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***  FLAVOPROTEIN 12-JUN-97 1AL7  ***

elNémo ID: 210428060209108430

Job options:

ID        	=	 210428060209108430
JOBID     	=	 FLAVOPROTEIN 12-JUN-97 1AL7
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    FLAVOPROTEIN                            12-JUN-97   1AL7              
TITLE     THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-  
TITLE    2 SITE INHIBITORS                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOLATE OXIDASE;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.1.3.15;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: GLYCOLATE OXIDASE COMPLEXED WITH FMN AND AN INHIBITOR 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE   3 ORGANISM_COMMON: SPINACH;                                            
SOURCE   4 ORGANISM_TAXID: 3562;                                                
SOURCE   5 CELL_LINE: BL21;                                                     
SOURCE   6 CELLULAR_LOCATION: PEROXISOME;                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;                          
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PKS20+                                    
KEYWDS    FLAVOPROTEIN, DRUG DESIGN, INHIBITOR BINDING                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.STENBERG,Y.LINDQVIST                                                
REVDAT   3   13-JUL-11 1AL7    1       VERSN                                    
REVDAT   2   24-FEB-09 1AL7    1       VERSN                                    
REVDAT   1   12-NOV-97 1AL7    0                                                
JRNL        AUTH   K.STENBERG,Y.LINDQVIST                                       
JRNL        TITL   THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND 
JRNL        TITL 2 ACTIVE-SITE INHIBITORS.                                      
JRNL        REF    PROTEIN SCI.                  V.   6  1009 1997              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9144771                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.STENBERG,Y.LINDQVIST                                       
REMARK   1  TITL   HIGH-LEVEL EXPRESSION, PURIFICATION, AND CRYSTALLIZATION OF  
REMARK   1  TITL 2 RECOMBINANT SPINACH GLYCOLATE OXIDASE IN ESCHERICHIA COLI    
REMARK   1  REF    PROTEIN EXPR.PURIF.           V.   8   295 1996              
REMARK   1  REFN                   ISSN 1046-5928                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.LINDQVIST                                                  
REMARK   1  TITL   REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 2 A        
REMARK   1  TITL 2 RESOLUTION                                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 209   151 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20005                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1579                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 12                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.76                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2697                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 292                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.20                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.37                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.95                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.28                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM11.DNA                                    
REMARK   3  PARAMETER FILE  3  : PARAM.FMN                                      
REMARK   3  PARAMETER FILE  4  : TACA.TOP                                       
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH11.DNA                                     
REMARK   3  TOPOLOGY FILE  3   : TOPOLOGY.FMN                                   
REMARK   3  TOPOLOGY FILE  4   : TACA.PAR                                       
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: TOPOLOGY AND PARAMETER FILES FOR THE      
REMARK   3  TKCA-INHIBITOR WERE CREATED USING THE PROGRAMME XPLO2D (REF: [O/X   
REMARK   3  -PLOR DICTIONARIES] G.J. KLEYWEGT, DICTIONARIES FOR HETEROS, ESF/   
REMARK   3  CCP4 NEWSLETTER 31,JUNE 1995, PP. 45-50). BOND LENGTHS AND ANGLES   
REMARK   3  ARE FROM IDEALIZED STRUCTURES.                                      
REMARK   4                                                                      
REMARK   4 1AL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20291                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200   FOR THE DATA SET  : 6.9900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.20600                            
REMARK 200   FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLISED FROM 50MM       
REMARK 280  TRIS-BUFFER PH 8.3, 0.25 MG/ML FMN, 4% TERTIARY BUTANOL,            
REMARK 280  SATURATED WITH THE INHIBITOR.                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       74.05000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       68.25000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       74.05000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       68.25000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       74.05000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       68.25000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       74.05000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       68.25000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.05000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       68.25000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.05000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       68.25000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       74.05000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       68.25000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       74.05000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       74.05000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       68.25000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 18100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      148.10000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      148.10000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      148.10000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      148.10000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 39360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 88780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      148.10000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      148.10000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      148.10000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      148.10000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000      148.10000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000      148.10000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000      148.10000            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000      148.10000            
REMARK 350   BIOMT3   8  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   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     MET A   191                                                      
REMARK 465     ASP A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     ASP A   196                                                      
REMARK 465     SER A   197                                                      
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    ASP A   187     O    HOH A   447              1.60            
REMARK 500   O    GLY A   185     N    ILE A   186              1.69            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY A 185   C     ILE A 186   N      -0.302                       
REMARK 500    ASP A 187   C     ASP A 187   O       0.166                       
REMARK 500    LEU A 188   CA    LEU A 188   C       0.198                       
REMARK 500    LEU A 188   C     LEU A 188   O      -0.163                       
REMARK 500    GLY A 198   C     GLY A 198   O      -0.154                       
REMARK 500    GLY A 198   C     LEU A 199   N       0.199                       
REMARK 500    SER A 200   CB    SER A 200   OG     -0.118                       
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 128   CA  -  CB  -  CG  ANGL. DEV. =  17.6 DEGREES          
REMARK 500    GLY A 185   CA  -  C   -  N   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    GLY A 185   O   -  C   -  N   ANGL. DEV. = -27.0 DEGREES          
REMARK 500    ASP A 187   CB  -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    LEU A 199   CA  -  CB  -  CG  ANGL. DEV. =  27.2 DEGREES          
REMARK 500    LEU A 199   CB  -  CG  -  CD1 ANGL. DEV. =  23.3 DEGREES          
REMARK 500    SER A 200   CA  -  CB  -  OG  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    SER A 201   C   -  N   -  CA  ANGL. DEV. = -15.2 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    GLU A   2      150.60    177.95                                   
REMARK 500    GLU A  30     -110.23     45.85                                   
REMARK 500    PRO A  72       40.00    -89.10                                   
REMARK 500    THR A  78     -132.37    -94.86                                   
REMARK 500    ALA A  79      138.95   -174.41                                   
REMARK 500    ARG A 171       61.20     63.37                                   
REMARK 500    HIS A 244       34.86    -91.57                                   
REMARK 500    GLN A 258      -92.70   -103.50                                   
REMARK 500    TYR A 261       18.21     81.58                                   
REMARK 500    ARG A 289      -10.57   -143.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 185         29.17                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 493        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 519        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 530        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH A 555        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A 566        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A 568        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A 612        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A 616        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A 626        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A 631        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A 633        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH A 645        DISTANCE =  5.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HST A 361                 
DBREF  1AL7 A    1   359  UNP    P05414   GOX_SPIOL        1    359             
SEQRES   1 A  359  MET GLU ILE THR ASN VAL ASN GLU TYR GLU ALA ILE ALA          
SEQRES   2 A  359  LYS GLN LYS LEU PRO LYS MET VAL TYR ASP TYR TYR ALA          
SEQRES   3 A  359  SER GLY ALA GLU ASP GLN TRP THR LEU ALA GLU ASN ARG          
SEQRES   4 A  359  ASN ALA PHE SER ARG ILE LEU PHE ARG PRO ARG ILE LEU          
SEQRES   5 A  359  ILE ASP VAL THR ASN ILE ASP MET THR THR THR ILE LEU          
SEQRES   6 A  359  GLY PHE LYS ILE SER MET PRO ILE MET ILE ALA PRO THR          
SEQRES   7 A  359  ALA MET GLN LYS MET ALA HIS PRO GLU GLY GLU TYR ALA          
SEQRES   8 A  359  THR ALA ARG ALA ALA SER ALA ALA GLY THR ILE MET THR          
SEQRES   9 A  359  LEU SER SER TRP ALA THR SER SER VAL GLU GLU VAL ALA          
SEQRES  10 A  359  SER THR GLY PRO GLY ILE ARG PHE PHE GLN LEU TYR VAL          
SEQRES  11 A  359  TYR LYS ASP ARG ASN VAL VAL ALA GLN LEU VAL ARG ARG          
SEQRES  12 A  359  ALA GLU ARG ALA GLY PHE LYS ALA ILE ALA LEU THR VAL          
SEQRES  13 A  359  ASP THR PRO ARG LEU GLY ARG ARG GLU ALA ASP ILE LYS          
SEQRES  14 A  359  ASN ARG PHE VAL LEU PRO PRO PHE LEU THR LEU LYS ASN          
SEQRES  15 A  359  PHE GLU GLY ILE ASP LEU GLY LYS MET ASP LYS ALA ASN          
SEQRES  16 A  359  ASP SER GLY LEU SER SER TYR VAL ALA GLY GLN ILE ASP          
SEQRES  17 A  359  ARG SER LEU SER TRP LYS ASP VAL ALA TRP LEU GLN THR          
SEQRES  18 A  359  ILE THR SER LEU PRO ILE LEU VAL LYS GLY VAL ILE THR          
SEQRES  19 A  359  ALA GLU ASP ALA ARG LEU ALA VAL GLN HIS GLY ALA ALA          
SEQRES  20 A  359  GLY ILE ILE VAL SER ASN HIS GLY ALA ARG GLN LEU ASP          
SEQRES  21 A  359  TYR VAL PRO ALA THR ILE MET ALA LEU GLU GLU VAL VAL          
SEQRES  22 A  359  LYS ALA ALA GLN GLY ARG ILE PRO VAL PHE LEU ASP GLY          
