -159    -18   -327       C  
ATOM   2112  O   PRO B  10      -7.041 -12.074  -1.347  1.00 28.53           O  
ANISOU 2112  O   PRO B  10     3337   4407   3097   -134    -24   -297       O  
ATOM   2113  CB  PRO B  10      -4.939 -11.728   1.187  1.00 33.57           C  
ANISOU 2113  CB  PRO B  10     3910   5233   3612   -209    -32   -287       C  
ATOM   2114  CG  PRO B  10      -5.530 -12.967   1.771  1.00 41.51           C  
ANISOU 2114  CG  PRO B  10     4901   6260   4609   -203    -44   -231       C  
ATOM   2115  CD  PRO B  10      -7.011 -12.790   1.937  1.00 44.25           C  
ANISOU 2115  CD  PRO B  10     5259   6586   4969   -206    -27   -255       C  
ATOM   2116  N   ILE B  11      -5.440 -10.516  -1.678  1.00 28.71           N  
ANISOU 2116  N   ILE B  11     3363   4441   3104   -153    -15   -354       N  
ATOM   2117  CA  ILE B  11      -5.349 -10.792  -3.104  1.00 28.44           C  
ANISOU 2117  CA  ILE B  11     3353   4333   3121   -115    -24   -342       C  
ATOM   2118  C   ILE B  11      -4.859 -12.225  -3.308  1.00 27.14           C  
ANISOU 2118  C   ILE B  11     3180   4168   2963    -92    -49   -275       C  
ATOM   2119  O   ILE B  11      -3.997 -12.719  -2.572  1.00 29.49           O  
ANISOU 2119  O   ILE B  11     3454   4523   3229   -104    -61   -243       O  
ATOM   2120  CB  ILE B  11      -4.412  -9.760  -3.757  1.00 28.46           C  
ANISOU 2120  CB  ILE B  11     3367   4318   3130   -118    -18   -380       C  
ATOM   2121  CG1 ILE B  11      -5.048  -8.369  -3.692  1.00 26.88           C  
ANISOU 2121  CG1 ILE B  11     3178   4102   2932   -136     10   -445       C  
ATOM   2122  CG2 ILE B  11      -4.005 -10.183  -5.193  1.00 27.57           C  
ANISOU 2122  CG2 ILE B  11     3274   4140   3062    -81    -31   -359       C  
ATOM   2123  CD1 ILE B  11      -4.092  -7.250  -4.028  1.00 26.55           C  
ANISOU 2123  CD1 ILE B  11     3143   4057   2886   -149     19   -486       C  
ATOM   2124  N   ILE B  12      -5.437 -12.918  -4.279  1.00 26.54           N  
ANISOU 2124  N   ILE B  12     3122   4029   2932    -60    -56   -254       N  
ATOM   2125  CA  ILE B  12      -4.957 -14.237  -4.670  1.00 27.64           C  
ANISOU 2125  CA  ILE B  12     3258   4155   3088    -35    -76   -195       C  
ATOM   2126  C   ILE B  12      -4.058 -14.054  -5.884  1.00 28.33           C  
ANISOU 2126  C   ILE B  12     3361   4198   3204    -13    -82   -201       C  
ATOM   2127  O   ILE B  12      -4.474 -13.448  -6.881  1.00 25.00           O  
ANISOU 2127  O   ILE B  12     2963   3721   2814     -1    -74   -234       O  
ATOM   2128  CB  ILE B  12      -6.120 -15.198  -4.981  1.00 28.99           C  
ANISOU 2128  CB  ILE B  12     3440   4287   3290    -15    -79   -167       C  
ATOM   2129  CG1 ILE B  12      -6.905 -15.527  -3.700  1.00 31.87           C  
ANISOU 2129  CG1 ILE B  12     3785   4701   3622    -37    -75   -153       C  
ATOM   2130  CG2 ILE B  12      -5.591 -16.472  -5.601  1.00 26.34           C  
ANISOU 2130  CG2 ILE B  12     3105   3923   2980     14    -97   -114       C  
ATOM   2131  CD1 ILE B  12      -8.239 -14.829  -3.609  1.00 35.23           C  
ANISOU 2131  CD1 ILE B  12     4221   5111   4052    -46    -56   -195       C  
ATOM   2132  N   PHE B  13      -2.827 -14.576  -5.797  1.00 24.85           N  
ANISOU 2132  N   PHE B  13     2905   3784   2751     -9    -97   -167       N  
ATOM   2133  CA  PHE B  13      -1.782 -14.449  -6.821  1.00 24.44           C  
ANISOU 2133  CA  PHE B  13     2863   3702   2721      9   -104   -169       C  
ATOM   2134  C   PHE B  13      -1.539 -15.825  -7.433  1.00 26.71           C  
ANISOU 2134  C   PHE B  13     3151   3958   3039     41   -119   -116       C  
ATOM   2135  O   PHE B  13      -0.947 -16.691  -6.782  1.00 24.02           O  
ANISOU 2135  O   PHE B  13     2789   3657   2682     42   -131    -69       O  
ATOM   2136  CB  PHE B  13      -0.497 -13.902  -6.182  1.00 24.54           C  
ANISOU 2136  CB  PHE B  13     2855   3777   2694    -14   -107   -176       C  
ATOM   2137  CG  PHE B  13       0.674 -13.682  -7.148  1.00 26.69           C  
ANISOU 2137  CG  PHE B  13     3133   4026   2982      1   -113   -181       C  
ATOM   2138  CD1 PHE B  13       0.524 -12.923  -8.304  1.00 25.00           C  
ANISOU 2138  CD1 PHE B  13     2946   3753   2799     11   -104   -220       C  
ATOM   2139  CD2 PHE B  13       1.943 -14.202  -6.854  1.00 23.43           C  
ANISOU 2139  CD2 PHE B  13     2698   3655   2551      2   -127   -145       C  
ATOM   2140  CE1 PHE B  13       1.597 -12.705  -9.171  1.00 27.77           C  
ANISOU 2140  CE1 PHE B  13     3302   4085   3163     22   -109   -225       C  
ATOM   2141  CE2 PHE B  13       3.034 -13.982  -7.717  1.00 28.70           C  
ANISOU 2141  CE2 PHE B  13     3369   4304   3231     14   -132   -150       C  
ATOM   2142  CZ  PHE B  13       2.862 -13.230  -8.876  1.00 24.40           C  
ANISOU 2142  CZ  PHE B  13     2852   3700   2717     24   -123   -191       C  
ATOM   2143  N   TYR B  14      -1.962 -16.027  -8.687  1.00 21.18           N  
ANISOU 2143  N   TYR B  14     2476   3187   2384     67   -118   -122       N  
ATOM   2144  CA  TYR B  14      -1.716 -17.297  -9.372  1.00 25.66           C  
ANISOU 2144  CA  TYR B  14     3047   3718   2984     97   -130    -77       C  
ATOM   2145  C   TYR B  14      -0.320 -17.286  -9.987  1.00 25.73           C  
ANISOU 2145  C   TYR B  14     3053   3726   2999    109   -138    -70       C  
ATOM   2146  O   TYR B  14      -0.050 -16.528 -10.924  1.00 23.26           O  
ANISOU 2146  O   TYR B  14     2757   3380   2701    114   -134   -105       O  
ATOM   2147  CB  TYR B  14      -2.784 -17.566 -10.428  1.00 20.65           C  
ANISOU 2147  CB  TYR B  14     2440   3015   2393    116   -125    -87       C  
ATOM   2148  CG  TYR B  14      -4.134 -17.848  -9.801  1.00 26.29           C  
ANISOU 2148  CG  TYR B  14     3153   3733   3103    107   -119    -82       C  
ATOM   2149  CD1 TYR B  14      -4.426 -19.097  -9.282  1.00 25.76           C  
ANISOU 2149  CD1 TYR B  14     3075   3675   3039    114   -126    -33       C  
ATOM   2150  CD2 TYR B  14      -5.104 -16.860  -9.713  1.00 25.36           C  
ANISOU 2150  CD2 TYR B  14     3046   3611   2980     93   -106   -126       C  
ATOM   2151  CE1 TYR B  14      -5.650 -19.369  -8.708  1.00 28.50           C  
ANISOU 2151  CE1 TYR B  14     3421   4026   3381    104   -121    -29       C  
ATOM   2152  CE2 TYR B  14      -6.352 -17.122  -9.132  1.00 25.15           C  
ANISOU 2152  CE2 TYR B  14     3017   3589   2949     85   -100   -123       C  
ATOM   2153  CZ  TYR B  14      -6.601 -18.382  -8.628  1.00 26.47           C  
ANISOU 2153  CZ  TYR B  14     3174   3767   3117     90   -108    -74       C  
ATOM   2154  OH  TYR B  14      -7.795 -18.671  -8.041  1.00 29.40           O  
ANISOU 2154  OH  TYR B  14     3542   4146   3484     80   -102    -69       O  
ATOM   2155  N   ASP B  15       0.557 -18.145  -9.472  1.00 27.31           N  
ANISOU 2155  N   ASP B  15     3230   3960   3188    115   -150    -23       N  
ATOM   2156  CA  ASP B  15       1.957 -18.263  -9.864  1.00 22.90           C  
ANISOU 2156  CA  ASP B  15     2661   3409   2629    126   -159     -9       C  
ATOM   2157  C   ASP B  15       2.191 -19.653 -10.455  1.00 28.52           C  
ANISOU 2157  C   ASP B  15     3374   4084   3379    159   -167     40       C  
ATOM   2158  O   ASP B  15       1.362 -20.556 -10.315  1.00 27.18           O  
ANISOU 2158  O   ASP B  15     3207   3893   3226    169   -167     68       O  
ATOM   2159  CB  ASP B  15       2.877 -18.021  -8.643  1.00 26.87           C  
ANISOU 2159  CB  ASP B  15     3132   3994   3083    103   -165      6       C  
ATOM   2160  CG  ASP B  15       4.291 -17.497  -9.017  1.00 29.29           C  
ANISOU 2160  CG  ASP B  15     3429   4319   3380    103   -169     -5       C  
ATOM   2161  OD1 ASP B  15       4.781 -17.763 -10.132  1.00 28.82           O  
ANISOU 2161  OD1 ASP B  15     3383   4213   3354    127   -172     -3       O  
ATOM   2162  OD2 ASP B  15       4.912 -16.814  -8.166  1.00 34.85           O  
ANISOU 2162  OD2 ASP B  15     4114   5088   4041     75   -170    -17       O  
ATOM   2163  N   ILE B  16       3.342 -19.840 -11.109  1.00 23.81           N  
ANISOU 2163  N   ILE B  16     2774   3478   2796    176   -173     50       N  
ATOM   2164  CA  ILE B  16       3.661 -21.085 -11.808  1.00 23.79           C  
ANISOU 2164  CA  ILE B  16     2774   3434   2833    209   -178     90       C  
ATOM   2165  C   ILE B  16       4.515 -21.964 -10.898  1.00 27.31           C  
ANISOU 2165  C   ILE B  16     3187   3928   3263    215   -188    148       C  
ATOM   2166  O   ILE B  16       5.610 -21.558 -10.483  1.00 28.33           O  
ANISOU 2166  O   ILE B  16     3294   4108   3363    206   -194    152       O  
ATOM   2167  CB  ILE B  16       4.386 -20.801 -13.134  1.00 27.96           C  
ANISOU 2167  CB  ILE B  16     3316   3919   3387    225   -176     66       C  
ATOM   2168  CG1 ILE B  16       3.454 -20.037 -14.089  1.00 24.02           C  
ANISOU 2168  CG1 ILE B  16     2850   3370   2908    222   -167     15       C  
ATOM   2169  CG2 ILE B  16       4.893 -22.095 -13.766  1.00 27.71           C  
ANISOU 2169  CG2 ILE B  16     3283   3852   3394    258   -180    108       C  
ATOM   2170  CD1 ILE B  16       4.092 -19.680 -15.407  1.00 26.07           C  
ANISOU 2170  CD1 ILE B  16     3125   3590   3191    235   -165    -10       C  
ATOM   2171  N   ALA B  17       4.029 -23.169 -10.587  1.00 26.26           N  
ANISOU 2171  N   ALA B  17     3048   3781   3147    229   -190    195       N  
ATOM   2172  CA  ALA B  17       4.794 -24.099  -9.754  1.00 30.04           C  
ANISOU 2172  CA  ALA B  17     3496   4302   3616    238   -199    257       C  
ATOM   2173  C   ALA B  17       5.918 -24.746 -10.559  1.00 30.15           C  
ANISOU 2173  C   ALA B  17     3504   4288   3661    269   -202    281       C  
ATOM   2174  O   ALA B  17       5.685 -25.254 -11.659  1.00 31.37           O  
ANISOU 2174  O   ALA B  17     3681   4375   3862    292   -196    275       O  
ATOM   2175  CB  ALA B  17       3.893 -25.191  -9.177  1.00 29.76           C  
ANISOU 2175  CB  ALA B  17     3458   4257   3594    244   -198    301       C  
ATOM   2176  N   GLN B  18       7.123 -24.729 -10.010  1.00 31.09           N  
ANISOU 2176  N   GLN B  18     3593   4463   3756    269   -212    308       N  
ATOM   2177  CA  GLN B  18       8.263 -25.452 -10.566  1.00 36.18           C  
ANISOU 2177  CA  GLN B  18     4226   5092   4427    300   -215    341       C  
ATOM   2178  C   GLN B  18       8.455 -26.745  -9.766  1.00 39.16           C  
ANISOU 2178  C   GLN B  18     4577   5490   4813    317   -221    415       C  
ATOM   2179  O   GLN B  18       7.464 -27.451  -9.549  1.00 43.71           O  
ANISOU 2179  O   GLN B  18     5163   6038   5407    320   -216    435       O  
ATOM   2180  CB  GLN B  18       9.497 -24.545 -10.587  1.00 33.51           C  
ANISOU 2180  CB  GLN B  18     3871   4801   4059    289   -221    320       C  
ATOM   2181  CG  GLN B  18       9.312 -23.225 -11.293  1.00 33.92           C  
ANISOU 2181  CG  GLN B  18     3948   4836   4102    270   -215    249       C  
ATOM   2182  CD  GLN B  18       9.088 -23.386 -12.788  1.00 33.27           C  
ANISOU 2182  CD  GLN B  18     3898   4673   4070    293   -206    222       C  
ATOM   2183  OE1 GLN B  18       9.451 -24.400 -13.387  1.00 35.41           O  
ANISOU 2183  OE1 GLN B  18     4168   4905   4380    324   -206    253       O  
ATOM   2184  NE2 GLN B  18       8.480 -22.375 -13.396  1.00 31.89           N  
ANISOU 2184  NE2 GLN B  18     3750   4472   3894    277   -199    165       N  
ATOM   2185  N   ARG B  19       9.665 -27.081  -9.322  1.00 41.42           N  
ANISOU 2185  N   ARG B  19     4829   5821   5086    328   -230    458       N  
ATOM   2186  CA  ARG B  19       9.966 -28.245  -8.507  1.00 43.39           C  
ANISOU 2186  CA  ARG B  19     5050   6096   5341    345   -235    533       C  
ATOM   2187  C   ARG B  19       9.821 -27.880  -7.033  1.00 40.70           C  
ANISOU 2187  C   ARG B  19     4682   5842   4941    313   -245    553       C  
ATOM   2188  O   ARG B  19      10.040 -26.727  -6.652  1.00 38.21           O  
ANISOU 2188  O   ARG B  19     4360   5579   4579    282   -249    514       O  
ATOM   2189  CB  ARG B  19      11.393 -28.727  -8.774  1.00 44.93           C  
ANISOU 2189  CB  ARG B  19     5219   6302   5550    373   -240    570       C  
ATOM   2190  CG  ARG B  19      11.613 -29.450 -10.099  1.00 47.46           C  
ANISOU 2190  CG  ARG B  19     5561   6539   5934    410   -230    568       C  
ATOM   2191  CD  ARG B  19      10.390 -30.226 -10.541  1.00 50.24           C  
ANISOU 2191  CD  ARG B  19     5942   6816   6329    421   -218    569       C  
ATOM   2192  NE  ARG B  19      10.345 -31.521  -9.873  1.00 56.17           N  
ANISOU 2192  NE  ARG B  19     6674   7567   7100    441   -218    642       N  
ATOM   2193  CZ  ARG B  19       9.262 -32.278  -9.775  1.00 56.00           C  
ANISOU 2193  CZ  ARG B  19     6669   7504   7105    443   -210    659       C  
ATOM   2194  NH1 ARG B  19       8.121 -31.928 -10.345  1.00 54.38           N  
ANISOU 2194  NH1 ARG B  19     6499   7252   6910    429   -202    608       N  
ATOM   2195  NH2 ARG B  19       9.325 -33.413  -9.080  1.00 58.35           N  
ANISOU 2195  NH2 ARG B  19     6946   7807   7419    461   -210    729       N  
ATOM   2196  N   PRO B  20       9.453 -28.836  -6.180  1.00 41.68           N  
ANISOU 2196  N   PRO B  20     4788   5982   5066    319   -248    613       N  
ATOM   2197  CA  PRO B  20       9.453 -28.558  -4.750  1.00 40.63           C  
ANISOU 2197  CA  PRO B  20     4624   5939   4874    289   -258    638       C  
ATOM   2198  C   PRO B  20      10.862 -28.280  -4.261  1.00 42.85           C  
ANISOU 2198  C   PRO B  20     4865   6295   5119    286   -270    661       C  
ATOM   2199  O   PRO B  20      11.843 -28.808  -4.814  1.00 41.31           O  
ANISOU 2199  O   PRO B  20     4660   6083   4954    318   -272    689       O  
ATOM   2200  CB  PRO B  20       8.879 -29.847  -4.137  1.00 41.80           C  
ANISOU 2200  CB  PRO B  20     4763   6078   5042    304   -258    706       C  
ATOM   2201  CG  PRO B  20       8.058 -30.445  -5.245  1.00 44.50           C  
ANISOU 2201  CG  PRO B  20     5144   6318   5446    327   -244    689       C  
ATOM   2202  CD  PRO B  20       8.833 -30.133  -6.494  1.00 44.39           C  
ANISOU 2202  CD  PRO B  20     5145   6260   5462    347   -240    653       C  
ATOM   2203  N   PRO B  21      11.019 -27.401  -3.267  1.00 44.14           N  
ANISOU 2203  N   PRO B  21     5007   6544   5219    248   -278    647       N  
ATOM   2204  CA  PRO B  21       9.994 -26.520  -2.686  1.00 43.49           C  
ANISOU 2204  CA  PRO B  21     4938   6487   5098    207   -273    599       C  
ATOM   2205  C   PRO B  21       9.658 -25.397  -3.665  1.00 41.51           C  
ANISOU 2205  C   PRO B  21     4724   6189   4857    195   -263    515       C  
ATOM   2206  O   PRO B  21      10.568 -24.733  -4.157  1.00 39.28           O  
ANISOU 2206  O   PRO B  21     4439   5916   4568    194   -264    486       O  
ATOM   2207  CB  PRO B  21      10.666 -26.016  -1.401  1.00 42.38           C  
ANISOU 2207  CB  PRO B  21     4755   6458   4889    174   -285    616       C  
ATOM   2208  CG  PRO B  21      12.141 -26.047  -1.715  1.00 45.27           C  
ANISOU 2208  CG  PRO B  21     5097   6849   5255    191   -294    636       C  
ATOM   2209  CD  PRO B  21      12.328 -27.248  -2.605  1.00 42.08           C  
ANISOU 2209  CD  PRO B  21     4703   6368   4919    242   -291    679       C  
ATOM   2210  N   VAL B  22       8.384 -25.162  -3.994  1.00 39.08           N  
ANISOU 2210  N   VAL B  22     4451   5831   4566    188   -252    476       N  
ATOM   2211  CA  VAL B  22       8.073 -24.191  -5.040  1.00 39.02           C  
ANISOU 2211  CA  VAL B  22     4479   5772   4575    183   -241    402       C  
ATOM   2212  C   VAL B  22       8.521 -22.779  -4.673  1.00 38.84           C  
ANISOU 2212  C   VAL B  22     4448   5806   4502    146   -241    350       C  
ATOM   2213  O   VAL B  22       8.803 -21.973  -5.566  1.00 37.47           O  
ANISOU 2213  O   VAL B  22     4295   5602   4340    146   -235    299       O  
ATOM   2214  CB  VAL B  22       6.568 -24.243  -5.398  1.00 39.27           C  
ANISOU 2214  CB  VAL B  22     4545   5742   4633    181   -230    375       C  
ATOM   2215  CG1 VAL B  22       6.121 -25.681  -5.638  1.00 36.49           C  
ANISOU 2215  CG1 VAL B  22     4198   5339   4327    213   -229    429       C  
ATOM   2216  CG2 VAL B  22       5.735 -23.633  -4.275  1.00 40.84           C  
ANISOU 2216  CG2 VAL B  22     4737   5995   4785    143   -227    357       C  
ATOM   2217  N   ALA B  23       8.639 -22.468  -3.378  1.00 39.88           N  
ANISOU 2217  N   ALA B  23     4550   6023   4578    114   -246    362       N  
ATOM   2218  CA  ALA B  23       9.044 -21.127  -2.961  1.00 37.84           C  
ANISOU 2218  CA  ALA B  23     4285   5823   4272     75   -244    310       C  
ATOM   2219  C   ALA B  23      10.532 -20.862  -3.172  1.00 45.88           C  
ANISOU 2219  C   ALA B  23     5280   6875   5276     78   -252    315       C  
ATOM   2220  O   ALA B  23      10.957 -19.698  -3.125  1.00 42.13           O  
ANISOU 2220  O   ALA B  23     4805   6433   4770     49   -248    264       O  
ATOM   2221  CB  ALA B  23       8.676 -20.901  -1.490  1.00 40.64           C  
ANISOU 2221  CB  ALA B  23     4613   6261   4568     37   -246    319       C  
ATOM   2222  N   GLU B  24      11.331 -21.907  -3.411  1.00 42.79           N  
ANISOU 2222  N   GLU B  24     4871   6478   4908    113   -263    374       N  
ATOM   2223  CA  GLU B  24      12.758 -21.751  -3.640  1.00 42.50           C  
ANISOU 2223  CA  GLU B  24     4811   6474   4862    119   -271    384       C  
ATOM   2224  C   GLU B  24      13.162 -21.923  -5.097  1.00 41.49           C  
ANISOU 2224  C   GLU B  24     4708   6267   4788    154   -267    370       C  
ATOM   2225  O   GLU B  24      14.277 -21.541  -5.458  1.00 42.74           O  
ANISOU 2225  O   GLU B  24     4854   6445   4940    156   -270    361       O  
ATOM   2226  CB  GLU B  24      13.542 -22.747  -2.776  1.00 44.16           C  
ANISOU 2226  CB  GLU B  24     4976   6748   5055    132   -286    465       C  
ATOM   2227  N   THR B  25      12.290 -22.463  -5.949  1.00 39.14           N  
ANISOU 2227  N   THR B  25     4445   5884   4544    180   -258    365       N  
ATOM   2228  CA  THR B  25      12.646 -22.723  -7.340  1.00 39.45           C  
ANISOU 2228  CA  THR B  25     4506   5848   4635    214   -254    354       C  
ATOM   2229  C   THR B  25      11.870 -21.878  -8.347  1.00 39.69           C  
ANISOU 2229  C   THR B  25     4580   5814   4687    207   -241    285       C  
ATOM   2230  O   THR B  25      12.107 -22.016  -9.556  1.00 36.96           O  
ANISOU 2230  O   THR B  25     4254   5406   4383    231   -237    270       O  
ATOM   2231  CB  THR B  25      12.422 -24.203  -7.667  1.00 39.58           C  
ANISOU 2231  CB  THR B  25     4524   5813   4702    255   -254    411       C  
ATOM   2232  OG1 THR B  25      11.029 -24.507  -7.508  1.00 37.60           O  
ANISOU 2232  OG1 THR B  25     4296   5526   4466    251   -247    408       O  
ATOM   2233  CG2 THR B  25      13.229 -25.086  -6.713  1.00 39.52           C  
ANISOU 2233  CG2 THR B  25     4471   5866   4677    266   -266    486       C  
ATOM   2234  N   CYS B  26      10.948 -21.024  -7.892  1.00 35.91           N  
ANISOU 2234  N   CYS B  26     4115   5347   4183    175   -234    243       N  
ATOM   2235  CA  CYS B  26      10.128 -20.218  -8.793  1.00 33.16           C  
ANISOU 2235  CA  CYS B  26     3806   4937   3854    169   -222    181       C  
ATOM   2236  C   CYS B  26      11.001 -19.314  -9.657  1.00 36.57           C  
ANISOU 2236  C   CYS B  26     4247   5360   4288    166   -219    138       C  
ATOM   2237  O   CYS B  26      11.885 -18.607  -9.153  1.00 35.41           O  
ANISOU 2237  O   CYS B  26     4078   5274   4102    143   -223    127       O  
ATOM   2238  CB  CYS B  26       9.117 -19.390  -7.985  1.00 34.23           C  
ANISOU 2238  CB  CYS B  26     3949   5101   3958    133   -214    145       C  
ATOM   2239  SG  CYS B  26       9.848 -18.402  -6.639  1.00 39.76           S  
ANISOU 2239  SG  CYS B  26     4615   5908   4586     87   -218    131       S  
ATOM   2240  N   CYS B  27      10.757 -19.344 -10.978  1.00 32.36           N  
ANISOU 2240  N   CYS B  27     3744   4751   3800    188   -213    115       N  
ATOM   2241  CA  CYS B  27      11.677 -18.717 -11.915  1.00 33.16           C  
ANISOU 2241  CA  CYS B  27     3853   4838   3910    191   -211     85       C  
ATOM   2242  C   CYS B  27      11.018 -18.046 -13.113  1.00 30.53           C  
ANISOU 2242  C   CYS B  27     3558   4436   3606    193   -200     32       C  
ATOM   2243  O   CYS B  27      11.745 -17.507 -13.951  1.00 28.74           O  
ANISOU 2243  O   CYS B  27     3339   4195   3387    195   -198      7       O  
ATOM   2244  CB  CYS B  27      12.699 -19.749 -12.438  1.00 29.37           C  
ANISOU 2244  CB  CYS B  27     3356   4346   3456    226   -219    129       C  
ATOM   2245  SG  CYS B  27      12.004 -21.094 -13.409  1.00 37.66           S  
ANISOU 2245  SG  CYS B  27     4429   5310   4571    268   -214    157       S  
ATOM   2246  N   ALA B  28       9.688 -18.069 -13.240  1.00 26.25           N  
ANISOU 2246  N   ALA B  28     3040   3853   3080    192   -193     18       N  
ATOM   2247  CA  ALA B  28       9.045 -17.467 -14.404  1.00 25.74           C  
ANISOU 2247  CA  ALA B  28     3011   3725   3044    196   -183    -28       C  
ATOM   2248  C   ALA B  28       9.212 -15.948 -14.366  1.00 27.17           C  
ANISOU 2248  C   ALA B  28     3198   3926   3198    166   -176    -81       C  
ATOM   2249  O   ALA B  28       9.038 -15.324 -13.316  1.00 25.88           O  
ANISOU 2249  O   ALA B  28     3023   3812   2997    137   -173    -94       O  
ATOM   2250  CB  ALA B  28       7.554 -17.831 -14.462  1.00 29.62           C  
ANISOU 2250  CB  ALA B  28     3523   4175   3557    201   -177    -29       C  
ATOM   2251  N   PRO B  29       9.570 -15.324 -15.492  1.00 27.85           N  
ANISOU 2251  N   PRO B  29     3304   3977   3303    170   -171   -114       N  
ATOM   2252  CA  PRO B  29       9.931 -13.896 -15.439  1.00 23.50           C  
ANISOU 2252  CA  PRO B  29     2757   3447   2726    141   -164   -161       C  
ATOM   2253  C   PRO B  29       8.756 -12.965 -15.218  1.00 24.69           C  
ANISOU 2253  C   PRO B  29     2927   3583   2871    120   -151   -201       C  
ATOM   2254  O   PRO B  29       8.868 -12.024 -14.422  1.00 22.91           O  
ANISOU 2254  O   PRO B  29     2693   3399   2611     89   -145   -228       O  
ATOM   2255  CB  PRO B  29      10.600 -13.657 -16.800  1.00 25.57           C  
ANISOU 2255  CB  PRO B  29     3033   3668   3013    156   -163   -178       C  
ATOM   2256  CG  PRO B  29      10.060 -14.753 -17.694  1.00 28.02           C  
ANISOU 2256  CG  PRO B  29     3359   3920   3368    189   -165   -154       C  
ATOM   2257  CD  PRO B  29       9.901 -15.947 -16.788  1.00 27.14           C  
ANISOU 2257  CD  PRO B  29     3227   3833   3253    200   -173   -105       C  
ATOM   2258  N   ASN B  30       7.636 -13.178 -15.909  1.00 24.01           N  
ANISOU 2258  N   ASN B  30     2866   3439   2818    136   -146   -208       N  
ATOM   2259  CA  ASN B  30       6.509 -12.276 -15.702  1.00 25.10           C  
ANISOU 2259  CA  ASN B  30     3021   3563   2953    118   -133   -245       C  
ATOM   2260  C   ASN B  30       5.933 -12.413 -14.298  1.00 22.39           C  
ANISOU 2260  C   ASN B  30     2661   3267   2580    100   -132   -235       C  
ATOM   2261  O   ASN B  30       5.645 -11.385 -13.674  1.00 24.34           O  
ANISOU 2261  O   ASN B  30     2908   3537   2802     72   -121   -270       O  
ATOM   2262  CB  ASN B  30       5.433 -12.492 -16.769  1.00 24.08           C  
ANISOU 2262  CB  ASN B  30     2919   3365   2864    139   -129   -252       C  
ATOM   2263  CG  ASN B  30       5.789 -11.818 -18.071  1.00 29.12           C  
ANISOU 2263  CG  ASN B  30     3577   3962   3525    146   -125   -280       C  
ATOM   2264  OD1 ASN B  30       6.136 -10.633 -18.088  1.00 28.62           O  
ANISOU 2264  OD1 ASN B  30     3518   3908   3447    126   -116   -315       O  
ATOM   2265  ND2 ASN B  30       5.735 -12.568 -19.170  1.00 28.09           N  
ANISOU 2265  ND2 ASN B  30     3458   3787   3427    172   -130   -265       N  
ATOM   2266  N   PRO B  31       5.721 -13.613 -13.747  1.00 23.57           N  
ANISOU 2266  N   PRO B  31     2795   3430   2729    112   -142   -189       N  
ATOM   2267  CA  PRO B  31       5.294 -13.647 -12.334  1.00 23.26           C  
ANISOU 2267  CA  PRO B  31     2737   3445   2655     90   -141   -180       C  
ATOM   2268  C   PRO B  31       6.290 -12.988 -11.386  1.00 25.51           C  
ANISOU 2268  C   PRO B  31     2998   3802   2894     60   -141   -189       C  
ATOM   2269  O   PRO B  31       5.864 -12.343 -10.420  1.00 22.99           O  
ANISOU 2269  O   PRO B  31     2672   3521   2543     31   -133   -211       O  
ATOM   2270  CB  PRO B  31       5.112 -15.140 -12.053  1.00 24.01           C  
ANISOU 2270  CB  PRO B  31     2821   3541   2762    112   -152   -123       C  
ATOM   2271  CG  PRO B  31       4.732 -15.705 -13.372  1.00 25.58           C  
ANISOU 2271  CG  PRO B  31     3043   3667   3010    143   -152   -118       C  
ATOM   2272  CD  PRO B  31       5.545 -14.928 -14.393  1.00 22.99           C  
ANISOU 2272  CD  PRO B  31     2726   3317   2691    145   -150   -149       C  
ATOM   2273  N   TRP B  32       7.601 -13.074 -11.656  1.00 24.70           N  
ANISOU 2273  N   TRP B  32     2882   3719   2785     65   -150   -177       N  
ATOM   2274  CA  TRP B  32       8.559 -12.355 -10.818  1.00 24.40           C  
ANISOU 2274  CA  TRP B  32     2820   3750   2701     33   -150   -191       C  
ATOM   2275  C   TRP B  32       8.339 -10.845 -10.867  1.00 25.35           C  
ANISOU 2275  C   TRP B  32     2957   3867   2810      4   -133   -254       C  
ATOM   2276  O   TRP B  32       8.455 -10.177  -9.836  1.00 24.05           O  
ANISOU 2276  O   TRP B  32     2777   3758   2604    -31   -126   -274       O  
ATOM   2277  CB  TRP B  32      10.001 -12.692 -11.215  1.00 23.74           C  
ANISOU 2277  CB  TRP B  32     2720   3685   2617     45   -162   -167       C  
ATOM   2278  CG  TRP B  32      10.608 -13.683 -10.294  1.00 25.22           C  
ANISOU 2278  CG  TRP B  32     2871   3930   2780     49   -176   -112       C  
ATOM   2279  CD1 TRP B  32      11.077 -14.928 -10.617  1.00 27.76           C  
ANISOU 2279  CD1 TRP B  32     3182   4241   3125     83   -189    -59       C  
ATOM   2280  CD2 TRP B  32      10.794 -13.537  -8.872  1.00 28.55           C  
ANISOU 2280  CD2 TRP B  32     3264   4434   3151     18   -179   -103       C  
ATOM   2281  NE1 TRP B  32      11.558 -15.559  -9.482  1.00 30.44           N  
ANISOU 2281  NE1 TRP B  32     3485   4648   3432     76   -200    -14       N  
ATOM   2282  CE2 TRP B  32      11.389 -14.727  -8.403  1.00 27.56           C  
ANISOU 2282  CE2 TRP B  32     3109   4344   3020     36   -195    -39       C  
ATOM   2283  CE3 TRP B  32      10.511 -12.516  -7.953  1.00 26.40           C  
ANISOU 2283  CE3 TRP B  32     2985   4207   2837    -24   -168   -142       C  
ATOM   2284  CZ2 TRP B  32      11.717 -14.922  -7.056  1.00 32.35           C  
ANISOU 2284  CZ2 TRP B  32     3680   5034   3579     14   -202    -11       C  
ATOM   2285  CZ3 TRP B  32      10.844 -12.712  -6.608  1.00 29.26           C  
ANISOU 2285  CZ3 TRP B  32     3312   4653   3151    -48   -175   -118       C  
ATOM   2286  CH2 TRP B  32      11.435 -13.907  -6.178  1.00 30.81           C  
ANISOU 2286  CH2 TRP B  32     3479   4887   3341    -29   -193    -52       C  
ATOM   2287  N   LYS B  33       8.030 -10.282 -12.049  1.00 23.34           N  
ANISOU 2287  N   LYS B  33     2732   3547   2590     15   -124   -285       N  
ATOM   2288  CA  LYS B  33       7.794  -8.837 -12.129  1.00 25.37           C  
ANISOU 2288  CA  LYS B  33     3005   3794   2840    -11   -106   -343       C  
ATOM   2289  C   LYS B  33       6.648  -8.424 -11.224  1.00 28.00           C  
ANISOU 2289  C   LYS B  33     3341   4140   3159    -31    -93   -364       C  
ATOM   2290  O   LYS B  33       6.702  -7.376 -10.565  1.00 25.49           O  
ANISOU 2290  O   LYS B  33     3019   3853   2813    -65    -79   -404       O  
ATOM   2291  CB  LYS B  33       7.447  -8.394 -13.554  1.00 25.18           C  
ANISOU 2291  CB  LYS B  33     3013   3694   2859      9    -99   -367       C  
ATOM   2292  CG  LYS B  33       8.459  -8.714 -14.667  1.00 25.30           C  
ANISOU 2292  CG  LYS B  33     3032   3687   2895     30   -109   -353       C  
ATOM   2293  CD  LYS B  33       7.779  -8.426 -16.034  1.00 25.28           C  
ANISOU 2293  CD  LYS B  33     3062   3607   2936     51   -102   -371       C  
ATOM   2294  CE  LYS B  33       8.691  -8.709 -17.247  1.00 24.38           C  
ANISOU 2294  CE  LYS B  33     2953   3465   2844     72   -110   -361       C  
ATOM   2295  NZ  LYS B  33       7.928  -8.387 -18.528  1.00 23.50           N  
ANISOU 2295  NZ  LYS B  33     2872   3284   2772     88   -104   -379       N  
ATOM   2296  N   SER B  34       5.570  -9.215 -11.236  1.00 24.56           N  
ANISOU 2296  N   SER B  34     2912   3677   2744    -11    -96   -341       N  
ATOM   2297  CA  SER B  34       4.389  -8.904 -10.445  1.00 24.22           C  
ANISOU 2297  CA  SER B  34     2871   3642   2689    -27    -83   -359       C  
ATOM   2298  C   SER B  34       4.635  -9.167  -8.970  1.00 26.10           C  
ANISOU 2298  C   SER B  34     3078   3959   2880    -53    -87   -343       C  
ATOM   2299  O   SER B  34       4.125  -8.436  -8.109  1.00 25.78           O  
ANISOU 2299  O   SER B  34     3033   3947   2814    -83    -73   -375       O  
ATOM   2300  CB  SER B  34       3.191  -9.725 -10.935  1.00 22.41           C  
ANISOU 2300  CB  SER B  34     2657   3361   2496      2    -86   -337       C  
ATOM   2301  OG  SER B  34       2.819  -9.377 -12.264  1.00 22.27           O  
ANISOU 2301  OG  SER B  34     2667   3274   2519     22    -81   -356       O  
ATOM   2302  N   ARG B  35       5.388 -10.222  -8.654  1.00 24.36           N  
ANISOU 2302  N   ARG B  35     2834   3774   2646    -43   -106   -292       N  
ATOM   2303  CA  ARG B  35       5.701 -10.469  -7.254  1.00 27.01           C  
ANISOU 2303  CA  ARG B  35     3138   4191   2934    -69   -111   -273       C  
ATOM   2304  C   ARG B  35       6.493  -9.300  -6.679  1.00 26.81           C  
ANISOU 2304  C   ARG B  35     3100   4218   2869   -109   -101   -315       C  
ATOM   2305  O   ARG B  35       6.224  -8.849  -5.558  1.00 28.48           O  
ANISOU 2305  O   ARG B  35     3297   4483   3041   -142    -92   -334       O  
ATOM   2306  CB  ARG B  35       6.452 -11.797  -7.102  1.00 27.03           C  
ANISOU 2306  CB  ARG B  35     3117   4220   2934    -47   -132   -207       C  
ATOM   2307  CG  ARG B  35       6.837 -12.101  -5.652  1.00 29.53           C  
ANISOU 2307  CG  ARG B  35     3396   4626   3198    -73   -140   -180       C  
ATOM   2308  CD  ARG B  35       7.374 -13.531  -5.425  1.00 30.43           C  
ANISOU 2308  CD  ARG B  35     3486   4763   3314    -48   -160   -107       C  
ATOM   2309  NE  ARG B  35       6.412 -14.583  -5.744  1.00 28.67           N  
ANISOU 2309  NE  ARG B  35     3276   4489   3128    -18   -164    -73       N  
ATOM   2310  CZ  ARG B  35       5.463 -15.005  -4.912  1.00 30.78           C  
ANISOU 2310  CZ  ARG B  35     3537   4775   3383    -26   -162    -56       C  
ATOM   2311  NH1 ARG B  35       5.280 -14.446  -3.719  1.00 28.96           N  
ANISOU 2311  NH1 ARG B  35     3288   4610   3104    -64   -157    -73       N  
ATOM   2312  NH2 ARG B  35       4.674 -16.007  -5.285  1.00 26.47           N  
ANISOU 2312  NH2 ARG B  35     3003   4181   2873      3   -166    -23       N  
ATOM   2313  N   LEU B  36       7.429  -8.754  -7.464  1.00 25.47           N  
ANISOU 2313  N   LEU B  36     2938   4032   2708   -107   -101   -334       N  
ATOM   2314  CA  LEU B  36       8.195  -7.588  -7.032  1.00 24.92           C  
ANISOU 2314  CA  LEU B  36     2859   4006   2603   -146    -89   -378       C  
ATOM   2315  C   LEU B  36       7.300  -6.374  -6.827  1.00 29.21           C  
ANISOU 2315  C   LEU B  36     3422   4531   3147   -171    -64   -439       C  
ATOM   2316  O   LEU B  36       7.452  -5.640  -5.841  1.00 24.07           O  
ANISOU 2316  O   LEU B  36     2756   3934   2454   -212    -52   -470       O  
ATOM   2317  CB  LEU B  36       9.284  -7.271  -8.064  1.00 24.16           C  
ANISOU 2317  CB  LEU B  36     2771   3886   2524   -136    -93   -385       C  
ATOM   2318  CG  LEU B  36      10.466  -8.235  -8.126  1.00 26.90           C  
ANISOU 2318  CG  LEU B  36     3091   4267   2861   -119   -116   -333       C  
ATOM   2319  CD1 LEU B  36      11.397  -7.859  -9.284  1.00 27.10           C  
ANISOU 2319  CD1 LEU B  36     3129   4259   2909   -107   -117   -346       C  
ATOM   2320  CD2 LEU B  36      11.245  -8.246  -6.803  1.00 27.36           C  
ANISOU 2320  CD2 LEU B  36     3111   4423   2862   -153   -122   -321       C  
ATOM   2321  N   ALA B  37       6.348  -6.152  -7.749  1.00 26.67           N  
ANISOU 2321  N   ALA B  37     3132   4131   2870   -148    -54   -456       N  
ATOM   2322  CA  ALA B  37       5.413  -5.036  -7.621  1.00 26.16           C  
ANISOU 2322  CA  ALA B  37     3086   4041   2812   -167    -29   -510       C  
ATOM   2323  C   ALA B  37       4.505  -5.196  -6.401  1.00 26.24           C  
ANISOU 2323  C   ALA B  37     3083   4092   2796   -186    -22   -511       C  
ATOM   2324  O   ALA B  37       4.248  -4.222  -5.680  1.00 24.93           O  
ANISOU 2324  O   ALA B  37     2915   3951   2607   -221     -1   -558       O  
ATOM   2325  CB  ALA B  37       4.578  -4.924  -8.906  1.00 25.69           C  
ANISOU 2325  CB  ALA B  37     3060   3893   2808   -134    -24   -518       C  
ATOM   2326  N   LEU B  38       3.973  -6.408  -6.183  1.00 26.80           N  
ANISOU 2326  N   LEU B  38     3146   4166   2871   -164    -37   -462       N  
ATOM   2327  CA  LEU B  38       3.076  -6.657  -5.056  1.00 23.92           C  
ANISOU 2327  CA  LEU B  38     2767   3839   2481   -180    -32   -458       C  
ATOM   2328  C   LEU B  38       3.777  -6.434  -3.725  1.00 27.08           C  
ANISOU 2328  C   LEU B  38     3135   4331   2822   -222    -31   -464       C  
ATOM   2329  O   LEU B  38       3.203  -5.850  -2.800  1.00 30.12           O  
ANISOU 2329  O   LEU B  38     3514   4750   3180   -254    -14   -497       O  
ATOM   2330  CB  LEU B  38       2.535  -8.088  -5.124  1.00 24.87           C  
ANISOU 2330  CB  LEU B  38     2883   3947   2619   -148    -51   -399       C  
ATOM   2331  CG  LEU B  38       1.377  -8.403  -6.078  1.00 26.58           C  
ANISOU 2331  CG  LEU B  38     3128   4084   2886   -114    -48   -395       C  
ATOM   2332  CD1 LEU B  38       1.355  -9.893  -6.346  1.00 26.79           C  
ANISOU 2332  CD1 LEU B  38     3149   4100   2930    -82    -70   -331       C  
ATOM   2333  CD2 LEU B  38       0.044  -7.975  -5.470  1.00 28.11           C  
ANISOU 2333  CD2 LEU B  38     3327   4276   3076   -128    -30   -423       C  
ATOM   2334  N   ASN B  39       5.008  -6.922  -3.600  1.00 27.73           N  
ANISOU 2334  N   ASN B  39     3195   4458   2882   -224    -50   -430       N  
ATOM   2335  CA  ASN B  39       5.779  -6.699  -2.381  1.00 27.98           C  
ANISOU 2335  CA  ASN B  39     3193   4583   2854   -265    -51   -434       C  
ATOM   2336  C   ASN B  39       6.100  -5.218  -2.197  1.00 27.18           C  
ANISOU 2336  C   ASN B  39     3099   4496   2734   -305    -27   -504       C  
ATOM   2337  O   ASN B  39       6.090  -4.707  -1.072  1.00 26.11           O  
ANISOU 2337  O   ASN B  39     2944   4424   2552   -347    -15   -531       O  
ATOM   2338  CB  ASN B  39       7.050  -7.552  -2.426  1.00 29.52           C  
ANISOU 2338  CB  ASN B  39     3363   4817   3034   -253    -76   -380       C  
ATOM   2339  CG  ASN B  39       6.759  -9.050  -2.271  1.00 33.05           C  
ANISOU 2339  CG  ASN B  39     3798   5268   3491   -221    -97   -309       C  
ATOM   2340  OD1 ASN B  39       5.715  -9.442  -1.739  1.00 31.98           O  
ANISOU 2340  OD1 ASN B  39     3663   5134   3355   -221    -94   -298       O  
ATOM   2341  ND2 ASN B  39       7.681  -9.888  -2.730  1.00 28.44           N  
ANISOU 2341  ND2 ASN B  39     3203   4685   2918   -195   -118   -260       N  
ATOM   2342  N   PHE B  40       6.361  -4.512  -3.296  1.00 26.40           N  
ANISOU 2342  N   PHE B  40     3026   4335   2671   -293    -18   -534       N  
ATOM   2343  CA  PHE B  40       6.609  -3.072  -3.261  1.00 25.05           C  
ANISOU 2343  CA  PHE B  40     2864   4162   2490   -328      7   -602       C  
ATOM   2344  C   PHE B  40       5.402  -2.312  -2.720  1.00 29.23           C  
ANISOU 2344  C   PHE B  40     3407   4680   3021   -348     35   -650       C  
ATOM   2345  O   PHE B  40       5.544  -1.418  -1.879  1.00 26.07           O  
ANISOU 2345  O   PHE B  40     2996   4324   2585   -393     55   -697       O  
ATOM   2346  CB  PHE B  40       6.965  -2.619  -4.681  1.00 26.88           C  
ANISOU 2346  CB  PHE B  40     3126   4321   2769   -303      9   -616       C  
ATOM   2347  CG  PHE B  40       7.169  -1.132  -4.867  1.00 26.90           C  
ANISOU 2347  CG  PHE B  40     3145   4304   2773   -333     37   -683       C  
ATOM   2348  CD1 PHE B  40       6.101  -0.288  -5.117  1.00 25.66           C  
ANISOU 2348  CD1 PHE B  40     3014   4091   2646   -333     62   -727       C  
ATOM   2349  CD2 PHE B  40       8.454  -0.599  -4.907  1.00 30.89           C  
ANISOU 2349  CD2 PHE B  40     3639   4842   3256   -358     36   -700       C  
ATOM   2350  CE1 PHE B  40       6.303   1.068  -5.359  1.00 28.17           C  
ANISOU 2350  CE1 PHE B  40     3348   4384   2972   -358     89   -786       C  
ATOM   2351  CE2 PHE B  40       8.661   0.760  -5.148  1.00 30.87           C  
ANISOU 2351  CE2 PHE B  40     3654   4817   3259   -385     63   -761       C  
ATOM   2352  CZ  PHE B  40       7.588   1.590  -5.371  1.00 29.16           C  
ANISOU 2352  CZ  PHE B  40     3463   4542   3073   -384     89   -804       C  
ATOM   2353  N   LYS B  41       4.195  -2.654  -3.199  1.00 27.14           N  
ANISOU 2353  N   LYS B  41     3163   4354   2796   -316     37   -640       N  
ATOM   2354  CA  LYS B  41       2.981  -2.009  -2.711  1.00 27.26           C  
ANISOU 2354  CA  LYS B  41     3187   4355   2815   -331     63   -681       C  
ATOM   2355  C   LYS B  41       2.600  -2.477  -1.314  1.00 30.25           C  
ANISOU 2355  C   LYS B  41     3538   4809   3147   -357     61   -669       C  
ATOM   2356  O   LYS B  41       1.812  -1.800  -0.648  1.00 28.65           O  
ANISOU 2356  O   LYS B  41     3336   4615   2933   -381     86   -712       O  
ATOM   2357  CB  LYS B  41       1.800  -2.260  -3.662  1.00 26.92           C  
ANISOU 2357  CB  LYS B  41     3173   4228   2829   -288     64   -672       C  
ATOM   2358  CG  LYS B  41       2.016  -1.795  -5.061  1.00 28.38           C  
ANISOU 2358  CG  LYS B  41     3386   4337   3060   -262     66   -683       C  
ATOM   2359  CD  LYS B  41       2.415  -0.323  -5.095  1.00 32.84           C  
ANISOU 2359  CD  LYS B  41     3961   4894   3623   -292     94   -746       C  
ATOM   2360  CE  LYS B  41       1.217   0.562  -5.248  1.00 28.86           C  
ANISOU 2360  CE  LYS B  41     3479   4338   3150   -291    122   -789       C  
ATOM   2361  NZ  LYS B  41       1.527   1.932  -5.758  1.00 28.69           N  
ANISOU 2361  NZ  LYS B  41     3476   4277   3147   -305    148   -843       N  
ATOM   2362  N   ALA B  42       3.128  -3.615  -0.864  1.00 31.13           N  
ANISOU 2362  N   ALA B  42     3623   4973   3231   -351     35   -611       N  
ATOM   2363  CA  ALA B  42       2.869  -4.125   0.482  1.00 28.18           C  
ANISOU 2363  CA  ALA B  42     3219   4678   2808   -377     31   -593       C  
ATOM   2364  C   ALA B  42       1.388  -4.414   0.719  1.00 34.29           C  
ANISOU 2364  C   ALA B  42     4003   5425   3600   -365     40   -592       C  
ATOM   2365  O   ALA B  42       0.923  -4.384   1.854  1.00 30.85           O  
ANISOU 2365  O   ALA B  42     3549   5047   3127   -395     49   -601       O  
ATOM   2366  CB  ALA B  42       3.394  -3.165   1.559  1.00 29.30           C  
ANISOU 2366  CB  ALA B  42     3342   4895   2896   -434     49   -642       C  
ATOM   2367  N   VAL B  43       0.622  -4.702  -0.330  1.00 30.27           N  
ANISOU 2367  N   VAL B  43     3521   4833   3146   -323     38   -580       N  
ATOM   2368  CA  VAL B  43      -0.773  -5.103  -0.143  1.00 32.24           C  
ANISOU 2368  CA  VAL B  43     3778   5060   3412   -309     43   -572       C  
ATOM   2369  C   VAL B  43      -0.825  -6.593   0.177  1.00 31.55           C  
ANISOU 2369  C   VAL B  43     3672   5000   3315   -290     16   -500       C  
ATOM   2370  O   VAL B  43      -0.088  -7.382  -0.434  1.00 36.27           O  
ANISOU 2370  O   VAL B  43     4269   5586   3927   -264     -7   -454       O  
ATOM   2371  CB  VAL B  43      -1.616  -4.758  -1.377  1.00 33.82           C  
ANISOU 2371  CB  VAL B  43     4014   5164   3674   -274     53   -590       C  
ATOM   2372  CG1 VAL B  43      -1.619  -3.254  -1.574  1.00 31.90           C  
ANISOU 2372  CG1 VAL B  43     3786   4895   3440   -295     83   -660       C  
ATOM   2373  CG2 VAL B  43      -1.062  -5.470  -2.612  1.00 32.56           C  
ANISOU 2373  CG2 VAL B  43     3867   4954   3551   -234     30   -548       C  
ATOM   2374  N   PRO B  44      -1.635  -7.020   1.144  1.00 30.34           N  
ANISOU 2374  N   PRO B  44     3504   4886   3138   -304     19   -488       N  
ATOM   2375  CA  PRO B  44      -1.675  -8.447   1.498  1.00 30.49           C  
ANISOU 2375  CA  PRO B  44     3504   4932   3147   -288     -6   -417       C  
ATOM   2376  C   PRO B  44      -2.077  -9.317   0.311  1.00 33.44           C  
ANISOU 2376  C   PRO B  44     3900   5227   3577   -238    -20   -378       C  
ATOM   2377  O   PRO B  44      -3.067  -9.046  -0.379  1.00 29.91           O  
ANISOU 2377  O   PRO B  44     3479   4715   3170   -219     -9   -400       O  
ATOM   2378  CB  PRO B  44      -2.718  -8.502   2.623  1.00 33.11           C  
ANISOU 2378  CB  PRO B  44     3823   5307   3450   -312      6   -425       C  
ATOM   2379  CG  PRO B  44      -2.639  -7.137   3.255  1.00 35.28           C  
ANISOU 2379  CG  PRO B  44     4094   5617   3695   -355     33   -495       C  
ATOM   2380  CD  PRO B  44      -2.325  -6.174   2.132  1.00 31.09           C  
ANISOU 2380  CD  PRO B  44     3592   5018   3203   -342     45   -539       C  
ATOM   2381  N   TYR B  45      -1.294 -10.371   0.074  1.00 27.43           N  
ANISOU 2381  N   TYR B  45     3129   4475   2819   -217    -45   -319       N  
ATOM   2382  CA  TYR B  45      -1.615 -11.329  -0.973  1.00 31.29           C  
ANISOU 2382  CA  TYR B  45     3635   4895   3358   -172    -59   -278       C  
ATOM   2383  C   TYR B  45      -1.169 -12.715  -0.527  1.00 31.24           C  
ANISOU 2383  C   TYR B  45     3606   4925   3339   -160    -82   -205       C  
ATOM   2384  O   TYR B  45      -0.306 -12.857   0.341  1.00 34.32           O  
ANISOU 2384  O   TYR B  45     3967   5388   3686   -182    -91   -184       O  
ATOM   2385  CB  TYR B  45      -0.960 -10.926  -2.312  1.00 28.30           C  
ANISOU 2385  CB  TYR B  45     3281   4456   3018   -149    -61   -295       C  
ATOM   2386  CG  TYR B  45       0.549 -11.134  -2.366  1.00 30.33           C  
ANISOU 2386  CG  TYR B  45     3520   4746   3257   -149    -76   -271       C  
ATOM   2387  CD1 TYR B  45       1.417 -10.155  -1.901  1.00 28.94           C  
ANISOU 2387  CD1 TYR B  45     3332   4619   3045   -182    -69   -307       C  
ATOM   2388  CD2 TYR B  45       1.101 -12.298  -2.912  1.00 28.01           C  
ANISOU 2388  CD2 TYR B  45     3223   4434   2986   -116    -98   -213       C  
ATOM   2389  CE1 TYR B  45       2.807 -10.328  -1.953  1.00 30.09           C  
ANISOU 2389  CE1 TYR B  45     3460   4798   3174   -183    -83   -285       C  
ATOM   2390  CE2 TYR B  45       2.491 -12.486  -2.962  1.00 30.97           C  
ANISOU 2390  CE2 TYR B  45     3580   4841   3345   -115   -111   -190       C  
ATOM   2391  CZ  TYR B  45       3.337 -11.491  -2.481  1.00 32.38           C  
ANISOU 2391  CZ  TYR B  45     3745   5072   3486   -149   -105   -226       C  
ATOM   2392  OH  TYR B  45       4.711 -11.652  -2.523  1.00 28.88           O  
ANISOU 2392  OH  TYR B  45     3283   4664   3026   -149   -118   -204       O  
ATOM   2393  N   THR B  46      -1.777 -13.738  -1.124  1.00 29.95           N  
ANISOU 2393  N   THR B  46     3455   4710   3214   -127    -92   -166       N  
ATOM   2394  CA  THR B  46      -1.339 -15.120  -0.982  1.00 31.46           C  
ANISOU 2394  CA  THR B  46     3630   4915   3409   -107   -112    -94       C  
ATOM   2395  C   THR B  46      -1.172 -15.737  -2.365  1.00 32.26           C  
ANISOU 2395  C   THR B  46     3754   4937   3565    -65   -121    -74       C  
ATOM   2396  O   THR B  46      -1.863 -15.355  -3.311  1.00 28.30           O  
ANISOU 2396  O   THR B  46     3281   4370   3101    -50   -111   -107       O  
ATOM   2397  CB  THR B  46      -2.341 -15.953  -0.166  1.00 31.64           C  
ANISOU 2397  CB  THR B  46     3641   4958   3421   -111   -114    -60       C  
ATOM   2398  OG1 THR B  46      -3.558 -16.078  -0.907  1.00 34.30           O  
ANISOU 2398  OG1 THR B  46     4007   5225   3802    -91   -105    -74       O  
ATOM   2399  CG2 THR B  46      -2.636 -15.296   1.161  1.00 34.26           C  
ANISOU 2399  CG2 THR B  46     3953   5365   3699   -154   -103    -85       C  
ATOM   2400  N   THR B  47      -0.267 -16.709  -2.474  1.00 29.08           N  
ANISOU 2400  N   THR B  47     3337   4543   3168    -45   -138    -19       N  
ATOM   2401  CA  THR B  47       0.038 -17.358  -3.744  1.00 29.93           C  
ANISOU 2401  CA  THR B  47     3463   4582   3326     -7   -146      1       C  
ATOM   2402  C   THR B  47      -0.671 -18.699  -3.847  1.00 29.15           C  
ANISOU 2402  C   THR B  47     3368   4451   3257     18   -153     52       C  
ATOM   2403  O   THR B  47      -0.597 -19.514  -2.926  1.00 26.65           O  
ANISOU 2403  O   THR B  47     3026   4179   2919     13   -161    101       O  
ATOM   2404  CB  THR B  47       1.545 -17.585  -3.899  1.00 30.58           C  
ANISOU 2404  CB  THR B  47     3528   4689   3401      2   -159     28       C  
ATOM   2405  OG1 THR B  47       2.246 -16.338  -3.829  1.00 28.42           O  
ANISOU 2405  OG1 THR B  47     3252   4446   3101    -22   -153    -21       O  
ATOM   2406  CG2 THR B  47       1.847 -18.279  -5.238  1.00 26.96           C  
ANISOU 2406  CG2 THR B  47     3089   4158   2997     43   -165     47       C  
ATOM   2407  N   THR B  48      -1.332 -18.935  -4.978  1.00 27.41           N  
ANISOU 2407  N   THR B  48     3177   4154   3085     42   -149     41       N  
ATOM   2408  CA  THR B  48      -1.754 -20.272  -5.373  1.00 28.07           C  
ANISOU 2408  CA  THR B  48     3266   4194   3205     70   -155     89       C  
ATOM   2409  C   THR B  48      -0.793 -20.758  -6.447  1.00 30.02           C  
ANISOU 2409  C   THR B  48     3521   4400   3487    100   -163    107       C  
ATOM   2410  O   THR B  48      -0.620 -20.088  -7.474  1.00 29.13           O  
ANISOU 2410  O   THR B  48     3428   4246   3395    108   -158     67       O  
ATOM   2411  CB  THR B  48      -3.195 -20.281  -5.891  1.00 29.65           C  
ANISOU 2411  CB  THR B  48     3491   4340   3433     75   -144     66       C  
ATOM   2412  OG1 THR B  48      -4.079 -19.931  -4.825  1.00 29.45           O  
ANISOU 2412  OG1 THR B  48     3456   4357   3376     48   -137     54       O  
ATOM   2413  CG2 THR B  48      -3.555 -21.660  -6.395  1.00 27.44           C  
ANISOU 2413  CG2 THR B  48     3220   4013   3194    102   -150    112       C  
ATOM   2414  N   TRP B  49      -0.143 -21.893  -6.197  1.00 28.32           N  
ANISOU 2414  N   TRP B  49     3287   4196   3278    117   -174    166       N  
ATOM   2415  CA  TRP B  49       0.885 -22.412  -7.092  1.00 26.50           C  
ANISOU 2415  CA  TRP B  49     3059   3933   3078    145   -180    186       C  
ATOM   2416  C   TRP B  49       0.236 -23.319  -8.128  1.00 30.53           C  
ANISOU 2416  C   TRP B  49     3594   4365   3643    173   -177    198       C  
ATOM   2417  O   TRP B  49      -0.280 -24.389  -7.787  1.00 36.44           O  
ANISOU 2417  O   TRP B  49     4338   5103   4405    182   -178    241       O  
ATOM   2418  CB  TRP B  49       1.949 -23.155  -6.297  1.00 30.68           C  
ANISOU 2418  CB  TRP B  49     3554   4515   3588    150   -192    245       C  
ATOM   2419  CG  TRP B  49       2.771 -22.223  -5.506  1.00 29.10           C  
ANISOU 2419  CG  TRP B  49     3331   4390   3337    123   -196    229       C  
ATOM   2420  CD1 TRP B  49       2.634 -21.949  -4.182  1.00 34.66           C  
ANISOU 2420  CD1 TRP B  49     4011   5168   3991     93   -198    237       C  
ATOM   2421  CD2 TRP B  49       3.847 -21.405  -5.978  1.00 32.30           C  
ANISOU 2421  CD2 TRP B  49     3735   4806   3733    121   -198    199       C  
ATOM   2422  NE1 TRP B  49       3.569 -21.029  -3.792  1.00 32.29           N  
ANISOU 2422  NE1 TRP B  49     3693   4924   3650     71   -200    213       N  
ATOM   2423  CE2 TRP B  49       4.329 -20.677  -4.873  1.00 33.23           C  
ANISOU 2423  CE2 TRP B  49     3826   5005   3794     87   -200    190       C  
ATOM   2424  CE3 TRP B  49       4.468 -21.237  -7.222  1.00 32.95           C  
ANISOU 2424  CE3 TRP B  49     3834   4838   3848    142   -197    179       C  
ATOM   2425  CZ2 TRP B  49       5.394 -19.778  -4.974  1.00 34.65           C  
ANISOU 2425  CZ2 TRP B  49     3998   5218   3952     74   -202    162       C  
ATOM   2426  CZ3 TRP B  49       5.530 -20.351  -7.325  1.00 29.10           C  
ANISOU 2426  CZ3 TRP B  49     3338   4382   3338    130   -199    153       C  
ATOM   2427  CH2 TRP B  49       5.984 -19.631  -6.208  1.00 33.82           C  
ANISOU 2427  CH2 TRP B  49     3910   5060   3881     97   -201    144       C  
ATOM   2428  N   VAL B  50       0.246 -22.889  -9.388  1.00 26.66           N  
ANISOU 2428  N   VAL B  50     3128   3819   3183    186   -172    160       N  
ATOM   2429  CA  VAL B  50      -0.418 -23.633 -10.455  1.00 27.88           C  
ANISOU 2429  CA  VAL B  50     3307   3900   3386    209   -167    162       C  
ATOM   2430  C   VAL B  50       0.517 -24.716 -10.974  1.00 30.98           C  
ANISOU 2430  C   VAL B  50     3694   4267   3810    238   -172    204       C  
ATOM   2431  O   VAL B  50       1.662 -24.439 -11.355  1.00 30.63           O  
ANISOU 2431  O   VAL B  50     3643   4230   3764    246   -177    200       O  
ATOM   2432  CB  VAL B  50      -0.847 -22.690 -11.588  1.00 26.60           C  
ANISOU 2432  CB  VAL B  50     3172   3692   3240    209   -159    104       C  
ATOM   2433  CG1 VAL B  50      -1.544 -23.463 -12.709  1.00 26.19           C  
ANISOU 2433  CG1 VAL B  50     3145   3569   3237    229   -155    105       C  
ATOM   2434  CG2 VAL B  50      -1.722 -21.591 -11.039  1.00 27.38           C  
ANISOU 2434  CG2 VAL B  50     3276   3817   3311    182   -152     63       C  
ATOM   2435  N   LYS B  51       0.025 -25.950 -11.002  1.00 29.96           N  
ANISOU 2435  N   LYS B  51     3567   4106   3710    253   -171    244       N  
ATOM   2436  CA  LYS B  51       0.778 -27.095 -11.488  1.00 33.16           C  
ANISOU 2436  CA  LYS B  51     3968   4480   4152    282   -172    285       C  
ATOM   2437  C   LYS B  51       0.381 -27.375 -12.932  1.00 35.57           C  
ANISOU 2437  C   LYS B  51     4303   4708   4504    299   -164    259       C  
ATOM   2438  O   LYS B  51      -0.805 -27.561 -13.229  1.00 31.39           O  
ANISOU 2438  O   LYS B  51     3792   4143   3990    294   -157    245       O  
ATOM   2439  CB  LYS B  51       0.536 -28.314 -10.600  1.00 33.14           C  
ANISOU 2439  CB  LYS B  51     3948   4489   4153    287   -174    347       C  
ATOM   2440  CG  LYS B  51       1.326 -28.222  -9.292  1.00 37.23           C  
ANISOU 2440  CG  LYS B  51     4432   5086   4629    277   -184    385       C  
ATOM   2441  CD  LYS B  51       0.891 -29.239  -8.239  1.00 42.95           C  
ANISOU 2441  CD  LYS B  51     5138   5832   5348    275   -186    444       C  
ATOM   2442  CE  LYS B  51       1.608 -29.000  -6.908  1.00 45.92           C  
ANISOU 2442  CE  LYS B  51     5478   6296   5674    259   -197    477       C  
ATOM   2443  NZ  LYS B  51       0.959 -27.908  -6.095  1.00 50.54           N  
ANISOU 2443  NZ  LYS B  51     6060   6935   6208    223   -198    440       N  
ATOM   2444  N   LEU B  52       1.370 -27.377 -13.826  1.00 31.83           N  
ANISOU 2444  N   LEU B  52     3832   4212   4050    317   -164    251       N  
ATOM   2445  CA  LEU B  52       1.185 -27.688 -15.233  1.00 38.03           C  
ANISOU 2445  CA  LEU B  52     4643   4929   4879    334   -156    228       C  
ATOM   2446  C   LEU B  52       2.157 -28.782 -15.635  1.00 35.80           C  
ANISOU 2446  C   LEU B  52     4352   4621   4631    362   -155    266       C  
ATOM   2447  O   LEU B  52       3.236 -28.895 -15.055  1.00 34.15           O  
ANISOU 2447  O   LEU B  52     4117   4450   4406    370   -162    297       O  
ATOM   2448  CB  LEU B  52       1.421 -26.463 -16.132  1.00 35.79           C  
ANISOU 2448  CB  LEU B  52     4374   4637   4587    327   -156    172       C  
ATOM   2449  CG  LEU B  52       0.507 -25.283 -15.844  1.00 35.82           C  
ANISOU 2449  CG  LEU B  52     4387   4660   4561    302   -155    130       C  
ATOM   2450  CD1 LEU B  52       0.704 -24.115 -16.802  1.00 22.56           C  
ANISOU 2450  CD1 LEU B  52     2724   2967   2880    297   -153     78       C  
ATOM   2451  CD2 LEU B  52      -0.894 -25.812 -15.897  1.00 36.48           C  
ANISOU 2451  CD2 LEU B  52     4485   4712   4663    298   -149    131       C  
ATOM   2452  N   PRO B  53       1.800 -29.607 -16.611  1.00 37.22           N  
ANISOU 2452  N   PRO B  53     4550   4737   4855    378   -145    265       N  
ATOM   2453  CA  PRO B  53       2.794 -30.515 -17.190  1.00 38.70           C  
ANISOU 2453  CA  PRO B  53     4732   4894   5079    406   -141    290       C  
ATOM   2454  C   PRO B  53       3.869 -29.732 -17.929  1.00 39.78           C  
ANISOU 2454  C   PRO B  53     4868   5038   5209    412   -144    260       C  
ATOM   2455  O   PRO B  53       3.698 -28.559 -18.280  1.00 35.43           O  
ANISOU 2455  O   PRO B  53     4328   4498   4635    396   -147    214       O  
ATOM   2456  CB  PRO B  53       1.973 -31.381 -18.152  1.00 39.43           C  
ANISOU 2456  CB  PRO B  53     4848   4915   5217    415   -127    281       C  
ATOM   2457  CG  PRO B  53       0.777 -30.553 -18.480  1.00 43.28           C  
ANISOU 2457  CG  PRO B  53     5358   5396   5691    392   -127    234       C  
ATOM   2458  CD  PRO B  53       0.470 -29.783 -17.216  1.00 36.55           C  
ANISOU 2458  CD  PRO B  53     4491   4606   4791    371   -136    239       C  
ATOM   2459  N   ASP B  54       5.006 -30.395 -18.150  1.00 39.23           N  
ANISOU 2459  N   ASP B  54     4784   4961   5160    436   -142    289       N  
ATOM   2460  CA  ASP B  54       6.011 -29.786 -19.002  1.00 38.53           C  
ANISOU 2460  CA  ASP B  54     4695   4871   5072    443   -143    260       C  
ATOM   2461  C   ASP B  54       5.368 -29.427 -20.340  1.00 41.95           C  
ANISOU 2461  C   ASP B  54     5161   5254   5526    439   -135    206       C  
ATOM   2462  O   ASP B  54       4.302 -29.936 -20.705  1.00 48.07           O  
ANISOU 2462  O   ASP B  54     5954   5986   6323    436   -127    199       O  
ATOM   2463  CB  ASP B  54       7.212 -30.716 -19.232  1.00 43.06           C  
ANISOU 2463  CB  ASP B  54     5252   5433   5675    474   -139    296       C  
ATOM   2464  CG  ASP B  54       7.836 -31.249 -17.944  1.00 46.94           C  
ANISOU 2464  CG  ASP B  54     5710   5973   6152    482   -147    358       C  
ATOM   2465  OD1 ASP B  54       7.796 -30.570 -16.894  1.00 45.52           O  
ANISOU 2465  OD1 ASP B  54     5515   5855   5927    462   -159    365       O  
ATOM   2466  OD2 ASP B  54       8.446 -32.339 -18.015  1.00 48.93           O  
ANISOU 2466  OD2 ASP B  54     5950   6203   6439    510   -141    399       O  
ATOM   2467  N   ILE B  55       6.004 -28.503 -21.043  1.00 39.57           N  
ANISOU 2467  N   ILE B  55     4863   4958   5212    435   -138    170       N  
ATOM   2468  CA  ILE B  55       5.589 -28.024 -22.358  1.00 37.03           C  
ANISOU 2468  CA  ILE B  55     4569   4596   4905    431   -131    120       C  
ATOM   2469  C   ILE B  55       4.506 -26.982 -22.135  1.00 34.92           C  
ANISOU 2469  C   ILE B  55     4315   4344   4610    405   -135     87       C  
ATOM   2470  O   ILE B  55       4.686 -25.821 -22.515  1.00 32.80           O  
ANISOU 2470  O   ILE B  55     4053   4089   4321    392   -139     50       O  
ATOM   2471  CB  ILE B  55       5.121 -29.139 -23.318  1.00 41.37           C  
ANISOU 2471  CB  ILE B  55     5136   5082   5503    445   -118    120       C  
ATOM   2472  CG1 ILE B  55       6.315 -29.849 -23.954  1.00 40.62           C  
ANISOU 2472  CG1 ILE B  55     5031   4965   5436    471   -111    133       C  
ATOM   2473  CG2 ILE B  55       4.300 -28.563 -24.453  1.00 40.33           C  
ANISOU 2473  CG2 ILE B  55     5031   4917   5376    433   -114     69       C  
ATOM   2474  CD1 ILE B  55       5.907 -30.938 -24.924  1.00 46.44           C  
ANISOU 2474  CD1 ILE B  55     5785   5638   6222    483    -95    129       C  
ATOM   2475  N   GLU B  56       3.386 -27.364 -21.501  1.00 36.37           N  
ANISOU 2475  N   GLU B  56     4502   4524   4792    396   -134    100       N  
ATOM   2476  CA  GLU B  56       2.399 -26.349 -21.144  1.00 35.15           C  
ANISOU 2476  CA  GLU B  56     4357   4389   4609    372   -137     72       C  
ATOM   2477  C   GLU B  56       3.010 -25.323 -20.200  1.00 29.78           C  
ANISOU 2477  C   GLU B  56     3659   3770   3886    358   -146     70       C  
ATOM   2478  O   GLU B  56       2.858 -24.113 -20.397  1.00 27.35           O  
ANISOU 2478  O   GLU B  56     3360   3475   3557    342   -148     31       O  
ATOM   2479  CB  GLU B  56       1.143 -26.959 -20.505  1.00 34.07           C  
ANISOU 2479  CB  GLU B  56     4224   4245   4477    364   -134     90       C  
ATOM   2480  CG  GLU B  56       0.179 -25.839 -20.071  1.00 32.79           C  
ANISOU 2480  CG  GLU B  56     4069   4107   4284    340   -137     60       C  
ATOM   2481  CD  GLU B  56      -1.136 -26.309 -19.449  1.00 38.29           C  
ANISOU 2481  CD  GLU B  56     4768   4800   4981    330   -134     73       C  
ATOM   2482  OE1 GLU B  56      -1.220 -27.467 -18.994  1.00 37.31           O  
ANISOU 2482  OE1 GLU B  56     4637   4668   4873    339   -132    113       O  
ATOM   2483  OE2 GLU B  56      -2.091 -25.495 -19.420  1.00 36.09           O  
ANISOU 2483  OE2 GLU B  56     4500   4526   4687    313   -133     43       O  
ATOM   2484  N   ARG B  57       3.704 -25.796 -19.166  1.00 29.14           N  
ANISOU 2484  N   ARG B  57     3553   3728   3791    362   -152    111       N  
ATOM   2485  CA  ARG B  57       4.388 -24.894 -18.248  1.00 32.46           C  
ANISOU 2485  CA  ARG B  57     3954   4211   4168    347   -160    110       C  
ATOM   2486  C   ARG B  57       5.407 -24.024 -18.979  1.00 31.31           C  
ANISOU 2486  C   ARG B  57     3809   4071   4016    347   -162     80       C  
ATOM   2487  O   ARG B  57       5.482 -22.811 -18.749  1.00 28.71           O  
ANISOU 2487  O   ARG B  57     3481   3773   3656    327   -164     48       O  
ATOM   2488  CB  ARG B  57       5.064 -25.701 -17.138  1.00 31.28           C  
ANISOU 2488  CB  ARG B  57     3775   4102   4009    355   -166    166       C  
ATOM   2489  CG  ARG B  57       5.720 -24.836 -16.076  1.00 36.35           C  
ANISOU 2489  CG  ARG B  57     4393   4816   4602    336   -175    168       C  
ATOM   2490  CD  ARG B  57       6.597 -25.659 -15.133  1.00 37.16           C  
ANISOU 2490  CD  ARG B  57     4462   4960   4695    347   -183    226       C  
ATOM   2491  NE  ARG B  57       6.063 -27.006 -14.985  1.00 43.24           N  
ANISOU 2491  NE  ARG B  57     5233   5699   5498    365   -179    270       N  
ATOM   2492  CZ  ARG B  57       6.703 -28.120 -15.305  1.00 42.33           C  
ANISOU 2492  CZ  ARG B  57     5109   5557   5417    393   -176    309       C  
ATOM   2493  NH1 ARG B  57       7.949 -28.100 -15.749  1.00 40.39           N  
ANISOU 2493  NH1 ARG B  57     4851   5317   5178    409   -179    313       N  
ATOM   2494  NH2 ARG B  57       6.078 -29.288 -15.160  1.00 41.91           N  
ANISOU 2494  NH2 ARG B  57     5059   5471   5394    406   -171    345       N  
ATOM   2495  N   VAL B  58       6.201 -24.621 -19.862  1.00 29.47           N  
ANISOU 2495  N   VAL B  58     3577   3808   3812    370   -159     87       N  
ATOM   2496  CA  VAL B  58       7.174 -23.835 -20.612  1.00 30.63           C  
ANISOU 2496  CA  VAL B  58     3725   3960   3953    370   -161     58       C  
ATOM   2497  C   VAL B  58       6.459 -22.782 -21.448  1.00 28.55           C  
ANISOU 2497  C   VAL B  58     3488   3672   3688    355   -156      6       C  
ATOM   2498  O   VAL B  58       6.892 -21.624 -21.530  1.00 26.99           O  
ANISOU 2498  O   VAL B  58     3291   3498   3467    340   -159    -24       O  
ATOM   2499  CB  VAL B  58       8.050 -24.760 -21.476  1.00 29.09           C  
ANISOU 2499  CB  VAL B  58     3527   3732   3794    397   -157     75       C  
ATOM   2500  CG1 VAL B  58       8.827 -23.947 -22.508  1.00 34.71           C  
ANISOU 2500  CG1 VAL B  58     4246   4437   4504    396   -156     38       C  
ATOM   2501  CG2 VAL B  58       8.994 -25.578 -20.589  1.00 27.69           C  
ANISOU 2501  CG2 VAL B  58     3318   3588   3614    413   -162    128       C  
ATOM   2502  N   CYS B  59       5.335 -23.161 -22.055  1.00 29.36           N  
ANISOU 2502  N   CYS B  59     3612   3728   3815    357   -150     -5       N  
ATOM   2503  CA  CYS B  59       4.577 -22.215 -22.862  1.00 31.28           C  
ANISOU 2503  CA  CYS B  59     3879   3948   4058    345   -146    -50       C  
ATOM   2504  C   CYS B  59       4.077 -21.046 -22.021  1.00 27.40           C  
ANISOU 2504  C   CYS B  59     3387   3494   3532    320   -149    -70       C  
ATOM   2505  O   CYS B  59       4.187 -19.883 -22.424  1.00 26.49           O  
ANISOU 2505  O   CYS B  59     3279   3382   3403    308   -147   -106       O  
ATOM   2506  CB  CYS B  59       3.418 -22.945 -23.539  1.00 31.92           C  
ANISOU 2506  CB  CYS B  59     3979   3980   4171    351   -140    -53       C  
ATOM   2507  SG  CYS B  59       2.493 -21.918 -24.665  1.00 32.65           S  
ANISOU 2507  SG  CYS B  59     4098   4042   4266    339   -136   -103       S  
ATOM   2508  N   LYS B  60       3.522 -21.342 -20.843  1.00 28.04           N  
ANISOU 2508  N   LYS B  60     3456   3601   3597    313   -150    -47       N  
ATOM   2509  CA  LYS B  60       2.962 -20.312 -19.971  1.00 28.87           C  
ANISOU 2509  CA  LYS B  60     3559   3741   3669    289   -150    -67       C  
ATOM   2510  C   LYS B  60       4.031 -19.344 -19.478  1.00 30.47           C  
ANISOU 2510  C   LYS B  60     3746   3991   3838    275   -154    -79       C  
ATOM   2511  O   LYS B  60       3.714 -18.192 -19.157  1.00 30.06           O  
ANISOU 2511  O   LYS B  60     3700   3959   3765    254   -150   -111       O  
ATOM   2512  CB  LYS B  60       2.279 -20.975 -18.764  1.00 30.16           C  
ANISOU 2512  CB  LYS B  60     3710   3928   3822    283   -152    -35       C  
ATOM   2513  CG  LYS B  60       0.849 -21.513 -18.970  1.00 33.08           C  
ANISOU 2513  CG  LYS B  60     4095   4262   4213    285   -146    -34       C  
ATOM   2514  CD  LYS B  60       0.056 -20.737 -19.954  1.00 35.30           C  
ANISOU 2514  CD  LYS B  60     4399   4507   4505    281   -141    -77       C  
ATOM   2515  CE  LYS B  60      -1.416 -21.204 -20.042  1.00 36.58           C  
ANISOU 2515  CE  LYS B  60     4575   4642   4684    279   -136    -76       C  
ATOM   2516  NZ  LYS B  60      -1.625 -22.581 -20.562  1.00 33.57           N  
ANISOU 2516  NZ  LYS B  60     4197   4222   4335    296   -135    -50       N  
ATOM   2517  N   GLU B  61       5.289 -19.806 -19.411  1.00 27.30           N  
ANISOU 2517  N   GLU B  61     3328   3609   3436    286   -159    -55       N  
ATOM   2518  CA  GLU B  61       6.460 -19.135 -18.837  1.00 32.74           C  
ANISOU 2518  CA  GLU B  61     3996   4350   4092    274   -164    -57       C  
ATOM   2519  C   GLU B  61       7.140 -18.185 -19.814  1.00 33.49           C  
ANISOU 2519  C   GLU B  61     4103   4434   4189    271   -162    -94       C  
ATOM   2520  O   GLU B  61       7.380 -17.016 -19.498  1.00 33.24           O  
ANISOU 2520  O   GLU B  61     4070   4431   4130    249   -160   -123       O  
ATOM   2521  CB  GLU B  61       7.520 -20.172 -18.434  1.00 30.62           C  
ANISOU 2521  CB  GLU B  61     3702   4106   3826    291   -172    -10       C  
ATOM   2522  CG  GLU B  61       7.466 -20.624 -17.039  1.00 35.21           C  
ANISOU 2522  CG  GLU B  61     4260   4736   4383    284   -177     27       C  
ATOM   2523  CD  GLU B  61       8.197 -21.936 -16.834  1.00 34.16           C  
ANISOU 2523  CD  GLU B  61     4106   4608   4267    309   -182     82       C  
ATOM   2524  OE1 GLU B  61       8.828 -22.484 -17.784  1.00 35.27           O  
ANISOU 2524  OE1 GLU B  61     4250   4713   4438    332   -181     89       O  
ATOM   2525  OE2 GLU B  61       8.090 -22.442 -15.714  1.00 36.71           O  
ANISOU 2525  OE2 GLU B  61     4409   4968   4572    305   -187    119       O  
ATOM   2526  N   ILE B  62       7.570 -18.722 -20.951  1.00 30.19           N  
ANISOU 2526  N   ILE B  62     3693   3976   3802    292   -161    -91       N  
ATOM   2527  CA  ILE B  62       8.175 -17.971 -22.031  1.00 30.32           C  
ANISOU 2527  CA  ILE B  62     3721   3975   3824    291   -158   -124       C  
ATOM   2528  C   ILE B  62       7.441 -18.363 -23.305  1.00 38.15           C  
ANISOU 2528  C   ILE B  62     4738   4905   4853    306   -153   -136       C  
ATOM   2529  O   ILE B  62       6.494 -19.149 -23.268  1.00 38.52           O  
ANISOU 2529  O   ILE B  62     4791   4926   4917    314   -151   -121       O  
ATOM   2530  CB  ILE B  62       9.697 -18.218 -22.134  1.00 31.04           C  
ANISOU 2530  CB  ILE B  62     3793   4091   3912    301   -163   -107       C  
ATOM   2531  CG1 ILE B  62       9.995 -19.429 -23.004  1.00 37.86           C  
ANISOU 2531  CG1 ILE B  62     4657   4914   4812    330   -162    -85       C  
ATOM   2532  CG2 ILE B  62      10.332 -18.365 -20.744  1.00 32.43           C  
ANISOU 2532  CG2 ILE B  62     3938   4329   4055    293   -171    -78       C  
ATOM   2533  CD1 ILE B  62      10.003 -20.683 -22.270  1.00 39.84           C  
ANISOU 2533  CD1 ILE B  62     4891   5173   5073    346   -165    -38       C  
ATOM   2534  N   GLY B  63       7.836 -17.808 -24.428  1.00 32.55           N  
ANISOU 2534  N   GLY B  63     4041   4173   4153    307   -150   -163       N  
ATOM   2535  CA  GLY B  63       6.837 -18.236 -25.403  1.00 43.74           C  
ANISOU 2535  CA  GLY B  63     5481   5539   5601    317   -145   -172       C  
ATOM   2536  C   GLY B  63       5.768 -17.185 -25.644  1.00 36.47           C  
ANISOU 2536  C   GLY B  63     4579   4604   4674    301   -141   -205       C  
ATOM   2537  O   GLY B  63       5.355 -16.451 -24.737  1.00 31.50           O  
ANISOU 2537  O   GLY B  63     3946   4001   4021    284   -140   -213       O  
ATOM   2538  N   ALA B  64       5.317 -17.105 -26.899  1.00 37.40           N  
ANISOU 2538  N   ALA B  64     4716   4681   4814    306   -137   -224       N  
ATOM   2539  CA  ALA B  64       4.789 -15.862 -27.435  1.00 33.40           C  
ANISOU 2539  CA  ALA B  64     4225   4163   4302    293   -133   -258       C  
ATOM   2540  C   ALA B  64       3.349 -15.623 -27.015  1.00 35.30           C  
ANISOU 2540  C   ALA B  64     4475   4396   4542    285   -130   -264       C  
ATOM   2541  O   ALA B  64       2.526 -16.541 -26.996  1.00 36.74           O  
ANISOU 2541  O   ALA B  64     4660   4560   4739    293   -130   -248       O  
ATOM   2542  CB  ALA B  64       4.882 -15.860 -28.958  1.00 38.38           C  
ANISOU 2542  CB  ALA B  64     4871   4758   4953    301   -131   -273       C  
ATOM   2543  N   GLU B  65       3.050 -14.388 -26.715  1.00 35.44           N  
ANISOU 2543  N   GLU B  65     4497   4426   4543    269   -126   -287       N  
ATOM   2544  CA  GLU B  65       1.704 -13.956 -26.382  1.00 41.25           C  
ANISOU 2544  CA  GLU B  65     5242   5154   5279    262   -121   -298       C  
ATOM   2545  C   GLU B  65       0.938 -13.587 -27.648  1.00 41.78           C  
ANISOU 2545  C   GLU B  65     5327   5182   5366    266   -118   -315       C  
ATOM   2546  O   GLU B  65       1.532 -13.255 -28.682  1.00 38.31           O  
ANISOU 2546  O   GLU B  65     4894   4727   4933    269   -118   -327       O  
ATOM   2547  CB  GLU B  65       1.761 -12.765 -25.423  1.00 36.89           C  
ANISOU 2547  CB  GLU B  65     4684   4632   4700    242   -116   -316       C  
ATOM   2548  N   PRO B  66      -0.390 -13.656 -27.614  1.00 41.64           N  
ANISOU 2548  N   PRO B  66     5316   5149   5356    266   -115   -317       N  
ATOM   2549  CA  PRO B  66      -1.163 -13.281 -28.803  1.00 43.77           C  
ANISOU 2549  CA  PRO B  66     5601   5387   5644    269   -113   -331       C  
ATOM   2550  C   PRO B  66      -0.985 -11.803 -29.114  1.00 45.16           C  
ANISOU 2550  C   PRO B  66     5784   5562   5813    260   -107   -357       C  
ATOM   2551  O   PRO B  66      -0.879 -10.968 -28.217  1.00 52.41           O  
ANISOU 2551  O   PRO B  66     6697   6501   6714    249   -102   -368       O  
ATOM   2552  CB  PRO B  66      -2.609 -13.610 -28.407  1.00 44.61           C  
ANISOU 2552  CB  PRO B  66     5708   5486   5755    269   -111   -326       C  
ATOM   2553  CG  PRO B  66      -2.487 -14.587 -27.262  1.00 40.97           C  
ANISOU 2553  CG  PRO B  66     5234   5046   5286    269   -114   -302       C  
ATOM   2554  CD  PRO B  66      -1.246 -14.171 -26.531  1.00 40.43           C  
ANISOU 2554  CD  PRO B  66     5155   5009   5197    263   -115   -302       C  
ATOM   2555  N   SER B  67      -0.930 -11.480 -30.400  1.00 50.92           N  
ANISOU 2555  N   SER B  67     6524   6267   6555    265   -107   -367       N  
ATOM   2556  CA  SER B  67      -0.881 -10.095 -30.832  1.00 57.05           C  
ANISOU 2556  CA  SER B  67     7309   7038   7330    258   -101   -388       C  
ATOM   2557  C   SER B  67      -2.200  -9.763 -31.535  1.00 61.75           C  
ANISOU 2557  C   SER B  67     7913   7608   7940    262    -98   -393       C  
ATOM   2558  O   SER B  67      -3.253 -10.307 -31.162  1.00 64.18           O  
ANISOU 2558  O   SER B  67     8220   7914   8253    265    -99   -384       O  
ATOM   2559  CB  SER B  67       0.357  -9.884 -31.705  1.00 60.91           C  
ANISOU 2559  CB  SER B  67     7801   7524   7819    258   -104   -394       C  
ATOM   2560  OG  SER B  67       0.481  -8.523 -32.073  1.00 63.38           O  
ANISOU 2560  OG  SER B  67     8121   7831   8130    250    -97   -413       O  
ATOM   2561  N   ALA B  68      -2.148  -8.878 -32.530  1.00 64.39           N  
ANISOU 2561  N   ALA B  68     8257   7927   8281    261    -96   -404       N  
ATOM   2562  CA  ALA B  68      -3.277  -8.493 -33.377  1.00 66.74           C  
ANISOU 2562  CA  ALA B  68     8563   8203   8594    266    -94   -406       C  
ATOM   2563  C   ALA B  68      -4.383  -7.780 -32.610  1.00 67.74           C  
ANISOU 2563  C   ALA B  68     8688   8331   8721    264    -85   -412       C  
ATOM   2564  O   ALA B  68      -5.487  -7.615 -33.143  1.00 69.00           O  
ANISOU 2564  O   ALA B  68     8849   8475   8892    269    -84   -409       O  
ATOM   2565  CB  ALA B  68      -3.870  -9.702 -34.120  1.00 66.64           C  
ANISOU 2565  CB  ALA B  68     8550   8179   8592    274   -102   -392       C  
ATOM   2566  N   PHE B  69      -4.125  -7.359 -31.373  1.00 67.63           N  
ANISOU 2566  N   PHE B  69     8668   8334   8693    255    -78   -420       N  
ATOM   2567  CA  PHE B  69      -5.089  -6.578 -30.610  1.00 67.39           C  
ANISOU 2567  CA  PHE B  69     8637   8305   8664    252    -67   -430       C  
ATOM   2568  C   PHE B  69      -4.371  -5.438 -29.899  1.00 70.63           C  
ANISOU 2568  C   PHE B  69     9047   8726   9063    239    -55   -450       C  
ATOM   2569  O   PHE B  69      -4.818  -4.285 -29.964  1.00 67.72           O  
ANISOU 2569  O   PHE B  69     8683   8344   8702    237    -43   -465       O  
ATOM   2570  CB  PHE B  69      -5.835  -7.457 -29.600  1.00 62.05           C  
ANISOU 2570  CB  PHE B  69     7951   7644   7982    252    -69   -420       C  
ATOM   2571  N   GLY B  70      -3.255  -5.759 -29.227  1.00 69.82           N  
ANISOU 2571  N   GLY B  70     8938   8648   8943    230    -59   -451       N  
ATOM   2572  CA  GLY B  70      -2.467  -4.818 -28.455  1.00 66.64           C  
ANISOU 2572  CA  GLY B  70     8533   8262   8524    214    -48   -471       C  
ATOM   2573  C   GLY B  70      -3.272  -3.739 -27.759  1.00 64.06           C  
ANISOU 2573  C   GLY B  70     8207   7932   8199    206    -31   -491       C  
ATOM   2574  O   GLY B  70      -2.837  -2.586 -27.667  1.00 66.00           O  
ANISOU 2574  O   GLY B  70     8459   8175   8445    195    -18   -512       O  
ATOM   2575  N   LEU B  71      -4.456  -4.095 -27.270  1.00 63.12           N  
ANISOU 2575  N   LEU B  71     8085   7814   8085    211    -29   -485       N  
ATOM   2576  CA  LEU B  71      -5.405  -3.085 -26.814  1.00 66.46           C  
ANISOU 2576  CA  LEU B  71     8510   8228   8516    208    -12   -503       C  
ATOM   2577  C   LEU B  71      -5.086  -2.643 -25.383  1.00 61.44           C  
ANISOU 2577  C   LEU B  71     7864   7621   7857    188      1   -523       C  
ATOM   2578  O   LEU B  71      -4.026  -2.057 -25.135  1.00 62.17           O  
ANISOU 2578  O   LEU B  71     7957   7725   7937    174      6   -538       O  
ATOM   2579  CB  LEU B  71      -6.839  -3.608 -26.953  1.00 56.82           C  
ANISOU 2579  CB  LEU B  71     7286   6995   7308    222    -14   -489       C  
ATOM   2580  N   LEU B  72      -5.980  -2.915 -24.434  1.00 57.05           N  
ANISOU 2580  N   LEU B  72     7301   7081   7296    186      6   -523       N  
ATOM   2581  CA  LEU B  72      -5.828  -2.390 -23.082  1.00 58.79           C  
ANISOU 2581  CA  LEU B  72     7512   7330   7495    165     20   -545       C  
ATOM   2582  C   LEU B  72      -6.837  -3.053 -22.150  1.00 59.17           C  
ANISOU 2582  C   LEU B  72     7549   7398   7534    165     20   -537       C  
ATOM   2583  O   LEU B  72      -7.811  -2.410 -21.725  1.00 61.35           O  
ANISOU 2583  O   LEU B  72     7824   7667   7818    164     36   -554       O  
ATOM   2584  CB  LEU B  72      -6.005  -0.868 -23.080  1.00 59.33           C  
ANISOU 2584  CB  LEU B  72     7589   7379   7576    158     43   -577       C  
ATOM   2585  N   LYS B  73      -6.624  -4.346 -21.855  1.00 49.75           N  
ANISOU 2585  N   LYS B  73     6348   6228   6328    167      3   -511       N  
ATOM   2586  CA  LYS B  73      -7.591  -5.170 -21.132  1.00 47.60           C  
ANISOU 2586  CA  LYS B  73     6065   5972   6049    169      0   -496       C  
ATOM   2587  C   LYS B  73      -8.904  -5.222 -21.910  1.00 46.40           C  
ANISOU 2587  C   LYS B  73     5919   5786   5923    187      1   -490       C  
ATOM   2588  O   LYS B  73      -9.321  -6.296 -22.361  1.00 45.52           O  
ANISOU 2588  O   LYS B  73     5807   5667   5819    199    -13   -464       O  
ATOM   2589  CB  LYS B  73      -7.830  -4.646 -19.706  1.00 43.47           C  
ANISOU 2589  CB  LYS B  73     5532   5482   5504    148     15   -518       C  
ATOM   2590  CG  LYS B  73      -6.728  -4.911 -18.690  1.00 46.03           C  
ANISOU 2590  CG  LYS B  73     5843   5852   5794    128     11   -517       C  
ATOM   2591  CD  LYS B  73      -6.971  -4.141 -17.359  1.00 43.41           C  
ANISOU 2591  CD  LYS B  73     5501   5553   5440    104     31   -546       C  
ATOM   2592  CE  LYS B  73      -5.853  -4.439 -16.344  1.00 44.49           C  
ANISOU 2592  CE  LYS B  73     5622   5741   5539     81     25   -543       C  
ATOM   2593  NZ  LYS B  73      -5.283  -3.331 -15.458  1.00 32.72           N  
ANISOU 2593  NZ  LYS B  73     4126   4280   4025     52     43   -581       N  
ATOM   2594  N   GLU B  74      -9.570  -4.075 -22.066  1.00 49.18           N  
ANISOU 2594  N   GLU B  74     6276   6117   6291    189     18   -512       N  
ATOM   2595  CA  GLU B  74     -10.747  -4.007 -22.927  1.00 50.39           C  
ANISOU 2595  CA  GLU B  74     6435   6240   6471    207     19   -505       C  
ATOM   2596  C   GLU B  74     -10.300  -4.213 -24.373  1.00 49.62           C  
ANISOU 2596  C   GLU B  74     6348   6116   6390    221      6   -490       C  
ATOM   2597  O   GLU B  74      -9.391  -3.531 -24.860  1.00 56.31           O  
ANISOU 2597  O   GLU B  74     7203   6952   7239    218      8   -501       O  
ATOM   2598  CB  GLU B  74     -11.480  -2.672 -22.735  1.00 48.87           C  
ANISOU 2598  CB  GLU B  74     6244   6032   6293    207     42   -531       C  
ATOM   2599  CG  GLU B  74     -10.708  -1.427 -23.169  1.00 53.38           C  
ANISOU 2599  CG  GLU B  74     6825   6583   6873    203     55   -553       C  
ATOM   2600  CD  GLU B  74     -11.600  -0.230 -23.461  1.00 56.07           C  
ANISOU 2600  CD  GLU B  74     7170   6894   7240    213     76   -569       C  
ATOM   2601  OE1 GLU B  74     -12.473   0.086 -22.620  1.00 51.59           O  
ANISOU 2601  OE1 GLU B  74     6595   6334   6673    210     91   -583       O  
ATOM   2602  OE2 GLU B  74     -11.431   0.389 -24.538  1.00 54.88           O  
ANISOU 2602  OE2 GLU B  74     7029   6712   7111    223     77   -567       O  
ATOM   2603  N   GLY B  75     -10.881  -5.194 -25.045  1.00 52.67           N  
ANISOU 2603  N   GLY B  75     6734   6493   6785    233     -8   -467       N  
ATOM   2604  CA  GLY B  75     -10.400  -5.611 -26.342  1.00 47.14           C  
ANISOU 2604  CA  GLY B  75     6042   5773   6096    244    -22   -452       C  
ATOM   2605  C   GLY B  75      -9.638  -6.919 -26.344  1.00 45.82           C  
ANISOU 2605  C   GLY B  75     5873   5620   5918    242    -39   -433       C  
ATOM   2606  O   GLY B  75      -9.479  -7.517 -27.415  1.00 42.49           O  
ANISOU 2606  O   GLY B  75     5456   5182   5506    251    -50   -419       O  
ATOM   2607  N   LYS B  76      -9.158  -7.387 -25.185  1.00 42.12           N  
ANISOU 2607  N   LYS B  76     5396   5181   5429    231    -40   -431       N  
ATOM   2608  CA  LYS B  76      -8.584  -8.733 -25.074  1.00 41.62           C  
ANISOU 2608  CA  LYS B  76     5328   5130   5357    232    -54   -407       C  
ATOM   2609  C   LYS B  76      -9.503  -9.597 -24.232  1.00 41.79           C  
ANISOU 2609  C   LYS B  76     5339   5166   5372    230    -55   -393       C  
ATOM   2610  O   LYS B  76      -9.798  -9.243 -23.076  1.00 36.29           O  
ANISOU 2610  O   LYS B  76     4635   4494   4661    219    -46   -402       O  
ATOM   2611  CB  LYS B  76      -7.185  -8.718 -24.459  1.00 43.12           C  
ANISOU 2611  CB  LYS B  76     5513   5345   5527    221    -56   -409       C  
ATOM   2612  CG  LYS B  76      -6.346  -7.563 -24.903  1.00 50.24           C  
ANISOU 2612  CG  LYS B  76     6422   6238   6429    217    -50   -430       C  
ATOM   2613  CD  LYS B  76      -5.039  -7.446 -24.132  1.00 45.43           C  
ANISOU 2613  CD  LYS B  76     5805   5660   5796    203    -50   -435       C  
ATOM   2614  CE  LYS B  76      -3.829  -7.527 -25.040  1.00 47.33           C  
ANISOU 2614  CE  LYS B  76     6051   5892   6040    207    -59   -431       C  
ATOM   2615  NZ  LYS B  76      -2.603  -7.373 -24.210  1.00 48.85           N  
ANISOU 2615  NZ  LYS B  76     6233   6119   6208    193    -59   -436       N  
ATOM   2616  N   PRO B  77      -9.986 -10.720 -24.764  1.00 34.98           N  
ANISOU 2616  N   PRO B  77     4478   4292   4522    239    -65   -372       N  
ATOM   2617  CA  PRO B  77     -10.778 -11.647 -23.950  1.00 35.54           C  
ANISOU 2617  CA  PRO B  77     4540   4377   4587    235    -67   -356       C  
ATOM   2618  C   PRO B  77      -9.945 -12.595 -23.099  1.00 33.54           C  
ANISOU 2618  C   PRO B  77     4278   4149   4317    230    -74   -336       C  
ATOM   2619  O   PRO B  77     -10.536 -13.364 -22.333  1.00 34.72           O  
ANISOU 2619  O   PRO B  77     4419   4312   4460    226    -75   -320       O  
ATOM   2620  CB  PRO B  77     -11.585 -12.420 -25.006  1.00 35.19           C  
ANISOU 2620  CB  PRO B  77     4501   4307   4563    246    -73   -343       C  
ATOM   2621  CG  PRO B  77     -10.657 -12.462 -26.180  1.00 34.55           C  
ANISOU 2621  CG  PRO B  77     4429   4206   4492    253    -80   -343       C  
ATOM   2622  CD  PRO B  77      -9.864 -11.169 -26.160  1.00 35.87           C  
ANISOU 2622  CD  PRO B  77     4599   4376   4652    250    -74   -364       C  
ATOM   2623  N   TYR B  78      -8.607 -12.556 -23.192  1.00 29.97           N  
ANISOU 2623  N   TYR B  78     3826   3703   3859    229    -78   -335       N  
ATOM   2624  CA  TYR B  78      -7.741 -13.553 -22.566  1.00 29.30           C  
ANISOU 2624  CA  TYR B  78     3732   3639   3762    228    -86   -311       C  
ATOM   2625  C   TYR B  78      -6.844 -12.963 -21.474  1.00 31.40           C  
ANISOU 2625  C   TYR B  78     3987   3943   4000    214    -83   -318       C  
ATOM   2626  O   TYR B  78      -6.636 -11.751 -21.372  1.00 29.75           O  
ANISOU 2626  O   TYR B  78     3780   3740   3783    206    -75   -344       O  
ATOM   2627  CB  TYR B  78      -6.849 -14.243 -23.599  1.00 29.16           C  
ANISOU 2627  CB  TYR B  78     3721   3601   3760    240    -96   -298       C  
ATOM   2628  CG  TYR B  78      -5.952 -13.288 -24.327  1.00 31.22           C  
ANISOU 2628  CG  TYR B  78     3989   3853   4021    241    -94   -319       C  
ATOM   2629  CD1 TYR B  78      -6.377 -12.673 -25.501  1.00 34.86           C  
ANISOU 2629  CD1 TYR B  78     4462   4284   4498    246    -92   -335       C  
ATOM   2630  CD2 TYR B  78      -4.688 -12.976 -23.838  1.00 32.46           C  
ANISOU 2630  CD2 TYR B  78     4139   4035   4161    234    -96   -320       C  
ATOM   2631  CE1 TYR B  78      -5.558 -11.786 -26.178  1.00 37.86           C  
ANISOU 2631  CE1 TYR B  78     4848   4656   4879    246    -90   -352       C  
ATOM   2632  CE2 TYR B  78      -3.859 -12.083 -24.503  1.00 35.61           C  
ANISOU 2632  CE2 TYR B  78     4544   4427   4559    233    -94   -339       C  
ATOM   2633  CZ  TYR B  78      -4.299 -11.493 -25.674  1.00 39.08           C  
ANISOU 2633  CZ  TYR B  78     4997   4834   5017    239    -91   -355       C  
ATOM   2634  OH  TYR B  78      -3.489 -10.603 -26.348  1.00 44.32           O  
ANISOU 2634  OH  TYR B  78     5667   5490   5681    238    -89   -372       O  
ATOM   2635  N   TYR B  79      -6.260 -13.883 -20.704  1.00 28.49           N  
ANISOU 2635  N   TYR B  79     3606   3600   3619    212    -90   -292       N  
ATOM   2636  CA  TYR B  79      -5.405 -13.624 -19.554  1.00 27.58           C  
ANISOU 2636  CA  TYR B  79     3476   3529   3474    198    -90   -290       C  
ATOM   2637  C   TYR B  79      -4.143 -14.455 -19.703  1.00 29.90           C  
ANISOU 2637  C   TYR B  79     3763   3830   3768    206   -101   -264       C  
ATOM   2638  O   TYR B  79      -4.226 -15.673 -19.889  1.00 27.69           O  
ANISOU 2638  O   TYR B  79     3482   3538   3502    218   -108   -235       O  
ATOM   2639  CB  TYR B  79      -6.089 -14.034 -18.237  1.00 24.85           C  
ANISOU 2639  CB  TYR B  79     3116   3216   3110    186    -88   -276       C  