SEQRES  23 A  359  GLY VAL ARG ARG GLY THR ASP VAL PHE LYS ALA LEU ALA          
SEQRES  24 A  359  LEU GLY ALA ALA GLY VAL PHE ILE GLY ARG PRO VAL VAL          
SEQRES  25 A  359  PHE SER LEU ALA ALA GLU GLY GLU ALA GLY VAL LYS LYS          
SEQRES  26 A  359  VAL LEU GLN MET MET ARG ASP GLU PHE GLU LEU THR MET          
SEQRES  27 A  359  ALA LEU SER GLY CYS ARG SER LEU LYS GLU ILE SER ARG          
SEQRES  28 A  359  SER HIS ILE ALA ALA ASP TRP ASP                              
HET    FMN  A 360      31                                                       
HET    HST  A 361      20                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     HST 4-CARBOXY-5-(1-PENTYL)HEXYLSULFANYL-1,2,3-TRIAZOLE               
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   2  FMN    C17 H21 N4 O9 P                                              
FORMUL   3  HST    C14 H25 N3 O2 S                                              
FORMUL   4  HOH   *292(H2 O)                                                    
HELIX    1   1 VAL A    6  LYS A   16  5                                  11    
HELIX    2   2 LYS A   19  ALA A   26  1                                   8    
HELIX    3   3 TRP A   33  ARG A   44  1                                  12    
HELIX    4   4 GLN A   81  MET A   83  5                                   3    
HELIX    5   5 GLU A   89  ALA A   99  1                                  11    
HELIX    6   6 VAL A  113  THR A  119  1                                   7    
HELIX    7   7 ARG A  134  ARG A  146  1                                  13    
HELIX    8   8 GLU A  165  ASN A  170  1                                   6    
HELIX    9   9 LEU A  199  GLY A  205  1                                   7    
HELIX   10  10 TRP A  213  THR A  221  1                                   9    
HELIX   11  11 ALA A  235  GLN A  243  1                                   9    
HELIX   12  12 HIS A  254  ALA A  256  5                                   3    
HELIX   13  13 THR A  265  ALA A  276  1                                  12    
HELIX   14  14 GLY A  291  ALA A  299  1                                   9    
HELIX   15  15 ARG A  309  SER A  341  1                                  33    
HELIX   16  16 LEU A  346  GLU A  348  5                                   3    
HELIX   17  17 ARG A  351  HIS A  353  5                                   3    
SHEET    1   A 2 ILE A  45  PHE A  47  0                                        
SHEET    2   A 2 ILE A 354  ALA A 356 -1  N  ALA A 355   O  LEU A  46           
SHEET    1   B 2 THR A  62  ILE A  64  0                                        
SHEET    2   B 2 PHE A  67  ILE A  69 -1  N  ILE A  69   O  THR A  62           
SHEET    1   C 2 ILE A  73  ILE A  75  0                                        
SHEET    2   C 2 VAL A 305  ILE A 307  1  N  VAL A 305   O  MET A  74           
SHEET    1   D 6 MET A 103  LEU A 105  0                                        
SHEET    2   D 6 ARG A 124  LEU A 128  1  N  PHE A 125   O  MET A 103           
SHEET    3   D 6 ALA A 151  THR A 155  1  N  ALA A 151   O  PHE A 126           
SHEET    4   D 6 PRO A 226  VAL A 232  1  N  PRO A 226   O  ILE A 152           
SHEET    5   D 6 GLY A 248  VAL A 251  1  N  GLY A 248   O  VAL A 229           
SHEET    6   D 6 PRO A 281  LEU A 284  1  N  PRO A 281   O  ILE A 249           
SITE     1 AC1 22 TYR A  24  TYR A  25  ALA A  76  PRO A  77                    
SITE     2 AC1 22 THR A  78  ALA A  79  SER A 106  GLN A 127                    
SITE     3 AC1 22 THR A 155  LYS A 230  SER A 252  HIS A 254                    
SITE     4 AC1 22 ARG A 257  ASP A 285  GLY A 286  GLY A 287                    
SITE     5 AC1 22 ARG A 289  GLY A 308  ARG A 309  HST A 361                    
SITE     6 AC1 22 HOH A 363  HOH A 398                                          
SITE     1 AC2 12 TYR A  24  TRP A 108  TYR A 129  TYR A 131                    
SITE     2 AC2 12 LEU A 161  ARG A 164  PHE A 172  ILE A 207                    
SITE     3 AC2 12 HIS A 254  ARG A 257  FMN A 360  HOH A 659                    
CRYST1  148.100  148.100  136.500  90.00  90.00  90.00 I 4 2 2      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      0.006752  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006752  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007326        0.00000                         
ATOM      1  N   MET A   1      79.171  47.773   3.446  1.00 85.56           N  
ATOM      2  CA  MET A   1      77.857  48.332   3.879  1.00 85.13           C  
ATOM      3  C   MET A   1      77.099  47.194   4.551  1.00 79.49           C  
ATOM      4  O   MET A   1      77.187  46.052   4.100  1.00 81.69           O  
ATOM      5  CB  MET A   1      77.058  48.846   2.675  1.00 91.61           C  
ATOM      6  CG  MET A   1      77.876  49.113   1.412  1.00 97.54           C  
ATOM      7  SD  MET A   1      79.348  50.133   1.667  1.00104.15           S  
ATOM      8  CE  MET A   1      80.583  49.210   0.718  1.00102.69           C  
ATOM      9  N   GLU A   2      76.359  47.513   5.611  1.00 70.24           N  
ATOM     10  CA  GLU A   2      75.597  46.531   6.378  1.00 57.52           C  
ATOM     11  C   GLU A   2      74.925  47.265   7.538  1.00 49.22           C  
ATOM     12  O   GLU A   2      75.449  48.271   8.025  1.00 48.59           O  
ATOM     13  CB  GLU A   2      76.546  45.468   6.946  1.00 61.51           C  
ATOM     14  CG  GLU A   2      75.880  44.418   7.821  1.00 66.27           C  
ATOM     15  CD  GLU A   2      76.872  43.674   8.701  1.00 68.19           C  
ATOM     16  OE1 GLU A   2      77.980  43.339   8.216  1.00 67.72           O  
ATOM     17  OE2 GLU A   2      76.537  43.425   9.881  1.00 67.95           O  
ATOM     18  N   ILE A   3      73.775  46.773   7.984  1.00 36.51           N  
ATOM     19  CA  ILE A   3      73.083  47.406   9.102  1.00 27.68           C  
ATOM     20  C   ILE A   3      73.809  47.049  10.393  1.00 20.73           C  
ATOM     21  O   ILE A   3      73.994  45.878  10.723  1.00 18.99           O  
ATOM     22  CB  ILE A   3      71.582  47.025   9.149  1.00 25.88           C  
ATOM     23  CG1 ILE A   3      70.873  47.648   7.940  1.00 25.68           C  
ATOM     24  CG2 ILE A   3      70.943  47.509  10.447  1.00 19.40           C  
ATOM     25  CD1 ILE A   3      69.406  47.375   7.861  1.00 31.12           C  
ATOM     26  N   THR A   4      74.260  48.077  11.095  1.00 11.49           N  
ATOM     27  CA  THR A   4      75.004  47.880  12.317  1.00  8.71           C  
ATOM     28  C   THR A   4      74.314  48.396  13.570  1.00 10.04           C  
ATOM     29  O   THR A   4      74.800  48.169  14.673  1.00  7.81           O  
ATOM     30  CB  THR A   4      76.401  48.508  12.186  1.00 13.86           C  
ATOM     31  OG1 THR A   4      76.277  49.911  11.913  1.00 12.25           O  
ATOM     32  CG2 THR A   4      77.165  47.848  11.028  1.00 10.84           C  
ATOM     33  N   ASN A   5      73.197  49.101  13.405  1.00  5.41           N  
ATOM     34  CA  ASN A   5      72.460  49.621  14.557  1.00  4.46           C  
ATOM     35  C   ASN A   5      70.971  49.797  14.266  1.00  7.37           C  
ATOM     36  O   ASN A   5      70.570  50.048  13.124  1.00  5.49           O  
ATOM     37  CB  ASN A   5      73.079  50.926  15.086  1.00  8.13           C  
ATOM     38  CG  ASN A   5      72.861  52.113  14.162  1.00  9.49           C  
ATOM     39  OD1 ASN A   5      71.728  52.519  13.902  1.00  8.07           O  
ATOM     40  ND2 ASN A   5      73.951  52.695  13.685  1.00 11.33           N  
ATOM     41  N   VAL A   6      70.158  49.642  15.305  1.00  8.05           N  
ATOM     42  CA  VAL A   6      68.703  49.761  15.201  1.00  9.78           C  
ATOM     43  C   VAL A   6      68.200  51.022  14.476  1.00  8.34           C  
ATOM     44  O   VAL A   6      67.352  50.928  13.584  1.00 12.61           O  
ATOM     45  CB  VAL A   6      68.065  49.676  16.604  1.00  9.01           C  
ATOM     46  CG1 VAL A   6      66.564  49.864  16.526  1.00 16.01           C  
ATOM     47  CG2 VAL A   6      68.388  48.340  17.228  1.00  4.18           C  
ATOM     48  N   ASN A   7      68.741  52.185  14.838  1.00  7.62           N  
ATOM     49  CA  ASN A   7      68.348  53.469  14.240  1.00  9.85           C  
ATOM     50  C   ASN A   7      68.409  53.535  12.719  1.00  9.22           C  
ATOM     51  O   ASN A   7      67.656  54.284  12.099  1.00 20.73           O  
ATOM     52  CB  ASN A   7      69.173  54.630  14.819  1.00  9.27           C  
ATOM     53  CG  ASN A   7      68.800  54.962  16.265  1.00 15.69           C  
ATOM     54  OD1 ASN A   7      69.671  55.187  17.105  1.00 18.84           O  
ATOM     55  ND2 ASN A   7      67.509  54.999  16.555  1.00 15.66           N  
ATOM     56  N   GLU A   8      69.288  52.757  12.106  1.00 10.83           N  
ATOM     57  CA  GLU A   8      69.408  52.777  10.649  1.00 12.69           C  
ATOM     58  C   GLU A   8      68.177  52.248   9.914  1.00 12.04           C  
ATOM     59  O   GLU A   8      68.004  52.494   8.714  1.00  9.39           O  
ATOM     60  CB  GLU A   8      70.660  52.022  10.206  1.00 14.40           C  
ATOM     61  CG  GLU A   8      71.924  52.637  10.744  1.00 18.71           C  
ATOM     62  CD  GLU A   8      73.135  51.806  10.459  1.00 26.07           C  
ATOM     63  OE1 GLU A   8      73.209  50.667  10.967  1.00 30.91           O  
ATOM     64  OE2 GLU A   8      74.016  52.292   9.727  1.00 32.62           O  
ATOM     65  N   TYR A   9      67.322  51.522  10.624  1.00 12.76           N  
ATOM     66  CA  TYR A   9      66.116  50.992  10.009  1.00 14.99           C  
ATOM     67  C   TYR A   9      65.124  52.110   9.691  1.00 17.70           C  
ATOM     68  O   TYR A   9      64.442  52.072   8.667  1.00 12.27           O  
ATOM     69  CB  TYR A   9      65.487  49.927  10.898  1.00  7.24           C  
ATOM     70  CG  TYR A   9      66.022  48.554  10.597  1.00 11.31           C  
ATOM     71  CD1 TYR A   9      65.887  48.011   9.324  1.00 10.48           C  
ATOM     72  CD2 TYR A   9      66.690  47.807  11.569  1.00  8.08           C  
ATOM     73  CE1 TYR A   9      66.399  46.766   9.018  1.00  8.32           C  
ATOM     74  CE2 TYR A   9      67.209  46.559  11.275  1.00  7.60           C  
ATOM     75  CZ  TYR A   9      67.060  46.046   9.992  1.00 11.99           C  
ATOM     76  OH  TYR A   9      67.583  44.821   9.667  1.00  8.48           O  
ATOM     77  N   GLU A  10      65.097  53.138  10.535  1.00 18.06           N  
ATOM     78  CA  GLU A  10      64.191  54.256  10.327  1.00 22.45           C  
ATOM     79  C   GLU A  10      64.379  54.870   8.938  1.00 22.62           C  
ATOM     80  O   GLU A  10      63.402  55.152   8.245  1.00 24.39           O  
ATOM     81  CB  GLU A  10      64.378  55.314  11.416  1.00 22.21           C  
ATOM     82  CG  GLU A  10      63.353  56.446  11.346  1.00 28.64           C  
ATOM     83  CD  GLU A  10      63.366  57.340  12.576  1.00 32.66           C  
ATOM     84  OE1 GLU A  10      64.110  57.034  13.536  1.00 38.42           O  
ATOM     85  OE2 GLU A  10      62.620  58.347  12.586  1.00 31.35           O  
ATOM     86  N   ALA A  11      65.631  55.013   8.513  1.00 18.34           N  
ATOM     87  CA  ALA A  11      65.939  55.590   7.205  1.00 17.24           C  
ATOM     88  C   ALA A  11      65.386  54.751   6.050  1.00 16.50           C  
ATOM     89  O   ALA A  11      64.816  55.278   5.093  1.00 14.18           O  
ATOM     90  CB  ALA A  11      67.428  55.751   7.059  1.00 16.09           C  
ATOM     91  N   ILE A  12      65.568  53.441   6.148  1.00 18.44           N  
ATOM     92  CA  ILE A  12      65.091  52.525   5.123  1.00 16.64           C  
ATOM     93  C   ILE A  12      63.572  52.541   5.105  1.00 16.96           C  
ATOM     94  O   ILE A  12      62.964  52.656   4.044  1.00 18.92           O  
ATOM     95  CB  ILE A  12      65.603  51.098   5.383  1.00 16.43           C  
ATOM     96  CG1 ILE A  12      67.135  51.105   5.368  1.00 15.02           C  
ATOM     97  CG2 ILE A  12      65.052  50.134   4.334  1.00 11.47           C  
ATOM     98  CD1 ILE A  12      67.770  49.835   5.885  1.00 24.27           C  
ATOM     99  N   ALA A  13      62.969  52.470   6.288  1.00 18.95           N  
ATOM    100  CA  ALA A  13      61.517  52.482   6.427  1.00 16.59           C  
ATOM    101  C   ALA A  13      60.968  53.723   5.749  1.00 19.32           C  
ATOM    102  O   ALA A  13      60.044  53.644   4.944  1.00 20.48           O  