ATOM   2640  CG  TYR B  79      -7.431 -13.390 -17.986  1.00 24.71           C  
ANISOU 2640  CG  TYR B  79     3102   3193   3093    179    -76   -298       C  
ATOM   2641  CD1 TYR B  79      -8.581 -13.863 -18.602  1.00 26.24           C  
ANISOU 2641  CD1 TYR B  79     3305   3356   3310    190    -76   -292       C  
ATOM   2642  CD2 TYR B  79      -7.543 -12.298 -17.137  1.00 22.35           C  
ANISOU 2642  CD2 TYR B  79     2797   2922   2772    161    -65   -325       C  
ATOM   2643  CE1 TYR B  79      -9.818 -13.262 -18.355  1.00 27.34           C  
ANISOU 2643  CE1 TYR B  79     3445   3493   3450    184    -66   -311       C  
ATOM   2644  CE2 TYR B  79      -8.751 -11.706 -16.893  1.00 24.14           C  
ANISOU 2644  CE2 TYR B  79     3026   3144   3002    156    -52   -345       C  
ATOM   2645  CZ  TYR B  79      -9.891 -12.190 -17.500  1.00 23.99           C  
ANISOU 2645  CZ  TYR B  79     3015   3095   3006    169    -53   -337       C  
ATOM   2646  OH  TYR B  79     -11.100 -11.578 -17.240  1.00 24.56           O  
ANISOU 2646  OH  TYR B  79     3087   3164   3080    165    -41   -356       O  
ATOM   2647  N   THR B  80      -2.985 -13.824 -19.590  1.00 26.72           N  
ANISOU 2647  N   THR B  80     3355   3448   3349    199   -102   -275       N  
ATOM   2648  CA  THR B  80      -1.766 -14.584 -19.387  1.00 25.91           C  
ANISOU 2648  CA  THR B  80     3240   3366   3240    204   -111   -248       C  
ATOM   2649  C   THR B  80      -1.411 -14.567 -17.902  1.00 27.60           C  
ANISOU 2649  C   THR B  80     3433   3636   3419    187   -112   -236       C  
ATOM   2650  O   THR B  80      -1.917 -13.743 -17.126  1.00 27.52           O  
ANISOU 2650  O   THR B  80     3419   3648   3389    168   -103   -258       O  
ATOM   2651  CB  THR B  80      -0.625 -14.011 -20.218  1.00 29.07           C  
ANISOU 2651  CB  THR B  80     3644   3756   3643    207   -113   -263       C  
ATOM   2652  OG1 THR B  80      -0.522 -12.602 -19.975  1.00 28.84           O  
ANISOU 2652  OG1 THR B  80     3619   3742   3597    189   -104   -299       O  
ATOM   2653  CG2 THR B  80      -0.913 -14.229 -21.679  1.00 29.63           C  
ANISOU 2653  CG2 THR B  80     3735   3777   3747    225   -114   -268       C  
ATOM   2654  N   LEU B  81      -0.548 -15.504 -17.505  1.00 24.46           N  
ANISOU 2654  N   LEU B  81     3019   3260   3015    193   -122   -201       N  
ATOM   2655  CA  LEU B  81      -0.074 -15.541 -16.130  1.00 26.92           C  
ANISOU 2655  CA  LEU B  81     3307   3631   3291    177   -125   -186       C  
ATOM   2656  C   LEU B  81       1.023 -14.498 -15.927  1.00 28.55           C  
ANISOU 2656  C   LEU B  81     3506   3870   3472    161   -123   -210       C  
ATOM   2657  O   LEU B  81       1.764 -14.179 -16.861  1.00 32.60           O  
ANISOU 2657  O   LEU B  81     4027   4361   3998    169   -124   -222       O  
ATOM   2658  CB  LEU B  81       0.460 -16.922 -15.783  1.00 24.23           C  
ANISOU 2658  CB  LEU B  81     2950   3303   2954    191   -135   -135       C  
ATOM   2659  CG  LEU B  81      -0.531 -18.079 -15.659  1.00 27.70           C  
ANISOU 2659  CG  LEU B  81     3392   3721   3412    202   -137   -105       C  
ATOM   2660  CD1 LEU B  81       0.215 -19.407 -15.488  1.00 26.26           C  
ANISOU 2660  CD1 LEU B  81     3195   3545   3239    219   -146    -54       C  
ATOM   2661  CD2 LEU B  81      -1.540 -17.856 -14.509  1.00 25.05           C  
ANISOU 2661  CD2 LEU B  81     3049   3417   3053    182   -132   -107       C  
ATOM   2662  N   PRO B  82       1.161 -13.956 -14.704  1.00 26.52           N  
ANISOU 2662  N   PRO B  82     3232   3666   3177    136   -119   -218       N  
ATOM   2663  CA  PRO B  82       0.377 -14.261 -13.509  1.00 25.27           C  
ANISOU 2663  CA  PRO B  82     3061   3541   2998    122   -118   -204       C  
ATOM   2664  C   PRO B  82      -1.007 -13.617 -13.573  1.00 24.34           C  
ANISOU 2664  C   PRO B  82     2960   3399   2890    116   -104   -236       C  
ATOM   2665  O   PRO B  82      -1.293 -12.742 -14.386  1.00 22.00           O  
ANISOU 2665  O   PRO B  82     2682   3067   2611    117    -96   -272       O  
ATOM   2666  CB  PRO B  82       1.237 -13.677 -12.382  1.00 23.51           C  
ANISOU 2666  CB  PRO B  82     2815   3387   2731     95   -117   -211       C  
ATOM   2667  CG  PRO B  82       1.839 -12.439 -13.007  1.00 26.12           C  
ANISOU 2667  CG  PRO B  82     3158   3707   3062     86   -109   -255       C  
ATOM   2668  CD  PRO B  82       2.094 -12.836 -14.469  1.00 25.70           C  
ANISOU 2668  CD  PRO B  82     3122   3594   3048    115   -115   -247       C  
ATOM   2669  N   ILE B  83      -1.890 -14.070 -12.701  1.00 25.24           N  
ANISOU 2669  N   ILE B  83     3065   3532   2993    108   -103   -222       N  
ATOM   2670  CA  ILE B  83      -3.237 -13.540 -12.573  1.00 21.26           C  
ANISOU 2670  CA  ILE B  83     2572   3012   2494    101    -90   -248       C  
ATOM   2671  C   ILE B  83      -3.461 -13.210 -11.108  1.00 23.64           C  
ANISOU 2671  C   ILE B  83     2854   3373   2755     73    -84   -254       C  
ATOM   2672  O   ILE B  83      -3.052 -13.981 -10.237  1.00 21.96           O  
ANISOU 2672  O   ILE B  83     2621   3204   2520     67    -93   -219       O  
ATOM   2673  CB  ILE B  83      -4.281 -14.561 -13.068  1.00 22.82           C  
ANISOU 2673  CB  ILE B  83     2779   3170   2721    121    -94   -224       C  
ATOM   2674  CG1 ILE B  83      -4.119 -14.774 -14.576  1.00 25.32           C  
ANISOU 2674  CG1 ILE B  83     3116   3429   3076    145    -98   -225       C  
ATOM   2675  CG2 ILE B  83      -5.694 -14.085 -12.733  1.00 22.81           C  
ANISOU 2675  CG2 ILE B  83     2784   3163   2721    112    -81   -247       C  
ATOM   2676  CD1 ILE B  83      -4.886 -15.959 -15.103  1.00 21.83           C  
ANISOU 2676  CD1 ILE B  83     2681   2951   2664    164   -103   -196       C  
ATOM   2677  N   ILE B  84      -4.096 -12.069 -10.829  1.00 24.46           N  
ANISOU 2677  N   ILE B  84     2964   3480   2851     56    -67   -298       N  
ATOM   2678  CA  ILE B  84      -4.546 -11.752  -9.478  1.00 24.44           C  
ANISOU 2678  CA  ILE B  84     2944   3529   2812     29    -58   -309       C  
ATOM   2679  C   ILE B  84      -6.058 -11.618  -9.484  1.00 25.76           C  
ANISOU 2679  C   ILE B  84     3121   3670   2995     31    -46   -324       C  
ATOM   2680  O   ILE B  84      -6.647 -11.113 -10.445  1.00 22.88           O  
ANISOU 2680  O   ILE B  84     2777   3254   2662     45    -39   -347       O  
ATOM   2681  CB  ILE B  84      -3.892 -10.480  -8.894  1.00 25.67           C  
ANISOU 2681  CB  ILE B  84     3094   3723   2938      0    -45   -351       C  
ATOM   2682  CG1 ILE B  84      -4.229  -9.231  -9.715  1.00 23.57           C  
ANISOU 2682  CG1 ILE B  84     2849   3410   2695      2    -28   -400       C  
ATOM   2683  CG2 ILE B  84      -2.370 -10.649  -8.750  1.00 26.66           C  
ANISOU 2683  CG2 ILE B  84     3204   3884   3042     -6    -58   -334       C  
ATOM   2684  CD1 ILE B  84      -4.070  -7.944  -8.938  1.00 25.22           C  
ANISOU 2684  CD1 ILE B  84     3052   3652   2877    -31     -9   -448       C  
ATOM   2685  N   HIS B  85      -6.674 -12.111  -8.421  1.00 23.39           N  
ANISOU 2685  N   HIS B  85     2806   3409   2673     18    -46   -308       N  
ATOM   2686  CA  HIS B  85      -8.029 -11.747  -8.043  1.00 26.23           C  
ANISOU 2686  CA  HIS B  85     3168   3763   3034     10    -31   -330       C  
ATOM   2687  C   HIS B  85      -7.927 -10.843  -6.826  1.00 27.53           C  
ANISOU 2687  C   HIS B  85     3318   3985   3158    -24    -16   -362       C  
ATOM   2688  O   HIS B  85      -7.287 -11.212  -5.834  1.00 24.69           O  
ANISOU 2688  O   HIS B  85     2937   3684   2761    -42    -23   -343       O  
ATOM   2689  CB  HIS B  85      -8.871 -12.979  -7.723  1.00 25.97           C  
ANISOU 2689  CB  HIS B  85     3130   3734   3006     18    -39   -289       C  
ATOM   2690  CG  HIS B  85     -10.200 -12.642  -7.126  1.00 28.19           C  
ANISOU 2690  CG  HIS B  85     3408   4022   3281      6    -24   -310       C  
ATOM   2691  ND1 HIS B  85     -10.593 -13.095  -5.885  1.00 29.33           N  
ANISOU 2691  ND1 HIS B  85     3532   4218   3393    -14    -23   -293       N  
ATOM   2692  CD2 HIS B  85     -11.211 -11.866  -7.583  1.00 30.19           C  
ANISOU 2692  CD2 HIS B  85     3674   4241   3555     11     -8   -346       C  
ATOM   2693  CE1 HIS B  85     -11.795 -12.623  -5.608  1.00 33.64           C  
ANISOU 2693  CE1 HIS B  85     4079   4760   3940    -21     -7   -320       C  
ATOM   2694  NE2 HIS B  85     -12.193 -11.873  -6.620  1.00 31.21           N  
ANISOU 2694  NE2 HIS B  85     3792   4400   3666     -5      2   -351       N  
ATOM   2695  N   ASP B  86      -8.520  -9.656  -6.914  1.00 26.82           N  
ANISOU 2695  N   ASP B  86     3237   3877   3075    -32      5   -412       N  
ATOM   2696  CA  ASP B  86      -8.540  -8.738  -5.778  1.00 28.22           C  
ANISOU 2696  CA  ASP B  86     3402   4105   3217    -66     24   -450       C  
ATOM   2697  C   ASP B  86      -9.950  -8.671  -5.209  1.00 29.59           C  
ANISOU 2697  C   ASP B  86     3571   4281   3389    -72     38   -463       C  
ATOM   2698  O   ASP B  86     -10.831  -8.052  -5.824  1.00 28.61           O  
ANISOU 2698  O   ASP B  86     3462   4111   3296    -59     52   -490       O  
ATOM   2699  CB  ASP B  86      -8.063  -7.340  -6.172  1.00 23.31           C  
ANISOU 2699  CB  ASP B  86     2791   3464   2601    -74     41   -501       C  
ATOM   2700  CG  ASP B  86      -7.890  -6.416  -4.958  1.00 26.62           C  
ANISOU 2700  CG  ASP B  86     3195   3938   2981   -113     61   -542       C  
ATOM   2701  OD1 ASP B  86      -8.320  -6.777  -3.832  1.00 27.21           O  
ANISOU 2701  OD1 ASP B  86     3252   4064   3024   -133     64   -535       O  
ATOM   2702  OD2 ASP B  86      -7.328  -5.321  -5.135  1.00 23.82           O  
ANISOU 2702  OD2 ASP B  86     2848   3577   2626   -126     76   -583       O  
ATOM   2703  N   PRO B  87     -10.200  -9.269  -4.045  1.00 30.17           N  
ANISOU 2703  N   PRO B  87     3625   4411   3429    -91     36   -443       N  
ATOM   2704  CA  PRO B  87     -11.538  -9.175  -3.443  1.00 31.36           C  
ANISOU 2704  CA  PRO B  87     3770   4569   3576    -99     51   -457       C  
ATOM   2705  C   PRO B  87     -11.999  -7.751  -3.152  1.00 33.44           C  
ANISOU 2705  C   PRO B  87     4036   4832   3837   -117     80   -520       C  
ATOM   2706  O   PRO B  87     -13.209  -7.519  -3.086  1.00 31.54           O  
ANISOU 2706  O   PRO B  87     3798   4574   3610   -113     95   -538       O  
ATOM   2707  CB  PRO B  87     -11.386  -9.986  -2.148  1.00 35.28           C  
ANISOU 2707  CB  PRO B  87     4240   5138   4027   -123     42   -425       C  
ATOM   2708  CG  PRO B  87     -10.267 -10.921  -2.420  1.00 33.55           C  
ANISOU 2708  CG  PRO B  87     4017   4926   3805   -111     17   -376       C  
ATOM   2709  CD  PRO B  87      -9.311 -10.167  -3.292  1.00 26.36           C  
ANISOU 2709  CD  PRO B  87     3120   3984   2911   -103     17   -401       C  
ATOM   2710  N   ALA B  88     -11.086  -6.789  -2.957  1.00 30.85           N  
ANISOU 2710  N   ALA B  88     3708   4521   3493   -136     91   -556       N  
ATOM   2711  CA  ALA B  88     -11.515  -5.440  -2.596  1.00 31.49           C  
ANISOU 2711  CA  ALA B  88     3791   4601   3572   -155    122   -617       C  
ATOM   2712  C   ALA B  88     -12.385  -4.814  -3.684  1.00 34.45           C  
ANISOU 2712  C   ALA B  88     4189   4902   3999   -127    136   -640       C  
ATOM   2713  O   ALA B  88     -13.302  -4.040  -3.376  1.00 32.81           O  
ANISOU 2713  O   ALA B  88     3982   4686   3799   -133    161   -678       O  
ATOM   2714  CB  ALA B  88     -10.304  -4.553  -2.302  1.00 30.84           C  
ANISOU 2714  CB  ALA B  88     3705   4545   3466   -181    131   -650       C  
ATOM   2715  N   THR B  89     -12.143  -5.164  -4.947  1.00 28.92           N  
ANISOU 2715  N   THR B  89     3506   4149   3335    -95    119   -615       N  
ATOM   2716  CA  THR B  89     -12.918  -4.664  -6.072  1.00 28.19           C  
ANISOU 2716  CA  THR B  89     3433   3988   3290    -67    128   -628       C  
ATOM   2717  C   THR B  89     -13.551  -5.772  -6.903  1.00 33.47           C  
ANISOU 2717  C   THR B  89     4109   4622   3986    -36    107   -583       C  
ATOM   2718  O   THR B  89     -14.251  -5.470  -7.883  1.00 31.67           O  
ANISOU 2718  O   THR B  89     3896   4341   3796    -12    112   -589       O  
ATOM   2719  CB  THR B  89     -12.027  -3.828  -6.999  1.00 31.09           C  
ANISOU 2719  CB  THR B  89     3817   4317   3677    -59    131   -648       C  
ATOM   2720  OG1 THR B  89     -10.977  -4.668  -7.509  1.00 27.82           O  
ANISOU 2720  OG1 THR B  89     3405   3905   3260    -50    104   -609       O  
ATOM   2721  CG2 THR B  89     -11.427  -2.640  -6.236  1.00 28.71           C  
ANISOU 2721  CG2 THR B  89     3512   4045   3353    -92    155   -698       C  
ATOM   2722  N   ASP B  90     -13.290  -7.034  -6.561  1.00 30.51           N  
ANISOU 2722  N   ASP B  90     3724   4277   3592    -37     85   -538       N  
ATOM   2723  CA  ASP B  90     -13.676  -8.205  -7.354  1.00 34.33           C  
ANISOU 2723  CA  ASP B  90     4214   4730   4100    -10     64   -493       C  
ATOM   2724  C   ASP B  90     -13.140  -8.156  -8.786  1.00 31.58           C  
ANISOU 2724  C   ASP B  90     3886   4327   3787     16     53   -486       C  
ATOM   2725  O   ASP B  90     -13.791  -8.599  -9.734  1.00 32.60           O  
ANISOU 2725  O   ASP B  90     4026   4413   3948     40     46   -469       O  
ATOM   2726  CB  ASP B  90     -15.187  -8.389  -7.337  1.00 36.15           C  
ANISOU 2726  CB  ASP B  90     4444   4946   4347     -1     72   -493       C  
ATOM   2727  CG  ASP B  90     -15.622  -9.281  -6.205  1.00 40.30           C  
ANISOU 2727  CG  ASP B  90     4951   5520   4842    -18     68   -468       C  
ATOM   2728  OD1 ASP B  90     -16.650  -8.963  -5.572  1.00 38.27           O  
ANISOU 2728  OD1 ASP B  90     4685   5279   4578    -28     84   -488       O  
ATOM   2729  OD2 ASP B  90     -14.894 -10.274  -5.930  1.00 40.19           O  
ANISOU 2729  OD2 ASP B  90     4929   5531   4810    -21     48   -428       O  
ATOM   2730  N   SER B  91     -11.926  -7.654  -8.942  1.00 30.46           N  
ANISOU 2730  N   SER B  91     3747   4190   3637      9     51   -497       N  
ATOM   2731  CA  SER B  91     -11.308  -7.570 -10.249  1.00 28.51           C  
ANISOU 2731  CA  SER B  91     3517   3897   3419     31     42   -492       C  
ATOM   2732  C   SER B  91     -10.448  -8.806 -10.483  1.00 29.88           C  
ANISOU 2732  C   SER B  91     3688   4079   3587     40     17   -446       C  
ATOM   2733  O   SER B  91      -9.921  -9.409  -9.544  1.00 28.95           O  
ANISOU 2733  O   SER B  91     3553   4010   3438     24      8   -425       O  
ATOM   2734  CB  SER B  91     -10.452  -6.310 -10.360  1.00 33.78           C  
ANISOU 2734  CB  SER B  91     4191   4562   4083     19     55   -531       C  
ATOM   2735  OG  SER B  91     -11.254  -5.147 -10.374  1.00 31.69           O  
ANISOU 2735  OG  SER B  91     3933   4276   3833     16     80   -572       O  
ATOM   2736  N   LEU B  92     -10.322  -9.189 -11.748  1.00 25.36           N  
ANISOU 2736  N   LEU B  92     3130   3459   3046     65      5   -429       N  
ATOM   2737  CA  LEU B  92      -9.434 -10.273 -12.147  1.00 22.30           C  
ANISOU 2737  CA  LEU B  92     2742   3071   2661     76    -16   -390       C  
ATOM   2738  C   LEU B  92      -8.570  -9.740 -13.270  1.00 26.73           C  
ANISOU 2738  C   LEU B  92     3317   3599   3241     88    -19   -402       C  
ATOM   2739  O   LEU B  92      -9.091  -9.340 -14.314  1.00 24.04           O  
ANISOU 2739  O   LEU B  92     2992   3211   2930    104    -15   -415       O  
ATOM   2740  CB  LEU B  92     -10.224 -11.510 -12.579  1.00 23.49           C  
ANISOU 2740  CB  LEU B  92     2895   3199   2832     95    -28   -354       C  
ATOM   2741  CG  LEU B  92      -9.471 -12.787 -12.956  1.00 27.07           C  
ANISOU 2741  CG  LEU B  92     3346   3646   3291    108    -48   -311       C  
ATOM   2742  CD1 LEU B  92      -9.115 -13.592 -11.696  1.00 25.44           C  
ANISOU 2742  CD1 LEU B  92     3120   3493   3054     94    -55   -280       C  
ATOM   2743  CD2 LEU B  92     -10.320 -13.628 -13.918  1.00 25.08           C  
ANISOU 2743  CD2 LEU B  92     3107   3349   3073    129    -54   -292       C  
ATOM   2744  N   ILE B  93      -7.262  -9.679 -13.029  1.00 24.30           N  
ANISOU 2744  N   ILE B  93     3002   3317   2913     79    -25   -399       N  
ATOM   2745  CA  ILE B  93      -6.323  -9.043 -13.939  1.00 25.58           C  
ANISOU 2745  CA  ILE B  93     3177   3456   3088     84    -26   -414       C  
ATOM   2746  C   ILE B  93      -5.227 -10.044 -14.254  1.00 24.84           C  
ANISOU 2746  C   ILE B  93     3077   3369   2992     95    -45   -378       C  
ATOM   2747  O   ILE B  93      -4.603 -10.592 -13.340  1.00 23.94           O  
ANISOU 2747  O   ILE B  93     2945   3301   2851     84    -53   -357       O  
ATOM   2748  CB  ILE B  93      -5.709  -7.752 -13.357  1.00 27.23           C  
ANISOU 2748  CB  ILE B  93     3382   3691   3275     60    -11   -454       C  
ATOM   2749  CG1 ILE B  93      -6.779  -6.742 -12.958  1.00 27.51           C  
ANISOU 2749  CG1 ILE B  93     3420   3720   3312     49     12   -492       C  
ATOM   2750  CG2 ILE B  93      -4.823  -7.104 -14.379  1.00 29.12           C  
ANISOU 2750  CG2 ILE B  93     3635   3902   3530     66    -11   -469       C  
ATOM   2751  CD1 ILE B  93      -7.017  -6.728 -11.519  1.00 28.71           C  
ANISOU 2751  CD1 ILE B  93     3554   3925   3429     24     20   -499       C  
ATOM   2752  N   GLY B  94      -5.009 -10.287 -15.546  1.00 21.88           N  
ANISOU 2752  N   GLY B  94     2717   2949   2647    116    -53   -371       N  
ATOM   2753  CA  GLY B  94      -3.859 -11.016 -16.027  1.00 23.97           C  
ANISOU 2753  CA  GLY B  94     2979   3214   2914    127    -68   -344       C  
ATOM   2754  C   GLY B  94      -2.928 -10.053 -16.740  1.00 27.18           C  
ANISOU 2754  C   GLY B  94     3394   3608   3324    125    -64   -370       C  
ATOM   2755  O   GLY B  94      -3.223  -8.871 -16.891  1.00 26.59           O  
ANISOU 2755  O   GLY B  94     3329   3520   3252    116    -50   -406       O  
ATOM   2756  N   ASP B  95      -1.795 -10.591 -17.177  1.00 26.03           N  
ANISOU 2756  N   ASP B  95     3246   3465   3181    134    -77   -351       N  
ATOM   2757  CA  ASP B  95      -0.729  -9.793 -17.780  1.00 28.40           C  
ANISOU 2757  CA  ASP B  95     3551   3760   3480    130    -75   -371       C  
ATOM   2758  C   ASP B  95      -0.026  -8.952 -16.714  1.00 25.67           C  
ANISOU 2758  C   ASP B  95     3191   3464   3098    102    -67   -392       C  
ATOM   2759  O   ASP B  95      -0.652  -8.114 -16.054  1.00 25.14           O  
ANISOU 2759  O   ASP B  95     3124   3408   3019     84    -53   -420       O  
ATOM   2760  CB  ASP B  95      -1.262  -8.904 -18.912  1.00 28.95           C  
ANISOU 2760  CB  ASP B  95     3643   3780   3576    138    -66   -399       C  
ATOM   2761  CG  ASP B  95      -0.150  -8.229 -19.703  1.00 35.83           C  
ANISOU 2761  CG  ASP B  95     4521   4642   4451    137    -65   -415       C  
ATOM   2762  OD1 ASP B  95       0.610  -7.414 -19.132  1.00 35.28           O  
ANISOU 2762  OD1 ASP B  95     4444   4602   4358    116    -59   -435       O  
ATOM   2763  OD2 ASP B  95      -0.040  -8.523 -20.910  1.00 41.09           O  
ANISOU 2763  OD2 ASP B  95     5199   5271   5142    155    -72   -407       O  
ATOM   2764  N   SER B  96       1.279  -9.179 -16.544  1.00 25.01           N  
ANISOU 2764  N   SER B  96     3094   3411   2997     97    -76   -379       N  
ATOM   2765  CA  SER B  96       2.012  -8.506 -15.479  1.00 24.77           C  
ANISOU 2765  CA  SER B  96     3046   3436   2928     68    -71   -396       C  
ATOM   2766  C   SER B  96       1.916  -6.992 -15.612  1.00 24.37           C  
ANISOU 2766  C   SER B  96     3009   3373   2876     49    -52   -446       C  
ATOM   2767  O   SER B  96       1.765  -6.290 -14.601  1.00 22.92           O  
ANISOU 2767  O   SER B  96     2817   3224   2667     22    -39   -471       O  
ATOM   2768  CB  SER B  96       3.471  -8.963 -15.464  1.00 26.05           C  
ANISOU 2768  CB  SER B  96     3193   3631   3076     69    -84   -374       C  
ATOM   2769  OG  SER B  96       4.061  -8.847 -16.752  1.00 26.55           O  
ANISOU 2769  OG  SER B  96     3271   3655   3164     85    -88   -378       O  
ATOM   2770  N   PHE B  97       1.975  -6.463 -16.847  1.00 22.56           N  
ANISOU 2770  N   PHE B  97     2800   3095   2676     62    -49   -461       N  
ATOM   2771  CA  PHE B  97       1.928  -5.010 -17.002  1.00 23.97           C  
ANISOU 2771  CA  PHE B  97     2992   3260   2858     45    -29   -506       C  
ATOM   2772  C   PHE B  97       0.606  -4.453 -16.494  1.00 22.78           C  
ANISOU 2772  C   PHE B  97     2847   3097   2711     38    -12   -529       C  
ATOM   2773  O   PHE B  97       0.572  -3.461 -15.754  1.00 21.30           O  
ANISOU 2773  O   PHE B  97     2657   2929   2507     12      5   -564       O  
ATOM   2774  CB  PHE B  97       2.111  -4.567 -18.456  1.00 23.49           C  
ANISOU 2774  CB  PHE B  97     2951   3145   2828     61    -29   -515       C  
ATOM   2775  CG  PHE B  97       2.365  -3.091 -18.562  1.00 26.16           C  
ANISOU 2775  CG  PHE B  97     3300   3474   3166     41     -9   -557       C  
ATOM   2776  CD1 PHE B  97       3.659  -2.590 -18.392  1.00 25.17           C  
ANISOU 2776  CD1 PHE B  97     3167   3378   3020     21     -8   -571       C  
ATOM   2777  CD2 PHE B  97       1.318  -2.194 -18.735  1.00 26.89           C  
ANISOU 2777  CD2 PHE B  97     3408   3531   3279     41      9   -584       C  
ATOM   2778  CE1 PHE B  97       3.906  -1.232 -18.437  1.00 25.38           C  
ANISOU 2778  CE1 PHE B  97     3204   3395   3046     -1     11   -611       C  
ATOM   2779  CE2 PHE B  97       1.564  -0.828 -18.781  1.00 28.15           C  
ANISOU 2779  CE2 PHE B  97     3577   3680   3441     22     29   -623       C  
ATOM   2780  CZ  PHE B  97       2.854  -0.351 -18.633  1.00 24.10           C  
ANISOU 2780  CZ  PHE B  97     3057   3193   2907      0     31   -637       C  
ATOM   2781  N   ASP B  98      -0.498  -5.048 -16.949  1.00 23.40           N  
ANISOU 2781  N   ASP B  98     2934   3142   2815     60    -16   -512       N  
ATOM   2782  CA  ASP B  98      -1.825  -4.661 -16.470  1.00 25.65           C  
ANISOU 2782  CA  ASP B  98     3222   3418   3106     57     -2   -528       C  
ATOM   2783  C   ASP B  98      -1.961  -4.834 -14.963  1.00 24.53           C  
ANISOU 2783  C   ASP B  98     3061   3332   2929     34      2   -530       C  
ATOM   2784  O   ASP B  98      -2.680  -4.064 -14.308  1.00 22.48           O  
ANISOU 2784  O   ASP B  98     2801   3078   2663     18     21   -560       O  
ATOM   2785  CB  ASP B  98      -2.887  -5.493 -17.192  1.00 29.72           C  
ANISOU 2785  CB  ASP B  98     3746   3895   3650     85    -10   -503       C  
ATOM   2786  CG  ASP B  98      -3.063  -5.071 -18.642  1.00 31.27           C  
ANISOU 2786  CG  ASP B  98     3963   4037   3882    104     -9   -509       C  
ATOM   2787  OD1 ASP B  98      -2.858  -3.874 -18.925  1.00 29.95           O  
ANISOU 2787  OD1 ASP B  98     3805   3854   3720     96      5   -540       O  
ATOM   2788  OD2 ASP B  98      -3.389  -5.923 -19.490  1.00 34.00           O  
ANISOU 2788  OD2 ASP B  98     4315   4356   4248    127    -22   -483       O  
ATOM   2789  N   ILE B  99      -1.306  -5.843 -14.393  1.00 23.31           N  
ANISOU 2789  N   ILE B  99     2888   3219   2751     32    -14   -497       N  
ATOM   2790  CA  ILE B  99      -1.364  -6.010 -12.944  1.00 23.09           C  
ANISOU 2790  CA  ILE B  99     2839   3249   2685      8    -11   -496       C  
ATOM   2791  C   ILE B  99      -0.692  -4.824 -12.255  1.00 23.83           C  
ANISOU 2791  C   ILE B  99     2926   3377   2750    -26      5   -537       C  
ATOM   2792  O   ILE B  99      -1.256  -4.206 -11.343  1.00 23.66           O  
ANISOU 2792  O   ILE B  99     2899   3379   2712    -48     22   -566       O  
ATOM   2793  CB  ILE B  99      -0.742  -7.360 -12.529  1.00 24.12           C  
ANISOU 2793  CB  ILE B  99     2950   3416   2797     14    -33   -448       C  
ATOM   2794  CG1 ILE B  99      -1.674  -8.523 -12.906  1.00 22.56           C  
ANISOU 2794  CG1 ILE B  99     2758   3189   2625     41    -44   -412       C  
ATOM   2795  CG2 ILE B  99      -0.460  -7.413 -11.036  1.00 21.11           C  
ANISOU 2795  CG2 ILE B  99     2544   3106   2371    -15    -32   -446       C  
ATOM   2796  CD1 ILE B  99      -1.049  -9.927 -12.632  1.00 24.04           C  
ANISOU 2796  CD1 ILE B  99     2928   3403   2803     52    -65   -360       C  
ATOM   2797  N   ALA B 100       0.510  -4.461 -12.705  1.00 24.56           N  
ANISOU 2797  N   ALA B 100     3020   3473   2839    -31      1   -544       N  
ATOM   2798  CA  ALA B 100       1.205  -3.320 -12.106  1.00 23.86           C  
ANISOU 2798  CA  ALA B 100     2926   3417   2724    -65     17   -585       C  
ATOM   2799  C   ALA B 100       0.388  -2.036 -12.266  1.00 23.63           C  
ANISOU 2799  C   ALA B 100     2914   3349   2714    -74     44   -633       C  
ATOM   2800  O   ALA B 100       0.226  -1.257 -11.313  1.00 23.78           O  
ANISOU 2800  O   ALA B 100     2927   3398   2711   -104     64   -668       O  
ATOM   2801  CB  ALA B 100       2.597  -3.184 -12.733  1.00 23.64           C  
ANISOU 2801  CB  ALA B 100     2898   3392   2694    -66      8   -582       C  
ATOM   2802  N   ALA B 101      -0.164  -1.817 -13.463  1.00 22.64           N  
ANISOU 2802  N   ALA B 101     2811   3159   2631    -47     47   -634       N  
ATOM   2803  CA  ALA B 101      -1.044  -0.669 -13.690  1.00 25.74           C  
ANISOU 2803  CA  ALA B 101     3222   3511   3049    -49     72   -673       C  
ATOM   2804  C   ALA B 101      -2.232  -0.679 -12.728  1.00 23.22           C  
ANISOU 2804  C   ALA B 101     2895   3207   2721    -57     85   -683       C  
ATOM   2805  O   ALA B 101      -2.591   0.359 -12.153  1.00 26.63           O  
ANISOU 2805  O   ALA B 101     3328   3641   3149    -78    111   -725       O  
ATOM   2806  CB  ALA B 101      -1.532  -0.664 -15.146  1.00 26.67           C  
ANISOU 2806  CB  ALA B 101     3361   3562   3211    -16     68   -661       C  
ATOM   2807  N   TYR B 102      -2.851  -1.839 -12.537  1.00 23.87           N  
ANISOU 2807  N   TYR B 102     2969   3299   2802    -41     69   -646       N  
ATOM   2808  CA  TYR B 102      -3.992  -1.907 -11.631  1.00 26.06           C  
ANISOU 2808  CA  TYR B 102     3238   3593   3071    -48     80   -654       C  
ATOM   2809  C   TYR B 102      -3.573  -1.563 -10.209  1.00 24.27           C  
ANISOU 2809  C   TYR B 102     2992   3431   2799    -87     91   -677       C  
ATOM   2810  O   TYR B 102      -4.281  -0.828  -9.508  1.00 23.55           O  
ANISOU 2810  O   TYR B 102     2899   3347   2702   -104    115   -713       O  
ATOM   2811  CB  TYR B 102      -4.638  -3.294 -11.680  1.00 24.57           C  
ANISOU 2811  CB  TYR B 102     3043   3405   2886    -26     59   -607       C  
ATOM   2812  CG  TYR B 102      -5.610  -3.530 -10.531  1.00 23.90           C  
ANISOU 2812  CG  TYR B 102     2944   3353   2782    -39     68   -610       C  
ATOM   2813  CD1 TYR B 102      -6.949  -3.175 -10.644  1.00 27.74           C  
ANISOU 2813  CD1 TYR B 102     3440   3809   3293    -29     83   -626       C  
ATOM   2814  CD2 TYR B 102      -5.186  -4.116  -9.343  1.00 23.32           C  
ANISOU 2814  CD2 TYR B 102     2849   3346   2667    -61     60   -595       C  
ATOM   2815  CE1 TYR B 102      -7.844  -3.390  -9.583  1.00 28.79           C  
ANISOU 2815  CE1 TYR B 102     3558   3973   3407    -41     91   -629       C  
ATOM   2816  CE2 TYR B 102      -6.060  -4.330  -8.288  1.00 25.28           C  
ANISOU 2816  CE2 TYR B 102     3083   3627   2895    -74     68   -597       C  
ATOM   2817  CZ  TYR B 102      -7.381  -3.968  -8.413  1.00 25.15           C  
ANISOU 2817  CZ  TYR B 102     3076   3578   2903    -65     84   -615       C  
ATOM   2818  OH  TYR B 102      -8.231  -4.191  -7.350  1.00 30.32           O  
ANISOU 2818  OH  TYR B 102     3716   4268   3536    -79     92   -618       O  
ATOM   2819  N   LEU B 103      -2.415  -2.070  -9.767  1.00 24.71           N  
ANISOU 2819  N   LEU B 103     3032   3537   2822   -101     75   -658       N  
ATOM   2820  CA  LEU B 103      -1.971  -1.794  -8.403  1.00 23.90           C  
ANISOU 2820  CA  LEU B 103     2907   3503   2671   -140     84   -678       C  
ATOM   2821  C   LEU B 103      -1.722  -0.306  -8.200  1.00 25.61           C  
ANISOU 2821  C   LEU B 103     3130   3716   2884   -169    113   -737       C  
ATOM   2822  O   LEU B 103      -2.113   0.260  -7.174  1.00 28.40           O  
ANISOU 2822  O   LEU B 103     3475   4103   3215   -198    134   -771       O  
ATOM   2823  CB  LEU B 103      -0.719  -2.606  -8.070  1.00 24.40           C  
ANISOU 2823  CB  LEU B 103     2950   3620   2701   -148     60   -643       C  
ATOM   2824  CG  LEU B 103      -0.879  -4.126  -8.025  1.00 23.41           C  
ANISOU 2824  CG  LEU B 103     2813   3507   2574   -125     34   -583       C  
ATOM   2825  CD1 LEU B 103       0.461  -4.819  -7.978  1.00 25.33           C  
ANISOU 2825  CD1 LEU B 103     3039   3789   2795   -125     11   -548       C  
ATOM   2826  CD2 LEU B 103      -1.728  -4.556  -6.850  1.00 26.64           C  
ANISOU 2826  CD2 LEU B 103     3205   3958   2958   -138     37   -575       C  
ATOM   2827  N   GLN B 104      -1.096   0.355  -9.172  1.00 26.36           N  
ANISOU 2827  N   GLN B 104     3243   3771   3003   -162    116   -752       N  
ATOM   2828  CA  GLN B 104      -0.866   1.792  -9.038  1.00 28.05           C  
ANISOU 2828  CA  GLN B 104     3464   3975   3217   -189    146   -808       C  
ATOM   2829  C   GLN B 104      -2.178   2.564  -9.006  1.00 28.45           C  
ANISOU 2829  C   GLN B 104     3530   3985   3297   -185    174   -842       C  
ATOM   2830  O   GLN B 104      -2.348   3.475  -8.191  1.00 28.68           O  
ANISOU 2830  O   GLN B 104     3554   4031   3311   -215    202   -888       O  
ATOM   2831  CB  GLN B 104       0.019   2.306 -10.171  1.00 29.70           C  
ANISOU 2831  CB  GLN B 104     3691   4145   3450   -180    144   -813       C  
ATOM   2832  CG  GLN B 104       0.426   3.788 -10.017  1.00 29.72           C  
ANISOU 2832  CG  GLN B 104     3702   4139   3452   -212    175   -871       C  
ATOM   2833  CD  GLN B 104       0.962   4.133  -8.633  1.00 29.53           C  
ANISOU 2833  CD  GLN B 104     3656   4187   3377   -259    187   -902       C  
ATOM   2834  OE1 GLN B 104       1.649   3.331  -7.997  1.00 26.44           O  
ANISOU 2834  OE1 GLN B 104     3242   3859   2945   -272    167   -876       O  
ATOM   2835  NE2 GLN B 104       0.665   5.346  -8.170  1.00 29.89           N  
ANISOU 2835  NE2 GLN B 104     3708   4224   3424   -287    222   -958       N  
ATOM   2836  N   ARG B 105      -3.124   2.207  -9.877  1.00 28.72           N  
ANISOU 2836  N   ARG B 105     3578   3965   3371   -147    168   -819       N  
ATOM   2837  CA  ARG B 105      -4.396   2.917  -9.920  1.00 31.39           C  
ANISOU 2837  CA  ARG B 105     3926   4261   3739   -138    193   -846       C  
ATOM   2838  C   ARG B 105      -5.188   2.728  -8.630  1.00 27.04           C  
ANISOU 2838  C   ARG B 105     3358   3754   3161   -157    204   -858       C  
ATOM   2839  O   ARG B 105      -5.813   3.670  -8.140  1.00 28.10           O  
ANISOU 2839  O   ARG B 105     3495   3881   3301   -172    235   -902       O  
ATOM   2840  CB  ARG B 105      -5.215   2.449 -11.130  1.00 33.65           C  
ANISOU 2840  CB  ARG B 105     4228   4487   4069    -94    180   -814       C  
ATOM   2841  CG  ARG B 105      -6.182   3.491 -11.673  1.00 41.45           C  
ANISOU 2841  CG  ARG B 105     5232   5416   5099    -80    207   -842       C  
ATOM   2842  CD  ARG B 105      -6.676   3.176 -13.104  1.00 45.50           C  
ANISOU 2842  CD  ARG B 105     5761   5870   5655    -39    192   -810       C  
ATOM   2843  NE  ARG B 105      -6.579   1.769 -13.489  1.00 47.24           N  
ANISOU 2843  NE  ARG B 105     5977   6102   5870    -20    159   -759       N  
ATOM   2844  CZ  ARG B 105      -5.710   1.278 -14.369  1.00 47.37           C  
ANISOU 2844  CZ  ARG B 105     5999   6109   5891     -7    136   -733       C  
ATOM   2845  NH1 ARG B 105      -4.796   2.046 -14.949  1.00 47.84           N  
ANISOU 2845  NH1 ARG B 105     6069   6150   5957    -13    142   -749       N  
ATOM   2846  NH2 ARG B 105      -5.757  -0.019 -14.673  1.00 40.43           N  
ANISOU 2846  NH2 ARG B 105     5115   5237   5009     11    109   -689       N  
ATOM   2847  N   THR B 106      -5.155   1.530  -8.054  1.00 27.19           N  
ANISOU 2847  N   THR B 106     3359   3821   3151   -158    181   -820       N  
ATOM   2848  CA  THR B 106      -6.025   1.174  -6.936  1.00 28.75           C  
ANISOU 2848  CA  THR B 106     3540   4058   3324   -171    187   -822       C  
ATOM   2849  C   THR B 106      -5.396   1.484  -5.583  1.00 28.45           C  
ANISOU 2849  C   THR B 106     3481   4094   3235   -217    198   -850       C  
ATOM   2850  O   THR B 106      -6.095   1.884  -4.644  1.00 27.69           O  
ANISOU 2850  O   THR B 106     3376   4022   3123   -238    221   -881       O  
ATOM   2851  CB  THR B 106      -6.372  -0.315  -7.017  1.00 27.55           C  
ANISOU 2851  CB  THR B 106     3380   3919   3169   -147    157   -764       C  
ATOM   2852  OG1 THR B 106      -6.876  -0.602  -8.328  1.00 29.50           O  
ANISOU 2852  OG1 THR B 106     3645   4100   3462   -107    146   -740       O  
ATOM   2853  CG2 THR B 106      -7.401  -0.717  -5.957  1.00 29.20           C  
ANISOU 2853  CG2 THR B 106     3574   4164   3359   -158    164   -763       C  
ATOM   2854  N   TYR B 107      -4.090   1.295  -5.461  1.00 28.31           N  
ANISOU 2854  N   TYR B 107     3455   4114   3188   -233    184   -840       N  
ATOM   2855  CA  TYR B 107      -3.365   1.571  -4.223  1.00 27.68           C  
ANISOU 2855  CA  TYR B 107     3353   4110   3055   -280    192   -864       C  
ATOM   2856  C   TYR B 107      -2.203   2.511  -4.522  1.00 29.49           C  
ANISOU 2856  C   TYR B 107     3588   4336   3280   -300    202   -897       C  
ATOM   2857  O   TYR B 107      -1.040   2.176  -4.299  1.00 27.62           O  
ANISOU 2857  O   TYR B 107     3338   4147   3012   -316    185   -880       O  
ATOM   2858  CB  TYR B 107      -2.888   0.266  -3.593  1.00 27.99           C  
ANISOU 2858  CB  TYR B 107     3367   4213   3054   -283    161   -812       C  
ATOM   2859  CG  TYR B 107      -3.983  -0.771  -3.496  1.00 29.51           C  
ANISOU 2859  CG  TYR B 107     3556   4400   3257   -258    148   -772       C  
ATOM   2860  CD1 TYR B 107      -4.932  -0.706  -2.479  1.00 29.56           C  
ANISOU 2860  CD1 TYR B 107     3550   4437   3243   -276    164   -789       C  
ATOM   2861  CD2 TYR B 107      -4.069  -1.812  -4.406  1.00 26.16           C  
ANISOU 2861  CD2 TYR B 107     3139   3939   2860   -218    121   -719       C  
ATOM   2862  CE1 TYR B 107      -5.921  -1.639  -2.371  1.00 30.01           C  
ANISOU 2862  CE1 TYR B 107     3604   4491   3308   -255    153   -754       C  
ATOM   2863  CE2 TYR B 107      -5.063  -2.763  -4.306  1.00 29.41           C  
ANISOU 2863  CE2 TYR B 107     3548   4346   3281   -197    111   -684       C  
ATOM   2864  CZ  TYR B 107      -5.993  -2.671  -3.290  1.00 31.27           C  
ANISOU 2864  CZ  TYR B 107     3772   4613   3497   -216    126   -701       C  
ATOM   2865  OH  TYR B 107      -7.004  -3.605  -3.180  1.00 28.90           O  
ANISOU 2865  OH  TYR B 107     3468   4308   3204   -198    116   -666       O  
ATOM   2866  N   PRO B 108      -2.497   3.721  -5.005  1.00 30.01           N  
ANISOU 2866  N   PRO B 108     3675   4348   3379   -302    231   -943       N  
ATOM   2867  CA  PRO B 108      -1.422   4.597  -5.506  1.00 28.18           C  
ANISOU 2867  CA  PRO B 108     3454   4101   3153   -316    240   -971       C  
ATOM   2868  C   PRO B 108      -0.409   5.001  -4.455  1.00 31.06           C  
ANISOU 2868  C   PRO B 108     3798   4539   3464   -368    248  -1001       C  
ATOM   2869  O   PRO B 108       0.741   5.302  -4.798  1.00 30.32           O  
ANISOU 2869  O   PRO B 108     3706   4453   3363   -380    243  -1006       O  
ATOM   2870  CB  PRO B 108      -2.190   5.819  -6.019  1.00 28.32           C  
ANISOU 2870  CB  PRO B 108     3496   4049   3217   -309    274  -1016       C  
ATOM   2871  CG  PRO B 108      -3.425   5.855  -5.126  1.00 32.60           C  
ANISOU 2871  CG  PRO B 108     4029   4604   3753   -316    293  -1035       C  
ATOM   2872  CD  PRO B 108      -3.801   4.407  -4.956  1.00 28.22           C  
ANISOU 2872  CD  PRO B 108     3460   4078   3183   -295    260   -977       C  
ATOM   2873  N   ALA B 109      -0.800   5.038  -3.183  1.00 27.06           N  
ANISOU 2873  N   ALA B 109     3273   4090   2920   -399    261  -1023       N  
ATOM   2874  CA  ALA B 109       0.090   5.495  -2.122  1.00 31.28           C  
ANISOU 2874  CA  ALA B 109     3787   4698   3401   -453    272  -1057       C  
ATOM   2875  C   ALA B 109       0.522   4.375  -1.182  1.00 31.09           C  
ANISOU 2875  C   ALA B 109     3730   4762   3321   -468    245  -1016       C  
ATOM   2876  O   ALA B 109       1.173   4.658  -0.175  1.00 34.13           O  
ANISOU 2876  O   ALA B 109     4093   5220   3655   -514    252  -1041       O  
ATOM   2877  CB  ALA B 109      -0.573   6.623  -1.311  1.00 30.33           C  
ANISOU 2877  CB  ALA B 109     3667   4580   3276   -488    316  -1126       C  
ATOM   2878  N   SER B 110       0.201   3.118  -1.483  1.00 28.13           N  
ANISOU 2878  N   SER B 110     3350   4383   2954   -431    213   -953       N  
ATOM   2879  CA  SER B 110       0.502   2.046  -0.541  1.00 32.19           C  
ANISOU 2879  CA  SER B 110     3833   4980   3419   -443    189   -911       C  
ATOM   2880  C   SER B 110       1.970   1.639  -0.627  1.00 30.07           C  
ANISOU 2880  C   SER B 110     3548   4755   3121   -452    164   -881       C  
ATOM   2881  O   SER B 110       2.619   1.799  -1.661  1.00 25.31           O  
ANISOU 2881  O   SER B 110     2961   4108   2546   -432    156   -875       O  
ATOM   2882  CB  SER B 110      -0.392   0.833  -0.798  1.00 30.38           C  
ANISOU 2882  CB  SER B 110     3605   4729   3210   -402    167   -854       C  
ATOM   2883  OG  SER B 110      -1.758   1.167  -0.604  1.00 30.79           O  
ANISOU 2883  OG  SER B 110     3667   4750   3283   -397    189   -880       O  
ATOM   2884  N   GLY B 111       2.495   1.124   0.482  1.00 32.04           N  
ANISOU 2884  N   GLY B 111     3764   5095   3313   -482    152   -863       N  
ATOM   2885  CA  GLY B 111       3.846   0.572   0.465  1.00 30.49           C  
ANISOU 2885  CA  GLY B 111     3548   4948   3088   -486    125   -826       C  
ATOM   2886  C   GLY B 111       4.916   1.603   0.150  1.00 30.91           C  
ANISOU 2886  C   GLY B 111     3607   5002   3136   -513    138   -869       C  
ATOM   2887  O   GLY B 111       4.961   2.696   0.729  1.00 30.74           O  
ANISOU 2887  O   GLY B 111     3585   5001   3094   -556    167   -931       O  
ATOM   2888  N   ALA B 112       5.810   1.244  -0.770  1.00 27.12           N  
ANISOU 2888  N   ALA B 112     3131   4499   2673   -488    116   -836       N  
ATOM   2889  CA  ALA B 112       6.943   2.086  -1.117  1.00 31.56           C  
ANISOU 2889  CA  ALA B 112     3696   5067   3229   -511    124   -868       C  
ATOM   2890  C   ALA B 112       6.571   3.267  -2.006  1.00 31.74           C  
ANISOU 2890  C   ALA B 112     3756   5005   3300   -506    153   -921       C  
ATOM   2891  O   ALA B 112       7.453   4.074  -2.334  1.00 31.02           O  
ANISOU 2891  O   ALA B 112     3669   4910   3206   -527    163   -953       O  
ATOM   2892  CB  ALA B 112       8.016   1.240  -1.804  1.00 32.94           C  
ANISOU 2892  CB  ALA B 112     3861   5247   3406   -484     91   -813       C  
ATOM   2893  N   GLY B 113       5.306   3.389  -2.416  1.00 31.89           N  
ANISOU 2893  N   GLY B 113     3798   4955   3362   -479    166   -930       N  
ATOM   2894  CA  GLY B 113       4.902   4.533  -3.219  1.00 30.66           C  
ANISOU 2894  CA  GLY B 113     3675   4721   3253   -473    194   -977       C  
ATOM   2895  C   GLY B 113       4.541   4.245  -4.669  1.00 29.77           C  
ANISOU 2895  C   GLY B 113     3590   4521   3200   -420    182   -947       C  
ATOM   2896  O   GLY B 113       3.929   3.219  -4.986  1.00 27.01           O  
ANISOU 2896  O   GLY B 113     3242   4153   2869   -382    161   -899       O  
ATOM   2897  N   ASP B 114       4.937   5.163  -5.551  1.00 30.91           N  
ANISOU 2897  N   ASP B 114     3758   4613   3376   -419    197   -976       N  
ATOM   2898  CA  ASP B 114       4.484   5.182  -6.934  1.00 29.49           C  
ANISOU 2898  CA  ASP B 114     3606   4345   3254   -374    193   -960       C  
ATOM   2899  C   ASP B 114       5.296   4.205  -7.785  1.00 30.68           C  
ANISOU 2899  C   ASP B 114     3754   4494   3410   -343    158   -905       C  
ATOM   2900  O   ASP B 114       6.525   4.308  -7.867  1.00 27.66           O  
ANISOU 2900  O   ASP B 114     3362   4143   3007   -360    150   -904       O  
ATOM   2901  CB  ASP B 114       4.605   6.607  -7.468  1.00 30.75           C  
ANISOU 2901  CB  ASP B 114     3789   4453   3442   -388    225  -1013       C  
ATOM   2902  CG  ASP B 114       4.002   6.786  -8.854  1.00 32.94           C  
ANISOU 2902  CG  ASP B 114     4097   4640   3780   -344    225  -1001       C  
ATOM   2903  OD1 ASP B 114       3.462   5.815  -9.429  1.00 29.92           O  
ANISOU 2903  OD1 ASP B 114     3717   4233   3417   -303    202   -954       O  
ATOM   2904  OD2 ASP B 114       4.087   7.920  -9.377  1.00 34.16           O  
ANISOU 2904  OD2 ASP B 114     4270   4746   3961   -352    250  -1038       O  
ATOM   2905  N   LEU B 115       4.610   3.252  -8.418  1.00 28.27           N  
ANISOU 2905  N   LEU B 115     3456   4153   3133   -299    138   -859       N  
ATOM   2906  CA  LEU B 115       5.288   2.351  -9.331  1.00 26.57           C  
ANISOU 2906  CA  LEU B 115     3240   3925   2930   -268    108   -810       C  
ATOM   2907  C   LEU B 115       5.623   3.012 -10.664  1.00 27.58           C  
ANISOU 2907  C   LEU B 115     3393   3988   3098   -252    114   -822       C  
ATOM   2908  O   LEU B 115       6.553   2.561 -11.346  1.00 30.54           O  
ANISOU 2908  O   LEU B 115     3766   4364   3474   -238     94   -795       O  
ATOM   2909  CB  LEU B 115       4.435   1.106  -9.584  1.00 28.39           C  
ANISOU 2909  CB  LEU B 115     3471   4138   3180   -228     87   -760       C  
ATOM   2910  CG  LEU B 115       4.417  -0.001  -8.534  1.00 26.23           C  
ANISOU 2910  CG  LEU B 115     3168   3929   2868   -233     69   -724       C  
ATOM   2911  CD1 LEU B 115       3.188  -0.848  -8.777  1.00 23.51           C  
ANISOU 2911  CD1 LEU B 115     2832   3550   2551   -198     61   -692       C  
ATOM   2912  CD2 LEU B 115       5.689  -0.827  -8.632  1.00 25.78           C  
ANISOU 2912  CD2 LEU B 115     3092   3913   2790   -228     42   -683       C  
ATOM   2913  N   PHE B 116       4.917   4.079 -11.045  1.00 27.33           N  
ANISOU 2913  N   PHE B 116     3385   3901   3098   -253    141   -861       N  
ATOM   2914  CA  PHE B 116       5.025   4.639 -12.397  1.00 26.82           C  
ANISOU 2914  CA  PHE B 116     3346   3767   3076   -232    145   -866       C  
ATOM   2915  C   PHE B 116       5.242   6.155 -12.412  1.00 30.68           C  
ANISOU 2915  C   PHE B 116     3850   4234   3575   -261    178   -922       C  
ATOM   2916  O   PHE B 116       4.512   6.883 -13.090  1.00 29.47           O  
ANISOU 2916  O   PHE B 116     3718   4015   3462   -247    196   -939       O  
ATOM   2917  CB  PHE B 116       3.762   4.300 -13.182  1.00 27.08           C  
ANISOU 2917  CB  PHE B 116     3397   3738   3154   -190    142   -845       C  
ATOM   2918  CG  PHE B 116       3.586   2.837 -13.491  1.00 28.47           C  
ANISOU 2918  CG  PHE B 116     3565   3921   3331   -157    110   -789       C  
ATOM   2919  CD1 PHE B 116       4.280   2.242 -14.543  1.00 28.54           C  
ANISOU 2919  CD1 PHE B 116     3578   3912   3354   -133     88   -756       C  
ATOM   2920  CD2 PHE B 116       2.690   2.067 -12.768  1.00 28.34           C  
ANISOU 2920  CD2 PHE B 116     3537   3925   3305   -150    105   -770       C  
ATOM   2921  CE1 PHE B 116       4.100   0.901 -14.845  1.00 25.68           C  
ANISOU 2921  CE1 PHE B 116     3209   3551   2996   -103     62   -707       C  
ATOM   2922  CE2 PHE B 116       2.501   0.735 -13.072  1.00 28.77           C  
ANISOU 2922  CE2 PHE B 116     3586   3982   3365   -120     78   -720       C  
ATOM   2923  CZ  PHE B 116       3.208   0.152 -14.120  1.00 26.78           C  
ANISOU 2923  CZ  PHE B 116     3338   3709   3127    -96     57   -689       C  
ATOM   2924  N   PRO B 117       6.256   6.674 -11.703  1.00 31.51           N  
ANISOU 2924  N   PRO B 117     3941   4390   3642   -304    187   -951       N  
ATOM   2925  CA  PRO B 117       6.555   8.100 -11.822  1.00 31.86           C  
ANISOU 2925  CA  PRO B 117     4001   4408   3698   -332    219  -1004       C  
ATOM   2926  C   PRO B 117       6.990   8.436 -13.235  1.00 33.14           C  
ANISOU 2926  C   PRO B 117     4183   4510   3896   -310    215   -994       C  
ATOM   2927  O   PRO B 117       7.546   7.583 -13.947  1.00 30.01           O  
ANISOU 2927  O   PRO B 117     3784   4118   3502   -286    186   -951       O  
ATOM   2928  CB  PRO B 117       7.710   8.308 -10.826  1.00 30.83           C  
ANISOU 2928  CB  PRO B 117     3847   4355   3514   -381    221  -1027       C  
ATOM   2929  CG  PRO B 117       8.374   7.008 -10.772  1.00 31.38           C  
ANISOU 2929  CG  PRO B 117     3893   4474   3555   -367    184   -975       C  
ATOM   2930  CD  PRO B 117       7.282   5.978 -10.905  1.00 28.50           C  
ANISOU 2930  CD  PRO B 117     3530   4090   3209   -326    167   -933       C  
ATOM   2931  N   PRO B 118       6.763   9.667 -13.685  1.00 35.15           N  
ANISOU 2931  N   PRO B 118     4460   4711   4183   -318    245  -1032       N  
ATOM   2932  CA  PRO B 118       7.234  10.061 -15.020  1.00 35.15           C  
ANISOU 2932  CA  PRO B 118     4480   4658   4216   -301    242  -1022       C  
ATOM   2933  C   PRO B 118       8.750   9.926 -15.131  1.00 36.60           C  
ANISOU 2933  C   PRO B 118     4652   4885   4369   -323    227  -1017       C  
ATOM   2934  O   PRO B 118       9.498  10.436 -14.293  1.00 31.77           O  
ANISOU 2934  O   PRO B 118     4027   4320   3723   -366    240  -1051       O  
ATOM   2935  CB  PRO B 118       6.780  11.523 -15.131  1.00 36.35           C  
ANISOU 2935  CB  PRO B 118     4654   4756   4401   -317    282  -1071       C  
ATOM   2936  CG  PRO B 118       5.576  11.605 -14.212  1.00 39.09           C  
ANISOU 2936  CG  PRO B 118     4997   5105   4749   -319    301  -1090       C  
ATOM   2937  CD  PRO B 118       5.946  10.715 -13.046  1.00 34.92           C  
ANISOU 2937  CD  PRO B 118     4440   4661   4166   -339    283  -1081       C  
ATOM   2938  N   GLN B 119       9.206   9.214 -16.161  1.00 33.18           N  
ANISOU 2938  N   GLN B 119     4221   4438   3948   -292    200   -975       N  
ATOM   2939  CA  GLN B 119      10.638   9.130 -16.427  1.00 33.02           C  
ANISOU 2939  CA  GLN B 119     4191   4452   3905   -309    186   -970       C  
ATOM   2940  C   GLN B 119      10.866   8.809 -17.896  1.00 36.91           C  
ANISOU 2940  C   GLN B 119     4697   4898   4428   -273    169   -936       C  
ATOM   2941  O   GLN B 119      10.005   8.241 -18.565  1.00 34.84           O  
ANISOU 2941  O   GLN B 119     4446   4596   4196   -234    158   -906       O  
ATOM   2942  CB  GLN B 119      11.331   8.079 -15.558  1.00 34.13           C  
ANISOU 2942  CB  GLN B 119     4299   4674   3996   -319    162   -946       C  
ATOM   2943  CG  GLN B 119      10.887   6.644 -15.796  1.00 31.19           C  
ANISOU 2943  CG  GLN B 119     3918   4305   3629   -277    131   -891       C  
ATOM   2944  CD  GLN B 119      11.630   5.686 -14.892  1.00 33.77           C  
ANISOU 2944  CD  GLN B 119     4212   4712   3908   -288    109   -867       C  
ATOM   2945  OE1 GLN B 119      12.861   5.746 -14.791  1.00 35.89           O  
ANISOU 2945  OE1 GLN B 119     4464   5022   4148   -309    102   -868       O  
ATOM   2946  NE2 GLN B 119      10.898   4.813 -14.215  1.00 30.41           N  
ANISOU 2946  NE2 GLN B 119     3774   4308   3472   -274     98   -843       N  
ATOM   2947  N   LYS B 120      12.044   9.168 -18.385  1.00 36.39           N  
ANISOU 2947  N   LYS B 120     4631   4841   4355   -289    167   -942       N  
ATOM   2948  CA  LYS B 120      12.407   8.926 -19.778  1.00 40.20           C  
ANISOU 2948  CA  LYS B 120     5126   5285   4864   -261    152   -914       C  
ATOM   2949  C   LYS B 120      13.009   7.526 -19.868  1.00 35.05           C  
ANISOU 2949  C   LYS B 120     4452   4675   4189   -240    117   -869       C  
ATOM   2950  O   LYS B 120      14.049   7.252 -19.260  1.00 35.75           O  
ANISOU 2950  O   LYS B 120     4518   4826   4241   -262    108   -868       O  
ATOM   2951  CB  LYS B 120      13.372  10.008 -20.263  1.00 39.96           C  
ANISOU 2951  CB  LYS B 120     5105   5242   4835   -289    168   -942       C  
ATOM   2952  CG  LYS B 120      14.090   9.714 -21.564  1.00 43.35           C  
ANISOU 2952  CG  LYS B 120     5540   5651   5279   -268    150   -914       C  
ATOM   2953  CD  LYS B 120      15.430  10.455 -21.630  1.00 43.84           C  
ANISOU 2953  CD  LYS B 120     5599   5738   5322   -305    159   -939       C  
ATOM   2954  CE  LYS B 120      15.478  11.447 -22.794  1.00 48.52           C  
ANISOU 2954  CE  LYS B 120     6218   6268   5951   -304    175   -951       C  
ATOM   2955  NZ  LYS B 120      16.611  12.424 -22.672  1.00 50.11           N  
ANISOU 2955  NZ  LYS B 120     6418   6487   6135   -348    192   -985       N  
ATOM   2956  N   LEU B 121      12.335   6.626 -20.581  1.00 28.39           N  
ANISOU 2956  N   LEU B 121     3615   3801   3371   -197     99   -830       N  
ATOM   2957  CA  LEU B 121      12.829   5.268 -20.788  1.00 30.64           C  
ANISOU 2957  CA  LEU B 121     3882   4116   3644   -173     68   -787       C  
ATOM   2958  C   LEU B 121      13.259   5.122 -22.247  1.00 33.09           C  
ANISOU 2958  C   LEU B 121     4205   4388   3980   -150     57   -767       C  
ATOM   2959  O   LEU B 121      12.589   4.480 -23.063  1.00 31.42           O  
ANISOU 2959  O   LEU B 121     4004   4139   3796   -114     46   -740       O  
ATOM   2960  CB  LEU B 121      11.757   4.238 -20.391  1.00 30.70           C  
ANISOU 2960  CB  LEU B 121     3885   4124   3657   -146     56   -759       C  
ATOM   2961  CG  LEU B 121      11.284   4.348 -18.932  1.00 32.29           C  
ANISOU 2961  CG  LEU B 121     4072   4366   3831   -170     67   -777       C  
ATOM   2962  CD1 LEU B 121       9.977   3.632 -18.751  1.00 31.27           C  
ANISOU 2962  CD1 LEU B 121     3947   4218   3718   -143     61   -756       C  
ATOM   2963  CD2 LEU B 121      12.311   3.801 -17.964  1.00 29.93           C  
ANISOU 2963  CD2 LEU B 121     3742   4144   3485   -191     54   -767       C  
ATOM   2964  N   ASP B 122      14.389   5.758 -22.579  1.00 27.80           N  
ANISOU 2964  N   ASP B 122     3534   3729   3299   -172     62   -783       N  
ATOM   2965  CA  ASP B 122      14.873   5.835 -23.960  1.00 33.14           C  
ANISOU 2965  CA  ASP B 122     4224   4371   3999   -156     56   -772       C  
ATOM   2966  C   ASP B 122      15.728   4.611 -24.279  1.00 30.87           C  
ANISOU 2966  C   ASP B 122     3916   4116   3697   -137     29   -735       C  
ATOM   2967  O   ASP B 122      16.936   4.691 -24.525  1.00 31.73           O  
ANISOU 2967  O   ASP B 122     4014   4252   3789   -150     24   -737       O  
ATOM   2968  CB  ASP B 122      15.641   7.129 -24.195  1.00 33.76           C  
ANISOU 2968  CB  ASP B 122     4311   4441   4074   -190     76   -807       C  
ATOM   2969  CG  ASP B 122      16.741   7.345 -23.181  1.00 37.81           C  
ANISOU 2969  CG  ASP B 122     4801   5020   4544   -229     79   -827       C  
ATOM   2970  OD1 ASP B 122      16.554   6.931 -22.019  1.00 35.51           O  
ANISOU 2970  OD1 ASP B 122     4492   4774   4228   -238     76   -827       O  
ATOM   2971  OD2 ASP B 122      17.794   7.924 -23.541  1.00 45.35           O  
ANISOU 2971  OD2 ASP B 122     5755   5986   5490   -251     83   -841       O  
ATOM   2972  N   TYR B 123      15.068   3.458 -24.261  1.00 29.64           N  
ANISOU 2972  N   TYR B 123     3755   3958   3550   -105     13   -703       N  
ATOM   2973  CA  TYR B 123      15.661   2.191 -24.659  1.00 30.90           C  
ANISOU 2973  CA  TYR B 123     3899   4137   3705    -80    -11   -665       C  
ATOM   2974  C   TYR B 123      15.049   1.755 -25.985  1.00 31.18           C  
ANISOU 2974  C   TYR B 123     3954   4117   3778    -45    -18   -645       C  
ATOM   2975  O   TYR B 123      13.818   1.697 -26.123  1.00 27.91           O  
ANISOU 2975  O   TYR B 123     3553   3664   3385    -29    -15   -642       O  
ATOM   2976  CB  TYR B 123      15.453   1.110 -23.591  1.00 28.98           C  
ANISOU 2976  CB  TYR B 123     3633   3936   3442    -72    -25   -641       C  
ATOM   2977  CG  TYR B 123      15.907  -0.253 -24.045  1.00 29.43           C  
ANISOU 2977  CG  TYR B 123     3675   4003   3503    -41    -47   -600       C  
ATOM   2978  CD1 TYR B 123      17.239  -0.490 -24.370  1.00 33.09           C  
ANISOU 2978  CD1 TYR B 123     4123   4496   3953    -44    -56   -591       C  
ATOM   2979  CD2 TYR B 123      15.007  -1.305 -24.161  1.00 30.96           C  
ANISOU 2979  CD2 TYR B 123     3872   4176   3715     -9    -57   -571       C  
ATOM   2980  CE1 TYR B 123      17.661  -1.741 -24.791  1.00 32.43           C  
ANISOU 2980  CE1 TYR B 123     4026   4420   3877    -14    -74   -554       C  
ATOM   2981  CE2 TYR B 123      15.416  -2.564 -24.580  1.00 29.72           C  
ANISOU 2981  CE2 TYR B 123     3703   4025   3565     19    -75   -535       C  
ATOM   2982  CZ  TYR B 123      16.742  -2.778 -24.896  1.00 32.36           C  
ANISOU 2982  CZ  TYR B 123     4021   4386   3887     17    -83   -526       C  
ATOM   2983  OH  TYR B 123      17.139  -4.032 -25.332  1.00 32.28           O  
ANISOU 2983  OH  TYR B 123     3999   4379   3888     47    -98   -491       O  
ATOM   2984  N   ALA B 124      15.915   1.474 -26.964  1.00 27.35           N  
ANISOU 2984  N   ALA B 124     3466   3627   3297    -35    -28   -633       N  
ATOM   2985  CA  ALA B 124      15.518   0.924 -28.260  1.00 27.56           C  
ANISOU 2985  CA  ALA B 124     3507   3610   3355     -4    -36   -613       C  
ATOM   2986  C   ALA B 124      14.483   1.792 -28.976  1.00 25.34           C  
ANISOU 2986  C   ALA B 124     3254   3273   3103     -1    -23   -627       C  
ATOM   2987  O   ALA B 124      13.615   1.280 -29.693  1.00 27.49           O  
ANISOU 2987  O   ALA B 124     3537   3510   3399     25    -28   -610       O  
ATOM   2988  CB  ALA B 124      15.000  -0.507 -28.112  1.00 29.57           C  
ANISOU 2988  CB  ALA B 124     3752   3869   3615     26    -53   -580       C  
ATOM   2989  N   VAL B 125      14.580   3.108 -28.809  1.00 26.90           N  
ANISOU 2989  N   VAL B 125     3461   3461   3297    -28     -4   -658       N  
ATOM   2990  CA  VAL B 125      13.657   4.024 -29.472  1.00 29.19           C  
ANISOU 2990  CA  VAL B 125     3777   3698   3617    -25     11   -670       C  
ATOM   2991  C   VAL B 125      13.777   3.847 -30.977  1.00 27.24           C  
ANISOU 2991  C   VAL B 125     3541   3418   3391     -6      3   -654       C  
ATOM   2992  O   VAL B 125      14.869   3.967 -31.544  1.00 26.64           O  
ANISOU 2992  O   VAL B 125     3461   3355   3308    -14      0   -655       O  
ATOM   2993  CB  VAL B 125      13.947   5.471 -29.059  1.00 30.95           C  
ANISOU 2993  CB  VAL B 125     4008   3918   3835    -60     35   -707       C  
ATOM   2994  CG1 VAL B 125      12.940   6.420 -29.696  1.00 28.95           C  
ANISOU 2994  CG1 VAL B 125     3780   3607   3615    -54     52   -716       C  
ATOM   2995  CG2 VAL B 125      13.941   5.607 -27.547  1.00 31.65           C  
ANISOU 2995  CG2 VAL B 125     4083   4047   3898    -83     43   -726       C  
ATOM   2996  N   GLY B 126      12.656   3.546 -31.636  1.00 25.78           N  
ANISOU 2996  N   GLY B 126     3369   3195   3232     20      0   -638       N  
ATOM   2997  CA  GLY B 126      12.664   3.349 -33.072  1.00 28.57           C  
ANISOU 2997  CA  GLY B 126     3732   3520   3604     37     -8   -622       C  
ATOM   2998  C   GLY B 126      12.891   1.922 -33.545  1.00 26.59           C  
ANISOU 2998  C   GLY B 126     3470   3282   3352     61    -28   -596       C  
ATOM   2999  O   GLY B 126      12.759   1.668 -34.747  1.00 26.34           O  
ANISOU 2999  O   GLY B 126     3446   3226   3335     76    -34   -583       O  
ATOM   3000  N   ARG B 127      13.212   0.988 -32.640  1.00 24.63           N  
ANISOU 3000  N   ARG B 127     3203   3070   3086     64    -38   -587       N  
ATOM   3001  CA  ARG B 127      13.353  -0.415 -33.017  1.00 27.73           C  
ANISOU 3001  CA  ARG B 127     3585   3471   3481     89    -55   -561       C  
ATOM   3002  C   ARG B 127      12.098  -0.928 -33.712  1.00 28.76           C  
ANISOU 3002  C   ARG B 127     3728   3564   3636    112    -59   -546       C  
ATOM   3003  O   ARG B 127      12.183  -1.735 -34.645  1.00 26.05           O  
ANISOU 3003  O   ARG B 127     3385   3211   3303    130    -69   -530       O  
ATOM   3004  CB  ARG B 127      13.661  -1.273 -31.780  1.00 29.22           C  
ANISOU 3004  CB  ARG B 127     3752   3701   3649     89    -63   -550       C  
ATOM   3005  CG  ARG B 127      14.004  -2.763 -32.069  1.00 32.93           C  
ANISOU 3005  CG  ARG B 127     4208   4182   4122    114    -79   -522       C  
ATOM   3006  CD  ARG B 127      14.517  -3.518 -30.814  1.00 32.56           C  
ANISOU 3006  CD  ARG B 127     4137   4181   4053    113    -86   -509       C  
ATOM   3007  NE  ARG B 127      15.862  -3.072 -30.453  1.00 36.12           N  
ANISOU 3007  NE  ARG B 127     4573   4672   4480     92    -85   -519       N  
ATOM   3008  CZ  ARG B 127      16.476  -3.306 -29.294  1.00 33.69           C  
ANISOU 3008  CZ  ARG B 127     4242   4413   4146     81    -89   -513       C  
ATOM   3009  NH1 ARG B 127      15.939  -4.082 -28.362  1.00 30.77           N  
ANISOU 3009  NH1 ARG B 127     3861   4059   3771     90    -95   -495       N  
ATOM   3010  NH2 ARG B 127      17.646  -2.720 -29.054  1.00 31.11           N  
ANISOU 3010  NH2 ARG B 127     3903   4122   3797     59    -86   -526       N  
ATOM   3011  N   ASP B 128      10.923  -0.466 -33.272  1.00 28.99           N  
ANISOU 3011  N   ASP B 128     3766   3573   3674    112    -51   -552       N  
ATOM   3012  CA  ASP B 128       9.637  -0.916 -33.797  1.00 30.41           C  
ANISOU 3012  CA  ASP B 128     3957   3722   3876    133    -55   -538       C  
ATOM   3013  C   ASP B 128       9.185  -0.121 -35.017  1.00 30.39           C  
ANISOU 3013  C   ASP B 128     3971   3682   3893    135    -49   -542       C  
ATOM   3014  O   ASP B 128       7.979  -0.057 -35.285  1.00 28.53           O  
ANISOU 3014  O   ASP B 128     3745   3420   3675    147    -47   -536       O  
ATOM   3015  CB  ASP B 128       8.570  -0.849 -32.697  1.00 31.75           C  
ANISOU 3015  CB  ASP B 128     4125   3892   4046    133    -49   -542       C  
ATOM   3016  CG  ASP B 128       8.332   0.578 -32.181  1.00 34.72           C  
ANISOU 3016  CG  ASP B 128     4511   4260   4422    112    -30   -567       C  
ATOM   3017  OD1 ASP B 128       9.249   1.439 -32.279  1.00 34.78           O  
ANISOU 3017  OD1 ASP B 128     4520   4274   4421     93    -22   -584       O  
ATOM   3018  OD2 ASP B 128       7.233   0.833 -31.640  1.00 36.82           O  
ANISOU 3018  OD2 ASP B 128     4781   4513   4696    115    -22   -571       O  
ATOM   3019  N   MET B 129      10.120   0.460 -35.779  1.00 25.71           N  
ANISOU 3019  N   MET B 129     3382   3088   3298    125    -46   -549       N  
ATOM   3020  CA  MET B 129       9.753   1.409 -36.830  1.00 27.58           C  
ANISOU 3020  CA  MET B 129     3636   3293   3552    123    -38   -551       C  
ATOM   3021  C   MET B 129       8.790   0.802 -37.850  1.00 28.92           C  
ANISOU 3021  C   MET B 129     3811   3438   3739    145    -47   -532       C  
ATOM   3022  O   MET B 129       7.875   1.485 -38.342  1.00 25.34           O  
ANISOU 3022  O   MET B 129     3370   2957   3303    149    -41   -530       O  
ATOM   3023  CB  MET B 129      11.008   1.924 -37.536  1.00 29.26           C  
ANISOU 3023  CB  MET B 129     3849   3512   3756    109    -37   -559       C  
ATOM   3024  CG  MET B 129      10.674   2.758 -38.752  1.00 28.22           C  
ANISOU 3024  CG  MET B 129     3733   3349   3642    109    -31   -556       C  
ATOM   3025  SD  MET B 129      10.048   4.281 -38.012  1.00 33.99           S  
ANISOU 3025  SD  MET B 129     4476   4057   4384     94     -9   -574       S  
ATOM   3026  CE  MET B 129      10.545   5.550 -39.133  1.00 39.75           C  
ANISOU 3026  CE  MET B 129     5219   4762   5124     80      2   -578       C  
ATOM   3027  N   GLN B 130       8.985  -0.474 -38.186  1.00 27.76           N  
ANISOU 3027  N   GLN B 130     3656   3303   3590    159    -61   -519       N  
ATOM   3028  CA  GLN B 130       8.096  -1.140 -39.132  1.00 29.91           C  
ANISOU 3028  CA  GLN B 130     3933   3556   3876    176    -69   -503       C  
ATOM   3029  C   GLN B 130       6.648  -1.100 -38.652  1.00 30.39           C  
ANISOU 3029  C   GLN B 130     3998   3601   3949    185    -66   -498       C  
ATOM   3030  O   GLN B 130       5.725  -0.921 -39.450  1.00 30.80           O  
ANISOU 3030  O   GLN B 130     4056   3630   4015    193    -66   -490       O  
ATOM   3031  CB  GLN B 130       8.556  -2.583 -39.342  1.00 30.29           C  
ANISOU 3031  CB  GLN B 130     3970   3620   3920    188    -81   -492       C  
ATOM   3032  CG  GLN B 130       7.836  -3.296 -40.471  1.00 31.69           C  
ANISOU 3032  CG  GLN B 130     4150   3780   4109    202    -89   -480       C  
ATOM   3033  CD  GLN B 130       8.362  -4.699 -40.711  1.00 33.60           C  
ANISOU 3033  CD  GLN B 130     4383   4034   4350    212    -98   -473       C  
ATOM   3034  OE1 GLN B 130       8.793  -5.038 -41.820  1.00 31.91           O  
ANISOU 3034  OE1 GLN B 130     4169   3817   4137    214   -101   -472       O  
ATOM   3035  NE2 GLN B 130       8.325  -5.522 -39.675  1.00 32.97           N  
ANISOU 3035  NE2 GLN B 130     4294   3967   4267    219   -100   -467       N  
ATOM   3036  N   GLN B 131       6.434  -1.235 -37.344  1.00 28.09           N  
ANISOU 3036  N   GLN B 131     3700   3323   3651    183    -63   -503       N  
ATOM   3037  CA  GLN B 131       5.085  -1.172 -36.787  1.00 32.10           C  
ANISOU 3037  CA  GLN B 131     4211   3818   4169    190    -59   -500       C  
ATOM   3038  C   GLN B 131       4.629   0.252 -36.495  1.00 32.54           C  
ANISOU 3038  C   GLN B 131     4275   3856   4232    180    -42   -514       C  
ATOM   3039  O   GLN B 131       3.424   0.481 -36.365  1.00 35.00           O  
ANISOU 3039  O   GLN B 131     4591   4150   4558    188    -37   -511       O  
ATOM   3040  CB  GLN B 131       5.002  -2.022 -35.518  1.00 32.87           C  
ANISOU 3040  CB  GLN B 131     4297   3938   4255    192    -62   -498       C  
ATOM   3041  CG  GLN B 131       4.901  -3.524 -35.802  1.00 33.61           C  
ANISOU 3041  CG  GLN B 131     4383   4038   4350    207    -76   -480       C  
ATOM   3042  CD  GLN B 131       6.129  -4.081 -36.507  1.00 36.32           C  
ANISOU 3042  CD  GLN B 131     4721   4392   4687    208    -84   -476       C  
ATOM   3043  OE1 GLN B 131       6.025  -4.682 -37.585  1.00 40.29           O  
ANISOU 3043  OE1 GLN B 131     5227   4882   5200    218    -91   -468       O  
ATOM   3044  NE2 GLN B 131       7.304  -3.874 -35.910  1.00 33.87           N  
ANISOU 3044  NE2 GLN B 131     4402   4105   4360    197    -83   -484       N  
ATOM   3045  N   LEU B 132       5.549   1.214 -36.377  1.00 30.49           N  
ANISOU 3045  N   LEU B 132     4019   3600   3966    163    -32   -530       N  
ATOM   3046  CA  LEU B 132       5.124   2.608 -36.293  1.00 29.10           C  
ANISOU 3046  CA  LEU B 132     3853   3401   3803    154    -15   -543       C  
ATOM   3047  C   LEU B 132       4.520   3.059 -37.610  1.00 31.74           C  
ANISOU 3047  C   LEU B 132     4198   3704   4157    165    -14   -530       C  
ATOM   3048  O   LEU B 132       3.496   3.758 -37.635  1.00 31.60           O  
ANISOU 3048  O   LEU B 132     4186   3661   4157    171     -4   -528       O  
ATOM   3049  CB  LEU B 132       6.300   3.510 -35.910  1.00 29.04           C  
ANISOU 3049  CB  LEU B 132     3847   3404   3783    130     -3   -564       C  
ATOM   3050  CG  LEU B 132       6.845   3.382 -34.481  1.00 31.38           C  
ANISOU 3050  CG  LEU B 132     4133   3733   4058    115      1   -581       C  
ATOM   3051  CD1 LEU B 132       8.015   4.336 -34.236  1.00 34.08           C  
ANISOU 3051  CD1 LEU B 132     4475   4085   4387     88     13   -604       C  
ATOM   3052  CD2 LEU B 132       5.745   3.618 -33.464  1.00 32.20           C  
ANISOU 3052  CD2 LEU B 132     4236   3830   4167    116     12   -590       C  
ATOM   3053  N   LEU B 133       5.133   2.647 -38.718  1.00 28.82           N  
ANISOU 3053  N   LEU B 133     3828   3337   3784    167    -26   -519       N  
ATOM   3054  CA  LEU B 133       4.629   3.022 -40.027  1.00 30.35           C  
ANISOU 3054  CA  LEU B 133     4030   3508   3994    176    -27   -504       C  
ATOM   3055  C   LEU B 133       3.373   2.237 -40.393  1.00 28.87           C  
ANISOU 3055  C   LEU B 133     3839   3314   3816    195    -37   -486       C  
ATOM   3056  O   LEU B 133       2.501   2.768 -41.084  1.00 31.51           O  
ANISOU 3056  O   LEU B 133     4179   3627   4166    203    -34   -473       O  
ATOM   3057  CB  LEU B 133       5.734   2.832 -41.069  1.00 29.90           C  
ANISOU 3057  CB  LEU B 133     3973   3461   3928    170    -35   -500       C  
ATOM   3058  CG  LEU B 133       6.973   3.716 -40.851  1.00 29.97           C  
ANISOU 3058  CG  LEU B 133     3984   3475   3927    149    -25   -517       C  
ATOM   3059  CD1 LEU B 133       8.176   3.265 -41.689  1.00 30.71           C  
ANISOU 3059  CD1 LEU B 133     4074   3587   4007    143    -35   -515       C  
ATOM   3060  CD2 LEU B 133       6.643   5.185 -41.090  1.00 30.80           C  
ANISOU 3060  CD2 LEU B 133     4102   3552   4049    141     -8   -520       C  
ATOM   3061  N   PHE B 134       3.250   0.995 -39.927  1.00 28.58           N  
ANISOU 3061  N   PHE B 134     3793   3294   3770    202    -48   -482       N  
ATOM   3062  CA  PHE B 134       2.096   0.147 -40.235  1.00 34.49           C  
ANISOU 3062  CA  PHE B 134     4539   4039   4526    218    -57   -467       C  
ATOM   3063  C   PHE B 134       1.622  -0.532 -38.951  1.00 34.50           C  
ANISOU 3063  C   PHE B 134     4534   4052   4523    222    -58   -471       C  
ATOM   3064  O   PHE B 134       1.855  -1.728 -38.727  1.00 33.79           O  
ANISOU 3064  O   PHE B 134     4436   3978   4425    226    -68   -466       O  
ATOM   3065  CB  PHE B 134       2.447  -0.848 -41.344  1.00 33.41           C  
ANISOU 3065  CB  PHE B 134     4399   3910   4384    222    -71   -456       C  
ATOM   3066  CG  PHE B 134       3.012  -0.174 -42.573  1.00 33.69           C  
ANISOU 3066  CG  PHE B 134     4441   3939   4421    216    -71   -453       C  
ATOM   3067  CD1 PHE B 134       2.180   0.449 -43.487  1.00 30.11           C  
ANISOU 3067  CD1 PHE B 134     3992   3469   3980    221    -70   -440       C  
ATOM   3068  CD2 PHE B 134       4.376  -0.105 -42.771  1.00 32.92           C  
ANISOU 3068  CD2 PHE B 134     4343   3854   4312    205    -71   -462       C  
ATOM   3069  CE1 PHE B 134       2.696   1.096 -44.600  1.00 31.21           C  
ANISOU 3069  CE1 PHE B 134     4136   3604   4120    214    -69   -435       C  
ATOM   3070  CE2 PHE B 134       4.910   0.535 -43.884  1.00 31.81           C  
ANISOU 3070  CE2 PHE B 134     4208   3709   4172    198    -70   -459       C  
ATOM   3071  CZ  PHE B 134       4.072   1.145 -44.796  1.00 27.78           C  
ANISOU 3071  CZ  PHE B 134     3702   3181   3673    202    -69   -445       C  
ATOM   3072  N   PRO B 135       0.938   0.214 -38.082  1.00 38.10           N  
ANISOU 3072  N   PRO B 135     4991   4499   4985    220    -45   -478       N  
ATOM   3073  CA  PRO B 135       0.521  -0.340 -36.785  1.00 38.05           C  
ANISOU 3073  CA  PRO B 135     4977   4508   4973    221    -44   -483       C  
ATOM   3074  C   PRO B 135      -0.398  -1.545 -36.931  1.00 42.00           C  
ANISOU 3074  C   PRO B 135     5472   5011   5476    235    -56   -467       C  
ATOM   3075  O   PRO B 135      -1.230  -1.617 -37.840  1.00 36.92           O  
ANISOU 3075  O   PRO B 135     4831   4352   4845    245    -60   -455       O  
ATOM   3076  CB  PRO B 135      -0.198   0.838 -36.115  1.00 36.47           C  
ANISOU 3076  CB  PRO B 135     4782   4293   4784    218    -26   -495       C  
ATOM   3077  CG  PRO B 135       0.341   2.057 -36.801  1.00 39.03           C  
ANISOU 3077  CG  PRO B 135     5115   4599   5116    210    -16   -501       C  
ATOM   3078  CD  PRO B 135       0.559   1.629 -38.230  1.00 32.65           C  
ANISOU 3078  CD  PRO B 135     4309   3787   4310    217    -30   -484       C  
ATOM   3079  N   LEU B 136      -0.214  -2.514 -36.025  1.00 42.71           N  
ANISOU 3079  N   LEU B 136     5554   5120   5554    235    -62   -466       N  
ATOM   3080  CA  LEU B 136      -1.153  -3.623 -35.910  1.00 43.61           C  
ANISOU 3080  CA  LEU B 136     5663   5236   5672    246    -70   -453       C  
ATOM   3081  C   LEU B 136      -2.500  -3.144 -35.379  1.00 48.59           C  
ANISOU 3081  C   LEU B 136     6293   5858   6313    250    -61   -453       C  
ATOM   3082  O   LEU B 136      -3.540  -3.739 -35.682  1.00 48.39           O  
ANISOU 3082  O   LEU B 136     6265   5825   6295    260    -67   -441       O  
ATOM   3083  CB  LEU B 136      -0.566  -4.708 -35.002  1.00 45.86           C  
ANISOU 3083  CB  LEU B 136     5939   5545   5943    244    -76   -450       C  
ATOM   3084  N   SER B 137      -2.493  -2.081 -34.584  1.00 47.77           N  
ANISOU 3084  N   SER B 137     6191   5752   6208    242    -47   -469       N  
ATOM   3085  CA  SER B 137      -3.705  -1.385 -34.179  1.00 49.65           C  
ANISOU 3085  CA  SER B 137     6429   5977   6458    246    -35   -472       C  
ATOM   3086  C   SER B 137      -3.297   0.034 -33.817  1.00 49.49           C  
ANISOU 3086  C   SER B 137     6414   5947   6441    236    -17   -492       C  
ATOM   3087  O   SER B 137      -2.125   0.307 -33.545  1.00 50.32           O  
ANISOU 3087  O   SER B 137     6522   6064   6534    222    -15   -504       O  
ATOM   3088  CB  SER B 137      -4.407  -2.087 -33.006  1.00 51.58           C  
ANISOU 3088  CB  SER B 137     6665   6238   6696    247    -35   -472       C  
ATOM   3089  OG  SER B 137      -4.137  -1.456 -31.764  1.00 53.63           O  
ANISOU 3089  OG  SER B 137     6922   6510   6945    234    -22   -491       O  
ATOM   3090  N   GLU B 138      -4.266   0.944 -33.843  1.00 47.95           N  
ANISOU 3090  N   GLU B 138     6223   5732   6265    242     -4   -495       N  
ATOM   3091  CA  GLU B 138      -4.016   2.311 -33.411  1.00 49.96           C  
ANISOU 3091  CA  GLU B 138     6483   5973   6526    232     17   -516       C  
ATOM   3092  C   GLU B 138      -4.463   2.551 -31.976  1.00 51.07           C  
ANISOU 3092  C   GLU B 138     6618   6125   6661    224     31   -534       C  
ATOM   3093  O   GLU B 138      -4.411   3.687 -31.500  1.00 53.09           O  
ANISOU 3093  O   GLU B 138     6879   6369   6925    215     52   -555       O  
ATOM   3094  CB  GLU B 138      -4.684   3.303 -34.366  1.00 50.52           C  
ANISOU 3094  CB  GLU B 138     6561   6012   6624    243     26   -507       C  
ATOM   3095  CG  GLU B 138      -3.720   3.820 -35.428  1.00 53.99           C  
ANISOU 3095  CG  GLU B 138     7008   6439   7065    238     24   -504       C  
ATOM   3096  CD  GLU B 138      -4.417   4.440 -36.627  1.00 56.46           C  
ANISOU 3096  CD  GLU B 138     7325   6725   7401    253     25   -484       C  
ATOM   3097  OE1 GLU B 138      -5.326   5.270 -36.419  1.00 56.50           O  
ANISOU 3097  OE1 GLU B 138     7331   6710   7428    261     41   -485       O  
ATOM   3098  OE2 GLU B 138      -4.049   4.103 -37.778  1.00 58.44           O  
ANISOU 3098  OE2 GLU B 138     7578   6977   7649    255     11   -468       O  
ATOM   3099  N   ILE B 139      -4.880   1.499 -31.274  1.00 50.82           N  
ANISOU 3099  N   ILE B 139     6577   6116   6617    226     22   -528       N  
ATOM   3100  CA  ILE B 139      -5.307   1.587 -29.880  1.00 51.71           C  
ANISOU 3100  CA  ILE B 139     6682   6244   6720    217     34   -545       C  
ATOM   3101  C   ILE B 139      -4.041   1.586 -29.028  1.00 54.19           C  
ANISOU 3101  C   ILE B 139     6994   6586   7009    196     36   -562       C  
ATOM   3102  O   ILE B 139      -3.417   0.541 -28.822  1.00 51.69           O  
ANISOU 3102  O   ILE B 139     6670   6295   6673    193     19   -551       O  
ATOM   3103  CB  ILE B 139      -6.252   0.445 -29.499  1.00 52.36           C  
ANISOU 3103  CB  ILE B 139     6756   6342   6798    227     23   -529       C  
ATOM   3104  CG1 ILE B 139      -7.479   0.442 -30.424  1.00 48.76           C  
ANISOU 3104  CG1 ILE B 139     6300   5861   6365    247     20   -511       C  
ATOM   3105  CG2 ILE B 139      -6.682   0.544 -28.037  1.00 51.42           C  
ANISOU 3105  CG2 ILE B 139     6627   6242   6667    216     35   -546       C  
ATOM   3106  CD1 ILE B 139      -8.170   1.789 -30.536  1.00 52.11           C  
ANISOU 3106  CD1 ILE B 139     6728   6258   6812    252     41   -522       C  
ATOM   3107  N   ARG B 140      -3.662   2.759 -28.532  1.00 52.46           N  
ANISOU 3107  N   ARG B 140     6780   6363   6791    180     56   -588       N  
ATOM   3108  CA  ARG B 140      -2.407   2.939 -27.819  1.00 53.79           C  
ANISOU 3108  CA  ARG B 140     6944   6557   6935    157     59   -607       C  
ATOM   3109  C   ARG B 140      -2.651   3.044 -26.319  1.00 53.68           C  
ANISOU 3109  C   ARG B 140     6922   6571   6904    140     72   -628       C  
ATOM   3110  O   ARG B 140      -3.743   3.387 -25.860  1.00 54.14           O  
ANISOU 3110  O   ARG B 140     6978   6618   6973    145     86   -636       O  
ATOM   3111  CB  ARG B 140      -1.670   4.186 -28.324  1.00 52.08           C  
ANISOU 3111  CB  ARG B 140     6740   6320   6729    145     74   -625       C  
ATOM   3112  N   ALA B 141      -1.605   2.734 -25.557  1.00 50.55           N  
ANISOU 3112  N   ALA B 141     6516   6212   6478    120     67   -636       N  
ATOM   3113  CA  ALA B 141      -1.660   2.876 -24.113  1.00 47.65           C  
ANISOU 3113  CA  ALA B 141     6139   5878   6089    100     79   -657       C  
ATOM   3114  C   ALA B 141      -1.872   4.337 -23.731  1.00 51.02           C  
ANISOU 3114  C   ALA B 141     6573   6286   6527     84    109   -694       C  
ATOM   3115  O   ALA B 141      -1.599   5.259 -24.506  1.00 51.11           O  
ANISOU 3115  O   ALA B 141     6597   6264   6558     85    120   -703       O  
ATOM   3116  CB  ALA B 141      -0.375   2.353 -23.473  1.00 45.82           C  
ANISOU 3116  CB  ALA B 141     5894   5692   5822     80     68   -657       C  
ATOM   3117  N   SER B 142      -2.368   4.543 -22.515  1.00 48.71           N  
ANISOU 3117  N   SER B 142     6272   6015   6222     70    124   -715       N  
ATOM   3118  CA  SER B 142      -2.514   5.899 -22.028  1.00 50.89           C  
ANISOU 3118  CA  SER B 142     6554   6275   6507     52    156   -754       C  
ATOM   3119  C   SER B 142      -1.136   6.544 -21.923  1.00 48.04           C  
ANISOU 3119  C   SER B 142     6196   5927   6130     25    163   -776       C  
ATOM   3120  O   SER B 142      -0.138   5.864 -21.644  1.00 45.12           O  
ANISOU 3120  O   SER B 142     5816   5599   5730     13    146   -767       O  
ATOM   3121  CB  SER B 142      -3.196   5.923 -20.660  1.00 51.40           C  
ANISOU 3121  CB  SER B 142     6606   6366   6555     38    171   -775       C  
ATOM   3122  OG  SER B 142      -2.752   4.846 -19.849  1.00 55.58           O  
ANISOU 3122  OG  SER B 142     7120   6950   7048     27    152   -762       O  
ATOM   3123  N   PRO B 143      -1.043   7.852 -22.141  1.00 48.44           N  
ANISOU 3123  N   PRO B 143     6258   5945   6200     14    189   -804       N  
ATOM   3124  CA  PRO B 143       0.150   8.569 -21.685  1.00 49.61           C  
ANISOU 3124  CA  PRO B 143     6407   6113   6330    -20    202   -835       C  
ATOM   3125  C   PRO B 143       0.323   8.282 -20.203  1.00 53.16           C  
ANISOU 3125  C   PRO B 143     6840   6618   6741    -47    206   -856       C  
ATOM   3126  O   PRO B 143      -0.559   7.706 -19.563  1.00 56.01           O  
ANISOU 3126  O   PRO B 143     7191   6995   7095    -39    203   -849       O  
ATOM   3127  CB  PRO B 143      -0.172  10.042 -21.954  1.00 53.24           C  
ANISOU 3127  CB  PRO B 143     6882   6523   6822    -25    236   -865       C  
ATOM   3128  CG  PRO B 143      -1.667  10.085 -22.162  1.00 49.97           C  
ANISOU 3128  CG  PRO B 143     6472   6073   6440      4    243   -854       C  
ATOM   3129  CD  PRO B 143      -2.057   8.752 -22.709  1.00 51.49           C  
ANISOU 3129  CD  PRO B 143     6658   6276   6629     32    210   -810       C  
ATOM   3130  N   GLU B 144       1.469   8.669 -19.656  1.00 51.69           N  
ANISOU 3130  N   GLU B 144     6648   6465   6527    -81    213   -881       N  
ATOM   3131  CA  GLU B 144       1.832   8.323 -18.280  1.00 48.21           C  
ANISOU 3131  CA  GLU B 144     6188   6087   6042   -110    213   -897       C  
ATOM   3132  C   GLU B 144       2.260   6.860 -18.206  1.00 43.20           C  
ANISOU 3132  C   GLU B 144     5538   5497   5381    -99    177   -856       C  
ATOM   3133  O   GLU B 144       3.184   6.520 -17.461  1.00 43.86           O  
ANISOU 3133  O   GLU B 144     5604   5636   5425   -123    169   -859       O  
ATOM   3134  CB  GLU B 144       0.687   8.588 -17.279  1.00 52.04           C  
ANISOU 3134  CB  GLU B 144     6668   6576   6528   -116    234   -920       C  
ATOM   3135  CG  GLU B 144       0.075   9.995 -17.324  1.00 52.69           C  
ANISOU 3135  CG  GLU B 144     6766   6609   6644   -122    272   -960       C  
ATOM   3136  CD  GLU B 144      -1.442   9.981 -17.581  1.00 58.32           C  
ANISOU 3136  CD  GLU B 144     7484   7281   7392    -90    280   -949       C  
ATOM   3137  OE1 GLU B 144      -2.027   8.883 -17.725  1.00 57.29           O  
ANISOU 3137  OE1 GLU B 144     7347   7162   7260    -66    255   -912       O  
ATOM   3138  OE2 GLU B 144      -2.057  11.071 -17.635  1.00 59.82           O  
ANISOU 3138  OE2 GLU B 144     7686   7428   7614    -90    311   -977       O  
ATOM   3139  N   LEU B 145       1.613   5.974 -18.970  1.00 41.20           N  
ANISOU 3139  N   LEU B 145     5287   5220   5146    -63    157   -817       N  
ATOM   3140  CA  LEU B 145       2.030   4.577 -19.000  1.00 40.44           C  
ANISOU 3140  CA  LEU B 145     5177   5158   5030    -50    125   -777       C  
ATOM   3141  C   LEU B 145       2.752   4.170 -20.284  1.00 35.54           C  
ANISOU 3141  C   LEU B 145     4564   4517   4422    -30    105   -749       C  
ATOM   3142  O   LEU B 145       3.473   3.165 -20.276  1.00 30.19           O  
ANISOU 3142  O   LEU B 145     3874   3872   3725    -26     82   -723       O  
ATOM   3143  CB  LEU B 145       0.811   3.662 -18.797  1.00 37.31           C  
ANISOU 3143  CB  LEU B 145     4776   4760   4641    -26    115   -751       C  
ATOM   3144  CG  LEU B 145       0.147   3.664 -17.409  1.00 40.40           C  
ANISOU 3144  CG  LEU B 145     5155   5186   5011    -44    127   -769       C  
ATOM   3145  CD1 LEU B 145      -0.902   2.559 -17.308  1.00 41.61           C  
ANISOU 3145  CD1 LEU B 145     5301   5340   5169    -19    112   -737       C  
ATOM   3146  CD2 LEU B 145       1.182   3.542 -16.272  1.00 37.81           C  
ANISOU 3146  CD2 LEU B 145     4807   4924   4637    -78    125   -781       C  
ATOM   3147  N   ALA B 146       2.593   4.932 -21.372  1.00 32.45           N  
ANISOU 3147  N   ALA B 146     4191   4073   4064    -19    114   -755       N  
ATOM   3148  CA  ALA B 146       3.008   4.458 -22.690  1.00 32.10           C  
ANISOU 3148  CA  ALA B 146     4155   4005   4035      4     95   -726       C  
ATOM   3149  C   ALA B 146       4.512   4.212 -22.762  1.00 31.33           C  
ANISOU 3149  C   ALA B 146     4049   3942   3914    -11     82   -723       C  
ATOM   3150  O   ALA B 146       4.954   3.284 -23.446  1.00 29.65           O  
ANISOU 3150  O   ALA B 146     3833   3733   3700      7     60   -692       O  
ATOM   3151  CB  ALA B 146       2.578   5.455 -23.765  1.00 34.43           C  
ANISOU 3151  CB  ALA B 146     4470   4242   4368     15    109   -734       C  
ATOM   3152  N   ASP B 147       5.313   5.018 -22.055  1.00 30.20           N  
ANISOU 3152  N   ASP B 147     3901   3825   3749    -45     97   -754       N  
ATOM   3153  CA  ASP B 147       6.756   4.809 -22.082  1.00 30.20           C  
ANISOU 3153  CA  ASP B 147     3891   3861   3723    -60     86   -751       C  
ATOM   3154  C   ASP B 147       7.134   3.531 -21.351  1.00 31.10           C  
ANISOU 3154  C   ASP B 147     3982   4030   3806    -58     64   -725       C  
ATOM   3155  O   ASP B 147       8.059   2.815 -21.762  1.00 27.03           O  
ANISOU 3155  O   ASP B 147     3456   3532   3280    -51     44   -702       O  
ATOM   3156  CB  ASP B 147       7.483   5.995 -21.453  1.00 31.78           C  
ANISOU 3156  CB  ASP B 147     4090   4079   3906   -100    108   -793       C  
ATOM   3157  CG  ASP B 147       8.145   6.887 -22.484  1.00 45.43           C  
ANISOU 3157  CG  ASP B 147     5835   5774   5654   -105    117   -805       C  
ATOM   3158  OD1 ASP B 147       7.605   6.999 -23.615  1.00 49.46           O  
ANISOU 3158  OD1 ASP B 147     6361   6232   6198    -79    116   -791       O  
ATOM   3159  OD2 ASP B 147       9.223   7.450 -22.171  1.00 47.25           O  
ANISOU 3159  OD2 ASP B 147     6060   6032   5863   -136    125   -828       O  
ATOM   3160  N   TYR B 148       6.450   3.259 -20.240  1.00 28.57           N  
ANISOU 3160  N   TYR B 148     3650   3735   3470    -65     67   -728       N  
ATOM   3161  CA  TYR B 148       6.642   2.010 -19.523  1.00 24.87           C  
ANISOU 3161  CA  TYR B 148     3159   3314   2975    -60     47   -699       C  
ATOM   3162  C   TYR B 148       6.178   0.821 -20.353  1.00 27.75           C  
ANISOU 3162  C   TYR B 148     3528   3654   3362    -21     25   -657       C  
ATOM   3163  O   TYR B 148       6.822  -0.234 -20.336  1.00 23.37           O  
ANISOU 3163  O   TYR B 148     2958   3127   2794    -12      5   -626       O  
ATOM   3164  CB  TYR B 148       5.884   2.049 -18.197  1.00 24.71           C  
ANISOU 3164  CB  TYR B 148     3129   3324   2936    -76     58   -712       C  
ATOM   3165  CG  TYR B 148       6.517   2.900 -17.117  1.00 25.98           C  
ANISOU 3165  CG  TYR B 148     3277   3530   3062   -118     75   -750       C  
ATOM   3166  CD1 TYR B 148       6.246   4.262 -17.014  1.00 28.18           C  
ANISOU 3166  CD1 TYR B 148     3570   3784   3352   -140    104   -795       C  
ATOM   3167  CD2 TYR B 148       7.350   2.332 -16.176  1.00 22.61           C  
ANISOU 3167  CD2 TYR B 148     2825   3171   2594   -138     63   -739       C  
ATOM   3168  CE1 TYR B 148       6.812   5.038 -15.993  1.00 25.89           C  