ATOM    103  CB  ALA A  13      61.136  52.477   7.894  1.00 14.95           C  
ATOM    104  N   LYS A  14      61.592  54.858   6.047  1.00 21.89           N  
ATOM    105  CA  LYS A  14      61.217  56.149   5.493  1.00 24.24           C  
ATOM    106  C   LYS A  14      61.307  56.145   3.980  1.00 28.15           C  
ATOM    107  O   LYS A  14      60.365  56.529   3.294  1.00 35.34           O  
ATOM    108  CB  LYS A  14      62.137  57.237   6.050  1.00 27.40           C  
ATOM    109  CG  LYS A  14      61.751  58.657   5.683  1.00 30.59           C  
ATOM    110  CD  LYS A  14      62.798  59.634   6.194  1.00 38.13           C  
ATOM    111  CE  LYS A  14      62.307  61.079   6.193  1.00 41.68           C  
ATOM    112  NZ  LYS A  14      62.004  61.621   4.838  1.00 44.86           N  
ATOM    113  N   GLN A  15      62.432  55.682   3.456  1.00 34.53           N  
ATOM    114  CA  GLN A  15      62.625  55.658   2.016  1.00 37.92           C  
ATOM    115  C   GLN A  15      61.706  54.704   1.260  1.00 32.25           C  
ATOM    116  O   GLN A  15      61.601  54.789   0.038  1.00 37.26           O  
ATOM    117  CB  GLN A  15      64.096  55.390   1.665  1.00 46.99           C  
ATOM    118  CG  GLN A  15      64.379  54.031   1.029  1.00 54.58           C  
ATOM    119  CD  GLN A  15      65.603  54.040   0.127  1.00 59.11           C  
ATOM    120  OE1 GLN A  15      66.258  53.012  -0.059  1.00 63.05           O  
ATOM    121  NE2 GLN A  15      65.901  55.193  -0.461  1.00 58.83           N  
ATOM    122  N   LYS A  16      61.031  53.802   1.960  1.00 30.41           N  
ATOM    123  CA  LYS A  16      60.153  52.872   1.261  1.00 35.32           C  
ATOM    124  C   LYS A  16      58.662  52.985   1.553  1.00 36.06           C  
ATOM    125  O   LYS A  16      57.844  52.652   0.693  1.00 38.88           O  
ATOM    126  CB  LYS A  16      60.621  51.425   1.434  1.00 39.25           C  
ATOM    127  CG  LYS A  16      60.657  50.907   2.861  1.00 43.77           C  
ATOM    128  CD  LYS A  16      60.768  49.388   2.873  1.00 46.49           C  
ATOM    129  CE  LYS A  16      61.903  48.886   1.983  1.00 48.42           C  
ATOM    130  NZ  LYS A  16      61.839  47.403   1.797  1.00 48.86           N  
ATOM    131  N   LEU A  17      58.310  53.435   2.755  1.00 32.95           N  
ATOM    132  CA  LEU A  17      56.908  53.587   3.151  1.00 23.18           C  
ATOM    133  C   LEU A  17      56.317  54.875   2.583  1.00 21.88           C  
ATOM    134  O   LEU A  17      57.053  55.804   2.237  1.00 29.60           O  
ATOM    135  CB  LEU A  17      56.787  53.647   4.676  1.00 18.24           C  
ATOM    136  CG  LEU A  17      57.106  52.418   5.516  1.00 15.18           C  
ATOM    137  CD1 LEU A  17      57.007  52.767   7.001  1.00 11.51           C  
ATOM    138  CD2 LEU A  17      56.143  51.316   5.168  1.00 16.28           C  
ATOM    139  N   PRO A  18      54.983  54.919   2.413  1.00 16.81           N  
ATOM    140  CA  PRO A  18      54.323  56.122   1.891  1.00 12.25           C  
ATOM    141  C   PRO A  18      54.398  57.176   2.999  1.00  9.74           C  
ATOM    142  O   PRO A  18      54.317  56.834   4.190  1.00  7.17           O  
ATOM    143  CB  PRO A  18      52.877  55.660   1.689  1.00 14.28           C  
ATOM    144  CG  PRO A  18      52.996  54.186   1.490  1.00 13.68           C  
ATOM    145  CD  PRO A  18      54.034  53.797   2.497  1.00 16.18           C  
ATOM    146  N   LYS A  19      54.525  58.445   2.620  1.00  6.50           N  
ATOM    147  CA  LYS A  19      54.629  59.527   3.598  1.00  6.23           C  
ATOM    148  C   LYS A  19      53.659  59.360   4.761  1.00  6.76           C  
ATOM    149  O   LYS A  19      54.069  59.364   5.921  1.00  8.97           O  
ATOM    150  CB  LYS A  19      54.405  60.880   2.935  1.00 12.49           C  
ATOM    151  CG  LYS A  19      54.853  62.050   3.787  1.00 16.72           C  
ATOM    152  CD  LYS A  19      54.284  63.361   3.280  1.00 19.71           C  
ATOM    153  CE  LYS A  19      55.019  64.552   3.885  1.00 27.36           C  
ATOM    154  NZ  LYS A  19      54.978  64.626   5.371  1.00 23.52           N  
ATOM    155  N   MET A  20      52.385  59.145   4.445  1.00 10.54           N  
ATOM    156  CA  MET A  20      51.345  58.965   5.458  1.00 10.54           C  
ATOM    157  C   MET A  20      51.694  57.896   6.493  1.00 12.54           C  
ATOM    158  O   MET A  20      51.586  58.134   7.695  1.00 21.74           O  
ATOM    159  CB  MET A  20      50.008  58.621   4.791  1.00 12.68           C  
ATOM    160  CG  MET A  20      48.905  58.229   5.768  1.00 22.11           C  
ATOM    161  SD  MET A  20      47.365  57.743   4.967  1.00 19.56           S  
ATOM    162  CE  MET A  20      46.898  59.327   4.195  1.00 25.41           C  
ATOM    163  N   VAL A  21      52.133  56.731   6.027  1.00 15.81           N  
ATOM    164  CA  VAL A  21      52.474  55.626   6.918  1.00 13.78           C  
ATOM    165  C   VAL A  21      53.715  55.929   7.747  1.00 11.74           C  
ATOM    166  O   VAL A  21      53.710  55.758   8.971  1.00 12.28           O  
ATOM    167  CB  VAL A  21      52.658  54.298   6.129  1.00 16.22           C  
ATOM    168  CG1 VAL A  21      52.971  53.152   7.074  1.00 14.59           C  
ATOM    169  CG2 VAL A  21      51.390  53.978   5.356  1.00 18.85           C  
ATOM    170  N   TYR A  22      54.765  56.416   7.096  1.00 11.19           N  
ATOM    171  CA  TYR A  22      55.982  56.734   7.820  1.00  8.73           C  
ATOM    172  C   TYR A  22      55.701  57.794   8.874  1.00 14.16           C  
ATOM    173  O   TYR A  22      56.042  57.614  10.042  1.00 13.81           O  
ATOM    174  CB  TYR A  22      57.093  57.208   6.885  1.00 12.33           C  
ATOM    175  CG  TYR A  22      58.315  57.672   7.637  1.00 14.24           C  
ATOM    176  CD1 TYR A  22      59.175  56.757   8.236  1.00  9.77           C  
ATOM    177  CD2 TYR A  22      58.580  59.034   7.800  1.00 17.35           C  
ATOM    178  CE1 TYR A  22      60.262  57.178   8.979  1.00 13.09           C  
ATOM    179  CE2 TYR A  22      59.664  59.465   8.543  1.00 14.84           C  
ATOM    180  CZ  TYR A  22      60.503  58.533   9.130  1.00 14.60           C  
ATOM    181  OH  TYR A  22      61.585  58.956   9.868  1.00 13.11           O  
ATOM    182  N   ASP A  23      55.063  58.890   8.466  1.00 14.77           N  
ATOM    183  CA  ASP A  23      54.742  59.963   9.398  1.00 16.67           C  
ATOM    184  C   ASP A  23      53.933  59.484  10.591  1.00 17.67           C  
ATOM    185  O   ASP A  23      54.199  59.902  11.715  1.00 21.67           O  
ATOM    186  CB  ASP A  23      54.020  61.109   8.696  1.00 16.94           C  
ATOM    187  CG  ASP A  23      54.937  61.919   7.812  1.00 14.83           C  
ATOM    188  OD1 ASP A  23      56.139  62.043   8.133  1.00 19.81           O  
ATOM    189  OD2 ASP A  23      54.451  62.432   6.790  1.00 16.80           O  
ATOM    190  N   TYR A  24      52.965  58.603  10.356  1.00 15.46           N  
ATOM    191  CA  TYR A  24      52.151  58.074  11.444  1.00 14.13           C  
ATOM    192  C   TYR A  24      53.032  57.357  12.479  1.00 14.19           C  
ATOM    193  O   TYR A  24      52.886  57.580  13.675  1.00  7.75           O  
ATOM    194  CB  TYR A  24      51.057  57.134  10.916  1.00 12.56           C  
ATOM    195  CG  TYR A  24      50.425  56.290  12.004  1.00 14.61           C  
ATOM    196  CD1 TYR A  24      49.688  56.877  13.035  1.00 12.07           C  
ATOM    197  CD2 TYR A  24      50.653  54.915  12.063  1.00 16.36           C  
ATOM    198  CE1 TYR A  24      49.209  56.116  14.104  1.00 12.38           C  
ATOM    199  CE2 TYR A  24      50.177  54.147  13.128  1.00 12.68           C  
ATOM    200  CZ  TYR A  24      49.463  54.753  14.145  1.00 11.90           C  
ATOM    201  OH  TYR A  24      49.036  53.999  15.215  1.00 10.94           O  
ATOM    202  N   TYR A  25      53.959  56.520  12.019  1.00 13.50           N  
ATOM    203  CA  TYR A  25      54.843  55.796  12.936  1.00 10.76           C  
ATOM    204  C   TYR A  25      55.927  56.686  13.551  1.00  8.03           C  
ATOM    205  O   TYR A  25      56.257  56.561  14.729  1.00 10.98           O  
ATOM    206  CB  TYR A  25      55.555  54.634  12.223  1.00  9.92           C  
ATOM    207  CG  TYR A  25      54.694  53.499  11.696  1.00 12.98           C  
ATOM    208  CD1 TYR A  25      53.638  52.963  12.443  1.00 11.25           C  
ATOM    209  CD2 TYR A  25      54.992  52.908  10.467  1.00 13.29           C  
ATOM    210  CE1 TYR A  25      52.907  51.856  11.971  1.00 11.91           C  
ATOM    211  CE2 TYR A  25      54.274  51.814   9.991  1.00 13.23           C  
ATOM    212  CZ  TYR A  25      53.238  51.290  10.742  1.00 16.18           C  
ATOM    213  OH  TYR A  25      52.563  50.192  10.251  1.00 18.10           O  
ATOM    214  N   ALA A  26      56.472  57.593  12.755  1.00 10.72           N  
ATOM    215  CA  ALA A  26      57.563  58.444  13.209  1.00 14.54           C  
ATOM    216  C   ALA A  26      57.261  59.690  14.019  1.00 16.17           C  
ATOM    217  O   ALA A  26      58.081  60.092  14.850  1.00 20.47           O  
ATOM    218  CB  ALA A  26      58.451  58.812  12.034  1.00 15.47           C  
ATOM    219  N   SER A  27      56.098  60.296  13.815  1.00 15.35           N  
ATOM    220  CA  SER A  27      55.790  61.542  14.511  1.00 11.94           C  
ATOM    221  C   SER A  27      55.538  61.525  16.008  1.00  8.83           C  
ATOM    222  O   SER A  27      55.154  60.510  16.588  1.00  8.07           O  
ATOM    223  CB  SER A  27      54.666  62.300  13.800  1.00 12.38           C  
ATOM    224  OG  SER A  27      53.476  61.535  13.745  1.00 33.09           O  
ATOM    225  N   GLY A  28      55.813  62.675  16.619  1.00 10.89           N  
ATOM    226  CA  GLY A  28      55.598  62.886  18.034  1.00  9.15           C  
ATOM    227  C   GLY A  28      54.473  63.906  18.153  1.00 11.35           C  
ATOM    228  O   GLY A  28      53.841  64.270  17.149  1.00  9.61           O  
ATOM    229  N   ALA A  29      54.241  64.414  19.354  1.00  7.11           N  
ATOM    230  CA  ALA A  29      53.171  65.382  19.552  1.00  9.58           C  
ATOM    231  C   ALA A  29      53.599  66.805  19.266  1.00 10.23           C  
ATOM    232  O   ALA A  29      54.641  67.262  19.745  1.00 11.08           O  
ATOM    233  CB  ALA A  29      52.617  65.280  20.967  1.00 10.85           C  
ATOM    234  N   GLU A  30      52.782  67.500  18.486  1.00 14.50           N  
ATOM    235  CA  GLU A  30      53.000  68.902  18.130  1.00 13.42           C  
ATOM    236  C   GLU A  30      54.413  69.280  17.696  1.00 11.75           C  
ATOM    237  O   GLU A  30      54.842  68.872  16.617  1.00 12.83           O  
ATOM    238  CB  GLU A  30      52.465  69.814  19.245  1.00 12.57           C  
ATOM    239  CG  GLU A  30      50.941  69.782  19.302  1.00 15.98           C  
ATOM    240  CD  GLU A  30      50.331  70.587  20.429  1.00 19.39           C  
ATOM    241  OE1 GLU A  30      50.836  70.531  21.571  1.00 18.89           O  
ATOM    242  OE2 GLU A  30      49.306  71.250  20.167  1.00 16.31           O  
ATOM    243  N   ASP A  31      55.141  70.046  18.509  1.00  8.09           N  
ATOM    244  CA  ASP A  31      56.492  70.444  18.125  1.00 10.05           C  
ATOM    245  C   ASP A  31      57.546  69.362  18.313  1.00 13.44           C  
ATOM    246  O   ASP A  31      58.721  69.563  18.005  1.00 17.52           O  
ATOM    247  CB  ASP A  31      56.901  71.758  18.795  1.00  9.99           C  
ATOM    248  CG  ASP A  31      56.244  72.972  18.143  1.00  9.67           C  
ATOM    249  OD1 ASP A  31      56.039  72.955  16.915  1.00  5.86           O  
ATOM    250  OD2 ASP A  31      55.923  73.942  18.857  1.00 11.44           O  
ATOM    251  N   GLN A  32      57.110  68.210  18.813  1.00 15.28           N  
ATOM    252  CA  GLN A  32      57.974  67.051  19.008  1.00  9.98           C  
ATOM    253  C   GLN A  32      59.254  67.298  19.803  1.00 13.31           C  
ATOM    254  O   GLN A  32      60.342  66.859  19.412  1.00 13.37           O  
ATOM    255  CB  GLN A  32      58.304  66.436  17.646  1.00  8.29           C  
ATOM    256  CG  GLN A  32      57.069  66.176  16.797  1.00  5.29           C  
ATOM    257  CD  GLN A  32      57.400  65.630  15.431  1.00  4.56           C  
ATOM    258  OE1 GLN A  32      57.291  64.435  15.193  1.00 11.75           O  
ATOM    259  NE2 GLN A  32      57.795  66.502  14.522  1.00 11.51           N  
ATOM    260  N   TRP A  33      59.122  67.974  20.939  1.00 12.40           N  
ATOM    261  CA  TRP A  33      60.274  68.241  21.789  1.00 10.56           C  
ATOM    262  C   TRP A  33      60.661  66.993  22.571  1.00 12.67           C  
ATOM    263  O   TRP A  33      61.841  66.628  22.650  1.00 10.12           O  
ATOM    264  CB  TRP A  33      59.963  69.367  22.765  1.00  6.73           C  
ATOM    265  CG  TRP A  33      61.118  69.720  23.637  1.00  7.58           C  
ATOM    266  CD1 TRP A  33      62.084  70.649  23.378  1.00  2.00           C  
ATOM    267  CD2 TRP A  33      61.422  69.176  24.931  1.00  7.12           C  
ATOM    268  NE1 TRP A  33      62.967  70.713  24.426  1.00  2.00           N  
ATOM    269  CE2 TRP A  33      62.587  69.815  25.390  1.00  4.92           C  
ATOM    270  CE3 TRP A  33      60.825  68.197  25.738  1.00 10.12           C  
ATOM    271  CZ2 TRP A  33      63.159  69.524  26.634  1.00  5.40           C  
ATOM    272  CZ3 TRP A  33      61.396  67.908  26.974  1.00  5.97           C  
ATOM    273  CH2 TRP A  33      62.554  68.565  27.402  1.00  3.65           C  
ATOM    274  N   THR A  34      59.663  66.358  23.178  1.00 10.79           N  
ATOM    275  CA  THR A  34      59.891  65.164  23.972  1.00  7.63           C  
ATOM    276  C   THR A  34      60.355  63.997  23.114  1.00  8.54           C  
ATOM    277  O   THR A  34      61.066  63.118  23.599  1.00  5.91           O  
ATOM    278  CB  THR A  34      58.645  64.812  24.793  1.00 10.84           C  
ATOM    279  OG1 THR A  34      58.415  65.858  25.750  1.00  3.53           O  
ATOM    280  CG2 THR A  34      58.805  63.452  25.517  1.00  2.75           C  
ATOM    281  N   LEU A  35      59.987  64.014  21.832  1.00  2.00           N  
ATOM    282  CA  LEU A  35      60.407  62.961  20.914  1.00  4.03           C  
ATOM    283  C   LEU A  35      61.936  62.997  20.872  1.00 11.62           C  
ATOM    284  O   LEU A  35      62.610  62.009  21.189  1.00 11.57           O  
ATOM    285  CB  LEU A  35      59.840  63.206  19.519  1.00  3.18           C  
ATOM    286  CG  LEU A  35      60.141  62.094  18.510  1.00  4.08           C  
ATOM    287  CD1 LEU A  35      59.408  60.826  18.908  1.00  2.00           C  
ATOM    288  CD2 LEU A  35      59.748  62.524  17.107  1.00  2.00           C  
ATOM    289  N   ALA A  36      62.467  64.172  20.547  1.00 10.31           N  
ATOM    290  CA  ALA A  36      63.898  64.394  20.483  1.00  5.77           C  
ATOM    291  C   ALA A  36      64.555  64.139  21.837  1.00  7.57           C  
ATOM    292  O   ALA A  36      65.609  63.507  21.921  1.00 11.65           O  
ATOM    293  CB  ALA A  36      64.165  65.809  20.037  1.00  5.13           C  
ATOM    294  N   GLU A  37      63.919  64.622  22.897  1.00  6.67           N  
ATOM    295  CA  GLU A  37      64.439  64.458  24.249  1.00  5.07           C  
ATOM    296  C   GLU A  37      64.503  62.991  24.712  1.00  8.33           C  
ATOM    297  O   GLU A  37      65.433  62.612  25.420  1.00 15.99           O  
ATOM    298  CB  GLU A  37      63.616  65.316  25.218  1.00  7.27           C  
ATOM    299  CG  GLU A  37      64.009  65.236  26.686  1.00 10.27           C  
ATOM    300  CD  GLU A  37      65.224  66.082  27.066  1.00 15.83           C  
ATOM    301  OE1 GLU A  37      66.164  66.227  26.256  1.00 10.01           O  
ATOM    302  OE2 GLU A  37      65.240  66.592  28.212  1.00 19.19           O  
ATOM    303  N   ASN A  38      63.541  62.163  24.300  1.00 11.53           N  
ATOM    304  CA  ASN A  38      63.529  60.744  24.685  1.00  6.74           C  
ATOM    305  C   ASN A  38      64.846  60.095  24.295  1.00  5.21           C  
ATOM    306  O   ASN A  38      65.346  59.230  25.002  1.00  6.88           O  
ATOM    307  CB  ASN A  38      62.376  59.968  24.024  1.00  3.93           C  
ATOM    308  CG  ASN A  38      61.087  59.960  24.866  1.00  2.00           C  
ATOM    309  OD1 ASN A  38      61.079  60.307  26.054  1.00  2.00           O  
ATOM    310  ND2 ASN A  38      59.996  59.545  24.244  1.00  2.00           N  
ATOM    311  N   ARG A  39      65.406  60.513  23.166  1.00  5.51           N  
ATOM    312  CA  ARG A  39      66.678  59.956  22.705  1.00 10.87           C  
ATOM    313  C   ARG A  39      67.870  60.679  23.354  1.00  9.27           C  
ATOM    314  O   ARG A  39      68.764  60.056  23.928  1.00  7.29           O  
ATOM    315  CB  ARG A  39      66.779  60.064  21.183  1.00  8.64           C  
ATOM    316  CG  ARG A  39      65.868  59.140  20.405  1.00  7.49           C  
ATOM    317  CD  ARG A  39      66.279  57.684  20.548  1.00 17.85           C  
ATOM    318  NE  ARG A  39      67.668  57.437  20.149  1.00 20.55           N  
ATOM    319  CZ  ARG A  39      68.601  56.922  20.951  1.00 17.82           C  
ATOM    320  NH1 ARG A  39      68.309  56.597  22.205  1.00 18.93           N  
ATOM    321  NH2 ARG A  39      69.828  56.717  20.496  1.00 17.28           N  
ATOM    322  N   ASN A  40      67.836  62.003  23.301  1.00  9.68           N  
ATOM    323  CA  ASN A  40      68.896  62.852  23.849  1.00 14.35           C  
ATOM    324  C   ASN A  40      69.178  62.692  25.344  1.00  9.71           C  
ATOM    325  O   ASN A  40      70.323  62.811  25.787  1.00 10.66           O  
ATOM    326  CB  ASN A  40      68.611  64.332  23.534  1.00 13.37           C  
ATOM    327  CG  ASN A  40      68.610  64.627  22.029  1.00 22.51           C  
ATOM    328  OD1 ASN A  40      69.053  63.813  21.207  1.00 24.46           O  
ATOM    329  ND2 ASN A  40      68.113  65.804  21.665  1.00 23.37           N  
ATOM    330  N   ALA A  41      68.155  62.392  26.126  1.00  5.15           N  
ATOM    331  CA  ALA A  41      68.365  62.257  27.549  1.00  2.00           C  
ATOM    332  C   ALA A  41      69.370  61.169  27.901  1.00  5.10           C  
ATOM    333  O   ALA A  41      70.188  61.362  28.793  1.00 11.41           O  
ATOM    334  CB  ALA A  41      67.064  62.032  28.243  1.00  2.00           C  
ATOM    335  N   PHE A  42      69.343  60.042  27.192  1.00  4.87           N  
ATOM    336  CA  PHE A  42      70.278  58.954  27.471  1.00  2.34           C  
ATOM    337  C   PHE A  42      71.733  59.443  27.383  1.00  7.55           C  
ATOM    338  O   PHE A  42      72.603  58.946  28.103  1.00  7.81           O  
ATOM    339  CB  PHE A  42      70.061  57.781  26.506  1.00  6.95           C  
ATOM    340  CG  PHE A  42      68.894  56.888  26.862  1.00  8.18           C  
ATOM    341  CD1 PHE A  42      68.962  56.035  27.958  1.00  7.83           C  
ATOM    342  CD2 PHE A  42      67.726  56.903  26.101  1.00  2.12           C  
ATOM    343  CE1 PHE A  42      67.884  55.218  28.291  1.00  8.08           C  
ATOM    344  CE2 PHE A  42      66.649  56.092  26.426  1.00  2.00           C  
ATOM    345  CZ  PHE A  42      66.726  55.250  27.522  1.00  2.00           C  
ATOM    346  N   SER A  43      71.985  60.429  26.517  1.00  4.38           N  
ATOM    347  CA  SER A  43      73.320  61.002  26.325  1.00  5.03           C  
ATOM    348  C   SER A  43      73.816  61.772  27.543  1.00  7.09           C  
ATOM    349  O   SER A  43      74.969  62.199  27.583  1.00 14.12           O  
ATOM    350  CB  SER A  43      73.339  61.940  25.117  1.00  6.85           C  
ATOM    351  OG  SER A  43      72.995  61.259  23.921  1.00 18.09           O  
ATOM    352  N   ARG A  44      72.946  61.960  28.529  1.00  8.14           N  
ATOM    353  CA  ARG A  44      73.304  62.689  29.734  1.00  8.09           C  
ATOM    354  C   ARG A  44      73.585  61.765  30.913  1.00  7.64           C  
ATOM    355  O   ARG A  44      73.595  62.196  32.071  1.00  7.83           O  
ATOM    356  CB  ARG A  44      72.201  63.697  30.081  1.00 12.80           C  
ATOM    357  CG  ARG A  44      71.945  64.699  28.965  1.00 16.82           C  
ATOM    358  CD  ARG A  44      71.171  65.912  29.438  1.00 19.74           C  
ATOM    359  NE  ARG A  44      69.792  65.596  29.791  1.00 23.94           N  
ATOM    360  CZ  ARG A  44      68.759  65.722  28.962  1.00 23.72           C  
ATOM    361  NH1 ARG A  44      68.936  66.156  27.714  1.00 18.46           N  
ATOM    362  NH2 ARG A  44      67.542  65.414  29.388  1.00 23.09           N  
ATOM    363  N   ILE A  45      73.783  60.485  30.621  1.00  6.56           N  
ATOM    364  CA  ILE A  45      74.080  59.501  31.652  1.00  7.61           C  
ATOM    365  C   ILE A  45      75.369  58.806  31.216  1.00  9.12           C  
ATOM    366  O   ILE A  45      75.481  58.353  30.080  1.00  2.00           O  
ATOM    367  CB  ILE A  45      72.950  58.472  31.791  1.00  7.80           C  
ATOM    368  CG1 ILE A  45      71.618  59.185  32.018  1.00  8.38           C  
ATOM    369  CG2 ILE A  45      73.243  57.536  32.954  1.00  7.22           C  
ATOM    370  CD1 ILE A  45      70.443  58.261  32.108  1.00 12.30           C  
ATOM    371  N   LEU A  46      76.350  58.758  32.106  1.00  6.76           N  
ATOM    372  CA  LEU A  46      77.619  58.149  31.775  1.00 11.67           C  
ATOM    373  C   LEU A  46      77.903  56.901  32.593  1.00 10.12           C  
ATOM    374  O   LEU A  46      77.276  56.664  33.635  1.00  4.48           O  
ATOM    375  CB  LEU A  46      78.749  59.176  31.926  1.00 14.94           C  
ATOM    376  CG  LEU A  46      78.519  60.475  31.141  1.00 18.53           C  
ATOM    377  CD1 LEU A  46      79.700  61.412  31.303  1.00 13.89           C  
ATOM    378  CD2 LEU A  46      78.279  60.170  29.664  1.00 17.88           C  
ATOM    379  N   PHE A  47      78.841  56.100  32.093  1.00 11.41           N  
ATOM    380  CA  PHE A  47      79.247  54.851  32.733  1.00  9.40           C  
ATOM    381  C   PHE A  47      80.435  55.020  33.663  1.00 12.01           C  
ATOM    382  O   PHE A  47      81.235  55.956  33.525  1.00 14.53           O  
ATOM    383  CB  PHE A  47      79.641  53.824  31.678  1.00  4.01           C  
ATOM    384  CG  PHE A  47      78.515  53.399  30.800  1.00  7.88           C  
ATOM    385  CD1 PHE A  47      77.371  52.825  31.346  1.00  2.00           C  
ATOM    386  CD2 PHE A  47      78.608  53.540  29.422  1.00  2.04           C  
ATOM    387  CE1 PHE A  47      76.343  52.396  30.529  1.00  2.00           C  
ATOM    388  CE2 PHE A  47      77.578  53.114  28.599  1.00  4.39           C  
ATOM    389  CZ  PHE A  47      76.446  52.540  29.152  1.00  4.38           C  
ATOM    390  N   ARG A  48      80.557  54.066  34.578  1.00  7.83           N  
ATOM    391  CA  ARG A  48      81.641  54.000  35.543  1.00  7.80           C  
ATOM    392  C   ARG A  48      81.962  52.516  35.566  1.00  8.10           C  
ATOM    393  O   ARG A  48      81.691  51.826  36.550  1.00  5.47           O  
ATOM    394  CB  ARG A  48      81.165  54.448  36.920  1.00  7.95           C  
ATOM    395  CG  ARG A  48      80.516  55.815  36.934  1.00 10.43           C  
ATOM    396  CD  ARG A  48      80.403  56.354  38.343  1.00 15.83           C  
ATOM    397  NE  ARG A  48      81.718  56.609  38.922  1.00 20.12           N  
ATOM    398  CZ  ARG A  48      82.253  55.895  39.906  1.00 22.12           C  
ATOM    399  NH1 ARG A  48      81.585  54.879  40.434  1.00 24.33           N  
ATOM    400  NH2 ARG A  48      83.472  56.176  40.339  1.00 21.13           N  
ATOM    401  N   PRO A  49      82.537  52.003  34.464  1.00  8.57           N  
ATOM    402  CA  PRO A  49      82.897  50.591  34.311  1.00 11.92           C  
ATOM    403  C   PRO A  49      83.955  50.046  35.268  1.00 17.28           C  
ATOM    404  O   PRO A  49      84.868  50.763  35.708  1.00 20.32           O  
ATOM    405  CB  PRO A  49      83.346  50.507  32.852  1.00  8.56           C  
ATOM    406  CG  PRO A  49      83.963  51.852  32.608  1.00  7.41           C  
ATOM    407  CD  PRO A  49      83.031  52.805  33.327  1.00  7.35           C  
ATOM    408  N   ARG A  50      83.794  48.779  35.625  1.00 14.61           N  
ATOM    409  CA  ARG A  50      84.731  48.119  36.504  1.00 11.89           C  
ATOM    410  C   ARG A  50      85.571  47.199  35.627  1.00 11.69           C  
ATOM    411  O   ARG A  50      85.028  46.403  34.862  1.00  4.47           O  
ATOM    412  CB  ARG A  50      83.988  47.326  37.579  1.00 11.51           C  
ATOM    413  CG  ARG A  50      83.071  48.173  38.460  1.00 17.25           C  
ATOM    414  CD  ARG A  50      83.811  49.352  39.073  1.00 17.33           C  
ATOM    415  NE  ARG A  50      85.027  48.928  39.765  1.00 19.82           N  
ATOM    416  CZ  ARG A  50      85.086  48.605  41.055  1.00 20.14           C  
ATOM    417  NH1 ARG A  50      83.993  48.661  41.810  1.00 18.58           N  