ANISOU 3168  CE1 TYR B 148     3270   3537   3030   -182    122   -833       C  
ATOM   3169  CE2 TYR B 148       7.918   3.091 -15.156  1.00 25.92           C  
ANISOU 3169  CE2 TYR B 148     3232   3637   2978   -180     78   -775       C  
ATOM   3170  CZ  TYR B 148       7.652   4.440 -15.076  1.00 25.89           C  
ANISOU 3170  CZ  TYR B 148     3244   3609   2985   -203    108   -823       C  
ATOM   3171  OH  TYR B 148       8.235   5.172 -14.058  1.00 28.11           O  
ANISOU 3171  OH  TYR B 148     3511   3937   3230   -248    125   -861       O  
ATOM   3172  N   ALA B 149       5.033   0.956 -21.044  1.00 24.61           N  
ANISOU 3172  N   ALA B 149     3148   3206   2999      0     31   -655       N  
ATOM   3173  CA  ALA B 149       4.533  -0.154 -21.848  1.00 25.48           C  
ANISOU 3173  CA  ALA B 149     3261   3291   3128     34     12   -618       C  
ATOM   3174  C   ALA B 149       5.499  -0.494 -22.979  1.00 26.57           C  
ANISOU 3174  C   ALA B 149     3403   3419   3275     46     -2   -602       C  
ATOM   3175  O   ALA B 149       5.717  -1.674 -23.285  1.00 25.08           O  
ANISOU 3175  O   ALA B 149     3206   3236   3087     65    -21   -570       O  
ATOM   3176  CB  ALA B 149       3.136   0.171 -22.402  1.00 23.22           C  
ANISOU 3176  CB  ALA B 149     2991   2955   2874     51     21   -621       C  
ATOM   3177  N   ARG B 150       6.069   0.532 -23.624  1.00 26.78           N  
ANISOU 3177  N   ARG B 150     3440   3425   3309     35      8   -623       N  
ATOM   3178  CA  ARG B 150       7.064   0.307 -24.666  1.00 26.97           C  
ANISOU 3178  CA  ARG B 150     3466   3442   3338     43     -3   -611       C  
ATOM   3179  C   ARG B 150       8.320  -0.346 -24.094  1.00 25.52           C  
ANISOU 3179  C   ARG B 150     3262   3311   3124     33    -16   -599       C  
ATOM   3180  O   ARG B 150       8.859  -1.292 -24.678  1.00 23.16           O  
ANISOU 3180  O   ARG B 150     2957   3016   2828     51    -33   -573       O  
ATOM   3181  CB  ARG B 150       7.413   1.635 -25.336  1.00 28.86           C  
ANISOU 3181  CB  ARG B 150     3723   3654   3590     30     13   -638       C  
ATOM   3182  CG  ARG B 150       8.485   1.511 -26.417  1.00 32.68           C  
ANISOU 3182  CG  ARG B 150     4208   4132   4077     35      3   -628       C  
ATOM   3183  CD  ARG B 150       8.906   2.855 -26.983  1.00 32.80           C  
ANISOU 3183  CD  ARG B 150     4238   4123   4101     18     20   -655       C  
ATOM   3184  NE  ARG B 150       9.646   3.664 -26.020  1.00 37.92           N  
ANISOU 3184  NE  ARG B 150     4879   4805   4725    -17     34   -684       N  
ATOM   3185  CZ  ARG B 150       9.918   4.952 -26.176  1.00 37.23           C  
ANISOU 3185  CZ  ARG B 150     4803   4699   4643    -39     54   -714       C  
ATOM   3186  NH1 ARG B 150       9.562   5.607 -27.267  1.00 41.45           N  
ANISOU 3186  NH1 ARG B 150     5358   5185   5208    -28     62   -715       N  
ATOM   3187  NH2 ARG B 150      10.578   5.599 -25.220  1.00 42.54           N  
ANISOU 3187  NH2 ARG B 150     5467   5406   5290    -72     67   -743       N  
ATOM   3188  N   PHE B 151       8.791   0.150 -22.946  1.00 25.60           N  
ANISOU 3188  N   PHE B 151     3259   3363   3104      4     -7   -619       N  
ATOM   3189  CA  PHE B 151       9.910  -0.473 -22.244  1.00 26.26           C  
ANISOU 3189  CA  PHE B 151     3318   3505   3156     -7    -20   -606       C  
ATOM   3190  C   PHE B 151       9.622  -1.935 -21.934  1.00 24.47           C  
ANISOU 3190  C   PHE B 151     3076   3294   2926     16    -38   -566       C  
ATOM   3191  O   PHE B 151      10.487  -2.791 -22.120  1.00 23.78           O  
ANISOU 3191  O   PHE B 151     2975   3228   2831     27    -54   -540       O  
ATOM   3192  CB  PHE B 151      10.203   0.301 -20.955  1.00 22.76           C  
ANISOU 3192  CB  PHE B 151     2863   3107   2680    -44     -6   -635       C  
ATOM   3193  CG  PHE B 151      11.536  -0.023 -20.318  1.00 26.42           C  
ANISOU 3193  CG  PHE B 151     3299   3632   3106    -62    -16   -628       C  
ATOM   3194  CD1 PHE B 151      12.740   0.308 -20.950  1.00 23.29           C  
ANISOU 3194  CD1 PHE B 151     2902   3242   2705    -70    -18   -633       C  
ATOM   3195  CD2 PHE B 151      11.586  -0.613 -19.057  1.00 26.39           C  
ANISOU 3195  CD2 PHE B 151     3272   3684   3071    -73    -22   -615       C  
ATOM   3196  CE1 PHE B 151      13.969   0.024 -20.340  1.00 27.21           C  
ANISOU 3196  CE1 PHE B 151     3372   3800   3167    -87    -28   -625       C  
ATOM   3197  CE2 PHE B 151      12.812  -0.899 -18.439  1.00 29.79           C  
ANISOU 3197  CE2 PHE B 151     3675   4177   3465    -90    -32   -605       C  
ATOM   3198  CZ  PHE B 151      14.008  -0.570 -19.090  1.00 24.36           C  
ANISOU 3198  CZ  PHE B 151     2985   3495   2774    -97    -35   -611       C  
ATOM   3199  N   ASN B 152       8.411  -2.243 -21.461  1.00 23.73           N  
ANISOU 3199  N   ASN B 152     2986   3190   2840     25    -36   -561       N  
ATOM   3200  CA  ASN B 152       8.092  -3.632 -21.139  1.00 23.83           C  
ANISOU 3200  CA  ASN B 152     2987   3217   2852     45    -52   -523       C  
ATOM   3201  C   ASN B 152       8.214  -4.523 -22.372  1.00 24.28           C  
ANISOU 3201  C   ASN B 152     3051   3240   2936     77    -66   -495       C  
ATOM   3202  O   ASN B 152       8.822  -5.599 -22.315  1.00 21.98           O  
ANISOU 3202  O   ASN B 152     2744   2968   2639     90    -81   -465       O  
ATOM   3203  CB  ASN B 152       6.684  -3.737 -20.544  1.00 24.86           C  
ANISOU 3203  CB  ASN B 152     3121   3336   2988     48    -46   -524       C  
ATOM   3204  CG  ASN B 152       6.388  -5.129 -20.012  1.00 22.85           C  
ANISOU 3204  CG  ASN B 152     2852   3102   2728     64    -61   -485       C  
ATOM   3205  OD1 ASN B 152       6.999  -5.584 -19.035  1.00 22.88           O  
ANISOU 3205  OD1 ASN B 152     2832   3157   2702     53    -68   -470       O  
ATOM   3206  ND2 ASN B 152       5.461  -5.820 -20.659  1.00 23.92           N  
ANISOU 3206  ND2 ASN B 152     2999   3198   2892     90    -66   -467       N  
ATOM   3207  N   SER B 153       7.640  -4.091 -23.503  1.00 21.86           N  
ANISOU 3207  N   SER B 153     2766   2880   2658     89    -61   -506       N  
ATOM   3208  CA  SER B 153       7.690  -4.917 -24.714  1.00 24.19           C  
ANISOU 3208  CA  SER B 153     3069   3144   2978    116    -72   -483       C  
ATOM   3209  C   SER B 153       9.108  -5.030 -25.272  1.00 22.64           C  
ANISOU 3209  C   SER B 153     2864   2961   2775    116    -80   -479       C  
ATOM   3210  O   SER B 153       9.509  -6.102 -25.742  1.00 24.09           O  
ANISOU 3210  O   SER B 153     3042   3143   2968    136    -92   -452       O  
ATOM   3211  CB  SER B 153       6.750  -4.364 -25.790  1.00 26.52           C  
ANISOU 3211  CB  SER B 153     3387   3385   3303    126    -65   -496       C  
ATOM   3212  OG  SER B 153       5.489  -4.062 -25.231  1.00 34.04           O  
ANISOU 3212  OG  SER B 153     4346   4328   4261    124    -56   -504       O  
ATOM   3213  N   ASN B 154       9.874  -3.935 -25.261  1.00 24.01           N  
ANISOU 3213  N   ASN B 154     3039   3147   2936     93    -71   -505       N  
ATOM   3214  CA  ASN B 154      11.235  -3.993 -25.798  1.00 27.84           C  
ANISOU 3214  CA  ASN B 154     3516   3647   3413     91    -77   -502       C  
ATOM   3215  C   ASN B 154      12.145  -4.857 -24.933  1.00 25.46           C  
ANISOU 3215  C   ASN B 154     3187   3399   3088     90    -89   -479       C  
ATOM   3216  O   ASN B 154      12.931  -5.655 -25.465  1.00 24.81           O  
ANISOU 3216  O   ASN B 154     3095   3321   3010    106   -100   -457       O  
ATOM   3217  CB  ASN B 154      11.818  -2.590 -25.940  1.00 25.19           C  
ANISOU 3217  CB  ASN B 154     3188   3313   3069     65    -63   -536       C  
ATOM   3218  CG  ASN B 154      11.184  -1.829 -27.070  1.00 25.89           C  
ANISOU 3218  CG  ASN B 154     3302   3348   3186     70    -54   -551       C  
ATOM   3219  OD1 ASN B 154      10.862  -2.423 -28.088  1.00 33.08           O  
ANISOU 3219  OD1 ASN B 154     4223   4228   4120     94    -62   -534       O  
ATOM   3220  ND2 ASN B 154      11.053  -0.520 -26.933  1.00 22.65           N  
ANISOU 3220  ND2 ASN B 154     2904   2928   2775     48    -37   -582       N  
ATOM   3221  N   VAL B 155      12.043  -4.728 -23.602  1.00 22.50           N  
ANISOU 3221  N   VAL B 155     2798   3065   2686     72    -86   -482       N  
ATOM   3222  CA  VAL B 155      12.868  -5.550 -22.712  1.00 25.17           C  
ANISOU 3222  CA  VAL B 155     3106   3457   2999     71    -98   -456       C  
ATOM   3223  C   VAL B 155      12.496  -7.020 -22.860  1.00 25.50           C  
ANISOU 3223  C   VAL B 155     3143   3488   3059    103   -111   -415       C  
ATOM   3224  O   VAL B 155      13.371  -7.892 -22.969  1.00 25.44           O  
ANISOU 3224  O   VAL B 155     3117   3499   3049    117   -122   -388       O  
ATOM   3225  CB  VAL B 155      12.747  -5.066 -21.249  1.00 25.19           C  
ANISOU 3225  CB  VAL B 155     3095   3509   2968     41    -91   -469       C  
ATOM   3226  CG1 VAL B 155      13.380  -6.072 -20.273  1.00 22.41           C  
ANISOU 3226  CG1 VAL B 155     2710   3213   2589     43   -105   -434       C  
ATOM   3227  CG2 VAL B 155      13.392  -3.692 -21.077  1.00 25.02           C  
ANISOU 3227  CG2 VAL B 155     3075   3505   2926      7    -78   -509       C  
ATOM   3228  N   ASP B 156      11.194  -7.312 -22.928  1.00 23.69           N  
ANISOU 3228  N   ASP B 156     2928   3224   2848    115   -108   -412       N  
ATOM   3229  CA  ASP B 156      10.738  -8.694 -23.057  1.00 23.65           C  
ANISOU 3229  CA  ASP B 156     2919   3204   2862    143   -119   -375       C  
ATOM   3230  C   ASP B 156      11.269  -9.328 -24.342  1.00 25.49           C  
ANISOU 3230  C   ASP B 156     3157   3406   3120    167   -125   -363       C  
ATOM   3231  O   ASP B 156      11.738 -10.472 -24.336  1.00 26.54           O  
ANISOU 3231  O   ASP B 156     3277   3548   3260    186   -134   -331       O  
ATOM   3232  CB  ASP B 156       9.213  -8.737 -23.066  1.00 24.49           C  
ANISOU 3232  CB  ASP B 156     3043   3275   2986    150   -113   -380       C  
ATOM   3233  CG  ASP B 156       8.606  -8.767 -21.662  1.00 29.90           C  
ANISOU 3233  CG  ASP B 156     3717   3995   3649    135   -111   -376       C  
ATOM   3234  OD1 ASP B 156       9.367  -8.793 -20.659  1.00 25.58           O  
ANISOU 3234  OD1 ASP B 156     3147   3502   3072    120   -115   -368       O  
ATOM   3235  OD2 ASP B 156       7.351  -8.709 -21.580  1.00 26.59           O  
ANISOU 3235  OD2 ASP B 156     3310   3551   3242    138   -105   -381       O  
ATOM   3236  N   ALA B 157      11.161  -8.613 -25.461  1.00 24.97           N  
ANISOU 3236  N   ALA B 157     3113   3303   3072    167   -119   -387       N  
ATOM   3237  CA  ALA B 157      11.668  -9.145 -26.722  1.00 26.34           C  
ANISOU 3237  CA  ALA B 157     3292   3449   3267    187   -123   -378       C  
ATOM   3238  C   ALA B 157      13.173  -9.391 -26.652  1.00 27.40           C  
ANISOU 3238  C   ALA B 157     3405   3619   3387    186   -129   -368       C  
ATOM   3239  O   ALA B 157      13.679 -10.375 -27.209  1.00 27.88           O  
ANISOU 3239  O   ALA B 157     3459   3673   3463    208   -136   -346       O  
ATOM   3240  CB  ALA B 157      11.342  -8.183 -27.865  1.00 24.18           C  
ANISOU 3240  CB  ALA B 157     3042   3136   3009    182   -115   -407       C  
ATOM   3241  N   ALA B 158      13.908  -8.491 -25.991  1.00 25.82           N  
ANISOU 3241  N   ALA B 158     3194   3459   3158    161   -126   -384       N  
ATOM   3242  CA  ALA B 158      15.365  -8.579 -25.987  1.00 28.25           C  
ANISOU 3242  CA  ALA B 158     3481   3803   3450    157   -131   -378       C  
ATOM   3243  C   ALA B 158      15.842  -9.771 -25.168  1.00 25.18           C  
ANISOU 3243  C   ALA B 158     3064   3451   3052    171   -142   -339       C  
ATOM   3244  O   ALA B 158      16.758 -10.486 -25.582  1.00 25.58           O  
ANISOU 3244  O   ALA B 158     3100   3508   3109    188   -148   -319       O  
ATOM   3245  CB  ALA B 158      15.969  -7.279 -25.451  1.00 27.71           C  
ANISOU 3245  CB  ALA B 158     3408   3769   3351    123   -124   -407       C  
ATOM   3246  N   PHE B 159      15.229 -10.005 -24.003  1.00 24.55           N  
ANISOU 3246  N   PHE B 159     2975   3395   2958    165   -144   -326       N  
ATOM   3247  CA  PHE B 159      15.565 -11.196 -23.230  1.00 25.72           C  
ANISOU 3247  CA  PHE B 159     3097   3574   3100    181   -154   -285       C  
ATOM   3248  C   PHE B 159      15.091 -12.467 -23.933  1.00 27.57           C  
ANISOU 3248  C   PHE B 159     3340   3765   3373    215   -157   -257       C  
ATOM   3249  O   PHE B 159      15.772 -13.499 -23.880  1.00 28.36           O  
ANISOU 3249  O   PHE B 159     3419   3876   3479    236   -164   -224       O  
ATOM   3250  CB  PHE B 159      14.978 -11.083 -21.821  1.00 24.62           C  
ANISOU 3250  CB  PHE B 159     2946   3472   2934    163   -154   -279       C  
ATOM   3251  CG  PHE B 159      15.861 -10.314 -20.849  1.00 26.05           C  
ANISOU 3251  CG  PHE B 159     3106   3719   3073    132   -154   -290       C  
ATOM   3252  CD1 PHE B 159      16.913 -10.940 -20.195  1.00 25.45           C  
ANISOU 3252  CD1 PHE B 159     2996   3697   2977    135   -165   -258       C  
ATOM   3253  CD2 PHE B 159      15.632  -8.969 -20.596  1.00 26.19           C  
ANISOU 3253  CD2 PHE B 159     3135   3744   3073    100   -143   -332       C  
ATOM   3254  CE1 PHE B 159      17.713 -10.234 -19.299  1.00 27.31           C  
ANISOU 3254  CE1 PHE B 159     3210   3997   3170    104   -165   -268       C  
ATOM   3255  CE2 PHE B 159      16.439  -8.254 -19.713  1.00 26.40           C  
ANISOU 3255  CE2 PHE B 159     3141   3831   3059     68   -142   -346       C  
ATOM   3256  CZ  PHE B 159      17.472  -8.890 -19.062  1.00 25.30           C  
ANISOU 3256  CZ  PHE B 159     2968   3749   2896     69   -154   -314       C  
ATOM   3257  N   THR B 160      13.957 -12.401 -24.637  1.00 22.05           N  
ANISOU 3257  N   THR B 160     2667   3013   2698    222   -152   -272       N  
ATOM   3258  CA  THR B 160      13.466 -13.573 -25.364  1.00 26.01           C  
ANISOU 3258  CA  THR B 160     3178   3471   3235    251   -153   -251       C  
ATOM   3259  C   THR B 160      14.442 -14.008 -26.465  1.00 27.45           C  
ANISOU 3259  C   THR B 160     3357   3637   3435    269   -154   -247       C  
ATOM   3260  O   THR B 160      14.627 -15.210 -26.703  1.00 23.27           O  
ANISOU 3260  O   THR B 160     2820   3095   2928    294   -157   -219       O  
ATOM   3261  CB  THR B 160      12.083 -13.270 -25.953  1.00 28.97           C  
ANISOU 3261  CB  THR B 160     3581   3798   3629    251   -147   -271       C  
ATOM   3262  OG1 THR B 160      11.163 -13.044 -24.882  1.00 27.95           O  
ANISOU 3262  OG1 THR B 160     3451   3683   3484    238   -146   -271       O  
ATOM   3263  CG2 THR B 160      11.569 -14.416 -26.826  1.00 26.78           C  
ANISOU 3263  CG2 THR B 160     3314   3475   3387    277   -147   -255       C  
ATOM   3264  N   ALA B 161      15.068 -13.047 -27.152  1.00 24.17           N  
ANISOU 3264  N   ALA B 161     2948   3222   3012    256   -151   -276       N  
ATOM   3265  CA  ALA B 161      16.073 -13.368 -28.168  1.00 27.22           C  
ANISOU 3265  CA  ALA B 161     3330   3599   3412    269   -151   -275       C  
ATOM   3266  C   ALA B 161      17.300 -14.072 -27.593  1.00 28.41           C  
ANISOU 3266  C   ALA B 161     3449   3792   3553    280   -157   -245       C  
ATOM   3267  O   ALA B 161      18.099 -14.627 -28.362  1.00 30.51           O  
ANISOU 3267  O   ALA B 161     3707   4049   3835    298   -157   -237       O  
ATOM   3268  CB  ALA B 161      16.515 -12.090 -28.889  1.00 29.34           C  
ANISOU 3268  CB  ALA B 161     3612   3867   3671    249   -146   -311       C  
ATOM   3269  N   HIS B 162      17.482 -14.048 -26.271  1.00 28.24           N  
ANISOU 3269  N   HIS B 162     3406   3818   3505    269   -163   -228       N  
ATOM   3270  CA  HIS B 162      18.600 -14.713 -25.610  1.00 27.24           C  
ANISOU 3270  CA  HIS B 162     3245   3738   3366    279   -170   -194       C  
ATOM   3271  C   HIS B 162      18.136 -15.842 -24.701  1.00 27.39           C  
ANISOU 3271  C   HIS B 162     3250   3765   3391    296   -175   -153       C  
ATOM   3272  O   HIS B 162      18.925 -16.332 -23.882  1.00 28.42           O  
ANISOU 3272  O   HIS B 162     3350   3942   3508    301   -182   -120       O  
ATOM   3273  CB  HIS B 162      19.411 -13.693 -24.818  1.00 26.95           C  
ANISOU 3273  CB  HIS B 162     3191   3761   3288    249   -173   -207       C  
ATOM   3274  CG  HIS B 162      20.016 -12.632 -25.678  1.00 29.54           C  
ANISOU 3274  CG  HIS B 162     3531   4085   3610    233   -168   -245       C  
ATOM   3275  ND1 HIS B 162      19.332 -11.494 -26.044  1.00 28.93           N  
ANISOU 3275  ND1 HIS B 162     3480   3982   3529    210   -160   -284       N  
ATOM   3276  CD2 HIS B 162      21.228 -12.559 -26.280  1.00 30.09           C  
ANISOU 3276  CD2 HIS B 162     3588   4169   3678    236   -168   -247       C  
ATOM   3277  CE1 HIS B 162      20.104 -10.754 -26.819  1.00 33.53           C  
ANISOU 3277  CE1 HIS B 162     4067   4565   4109    200   -156   -308       C  
ATOM   3278  NE2 HIS B 162      21.258 -11.380 -26.980  1.00 29.80           N  
ANISOU 3278  NE2 HIS B 162     3571   4117   3636    214   -161   -287       N  
ATOM   3279  N   VAL B 163      16.881 -16.280 -24.840  1.00 28.81           N  
ANISOU 3279  N   VAL B 163     3452   3903   3594    305   -171   -151       N  
ATOM   3280  CA  VAL B 163      16.320 -17.255 -23.909  1.00 30.61           C  
ANISOU 3280  CA  VAL B 163     3667   4137   3825    316   -175   -113       C  
ATOM   3281  C   VAL B 163      16.959 -18.622 -24.093  1.00 31.67           C  
ANISOU 3281  C   VAL B 163     3783   4263   3986    349   -177    -72       C  
ATOM   3282  O   VAL B 163      16.897 -19.458 -23.179  1.00 31.62           O  
ANISOU 3282  O   VAL B 163     3758   4276   3979    360   -181    -32       O  
ATOM   3283  CB  VAL B 163      14.778 -17.304 -24.042  1.00 26.71           C  
ANISOU 3283  CB  VAL B 163     3202   3600   3348    315   -170   -125       C  
ATOM   3284  CG1 VAL B 163      14.348 -18.115 -25.241  1.00 26.60           C  
ANISOU 3284  CG1 VAL B 163     3206   3524   3376    339   -165   -125       C  
ATOM   3285  CG2 VAL B 163      14.163 -17.863 -22.766  1.00 30.99           C  
ANISOU 3285  CG2 VAL B 163     3730   4166   3878    313   -175    -94       C  
ATOM   3286  N   GLY B 164      17.607 -18.858 -25.241  1.00 28.68           N  
ANISOU 3286  N   GLY B 164     3409   3856   3631    365   -172    -81       N  
ATOM   3287  CA  GLY B 164      18.359 -20.086 -25.424  1.00 31.76           C  
ANISOU 3287  CA  GLY B 164     3779   4240   4047    397   -172    -45       C  
ATOM   3288  C   GLY B 164      19.382 -20.342 -24.331  1.00 30.01           C  
ANISOU 3288  C   GLY B 164     3519   4081   3802    400   -180     -6       C  
ATOM   3289  O   GLY B 164      19.655 -21.493 -23.999  1.00 31.50           O  
ANISOU 3289  O   GLY B 164     3689   4270   4011    426   -181     37       O  
ATOM   3290  N   LEU B 165      19.957 -19.282 -23.753  1.00 28.13           N  
ANISOU 3290  N   LEU B 165     3268   3898   3522    373   -187    -21       N  
ATOM   3291  CA  LEU B 165      20.923 -19.453 -22.664  1.00 30.97           C  
ANISOU 3291  CA  LEU B 165     3589   4326   3854    372   -196     14       C  
ATOM   3292  C   LEU B 165      20.296 -20.056 -21.414  1.00 32.03           C  
ANISOU 3292  C   LEU B 165     3709   4482   3978    373   -202     53       C  
ATOM   3293  O   LEU B 165      21.021 -20.581 -20.560  1.00 31.34           O  
ANISOU 3293  O   LEU B 165     3586   4444   3876    381   -210     96       O  
ATOM   3294  CB  LEU B 165      21.554 -18.116 -22.282  1.00 25.65           C  
ANISOU 3294  CB  LEU B 165     2905   3706   3134    336   -200    -15       C  
ATOM   3295  CG  LEU B 165      22.481 -17.463 -23.296  1.00 30.13           C  
ANISOU 3295  CG  LEU B 165     3476   4269   3701    332   -197    -47       C  
ATOM   3296  CD1 LEU B 165      22.878 -16.056 -22.817  1.00 28.52           C  
ANISOU 3296  CD1 LEU B 165     3269   4117   3453    291   -199    -80       C  
ATOM   3297  CD2 LEU B 165      23.692 -18.358 -23.540  1.00 32.18           C  
ANISOU 3297  CD2 LEU B 165     3705   4544   3976    361   -199    -12       C  
ATOM   3298  N   MET B 166      18.974 -19.973 -21.277  1.00 32.25           N  
ANISOU 3298  N   MET B 166     3763   4480   4011    364   -199     40       N  
ATOM   3299  CA  MET B 166      18.300 -20.407 -20.067  1.00 33.77           C  
ANISOU 3299  CA  MET B 166     3944   4697   4190    359   -204     72       C  
ATOM   3300  C   MET B 166      17.524 -21.705 -20.223  1.00 34.87           C  
ANISOU 3300  C   MET B 166     4092   4786   4370    388   -199    104       C  
ATOM   3301  O   MET B 166      16.984 -22.202 -19.229  1.00 34.57           O  
ANISOU 3301  O   MET B 166     4043   4766   4324    387   -203    136       O  
ATOM   3302  CB  MET B 166      17.358 -19.300 -19.579  1.00 33.11           C  
ANISOU 3302  CB  MET B 166     3878   4624   4076    324   -203     34       C  
ATOM   3303  CG  MET B 166      18.109 -18.113 -19.013  1.00 35.42           C  
ANISOU 3303  CG  MET B 166     4156   4980   4322    291   -207     11       C  
ATOM   3304  SD  MET B 166      17.019 -16.768 -18.539  1.00 46.71           S  
ANISOU 3304  SD  MET B 166     5609   6416   5722    251   -201    -38       S  
ATOM   3305  CE  MET B 166      17.387 -15.602 -19.860  1.00 41.07           C  
ANISOU 3305  CE  MET B 166     4921   5669   5016    240   -193    -95       C  
ATOM   3306  N   VAL B 167      17.455 -22.281 -21.424  1.00 34.79           N  
ANISOU 3306  N   VAL B 167     4101   4714   4405    412   -190     96       N  
ATOM   3307  CA  VAL B 167      16.610 -23.465 -21.562  1.00 39.79           C  
ANISOU 3307  CA  VAL B 167     4745   5297   5077    435   -184    121       C  
ATOM   3308  C   VAL B 167      17.206 -24.642 -20.798  1.00 38.37           C  
ANISOU 3308  C   VAL B 167     4533   5140   4907    460   -188    184       C  
ATOM   3309  O   VAL B 167      16.475 -25.533 -20.351  1.00 41.09           O  
ANISOU 3309  O   VAL B 167     4879   5464   5270    471   -185    215       O  
ATOM   3310  CB  VAL B 167      16.376 -23.823 -23.043  1.00 39.14           C  
ANISOU 3310  CB  VAL B 167     4690   5144   5038    452   -172     95       C  
ATOM   3311  CG1 VAL B 167      15.995 -22.597 -23.854  1.00 35.92           C  
ANISOU 3311  CG1 VAL B 167     4309   4721   4617    428   -170     38       C  
ATOM   3312  CG2 VAL B 167      17.594 -24.486 -23.613  1.00 39.93           C  
ANISOU 3312  CG2 VAL B 167     4771   5239   5161    479   -169    114       C  
ATOM   3313  N   HIS B 168      18.527 -24.661 -20.613  1.00 37.54           N  
ANISOU 3313  N   HIS B 168     4397   5076   4790    469   -193    204       N  
ATOM   3314  CA  HIS B 168      19.152 -25.759 -19.882  1.00 39.51           C  
ANISOU 3314  CA  HIS B 168     4612   5350   5050    495   -196    267       C  
ATOM   3315  C   HIS B 168      18.681 -25.797 -18.430  1.00 40.80           C  
ANISOU 3315  C   HIS B 168     4758   5564   5181    479   -206    301       C  
ATOM   3316  O   HIS B 168      18.528 -26.876 -17.843  1.00 40.17           O  
ANISOU 3316  O   HIS B 168     4663   5481   5118    499   -206    354       O  
ATOM   3317  CB  HIS B 168      20.676 -25.624 -19.957  1.00 45.93           C  
ANISOU 3317  CB  HIS B 168     5394   6206   5852    504   -201    280       C  
ATOM   3318  CG  HIS B 168      21.406 -26.524 -19.014  1.00 46.80           C  
ANISOU 3318  CG  HIS B 168     5461   6358   5961    526   -207    347       C  
ATOM   3319  ND1 HIS B 168      21.410 -27.896 -19.152  1.00 49.60           N  
ANISOU 3319  ND1 HIS B 168     5809   6672   6364    564   -199    392       N  
ATOM   3320  CD2 HIS B 168      22.120 -26.254 -17.896  1.00 49.02           C  
ANISOU 3320  CD2 HIS B 168     5705   6720   6199    514   -221    378       C  
ATOM   3321  CE1 HIS B 168      22.114 -28.431 -18.169  1.00 55.01           C  
ANISOU 3321  CE1 HIS B 168     6453   7410   7037    577   -208    452       C  
ATOM   3322  NE2 HIS B 168      22.554 -27.457 -17.392  1.00 52.52           N  
ANISOU 3322  NE2 HIS B 168     6118   7171   6665    547   -222    444       N  
ATOM   3323  N   GLY B 169      18.447 -24.631 -17.834  1.00 36.68           N  
ANISOU 3323  N   GLY B 169     4238   5089   4611    442   -214    271       N  
ATOM   3324  CA  GLY B 169      18.017 -24.552 -16.459  1.00 37.69           C  
ANISOU 3324  CA  GLY B 169     4349   5270   4702    422   -223    297       C  
ATOM   3325  C   GLY B 169      16.524 -24.553 -16.220  1.00 38.35           C  
ANISOU 3325  C   GLY B 169     4459   5322   4788    409   -218    284       C  
ATOM   3326  O   GLY B 169      16.100 -24.516 -15.057  1.00 36.65           O  
ANISOU 3326  O   GLY B 169     4230   5152   4543    392   -225    305       O  
ATOM   3327  N   LEU B 170      15.710 -24.584 -17.271  1.00 37.45           N  
ANISOU 3327  N   LEU B 170     4382   5137   4709    415   -208    249       N  
ATOM   3328  CA  LEU B 170      14.254 -24.587 -17.103  1.00 37.91           C  
ANISOU 3328  CA  LEU B 170     4466   5165   4773    403   -203    236       C  
ATOM   3329  C   LEU B 170      13.828 -25.875 -16.416  1.00 38.05           C  
ANISOU 3329  C   LEU B 170     4472   5176   4810    422   -203    293       C  
ATOM   3330  O   LEU B 170      14.102 -26.957 -16.947  1.00 43.09           O  
ANISOU 3330  O   LEU B 170     5109   5773   5492    454   -197    322       O  
ATOM   3331  CB  LEU B 170      13.555 -24.463 -18.457  1.00 39.90           C  
ANISOU 3331  CB  LEU B 170     4756   5342   5060    409   -192    191       C  
ATOM   3332  CG  LEU B 170      13.276 -23.073 -19.044  1.00 39.78           C  
ANISOU 3332  CG  LEU B 170     4765   5323   5026    383   -190    129       C  
ATOM   3333  CD1 LEU B 170      12.433 -23.187 -20.306  1.00 37.73           C  
ANISOU 3333  CD1 LEU B 170     4541   4990   4804    391   -180     97       C  
ATOM   3334  CD2 LEU B 170      12.602 -22.142 -18.039  1.00 37.29           C  
ANISOU 3334  CD2 LEU B 170     4450   5050   4668    349   -194    112       C  
ATOM   3335  N   PRO B 171      13.178 -25.818 -15.249  1.00 38.93           N  
ANISOU 3335  N   PRO B 171     4574   5326   4892    403   -209    311       N  
ATOM   3336  CA  PRO B 171      12.816 -27.056 -14.543  1.00 40.97           C  
ANISOU 3336  CA  PRO B 171     4819   5581   5167    420   -209    370       C  
ATOM   3337  C   PRO B 171      11.881 -27.931 -15.364  1.00 40.45           C  
ANISOU 3337  C   PRO B 171     4782   5433   5153    439   -197    369       C  
ATOM   3338  O   PRO B 171      10.973 -27.444 -16.042  1.00 39.91           O  
ANISOU 3338  O   PRO B 171     4746   5325   5094    427   -190    322       O  
ATOM   3339  CB  PRO B 171      12.145 -26.547 -13.262  1.00 38.55           C  
ANISOU 3339  CB  PRO B 171     4503   5332   4814    388   -217    374       C  
ATOM   3340  CG  PRO B 171      12.811 -25.227 -13.018  1.00 36.73           C  
ANISOU 3340  CG  PRO B 171     4262   5158   4536    360   -223    337       C  
ATOM   3341  CD  PRO B 171      12.981 -24.632 -14.398  1.00 40.16           C  
ANISOU 3341  CD  PRO B 171     4724   5542   4993    365   -216    284       C  
ATOM   3342  N   LEU B 172      12.108 -29.247 -15.284  1.00 44.00           N  
ANISOU 3342  N   LEU B 172     5219   5859   5639    469   -193    422       N  
ATOM   3343  CA  LEU B 172      11.485 -30.150 -16.243  1.00 47.22           C  
ANISOU 3343  CA  LEU B 172     5654   6186   6103    490   -179    419       C  
ATOM   3344  C   LEU B 172      10.991 -31.465 -15.652  1.00 53.43           C  
ANISOU 3344  C   LEU B 172     6433   6952   6917    507   -174    476       C  
ATOM   3345  O   LEU B 172      10.866 -32.436 -16.403  1.00 60.78           O  
ANISOU 3345  O   LEU B 172     7377   7819   7899    531   -161    486       O  
ATOM   3346  CB  LEU B 172      12.457 -30.502 -17.376  1.00 45.97           C  
ANISOU 3346  CB  LEU B 172     5497   5990   5981    518   -171    412       C  
ATOM   3347  CG  LEU B 172      12.487 -29.659 -18.646  1.00 46.40           C  
ANISOU 3347  CG  LEU B 172     5577   6012   6040    510   -166    347       C  
ATOM   3348  CD1 LEU B 172      13.259 -30.423 -19.719  1.00 46.24           C  
ANISOU 3348  CD1 LEU B 172     5558   5945   6067    541   -154    351       C  
ATOM   3349  CD2 LEU B 172      11.077 -29.272 -19.110  1.00 39.89           C  
ANISOU 3349  CD2 LEU B 172     4788   5148   5219    490   -160    303       C  
ATOM   3350  N   ASP B 173      10.736 -31.547 -14.343  1.00 53.01           N  
ANISOU 3350  N   ASP B 173     6358   6951   6831    494   -183    515       N  
ATOM   3351  CA  ASP B 173      10.012 -32.683 -13.763  1.00 57.03           C  
ANISOU 3351  CA  ASP B 173     6865   7439   7363    503   -178    564       C  
ATOM   3352  C   ASP B 173      10.683 -34.020 -14.073  1.00 56.48           C  
ANISOU 3352  C   ASP B 173     6784   7330   7347    543   -169    615       C  
ATOM   3353  O   ASP B 173      10.488 -34.585 -15.157  1.00 54.79           O  
ANISOU 3353  O   ASP B 173     6593   7042   7181    561   -154    597       O  
ATOM   3354  CB  ASP B 173       8.567 -32.686 -14.275  1.00 55.82           C  
ANISOU 3354  CB  ASP B 173     6750   7232   7228    490   -168    526       C  
ATOM   3355  CG  ASP B 173       7.695 -33.770 -13.639  1.00 60.13           C  
ANISOU 3355  CG  ASP B 173     7296   7757   7794    494   -163    572       C  
ATOM   3356  OD1 ASP B 173       8.194 -34.710 -12.972  1.00 60.28           O  
ANISOU 3356  OD1 ASP B 173     7289   7789   7825    513   -164    637       O  
ATOM   3357  OD2 ASP B 173       6.465 -33.668 -13.831  1.00 61.56           O  
ANISOU 3357  OD2 ASP B 173     7502   7908   7979    477   -158    544       O  
ATOM   3358  N   PRO B 174      11.400 -34.598 -13.120  1.00 58.21           N  
ANISOU 3358  N   PRO B 174     6967   7593   7558    557   -176    681       N  
ATOM   3359  CA  PRO B 174      12.244 -35.765 -13.424  1.00 59.79           C  
ANISOU 3359  CA  PRO B 174     7150   7759   7807    597   -166    730       C  
ATOM   3360  C   PRO B 174      11.484 -37.059 -13.688  1.00 59.71           C  
ANISOU 3360  C   PRO B 174     7158   7675   7854    617   -149    757       C  
ATOM   3361  O   PRO B 174      11.936 -38.132 -13.281  1.00 68.99           O  
ANISOU 3361  O   PRO B 174     8312   8843   9060    644   -144    822       O  
ATOM   3362  CB  PRO B 174      13.111 -35.888 -12.165  1.00 57.09           C  
ANISOU 3362  CB  PRO B 174     6763   7498   7432    602   -181    795       C  
ATOM   3363  CG  PRO B 174      12.219 -35.378 -11.077  1.00 59.71           C  
ANISOU 3363  CG  PRO B 174     7092   7881   7713    566   -193    796       C  
ATOM   3364  CD  PRO B 174      11.426 -34.248 -11.690  1.00 58.19           C  
ANISOU 3364  CD  PRO B 174     6935   7674   7501    536   -192    715       C  
ATOM   3365  N   ALA B 175      10.340 -36.985 -14.354  1.00 58.63           N  
ANISOU 3365  N   ALA B 175     7058   7484   7733    602   -139    711       N  
ATOM   3366  CA  ALA B 175       9.592 -38.186 -14.703  1.00 58.86           C  
ANISOU 3366  CA  ALA B 175     7107   7439   7818    617   -120    729       C  
ATOM   3367  C   ALA B 175       9.198 -38.131 -16.170  1.00 58.51           C  
ANISOU 3367  C   ALA B 175     7099   7322   7809    618   -105    666       C  
ATOM   3368  O   ALA B 175       9.097 -39.161 -16.846  1.00 56.87           O  
ANISOU 3368  O   ALA B 175     6904   7046   7658    639    -86    674       O  
ATOM   3369  CB  ALA B 175       8.352 -38.328 -13.819  1.00 57.11           C  
ANISOU 3369  CB  ALA B 175     6892   7230   7578    593   -124    746       C  
ATOM   3370  N   THR B 176       8.971 -36.918 -16.658  1.00 56.69           N  
ANISOU 3370  N   THR B 176     6886   7110   7546    593   -113    603       N  
ATOM   3371  CA  THR B 176       8.641 -36.668 -18.048  1.00 54.67           C  
ANISOU 3371  CA  THR B 176     6662   6797   7314    591   -101    541       C  
ATOM   3372  C   THR B 176       9.758 -35.932 -18.768  1.00 51.20           C  
ANISOU 3372  C   THR B 176     6217   6373   6865    598   -105    509       C  
ATOM   3373  O   THR B 176       9.611 -35.608 -19.950  1.00 49.79           O  
ANISOU 3373  O   THR B 176     6062   6154   6700    594    -97    456       O  
ATOM   3374  CB  THR B 176       7.341 -35.862 -18.128  1.00 53.41           C  
ANISOU 3374  CB  THR B 176     6529   6638   7127    557   -106    492       C  
ATOM   3375  OG1 THR B 176       7.449 -34.725 -17.265  1.00 54.59           O  
ANISOU 3375  OG1 THR B 176     6664   6862   7217    534   -124    486       O  
ATOM   3376  CG2 THR B 176       6.161 -36.709 -17.671  1.00 52.41           C  
ANISOU 3376  CG2 THR B 176     6413   6483   7019    550    -98    517       C  
ATOM   3377  N   ALA B 177      10.873 -35.679 -18.079  1.00 52.48           N  
ANISOU 3377  N   ALA B 177     6345   6593   7001    607   -117    541       N  
ATOM   3378  CA  ALA B 177      11.935 -34.837 -18.616  1.00 54.56           C  
ANISOU 3378  CA  ALA B 177     6600   6883   7246    608   -123    511       C  
ATOM   3379  C   ALA B 177      12.437 -35.352 -19.957  1.00 53.98           C  
ANISOU 3379  C   ALA B 177     6540   6748   7223    632   -106    489       C  
ATOM   3380  O   ALA B 177      12.596 -34.584 -20.911  1.00 51.01           O  
ANISOU 3380  O   ALA B 177     6180   6361   6840    623   -105    434       O  
ATOM   3381  CB  ALA B 177      13.086 -34.749 -17.611  1.00 48.16           C  
ANISOU 3381  CB  ALA B 177     5748   6144   6408    618   -137    560       C  
ATOM   3382  N   GLU B 178      12.673 -36.661 -20.050  1.00 53.25           N  
ANISOU 3382  N   GLU B 178     6440   6611   7181    663    -91    531       N  
ATOM   3383  CA  GLU B 178      13.267 -37.214 -21.261  1.00 54.10           C  
ANISOU 3383  CA  GLU B 178     6555   6662   7336    687    -73    512       C  
ATOM   3384  C   GLU B 178      12.281 -37.190 -22.426  1.00 53.72           C  
ANISOU 3384  C   GLU B 178     6549   6552   7312    673    -59    453       C  
ATOM   3385  O   GLU B 178      12.671 -36.912 -23.567  1.00 52.33           O  
ANISOU 3385  O   GLU B 178     6385   6352   7148    676    -51    409       O  
ATOM   3386  CB  GLU B 178      13.772 -38.633 -20.983  1.00 57.22           C  
ANISOU 3386  CB  GLU B 178     6932   7027   7783    724    -58    574       C  
ATOM   3387  CG  GLU B 178      15.071 -39.014 -21.693  1.00 59.00           C  
ANISOU 3387  CG  GLU B 178     7140   7235   8041    757    -46    579       C  
ATOM   3388  CD  GLU B 178      16.248 -38.106 -21.348  1.00 65.66           C  
ANISOU 3388  CD  GLU B 178     7955   8153   8841    757    -65    583       C  
ATOM   3389  OE1 GLU B 178      16.306 -37.589 -20.209  1.00 62.73           O  
ANISOU 3389  OE1 GLU B 178     7562   7850   8423    743    -85    612       O  
ATOM   3390  OE2 GLU B 178      17.127 -37.919 -22.222  1.00 69.83           O  
ANISOU 3390  OE2 GLU B 178     8479   8672   9381    769    -59    557       O  
ATOM   3391  N   VAL B 179      10.997 -37.448 -22.162  1.00 50.52           N  
ANISOU 3391  N   VAL B 179     6162   6124   6908    656    -56    452       N  
ATOM   3392  CA  VAL B 179      10.021 -37.472 -23.248  1.00 52.46           C  
ANISOU 3392  CA  VAL B 179     6444   6313   7174    642    -44    399       C  
ATOM   3393  C   VAL B 179       9.719 -36.059 -23.736  1.00 52.94           C  
ANISOU 3393  C   VAL B 179     6521   6401   7192    613    -57    339       C  
ATOM   3394  O   VAL B 179       9.599 -35.821 -24.945  1.00 51.87           O  
ANISOU 3394  O   VAL B 179     6407   6232   7070    608    -48    290       O  
ATOM   3395  CB  VAL B 179       8.743 -38.211 -22.812  1.00 51.85           C  
ANISOU 3395  CB  VAL B 179     6382   6205   7114    632    -36    416       C  
ATOM   3396  CG1 VAL B 179       7.534 -37.689 -23.569  1.00 51.88           C  
ANISOU 3396  CG1 VAL B 179     6418   6183   7109    603    -34    358       C  
ATOM   3397  CG2 VAL B 179       8.899 -39.701 -23.051  1.00 53.19           C  
ANISOU 3397  CG2 VAL B 179     6551   6313   7346    659    -13    450       C  
ATOM   3398  N   THR B 180       9.589 -35.098 -22.813  1.00 52.45           N  
ANISOU 3398  N   THR B 180     6449   6401   7079    593    -76    343       N  
ATOM   3399  CA  THR B 180       9.399 -33.713 -23.236  1.00 51.07           C  
ANISOU 3399  CA  THR B 180     6287   6252   6864    568    -87    289       C  
ATOM   3400  C   THR B 180      10.659 -33.165 -23.901  1.00 48.25           C  
ANISOU 3400  C   THR B 180     5921   5911   6503    578    -89    269       C  
ATOM   3401  O   THR B 180      10.571 -32.416 -24.881  1.00 49.62           O  
ANISOU 3401  O   THR B 180     6112   6072   6669    566    -88    218       O  
ATOM   3402  CB  THR B 180       8.970 -32.834 -22.054  1.00 48.05           C  
ANISOU 3402  CB  THR B 180     5896   5931   6430    544   -105    297       C  
ATOM   3403  OG1 THR B 180      10.017 -32.780 -21.085  1.00 52.09           O  
ANISOU 3403  OG1 THR B 180     6374   6499   6920    554   -116    339       O  
ATOM   3404  CG2 THR B 180       7.717 -33.389 -21.397  1.00 46.51           C  
ANISOU 3404  CG2 THR B 180     5709   5722   6240    534   -103    317       C  
ATOM   3405  N   LYS B 181      11.842 -33.528 -23.394  1.00 52.80           N  
ANISOU 3405  N   LYS B 181     6466   6514   7081    600    -92    311       N  
ATOM   3406  CA  LYS B 181      13.072 -33.139 -24.078  1.00 52.83           C  
ANISOU 3406  CA  LYS B 181     6460   6530   7085    611    -92    293       C  
ATOM   3407  C   LYS B 181      13.070 -33.648 -25.512  1.00 52.88           C  
ANISOU 3407  C   LYS B 181     6488   6471   7135    623    -73    260       C  
ATOM   3408  O   LYS B 181      13.491 -32.941 -26.435  1.00 50.72           O  
ANISOU 3408  O   LYS B 181     6222   6197   6853    617    -72    217       O  
ATOM   3409  CB  LYS B 181      14.298 -33.669 -23.328  1.00 51.63           C  
ANISOU 3409  CB  LYS B 181     6270   6412   6936    637    -95    349       C  
ATOM   3410  CG  LYS B 181      14.898 -32.713 -22.304  1.00 51.08           C  
ANISOU 3410  CG  LYS B 181     6174   6423   6811    622   -116    363       C  
ATOM   3411  CD  LYS B 181      16.136 -33.318 -21.646  1.00 53.23           C  
ANISOU 3411  CD  LYS B 181     6406   6730   7088    650   -119    421       C  
ATOM   3412  CE  LYS B 181      16.263 -32.873 -20.199  1.00 54.36           C  
ANISOU 3412  CE  LYS B 181     6523   6950   7183    635   -138    457       C  
ATOM   3413  NZ  LYS B 181      17.514 -33.360 -19.547  1.00 50.11           N  
ANISOU 3413  NZ  LYS B 181     5942   6454   6644    659   -143    514       N  
ATOM   3414  N   ALA B 182      12.568 -34.865 -25.715  1.00 54.29           N  
ANISOU 3414  N   ALA B 182     6675   6593   7359    638    -56    277       N  
ATOM   3415  CA  ALA B 182      12.528 -35.479 -27.031  1.00 51.75           C  
ANISOU 3415  CA  ALA B 182     6372   6208   7082    648    -35    246       C  
ATOM   3416  C   ALA B 182      11.404 -34.945 -27.900  1.00 54.55           C  
ANISOU 3416  C   ALA B 182     6761   6537   7430    621    -33    190       C  
ATOM   3417  O   ALA B 182      11.447 -35.133 -29.117  1.00 57.53           O  
ANISOU 3417  O   ALA B 182     7154   6873   7831    622    -19    153       O  
ATOM   3418  CB  ALA B 182      12.386 -36.993 -26.900  1.00 52.85           C  
ANISOU 3418  CB  ALA B 182     6509   6297   7275    672    -15    285       C  
ATOM   3419  N   GLU B 183      10.389 -34.311 -27.318  1.00 51.90           N  
ANISOU 3419  N   GLU B 183     6436   6223   7061    595    -46    183       N  
ATOM   3420  CA  GLU B 183       9.355 -33.709 -28.149  1.00 53.21           C  
ANISOU 3420  CA  GLU B 183     6631   6369   7218    570    -45    131       C  
ATOM   3421  C   GLU B 183       9.782 -32.335 -28.654  1.00 53.94           C  
ANISOU 3421  C   GLU B 183     6727   6496   7274    555    -57     91       C  
ATOM   3422  O   GLU B 183       9.456 -31.960 -29.785  1.00 53.15           O  
ANISOU 3422  O   GLU B 183     6646   6372   7177    544    -52     46       O  
ATOM   3423  CB  GLU B 183       8.038 -33.620 -27.373  1.00 52.47           C  
ANISOU 3423  CB  GLU B 183     6547   6282   7108    550    -52    140       C  
ATOM   3424  CG  GLU B 183       6.911 -32.906 -28.106  1.00 52.99           C  
ANISOU 3424  CG  GLU B 183     6640   6334   7160    524    -53     90       C  
ATOM   3425  CD  GLU B 183       6.482 -33.616 -29.387  1.00 60.37           C  
ANISOU 3425  CD  GLU B 183     7596   7210   8133    525    -35     61       C  
ATOM   3426  OE1 GLU B 183       6.840 -34.803 -29.564  1.00 61.25           O  
ANISOU 3426  OE1 GLU B 183     7703   7284   8286    545    -18     81       O  
ATOM   3427  OE2 GLU B 183       5.780 -32.988 -30.215  1.00 59.24           O  
ANISOU 3427  OE2 GLU B 183     7471   7057   7978    505    -36     17       O  
ATOM   3428  N   PHE B 184      10.523 -31.586 -27.835  1.00 49.96           N  
ANISOU 3428  N   PHE B 184     6201   6047   6734    554    -72    108       N  
ATOM   3429  CA  PHE B 184      11.002 -30.272 -28.244  1.00 51.47           C  
ANISOU 3429  CA  PHE B 184     6394   6271   6891    539    -83     72       C  
ATOM   3430  C   PHE B 184      11.981 -30.398 -29.410  1.00 55.39           C  
ANISOU 3430  C   PHE B 184     6890   6748   7409    553    -73     50       C  
ATOM   3431  O   PHE B 184      11.756 -29.851 -30.497  1.00 49.42           O  
ANISOU 3431  O   PHE B 184     6152   5973   6650    541    -70      6       O  
ATOM   3432  CB  PHE B 184      11.640 -29.566 -27.045  1.00 47.25           C  