ATOM    418  NH2 ARG A  50      86.233  48.191  41.583  1.00 12.91           N  
ATOM    419  N   ILE A  51      86.892  47.346  35.704  1.00  9.17           N  
ATOM    420  CA  ILE A  51      87.789  46.528  34.900  1.00  6.42           C  
ATOM    421  C   ILE A  51      88.328  45.313  35.655  1.00  8.62           C  
ATOM    422  O   ILE A  51      88.105  45.175  36.858  1.00  4.58           O  
ATOM    423  CB  ILE A  51      88.948  47.377  34.317  1.00 10.38           C  
ATOM    424  CG1 ILE A  51      89.609  48.233  35.400  1.00 12.88           C  
ATOM    425  CG2 ILE A  51      88.437  48.269  33.196  1.00  4.31           C  
ATOM    426  CD1 ILE A  51      90.526  47.475  36.333  1.00 16.37           C  
ATOM    427  N   LEU A  52      88.999  44.421  34.933  1.00  9.49           N  
ATOM    428  CA  LEU A  52      89.592  43.213  35.506  1.00  9.00           C  
ATOM    429  C   LEU A  52      88.630  42.335  36.302  1.00 13.95           C  
ATOM    430  O   LEU A  52      88.899  41.952  37.447  1.00 15.86           O  
ATOM    431  CB  LEU A  52      90.831  43.560  36.336  1.00  8.81           C  
ATOM    432  CG  LEU A  52      92.049  44.010  35.525  1.00  6.67           C  
ATOM    433  CD1 LEU A  52      93.156  44.462  36.453  1.00 10.50           C  
ATOM    434  CD2 LEU A  52      92.535  42.878  34.637  1.00  9.06           C  
ATOM    435  N   ILE A  53      87.513  42.000  35.672  1.00 14.53           N  
ATOM    436  CA  ILE A  53      86.512  41.150  36.283  1.00 15.27           C  
ATOM    437  C   ILE A  53      86.258  40.016  35.302  1.00 12.43           C  
ATOM    438  O   ILE A  53      86.210  40.240  34.096  1.00  8.75           O  
ATOM    439  CB  ILE A  53      85.202  41.927  36.559  1.00 19.94           C  
ATOM    440  CG1 ILE A  53      85.429  42.917  37.704  1.00 17.84           C  
ATOM    441  CG2 ILE A  53      84.061  40.962  36.889  1.00 20.05           C  
ATOM    442  CD1 ILE A  53      84.202  43.676  38.118  1.00 21.11           C  
ATOM    443  N   ASP A  54      86.120  38.800  35.818  1.00 11.42           N  
ATOM    444  CA  ASP A  54      85.880  37.648  34.954  1.00  9.89           C  
ATOM    445  C   ASP A  54      84.534  37.794  34.264  1.00  6.36           C  
ATOM    446  O   ASP A  54      83.497  37.506  34.857  1.00  7.93           O  
ATOM    447  CB  ASP A  54      85.912  36.358  35.779  1.00 12.21           C  
ATOM    448  CG  ASP A  54      85.796  35.104  34.917  1.00 15.79           C  
ATOM    449  OD1 ASP A  54      85.484  35.203  33.714  1.00 18.45           O  
ATOM    450  OD2 ASP A  54      86.021  34.004  35.458  1.00 21.87           O  
ATOM    451  N   VAL A  55      84.549  38.212  33.009  1.00  6.62           N  
ATOM    452  CA  VAL A  55      83.308  38.380  32.264  1.00  9.26           C  
ATOM    453  C   VAL A  55      83.206  37.347  31.145  1.00 13.03           C  
ATOM    454  O   VAL A  55      82.828  37.659  30.012  1.00 13.72           O  
ATOM    455  CB  VAL A  55      83.153  39.832  31.710  1.00  5.60           C  
ATOM    456  CG1 VAL A  55      83.145  40.825  32.859  1.00  2.00           C  
ATOM    457  CG2 VAL A  55      84.256  40.163  30.730  1.00  2.18           C  
ATOM    458  N   THR A  56      83.508  36.099  31.494  1.00 16.79           N  
ATOM    459  CA  THR A  56      83.469  34.995  30.545  1.00 17.70           C  
ATOM    460  C   THR A  56      82.047  34.635  30.153  1.00 19.24           C  
ATOM    461  O   THR A  56      81.750  34.470  28.965  1.00 18.46           O  
ATOM    462  CB  THR A  56      84.158  33.760  31.125  1.00 18.12           C  
ATOM    463  OG1 THR A  56      85.521  34.085  31.417  1.00 25.27           O  
ATOM    464  CG2 THR A  56      84.127  32.603  30.134  1.00 21.96           C  
ATOM    465  N   ASN A  57      81.175  34.521  31.150  1.00 17.75           N  
ATOM    466  CA  ASN A  57      79.780  34.176  30.913  1.00 21.40           C  
ATOM    467  C   ASN A  57      78.855  35.277  31.398  1.00 21.43           C  
ATOM    468  O   ASN A  57      78.841  35.604  32.587  1.00 25.66           O  
ATOM    469  CB  ASN A  57      79.433  32.875  31.631  1.00 31.16           C  
ATOM    470  CG  ASN A  57      80.254  31.699  31.139  1.00 36.23           C  
ATOM    471  OD1 ASN A  57      80.295  31.410  29.938  1.00 36.21           O  
ATOM    472  ND2 ASN A  57      80.926  31.022  32.063  1.00 37.04           N  
ATOM    473  N   ILE A  58      78.102  35.865  30.476  1.00 17.59           N  
ATOM    474  CA  ILE A  58      77.161  36.925  30.822  1.00 18.05           C  
ATOM    475  C   ILE A  58      75.734  36.362  30.806  1.00 18.59           C  
ATOM    476  O   ILE A  58      75.302  35.783  29.808  1.00 17.38           O  
ATOM    477  CB  ILE A  58      77.240  38.107  29.819  1.00 16.17           C  
ATOM    478  CG1 ILE A  58      78.668  38.670  29.743  1.00  8.19           C  
ATOM    479  CG2 ILE A  58      76.243  39.188  30.213  1.00 16.18           C  
ATOM    480  CD1 ILE A  58      79.140  39.382  30.984  1.00  6.85           C  
ATOM    481  N   ASP A  59      75.012  36.544  31.908  1.00 17.81           N  
ATOM    482  CA  ASP A  59      73.636  36.074  32.038  1.00 16.94           C  
ATOM    483  C   ASP A  59      72.640  37.237  31.951  1.00 20.34           C  
ATOM    484  O   ASP A  59      72.580  38.095  32.840  1.00 16.08           O  
ATOM    485  CB  ASP A  59      73.460  35.343  33.375  1.00 21.57           C  
ATOM    486  CG  ASP A  59      72.061  34.772  33.553  1.00 25.63           C  
ATOM    487  OD1 ASP A  59      71.507  34.234  32.569  1.00 25.58           O  
ATOM    488  OD2 ASP A  59      71.516  34.864  34.676  1.00 28.10           O  
ATOM    489  N   MET A  60      71.855  37.254  30.881  1.00 16.87           N  
ATOM    490  CA  MET A  60      70.862  38.297  30.660  1.00 19.20           C  
ATOM    491  C   MET A  60      69.441  37.831  30.960  1.00 21.67           C  
ATOM    492  O   MET A  60      68.489  38.580  30.745  1.00 23.95           O  
ATOM    493  CB  MET A  60      70.908  38.760  29.211  1.00 13.27           C  
ATOM    494  CG  MET A  60      72.216  39.356  28.776  1.00 20.09           C  
ATOM    495  SD  MET A  60      72.234  39.688  27.005  1.00 26.68           S  
ATOM    496  CE  MET A  60      70.579  39.255  26.535  1.00 21.09           C  
ATOM    497  N   THR A  61      69.285  36.601  31.433  1.00 22.49           N  
ATOM    498  CA  THR A  61      67.949  36.092  31.715  1.00 24.40           C  
ATOM    499  C   THR A  61      67.328  36.776  32.922  1.00 22.43           C  
ATOM    500  O   THR A  61      68.026  37.149  33.872  1.00 23.01           O  
ATOM    501  CB  THR A  61      67.938  34.565  31.915  1.00 22.50           C  
ATOM    502  OG1 THR A  61      68.696  34.224  33.082  1.00 27.70           O  
ATOM    503  CG2 THR A  61      68.536  33.864  30.700  1.00 22.77           C  
ATOM    504  N   THR A  62      66.012  36.941  32.877  1.00 19.14           N  
ATOM    505  CA  THR A  62      65.300  37.583  33.960  1.00 19.73           C  
ATOM    506  C   THR A  62      63.911  36.971  34.083  1.00 22.33           C  
ATOM    507  O   THR A  62      63.429  36.301  33.162  1.00 16.56           O  
ATOM    508  CB  THR A  62      65.201  39.109  33.727  1.00 20.28           C  
ATOM    509  OG1 THR A  62      64.583  39.740  34.858  1.00 16.56           O  
ATOM    510  CG2 THR A  62      64.410  39.416  32.460  1.00 19.23           C  
ATOM    511  N   THR A  63      63.289  37.184  35.236  1.00 26.80           N  
ATOM    512  CA  THR A  63      61.959  36.661  35.503  1.00 27.13           C  
ATOM    513  C   THR A  63      60.966  37.811  35.638  1.00 26.12           C  
ATOM    514  O   THR A  63      61.005  38.572  36.611  1.00 23.69           O  
ATOM    515  CB  THR A  63      61.943  35.834  36.800  1.00 31.01           C  
ATOM    516  OG1 THR A  63      63.083  34.964  36.828  1.00 33.63           O  
ATOM    517  CG2 THR A  63      60.669  35.002  36.885  1.00 30.68           C  
ATOM    518  N   ILE A  64      60.094  37.943  34.644  1.00 25.30           N  
ATOM    519  CA  ILE A  64      59.074  38.984  34.637  1.00 27.68           C  
ATOM    520  C   ILE A  64      57.712  38.363  34.921  1.00 28.46           C  
ATOM    521  O   ILE A  64      57.214  37.549  34.138  1.00 31.83           O  
ATOM    522  CB  ILE A  64      59.044  39.710  33.282  1.00 26.16           C  
ATOM    523  CG1 ILE A  64      60.353  40.467  33.091  1.00 25.63           C  
ATOM    524  CG2 ILE A  64      57.850  40.655  33.203  1.00 22.11           C  
ATOM    525  CD1 ILE A  64      60.488  41.103  31.750  1.00 33.37           C  
ATOM    526  N   LEU A  65      57.137  38.719  36.064  1.00 26.78           N  
ATOM    527  CA  LEU A  65      55.832  38.210  36.477  1.00 27.89           C  
ATOM    528  C   LEU A  65      55.790  36.680  36.531  1.00 27.25           C  
ATOM    529  O   LEU A  65      54.788  36.047  36.192  1.00 28.16           O  
ATOM    530  CB  LEU A  65      54.729  38.770  35.571  1.00 28.41           C  
ATOM    531  CG  LEU A  65      54.505  40.282  35.702  1.00 28.12           C  
ATOM    532  CD1 LEU A  65      53.617  40.794  34.584  1.00 29.24           C  
ATOM    533  CD2 LEU A  65      53.905  40.602  37.066  1.00 27.60           C  
ATOM    534  N   GLY A  66      56.896  36.095  36.974  1.00 26.75           N  
ATOM    535  CA  GLY A  66      56.976  34.653  37.096  1.00 25.36           C  
ATOM    536  C   GLY A  66      57.506  33.975  35.855  1.00 22.74           C  
ATOM    537  O   GLY A  66      58.003  32.852  35.919  1.00 28.65           O  
ATOM    538  N   PHE A  67      57.421  34.665  34.728  1.00 23.52           N  
ATOM    539  CA  PHE A  67      57.891  34.135  33.461  1.00 22.87           C  
ATOM    540  C   PHE A  67      59.375  34.436  33.280  1.00 24.40           C  
ATOM    541  O   PHE A  67      59.835  35.531  33.592  1.00 26.67           O  
ATOM    542  CB  PHE A  67      57.065  34.741  32.329  1.00 24.06           C  
ATOM    543  CG  PHE A  67      55.583  34.644  32.557  1.00 29.86           C  
ATOM    544  CD1 PHE A  67      54.935  33.418  32.479  1.00 25.85           C  
ATOM    545  CD2 PHE A  67      54.846  35.767  32.920  1.00 31.96           C  
ATOM    546  CE1 PHE A  67      53.587  33.310  32.765  1.00 25.74           C  
ATOM    547  CE2 PHE A  67      53.492  35.666  33.207  1.00 32.01           C  
ATOM    548  CZ  PHE A  67      52.863  34.436  33.132  1.00 30.67           C  
ATOM    549  N   LYS A  68      60.124  33.438  32.830  1.00 25.42           N  
ATOM    550  CA  LYS A  68      61.558  33.572  32.597  1.00 26.27           C  
ATOM    551  C   LYS A  68      61.800  33.864  31.111  1.00 24.05           C  
ATOM    552  O   LYS A  68      61.325  33.127  30.238  1.00 24.92           O  
ATOM    553  CB  LYS A  68      62.270  32.277  33.024  1.00 29.83           C  
ATOM    554  CG  LYS A  68      63.673  32.055  32.450  1.00 41.54           C  
ATOM    555  CD  LYS A  68      64.753  32.922  33.102  1.00 50.44           C  
ATOM    556  CE  LYS A  68      65.293  32.311  34.392  1.00 54.08           C  
ATOM    557  NZ  LYS A  68      64.281  32.269  35.485  1.00 58.10           N  
ATOM    558  N   ILE A  69      62.491  34.967  30.826  1.00 19.08           N  
ATOM    559  CA  ILE A  69      62.801  35.336  29.445  1.00 17.23           C  
ATOM    560  C   ILE A  69      64.314  35.452  29.196  1.00 15.81           C  
ATOM    561  O   ILE A  69      65.110  35.559  30.138  1.00 10.59           O  
ATOM    562  CB  ILE A  69      62.037  36.617  28.980  1.00 15.66           C  
ATOM    563  CG1 ILE A  69      62.420  37.838  29.813  1.00 13.46           C  
ATOM    564  CG2 ILE A  69      60.533  36.396  29.085  1.00 12.06           C  
ATOM    565  CD1 ILE A  69      61.769  39.105  29.312  1.00 11.01           C  
ATOM    566  N   SER A  70      64.697  35.409  27.923  1.00 12.13           N  
ATOM    567  CA  SER A  70      66.098  35.459  27.507  1.00 13.51           C  
ATOM    568  C   SER A  70      66.825  36.755  27.830  1.00 13.83           C  
ATOM    569  O   SER A  70      67.997  36.735  28.214  1.00 15.75           O  
ATOM    570  CB  SER A  70      66.213  35.184  26.004  1.00 12.39           C  
ATOM    571  OG  SER A  70      65.496  36.148  25.245  1.00 12.47           O  
ATOM    572  N   MET A  71      66.115  37.871  27.702  1.00 12.31           N  
ATOM    573  CA  MET A  71      66.678  39.198  27.938  1.00 10.44           C  
ATOM    574  C   MET A  71      65.629  40.180  28.477  1.00 13.63           C  
ATOM    575  O   MET A  71      64.432  39.942  28.372  1.00 12.04           O  
ATOM    576  CB  MET A  71      67.233  39.717  26.623  1.00  8.91           C  
ATOM    577  CG  MET A  71      66.241  39.606  25.500  1.00  7.34           C  
ATOM    578  SD  MET A  71      66.905  40.179  23.957  1.00  9.55           S  
ATOM    579  CE  MET A  71      65.450  40.024  22.928  1.00  2.00           C  
ATOM    580  N   PRO A  72      66.081  41.315  29.056  1.00 14.69           N  
ATOM    581  CA  PRO A  72      65.141  42.311  29.588  1.00 14.70           C  
ATOM    582  C   PRO A  72      64.730  43.341  28.537  1.00 13.29           C  
ATOM    583  O   PRO A  72      64.613  44.536  28.821  1.00 11.34           O  
ATOM    584  CB  PRO A  72      65.958  42.945  30.716  1.00 15.53           C  
ATOM    585  CG  PRO A  72      67.320  42.980  30.134  1.00 17.15           C  
ATOM    586  CD  PRO A  72      67.460  41.633  29.442  1.00 16.02           C  
ATOM    587  N   ILE A  73      64.517  42.862  27.314  1.00 11.69           N  
ATOM    588  CA  ILE A  73      64.128  43.699  26.183  1.00  8.06           C  
ATOM    589  C   ILE A  73      62.877  43.070  25.593  1.00 12.52           C  
ATOM    590  O   ILE A  73      62.925  41.988  24.998  1.00 15.63           O  
ATOM    591  CB  ILE A  73      65.240  43.732  25.109  1.00  7.07           C  
ATOM    592  CG1 ILE A  73      66.522  44.316  25.702  1.00 10.62           C  
ATOM    593  CG2 ILE A  73      64.802  44.548  23.909  1.00 10.97           C  
ATOM    594  CD1 ILE A  73      67.680  44.320  24.750  1.00 17.17           C  
ATOM    595  N   MET A  74      61.749  43.734  25.790  1.00  9.92           N  
ATOM    596  CA  MET A  74      60.482  43.223  25.299  1.00  5.80           C  
ATOM    597  C   MET A  74      59.923  44.146  24.244  1.00  4.25           C  
ATOM    598  O   MET A  74      60.450  45.242  24.029  1.00 13.04           O  
ATOM    599  CB  MET A  74      59.524  43.074  26.474  1.00  6.97           C  
ATOM    600  CG  MET A  74      60.058  42.149  27.558  1.00  8.72           C  
ATOM    601  SD  MET A  74      59.341  42.494  29.149  1.00  9.24           S  
ATOM    602  CE  MET A  74      60.381  43.823  29.680  1.00 13.70           C  
ATOM    603  N   ILE A  75      58.877  43.703  23.560  1.00  5.48           N  
ATOM    604  CA  ILE A  75      58.270  44.519  22.509  1.00  9.31           C  
ATOM    605  C   ILE A  75      57.019  45.239  23.008  1.00  9.51           C  
ATOM    606  O   ILE A  75      56.147  44.631  23.631  1.00  7.97           O  
ATOM    607  CB  ILE A  75      57.936  43.670  21.264  1.00  7.69           C  
ATOM    608  CG1 ILE A  75      59.211  43.053  20.696  1.00  3.38           C  
ATOM    609  CG2 ILE A  75      57.256  44.528  20.196  1.00  9.53           C  
ATOM    610  CD1 ILE A  75      58.963  42.097  19.555  1.00 11.24           C  
ATOM    611  N   ALA A  76      56.961  46.543  22.745  1.00 14.10           N  
ATOM    612  CA  ALA A  76      55.834  47.390  23.139  1.00  9.00           C  
ATOM    613  C   ALA A  76      54.702  47.268  22.129  1.00  9.51           C  
ATOM    614  O   ALA A  76      54.930  46.944  20.960  1.00 15.63           O  
ATOM    615  CB  ALA A  76      56.278  48.811  23.217  1.00  6.52           C  
ATOM    616  N   PRO A  77      53.462  47.530  22.560  1.00  8.35           N  
ATOM    617  CA  PRO A  77      52.348  47.425  21.616  1.00  7.70           C  
ATOM    618  C   PRO A  77      52.289  48.611  20.671  1.00 10.03           C  
ATOM    619  O   PRO A  77      52.188  49.750  21.122  1.00 13.23           O  
ATOM    620  CB  PRO A  77      51.123  47.397  22.536  1.00  7.62           C  
ATOM    621  CG  PRO A  77      51.536  48.243  23.691  1.00  6.56           C  
ATOM    622  CD  PRO A  77      52.999  47.902  23.909  1.00 12.53           C  
ATOM    623  N   THR A  78      52.479  48.374  19.379  1.00  9.10           N  
ATOM    624  CA  THR A  78      52.376  49.472  18.429  1.00 16.49           C  
ATOM    625  C   THR A  78      50.946  49.423  17.915  1.00 23.41           C  
ATOM    626  O   THR A  78      50.039  49.301  18.727  1.00 35.17           O  
ATOM    627  CB  THR A  78      53.415  49.416  17.301  1.00 17.34           C  
ATOM    628  OG1 THR A  78      53.819  48.063  17.069  1.00 19.54           O  
ATOM    629  CG2 THR A  78      54.630  50.259  17.670  1.00 16.65           C  
ATOM    630  N   ALA A  79      50.709  49.495  16.611  1.00 20.13           N  
ATOM    631  CA  ALA A  79      49.332  49.448  16.123  1.00 16.96           C  
ATOM    632  C   ALA A  79      49.287  49.407  14.616  1.00 20.90           C  
ATOM    633  O   ALA A  79      50.075  50.087  13.948  1.00 24.33           O  
ATOM    634  CB  ALA A  79      48.534  50.648  16.633  1.00 15.76           C  
ATOM    635  N   MET A  80      48.388  48.585  14.081  1.00 14.06           N  
ATOM    636  CA  MET A  80      48.237  48.465  12.637  1.00 20.46           C  
ATOM    637  C   MET A  80      49.579  48.126  11.972  1.00 19.32           C  
ATOM    638  O   MET A  80      49.983  48.750  10.995  1.00 24.29           O  
ATOM    639  CB  MET A  80      47.663  49.777  12.072  1.00 22.14           C  
ATOM    640  CG  MET A  80      46.258  50.122  12.581  1.00 26.41           C  
ATOM    641  SD  MET A  80      46.005  51.886  12.912  1.00 25.91           S  
ATOM    642  CE  MET A  80      46.022  52.542  11.297  1.00 26.86           C  
ATOM    643  N   GLN A  81      50.256  47.118  12.502  1.00 18.97           N  
ATOM    644  CA  GLN A  81      51.547  46.700  11.970  1.00 19.50           C  
ATOM    645  C   GLN A  81      51.520  46.259  10.516  1.00 18.93           C  
ATOM    646  O   GLN A  81      52.542  46.311   9.834  1.00 22.26           O  
ATOM    647  CB  GLN A  81      52.155  45.597  12.837  1.00 16.29           C  
ATOM    648  CG  GLN A  81      52.725  46.099  14.151  1.00 16.53           C  
ATOM    649  CD  GLN A  81      53.249  44.983  15.023  1.00 16.74           C  
ATOM    650  OE1 GLN A  81      53.306  43.833  14.601  1.00 25.76           O  
ATOM    651  NE2 GLN A  81      53.616  45.309  16.255  1.00 14.85           N  
ATOM    652  N   LYS A  82      50.364  45.817  10.034  1.00 19.71           N  
ATOM    653  CA  LYS A  82      50.269  45.379   8.648  1.00 16.58           C  
ATOM    654  C   LYS A  82      50.450  46.504   7.638  1.00 17.26           C  
ATOM    655  O   LYS A  82      50.519  46.249   6.435  1.00 17.60           O  
ATOM    656  CB  LYS A  82      48.983  44.594   8.390  1.00 17.14           C  
ATOM    657  CG  LYS A  82      49.023  43.184   8.959  1.00 21.55           C  
ATOM    658  CD  LYS A  82      47.951  42.299   8.363  1.00 23.81           C  
ATOM    659  CE  LYS A  82      48.116  40.867   8.836  1.00 30.03           C  
ATOM    660  NZ  LYS A  82      47.094  39.954   8.253  1.00 30.82           N  
ATOM    661  N   MET A  83      50.504  47.748   8.116  1.00 13.61           N  
ATOM    662  CA  MET A  83      50.731  48.882   7.228  1.00 13.70           C  
ATOM    663  C   MET A  83      52.214  48.899   6.851  1.00 15.42           C  
ATOM    664  O   MET A  83      52.604  49.482   5.835  1.00 11.64           O  
ATOM    665  CB  MET A  83      50.417  50.206   7.919  1.00 13.65           C  
ATOM    666  CG  MET A  83      48.963  50.504   8.104  1.00 16.38           C  
ATOM    667  SD  MET A  83      48.737  52.222   8.560  1.00 22.26           S  
ATOM    668  CE  MET A  83      49.619  52.274  10.111  1.00 15.95           C  
ATOM    669  N   ALA A  84      53.035  48.298   7.708  1.00  9.93           N  
ATOM    670  CA  ALA A  84      54.476  48.247   7.500  1.00 11.37           C  
ATOM    671  C   ALA A  84      54.933  47.055   6.661  1.00 14.06           C  
ATOM    672  O   ALA A  84      55.940  47.131   5.952  1.00 16.69           O  
ATOM    673  CB  ALA A  84      55.193  48.240   8.850  1.00  7.79           C  
ATOM    674  N   HIS A  85      54.185  45.961   6.727  1.00 15.18           N  
ATOM    675  CA  HIS A  85      54.543  44.750   6.001  1.00 13.23           C  
ATOM    676  C   HIS A  85      53.330  43.841   6.012  1.00 14.99           C  
ATOM    677  O   HIS A  85      52.685  43.696   7.045  1.00 16.82           O  
ATOM    678  CB  HIS A  85      55.709  44.062   6.719  1.00 15.84           C  
ATOM    679  CG  HIS A  85      56.238  42.858   6.010  1.00 18.64           C  
ATOM    680  ND1 HIS A  85      57.290  42.922   5.122  1.00 19.25           N  
ATOM    681  CD2 HIS A  85      55.854  41.561   6.048  1.00 15.68           C  
ATOM    682  CE1 HIS A  85      57.531  41.715   4.645  1.00 18.37           C  
ATOM    683  NE2 HIS A  85      56.673  40.873   5.188  1.00 18.53           N  
ATOM    684  N   PRO A  86      53.041  43.170   4.884  1.00 16.40           N  
ATOM    685  CA  PRO A  86      51.889  42.267   4.785  1.00 18.71           C  
ATOM    686  C   PRO A  86      51.686  41.343   5.988  1.00 18.94           C  
ATOM    687  O   PRO A  86      50.551  41.097   6.402  1.00 21.13           O  
ATOM    688  CB  PRO A  86      52.195  41.468   3.519  1.00 16.03           C  
ATOM    689  CG  PRO A  86      52.879  42.455   2.659  1.00 13.68           C  
ATOM    690  CD  PRO A  86      53.799  43.192   3.619  1.00 18.38           C  
ATOM    691  N   GLU A  87      52.783  40.823   6.534  1.00 18.23           N  
ATOM    692  CA  GLU A  87      52.720  39.917   7.681  1.00 19.18           C  
ATOM    693  C   GLU A  87      52.466  40.598   9.021  1.00 13.03           C  
ATOM    694  O   GLU A  87      51.997  39.962   9.957  1.00 18.53           O  
ATOM    695  CB  GLU A  87      53.976  39.040   7.746  1.00 26.35           C  
ATOM    696  CG  GLU A  87      54.025  37.961   6.661  1.00 35.42           C  
ATOM    697  CD  GLU A  87      55.412  37.366   6.486  1.00 45.67           C  
ATOM    698  OE1 GLU A  87      55.889  36.655   7.398  1.00 50.00           O  
ATOM    699  OE2 GLU A  87      56.033  37.610   5.429  1.00 50.82           O  
ATOM    700  N   GLY A  88      52.806  41.878   9.114  1.00  6.75           N  
ATOM    701  CA  GLY A  88      52.595  42.638  10.334  1.00  8.72           C  
ATOM    702  C   GLY A  88      52.833  41.943  11.663  1.00 10.79           C  
ATOM    703  O   GLY A  88      53.941  41.477  11.951  1.00 13.92           O  
ATOM    704  N   GLU A  89      51.772  41.837  12.458  1.00 10.73           N  
ATOM    705  CA  GLU A  89      51.842  41.216  13.773  1.00 12.84           C  
ATOM    706  C   GLU A  89      52.362  39.780  13.761  1.00 19.63           C  
ATOM    707  O   GLU A  89      52.932  39.322  14.745  1.00 22.06           O  
ATOM    708  CB  GLU A  89      50.483  41.264  14.472  1.00 14.93           C  
ATOM    709  CG  GLU A  89      50.024  42.649  14.923  1.00 13.43           C  
ATOM    710  CD  GLU A  89      49.392  43.479  13.813  1.00 13.87           C  
ATOM    711  OE1 GLU A  89      49.069  42.934  12.738  1.00 13.11           O  
ATOM    712  OE2 GLU A  89      49.211  44.693  14.027  1.00 17.46           O  
ATOM    713  N   TYR A  90      52.150  39.067  12.658  1.00 23.32           N  
ATOM    714  CA  TYR A  90      52.611  37.689  12.534  1.00 24.43           C  
ATOM    715  C   TYR A  90      54.131  37.628  12.636  1.00 23.68           C  
ATOM    716  O   TYR A  90      54.684  36.871  13.438  1.00 23.06           O  
ATOM    717  CB  TYR A  90      52.200  37.111  11.183  1.00 27.00           C  
ATOM    718  CG  TYR A  90      50.781  36.623  11.094  1.00 30.27           C  
ATOM    719  CD1 TYR A  90      49.723  37.512  10.915  1.00 33.72           C  
ATOM    720  CD2 TYR A  90      50.500  35.260  11.126  1.00 34.27           C  
ATOM    721  CE1 TYR A  90      48.416  37.050  10.763  1.00 34.96           C  
ATOM    722  CE2 TYR A  90      49.203  34.786  10.974  1.00 36.32           C  
ATOM    723  CZ  TYR A  90      48.166  35.683  10.790  1.00 38.05           C  
ATOM    724  OH  TYR A  90      46.888  35.204  10.607  1.00 41.62           O  
ATOM    725  N   ALA A  91      54.796  38.421  11.802  1.00 19.56           N  
ATOM    726  CA  ALA A  91      56.251  38.455  11.774  1.00 13.35           C  
ATOM    727  C   ALA A  91      56.774  38.841  13.140  1.00 11.97           C  
ATOM    728  O   ALA A  91      57.677  38.207  13.671  1.00 16.97           O  
ATOM    729  CB  ALA A  91      56.734  39.442  10.728  1.00  7.81           C  
ATOM    730  N   THR A  92      56.166  39.860  13.726  1.00 13.17           N  
ATOM    731  CA  THR A  92      56.589  40.330  15.032  1.00 13.43           C  