ANISOU 3432  CB  PHE B 184     5835   5801   6316    534    -99     96       C  
ATOM   3433  CG  PHE B 184      10.643 -28.897 -26.126  1.00 42.82           C  
ANISOU 3433  CG  PHE B 184     5280   5269   5722    510   -110     96       C  
ATOM   3434  CD1 PHE B 184       9.625 -28.102 -26.638  1.00 39.78           C  
ANISOU 3434  CD1 PHE B 184     4919   4870   5324    488   -112     54       C  
ATOM   3435  CD2 PHE B 184      10.726 -29.065 -24.753  1.00 45.62           C  
ANISOU 3435  CD2 PHE B 184     5612   5665   6057    510   -119    138       C  
ATOM   3436  CE1 PHE B 184       8.720 -27.481 -25.788  1.00 39.80           C  
ANISOU 3436  CE1 PHE B 184     4926   4899   5297    467   -120     52       C  
ATOM   3437  CE2 PHE B 184       9.816 -28.452 -23.899  1.00 38.25           C  
ANISOU 3437  CE2 PHE B 184     4682   4758   5091    487   -128    136       C  
ATOM   3438  CZ  PHE B 184       8.828 -27.661 -24.412  1.00 36.58           C  
ANISOU 3438  CZ  PHE B 184     4496   4532   4870    466   -128     92       C  
ATOM   3439  N   VAL B 185      13.081 -31.126 -29.205  1.00 52.35           N  
ANISOU 3439  N   VAL B 185     6482   6366   7044    579    -67     83       N  
ATOM   3440  CA  VAL B 185      13.793 -31.664 -30.353  1.00 57.84           C  
ANISOU 3440  CA  VAL B 185     7178   7025   7772    596    -52     66       C  
ATOM   3441  C   VAL B 185      12.785 -32.504 -31.117  1.00 58.90           C  
ANISOU 3441  C   VAL B 185     7338   7099   7944    595    -35     48       C  
ATOM   3442  O   VAL B 185      11.890 -33.103 -30.514  1.00 61.53           O  
ANISOU 3442  O   VAL B 185     7676   7414   8288    593    -32     70       O  
ATOM   3443  CB  VAL B 185      15.031 -32.464 -29.908  1.00 57.14           C  
ANISOU 3443  CB  VAL B 185     7059   6946   7705    628    -46    110       C  
ATOM   3444  CG1 VAL B 185      14.653 -33.841 -29.409  1.00 58.36           C  
ANISOU 3444  CG1 VAL B 185     7209   7065   7900    648    -34    152       C  
ATOM   3445  CG2 VAL B 185      16.032 -32.577 -31.043  1.00 64.68           C  
ANISOU 3445  CG2 VAL B 185     8011   7885   8680    642    -34     86       C  
ATOM   3446  N   ARG B 186      12.876 -32.479 -32.450  1.00 60.14           N  
ANISOU 3446  N   ARG B 186     7509   7224   8116    592    -23      6       N  
ATOM   3447  CA  ARG B 186      11.898 -33.044 -33.386  1.00 60.95           C  
ANISOU 3447  CA  ARG B 186     7638   7274   8246    583     -7    -23       C  
ATOM   3448  C   ARG B 186      10.897 -31.975 -33.798  1.00 61.27           C  
ANISOU 3448  C   ARG B 186     7700   7324   8254    552    -19    -62       C  
ATOM   3449  O   ARG B 186      10.688 -31.757 -34.997  1.00 63.94           O  
ANISOU 3449  O   ARG B 186     8056   7643   8596    541    -12   -104       O  
ATOM   3450  CB  ARG B 186      11.157 -34.273 -32.836  1.00 60.48           C  
ANISOU 3450  CB  ARG B 186     7581   7177   8220    592      4      8       C  
ATOM   3451  CG  ARG B 186       9.865 -34.590 -33.562  1.00 61.09           C  
ANISOU 3451  CG  ARG B 186     7686   7212   8311    573     15    -24       C  
ATOM   3452  CD  ARG B 186       8.668 -34.316 -32.690  1.00 59.90           C  
ANISOU 3452  CD  ARG B 186     7544   7076   8140    555      2    -11       C  
ATOM   3453  NE  ARG B 186       7.433 -34.752 -33.327  1.00 61.17           N  
ANISOU 3453  NE  ARG B 186     7728   7197   8317    538     13    -36       N  
ATOM   3454  CZ  ARG B 186       6.566 -33.934 -33.912  1.00 64.55           C  
ANISOU 3454  CZ  ARG B 186     8174   7632   8721    513      5    -74       C  
ATOM   3455  NH1 ARG B 186       6.786 -32.630 -33.987  1.00 64.11           N  
ANISOU 3455  NH1 ARG B 186     8117   7615   8625    501    -11    -93       N  
ATOM   3456  NH2 ARG B 186       5.454 -34.438 -34.440  1.00 69.40           N  
ANISOU 3456  NH2 ARG B 186     8807   8211   9351    497     16    -94       N  
ATOM   3457  N   ARG B 187      10.265 -31.306 -32.827  1.00 57.19           N  
ANISOU 3457  N   ARG B 187     7184   6840   7706    538    -35    -49       N  
ATOM   3458  CA  ARG B 187       9.556 -30.074 -33.162  1.00 58.84           C  
ANISOU 3458  CA  ARG B 187     7409   7067   7881    511    -47    -84       C  
ATOM   3459  C   ARG B 187      10.512 -29.062 -33.785  1.00 55.05           C  
ANISOU 3459  C   ARG B 187     6925   6613   7378    507    -53   -110       C  
ATOM   3460  O   ARG B 187      10.196 -28.441 -34.804  1.00 55.56           O  
ANISOU 3460  O   ARG B 187     7006   6669   7435    492    -53   -149       O  
ATOM   3461  CB  ARG B 187       8.867 -29.485 -31.924  1.00 55.38           C  
ANISOU 3461  CB  ARG B 187     6968   6663   7411    498    -62    -65       C  
ATOM   3462  CG  ARG B 187       7.484 -30.078 -31.645  1.00 57.63           C  
ANISOU 3462  CG  ARG B 187     7266   6921   7709    490    -58    -59       C  
ATOM   3463  CD  ARG B 187       7.096 -30.026 -30.162  1.00 56.21           C  
ANISOU 3463  CD  ARG B 187     7075   6773   7510    487    -69    -23       C  
ATOM   3464  NE  ARG B 187       6.740 -28.692 -29.699  1.00 50.07           N  
ANISOU 3464  NE  ARG B 187     6299   6036   6690    467    -84    -38       N  
ATOM   3465  CZ  ARG B 187       5.662 -28.401 -28.980  1.00 48.25           C  
ANISOU 3465  CZ  ARG B 187     6074   5816   6442    452    -90    -34       C  
ATOM   3466  NH1 ARG B 187       4.798 -29.334 -28.609  1.00 48.06           N  
ANISOU 3466  NH1 ARG B 187     6054   5769   6437    453    -84    -14       N  
ATOM   3467  NH2 ARG B 187       5.451 -27.142 -28.614  1.00 42.62           N  
ANISOU 3467  NH2 ARG B 187     5362   5139   5693    434   -102    -51       N  
ATOM   3468  N   ALA B 188      11.702 -28.914 -33.207  1.00 56.17           N  
ANISOU 3468  N   ALA B 188     7043   6787   7510    521    -59    -87       N  
ATOM   3469  CA  ALA B 188      12.734 -28.030 -33.734  1.00 57.54           C  
ANISOU 3469  CA  ALA B 188     7210   6988   7664    518    -64   -108       C  
ATOM   3470  C   ALA B 188      13.597 -28.697 -34.803  1.00 63.86           C  
ANISOU 3470  C   ALA B 188     8008   7762   8496    535    -48   -120       C  
ATOM   3471  O   ALA B 188      14.761 -28.304 -34.976  1.00 63.53           O  
ANISOU 3471  O   ALA B 188     7951   7745   8444    541    -50   -122       O  
ATOM   3472  CB  ALA B 188      13.613 -27.519 -32.593  1.00 53.29           C  
ANISOU 3472  CB  ALA B 188     6647   6502   7098    522    -77    -80       C  
ATOM   3473  N   GLY B 189      13.055 -29.692 -35.513  1.00 65.40           N  
ANISOU 3473  N   GLY B 189     8215   7907   8726    540    -31   -130       N  
ATOM   3474  CA  GLY B 189      13.767 -30.456 -36.527  1.00 64.57           C  
ANISOU 3474  CA  GLY B 189     8109   7772   8654    556    -13   -144       C  
ATOM   3475  C   GLY B 189      15.253 -30.629 -36.287  1.00 68.50           C  
ANISOU 3475  C   GLY B 189     8579   8290   9157    579    -11   -122       C  
ATOM   3476  O   GLY B 189      16.065 -30.326 -37.168  1.00 74.63           O  
ANISOU 3476  O   GLY B 189     9352   9072   9932    580     -6   -147       O  
ATOM   3477  N   LEU B 190      15.626 -31.100 -35.101  1.00 67.06           N  
ANISOU 3477  N   LEU B 190     8376   8125   8980    597    -15    -75       N  
ATOM   3478  CA  LEU B 190      17.015 -31.138 -34.663  1.00 67.82           C  
ANISOU 3478  CA  LEU B 190     8441   8253   9073    618    -18    -49       C  
ATOM   3479  C   LEU B 190      17.393 -32.574 -34.302  1.00 66.90           C  
ANISOU 3479  C   LEU B 190     8308   8107   9002    651     -1     -9       C  
ATOM   3480  O   LEU B 190      16.594 -33.499 -34.456  1.00 66.23           O  
ANISOU 3480  O   LEU B 190     8238   7975   8951    655     13     -6       O  
ATOM   3481  CB  LEU B 190      17.217 -30.158 -33.502  1.00 69.24           C  
ANISOU 3481  CB  LEU B 190     8607   8492   9207    607    -41    -28       C  
ATOM   3482  CG  LEU B 190      18.553 -29.435 -33.343  1.00 68.39           C  
ANISOU 3482  CG  LEU B 190     8475   8435   9074    610    -50    -24       C  
ATOM   3483  CD1 LEU B 190      18.998 -28.842 -34.659  1.00 66.51           C  
ANISOU 3483  CD1 LEU B 190     8248   8191   8833    600    -44    -71       C  
ATOM   3484  CD2 LEU B 190      18.355 -28.329 -32.336  1.00 66.95           C  
ANISOU 3484  CD2 LEU B 190     8289   8306   8845    588    -71    -17       C  
ATOM   3485  N   SER B 191      18.629 -32.767 -33.828  1.00 67.72           N  
ANISOU 3485  N   SER B 191     8383   8239   9110    674     -3     23       N  
ATOM   3486  CA  SER B 191      19.186 -34.108 -33.665  1.00 68.34           C  
ANISOU 3486  CA  SER B 191     8443   8287   9236    709     16     59       C  
ATOM   3487  C   SER B 191      19.518 -34.500 -32.229  1.00 68.86           C  
ANISOU 3487  C   SER B 191     8480   8384   9299    728      6    123       C  
ATOM   3488  O   SER B 191      19.416 -35.684 -31.896  1.00 71.53           O  
ANISOU 3488  O   SER B 191     8812   8688   9679    752     20    158       O  
ATOM   3489  CB  SER B 191      20.449 -34.260 -34.522  1.00 69.53           C  
ANISOU 3489  CB  SER B 191     8578   8435   9404    728     29     45       C  
ATOM   3490  OG  SER B 191      21.484 -33.427 -34.034  1.00 72.55           O  
ANISOU 3490  OG  SER B 191     8936   8880   9751    729     11     58       O  
ATOM   3491  N   SER B 192      19.931 -33.567 -31.378  1.00 67.17           N  
ANISOU 3491  N   SER B 192     8249   8235   9039    717    -17    138       N  
ATOM   3492  CA  SER B 192      20.179 -33.857 -29.972  1.00 65.96           C  
ANISOU 3492  CA  SER B 192     8068   8119   8875    730    -28    198       C  
ATOM   3493  C   SER B 192      19.520 -32.778 -29.128  1.00 66.15           C  
ANISOU 3493  C   SER B 192     8097   8190   8845    698    -52    194       C  
ATOM   3494  O   SER B 192      18.957 -31.816 -29.650  1.00 64.41           O  
ANISOU 3494  O   SER B 192     7902   7973   8600    669    -58    147       O  
ATOM   3495  CB  SER B 192      21.677 -33.927 -29.656  1.00 65.38           C  
ANISOU 3495  CB  SER B 192     7956   8087   8800    754    -31    230       C  
ATOM   3496  OG  SER B 192      22.212 -32.628 -29.474  1.00 67.86           O  
ANISOU 3496  OG  SER B 192     8260   8463   9061    732    -51    211       O  
ATOM   3497  N   TRP B 193      19.576 -32.949 -27.807  1.00 63.30           N  
ANISOU 3497  N   TRP B 193     7714   7869   8469    702    -64    245       N  
ATOM   3498  CA  TRP B 193      19.141 -31.881 -26.916  1.00 62.96           C  
ANISOU 3498  CA  TRP B 193     7670   7879   8371    672    -85    242       C  
ATOM   3499  C   TRP B 193      20.222 -30.820 -26.738  1.00 65.29           C  
ANISOU 3499  C   TRP B 193     7945   8239   8625    662    -99    233       C  
ATOM   3500  O   TRP B 193      19.897 -29.674 -26.406  1.00 63.19           O  
ANISOU 3500  O   TRP B 193     7686   8010   8313    631   -114    209       O  
ATOM   3501  CB  TRP B 193      18.717 -32.465 -25.558  1.00 62.33           C  
ANISOU 3501  CB  TRP B 193     7575   7820   8288    677    -92    298       C  
ATOM   3502  CG  TRP B 193      18.279 -31.445 -24.515  1.00 59.10           C  
ANISOU 3502  CG  TRP B 193     7163   7470   7823    646   -113    298       C  
ATOM   3503  CD1 TRP B 193      18.983 -31.056 -23.409  1.00 59.13           C  
ANISOU 3503  CD1 TRP B 193     7134   7545   7789    642   -128    332       C  
ATOM   3504  CD2 TRP B 193      17.038 -30.716 -24.473  1.00 55.80           C  
ANISOU 3504  CD2 TRP B 193     6774   7047   7381    615   -118    263       C  
ATOM   3505  NE1 TRP B 193      18.268 -30.123 -22.692  1.00 59.60           N  
ANISOU 3505  NE1 TRP B 193     7201   7642   7802    609   -142    317       N  
ATOM   3506  CE2 TRP B 193      17.073 -29.897 -23.323  1.00 55.09           C  
ANISOU 3506  CE2 TRP B 193     6668   7024   7241    593   -136    276       C  
ATOM   3507  CE3 TRP B 193      15.911 -30.666 -25.300  1.00 52.58           C  
ANISOU 3507  CE3 TRP B 193     6402   6586   6990    602   -109    223       C  
ATOM   3508  CZ2 TRP B 193      16.026 -29.045 -22.980  1.00 49.48           C  
ANISOU 3508  CZ2 TRP B 193     5977   6325   6498    561   -143    248       C  
ATOM   3509  CZ3 TRP B 193      14.875 -29.817 -24.956  1.00 52.03           C  
ANISOU 3509  CZ3 TRP B 193     6350   6530   6888    572   -118    198       C  
ATOM   3510  CH2 TRP B 193      14.940 -29.020 -23.806  1.00 49.96           C  
ANISOU 3510  CH2 TRP B 193     6073   6332   6579    552   -135    210       C  
ATOM   3511  N   ASP B 194      21.491 -31.169 -26.986  1.00 66.94           N  
ANISOU 3511  N   ASP B 194     8128   8460   8848    686    -94    250       N  
ATOM   3512  CA  ASP B 194      22.588 -30.208 -26.859  1.00 66.01           C  
ANISOU 3512  CA  ASP B 194     7987   8403   8690    676   -107    241       C  
ATOM   3513  C   ASP B 194      22.453 -29.088 -27.885  1.00 65.94           C  
ANISOU 3513  C   ASP B 194     8005   8387   8662    649   -107    177       C  
ATOM   3514  O   ASP B 194      22.406 -27.902 -27.532  1.00 63.87           O  
ANISOU 3514  O   ASP B 194     7746   8169   8354    619   -122    155       O  
ATOM   3515  CB  ASP B 194      23.925 -30.932 -27.005  1.00 67.30           C  
ANISOU 3515  CB  ASP B 194     8117   8574   8880    711    -99    273       C  
ATOM   3516  CG  ASP B 194      24.216 -31.832 -25.826  1.00 70.88           C  
ANISOU 3516  CG  ASP B 194     8537   9051   9342    736   -103    344       C  
ATOM   3517  OD1 ASP B 194      23.297 -32.022 -24.996  1.00 68.70           O  
ANISOU 3517  OD1 ASP B 194     8268   8777   9059    726   -109    366       O  
ATOM   3518  OD2 ASP B 194      25.349 -32.353 -25.730  1.00 72.39           O  
ANISOU 3518  OD2 ASP B 194     8694   9261   9549    764    -99    378       O  
ATOM   3519  N   ASP B 195      22.401 -29.442 -29.166  1.00 68.40           N  
ANISOU 3519  N   ASP B 195     8336   8643   9008    659    -91    145       N  
ATOM   3520  CA  ASP B 195      21.779 -28.528 -30.112  1.00 67.71           C  
ANISOU 3520  CA  ASP B 195     8283   8537   8908    631    -91     87       C  
ATOM   3521  C   ASP B 195      20.331 -28.383 -29.660  1.00 65.63           C  
ANISOU 3521  C   ASP B 195     8043   8257   8635    612    -95     82       C  
ATOM   3522  O   ASP B 195      19.578 -29.356 -29.741  1.00 68.31           O  
ANISOU 3522  O   ASP B 195     8395   8550   9010    624    -85     94       O  
ATOM   3523  CB  ASP B 195      21.882 -29.055 -31.551  1.00 66.13           C  
ANISOU 3523  CB  ASP B 195     8099   8281   8748    644    -71     55       C  
ATOM   3524  N   LEU B 196      19.966 -27.193 -29.153  1.00 63.96           N  
ANISOU 3524  N   LEU B 196     7838   8084   8379    581   -110     64       N  
ATOM   3525  CA  LEU B 196      18.690 -26.800 -28.543  1.00 58.87           C  
ANISOU 3525  CA  LEU B 196     7213   7439   7716    559   -118     59       C  
ATOM   3526  C   LEU B 196      18.938 -26.269 -27.136  1.00 58.01           C  
ANISOU 3526  C   LEU B 196     7080   7395   7565    546   -134     87       C  
ATOM   3527  O   LEU B 196      18.278 -25.323 -26.701  1.00 58.20           O  
ANISOU 3527  O   LEU B 196     7116   7440   7557    518   -142     67       O  
ATOM   3528  CB  LEU B 196      17.653 -27.928 -28.475  1.00 58.53           C  
ANISOU 3528  CB  LEU B 196     7184   7347   7709    572   -108     78       C  
ATOM   3529  CG  LEU B 196      16.199 -27.520 -28.233  1.00 58.89           C  
ANISOU 3529  CG  LEU B 196     7255   7379   7742    548   -112     61       C  
ATOM   3530  CD1 LEU B 196      15.764 -26.431 -29.200  1.00 57.07           C  
ANISOU 3530  CD1 LEU B 196     7050   7137   7496    524   -113      6       C  
ATOM   3531  CD2 LEU B 196      15.270 -28.715 -28.349  1.00 54.68           C  
ANISOU 3531  CD2 LEU B 196     6735   6793   7248    562   -100     76       C  
ATOM   3532  N   GLU B 197      19.868 -26.877 -26.403  1.00 55.41           N  
ANISOU 3532  N   GLU B 197     6717   7098   7237    566   -137    133       N  
ATOM   3533  CA  GLU B 197      20.252 -26.357 -25.096  1.00 51.31           C  
ANISOU 3533  CA  GLU B 197     6171   6649   6675    552   -152    158       C  
ATOM   3534  C   GLU B 197      21.407 -25.363 -25.192  1.00 50.03           C  
ANISOU 3534  C   GLU B 197     5992   6538   6479    539   -160    140       C  
ATOM   3535  O   GLU B 197      21.633 -24.588 -24.250  1.00 43.03           O  
ANISOU 3535  O   GLU B 197     5089   5711   5548    516   -172    144       O  
ATOM   3536  CB  GLU B 197      20.576 -27.532 -24.169  1.00 53.96           C  
ANISOU 3536  CB  GLU B 197     6476   6999   7026    579   -153    223       C  
ATOM   3537  CG  GLU B 197      21.578 -27.276 -23.081  1.00 56.08           C  
ANISOU 3537  CG  GLU B 197     6704   7344   7258    577   -167    259       C  
ATOM   3538  CD  GLU B 197      21.773 -28.492 -22.208  1.00 62.54           C  
ANISOU 3538  CD  GLU B 197     7494   8172   8096    605   -167    326       C  
ATOM   3539  OE1 GLU B 197      22.909 -29.011 -22.159  1.00 64.36           O  
ANISOU 3539  OE1 GLU B 197     7693   8422   8338    630   -166    360       O  
ATOM   3540  OE2 GLU B 197      20.781 -28.926 -21.576  1.00 61.56           O  
ANISOU 3540  OE2 GLU B 197     7379   8035   7976    602   -168    346       O  
ATOM   3541  N   MET B 198      22.094 -25.346 -26.340  1.00 47.68           N  
ANISOU 3541  N   MET B 198     5699   6217   6201    550   -151    116       N  
ATOM   3542  CA  MET B 198      23.123 -24.385 -26.725  1.00 44.69           C  
ANISOU 3542  CA  MET B 198     5309   5875   5796    536   -155     89       C  
ATOM   3543  C   MET B 198      24.458 -24.668 -26.060  1.00 41.93           C  
ANISOU 3543  C   MET B 198     4917   5582   5434    551   -162    129       C  
ATOM   3544  O   MET B 198      24.631 -24.475 -24.851  1.00 36.55           O  
ANISOU 3544  O   MET B 198     4211   4956   4719    540   -174    158       O  
ATOM   3545  CB  MET B 198      22.696 -22.946 -26.447  1.00 43.39           C  
ANISOU 3545  CB  MET B 198     5161   5740   5587    495   -164     52       C  
ATOM   3546  CG  MET B 198      21.327 -22.614 -26.993  1.00 43.33           C  
ANISOU 3546  CG  MET B 198     5193   5682   5588    481   -159     17       C  
ATOM   3547  SD  MET B 198      21.348 -20.961 -27.666  1.00 47.57           S  
ANISOU 3547  SD  MET B 198     5752   6229   6095    445   -161    -43       S  
ATOM   3548  CE  MET B 198      22.820 -20.988 -28.690  1.00 32.80           C  
ANISOU 3548  CE  MET B 198     3867   4363   4235    459   -156    -52       C  
ATOM   3549  N   VAL B 199      25.408 -25.101 -26.882  1.00 41.14           N  
ANISOU 3549  N   VAL B 199     4805   5468   5359    574   -153    130       N  
ATOM   3550  CA  VAL B 199      26.738 -25.497 -26.454  1.00 42.18           C  
ANISOU 3550  CA  VAL B 199     4893   5646   5487    594   -157    168       C  
ATOM   3551  C   VAL B 199      27.746 -24.875 -27.415  1.00 42.28           C  
ANISOU 3551  C   VAL B 199     4903   5669   5494    589   -153    134       C  
ATOM   3552  O   VAL B 199      27.396 -24.380 -28.489  1.00 42.22           O  
ANISOU 3552  O   VAL B 199     4926   5623   5494    577   -146     86       O  
ATOM   3553  CB  VAL B 199      26.893 -27.031 -26.421  1.00 42.12           C  
ANISOU 3553  CB  VAL B 199     4870   5605   5530    638   -146    216       C  
ATOM   3554  CG1 VAL B 199      25.899 -27.657 -25.441  1.00 47.09           C  
ANISOU 3554  CG1 VAL B 199     5501   6225   6164    641   -149    253       C  
ATOM   3555  CG2 VAL B 199      26.680 -27.599 -27.812  1.00 42.96           C  
ANISOU 3555  CG2 VAL B 199     5002   5637   5684    656   -126    187       C  
ATOM   3556  N   GLY B 200      29.010 -24.897 -27.009  1.00 41.06           N  
ANISOU 3556  N   GLY B 200     4707   5569   5324    598   -159    160       N  
ATOM   3557  CA  GLY B 200      30.080 -24.549 -27.924  1.00 41.49           C  
ANISOU 3557  CA  GLY B 200     4753   5632   5380    601   -153    135       C  
ATOM   3558  C   GLY B 200      30.050 -23.103 -28.368  1.00 38.40           C  
ANISOU 3558  C   GLY B 200     4383   5257   4951    560   -158     81       C  
ATOM   3559  O   GLY B 200      29.711 -22.190 -27.606  1.00 36.49           O  
ANISOU 3559  O   GLY B 200     4144   5052   4667    527   -170     71       O  
ATOM   3560  N   GLU B 201      30.420 -22.892 -29.635  1.00 38.28           N  
ANISOU 3560  N   GLU B 201     4381   5212   4951    562   -148     44       N  
ATOM   3561  CA  GLU B 201      30.587 -21.538 -30.154  1.00 40.54           C  
ANISOU 3561  CA  GLU B 201     4684   5516   5205    525   -151     -5       C  
ATOM   3562  C   GLU B 201      29.262 -20.781 -30.212  1.00 36.37           C  
ANISOU 3562  C   GLU B 201     4196   4957   4664    496   -153    -38       C  
ATOM   3563  O   GLU B 201      29.228 -19.563 -29.992  1.00 35.41           O  
ANISOU 3563  O   GLU B 201     4083   4866   4505    460   -160    -66       O  
ATOM   3564  CB  GLU B 201      31.225 -21.590 -31.540  1.00 39.77           C  
ANISOU 3564  CB  GLU B 201     4593   5390   5130    535   -138    -33       C  
ATOM   3565  CG  GLU B 201      31.474 -20.221 -32.131  1.00 45.76           C  
ANISOU 3565  CG  GLU B 201     5366   6165   5856    499   -141    -81       C  
ATOM   3566  CD  GLU B 201      32.410 -20.252 -33.324  1.00 53.65           C  
ANISOU 3566  CD  GLU B 201     6360   7156   6870    508   -130   -102       C  
ATOM   3567  OE1 GLU B 201      32.457 -21.289 -34.029  1.00 54.05           O  
ANISOU 3567  OE1 GLU B 201     6410   7164   6962    540   -117    -95       O  
ATOM   3568  OE2 GLU B 201      33.116 -19.239 -33.535  1.00 53.58           O  
ANISOU 3568  OE2 GLU B 201     6345   7183   6829    482   -134   -126       O  
ATOM   3569  N   ALA B 202      28.170 -21.476 -30.532  1.00 33.26           N  
ANISOU 3569  N   ALA B 202     3829   4505   4304    510   -145    -38       N  
ATOM   3570  CA  ALA B 202      26.855 -20.837 -30.545  1.00 33.65           C  
ANISOU 3570  CA  ALA B 202     3914   4526   4344    485   -147    -65       C  
ATOM   3571  C   ALA B 202      26.543 -20.222 -29.189  1.00 33.01           C  
ANISOU 3571  C   ALA B 202     3825   4494   4225    462   -160    -52       C  
ATOM   3572  O   ALA B 202      26.076 -19.078 -29.097  1.00 31.12           O  
ANISOU 3572  O   ALA B 202     3603   4264   3956    429   -164    -84       O  
ATOM   3573  CB  ALA B 202      25.781 -21.856 -30.922  1.00 30.14           C  
ANISOU 3573  CB  ALA B 202     3492   4019   3941    506   -138    -58       C  
ATOM   3574  N   ARG B 203      26.796 -20.975 -28.118  1.00 31.47           N  
ANISOU 3574  N   ARG B 203     3599   4329   4027    478   -166     -5       N  
ATOM   3575  CA  ARG B 203      26.528 -20.452 -26.786  1.00 34.26           C  
ANISOU 3575  CA  ARG B 203     3942   4734   4342    455   -179      9       C  
ATOM   3576  C   ARG B 203      27.438 -19.277 -26.479  1.00 32.91           C  
ANISOU 3576  C   ARG B 203     3755   4626   4126    424   -186    -11       C  
ATOM   3577  O   ARG B 203      26.995 -18.273 -25.910  1.00 26.79           O  
ANISOU 3577  O   ARG B 203     2990   3875   3316    390   -191    -33       O  
ATOM   3578  CB  ARG B 203      26.682 -21.553 -25.738  1.00 36.82           C  
ANISOU 3578  CB  ARG B 203     4235   5082   4674    479   -184     68       C  
ATOM   3579  CG  ARG B 203      26.111 -21.149 -24.396  1.00 37.25           C  
ANISOU 3579  CG  ARG B 203     4283   5180   4691    455   -195     82       C  
ATOM   3580  CD  ARG B 203      26.360 -22.163 -23.284  1.00 39.18           C  
ANISOU 3580  CD  ARG B 203     4492   5458   4936    477   -202    144       C  
ATOM   3581  NE  ARG B 203      25.659 -21.724 -22.083  1.00 37.69           N  
ANISOU 3581  NE  ARG B 203     4302   5307   4711    450   -211    151       N  
ATOM   3582  CZ  ARG B 203      24.350 -21.832 -21.885  1.00 35.27           C  
ANISOU 3582  CZ  ARG B 203     4023   4965   4414    444   -208    145       C  
ATOM   3583  NH1 ARG B 203      23.565 -22.462 -22.748  1.00 35.23           N  
ANISOU 3583  NH1 ARG B 203     4048   4887   4454    464   -198    136       N  
ATOM   3584  NH2 ARG B 203      23.815 -21.287 -20.797  1.00 33.62           N  
ANISOU 3584  NH2 ARG B 203     3811   4797   4167    416   -216    145       N  
ATOM   3585  N   ASP B 204      28.713 -19.369 -26.883  1.00 30.93           N  
ANISOU 3585  N   ASP B 204     3479   4399   3875    435   -185     -5       N  
ATOM   3586  CA  ASP B 204      29.641 -18.268 -26.659  1.00 33.10           C  
ANISOU 3586  CA  ASP B 204     3737   4733   4107    405   -191    -25       C  
ATOM   3587  C   ASP B 204      29.228 -17.029 -27.437  1.00 29.32           C  
ANISOU 3587  C   ASP B 204     3293   4230   3617    372   -186    -82       C  
ATOM   3588  O   ASP B 204      29.350 -15.906 -26.938  1.00 31.31           O  
ANISOU 3588  O   ASP B 204     3546   4522   3830    336   -191   -105       O  
ATOM   3589  CB  ASP B 204      31.065 -18.681 -27.055  1.00 38.29           C  
ANISOU 3589  CB  ASP B 204     4360   5417   4771    425   -190     -8       C  
ATOM   3590  CG  ASP B 204      31.746 -19.564 -26.016  1.00 41.83           C  
ANISOU 3590  CG  ASP B 204     4764   5916   5215    448   -198     51       C  
ATOM   3591  OD1 ASP B 204      31.147 -19.862 -24.954  1.00 43.41           O  
ANISOU 3591  OD1 ASP B 204     4957   6134   5405    446   -206     79       O  
ATOM   3592  OD2 ASP B 204      32.894 -19.976 -26.285  1.00 46.13           O  
ANISOU 3592  OD2 ASP B 204     5277   6483   5767    468   -197     69       O  
ATOM   3593  N   LYS B 205      28.774 -17.202 -28.679  1.00 31.08           N  
ANISOU 3593  N   LYS B 205     3546   4389   3874    385   -176   -105       N  
ATOM   3594  CA  LYS B 205      28.325 -16.043 -29.448  1.00 31.87           C  
ANISOU 3594  CA  LYS B 205     3681   4465   3965    356   -171   -155       C  
ATOM   3595  C   LYS B 205      27.055 -15.447 -28.842  1.00 32.79           C  
ANISOU 3595  C   LYS B 205     3821   4568   4068    333   -173   -169       C  
ATOM   3596  O   LYS B 205      26.886 -14.219 -28.796  1.00 29.83           O  
ANISOU 3596  O   LYS B 205     3461   4205   3667    299   -173   -203       O  
ATOM   3597  CB  LYS B 205      28.088 -16.432 -30.911  1.00 30.21           C  
ANISOU 3597  CB  LYS B 205     3494   4192   3793    374   -160   -175       C  
ATOM   3598  CG  LYS B 205      29.370 -16.513 -31.823  1.00 34.38           C  
ANISOU 3598  CG  LYS B 205     4006   4730   4328    384   -155   -182       C  
ATOM   3599  CD  LYS B 205      28.942 -16.929 -33.252  1.00 35.39           C  
ANISOU 3599  CD  LYS B 205     4161   4794   4493    399   -143   -203       C  
ATOM   3600  CE  LYS B 205      30.095 -16.970 -34.278  1.00 45.28           C  
ANISOU 3600  CE  LYS B 205     5401   6051   5753    407   -136   -215       C  
ATOM   3601  NZ  LYS B 205      29.589 -16.839 -35.716  1.00 37.46           N  
ANISOU 3601  NZ  LYS B 205     4443   5007   4784    405   -125   -250       N  
ATOM   3602  N   MET B 206      26.142 -16.296 -28.382  1.00 31.04           N  
ANISOU 3602  N   MET B 206     3606   4323   3865    351   -174   -145       N  
ATOM   3603  CA  MET B 206      24.928 -15.753 -27.786  1.00 30.15           C  
ANISOU 3603  CA  MET B 206     3515   4201   3740    330   -175   -158       C  
ATOM   3604  C   MET B 206      25.232 -15.084 -26.446  1.00 31.53           C  
ANISOU 3604  C   MET B 206     3668   4442   3870    302   -184   -152       C  
ATOM   3605  O   MET B 206      24.618 -14.063 -26.104  1.00 31.50           O  
ANISOU 3605  O   MET B 206     3682   4443   3845    272   -182   -180       O  
ATOM   3606  CB  MET B 206      23.887 -16.853 -27.635  1.00 30.71           C  
ANISOU 3606  CB  MET B 206     3596   4231   3842    355   -174   -132       C  
ATOM   3607  CG  MET B 206      22.720 -16.462 -26.726  1.00 33.12           C  
ANISOU 3607  CG  MET B 206     3915   4540   4131    336   -177   -135       C  
ATOM   3608  SD  MET B 206      21.281 -17.487 -27.006  1.00 39.00           S  
ANISOU 3608  SD  MET B 206     4684   5219   4915    359   -172   -123       S  
ATOM   3609  CE  MET B 206      20.877 -17.067 -28.710  1.00 31.60           C  
ANISOU 3609  CE  MET B 206     3782   4220   4003    359   -162   -166       C  
ATOM   3610  N   MET B 207      26.206 -15.611 -25.702  1.00 33.10           N  
ANISOU 3610  N   MET B 207     3828   4694   4054    312   -191   -116       N  
ATOM   3611  CA  MET B 207      26.643 -14.941 -24.482  1.00 32.21           C  
ANISOU 3611  CA  MET B 207     3691   4652   3895    282   -199   -113       C  
ATOM   3612  C   MET B 207      27.188 -13.555 -24.785  1.00 31.53           C  
ANISOU 3612  C   MET B 207     3611   4588   3780    246   -196   -157       C  
ATOM   3613  O   MET B 207      26.896 -12.592 -24.067  1.00 29.08           O  
ANISOU 3613  O   MET B 207     3305   4306   3437    211   -196   -180       O  
ATOM   3614  CB  MET B 207      27.708 -15.771 -23.757  1.00 29.54           C  
ANISOU 3614  CB  MET B 207     3307   4371   3547    300   -208    -64       C  
ATOM   3615  CG  MET B 207      27.134 -16.734 -22.723  1.00 35.16           C  
ANISOU 3615  CG  MET B 207     4004   5093   4262    317   -214    -18       C  
ATOM   3616  SD  MET B 207      26.496 -15.870 -21.254  1.00 37.04           S  
ANISOU 3616  SD  MET B 207     4239   5385   4450    274   -220    -27       S  
ATOM   3617  CE  MET B 207      25.285 -17.021 -20.672  1.00 42.15           C  
ANISOU 3617  CE  MET B 207     4892   6000   5121    299   -222     13       C  
ATOM   3618  N   GLN B 208      28.003 -13.440 -25.839  1.00 31.05           N  
ANISOU 3618  N   GLN B 208     3551   4515   3732    253   -192   -171       N  
ATOM   3619  CA  GLN B 208      28.524 -12.138 -26.243  1.00 33.37           C  
ANISOU 3619  CA  GLN B 208     3853   4823   4002    219   -187   -213       C  
ATOM   3620  C   GLN B 208      27.400 -11.214 -26.693  1.00 32.42           C  
ANISOU 3620  C   GLN B 208     3775   4654   3888    198   -179   -255       C  
ATOM   3621  O   GLN B 208      27.390 -10.023 -26.355  1.00 31.21           O  
ANISOU 3621  O   GLN B 208     3630   4522   3707    161   -175   -286       O  
ATOM   3622  CB  GLN B 208      29.559 -12.301 -27.366  1.00 32.38           C  
ANISOU 3622  CB  GLN B 208     3721   4690   3893    233   -184   -218       C  
ATOM   3623  CG  GLN B 208      30.863 -12.983 -26.937  1.00 36.95           C  
ANISOU 3623  CG  GLN B 208     4253   5325   4460    249   -191   -182       C  
ATOM   3624  CD  GLN B 208      31.663 -13.498 -28.136  1.00 43.38           C  
ANISOU 3624  CD  GLN B 208     5062   6116   5303    276   -186   -180       C  
ATOM   3625  OE1 GLN B 208      32.381 -14.500 -28.043  1.00 39.04           O  
ANISOU 3625  OE1 GLN B 208     4482   5585   4767    306   -189   -143       O  
ATOM   3626  NE2 GLN B 208      31.542 -12.803 -29.271  1.00 40.76           N  
ANISOU 3626  NE2 GLN B 208     4760   5746   4981    264   -178   -220       N  
ATOM   3627  N   SER B 209      26.456 -11.737 -27.478  1.00 31.65           N  
ANISOU 3627  N   SER B 209     3705   4492   3827    221   -174   -255       N  
ATOM   3628  CA  SER B 209      25.262 -10.960 -27.803  1.00 31.95           C  
ANISOU 3628  CA  SER B 209     3782   4486   3873    205   -167   -288       C  
ATOM   3629  C   SER B 209      24.539 -10.516 -26.536  1.00 30.94           C  
ANISOU 3629  C   SER B 209     3653   4382   3719    183   -168   -289       C  
ATOM   3630  O   SER B 209      24.115  -9.359 -26.423  1.00 29.26           O  
ANISOU 3630  O   SER B 209     3459   4167   3492    152   -162   -324       O  
ATOM   3631  CB  SER B 209      24.322 -11.783 -28.688  1.00 30.07           C  
ANISOU 3631  CB  SER B 209     3568   4182   3677    235   -163   -281       C  
ATOM   3632  OG  SER B 209      23.125 -11.073 -28.984  1.00 29.30           O  
ANISOU 3632  OG  SER B 209     3505   4044   3586    221   -157   -309       O  
ATOM   3633  N   PHE B 210      24.403 -11.426 -25.569  1.00 30.01           N  
ANISOU 3633  N   PHE B 210     3514   4290   3597    197   -176   -252       N  
ATOM   3634  CA  PHE B 210      23.688 -11.126 -24.326  1.00 30.97           C  
ANISOU 3634  CA  PHE B 210     3634   4438   3695    177   -178   -251       C  
ATOM   3635  C   PHE B 210      24.306  -9.931 -23.611  1.00 34.28           C  
ANISOU 3635  C   PHE B 210     4040   4913   4070    135   -176   -277       C  
ATOM   3636  O   PHE B 210      23.595  -9.032 -23.137  1.00 32.46           O  
ANISOU 3636  O   PHE B 210     3827   4682   3825    107   -170   -306       O  
ATOM   3637  CB  PHE B 210      23.724 -12.364 -23.427  1.00 30.28           C  
ANISOU 3637  CB  PHE B 210     3518   4379   3608    200   -188   -201       C  
ATOM   3638  CG  PHE B 210      22.804 -12.309 -22.246  1.00 33.44           C  
ANISOU 3638  CG  PHE B 210     3918   4798   3990    185   -189   -194       C  
ATOM   3639  CD1 PHE B 210      21.563 -11.684 -22.318  1.00 31.58           C  
ANISOU 3639  CD1 PHE B 210     3715   4524   3760    172   -181   -224       C  
ATOM   3640  CD2 PHE B 210      23.182 -12.910 -21.047  1.00 31.67           C  
ANISOU 3640  CD2 PHE B 210     3660   4633   3742    187   -199   -156       C  
ATOM   3641  CE1 PHE B 210      20.725 -11.655 -21.214  1.00 31.28           C  
ANISOU 3641  CE1 PHE B 210     3675   4505   3705    158   -182   -219       C  
ATOM   3642  CE2 PHE B 210      22.353 -12.879 -19.954  1.00 33.11           C  
ANISOU 3642  CE2 PHE B 210     3841   4836   3906    172   -200   -149       C  
ATOM   3643  CZ  PHE B 210      21.122 -12.254 -20.034  1.00 30.74           C  
ANISOU 3643  CZ  PHE B 210     3573   4496   3611    158   -192   -182       C  
ATOM   3644  N   ARG B 211      25.641  -9.913 -23.525  1.00 33.03           N  
ANISOU 3644  N   ARG B 211     3853   4805   3893    130   -181   -268       N  
ATOM   3645  CA  ARG B 211      26.354  -8.837 -22.847  1.00 34.16           C  
ANISOU 3645  CA  ARG B 211     3981   5006   3993     89   -180   -292       C  
ATOM   3646  C   ARG B 211      26.151  -7.504 -23.554  1.00 33.77           C  
ANISOU 3646  C   ARG B 211     3963   4924   3944     61   -167   -344       C  
ATOM   3647  O   ARG B 211      25.989  -6.466 -22.901  1.00 31.87           O  
ANISOU 3647  O   ARG B 211     3727   4707   3676     23   -160   -374       O  
ATOM   3648  CB  ARG B 211      27.847  -9.181 -22.775  1.00 33.47           C  
ANISOU 3648  CB  ARG B 211     3855   4974   3888     93   -188   -270       C  
ATOM   3649  CG  ARG B 211      28.675  -8.189 -22.000  1.00 33.61           C  
ANISOU 3649  CG  ARG B 211     3850   5061   3857     49   -188   -291       C  
ATOM   3650  CD  ARG B 211      30.179  -8.501 -22.082  1.00 41.91           C  
ANISOU 3650  CD  ARG B 211     4865   6167   4894     54   -196   -271       C  
ATOM   3651  NE  ARG B 211      30.951  -7.286 -21.840  1.00 45.42           N  
ANISOU 3651  NE  ARG B 211     5300   6657   5300      8   -191   -307       N  
ATOM   3652  CZ  ARG B 211      31.308  -6.419 -22.778  1.00 45.67           C  
ANISOU 3652  CZ  ARG B 211     5351   6663   5337     -8   -181   -344       C  
ATOM   3653  NH1 ARG B 211      31.089  -6.659 -24.065  1.00 43.30           N  
ANISOU 3653  NH1 ARG B 211     5076   6297   5077     19   -177   -349       N  
ATOM   3654  NH2 ARG B 211      31.887  -5.279 -22.415  1.00 47.51           N  
ANISOU 3654  NH2 ARG B 211     5579   6939   5535    -54   -175   -378       N  
ATOM   3655  N   ASN B 212      26.213  -7.506 -24.891  1.00 32.11           N  
ANISOU 3655  N   ASN B 212     3773   4663   3764     77   -162   -355       N  
ATOM   3656  CA  ASN B 212      25.923  -6.297 -25.656  1.00 29.92           C  
ANISOU 3656  CA  ASN B 212     3527   4347   3492     55   -150   -399       C  
ATOM   3657  C   ASN B 212      24.512  -5.799 -25.385  1.00 34.06           C  
ANISOU 3657  C   ASN B 212     4081   4834   4025     45   -141   -418       C  
ATOM   3658  O   ASN B 212      24.292  -4.594 -25.221  1.00 32.74           O  
ANISOU 3658  O   ASN B 212     3930   4665   3845     12   -130   -455       O  
ATOM   3659  CB  ASN B 212      26.101  -6.568 -27.149  1.00 34.49           C  
ANISOU 3659  CB  ASN B 212     4123   4877   4105     78   -148   -401       C  
ATOM   3660  CG  ASN B 212      27.564  -6.707 -27.543  1.00 38.07           C  
ANISOU 3660  CG  ASN B 212     4550   5366   4548     80   -152   -394       C  
ATOM   3661  OD1 ASN B 212      28.455  -6.316 -26.792  1.00 36.53           O  
ANISOU 3661  OD1 ASN B 212     4329   5231   4318     56   -154   -396       O  
ATOM   3662  ND2 ASN B 212      27.813  -7.287 -28.711  1.00 39.31           N  
ANISOU 3662  ND2 ASN B 212     4714   5489   4734    107   -152   -386       N  
ATOM   3663  N   MET B 213      23.538  -6.711 -25.361  1.00 30.22           N  
ANISOU 3663  N   MET B 213     3603   4315   3562     74   -146   -395       N  
ATOM   3664  CA  MET B 213      22.166  -6.318 -25.061  1.00 32.79           C  
ANISOU 3664  CA  MET B 213     3955   4609   3897     67   -138   -410       C  
ATOM   3665  C   MET B 213      22.074  -5.644 -23.704  1.00 30.05           C  
ANISOU 3665  C   MET B 213     3595   4309   3512     33   -135   -424       C  
ATOM   3666  O   MET B 213      21.446  -4.589 -23.562  1.00 29.91           O  
ANISOU 3666  O   MET B 213     3598   4275   3490      8   -122   -459       O  
ATOM   3667  CB  MET B 213      21.248  -7.534 -25.119  1.00 30.02           C  
ANISOU 3667  CB  MET B 213     3608   4225   3572    102   -145   -379       C  
ATOM   3668  CG  MET B 213      19.762  -7.190 -25.059  1.00 32.52           C  
ANISOU 3668  CG  MET B 213     3953   4499   3904    100   -137   -394       C  
ATOM   3669  SD  MET B 213      19.185  -7.080 -23.351  1.00 32.83           S  
ANISOU 3669  SD  MET B 213     3978   4584   3912     79   -137   -390       S  
ATOM   3670  CE  MET B 213      19.066  -8.815 -22.922  1.00 30.28           C  
ANISOU 3670  CE  MET B 213     3633   4271   3600    115   -152   -335       C  
ATOM   3671  N   LEU B 214      22.702  -6.234 -22.690  1.00 31.16           N  
ANISOU 3671  N   LEU B 214     3702   4511   3626     31   -145   -397       N  
ATOM   3672  CA  LEU B 214      22.668  -5.612 -21.377  1.00 28.01           C  
ANISOU 3672  CA  LEU B 214     3289   4165   3188     -5   -141   -411       C  
ATOM   3673  C   LEU B 214      23.411  -4.281 -21.378  1.00 30.67           C  
ANISOU 3673  C   LEU B 214     3626   4526   3500    -45   -131   -453       C  
ATOM   3674  O   LEU B 214      23.095  -3.400 -20.574  1.00 28.56           O  
ANISOU 3674  O   LEU B 214     3362   4280   3209    -80   -120   -482       O  
ATOM   3675  CB  LEU B 214      23.219  -6.581 -20.329  1.00 31.61           C  
ANISOU 3675  CB  LEU B 214     3705   4685   3619      3   -156   -369       C  
ATOM   3676  CG  LEU B 214      22.318  -7.808 -20.157  1.00 32.08           C  
ANISOU 3676  CG  LEU B 214     3766   4720   3703     38   -164   -330       C  
ATOM   3677  CD1 LEU B 214      22.985  -8.882 -19.297  1.00 33.65           C  
ANISOU 3677  CD1 LEU B 214     3924   4977   3883     51   -179   -280       C  
ATOM   3678  CD2 LEU B 214      20.955  -7.414 -19.580  1.00 29.49           C  
ANISOU 3678  CD2 LEU B 214     3459   4371   3374     25   -155   -348       C  
ATOM   3679  N   GLY B 215      24.366  -4.097 -22.296  1.00 34.02           N  
ANISOU 3679  N   GLY B 215     4049   4945   3931    -43   -131   -458       N  
ATOM   3680  CA  GLY B 215      25.085  -2.836 -22.353  1.00 32.67           C  
ANISOU 3680  CA  GLY B 215     3881   4795   3739    -83   -120   -498       C  
ATOM   3681  C   GLY B 215      24.197  -1.672 -22.755  1.00 33.26           C  
ANISOU 3681  C   GLY B 215     3993   4816   3829   -101   -102   -540       C  
ATOM   3682  O   GLY B 215      24.297  -0.575 -22.192  1.00 30.00           O  
ANISOU 3682  O   GLY B 215     3582   4423   3392   -142    -88   -576       O  
ATOM   3683  N   ASP B 216      23.322  -1.885 -23.737  1.00 33.96           N  
ANISOU 3683  N   ASP B 216     4111   4835   3957    -73    -99   -537       N  
ATOM   3684  CA  ASP B 216      22.380  -0.838 -24.111  1.00 30.45           C  
ANISOU 3684  CA  ASP B 216     3701   4338   3531    -86    -82   -572       C  
ATOM   3685  C   ASP B 216      21.422  -0.538 -22.967  1.00 31.73           C  
ANISOU 3685  C   ASP B 216     3865   4509   3680   -103    -74   -585       C  
ATOM   3686  O   ASP B 216      21.098   0.623 -22.705  1.00 33.09           O  
ANISOU 3686  O   ASP B 216     4053   4672   3847   -133    -57   -623       O  
ATOM   3687  CB  ASP B 216      21.603  -1.256 -25.354  1.00 35.17           C  
ANISOU 3687  CB  ASP B 216     4325   4867   4172    -51    -84   -561       C  
ATOM   3688  CG  ASP B 216      22.511  -1.663 -26.497  1.00 37.16           C  
ANISOU 3688  CG  ASP B 216     4573   5109   4436    -33    -92   -548       C  
ATOM   3689  OD1 ASP B 216      22.105  -2.554 -27.276  1.00 40.05           O  
ANISOU 3689  OD1 ASP B 216     4946   5440   4829      2    -99   -525       O  
ATOM   3690  OD2 ASP B 216      23.616  -1.089 -26.618  1.00 35.94           O  
ANISOU 3690  OD2 ASP B 216     4408   4985   4263    -55    -89   -562       O  
ATOM   3691  N   LEU B 217      20.950  -1.575 -22.285  1.00 27.93           N  
ANISOU 3691  N   LEU B 217     3370   4046   3195    -83    -86   -553       N  
ATOM   3692  CA  LEU B 217      20.134  -1.360 -21.097  1.00 31.79           C  
ANISOU 3692  CA  LEU B 217     3857   4555   3667   -101    -79   -563       C  
ATOM   3693  C   LEU B 217      20.926  -0.604 -20.039  1.00 36.01           C  
ANISOU 3693  C   LEU B 217     4370   5155   4157   -146    -73   -588       C  
ATOM   3694  O   LEU B 217      20.395   0.296 -19.375  1.00 33.74           O  
ANISOU 3694  O   LEU B 217     4091   4871   3857   -176    -56   -622       O  
ATOM   3695  CB  LEU B 217      19.657  -2.709 -20.564  1.00 31.19           C  
ANISOU 3695  CB  LEU B 217     3765   4492   3593    -72    -95   -520       C  
ATOM   3696  CG  LEU B 217      18.215  -2.997 -20.172  1.00 38.03           C  
ANISOU 3696  CG  LEU B 217     4645   5329   4474    -60    -92   -515       C  
ATOM   3697  CD1 LEU B 217      17.222  -2.315 -21.102  1.00 30.90           C  
ANISOU 3697  CD1 LEU B 217     3781   4354   3607    -53    -78   -541       C  
ATOM   3698  CD2 LEU B 217      18.000  -4.496 -20.162  1.00 30.32           C  
ANISOU 3698  CD2 LEU B 217     3656   4352   3510    -22   -109   -466       C  
ATOM   3699  N   ALA B 218      22.219  -0.934 -19.898  1.00 33.79           N  
ANISOU 3699  N   ALA B 218     4059   4928   3851   -152    -84   -572       N  
ATOM   3700  CA  ALA B 218      23.033  -0.333 -18.846  1.00 37.07           C  
ANISOU 3700  CA  ALA B 218     4450   5417   4220   -195    -80   -591       C  
ATOM   3701  C   ALA B 218      23.158   1.177 -19.019  1.00 37.57           C  
ANISOU 3701  C   ALA B 218     4532   5464   4278   -236    -57   -646       C  
ATOM   3702  O   ALA B 218      23.274   1.907 -18.026  1.00 36.56           O  
ANISOU 3702  O   ALA B 218     4395   5379   4117   -277    -46   -675       O  
ATOM   3703  CB  ALA B 218      24.417  -0.991 -18.810  1.00 34.11           C  
ANISOU 3703  CB  ALA B 218     4039   5100   3822   -191    -97   -561       C  
ATOM   3704  N   ALA B 219      23.135   1.658 -20.266  1.00 36.97           N  
ANISOU 3704  N   ALA B 219     4484   5328   4236   -225    -50   -660       N  
ATOM   3705  CA  ALA B 219      23.165   3.097 -20.517  1.00 36.51           C  
ANISOU 3705  CA  ALA B 219     4447   5244   4179   -260    -27   -709       C  
ATOM   3706  C   ALA B 219      22.113   3.829 -19.696  1.00 35.47           C  
ANISOU 3706  C   ALA B 219     4330   5100   4045   -283     -7   -741       C  
ATOM   3707  O   ALA B 219      22.374   4.908 -19.152  1.00 38.81           O  
ANISOU 3707  O   ALA B 219     4755   5544   4448   -327     12   -783       O  
ATOM   3708  CB  ALA B 219      22.951   3.369 -22.006  1.00 32.66           C  
ANISOU 3708  CB  ALA B 219     3992   4684   3735   -238    -22   -712       C  
ATOM   3709  N   LEU B 220      20.908   3.258 -19.605  1.00 34.09           N  
ANISOU 3709  N   LEU B 220     4168   4894   3893   -255    -10   -724       N  
ATOM   3710  CA  LEU B 220      19.850   3.880 -18.818  1.00 34.00           C  
ANISOU 3710  CA  LEU B 220     4168   4870   3879   -273      8   -753       C  
ATOM   3711  C   LEU B 220      20.179   3.839 -17.333  1.00 36.58           C  
ANISOU 3711  C   LEU B 220     4466   5276   4158   -307      8   -761       C  
ATOM   3712  O   LEU B 220      19.951   4.818 -16.613  1.00 36.16           O  
ANISOU 3712  O   LEU B 220     4416   5234   4089   -346     30   -803       O  
ATOM   3713  CB  LEU B 220      18.518   3.174 -19.087  1.00 34.41           C  
ANISOU 3713  CB  LEU B 220     4236   4872   3964   -233      2   -729       C  
ATOM   3714  CG  LEU B 220      17.772   3.573 -20.356  1.00 31.31           C  
ANISOU 3714  CG  LEU B 220     3879   4397   3619   -209     11   -735       C  
ATOM   3715  CD1 LEU B 220      18.393   2.902 -21.599  1.00 32.26           C  
ANISOU 3715  CD1 LEU B 220     4001   4497   3760   -178     -6   -704       C  
ATOM   3716  CD2 LEU B 220      16.288   3.231 -20.226  1.00 32.74           C  
ANISOU 3716  CD2 LEU B 220     4075   4540   3825   -185     13   -726       C  
ATOM   3717  N   PHE B 221      20.698   2.704 -16.854  1.00 37.24           N  
ANISOU 3717  N   PHE B 221     4518   5415   4218   -293    -15   -719       N  
ATOM   3718  CA  PHE B 221      21.000   2.541 -15.436  1.00 38.90           C  
ANISOU 3718  CA  PHE B 221     4695   5706   4380   -323    -19   -719       C  
ATOM   3719  C   PHE B 221      22.258   3.293 -15.020  1.00 39.90           C  
ANISOU 3719  C   PHE B 221     4801   5892   4465   -370    -12   -746       C  
ATOM   3720  O   PHE B 221      22.550   3.366 -13.819  1.00 42.83           O  
ANISOU 3720  O   PHE B 221     5146   6337   4793   -403    -11   -754       O  
ATOM   3721  CB  PHE B 221      21.127   1.050 -15.095  1.00 36.83           C  
ANISOU 3721  CB  PHE B 221     4405   5480   4107   -290    -46   -660       C  
ATOM   3722  CG  PHE B 221      19.806   0.331 -15.046  1.00 38.84           C  
ANISOU 3722  CG  PHE B 221     4673   5695   4388   -257    -50   -637       C  
ATOM   3723  CD1 PHE B 221      19.087   0.249 -13.863  1.00 36.58           C  
ANISOU 3723  CD1 PHE B 221     4378   5443   4080   -273    -45   -640       C  
ATOM   3724  CD2 PHE B 221      19.273  -0.252 -16.187  1.00 36.88           C  
ANISOU 3724  CD2 PHE B 221     4447   5377   4186   -212    -57   -613       C  
ATOM   3725  CE1 PHE B 221      17.866  -0.399 -13.817  1.00 33.69           C  
ANISOU 3725  CE1 PHE B 221     4023   5040   3737   -244    -48   -620       C  
ATOM   3726  CE2 PHE B 221      18.041  -0.910 -16.144  1.00 37.51           C  
ANISOU 3726  CE2 PHE B 221     4540   5422   4291   -184    -60   -594       C  
ATOM   3727  CZ  PHE B 221      17.345  -0.980 -14.955  1.00 34.45           C  
ANISOU 3727  CZ  PHE B 221     4142   5067   3880   -200    -56   -596       C  
ATOM   3728  N   ARG B 222      23.003   3.859 -15.972  1.00 40.99           N  
ANISOU 3728  N   ARG B 222     4951   6006   4617   -374     -7   -761       N  
ATOM   3729  CA  ARG B 222      24.165   4.682 -15.648  1.00 43.98           C  
ANISOU 3729  CA  ARG B 222     5313   6437   4960   -421      1   -793       C  
ATOM   3730  C   ARG B 222      23.821   6.157 -15.507  1.00 42.27           C  
ANISOU 3730  C   ARG B 222     5122   6193   4747   -464     34   -855       C  
ATOM   3731  O   ARG B 222      24.628   6.916 -14.959  1.00 45.44           O  
ANISOU 3731  O   ARG B 222     5509   6644   5113   -512     45   -889       O  
ATOM   3732  CB  ARG B 222      25.260   4.526 -16.716  1.00 41.51           C  
ANISOU 3732  CB  ARG B 222     4996   6118   4658   -407    -10   -777       C  
ATOM   3733  CG  ARG B 222      26.086   3.262 -16.589  1.00 47.73           C  
ANISOU 3733  CG  ARG B 222     5747   6962   5428   -382    -39   -723       C  
ATOM   3734  CD  ARG B 222      27.317   3.273 -17.501  1.00 46.98           C  
ANISOU 3734  CD  ARG B 222     5644   6873   5335   -378    -46   -716       C  
ATOM   3735  NE  ARG B 222      27.021   2.600 -18.761  1.00 47.16           N  
ANISOU 3735  NE  ARG B 222     5685   6829   5403   -327    -56   -686       N  
ATOM   3736  CZ  ARG B 222      27.585   1.469 -19.159  1.00 45.75           C  
ANISOU 3736  CZ  ARG B 222     5487   6665   5231   -290    -77   -640       C  
ATOM   3737  NH1 ARG B 222      28.490   0.851 -18.416  1.00 49.34           N  
ANISOU 3737  NH1 ARG B 222     5899   7198   5650   -296    -93   -613       N  
ATOM   3738  NH2 ARG B 222      27.221   0.936 -20.327  1.00 50.73           N  
ANISOU 3738  NH2 ARG B 222     6139   7231   5905   -248    -83   -620       N  
ATOM   3739  N   LYS B 223      22.638   6.576 -15.960  1.00 43.92           N  
ANISOU 3739  N   LYS B 223     5366   6325   4997   -448     50   -871       N  
ATOM   3740  CA  LYS B 223      22.320   7.998 -15.964  1.00 44.58           C  
ANISOU 3740  CA  LYS B 223     5476   6372   5091   -484     83   -929       C  
ATOM   3741  C   LYS B 223      22.314   8.571 -14.546  1.00 47.08           C  
ANISOU 3741  C   LYS B 223     5775   6748   5364   -535    100   -967       C  
ATOM   3742  O   LYS B 223      22.764   9.703 -14.326  1.00 52.29           O  
ANISOU 3742  O   LYS B 223     6441   7416   6012   -581    124  -1016       O  
ATOM   3743  CB  LYS B 223      20.984   8.221 -16.668  1.00 45.41           C  
ANISOU 3743  CB  LYS B 223     5618   6387   5249   -452     94   -932       C  
ATOM   3744  CG  LYS B 223      20.885   9.539 -17.414  1.00 50.33           C  
ANISOU 3744  CG  LYS B 223     6273   6946   5902   -469    122   -973       C  
ATOM   3745  CD  LYS B 223      21.263   9.398 -18.890  1.00 51.35           C  
ANISOU 3745  CD  LYS B 223     6418   7026   6065   -437    112   -949       C  
ATOM   3746  CE  LYS B 223      20.974  10.688 -19.645  1.00 53.45           C  
ANISOU 3746  CE  LYS B 223     6718   7222   6366   -450    140   -985       C  
ATOM   3747  NZ  LYS B 223      21.793  11.824 -19.117  1.00 56.81           N  
ANISOU 3747  NZ  LYS B 223     7141   7678   6767   -507    164  -1034       N  
ATOM   3748  N   ASP B 224      21.850   7.797 -13.565  1.00 46.21           N  
ANISOU 3748  N   ASP B 224     5645   6683   5231   -530     88   -946       N  
ATOM   3749  CA  ASP B 224      21.800   8.228 -12.164  1.00 45.99           C  
ANISOU 3749  CA  ASP B 224     5598   6719   5158   -578    102   -980       C  
ATOM   3750  C   ASP B 224      22.664   7.280 -11.335  1.00 44.85           C  
ANISOU 3750  C   ASP B 224     5407   6672   4961   -585     76   -944       C  
ATOM   3751  O   ASP B 224      22.189   6.236 -10.877  1.00 44.68           O  
ANISOU 3751  O   ASP B 224     5370   6673   4933   -558     56   -902       O  
ATOM   3752  CB  ASP B 224      20.366   8.256 -11.641  1.00 42.32           C  
ANISOU 3752  CB  ASP B 224     5148   6223   4709   -569    116   -991       C  
ATOM   3753  CG  ASP B 224      20.257   8.882 -10.249  1.00 48.17           C  
ANISOU 3753  CG  ASP B 224     5873   7022   5406   -623    137  -1036       C  
ATOM   3754  OD1 ASP B 224      21.293   8.961  -9.537  1.00 47.38           O  
ANISOU 3754  OD1 ASP B 224     5742   7004   5255   -664    132  -1045       O  
ATOM   3755  OD2 ASP B 224      19.134   9.280  -9.859  1.00 42.98           O  
ANISOU 3755  OD2 ASP B 224     5234   6333   4765   -626    157  -1062       O  
ATOM   3756  N   ALA B 225      23.916   7.661 -11.102  1.00 49.87           N  
ANISOU 3756  N   ALA B 225     6020   7368   5560   -624     75   -958       N  
ATOM   3757  CA  ALA B 225      24.848   6.797 -10.384  1.00 49.55           C  
ANISOU 3757  CA  ALA B 225     5933   7423   5470   -630     49   -921       C  
ATOM   3758  C   ALA B 225      24.676   6.831  -8.866  1.00 45.92           C  
ANISOU 3758  C   ALA B 225     5445   7044   4958   -671     54   -936       C  
ATOM   3759  O   ALA B 225      25.365   6.076  -8.169  1.00 41.88           O  
ANISOU 3759  O   ALA B 225     4893   6618   4403   -677     32   -901       O  
ATOM   3760  CB  ALA B 225      26.287   7.166 -10.754  1.00 50.43           C  
ANISOU 3760  CB  ALA B 225     6028   7573   5560   -655     45   -929       C  
ATOM   3761  N   SER B 226      23.759   7.652  -8.334  1.00 46.27           N  
ANISOU 3761  N   SER B 226     5510   7065   5005   -699     82   -985       N  
ATOM   3762  CA  SER B 226      23.567   7.729  -6.887  1.00 44.37           C  
ANISOU 3762  CA  SER B 226     5243   6903   4713   -741     89  -1004       C  
ATOM   3763  C   SER B 226      22.943   6.469  -6.304  1.00 45.12           C  
ANISOU 3763  C   SER B 226     5318   7026   4798   -707     65   -949       C  
ATOM   3764  O   SER B 226      22.872   6.338  -5.077  1.00 46.01           O  
ANISOU 3764  O   SER B 226     5403   7214   4863   -739     65   -953       O  
ATOM   3765  CB  SER B 226      22.690   8.929  -6.519  1.00 45.74           C  
ANISOU 3765  CB  SER B 226     5445   7037   4898   -776    129  -1073       C  
ATOM   3766  OG  SER B 226      21.358   8.767  -6.995  1.00 45.89           O  
ANISOU 3766  OG  SER B 226     5497   6970   4968   -734    135  -1065       O  
ATOM   3767  N   GLY B 227      22.476   5.554  -7.142  1.00 42.54           N  
ANISOU 3767  N   GLY B 227     5005   6641   4515   -646     46   -899       N  
ATOM   3768  CA  GLY B 227      21.874   4.337  -6.669  1.00 41.67           C  
ANISOU 3768  CA  GLY B 227     4879   6551   4401   -612     24   -845       C  
ATOM   3769  C   GLY B 227      21.769   3.332  -7.791  1.00 36.24           C  
ANISOU 3769  C   GLY B 227     4204   5805   3761   -547      1   -789       C  
ATOM   3770  O   GLY B 227      22.098   3.619  -8.944  1.00 35.55           O  
ANISOU 3770  O   GLY B 227     4138   5660   3708   -529      3   -794       O  
ATOM   3771  N   PRO B 228      21.299   2.125  -7.474  1.00 34.70           N  
ANISOU 3771  N   PRO B 228     3994   5623   3566   -512    -21   -734       N  
ATOM   3772  CA  PRO B 228      21.277   1.051  -8.472  1.00 36.71           C  
ANISOU 3772  CA  PRO B 228     4256   5829   3863   -452    -43   -679       C  
ATOM   3773  C   PRO B 228      20.050   1.031  -9.379  1.00 36.29           C  
ANISOU 3773  C   PRO B 228     4245   5674   3868   -413    -34   -683       C  
ATOM   3774  O   PRO B 228      20.078   0.330 -10.401  1.00 36.65           O  
ANISOU 3774  O   PRO B 228     4303   5671   3953   -367    -49   -648       O  
ATOM   3775  CB  PRO B 228      21.341  -0.206  -7.599  1.00 35.04           C  
ANISOU 3775  CB  PRO B 228     4008   5684   3623   -437    -67   -620       C  
ATOM   3776  CG  PRO B 228      20.671   0.202  -6.323  1.00 36.83           C  
ANISOU 3776  CG  PRO B 228     4225   5956   3812   -476    -54   -647       C  
ATOM   3777  CD  PRO B 228      20.888   1.666  -6.136  1.00 37.91           C  
ANISOU 3777  CD  PRO B 228     4374   6099   3932   -530    -25   -720       C  
ATOM   3778  N   PHE B 229      19.004   1.783  -9.063  1.00 32.69           N  
ANISOU 3778  N   PHE B 229     3813   5187   3422   -431    -11   -725       N  
ATOM   3779  CA  PHE B 229      17.803   1.807  -9.887  1.00 35.26           C  
ANISOU 3779  CA  PHE B 229     4176   5419   3801   -396     -2   -729       C  
ATOM   3780  C   PHE B 229      17.913   2.887 -10.959  1.00 35.21           C  
ANISOU 3780  C   PHE B 229     4203   5347   3830   -400     17   -771       C  
ATOM   3781  O   PHE B 229      18.845   3.700 -10.971  1.00 32.81           O  
ANISOU 3781  O   PHE B 229     3894   5067   3506   -434     27   -802       O  
ATOM   3782  CB  PHE B 229      16.555   2.032  -9.028  1.00 29.31           C  
ANISOU 3782  CB  PHE B 229     3429   4663   3042   -408     14   -751       C  
ATOM   3783  CG  PHE B 229      16.392   1.026  -7.931  1.00 30.63           C  
ANISOU 3783  CG  PHE B 229     3566   4898   3176   -408     -4   -711       C  
ATOM   3784  CD1 PHE B 229      16.165  -0.305  -8.227  1.00 29.66           C  
ANISOU 3784  CD1 PHE B 229     3435   4763   3070   -361    -28   -649       C  
ATOM   3785  CD2 PHE B 229      16.470   1.416  -6.595  1.00 35.95           C  
ANISOU 3785  CD2 PHE B 229     4215   5647   3797   -455      6   -736       C  
ATOM   3786  CE1 PHE B 229      16.012  -1.243  -7.218  1.00 31.00           C  
ANISOU 3786  CE1 PHE B 229     3576   4993   3209   -360    -44   -609       C  
ATOM   3787  CE2 PHE B 229      16.321   0.481  -5.570  1.00 35.89           C  
ANISOU 3787  CE2 PHE B 229     4176   5705   3755   -456    -10   -696       C  
ATOM   3788  CZ  PHE B 229      16.087  -0.850  -5.885  1.00 32.92           C  
ANISOU 3788  CZ  PHE B 229     3794   5314   3400   -407    -36   -631       C  
ATOM   3789  N   LEU B 230      16.944   2.878 -11.881  1.00 29.76           N  
ANISOU 3789  N   LEU B 230     3546   4572   3190   -364     22   -768       N  
ATOM   3790  CA  LEU B 230      16.941   3.873 -12.948  1.00 32.68           C  
ANISOU 3790  CA  LEU B 230     3947   4874   3595   -364     40   -802       C  
ATOM   3791  C   LEU B 230      16.929   5.287 -12.381  1.00 34.98           C  
ANISOU 3791  C   LEU B 230     4247   5172   3871   -415     71   -866       C  
ATOM   3792  O   LEU B 230      17.631   6.172 -12.888  1.00 36.83           O  
ANISOU 3792  O   LEU B 230     4491   5392   4109   -436     84   -896       O  
ATOM   3793  CB  LEU B 230      15.739   3.669 -13.877  1.00 32.34           C  
ANISOU 3793  CB  LEU B 230     3937   4746   3606   -321     42   -791       C  
ATOM   3794  CG  LEU B 230      15.852   2.517 -14.875  1.00 33.18           C  
ANISOU 3794  CG  LEU B 230     4044   4823   3739   -272     16   -738       C  
ATOM   3795  CD1 LEU B 230      14.489   2.111 -15.367  1.00 32.54           C  
ANISOU 3795  CD1 LEU B 230     3986   4679   3699   -235     16   -723       C  
ATOM   3796  CD2 LEU B 230      16.748   2.912 -16.035  1.00 33.91           C  
ANISOU 3796  CD2 LEU B 230     4147   4887   3849   -268     15   -743       C  
ATOM   3797  N   LEU B 231      16.133   5.522 -11.339  1.00 32.06           N  
ANISOU 3797  N   LEU B 231     3873   4823   3485   -436     86   -888       N  
ATOM   3798  CA  LEU B 231      16.049   6.830 -10.689  1.00 35.14           C  
ANISOU 3798  CA  LEU B 231     4271   5222   3860   -486    119   -952       C  
ATOM   3799  C   LEU B 231      16.891   6.871  -9.417  1.00 36.92           C  
ANISOU 3799  C   LEU B 231     4460   5547   4023   -534    118   -965       C  
ATOM   3800  O   LEU B 231      16.462   7.389  -8.381  1.00 35.84           O  
ANISOU 3800  O   LEU B 231     4317   5441   3860   -570    138  -1002       O  
ATOM   3801  CB  LEU B 231      14.593   7.183 -10.389  1.00 33.26           C  
ANISOU 3801  CB  LEU B 231     4052   4939   3646   -480    140   -975       C  
ATOM   3802  CG  LEU B 231      13.645   7.289 -11.592  1.00 33.09           C  
ANISOU 3802  CG  LEU B 231     4067   4820   3687   -435    145   -966       C  
ATOM   3803  CD1 LEU B 231      12.237   7.714 -11.164  1.00 32.06           C  
ANISOU 3803  CD1 LEU B 231     3952   4654   3576   -434    168   -992       C  
ATOM   3804  CD2 LEU B 231      14.211   8.252 -12.663  1.00 32.93           C  
ANISOU 3804  CD2 LEU B 231     4070   4748   3695   -440    159   -991       C  
ATOM   3805  N   GLY B 232      18.086   6.292  -9.463  1.00 37.38           N  
ANISOU 3805  N   GLY B 232     4492   5659   4053   -536     94   -934       N  
ATOM   3806  CA  GLY B 232      18.995   6.344  -8.339  1.00 37.54           C  
ANISOU 3806  CA  GLY B 232     4474   5778   4011   -582     91   -944       C  
ATOM   3807  C   GLY B 232      18.618   5.403  -7.216  1.00 36.08           C  
ANISOU 3807  C   GLY B 232     4260   5658   3791   -581     75   -911       C  
ATOM   3808  O   GLY B 232      18.703   4.184  -7.368  1.00 35.97           O  
ANISOU 3808  O   GLY B 232     4230   5657   3779   -542     46   -851       O  
ATOM   3809  N   GLN B 233      18.220   5.952  -6.076  1.00 35.51           N  
ANISOU 3809  N   GLN B 233     4179   5629   3685   -624     95   -951       N  
ATOM   3810  CA  GLN B 233      17.769   5.133  -4.959  1.00 39.07           C  
ANISOU 3810  CA  GLN B 233     4603   6142   4101   -627     83   -922       C  
ATOM   3811  C   GLN B 233      16.263   4.894  -4.967  1.00 37.51           C  
ANISOU 3811  C   GLN B 233     4428   5886   3938   -597     90   -919       C  
ATOM   3812  O   GLN B 233      15.757   4.189  -4.089  1.00 37.54           O  
ANISOU 3812  O   GLN B 233     4412   5935   3917   -596     81   -894       O  
ATOM   3813  CB  GLN B 233      18.185   5.776  -3.634  1.00 38.95           C  
ANISOU 3813  CB  GLN B 233     4560   6216   4023   -693     98   -965       C  
ATOM   3814  CG  GLN B 233      19.585   6.380  -3.684  1.00 42.67           C  
ANISOU 3814  CG  GLN B 233     5015   6734   4465   -732    100   -988       C  
ATOM   3815  CD  GLN B 233      20.552   5.619  -2.817  1.00 44.02           C  
ANISOU 3815  CD  GLN B 233     5136   7016   4574   -750     74   -949       C  
ATOM   3816  OE1 GLN B 233      20.577   4.384  -2.841  1.00 48.61           O  
ANISOU 3816  OE1 GLN B 233     5699   7615   5155   -710     43   -882       O  
ATOM   3817  NE2 GLN B 233      21.370   6.338  -2.061  1.00 40.70           N  
ANISOU 3817  NE2 GLN B 233     4692   6670   4101   -811     86   -989       N  
ATOM   3818  N   ARG B 234      15.542   5.449  -5.935  1.00 36.46           N  
ANISOU 3818  N   ARG B 234     4335   5659   3861   -573    107   -941       N  
ATOM   3819  CA  ARG B 234      14.099   5.270  -6.030  1.00 34.99           C  
ANISOU 3819  CA  ARG B 234     4170   5414   3710   -544    115   -938       C  
ATOM   3820  C   ARG B 234      13.795   4.138  -7.005  1.00 35.05           C  
ANISOU 3820  C   ARG B 234     4187   5372   3757   -482     88   -877       C  
ATOM   3821  O   ARG B 234      14.217   4.185  -8.166  1.00 33.63           O  
ANISOU 3821  O   ARG B 234     4024   5143   3611   -457     81   -866       O  
ATOM   3822  CB  ARG B 234      13.432   6.564  -6.490  1.00 37.50           C  
ANISOU 3822  CB  ARG B 234     4524   5657   4066   -554    151   -998       C  
ATOM   3823  CG  ARG B 234      11.909   6.492  -6.564  1.00 31.56           C  
ANISOU 3823  CG  ARG B 234     3793   4846   3351   -526    163   -999       C  
ATOM   3824  CD  ARG B 234      11.349   7.814  -7.020  1.00 33.46           C  
ANISOU 3824  CD  ARG B 234     4067   5016   3630   -536    199  -1056       C  
ATOM   3825  NE  ARG B 234       9.890   7.820  -6.988  1.00 31.10           N  
ANISOU 3825  NE  ARG B 234     3785   4667   3364   -513    213  -1061       N  
ATOM   3826  CZ  ARG B 234       9.133   8.796  -7.472  1.00 34.43           C  
ANISOU 3826  CZ  ARG B 234     4237   5016   3829   -509    242  -1099       C  
ATOM   3827  NH1 ARG B 234       9.664   9.832  -8.100  1.00 33.48           N  
ANISOU 3827  NH1 ARG B 234     4135   4858   3729   -523    262  -1134       N  
ATOM   3828  NH2 ARG B 234       7.808   8.729  -7.324  1.00 31.08           N  
ANISOU 3828  NH2 ARG B 234     3823   4557   3429   -488    253  -1101       N  
ATOM   3829  N   ALA B 235      13.063   3.127  -6.544  1.00 32.81           N  
ANISOU 3829  N   ALA B 235     3892   5103   3470   -459     72   -837       N  
ATOM   3830  CA  ALA B 235      12.688   2.015  -7.408  1.00 32.23           C  
ANISOU 3830  CA  ALA B 235     3828   4983   3434   -403     49   -781       C  
ATOM   3831  C   ALA B 235      11.364   2.309  -8.104  1.00 28.30           C  
ANISOU 3831  C   ALA B 235     3367   4398   2989   -375     64   -795       C  
ATOM   3832  O   ALA B 235      10.488   2.983  -7.552  1.00 33.94           O  
ANISOU 3832  O   ALA B 235     4090   5103   3704   -394     87   -834       O  
ATOM   3833  CB  ALA B 235      12.584   0.716  -6.609  1.00 32.24           C  
ANISOU 3833  CB  ALA B 235     3800   5042   3408   -390     24   -726       C  
ATOM   3834  N   THR B 236      11.232   1.812  -9.335  1.00 28.93           N  
ANISOU 3834  N   THR B 236     3465   4414   3113   -330     50   -765       N  
ATOM   3835  CA  THR B 236      10.006   1.934 -10.115  1.00 26.25           C  
ANISOU 3835  CA  THR B 236     3157   3993   2824   -298     60   -769       C  
ATOM   3836  C   THR B 236       9.716   0.601 -10.789  1.00 26.60           C  
ANISOU 3836  C   THR B 236     3202   4011   2893   -249     33   -710       C  
ATOM   3837  O   THR B 236      10.559  -0.299 -10.821  1.00 24.09           O  
ANISOU 3837  O   THR B 236     2864   3728   2560   -238      9   -670       O  
ATOM   3838  CB  THR B 236      10.098   3.012 -11.198  1.00 26.78           C  
ANISOU 3838  CB  THR B 236     3253   3994   2927   -296     77   -804       C  
ATOM   3839  OG1 THR B 236      10.926   2.525 -12.262  1.00 27.33           O  
ANISOU 3839  OG1 THR B 236     3326   4045   3013   -271     57   -773       O  
ATOM   3840  CG2 THR B 236      10.701   4.277 -10.649  1.00 30.64           C  
ANISOU 3840  CG2 THR B 236     3740   4511   3392   -346    103   -860       C  
ATOM   3841  N   TYR B 237       8.515   0.492 -11.374  1.00 25.00           N  
ANISOU 3841  N   TYR B 237     3023   3746   2731   -220     38   -707       N  
ATOM   3842  CA  TYR B 237       8.163  -0.734 -12.081  1.00 25.02           C  
ANISOU 3842  CA  TYR B 237     3029   3718   2761   -175     15   -656       C  
ATOM   3843  C   TYR B 237       9.126  -1.031 -13.231  1.00 24.39           C  
ANISOU 3843  C   TYR B 237     2954   3615   2699   -154      0   -635       C  
ATOM   3844  O   TYR B 237       9.318  -2.199 -13.582  1.00 23.79           O  
ANISOU 3844  O   TYR B 237     2870   3538   2630   -125    -22   -588       O  
ATOM   3845  CB  TYR B 237       6.726  -0.687 -12.624  1.00 22.68           C  
ANISOU 3845  CB  TYR B 237     2757   3355   2505   -150     24   -660       C  
ATOM   3846  CG  TYR B 237       6.304  -2.049 -13.125  1.00 23.64           C  
ANISOU 3846  CG  TYR B 237     2879   3456   2647   -110      1   -607       C  
ATOM   3847  CD1 TYR B 237       6.270  -3.133 -12.256  1.00 21.07           C  
ANISOU 3847  CD1 TYR B 237     2530   3179   2297   -108    -14   -571       C  
ATOM   3848  CD2 TYR B 237       6.015  -2.273 -14.473  1.00 23.63           C  
ANISOU 3848  CD2 TYR B 237     2899   3390   2688    -76     -5   -594       C  
ATOM   3849  CE1 TYR B 237       5.927  -4.401 -12.695  1.00 23.23           C  
ANISOU 3849  CE1 TYR B 237     2803   3432   2591    -73    -33   -523       C  
ATOM   3850  CE2 TYR B 237       5.655  -3.544 -14.933  1.00 23.66           C  
ANISOU 3850  CE2 TYR B 237     2903   3376   2711    -42    -24   -549       C  
ATOM   3851  CZ  TYR B 237       5.631  -4.608 -14.040  1.00 24.72           C  
ANISOU 3851  CZ  TYR B 237     3015   3556   2823    -40    -38   -514       C  
ATOM   3852  OH  TYR B 237       5.282  -5.873 -14.464  1.00 24.40           O  
ANISOU 3852  OH  TYR B 237     2974   3495   2803     -8    -54   -470       O  
ATOM   3853  N   ALA B 238       9.727  -0.011 -13.844  1.00 23.79           N  
ANISOU 3853  N   ALA B 238     2891   3517   2630   -168     12   -668       N  
ATOM   3854  CA  ALA B 238      10.686  -0.306 -14.913  1.00 25.76           C  
ANISOU 3854  CA  ALA B 238     3143   3750   2894   -150     -2   -648       C  
ATOM   3855  C   ALA B 238      11.885  -1.088 -14.391  1.00 27.58           C  
ANISOU 3855  C   ALA B 238     3342   4047   3089   -156    -22   -617       C  
ATOM   3856  O   ALA B 238      12.454  -1.907 -15.122  1.00 26.84           O  
ANISOU 3856  O   ALA B 238     3244   3944   3009   -128    -40   -582       O  
ATOM   3857  CB  ALA B 238      11.159   0.976 -15.597  1.00 26.13           C  
ANISOU 3857  CB  ALA B 238     3209   3767   2954   -167     16   -689       C  
ATOM   3858  N   ASP B 239      12.285  -0.861 -13.137  1.00 25.74           N  
ANISOU 3858  N   ASP B 239     3085   3883   2811   -191    -18   -629       N  
ATOM   3859  CA  ASP B 239      13.366  -1.668 -12.580  1.00 25.49           C  
ANISOU 3859  CA  ASP B 239     3020   3921   2746   -195    -38   -594       C  
ATOM   3860  C   ASP B 239      12.922  -3.104 -12.379  1.00 26.90           C  
ANISOU 3860  C   ASP B 239     3186   4105   2930   -162    -59   -538       C  
ATOM   3861  O   ASP B 239      13.734  -4.027 -12.480  1.00 24.82           O  
ANISOU 3861  O   ASP B 239     2902   3867   2660   -145    -79   -496       O  
ATOM   3862  CB  ASP B 239      13.838  -1.086 -11.246  1.00 25.04           C  
ANISOU 3862  CB  ASP B 239     2937   3940   2635   -244    -30   -619       C  
ATOM   3863  CG  ASP B 239      14.138   0.391 -11.338  1.00 29.74           C  
ANISOU 3863  CG  ASP B 239     3547   4527   3226   -281     -5   -679       C  
ATOM   3864  OD1 ASP B 239      15.290   0.731 -11.686  1.00 31.05           O  
ANISOU 3864  OD1 ASP B 239     3705   4711   3380   -294     -8   -686       O  
ATOM   3865  OD2 ASP B 239      13.228   1.215 -11.082  1.00 32.72           O  
ANISOU 3865  OD2 ASP B 239     3943   4878   3612   -296     18   -719       O  
ATOM   3866  N   MET B 240      11.635  -3.305 -12.092  1.00 22.99           N  
ANISOU 3866  N   MET B 240     2702   3585   2449   -153    -53   -538       N  
ATOM   3867  CA  MET B 240      11.117  -4.649 -11.886  1.00 24.12           C  
ANISOU 3867  CA  MET B 240     2835   3730   2599   -123    -70   -487       C  
ATOM   3868  C   MET B 240      10.911  -5.388 -13.197  1.00 24.36           C  
ANISOU 3868  C   MET B 240     2884   3694   2677    -79    -81   -459       C  
ATOM   3869  O   MET B 240      10.966  -6.626 -13.216  1.00 23.80           O  
ANISOU 3869  O   MET B 240     2802   3629   2613    -52    -98   -411       O  
ATOM   3870  CB  MET B 240       9.817  -4.569 -11.081  1.00 21.11           C  
ANISOU 3870  CB  MET B 240     2459   3350   2213   -132    -59   -498       C  
ATOM   3871  CG  MET B 240       9.927  -3.538  -9.939  1.00 24.60           C  
ANISOU 3871  CG  MET B 240     2889   3846   2613   -181    -42   -541       C  
ATOM   3872  SD  MET B 240       8.379  -3.395  -9.017  1.00 29.47           S  
ANISOU 3872  SD  MET B 240     3511   4463   3225   -192    -26   -559       S  
ATOM   3873  CE  MET B 240       8.941  -2.370  -7.672  1.00 25.15           C  
ANISOU 3873  CE  MET B 240     2940   3995   2620   -251     -9   -603       C  
ATOM   3874  N   ILE B 241      10.651  -4.659 -14.287  1.00 24.80           N  
ANISOU 3874  N   ILE B 241     2969   3689   2765    -71    -70   -489       N  
ATOM   3875  CA  ILE B 241      10.583  -5.283 -15.605  1.00 23.30           C  
ANISOU 3875  CA  ILE B 241     2796   3441   2617    -33    -79   -466       C  
ATOM   3876  C   ILE B 241      11.902  -5.987 -15.925  1.00 25.07           C  
ANISOU 3876  C   ILE B 241     3001   3690   2834    -21    -96   -435       C  
ATOM   3877  O   ILE B 241      11.926  -7.161 -16.318  1.00 25.27           O  
ANISOU 3877  O   ILE B 241     3022   3702   2878     11   -110   -394       O  
ATOM   3878  CB  ILE B 241      10.219  -4.226 -16.659  1.00 26.99           C  
ANISOU 3878  CB  ILE B 241     3295   3848   3114    -33    -64   -505       C  
ATOM   3879  CG1 ILE B 241       8.760  -3.787 -16.468  1.00 24.14           C  
ANISOU 3879  CG1 ILE B 241     2952   3453   2768    -34    -49   -526       C  
ATOM   3880  CG2 ILE B 241      10.438  -4.769 -18.086  1.00 24.41           C  
ANISOU 3880  CG2 ILE B 241     2981   3470   2822      1    -74   -485       C  
ATOM   3881  CD1 ILE B 241       8.374  -2.601 -17.294  1.00 23.67           C  
ANISOU 3881  CD1 ILE B 241     2919   3341   2733    -38    -31   -565       C  
ATOM   3882  N   VAL B 242      13.020  -5.283 -15.742  1.00 25.02           N  
ANISOU 3882  N   VAL B 242     2983   3723   2802    -46    -93   -454       N  
ATOM   3883  CA  VAL B 242      14.334  -5.910 -15.895  1.00 24.89           C  
ANISOU 3883  CA  VAL B 242     2942   3740   2773    -38   -109   -424       C  
ATOM   3884  C   VAL B 242      14.591  -6.908 -14.766  1.00 26.16           C  
ANISOU 3884  C   VAL B 242     3070   3963   2906    -37   -123   -382       C  
ATOM   3885  O   VAL B 242      15.135  -7.996 -14.992  1.00 26.89           O  
ANISOU 3885  O   VAL B 242     3148   4063   3008    -10   -139   -338       O  
ATOM   3886  CB  VAL B 242      15.436  -4.833 -15.960  1.00 26.69           C  
ANISOU 3886  CB  VAL B 242     3166   3996   2979    -69   -101   -458       C  
ATOM   3887  CG1 VAL B 242      16.813  -5.484 -16.038  1.00 27.60           C  
ANISOU 3887  CG1 VAL B 242     3253   4154   3080    -61   -118   -427       C  
ATOM   3888  CG2 VAL B 242      15.223  -3.917 -17.154  1.00 27.35           C  
ANISOU 3888  CG2 VAL B 242     3281   4015   3094    -67    -88   -494       C  
ATOM   3889  N   GLY B 243      14.187  -6.569 -13.537  1.00 23.81           N  
ANISOU 3889  N   GLY B 243     2761   3711   2575    -66   -117   -394       N  
ATOM   3890  CA  GLY B 243      14.520  -7.413 -12.397  1.00 26.07           C  
ANISOU 3890  CA  GLY B 243     3012   4066   2829    -70   -131   -353       C  
ATOM   3891  C   GLY B 243      13.876  -8.788 -12.435  1.00 29.07           C  
ANISOU 3891  C   GLY B 243     3389   4423   3232    -33   -143   -302       C  
ATOM   3892  O   GLY B 243      14.466  -9.769 -11.963  1.00 26.54           O  
ANISOU 3892  O   GLY B 243     3041   4144   2900    -21   -158   -254       O  
ATOM   3893  N   GLY B 244      12.660  -8.885 -12.975  1.00 26.78           N  
ANISOU 3893  N   GLY B 244     3129   4070   2978    -15   -136   -310       N  
ATOM   3894  CA  GLY B 244      12.036 -10.190 -13.087  1.00 26.83           C  
ANISOU 3894  CA  GLY B 244     3135   4050   3009     19   -147   -264       C  
ATOM   3895  C   GLY B 244      12.802 -11.101 -14.025  1.00 27.13           C  
ANISOU 3895  C   GLY B 244     3170   4063   3076     54   -159   -230       C  
ATOM   3896  O   GLY B 244      12.900 -12.312 -13.801  1.00 25.96           O  
ANISOU 3896  O   GLY B 244     3005   3923   2934     77   -171   -180       O  
ATOM   3897  N   TRP B 245      13.343 -10.536 -15.098  1.00 24.01           N  
ANISOU 3897  N   TRP B 245     2790   3635   2698     58   -155   -255       N  
ATOM   3898  CA  TRP B 245      14.212 -11.318 -15.959  1.00 25.61           C  
ANISOU 3898  CA  TRP B 245     2987   3821   2924     88   -165   -226       C  
ATOM   3899  C   TRP B 245      15.504 -11.690 -15.226  1.00 26.89           C  
ANISOU 3899  C   TRP B 245     3110   4054   3053     81   -176   -196       C  
ATOM   3900  O   TRP B 245      16.015 -12.805 -15.384  1.00 26.28           O  
ANISOU 3900  O   TRP B 245     3017   3978   2990    110   -187   -150       O  
ATOM   3901  CB  TRP B 245      14.500 -10.534 -17.240  1.00 27.70           C  
ANISOU 3901  CB  TRP B 245     3276   4039   3210     89   -157   -263       C  
ATOM   3902  CG  TRP B 245      13.360 -10.597 -18.251  1.00 27.05           C  
ANISOU 3902  CG  TRP B 245     3227   3881   3169    109   -150   -276       C  
ATOM   3903  CD1 TRP B 245      12.455  -9.608 -18.550  1.00 26.76           C  
ANISOU 3903  CD1 TRP B 245     3218   3810   3141     95   -137   -317       C  
ATOM   3904  CD2 TRP B 245      13.040 -11.702 -19.099  1.00 23.67           C  
ANISOU 3904  CD2 TRP B 245     2810   3405   2780    145   -156   -248       C  
ATOM   3905  NE1 TRP B 245      11.579 -10.048 -19.530  1.00 26.33           N  
ANISOU 3905  NE1 TRP B 245     3188   3693   3126    121   -136   -313       N  
ATOM   3906  CE2 TRP B 245      11.918 -11.331 -19.874  1.00 27.05           C  
ANISOU 3906  CE2 TRP B 245     3269   3774   3234    150   -147   -273       C  
ATOM   3907  CE3 TRP B 245      13.599 -12.976 -19.282  1.00 26.84           C  
ANISOU 3907  CE3 TRP B 245     3195   3807   3196    173   -166   -204       C  
ATOM   3908  CZ2 TRP B 245      11.344 -12.185 -20.811  1.00 26.56           C  
ANISOU 3908  CZ2 TRP B 245     3223   3659   3211    179   -149   -257       C  
ATOM   3909  CZ3 TRP B 245      13.021 -13.827 -20.199  1.00 26.91           C  
ANISOU 3909  CZ3 TRP B 245     3221   3759   3246    203   -166   -190       C  
ATOM   3910  CH2 TRP B 245      11.914 -13.425 -20.964  1.00 27.71           C  
ANISOU 3910  CH2 TRP B 245     3353   3805   3370    204   -158   -218       C  
ATOM   3911  N   LEU B 246      16.032 -10.778 -14.398  1.00 25.00           N  
ANISOU 3911  N   LEU B 246     2854   3874   2770     44   -173   -219       N  
ATOM   3912  CA  LEU B 246      17.225 -11.110 -13.618  1.00 29.45           C  
ANISOU 3912  CA  LEU B 246     3378   4513   3298     35   -185   -189       C  
ATOM   3913  C   LEU B 246      16.955 -12.245 -12.641  1.00 30.85           C  
ANISOU 3913  C   LEU B 246     3530   4725   3465     48   -196   -135       C  
ATOM   3914  O   LEU B 246      17.854 -13.050 -12.360  1.00 28.75           O  
ANISOU 3914  O   LEU B 246     3233   4499   3192     62   -209    -90       O  
ATOM   3915  CB  LEU B 246      17.754  -9.885 -12.861  1.00 27.08           C  
ANISOU 3915  CB  LEU B 246     3065   4273   2950    -12   -178   -228       C  
ATOM   3916  CG  LEU B 246      18.355  -8.760 -13.716  1.00 29.79           C  
ANISOU 3916  CG  LEU B 246     3425   4596   3298    -29   -168   -276       C  
ATOM   3917  CD1 LEU B 246      18.838  -7.594 -12.860  1.00 32.27           C  
ANISOU 3917  CD1 LEU B 246     3726   4973   3564    -79   -159   -315       C  
ATOM   3918  CD2 LEU B 246      19.461  -9.259 -14.631  1.00 27.13           C  
ANISOU 3918  CD2 LEU B 246     3079   4250   2979     -3   -177   -253       C  
ATOM   3919  N   ARG B 247      15.725 -12.343 -12.123  1.00 28.21           N  
ANISOU 3919  N   ARG B 247     3208   4377   3133     43   -191   -137       N  
ATOM   3920  CA  ARG B 247      15.423 -13.456 -11.230  1.00 30.07           C  
ANISOU 3920  CA  ARG B 247     3421   4643   3360     55   -202    -84       C  
ATOM   3921  C   ARG B 247      15.378 -14.767 -12.002  1.00 29.43           C  
ANISOU 3921  C   ARG B 247     3345   4511   3327    103   -209    -38       C  
ATOM   3922  O   ARG B 247      15.832 -15.801 -11.505  1.00 30.67           O  
ANISOU 3922  O   ARG B 247     3474   4698   3480    120   -220     17       O  
ATOM   3923  CB  ARG B 247      14.103 -13.218 -10.489  1.00 29.34           C  
ANISOU 3923  CB  ARG B 247     3340   4549   3257     37   -193    -99       C  
ATOM   3924  CG  ARG B 247      14.084 -11.966  -9.632  1.00 29.29           C  
ANISOU 3924  CG  ARG B 247     3329   4596   3205    -11   -184   -145       C  
ATOM   3925  CD  ARG B 247      14.505 -12.258  -8.180  1.00 28.80           C  
ANISOU 3925  CD  ARG B 247     3226   4626   3092    -34   -193   -114       C  
ATOM   3926  NE  ARG B 247      15.055 -11.048  -7.583  1.00 30.78           N  
ANISOU 3926  NE  ARG B 247     3466   4934   3296    -80   -185   -159       N  
ATOM   3927  CZ  ARG B 247      15.676 -10.983  -6.412  1.00 34.84           C  
ANISOU 3927  CZ  ARG B 247     3942   5538   3757   -110   -191   -145       C  
ATOM   3928  NH1 ARG B 247      15.768 -12.037  -5.615  1.00 31.20           N  
ANISOU 3928  NH1 ARG B 247     3451   5124   3281   -100   -206    -86       N  
ATOM   3929  NH2 ARG B 247      16.198  -9.823  -6.024  1.00 31.56           N  
ANISOU 3929  NH2 ARG B 247     3520   5167   3304   -153   -182   -193       N  
ATOM   3930  N   MET B 248      14.822 -14.755 -13.211  1.00 25.81           N  
ANISOU 3930  N   MET B 248     2921   3974   2912    123   -202    -60       N  
ATOM   3931  CA  MET B 248      14.807 -15.994 -13.974  1.00 29.25           C  
ANISOU 3931  CA  MET B 248     3362   4361   3393    165   -206    -21       C  
ATOM   3932  C   MET B 248      16.228 -16.413 -14.354  1.00 30.35           C  
ANISOU 3932  C   MET B 248     3477   4519   3535    183   -214      5       C  
ATOM   3933  O   MET B 248      16.542 -17.609 -14.366  1.00 30.26           O  
ANISOU 3933  O   MET B 248     3450   4502   3544    213   -221     55       O  
ATOM   3934  CB  MET B 248      13.931 -15.844 -15.215  1.00 26.79           C  
ANISOU 3934  CB  MET B 248     3090   3966   3124    180   -196    -52       C  
ATOM   3935  CG  MET B 248      14.183 -16.928 -16.246  1.00 31.69           C  
ANISOU 3935  CG  MET B 248     3716   4534   3790    220   -199    -24       C  
ATOM   3936  SD  MET B 248      13.466 -16.548 -17.846  1.00 34.82           S  
ANISOU 3936  SD  MET B 248     4156   4844   4228    231   -188    -68       S  
ATOM   3937  CE  MET B 248      13.471 -18.180 -18.611  1.00 32.17           C  
ANISOU 3937  CE  MET B 248     3823   4459   3944    275   -190    -24       C  
ATOM   3938  N   MET B 249      17.108 -15.444 -14.608  1.00 27.42           N  
ANISOU 3938  N   MET B 249     3102   4173   3144    163   -213    -28       N  
ATOM   3939  CA  MET B 249      18.507 -15.761 -14.908  1.00 31.70           C  
ANISOU 3939  CA  MET B 249     3619   4740   3684    177   -220     -6       C  
ATOM   3940  C   MET B 249      19.187 -16.448 -13.723  1.00 31.74           C  
ANISOU 3940  C   MET B 249     3580   4820   3660    177   -233     47       C  
ATOM   3941  O   MET B 249      19.852 -17.482 -13.883  1.00 34.17           O  
ANISOU 3941  O   MET B 249     3867   5129   3987    209   -240     95       O  
ATOM   3942  CB  MET B 249      19.263 -14.483 -15.248  1.00 31.07           C  
ANISOU 3942  CB  MET B 249     3543   4681   3582    148   -216    -54       C  
ATOM   3943  CG  MET B 249      19.232 -14.051 -16.695  1.00 35.09           C  
ANISOU 3943  CG  MET B 249     4083   5123   4125    159   -207    -90       C  
ATOM   3944  SD  MET B 249      19.381 -12.239 -16.766  1.00 33.95           S  
ANISOU 3944  SD  MET B 249     3955   4994   3951    113   -196   -158       S  
ATOM   3945  CE  MET B 249      21.156 -12.064 -16.522  1.00 36.41           C  
ANISOU 3945  CE  MET B 249     4227   5378   4229    101   -204   -147       C  
ATOM   3946  N   ARG B 250      19.070 -15.859 -12.524  1.00 33.58           N  
ANISOU 3946  N   ARG B 250     3796   5118   3844    141   -235     40       N  
ATOM   3947  CA  ARG B 250      19.713 -16.460 -11.356  1.00 33.90           C  
ANISOU 3947  CA  ARG B 250     3792   5237   3851    138   -248     92       C  
ATOM   3948  C   ARG B 250      19.228 -17.883 -11.145  1.00 33.79           C  
ANISOU 3948  C   ARG B 250     3771   5200   3866    174   -253    152       C  
ATOM   3949  O   ARG B 250      20.011 -18.757 -10.756  1.00 35.72           O  
ANISOU 3949  O   ARG B 250     3982   5482   4109    194   -264    208       O  
ATOM   3950  CB  ARG B 250      19.466 -15.625 -10.089  1.00 37.10           C  
ANISOU 3950  CB  ARG B 250     4184   5714   4200     91   -247     72       C  
ATOM   3951  CG  ARG B 250      20.079 -16.216  -8.781  1.00 40.50           C  
ANISOU 3951  CG  ARG B 250     4565   6234   4588     83   -261    127       C  
ATOM   3952  CD  ARG B 250      20.773 -15.156  -7.883  1.00 40.82           C  
ANISOU 3952  CD  ARG B 250     4579   6364   4565     33   -263     99       C  
ATOM   3953  NE  ARG B 250      22.091 -15.587  -7.406  1.00 52.95           N  
ANISOU 3953  NE  ARG B 250     6068   7975   6074     37   -277    145       N  
ATOM   3954  CZ  ARG B 250      22.988 -14.805  -6.800  1.00 53.53           C  
ANISOU 3954  CZ  ARG B 250     6113   8129   6095     -2   -281    128       C  
ATOM   3955  NH1 ARG B 250      22.744 -13.526  -6.549  1.00 50.78           N  
ANISOU 3955  NH1 ARG B 250     5779   7799   5715    -48   -269     63       N  
ATOM   3956  NH2 ARG B 250      24.174 -15.312  -6.461  1.00 51.49           N  
ANISOU 3956  NH2 ARG B 250     5811   7936   5818      7   -295    175       N  
ATOM   3957  N   ALA B 251      17.955 -18.141 -11.427  1.00 30.96           N  
ANISOU 3957  N   ALA B 251     3444   4781   3537    183   -246    143       N  
ATOM   3958  CA  ALA B 251      17.401 -19.473 -11.219  1.00 33.36           C  
ANISOU 3958  CA  ALA B 251     3745   5060   3871    215   -249    197       C  
ATOM   3959  C   ALA B 251      17.817 -20.462 -12.304  1.00 34.13           C  
ANISOU 3959  C   ALA B 251     3848   5097   4022    260   -248    224       C  
ATOM   3960  O   ALA B 251      17.897 -21.668 -12.033  1.00 34.73           O  