ATOM    732  C   THR A  92      56.390  39.239  16.093  1.00 10.91           C  
ATOM    733  O   THR A  92      57.246  39.042  16.963  1.00 17.09           O  
ATOM    734  CB  THR A  92      55.842  41.633  15.413  1.00  9.84           C  
ATOM    735  OG1 THR A  92      55.889  42.544  14.307  1.00 11.81           O  
ATOM    736  CG2 THR A  92      56.500  42.306  16.602  1.00 10.66           C  
ATOM    737  N   ALA A  93      55.293  38.495  15.983  1.00  8.46           N  
ATOM    738  CA  ALA A  93      54.980  37.422  16.928  1.00  5.98           C  
ATOM    739  C   ALA A  93      56.020  36.298  16.889  1.00  5.70           C  
ATOM    740  O   ALA A  93      56.548  35.890  17.921  1.00  3.14           O  
ATOM    741  CB  ALA A  93      53.582  36.869  16.660  1.00  2.00           C  
ATOM    742  N   ARG A  94      56.325  35.816  15.692  1.00  7.76           N  
ATOM    743  CA  ARG A  94      57.301  34.754  15.535  1.00 11.92           C  
ATOM    744  C   ARG A  94      58.690  35.213  15.982  1.00 17.56           C  
ATOM    745  O   ARG A  94      59.404  34.487  16.686  1.00 17.87           O  
ATOM    746  CB  ARG A  94      57.320  34.270  14.088  1.00 10.23           C  
ATOM    747  CG  ARG A  94      56.018  33.596  13.691  1.00 16.12           C  
ATOM    748  CD  ARG A  94      56.112  32.846  12.374  1.00 14.80           C  
ATOM    749  NE  ARG A  94      56.194  33.749  11.236  1.00 20.44           N  
ATOM    750  CZ  ARG A  94      55.162  34.099  10.471  1.00 27.81           C  
ATOM    751  NH1 ARG A  94      53.945  33.616  10.709  1.00 24.15           N  
ATOM    752  NH2 ARG A  94      55.345  34.969   9.483  1.00 31.03           N  
ATOM    753  N   ALA A  95      59.040  36.446  15.630  1.00 15.68           N  
ATOM    754  CA  ALA A  95      60.335  37.012  15.988  1.00 11.87           C  
ATOM    755  C   ALA A  95      60.503  37.126  17.499  1.00  8.38           C  
ATOM    756  O   ALA A  95      61.574  36.847  18.034  1.00  4.46           O  
ATOM    757  CB  ALA A  95      60.508  38.376  15.323  1.00 10.17           C  
ATOM    758  N   ALA A  96      59.436  37.520  18.185  1.00  9.98           N  
ATOM    759  CA  ALA A  96      59.480  37.672  19.637  1.00  9.03           C  
ATOM    760  C   ALA A  96      59.689  36.319  20.308  1.00 13.45           C  
ATOM    761  O   ALA A  96      60.567  36.166  21.160  1.00 17.38           O  
ATOM    762  CB  ALA A  96      58.202  38.335  20.141  1.00  2.31           C  
ATOM    763  N   SER A  97      58.890  35.336  19.910  1.00 16.37           N  
ATOM    764  CA  SER A  97      59.000  33.994  20.465  1.00 18.57           C  
ATOM    765  C   SER A  97      60.383  33.410  20.234  1.00 15.99           C  
ATOM    766  O   SER A  97      60.988  32.880  21.160  1.00 21.09           O  
ATOM    767  CB  SER A  97      57.933  33.076  19.871  1.00 13.24           C  
ATOM    768  OG  SER A  97      56.678  33.340  20.461  1.00 23.42           O  
ATOM    769  N   ALA A  98      60.884  33.523  19.005  1.00 14.65           N  
ATOM    770  CA  ALA A  98      62.208  33.007  18.661  1.00 11.89           C  
ATOM    771  C   ALA A  98      63.295  33.692  19.505  1.00 15.50           C  
ATOM    772  O   ALA A  98      64.225  33.045  20.000  1.00 20.87           O  
ATOM    773  CB  ALA A  98      62.484  33.195  17.158  1.00  2.00           C  
ATOM    774  N   ALA A  99      63.152  34.999  19.698  1.00 12.74           N  
ATOM    775  CA  ALA A  99      64.109  35.755  20.491  1.00 10.98           C  
ATOM    776  C   ALA A  99      64.021  35.361  21.962  1.00 12.53           C  
ATOM    777  O   ALA A  99      64.873  35.745  22.763  1.00 17.92           O  
ATOM    778  CB  ALA A  99      63.856  37.243  20.333  1.00  9.21           C  
ATOM    779  N   GLY A 100      62.980  34.611  22.315  1.00  8.55           N  
ATOM    780  CA  GLY A 100      62.791  34.185  23.689  1.00  2.89           C  
ATOM    781  C   GLY A 100      62.266  35.288  24.589  1.00  8.83           C  
ATOM    782  O   GLY A 100      62.510  35.272  25.792  1.00 11.29           O  
ATOM    783  N   THR A 101      61.528  36.240  24.029  1.00 11.26           N  
ATOM    784  CA  THR A 101      61.015  37.336  24.843  1.00 15.93           C  
ATOM    785  C   THR A 101      59.499  37.572  24.699  1.00 18.19           C  
ATOM    786  O   THR A 101      58.818  36.876  23.944  1.00 15.64           O  
ATOM    787  CB  THR A 101      61.830  38.650  24.606  1.00 16.11           C  
ATOM    788  OG1 THR A 101      61.416  39.655  25.543  1.00 15.83           O  
ATOM    789  CG2 THR A 101      61.652  39.166  23.181  1.00 11.05           C  
ATOM    790  N   ILE A 102      58.991  38.541  25.455  1.00 15.27           N  
ATOM    791  CA  ILE A 102      57.575  38.894  25.480  1.00 16.56           C  
ATOM    792  C   ILE A 102      57.180  39.933  24.437  1.00 16.55           C  
ATOM    793  O   ILE A 102      57.948  40.843  24.126  1.00 19.43           O  
ATOM    794  CB  ILE A 102      57.197  39.461  26.862  1.00 16.89           C  
ATOM    795  CG1 ILE A 102      57.442  38.407  27.941  1.00 12.79           C  
ATOM    796  CG2 ILE A 102      55.751  39.930  26.875  1.00 14.60           C  
ATOM    797  CD1 ILE A 102      57.458  38.959  29.358  1.00 10.78           C  
ATOM    798  N   MET A 103      55.971  39.791  23.910  1.00 15.94           N  
ATOM    799  CA  MET A 103      55.443  40.718  22.928  1.00 13.69           C  
ATOM    800  C   MET A 103      54.087  41.201  23.410  1.00 14.06           C  
ATOM    801  O   MET A 103      53.239  40.391  23.787  1.00 17.15           O  
ATOM    802  CB  MET A 103      55.270  40.034  21.580  1.00 12.57           C  
ATOM    803  CG  MET A 103      54.707  40.948  20.522  1.00 11.73           C  
ATOM    804  SD  MET A 103      53.300  40.227  19.718  1.00 21.43           S  
ATOM    805  CE  MET A 103      53.470  40.866  18.017  1.00 14.05           C  
ATOM    806  N   THR A 104      53.907  42.517  23.473  1.00 11.98           N  
ATOM    807  CA  THR A 104      52.641  43.089  23.902  1.00  8.23           C  
ATOM    808  C   THR A 104      51.808  43.406  22.669  1.00 14.52           C  
ATOM    809  O   THR A 104      52.250  44.153  21.790  1.00 14.78           O  
ATOM    810  CB  THR A 104      52.841  44.373  24.699  1.00  5.70           C  
ATOM    811  OG1 THR A 104      53.837  44.169  25.711  1.00  3.19           O  
ATOM    812  CG2 THR A 104      51.528  44.784  25.348  1.00  5.15           C  
ATOM    813  N   LEU A 105      50.623  42.808  22.583  1.00 15.37           N  
ATOM    814  CA  LEU A 105      49.746  43.033  21.444  1.00 14.28           C  
ATOM    815  C   LEU A 105      48.805  44.193  21.702  1.00 11.38           C  
ATOM    816  O   LEU A 105      48.289  44.351  22.807  1.00  6.09           O  
ATOM    817  CB  LEU A 105      48.932  41.776  21.125  1.00 17.86           C  
ATOM    818  CG  LEU A 105      48.121  41.833  19.823  1.00 18.33           C  
ATOM    819  CD1 LEU A 105      49.053  41.999  18.633  1.00 19.49           C  
ATOM    820  CD2 LEU A 105      47.289  40.582  19.659  1.00 20.50           C  
ATOM    821  N   SER A 106      48.613  45.017  20.682  1.00 10.87           N  
ATOM    822  CA  SER A 106      47.721  46.161  20.759  1.00 12.55           C  
ATOM    823  C   SER A 106      46.297  45.739  20.386  1.00 17.17           C  
ATOM    824  O   SER A 106      46.096  44.880  19.515  1.00 14.40           O  
ATOM    825  CB  SER A 106      48.202  47.250  19.795  1.00 12.89           C  
ATOM    826  OG  SER A 106      47.249  48.297  19.653  1.00 13.99           O  
ATOM    827  N   SER A 107      45.312  46.374  21.014  1.00 22.17           N  
ATOM    828  CA  SER A 107      43.910  46.090  20.733  1.00 23.63           C  
ATOM    829  C   SER A 107      43.575  46.504  19.292  1.00 22.51           C  
ATOM    830  O   SER A 107      42.712  45.906  18.652  1.00 21.72           O  
ATOM    831  CB  SER A 107      43.015  46.825  21.740  1.00 26.99           C  
ATOM    832  OG  SER A 107      43.354  48.201  21.816  1.00 33.99           O  
ATOM    833  N   TRP A 108      44.301  47.504  18.787  1.00 24.88           N  
ATOM    834  CA  TRP A 108      44.151  48.045  17.423  1.00 23.62           C  
ATOM    835  C   TRP A 108      45.027  47.299  16.414  1.00 16.03           C  
ATOM    836  O   TRP A 108      45.427  47.871  15.399  1.00 17.74           O  
ATOM    837  CB  TRP A 108      44.587  49.517  17.394  1.00 28.71           C  
ATOM    838  CG  TRP A 108      43.537  50.534  17.078  1.00 33.47           C  
ATOM    839  CD1 TRP A 108      43.416  51.286  15.926  1.00 35.36           C  
ATOM    840  CD2 TRP A 108      42.520  51.014  17.964  1.00 33.33           C  
ATOM    841  NE1 TRP A 108      42.421  52.209  16.052  1.00 31.74           N  
ATOM    842  CE2 TRP A 108      41.852  52.081  17.282  1.00 33.68           C  
ATOM    843  CE3 TRP A 108      42.121  50.678  19.253  1.00 33.58           C  
ATOM    844  CZ2 TRP A 108      40.818  52.794  17.876  1.00 34.87           C  
ATOM    845  CZ3 TRP A 108      41.089  51.391  19.840  1.00 38.51           C  
ATOM    846  CH2 TRP A 108      40.444  52.437  19.139  1.00 40.14           C  
ATOM    847  N   ALA A 109      45.367  46.049  16.698  1.00 15.02           N  
ATOM    848  CA  ALA A 109      46.219  45.280  15.798  1.00 11.62           C  
ATOM    849  C   ALA A 109      45.475  44.870  14.539  1.00  9.11           C  
ATOM    850  O   ALA A 109      44.262  44.701  14.554  1.00 19.09           O  
ATOM    851  CB  ALA A 109      46.778  44.055  16.509  1.00 13.60           C  
ATOM    852  N   THR A 110      46.218  44.717  13.451  1.00  7.41           N  
ATOM    853  CA  THR A 110      45.660  44.314  12.164  1.00 13.45           C  
ATOM    854  C   THR A 110      45.623  42.780  12.064  1.00 15.01           C  
ATOM    855  O   THR A 110      45.558  42.208  10.968  1.00 11.54           O  
ATOM    856  CB  THR A 110      46.461  44.938  10.982  1.00 14.84           C  
ATOM    857  OG1 THR A 110      47.812  45.189  11.393  1.00 17.39           O  
ATOM    858  CG2 THR A 110      45.844  46.262  10.551  1.00 15.94           C  
ATOM    859  N   SER A 111      45.685  42.143  13.234  1.00 12.74           N  
ATOM    860  CA  SER A 111      45.646  40.690  13.407  1.00 14.41           C  
ATOM    861  C   SER A 111      44.987  40.492  14.773  1.00 20.97           C  
ATOM    862  O   SER A 111      45.123  41.348  15.657  1.00 26.04           O  
ATOM    863  CB  SER A 111      47.058  40.090  13.438  1.00 15.72           C  
ATOM    864  OG  SER A 111      47.764  40.325  12.231  1.00 17.28           O  
ATOM    865  N   SER A 112      44.257  39.396  14.947  1.00 18.32           N  
ATOM    866  CA  SER A 112      43.574  39.135  16.204  1.00 18.24           C  
ATOM    867  C   SER A 112      44.428  38.352  17.183  1.00 16.54           C  
ATOM    868  O   SER A 112      45.386  37.685  16.783  1.00 19.26           O  
ATOM    869  CB  SER A 112      42.278  38.380  15.935  1.00 23.50           C  
ATOM    870  OG  SER A 112      42.527  37.210  15.173  1.00 22.62           O  
ATOM    871  N   VAL A 113      44.058  38.399  18.457  1.00 12.35           N  
ATOM    872  CA  VAL A 113      44.788  37.677  19.487  1.00 17.54           C  
ATOM    873  C   VAL A 113      44.977  36.217  19.084  1.00 24.22           C  
ATOM    874  O   VAL A 113      46.090  35.693  19.134  1.00 28.70           O  
ATOM    875  CB  VAL A 113      44.073  37.741  20.848  1.00 16.27           C  
ATOM    876  CG1 VAL A 113      44.227  39.116  21.460  1.00 20.11           C  
ATOM    877  CG2 VAL A 113      42.610  37.420  20.689  1.00 19.02           C  
ATOM    878  N   GLU A 114      43.906  35.578  18.621  1.00 27.91           N  
ATOM    879  CA  GLU A 114      43.987  34.182  18.208  1.00 29.79           C  
ATOM    880  C   GLU A 114      44.846  33.985  16.961  1.00 27.52           C  
ATOM    881  O   GLU A 114      45.513  32.959  16.830  1.00 30.71           O  
ATOM    882  CB  GLU A 114      42.599  33.541  18.051  1.00 28.19           C  
ATOM    883  CG  GLU A 114      41.536  34.404  17.397  1.00 32.72           C  
ATOM    884  CD  GLU A 114      40.826  35.321  18.383  1.00 31.16           C  
ATOM    885  OE1 GLU A 114      40.323  34.836  19.418  1.00 29.49           O  
ATOM    886  OE2 GLU A 114      40.771  36.533  18.116  1.00 33.63           O  
ATOM    887  N   GLU A 115      44.861  34.975  16.072  1.00 24.07           N  
ATOM    888  CA  GLU A 115      45.685  34.890  14.868  1.00 27.60           C  