ANISOU 3960  O   ALA B 251     3907   5170   4118    288   -253    282       O  
ATOM   3961  CB  ALA B 251      15.878 -19.392 -11.129  1.00 34.66           C  
ANISOU 3961  CB  ALA B 251     3940   5182   4046    206   -241    176       C  
ATOM   3962  N   THR B 252      18.097 -19.998 -13.525  1.00 29.43           N  
ANISOU 3962  N   THR B 252     3276   4455   3451    267   -241    184       N  
ATOM   3963  CA  THR B 252      18.250 -20.917 -14.644  1.00 31.04           C  
ANISOU 3963  CA  THR B 252     3492   4592   3709    308   -237    200       C  
ATOM   3964  C   THR B 252      19.619 -20.904 -15.318  1.00 33.07           C  
ANISOU 3964  C   THR B 252     3733   4859   3974    322   -239    203       C  
ATOM   3965  O   THR B 252      19.933 -21.863 -16.030  1.00 32.92           O  
ANISOU 3965  O   THR B 252     3714   4797   3997    359   -236    229       O  
ATOM   3966  CB  THR B 252      17.185 -20.641 -15.719  1.00 34.74           C  
ANISOU 3966  CB  THR B 252     4007   4981   4213    310   -225    155       C  
ATOM   3967  OG1 THR B 252      17.287 -19.282 -16.165  1.00 34.03           O  
ANISOU 3967  OG1 THR B 252     3935   4894   4103    282   -221     96       O  
ATOM   3968  CG2 THR B 252      15.789 -20.876 -15.150  1.00 34.46           C  
ANISOU 3968  CG2 THR B 252     3987   4928   4178    303   -223    159       C  
ATOM   3969  N   LEU B 253      20.427 -19.861 -15.143  1.00 32.88           N  
ANISOU 3969  N   LEU B 253     3695   4886   3910    295   -242    175       N  
ATOM   3970  CA  LEU B 253      21.736 -19.894 -15.793  1.00 35.29           C  
ANISOU 3970  CA  LEU B 253     3984   5202   4223    310   -244    178       C  
ATOM   3971  C   LEU B 253      22.696 -20.795 -15.019  1.00 35.07           C  
ANISOU 3971  C   LEU B 253     3910   5230   4186    329   -255    243       C  
ATOM   3972  O   LEU B 253      22.558 -20.959 -13.805  1.00 33.71           O  
ANISOU 3972  O   LEU B 253     3713   5114   3982    316   -263    275       O  
ATOM   3973  CB  LEU B 253      22.335 -18.492 -15.882  1.00 35.01           C  
ANISOU 3973  CB  LEU B 253     3949   5204   4150    273   -244    128       C  
ATOM   3974  CG  LEU B 253      21.735 -17.554 -16.925  1.00 32.34           C  
ANISOU 3974  CG  LEU B 253     3655   4807   3827    259   -232     65       C  
ATOM   3975  CD1 LEU B 253      22.250 -16.158 -16.710  1.00 34.42           C  
ANISOU 3975  CD1 LEU B 253     3915   5115   4047    218   -231     20       C  
ATOM   3976  CD2 LEU B 253      22.082 -18.045 -18.321  1.00 34.30           C  
ANISOU 3976  CD2 LEU B 253     3917   4993   4121    292   -226     61       C  
ATOM   3977  N   PRO B 254      23.691 -21.379 -15.685  1.00 40.42           N  
ANISOU 3977  N   PRO B 254     4571   5896   4889    359   -255    265       N  
ATOM   3978  CA  PRO B 254      24.806 -21.958 -14.932  1.00 38.16           C  
ANISOU 3978  CA  PRO B 254     4235   5677   4586    372   -266    322       C  
ATOM   3979  C   PRO B 254      25.369 -20.908 -13.986  1.00 39.74           C  
ANISOU 3979  C   PRO B 254     4410   5969   4721    329   -276    307       C  
ATOM   3980  O   PRO B 254      25.400 -19.715 -14.302  1.00 35.96           O  
ANISOU 3980  O   PRO B 254     3949   5495   4219    296   -272    249       O  
ATOM   3981  CB  PRO B 254      25.816 -22.349 -16.019  1.00 42.24           C  
ANISOU 3981  CB  PRO B 254     4746   6166   5138    404   -261    325       C  
ATOM   3982  CG  PRO B 254      25.012 -22.512 -17.248  1.00 39.74           C  
ANISOU 3982  CG  PRO B 254     4475   5756   4870    420   -247    290       C  
ATOM   3983  CD  PRO B 254      23.872 -21.521 -17.140  1.00 38.61           C  
ANISOU 3983  CD  PRO B 254     4366   5598   4705    383   -245    239       C  
ATOM   3984  N   VAL B 255      25.792 -21.363 -12.804  1.00 37.14           N  
ANISOU 3984  N   VAL B 255     4037   5712   4361    328   -288    361       N  
ATOM   3985  CA  VAL B 255      26.274 -20.442 -11.777  1.00 42.12           C  
ANISOU 3985  CA  VAL B 255     4641   6437   4926    283   -297    350       C  
ATOM   3986  C   VAL B 255      27.358 -19.526 -12.329  1.00 42.44           C  
ANISOU 3986  C   VAL B 255     4674   6504   4948    266   -296    311       C  
ATOM   3987  O   VAL B 255      27.342 -18.309 -12.097  1.00 39.07           O  
ANISOU 3987  O   VAL B 255     4255   6109   4480    221   -295    260       O  
ATOM   3988  CB  VAL B 255      26.770 -21.227 -10.548  1.00 45.80           C  
ANISOU 3988  CB  VAL B 255     5056   6980   5366    291   -311    423       C  
ATOM   3989  CG1 VAL B 255      27.158 -20.276  -9.433  1.00 46.87           C  
ANISOU 3989  CG1 VAL B 255     5163   7215   5429    240   -320    409       C  
ATOM   3990  CG2 VAL B 255      25.687 -22.199 -10.080  1.00 46.61           C  
ANISOU 3990  CG2 VAL B 255     5168   7050   5493    310   -311    464       C  
ATOM   3991  N   SER B 256      28.311 -20.089 -13.080  1.00 40.85           N  
ANISOU 3991  N   SER B 256     4458   6287   4776    300   -296    333       N  
ATOM   3992  CA  SER B 256      29.420 -19.277 -13.567  1.00 41.90           C  
ANISOU 3992  CA  SER B 256     4580   6451   4889    284   -297    300       C  
ATOM   3993  C   SER B 256      28.938 -18.171 -14.507  1.00 41.40           C  
ANISOU 3993  C   SER B 256     4564   6334   4833    259   -284    224       C  
ATOM   3994  O   SER B 256      29.438 -17.041 -14.441  1.00 38.91           O  
ANISOU 3994  O   SER B 256     4245   6059   4479    221   -284    182       O  
ATOM   3995  CB  SER B 256      30.467 -20.177 -14.233  1.00 46.79           C  
ANISOU 3995  CB  SER B 256     5174   7059   5544    329   -297    340       C  
ATOM   3996  OG  SER B 256      30.232 -20.323 -15.619  1.00 46.67           O  
ANISOU 3996  OG  SER B 256     5196   6955   5581    354   -284    310       O  
ATOM   3997  N   GLU B 257      27.940 -18.461 -15.359  1.00 37.50           N  
ANISOU 3997  N   GLU B 257     4113   5750   4386    280   -273    206       N  
ATOM   3998  CA  GLU B 257      27.443 -17.453 -16.300  1.00 41.20           C  
ANISOU 3998  CA  GLU B 257     4626   6165   4864    260   -262    138       C  
ATOM   3999  C   GLU B 257      26.616 -16.379 -15.592  1.00 39.87           C  
ANISOU 3999  C   GLU B 257     4475   6017   4657    213   -259     97       C  
ATOM   4000  O   GLU B 257      26.674 -15.198 -15.958  1.00 34.16           O  
ANISOU 4000  O   GLU B 257     3770   5291   3916    182   -252     42       O  
ATOM   4001  CB  GLU B 257      26.628 -18.123 -17.411  1.00 39.85           C  
ANISOU 4001  CB  GLU B 257     4493   5897   4753    294   -252    133       C  
ATOM   4002  CG  GLU B 257      27.455 -19.072 -18.297  1.00 43.02           C  
ANISOU 4002  CG  GLU B 257     4882   6270   5196    338   -250    161       C  
ATOM   4003  CD  GLU B 257      26.618 -19.816 -19.335  1.00 42.84           C  
ANISOU 4003  CD  GLU B 257     4894   6153   5230    371   -239    157       C  
ATOM   4004  OE1 GLU B 257      25.364 -19.728 -19.288  1.00 42.59           O  
ANISOU 4004  OE1 GLU B 257     4894   6081   5207    362   -234    140       O  
ATOM   4005  OE2 GLU B 257      27.213 -20.491 -20.202  1.00 40.12           O  
ANISOU 4005  OE2 GLU B 257     4546   5777   4923    403   -233    170       O  
ATOM   4006  N   TRP B 258      25.838 -16.766 -14.576  1.00 38.22           N  
ANISOU 4006  N   TRP B 258     4260   5827   4435    209   -264    123       N  
ATOM   4007  CA  TRP B 258      25.176 -15.760 -13.749  1.00 38.48           C  
ANISOU 4007  CA  TRP B 258     4302   5893   4426    163   -261     86       C  
ATOM   4008  C   TRP B 258      26.201 -14.858 -13.067  1.00 39.67           C  
ANISOU 4008  C   TRP B 258     4421   6130   4520    122   -266     71       C  
ATOM   4009  O   TRP B 258      25.985 -13.648 -12.934  1.00 36.74           O  
ANISOU 4009  O   TRP B 258     4067   5771   4122     81   -258     16       O  
ATOM   4010  CB  TRP B 258      24.272 -16.431 -12.715  1.00 36.69           C  
ANISOU 4010  CB  TRP B 258     4068   5680   4192    165   -266    123       C  
ATOM   4011  CG  TRP B 258      23.798 -15.489 -11.638  1.00 39.59           C  
ANISOU 4011  CG  TRP B 258     4433   6101   4508    117   -264     93       C  
ATOM   4012  CD1 TRP B 258      24.211 -15.462 -10.336  1.00 41.20           C  
ANISOU 4012  CD1 TRP B 258     4597   6395   4661     92   -274    119       C  
ATOM   4013  CD2 TRP B 258      22.843 -14.427 -11.774  1.00 37.83           C  
ANISOU 4013  CD2 TRP B 258     4248   5846   4281     86   -251     32       C  
ATOM   4014  NE1 TRP B 258      23.574 -14.453  -9.659  1.00 41.16           N  
ANISOU 4014  NE1 TRP B 258     4604   6417   4620     46   -267     74       N  
ATOM   4015  CE2 TRP B 258      22.724 -13.806 -10.516  1.00 39.54           C  
ANISOU 4015  CE2 TRP B 258     4446   6135   4444     44   -252     21       C  
ATOM   4016  CE3 TRP B 258      22.074 -13.942 -12.837  1.00 35.89           C  
ANISOU 4016  CE3 TRP B 258     4048   5518   4071     92   -238    -13       C  
ATOM   4017  CZ2 TRP B 258      21.872 -12.725 -10.293  1.00 37.89           C  
ANISOU 4017  CZ2 TRP B 258     4264   5915   4219      7   -239    -36       C  
ATOM   4018  CZ3 TRP B 258      21.224 -12.869 -12.607  1.00 33.76           C  
ANISOU 4018  CZ3 TRP B 258     3803   5238   3785     57   -226    -66       C  
ATOM   4019  CH2 TRP B 258      21.131 -12.278 -11.348  1.00 37.41           C  
ANISOU 4019  CH2 TRP B 258     4247   5770   4197     16   -226    -77       C  
ATOM   4020  N   GLN B 259      27.336 -15.423 -12.645  1.00 37.04           N  
ANISOU 4020  N   GLN B 259     4042   5859   4170    134   -278    117       N  
ATOM   4021  CA  GLN B 259      28.358 -14.579 -12.034  1.00 42.57           C  
ANISOU 4021  CA  GLN B 259     4712   6647   4817     94   -283    101       C  
ATOM   4022  C   GLN B 259      28.953 -13.614 -13.054  1.00 38.78           C  
ANISOU 4022  C   GLN B 259     4251   6144   4341     79   -274     47       C  
ATOM   4023  O   GLN B 259      29.261 -12.465 -12.717  1.00 40.24           O  
ANISOU 4023  O   GLN B 259     4433   6371   4485     33   -270      4       O  
ATOM   4024  CB  GLN B 259      29.448 -15.436 -11.386  1.00 41.72           C  
ANISOU 4024  CB  GLN B 259     4548   6613   4689    112   -299    167       C  
ATOM   4025  CG  GLN B 259      29.049 -15.961 -10.008  1.00 47.34           C  
ANISOU 4025  CG  GLN B 259     5231   7384   5370    104   -309    213       C  
ATOM   4026  CD  GLN B 259      28.545 -14.860  -9.072  1.00 52.83           C  
ANISOU 4026  CD  GLN B 259     5932   8130   6012     46   -305    168       C  
ATOM   4027  OE1 GLN B 259      29.131 -13.770  -8.990  1.00 53.81           O  
ANISOU 4027  OE1 GLN B 259     6051   8296   6099      4   -301    123       O  
ATOM   4028  NE2 GLN B 259      27.444 -15.137  -8.372  1.00 49.90           N  
ANISOU 4028  NE2 GLN B 259     5571   7752   5637     41   -304    179       N  
ATOM   4029  N   GLU B 260      29.116 -14.050 -14.305  1.00 37.37           N  
ANISOU 4029  N   GLU B 260     4091   5897   4212    116   -269     48       N  
ATOM   4030  CA  GLU B 260      29.631 -13.137 -15.319  1.00 38.03           C  
ANISOU 4030  CA  GLU B 260     4194   5955   4301    102   -260     -2       C  
ATOM   4031  C   GLU B 260      28.644 -12.014 -15.594  1.00 38.45           C  
ANISOU 4031  C   GLU B 260     4292   5963   4353     71   -247    -65       C  
ATOM   4032  O   GLU B 260      29.011 -10.832 -15.553  1.00 37.95           O  
ANISOU 4032  O   GLU B 260     4233   5927   4261     30   -240   -111       O  
ATOM   4033  CB  GLU B 260      29.973 -13.893 -16.601  1.00 42.07           C  
ANISOU 4033  CB  GLU B 260     4715   6405   4866    149   -258     13       C  
ATOM   4034  CG  GLU B 260      30.942 -15.045 -16.391  1.00 44.20           C  
ANISOU 4034  CG  GLU B 260     4940   6712   5142    185   -269     76       C  
ATOM   4035  CD  GLU B 260      31.041 -15.956 -17.597  1.00 49.80           C  
ANISOU 4035  CD  GLU B 260     5662   7350   5910    235   -264     93       C  
ATOM   4036  OE1 GLU B 260      30.742 -15.494 -18.722  1.00 46.37           O  
ANISOU 4036  OE1 GLU B 260     5265   6851   5502    235   -253     49       O  
ATOM   4037  OE2 GLU B 260      31.401 -17.141 -17.416  1.00 53.37           O  
ANISOU 4037  OE2 GLU B 260     6087   7808   6383    273   -270    150       O  
ATOM   4038  N   ALA B 261      27.375 -12.359 -15.847  1.00 37.28           N  
ANISOU 4038  N   ALA B 261     4177   5748   4238     89   -241    -67       N  
ATOM   4039  CA  ALA B 261      26.376 -11.328 -16.106  1.00 37.05           C  
ANISOU 4039  CA  ALA B 261     4190   5674   4212     62   -227   -123       C  
ATOM   4040  C   ALA B 261      26.278 -10.348 -14.940  1.00 40.11           C  
ANISOU 4040  C   ALA B 261     4567   6125   4547     11   -224   -151       C  
ATOM   4041  O   ALA B 261      26.144  -9.134 -15.148  1.00 38.66           O  
ANISOU 4041  O   ALA B 261     4406   5931   4352    -23   -212   -206       O  
ATOM   4042  CB  ALA B 261      25.024 -11.978 -16.394  1.00 36.05           C  
ANISOU 4042  CB  ALA B 261     4094   5477   4125     90   -224   -113       C  
ATOM   4043  N   ARG B 262      26.364 -10.857 -13.703  1.00 33.87           N  
ANISOU 4043  N   ARG B 262     3742   5402   3724      4   -235   -114       N  
ATOM   4044  CA  ARG B 262      26.367  -9.995 -12.523  1.00 36.37           C  
ANISOU 4044  CA  ARG B 262     4044   5789   3986    -47   -232   -138       C  
ATOM   4045  C   ARG B 262      27.453  -8.926 -12.603  1.00 40.74           C  
ANISOU 4045  C   ARG B 262     4585   6388   4506    -85   -228   -177       C  
ATOM   4046  O   ARG B 262      27.266  -7.802 -12.118  1.00 37.24           O  
ANISOU 4046  O   ARG B 262     4151   5968   4032   -131   -217   -225       O  
ATOM   4047  CB  ARG B 262      26.600 -10.836 -11.265  1.00 43.10           C  
ANISOU 4047  CB  ARG B 262     4852   6718   4806    -45   -247    -82       C  
ATOM   4048  CG  ARG B 262      25.380 -11.483 -10.663  1.00 43.24           C  
ANISOU 4048  CG  ARG B 262     4879   6716   4833    -32   -249    -58       C  
ATOM   4049  CD  ARG B 262      25.633 -11.788  -9.184  1.00 41.09           C  
ANISOU 4049  CD  ARG B 262     4563   6541   4510    -54   -260    -22       C  
ATOM   4050  NE  ARG B 262      26.065 -10.596  -8.466  1.00 42.96           N  
ANISOU 4050  NE  ARG B 262     4786   6846   4690   -111   -254    -67       N  
ATOM   4051  CZ  ARG B 262      25.354 -10.005  -7.513  1.00 46.23           C  
ANISOU 4051  CZ  ARG B 262     5202   7292   5069   -150   -247    -94       C  
ATOM   4052  NH1 ARG B 262      24.167 -10.470  -7.147  1.00 37.17           N  
ANISOU 4052  NH1 ARG B 262     4070   6116   3936   -139   -245    -81       N  
ATOM   4053  NH2 ARG B 262      25.833  -8.908  -6.929  1.00 41.95           N  
ANISOU 4053  NH2 ARG B 262     4649   6813   4479   -204   -240   -138       N  
ATOM   4054  N   ALA B 263      28.616  -9.274 -13.158  1.00 38.85           N  
ANISOU 4054  N   ALA B 263     4324   6164   4272    -67   -236   -155       N  
ATOM   4055  CA  ALA B 263      29.771  -8.389 -13.095  1.00 39.44           C  
ANISOU 4055  CA  ALA B 263     4378   6296   4310   -103   -235   -183       C  
ATOM   4056  C   ALA B 263      29.908  -7.476 -14.304  1.00 40.95           C  
ANISOU 4056  C   ALA B 263     4606   6429   4525   -111   -221   -235       C  
ATOM   4057  O   ALA B 263      30.611  -6.463 -14.205  1.00 39.79           O  
ANISOU 4057  O   ALA B 263     4452   6320   4347   -153   -214   -273       O  
ATOM   4058  CB  ALA B 263      31.054  -9.204 -12.932  1.00 39.04           C  
ANISOU 4058  CB  ALA B 263     4280   6308   4247    -83   -251   -130       C  
ATOM   4059  N   TRP B 264      29.250  -7.797 -15.422  1.00 38.54           N  
ANISOU 4059  N   TRP B 264     4337   6034   4274    -75   -215   -238       N  
ATOM   4060  CA  TRP B 264      29.399  -7.020 -16.646  1.00 39.12           C  
ANISOU 4060  CA  TRP B 264     4442   6050   4371    -79   -203   -281       C  
ATOM   4061  C   TRP B 264      29.037  -5.560 -16.411  1.00 37.05           C  
ANISOU 4061  C   TRP B 264     4204   5788   4087   -130   -186   -343       C  
ATOM   4062  O   TRP B 264      28.270  -5.217 -15.509  1.00 36.19           O  
ANISOU 4062  O   TRP B 264     4099   5694   3958   -154   -181   -357       O  
ATOM   4063  CB  TRP B 264      28.508  -7.572 -17.759  1.00 36.39           C  
ANISOU 4063  CB  TRP B 264     4134   5610   4083    -37   -199   -275       C  
ATOM   4064  CG  TRP B 264      28.947  -8.885 -18.326  1.00 34.79           C  
ANISOU 4064  CG  TRP B 264     3916   5392   3912     13   -211   -225       C  
ATOM   4065  CD1 TRP B 264      30.203  -9.418 -18.299  1.00 36.75           C  
ANISOU 4065  CD1 TRP B 264     4125   5689   4149     26   -221   -193       C  
ATOM   4066  CD2 TRP B 264      28.117  -9.838 -19.000  1.00 37.31           C  
ANISOU 4066  CD2 TRP B 264     4257   5640   4280     58   -211   -202       C  
ATOM   4067  NE1 TRP B 264      30.205 -10.653 -18.906  1.00 33.75           N  
ANISOU 4067  NE1 TRP B 264     3742   5272   3810     76   -227   -151       N  
ATOM   4068  CE2 TRP B 264      28.941 -10.928 -19.358  1.00 38.21           C  
ANISOU 4068  CE2 TRP B 264     4344   5762   4411     95   -220   -158       C  
ATOM   4069  CE3 TRP B 264      26.756  -9.875 -19.338  1.00 35.05           C  
ANISOU 4069  CE3 TRP B 264     4008   5285   4023     68   -204   -216       C  
ATOM   4070  CZ2 TRP B 264      28.451 -12.044 -20.033  1.00 35.17           C  
ANISOU 4070  CZ2 TRP B 264     3972   5317   4074    142   -221   -129       C  
ATOM   4071  CZ3 TRP B 264      26.269 -10.987 -20.000  1.00 35.29           C  
ANISOU 4071  CZ3 TRP B 264     4050   5260   4098    113   -206   -186       C  
ATOM   4072  CH2 TRP B 264      27.116 -12.056 -20.344  1.00 35.82           C  
ANISOU 4072  CH2 TRP B 264     4093   5335   4183    148   -214   -144       C  
ATOM   4073  N   HIS B 265      29.613  -4.699 -17.247  1.00 33.76           N  
ANISOU 4073  N   HIS B 265     3801   5352   3675   -147   -177   -380       N  
ATOM   4074  CA  HIS B 265      29.288  -3.275 -17.276  1.00 34.73           C  
ANISOU 4074  CA  HIS B 265     3951   5457   3786   -191   -158   -440       C  
ATOM   4075  C   HIS B 265      29.440  -2.644 -15.896  1.00 38.74           C  
ANISOU 4075  C   HIS B 265     4436   6041   4241   -241   -154   -460       C  
ATOM   4076  O   HIS B 265      28.611  -1.845 -15.456  1.00 37.97           O  
ANISOU 4076  O   HIS B 265     4361   5928   4136   -270   -139   -498       O  
ATOM   4077  CB  HIS B 265      27.881  -3.065 -17.836  1.00 38.09           C  
ANISOU 4077  CB  HIS B 265     4424   5796   4253   -176   -146   -460       C  
ATOM   4078  CG  HIS B 265      27.600  -3.888 -19.053  1.00 35.22           C  
ANISOU 4078  CG  HIS B 265     4079   5364   3940   -126   -151   -435       C  
ATOM   4079  ND1 HIS B 265      28.243  -3.675 -20.253  1.00 38.09           N  
ANISOU 4079  ND1 HIS B 265     4452   5696   4323   -116   -149   -445       N  
ATOM   4080  CD2 HIS B 265      26.778  -4.946 -19.249  1.00 37.01           C  
ANISOU 4080  CD2 HIS B 265     4314   5550   4198    -84   -159   -401       C  
ATOM   4081  CE1 HIS B 265      27.815  -4.555 -21.142  1.00 39.17           C  
ANISOU 4081  CE1 HIS B 265     4604   5777   4502    -71   -154   -420       C  
ATOM   4082  NE2 HIS B 265      26.923  -5.336 -20.560  1.00 36.15           N  
ANISOU 4082  NE2 HIS B 265     4221   5386   4127    -51   -160   -393       N  
ATOM   4083  N   GLY B 266      30.517  -3.011 -15.204  1.00 39.55           N  
ANISOU 4083  N   GLY B 266     4494   6230   4305   -252   -167   -433       N  
ATOM   4084  CA  GLY B 266      30.750  -2.500 -13.866  1.00 42.83           C  
ANISOU 4084  CA  GLY B 266     4881   6727   4664   -301   -165   -448       C  
ATOM   4085  C   GLY B 266      29.742  -2.960 -12.831  1.00 41.17           C  
ANISOU 4085  C   GLY B 266     4667   6532   4443   -299   -168   -431       C  
ATOM   4086  O   GLY B 266      29.460  -2.220 -11.886  1.00 44.34           O  
ANISOU 4086  O   GLY B 266     5065   6973   4808   -344   -158   -464       O  
ATOM   4087  N   GLY B 267      29.188  -4.164 -12.990  1.00 39.08           N  
ANISOU 4087  N   GLY B 267     4403   6236   4209   -249   -181   -381       N  
ATOM   4088  CA  GLY B 267      28.329  -4.772 -11.987  1.00 37.00           C  
ANISOU 4088  CA  GLY B 267     4131   5993   3934   -244   -187   -354       C  
ATOM   4089  C   GLY B 267      26.940  -4.187 -11.846  1.00 36.76           C  
ANISOU 4089  C   GLY B 267     4139   5910   3918   -256   -170   -393       C  
ATOM   4090  O   GLY B 267      26.291  -4.427 -10.823  1.00 37.42           O  
ANISOU 4090  O   GLY B 267     4213   6025   3981   -267   -171   -382       O  
ATOM   4091  N   ILE B 268      26.461  -3.434 -12.844  1.00 35.65           N  
ANISOU 4091  N   ILE B 268     4042   5691   3813   -255   -153   -435       N  
ATOM   4092  CA  ILE B 268      25.183  -2.725 -12.724  1.00 37.84           C  
ANISOU 4092  CA  ILE B 268     4355   5918   4103   -270   -135   -476       C  
ATOM   4093  C   ILE B 268      24.051  -3.692 -12.408  1.00 35.45           C  
ANISOU 4093  C   ILE B 268     4058   5591   3821   -237   -142   -441       C  
ATOM   4094  O   ILE B 268      23.208  -3.433 -11.540  1.00 33.91           O  
ANISOU 4094  O   ILE B 268     3866   5409   3609   -258   -134   -456       O  
ATOM   4095  CB  ILE B 268      24.885  -1.928 -14.008  1.00 40.18           C  
ANISOU 4095  CB  ILE B 268     4695   6130   4442   -264   -119   -516       C  
ATOM   4096  CG1 ILE B 268      25.572  -0.562 -13.964  1.00 38.15           C  
ANISOU 4096  CG1 ILE B 268     4440   5895   4159   -315   -102   -570       C  
ATOM   4097  CG2 ILE B 268      23.367  -1.793 -14.243  1.00 39.85           C  
ANISOU 4097  CG2 ILE B 268     4691   6014   4435   -249   -107   -531       C  
ATOM   4098  CD1 ILE B 268      25.687   0.079 -15.318  1.00 40.78           C  
ANISOU 4098  CD1 ILE B 268     4807   6158   4530   -306    -91   -597       C  
ATOM   4099  N   PHE B 269      24.007  -4.819 -13.105  1.00 35.23           N  
ANISOU 4099  N   PHE B 269     4031   5526   3829   -187   -156   -394       N  
ATOM   4100  CA  PHE B 269      22.860  -5.697 -12.933  1.00 36.09           C  
ANISOU 4100  CA  PHE B 269     4151   5600   3962   -156   -161   -364       C  
ATOM   4101  C   PHE B 269      23.002  -6.600 -11.717  1.00 37.53           C  
ANISOU 4101  C   PHE B 269     4293   5855   4111   -155   -176   -316       C  
ATOM   4102  O   PHE B 269      21.981  -7.027 -11.157  1.00 32.34           O  
ANISOU 4102  O   PHE B 269     3641   5189   3457   -148   -176   -302       O  
ATOM   4103  CB  PHE B 269      22.630  -6.484 -14.224  1.00 31.40           C  
ANISOU 4103  CB  PHE B 269     3578   4930   3422   -105   -166   -339       C  
ATOM   4104  CG  PHE B 269      22.310  -5.597 -15.383  1.00 33.56           C  
ANISOU 4104  CG  PHE B 269     3891   5132   3728   -106   -151   -385       C  
ATOM   4105  CD1 PHE B 269      21.069  -5.000 -15.478  1.00 35.08           C  
ANISOU 4105  CD1 PHE B 269     4118   5274   3938   -113   -136   -417       C  
ATOM   4106  CD2 PHE B 269      23.263  -5.315 -16.347  1.00 34.13           C  
ANISOU 4106  CD2 PHE B 269     3966   5192   3811   -102   -151   -394       C  
ATOM   4107  CE1 PHE B 269      20.763  -4.155 -16.535  1.00 36.99           C  
ANISOU 4107  CE1 PHE B 269     4395   5451   4209   -114   -122   -456       C  
ATOM   4108  CE2 PHE B 269      22.968  -4.475 -17.399  1.00 36.08           C  
ANISOU 4108  CE2 PHE B 269     4248   5375   4085   -105   -138   -433       C  
ATOM   4109  CZ  PHE B 269      21.715  -3.892 -17.492  1.00 35.41           C  
ANISOU 4109  CZ  PHE B 269     4197   5239   4019   -110   -123   -463       C  
ATOM   4110  N   GLY B 270      24.229  -6.857 -11.256  1.00 32.25           N  
ANISOU 4110  N   GLY B 270     3584   5260   3408   -164   -189   -290       N  
ATOM   4111  CA  GLY B 270      24.384  -7.436  -9.930  1.00 32.72           C  
ANISOU 4111  CA  GLY B 270     3604   5403   3426   -176   -201   -252       C  
ATOM   4112  C   GLY B 270      23.836  -6.523  -8.850  1.00 35.68           C  
ANISOU 4112  C   GLY B 270     3979   5820   3759   -227   -188   -294       C  
ATOM   4113  O   GLY B 270      23.097  -6.957  -7.958  1.00 35.57           O  
ANISOU 4113  O   GLY B 270     3956   5828   3730   -229   -191   -274       O  
ATOM   4114  N   ARG B 271      24.170  -5.232  -8.930  1.00 33.92           N  
ANISOU 4114  N   ARG B 271     3767   5605   3518   -269   -172   -354       N  
ATOM   4115  CA  ARG B 271      23.677  -4.282  -7.941  1.00 34.56           C  
ANISOU 4115  CA  ARG B 271     3849   5723   3560   -320   -156   -400       C  
ATOM   4116  C   ARG B 271      22.156  -4.134  -8.022  1.00 34.04           C  
ANISOU 4116  C   ARG B 271     3821   5588   3525   -311   -142   -422       C  
ATOM   4117  O   ARG B 271      21.472  -4.093  -6.992  1.00 29.94           O  
ANISOU 4117  O   ARG B 271     3293   5102   2979   -332   -137   -427       O  
ATOM   4118  CB  ARG B 271      24.365  -2.929  -8.125  1.00 36.59           C  
ANISOU 4118  CB  ARG B 271     4113   5993   3797   -366   -139   -462       C  
ATOM   4119  CG  ARG B 271      25.822  -2.877  -7.633  1.00 40.24           C  
ANISOU 4119  CG  ARG B 271     4529   6549   4210   -393   -150   -450       C  
ATOM   4120  CD  ARG B 271      26.273  -1.432  -7.395  1.00 36.22           C  
ANISOU 4120  CD  ARG B 271     4025   6068   3669   -453   -130   -518       C  
ATOM   4121  NE  ARG B 271      26.498  -0.727  -8.652  1.00 41.71           N  
ANISOU 4121  NE  ARG B 271     4754   6692   4403   -447   -117   -553       N  
ATOM   4122  CZ  ARG B 271      27.459  -1.018  -9.521  1.00 43.85           C  
ANISOU 4122  CZ  ARG B 271     5018   6955   4689   -425   -128   -532       C  
ATOM   4123  NH1 ARG B 271      28.344  -1.974  -9.280  1.00 45.80           N  
ANISOU 4123  NH1 ARG B 271     5224   7262   4917   -406   -152   -477       N  
ATOM   4124  NH2 ARG B 271      27.527  -0.342 -10.669  1.00 40.91           N  
ANISOU 4124  NH2 ARG B 271     4679   6513   4352   -420   -116   -565       N  
ATOM   4125  N   LEU B 272      21.607  -4.036  -9.236  1.00 31.56           N  
ANISOU 4125  N   LEU B 272     3547   5180   3265   -280   -135   -435       N  
ATOM   4126  CA  LEU B 272      20.154  -3.930  -9.371  1.00 32.25           C  
ANISOU 4126  CA  LEU B 272     3669   5202   3384   -268   -122   -452       C  
ATOM   4127  C   LEU B 272      19.462  -5.144  -8.758  1.00 31.83           C  
ANISOU 4127  C   LEU B 272     3602   5162   3332   -242   -136   -400       C  
ATOM   4128  O   LEU B 272      18.516  -5.007  -7.972  1.00 32.22           O  
ANISOU 4128  O   LEU B 272     3654   5220   3368   -257   -128   -412       O  
ATOM   4129  CB  LEU B 272      19.769  -3.774 -10.845  1.00 29.78           C  
ANISOU 4129  CB  LEU B 272     3396   4791   3128   -235   -116   -465       C  
ATOM   4130  CG  LEU B 272      18.267  -3.829 -11.171  1.00 32.51           C  
ANISOU 4130  CG  LEU B 272     3776   5064   3513   -214   -106   -474       C  
ATOM   4131  CD1 LEU B 272      17.527  -2.697 -10.483  1.00 30.22           C  
ANISOU 4131  CD1 LEU B 272     3499   4778   3205   -254    -83   -529       C  
ATOM   4132  CD2 LEU B 272      18.027  -3.789 -12.680  1.00 29.99           C  
ANISOU 4132  CD2 LEU B 272     3491   4656   3247   -180   -103   -480       C  
ATOM   4133  N   HIS B 273      19.937  -6.345  -9.095  1.00 30.04           N  
ANISOU 4133  N   HIS B 273     3357   4935   3120   -202   -157   -341       N  
ATOM   4134  CA  HIS B 273      19.360  -7.561  -8.530  1.00 33.09           C  
ANISOU 4134  CA  HIS B 273     3729   5333   3510   -175   -170   -286       C  
ATOM   4135  C   HIS B 273      19.369  -7.519  -7.008  1.00 34.51           C  
ANISOU 4135  C   HIS B 273     3876   5603   3633   -212   -173   -279       C  
ATOM   4136  O   HIS B 273      18.359  -7.818  -6.363  1.00 34.04           O  
ANISOU 4136  O   HIS B 273     3820   5544   3571   -213   -171   -270       O  
ATOM   4137  CB  HIS B 273      20.123  -8.788  -9.030  1.00 31.61           C  
ANISOU 4137  CB  HIS B 273     3523   5144   3344   -132   -190   -224       C  
ATOM   4138  CG  HIS B 273      19.616 -10.079  -8.466  1.00 34.82           C  
ANISOU 4138  CG  HIS B 273     3914   5561   3756   -104   -204   -164       C  
ATOM   4139  ND1 HIS B 273      18.539 -10.752  -9.003  1.00 33.87           N  
ANISOU 4139  ND1 HIS B 273     3820   5367   3681    -69   -202   -149       N  
ATOM   4140  CD2 HIS B 273      20.024 -10.815  -7.402  1.00 37.23           C  
ANISOU 4140  CD2 HIS B 273     4178   5942   4027   -107   -218   -114       C  
ATOM   4141  CE1 HIS B 273      18.315 -11.852  -8.306  1.00 33.38           C  
ANISOU 4141  CE1 HIS B 273     3737   5333   3615    -52   -214    -93       C  
ATOM   4142  NE2 HIS B 273      19.197 -11.911  -7.325  1.00 35.43           N  
ANISOU 4142  NE2 HIS B 273     3955   5682   3826    -74   -224    -70       N  
ATOM   4143  N   ASP B 274      20.511  -7.137  -6.421  1.00 33.36           N  
ANISOU 4143  N   ASP B 274     3697   5538   3441   -245   -177   -282       N  
ATOM   4144  CA  ASP B 274      20.667  -7.127  -4.971  1.00 35.48           C  
ANISOU 4144  CA  ASP B 274     3929   5903   3650   -283   -181   -273       C  
ATOM   4145  C   ASP B 274      19.721  -6.131  -4.315  1.00 29.88           C  
ANISOU 4145  C   ASP B 274     3237   5196   2921   -325   -160   -331       C  
ATOM   4146  O   ASP B 274      19.128  -6.422  -3.277  1.00 30.45           O  
ANISOU 4146  O   ASP B 274     3293   5311   2964   -339   -161   -317       O  
ATOM   4147  CB  ASP B 274      22.122  -6.793  -4.609  1.00 35.70           C  
ANISOU 4147  CB  ASP B 274     3918   6014   3631   -312   -189   -272       C  
ATOM   4148  CG  ASP B 274      23.094  -7.917  -4.971  1.00 39.67           C  
ANISOU 4148  CG  ASP B 274     4393   6534   4146   -272   -212   -204       C  
ATOM   4149  OD1 ASP B 274      22.619  -9.036  -5.262  1.00 37.56           O  
ANISOU 4149  OD1 ASP B 274     4130   6225   3915   -225   -223   -154       O  
ATOM   4150  OD2 ASP B 274      24.336  -7.684  -4.940  1.00 40.30           O  
ANISOU 4150  OD2 ASP B 274     4444   6669   4198   -287   -219   -202       O  
ATOM   4151  N   ALA B 275      19.573  -4.951  -4.909  1.00 28.74           N  
ANISOU 4151  N   ALA B 275     3124   5005   2790   -345   -139   -395       N  
ATOM   4152  CA  ALA B 275      18.695  -3.931  -4.372  1.00 31.70           C  
ANISOU 4152  CA  ALA B 275     3517   5374   3152   -383   -114   -455       C  
ATOM   4153  C   ALA B 275      17.212  -4.289  -4.522  1.00 31.15           C  
ANISOU 4153  C   ALA B 275     3476   5238   3119   -356   -108   -451       C  
ATOM   4154  O   ALA B 275      16.368  -3.663  -3.870  1.00 32.33           O  
ANISOU 4154  O   ALA B 275     3636   5393   3255   -384    -90   -490       O  
ATOM   4155  CB  ALA B 275      18.992  -2.602  -5.056  1.00 33.79           C  
ANISOU 4155  CB  ALA B 275     3808   5601   3428   -407    -93   -521       C  
ATOM   4156  N   LEU B 276      16.876  -5.257  -5.372  1.00 32.07           N  
ANISOU 4156  N   LEU B 276     3607   5293   3283   -303   -121   -407       N  
ATOM   4157  CA  LEU B 276      15.500  -5.738  -5.467  1.00 31.90           C  
ANISOU 4157  CA  LEU B 276     3610   5217   3295   -277   -118   -397       C  
ATOM   4158  C   LEU B 276      15.200  -6.868  -4.491  1.00 33.54           C  
ANISOU 4158  C   LEU B 276     3788   5475   3480   -268   -134   -340       C  
ATOM   4159  O   LEU B 276      14.025  -7.233  -4.348  1.00 30.90           O  
ANISOU 4159  O   LEU B 276     3469   5108   3164   -254   -130   -333       O  
ATOM   4160  CB  LEU B 276      15.184  -6.201  -6.898  1.00 28.00           C  
ANISOU 4160  CB  LEU B 276     3147   4629   2864   -226   -122   -381       C  
ATOM   4161  CG  LEU B 276      14.962  -5.095  -7.943  1.00 30.76           C  
ANISOU 4161  CG  LEU B 276     3534   4906   3246   -229   -103   -437       C  
ATOM   4162  CD1 LEU B 276      14.942  -5.668  -9.363  1.00 23.86           C  
ANISOU 4162  CD1 LEU B 276     2684   3955   2427   -181   -111   -414       C  
ATOM   4163  CD2 LEU B 276      13.678  -4.289  -7.653  1.00 28.51           C  
ANISOU 4163  CD2 LEU B 276     3275   4590   2968   -247    -80   -484       C  
ATOM   4164  N   ASP B 277      16.228  -7.416  -3.811  1.00 31.04           N  
ANISOU 4164  N   ASP B 277     3429   5240   3124   -277   -151   -299       N  
ATOM   4165  CA  ASP B 277      16.009  -8.469  -2.817  1.00 30.55           C  
ANISOU 4165  CA  ASP B 277     3337   5233   3038   -271   -167   -242       C  
ATOM   4166  C   ASP B 277      14.980  -8.052  -1.780  1.00 29.34           C  
ANISOU 4166  C   ASP B 277     3185   5108   2856   -305   -153   -270       C  
ATOM   4167  O   ASP B 277      14.215  -8.887  -1.295  1.00 31.45           O  
ANISOU 4167  O   ASP B 277     3446   5378   3125   -290   -160   -231       O  
ATOM   4168  CB  ASP B 277      17.310  -8.819  -2.088  1.00 35.50           C  
ANISOU 4168  CB  ASP B 277     3915   5957   3616   -287   -184   -203       C  
ATOM   4169  CG  ASP B 277      18.252  -9.650  -2.925  1.00 38.86           C  
ANISOU 4169  CG  ASP B 277     4331   6363   4070   -244   -202   -154       C  
ATOM   4170  OD1 ASP B 277      17.788 -10.442  -3.772  1.00 38.26           O  
ANISOU 4170  OD1 ASP B 277     4276   6212   4047   -196   -207   -125       O  
ATOM   4171  OD2 ASP B 277      19.479  -9.505  -2.718  1.00 43.05           O  
ANISOU 4171  OD2 ASP B 277     4831   6956   4569   -260   -211   -145       O  
ATOM   4172  N   LYS B 278      14.955  -6.765  -1.411  1.00 26.60           N  
ANISOU 4172  N   LYS B 278     2844   4782   2481   -352   -132   -337       N  
ATOM   4173  CA  LYS B 278      13.964  -6.294  -0.440  1.00 31.00           C  
ANISOU 4173  CA  LYS B 278     3403   5365   3012   -385   -116   -370       C  
ATOM   4174  C   LYS B 278      12.531  -6.336  -0.961  1.00 32.54           C  
ANISOU 4174  C   LYS B 278     3636   5472   3255   -359   -103   -384       C  
ATOM   4175  O   LYS B 278      11.598  -6.158  -0.173  1.00 30.94           O  
ANISOU 4175  O   LYS B 278     3434   5287   3035   -380    -91   -402       O  
ATOM   4176  CB  LYS B 278      14.282  -4.871   0.026  1.00 32.71           C  
ANISOU 4176  CB  LYS B 278     3618   5619   3191   -442    -93   -443       C  
ATOM   4177  CG  LYS B 278      14.077  -3.772  -0.997  1.00 33.67           C  
ANISOU 4177  CG  LYS B 278     3782   5660   3353   -442    -70   -505       C  
ATOM   4178  CD  LYS B 278      14.472  -2.398  -0.429  1.00 39.12           C  
ANISOU 4178  CD  LYS B 278     4468   6393   4004   -502    -46   -576       C  
ATOM   4179  CE  LYS B 278      15.290  -1.540  -1.426  1.00 40.97           C  
ANISOU 4179  CE  LYS B 278     4720   6586   4259   -505    -38   -613       C  
ATOM   4180  NZ  LYS B 278      16.734  -1.963  -1.593  1.00 39.74           N  
ANISOU 4180  NZ  LYS B 278     4536   6482   4083   -503    -60   -577       N  
ATOM   4181  N   TYR B 279      12.314  -6.561  -2.251  1.00 29.89           N  
ANISOU 4181  N   TYR B 279     3332   5048   2978   -316   -105   -378       N  
ATOM   4182  CA  TYR B 279      10.957  -6.751  -2.746  1.00 31.08           C  
ANISOU 4182  CA  TYR B 279     3515   5121   3174   -289    -97   -383       C  
ATOM   4183  C   TYR B 279      10.713  -8.179  -3.219  1.00 32.79           C  
ANISOU 4183  C   TYR B 279     3732   5303   3425   -239   -118   -315       C  
ATOM   4184  O   TYR B 279       9.693  -8.450  -3.867  1.00 28.95           O  
ANISOU 4184  O   TYR B 279     3274   4745   2982   -210   -113   -314       O  
ATOM   4185  CB  TYR B 279      10.658  -5.739  -3.858  1.00 28.95           C  
ANISOU 4185  CB  TYR B 279     3284   4769   2945   -283    -78   -438       C  
ATOM   4186  CG  TYR B 279      10.872  -4.307  -3.419  1.00 32.01           C  
ANISOU 4186  CG  TYR B 279     3675   5184   3304   -332    -54   -507       C  
ATOM   4187  CD1 TYR B 279      10.205  -3.793  -2.307  1.00 32.61           C  
ANISOU 4187  CD1 TYR B 279     3743   5301   3346   -370    -37   -539       C  
ATOM   4188  CD2 TYR B 279      11.758  -3.475  -4.093  1.00 32.82           C  
ANISOU 4188  CD2 TYR B 279     3787   5271   3413   -343    -47   -540       C  
ATOM   4189  CE1 TYR B 279      10.408  -2.479  -1.890  1.00 33.97           C  
ANISOU 4189  CE1 TYR B 279     3917   5496   3493   -417    -12   -605       C  
ATOM   4190  CE2 TYR B 279      11.964  -2.164  -3.687  1.00 34.14           C  
ANISOU 4190  CE2 TYR B 279     3957   5461   3556   -389    -23   -604       C  
ATOM   4191  CZ  TYR B 279      11.287  -1.673  -2.586  1.00 33.14           C  
ANISOU 4191  CZ  TYR B 279     3822   5372   3397   -426     -5   -637       C  
ATOM   4192  OH  TYR B 279      11.483  -0.377  -2.174  1.00 36.21           O  
ANISOU 4192  OH  TYR B 279     4214   5780   3762   -474     21   -703       O  
ATOM   4193  N   ALA B 280      11.605  -9.112  -2.886  1.00 30.30           N  
ANISOU 4193  N   ALA B 280     3383   5038   3089   -228   -139   -258       N  
ATOM   4194  CA  ALA B 280      11.587 -10.437  -3.494  1.00 30.01           C  
ANISOU 4194  CA  ALA B 280     3349   4963   3092   -179   -157   -195       C  
ATOM   4195  C   ALA B 280      11.088 -11.525  -2.547  1.00 30.92           C  
ANISOU 4195  C   ALA B 280     3440   5117   3190   -172   -169   -139       C  
ATOM   4196  O   ALA B 280      11.271 -12.711  -2.831  1.00 33.67           O  
ANISOU 4196  O   ALA B 280     3780   5449   3562   -136   -185    -79       O  
ATOM   4197  CB  ALA B 280      12.978 -10.793  -4.026  1.00 30.43           C  
ANISOU 4197  CB  ALA B 280     3384   5029   3147   -162   -173   -165       C  
ATOM   4198  N   GLU B 281      10.447 -11.158  -1.442  1.00 30.94           N  
ANISOU 4198  N   GLU B 281     3433   5169   3155   -208   -160   -157       N  
ATOM   4199  CA  GLU B 281       9.880 -12.161  -0.553  1.00 34.40           C  
ANISOU 4199  CA  GLU B 281     3851   5642   3578   -203   -170   -105       C  
ATOM   4200  C   GLU B 281       8.843 -13.017  -1.275  1.00 36.22           C  
ANISOU 4200  C   GLU B 281     4109   5790   3864   -160   -171    -80       C  
ATOM   4201  O   GLU B 281       7.959 -12.501  -1.974  1.00 32.86           O  
ANISOU 4201  O   GLU B 281     3719   5295   3473   -153   -157   -122       O  
ATOM   4202  CB  GLU B 281       9.245 -11.488   0.658  1.00 37.35           C  
ANISOU 4202  CB  GLU B 281     4214   6075   3903   -250   -156   -140       C  
ATOM   4203  CG  GLU B 281       8.548 -12.467   1.572  1.00 39.69           C  
ANISOU 4203  CG  GLU B 281     4491   6406   4184   -247   -165    -89       C  
ATOM   4204  CD  GLU B 281       8.203 -11.871   2.929  1.00 48.10           C  
ANISOU 4204  CD  GLU B 281     5535   7552   5189   -299   -155   -116       C  
ATOM   4205  OE1 GLU B 281       7.578 -10.789   2.976  1.00 51.03           O  
ANISOU 4205  OE1 GLU B 281     5925   7907   5556   -325   -132   -184       O  
ATOM   4206  OE2 GLU B 281       8.576 -12.484   3.953  1.00 53.95           O  
ANISOU 4206  OE2 GLU B 281     6237   8374   5886   -314   -168    -69       O  
ATOM   4207  N   VAL B 282       8.954 -14.333  -1.100  1.00 31.38           N  
ANISOU 4207  N   VAL B 282     3478   5185   3260   -133   -189     -9       N  
ATOM   4208  CA  VAL B 282       8.022 -15.273  -1.703  1.00 36.08           C  
ANISOU 4208  CA  VAL B 282     4096   5708   3906    -94   -190     21       C  
ATOM   4209  C   VAL B 282       6.943 -15.616  -0.682  1.00 36.28           C  
ANISOU 4209  C   VAL B 282     4113   5762   3910   -110   -187     35       C  
ATOM   4210  O   VAL B 282       6.970 -16.685  -0.071  1.00 36.64           O  
ANISOU 4210  O   VAL B 282     4136   5839   3948   -100   -200     98       O  
ATOM   4211  CB  VAL B 282       8.741 -16.538  -2.212  1.00 37.56           C  
ANISOU 4211  CB  VAL B 282     4271   5875   4123    -52   -208     88       C  
ATOM   4212  CG1 VAL B 282       7.791 -17.387  -3.046  1.00 32.99           C  
ANISOU 4212  CG1 VAL B 282     3722   5211   3603    -14   -206    107       C  
ATOM   4213  CG2 VAL B 282       9.974 -16.159  -3.039  1.00 36.98           C  
ANISOU 4213  CG2 VAL B 282     4199   5793   4061    -42   -212     75       C  
ATOM   4214  N   LYS B 283       6.002 -14.700  -0.474  1.00 36.94           N  
ANISOU 4214  N   LYS B 283     4215   5836   3985   -135   -169    -22       N  
ATOM   4215  CA  LYS B 283       4.820 -14.983   0.343  1.00 40.70           C  
ANISOU 4215  CA  LYS B 283     4688   6327   4448   -148   -163    -15       C  
ATOM   4216  C   LYS B 283       3.761 -15.764  -0.421  1.00 40.50           C  
ANISOU 4216  C   LYS B 283     4691   6220   4477   -111   -163      4       C  
ATOM   4217  O   LYS B 283       3.729 -15.797  -1.656  1.00 36.95           O  
ANISOU 4217  O   LYS B 283     4269   5694   4076    -81   -161     -7       O  
ATOM   4218  CB  LYS B 283       4.190 -13.694   0.872  1.00 41.03           C  
ANISOU 4218  CB  LYS B 283     4738   6391   4462   -189   -142    -85       C  
ATOM   4219  CG  LYS B 283       5.163 -12.557   1.121  1.00 42.96           C  
ANISOU 4219  CG  LYS B 283     4971   6683   4669   -223   -135   -131       C  
ATOM   4220  CD  LYS B 283       4.417 -11.299   1.554  1.00 42.95           C  
ANISOU 4220  CD  LYS B 283     4982   6690   4649   -261   -110   -203       C  
ATOM   4221  CE  LYS B 283       5.192 -10.052   1.126  1.00 44.96           C  
ANISOU 4221  CE  LYS B 283     5245   6940   4897   -281    -98   -262       C  
ATOM   4222  NZ  LYS B 283       4.559  -8.748   1.500  1.00 44.35           N  
ANISOU 4222  NZ  LYS B 283     5181   6866   4805   -317    -70   -337       N  
ATOM   4223  OXT LYS B 283       2.877 -16.358   0.204  1.00 46.32           O  
ANISOU 4223  OXT LYS B 283     5422   6967   5209   -114   -163     29       O  
TER    4224      LYS B 283                                                      
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.