ATOM    889  C   GLU A 115      47.151  34.859  15.305  1.00 30.07           C  
ATOM    890  O   GLU A 115      47.941  34.056  14.817  1.00 29.75           O  
ATOM    891  CB  GLU A 115      45.466  36.100  13.959  1.00 26.39           C  
ATOM    892  CG  GLU A 115      44.276  35.999  13.035  1.00 29.40           C  
ATOM    893  CD  GLU A 115      44.268  37.099  11.977  1.00 33.04           C  
ATOM    894  OE1 GLU A 115      43.777  38.211  12.260  1.00 34.13           O  
ATOM    895  OE2 GLU A 115      44.752  36.853  10.854  1.00 31.12           O  
ATOM    896  N   VAL A 116      47.497  35.737  16.241  1.00 28.95           N  
ATOM    897  CA  VAL A 116      48.855  35.821  16.763  1.00 26.22           C  
ATOM    898  C   VAL A 116      49.225  34.534  17.501  1.00 28.22           C  
ATOM    899  O   VAL A 116      50.302  33.973  17.282  1.00 25.22           O  
ATOM    900  CB  VAL A 116      49.006  37.046  17.710  1.00 23.03           C  
ATOM    901  CG1 VAL A 116      50.296  36.963  18.502  1.00 20.35           C  
ATOM    902  CG2 VAL A 116      48.990  38.328  16.904  1.00 23.89           C  
ATOM    903  N   ALA A 117      48.311  34.055  18.343  1.00 28.43           N  
ATOM    904  CA  ALA A 117      48.522  32.839  19.131  1.00 29.29           C  
ATOM    905  C   ALA A 117      48.864  31.606  18.301  1.00 29.59           C  
ATOM    906  O   ALA A 117      49.599  30.727  18.760  1.00 32.86           O  
ATOM    907  CB  ALA A 117      47.305  32.561  19.994  1.00 28.87           C  
ATOM    908  N   SER A 118      48.349  31.545  17.079  1.00 28.32           N  
ATOM    909  CA  SER A 118      48.607  30.405  16.210  1.00 28.55           C  
ATOM    910  C   SER A 118      50.035  30.334  15.675  1.00 28.55           C  
ATOM    911  O   SER A 118      50.516  29.254  15.335  1.00 34.90           O  
ATOM    912  CB  SER A 118      47.613  30.378  15.048  1.00 30.85           C  
ATOM    913  OG  SER A 118      47.673  31.578  14.299  1.00 32.78           O  
ATOM    914  N   THR A 119      50.720  31.469  15.605  1.00 23.13           N  
ATOM    915  CA  THR A 119      52.092  31.474  15.105  1.00 20.50           C  
ATOM    916  C   THR A 119      52.953  30.446  15.846  1.00 17.81           C  
ATOM    917  O   THR A 119      53.776  29.757  15.239  1.00 17.02           O  
ATOM    918  CB  THR A 119      52.739  32.860  15.224  1.00 14.31           C  
ATOM    919  OG1 THR A 119      52.838  33.231  16.604  1.00 18.81           O  
ATOM    920  CG2 THR A 119      51.918  33.892  14.487  1.00 16.47           C  
ATOM    921  N   GLY A 120      52.736  30.331  17.148  1.00 13.03           N  
ATOM    922  CA  GLY A 120      53.493  29.387  17.943  1.00 16.89           C  
ATOM    923  C   GLY A 120      53.443  29.771  19.402  1.00 21.76           C  
ATOM    924  O   GLY A 120      52.821  30.770  19.753  1.00 27.92           O  
ATOM    925  N   PRO A 121      54.040  28.981  20.290  1.00 25.52           N  
ATOM    926  CA  PRO A 121      54.020  29.322  21.713  1.00 26.33           C  
ATOM    927  C   PRO A 121      54.931  30.496  22.048  1.00 25.91           C  
ATOM    928  O   PRO A 121      55.966  30.686  21.404  1.00 31.54           O  
ATOM    929  CB  PRO A 121      54.506  28.036  22.386  1.00 24.25           C  
ATOM    930  CG  PRO A 121      55.411  27.429  21.356  1.00 25.26           C  
ATOM    931  CD  PRO A 121      54.660  27.656  20.067  1.00 26.04           C  
ATOM    932  N   GLY A 122      54.540  31.269  23.056  1.00 26.48           N  
ATOM    933  CA  GLY A 122      55.318  32.414  23.496  1.00 23.19           C  
ATOM    934  C   GLY A 122      54.564  33.190  24.559  1.00 20.23           C  
ATOM    935  O   GLY A 122      53.336  33.155  24.591  1.00 26.71           O  
ATOM    936  N   ILE A 123      55.283  33.881  25.435  1.00 17.16           N  
ATOM    937  CA  ILE A 123      54.650  34.669  26.487  1.00 20.43           C  
ATOM    938  C   ILE A 123      54.218  35.993  25.871  1.00 18.11           C  
ATOM    939  O   ILE A 123      55.036  36.723  25.320  1.00 21.92           O  
ATOM    940  CB  ILE A 123      55.615  34.907  27.667  1.00 23.65           C  
ATOM    941  CG1 ILE A 123      56.064  33.556  28.227  1.00 23.09           C  
ATOM    942  CG2 ILE A 123      54.925  35.702  28.775  1.00 15.89           C  
ATOM    943  CD1 ILE A 123      57.250  33.643  29.148  1.00 30.90           C  
ATOM    944  N   ARG A 124      52.928  36.290  25.947  1.00 15.49           N  
ATOM    945  CA  ARG A 124      52.399  37.507  25.364  1.00 12.85           C  
ATOM    946  C   ARG A 124      51.514  38.295  26.322  1.00 15.31           C  
ATOM    947  O   ARG A 124      50.866  37.719  27.193  1.00 15.31           O  
ATOM    948  CB  ARG A 124      51.611  37.170  24.102  1.00 11.48           C  
ATOM    949  CG  ARG A 124      52.439  36.526  23.026  1.00 14.69           C  
ATOM    950  CD  ARG A 124      51.595  36.149  21.833  1.00 18.91           C  
ATOM    951  NE  ARG A 124      52.393  35.474  20.814  1.00 27.08           N  
ATOM    952  CZ  ARG A 124      52.458  34.155  20.657  1.00 26.81           C  
ATOM    953  NH1 ARG A 124      51.767  33.353  21.452  1.00 28.81           N  
ATOM    954  NH2 ARG A 124      53.229  33.638  19.710  1.00 27.34           N  
ATOM    955  N   PHE A 125      51.519  39.618  26.161  1.00 18.81           N  
ATOM    956  CA  PHE A 125      50.710  40.524  26.978  1.00 17.43           C  
ATOM    957  C   PHE A 125      49.720  41.209  26.040  1.00 17.68           C  
ATOM    958  O   PHE A 125      49.988  41.343  24.840  1.00 13.40           O  
ATOM    959  CB  PHE A 125      51.573  41.601  27.647  1.00 15.61           C  
ATOM    960  CG  PHE A 125      52.479  41.091  28.733  1.00 21.84           C  
ATOM    961  CD1 PHE A 125      52.378  39.784  29.204  1.00 20.81           C  
ATOM    962  CD2 PHE A 125      53.442  41.930  29.290  1.00 20.76           C  
ATOM    963  CE1 PHE A 125      53.220  39.320  30.207  1.00 21.14           C  
ATOM    964  CE2 PHE A 125      54.288  41.475  30.293  1.00 21.50           C  
ATOM    965  CZ  PHE A 125      54.173  40.166  30.755  1.00 21.87           C  
ATOM    966  N   PHE A 126      48.583  41.635  26.577  1.00 15.01           N  
ATOM    967  CA  PHE A 126      47.572  42.304  25.769  1.00 16.30           C  
ATOM    968  C   PHE A 126      47.373  43.720  26.277  1.00 16.54           C  
ATOM    969  O   PHE A 126      47.150  43.927  27.473  1.00 15.03           O  
ATOM    970  CB  PHE A 126      46.242  41.548  25.830  1.00 14.79           C  
ATOM    971  CG  PHE A 126      45.185  42.104  24.915  1.00 13.43           C  
ATOM    972  CD1 PHE A 126      45.385  42.134  23.530  1.00 14.58           C  
ATOM    973  CD2 PHE A 126      43.981  42.575  25.425  1.00 13.87           C  
ATOM    974  CE1 PHE A 126      44.395  42.622  22.661  1.00  7.90           C  
ATOM    975  CE2 PHE A 126      42.985  43.065  24.567  1.00 14.65           C  
ATOM    976  CZ  PHE A 126      43.197  43.085  23.178  1.00  5.34           C  
ATOM    977  N   GLN A 127      47.470  44.684  25.367  1.00 11.93           N  
ATOM    978  CA  GLN A 127      47.296  46.090  25.699  1.00 12.31           C  
ATOM    979  C   GLN A 127      45.849  46.447  25.405  1.00 13.99           C  
ATOM    980  O   GLN A 127      45.313  46.112  24.338  1.00 16.72           O  
ATOM    981  CB  GLN A 127      48.246  46.953  24.869  1.00 11.96           C  
ATOM    982  CG  GLN A 127      48.274  48.411  25.262  1.00  8.23           C  
ATOM    983  CD  GLN A 127      47.205  49.211  24.572  1.00 13.00           C  
ATOM    984  OE1 GLN A 127      47.032  49.120  23.357  1.00 18.30           O  
ATOM    985  NE2 GLN A 127      46.472  50.003  25.338  1.00 17.03           N  
ATOM    986  N   LEU A 128      45.245  47.223  26.289  1.00 14.31           N  
ATOM    987  CA  LEU A 128      43.850  47.555  26.121  1.00 15.63           C  
ATOM    988  C   LEU A 128      43.479  48.904  26.768  1.00 18.04           C  
ATOM    989  O   LEU A 128      44.254  49.463  27.554  1.00 14.30           O  
ATOM    990  CB  LEU A 128      43.065  46.344  26.667  1.00 19.52           C  
ATOM    991  CG  LEU A 128      41.665  46.192  27.248  1.00 21.02           C  
ATOM    992  CD1 LEU A 128      41.657  46.757  28.662  1.00 23.05           C  
ATOM    993  CD2 LEU A 128      40.623  46.833  26.334  1.00 26.80           C  
ATOM    994  N   TYR A 129      42.366  49.485  26.319  1.00 18.19           N  
ATOM    995  CA  TYR A 129      41.858  50.754  26.850  1.00 13.47           C  
ATOM    996  C   TYR A 129      40.440  50.471  27.328  1.00 13.13           C  
ATOM    997  O   TYR A 129      39.681  49.801  26.632  1.00 18.35           O  
ATOM    998  CB  TYR A 129      41.759  51.828  25.758  1.00 10.48           C  
ATOM    999  CG  TYR A 129      43.055  52.407  25.244  1.00 11.55           C  
ATOM   1000  CD1 TYR A 129      43.791  53.318  26.004  1.00 17.20           C  
ATOM   1001  CD2 TYR A 129      43.530  52.070  23.979  1.00 11.83           C  
ATOM   1002  CE1 TYR A 129      44.976  53.877  25.513  1.00 16.74           C  
ATOM   1003  CE2 TYR A 129      44.705  52.621  23.479  1.00 13.07           C  
ATOM   1004  CZ  TYR A 129      45.426  53.517  24.249  1.00 13.78           C  
ATOM   1005  OH  TYR A 129      46.616  54.011  23.767  1.00 10.79           O  
ATOM   1006  N   VAL A 130      40.069  50.959  28.502  1.00 11.34           N  
ATOM   1007  CA  VAL A 130      38.711  50.740  28.990  1.00 12.56           C  
ATOM   1008  C   VAL A 130      37.753  51.611  28.159  1.00 14.97           C  
ATOM   1009  O   VAL A 130      37.646  52.821  28.382  1.00 16.66           O  
ATOM   1010  CB  VAL A 130      38.597  51.082  30.492  1.00 10.28           C  
ATOM   1011  CG1 VAL A 130      37.181  50.857  30.981  1.00 10.93           C  
ATOM   1012  CG2 VAL A 130      39.575  50.236  31.292  1.00  9.32           C  
ATOM   1013  N   TYR A 131      37.130  51.011  27.151  1.00 13.25           N  
ATOM   1014  CA  TYR A 131      36.203  51.734  26.288  1.00 18.18           C  
ATOM   1015  C   TYR A 131      34.862  51.991  26.968  1.00 21.43           C  
ATOM   1016  O   TYR A 131      34.550  51.380  27.992  1.00 24.77           O  
ATOM   1017  CB  TYR A 131      35.975  50.967  24.988  1.00 18.43           C  
ATOM   1018  CG  TYR A 131      37.244  50.668  24.227  1.00 24.82           C  
ATOM   1019  CD1 TYR A 131      37.881  51.653  23.473  1.00 24.42           C  
ATOM   1020  CD2 TYR A 131      37.832  49.402  24.288  1.00 27.28           C  
ATOM   1021  CE1 TYR A 131      39.073  51.387  22.802  1.00 20.38           C  
ATOM   1022  CE2 TYR A 131      39.023  49.131  23.621  1.00 22.18           C  
ATOM   1023  CZ  TYR A 131      39.636  50.126  22.885  1.00 19.59           C  
ATOM   1024  OH  TYR A 131      40.823  49.850  22.248  1.00 23.47           O  
ATOM   1025  N   LYS A 132      34.073  52.895  26.389  1.00 20.80           N  
ATOM   1026  CA  LYS A 132      32.759  53.238  26.923  1.00 23.70           C  
ATOM   1027  C   LYS A 132      31.923  51.974  27.063  1.00 24.42           C  
ATOM   1028  O   LYS A 132      31.268  51.753  28.083  1.00 25.36           O  
ATOM   1029  CB  LYS A 132      32.038  54.208  25.987  1.00 28.07           C  
ATOM   1030  CG  LYS A 132      32.669  55.574  25.884  1.00 35.20           C  
ATOM   1031  CD  LYS A 132      31.914  56.429  24.885  1.00 43.44           C  
ATOM   1032  CE  LYS A 132      32.646  57.735  24.609  1.00 48.04           C  
ATOM   1033  NZ  LYS A 132      31.949  58.562  23.582  1.00 50.97           N  
ATOM   1034  N   ASP A 133      31.932  51.157  26.016  1.00 23.55           N  
ATOM   1035  CA  ASP A 133      31.191  49.909  26.028  1.00 23.04           C  
ATOM   1036  C   ASP A 133      32.002  48.899  26.843  1.00 20.65           C  
ATOM   1037  O   ASP A 133      32.810  48.144  26.297  1.00 23.58           O  
ATOM   1038  CB  ASP A 133      30.979  49.412  24.592  1.00 24.41           C  
ATOM   1039  CG  ASP A 133      29.889  48.349  24.486  1.00 26.93           C  
ATOM   1040  OD1 ASP A 133      29.561  47.685  25.493  1.00 24.86           O  
ATOM   1041  OD2 ASP A 133      29.359  48.175  23.369  1.00 28.03           O  
ATOM   1042  N   ARG A 134      31.790  48.903  28.153  1.00 19.93           N  
ATOM   1043  CA  ARG A 134      32.480  47.994  29.059  1.00 18.41           C  
ATOM   1044  C   ARG A 134      32.290  46.542  28.628  1.00 18.19           C  
ATOM   1045  O   ARG A 134      33.123  45.677  28.907  1.00 17.84           O  
ATOM   1046  CB  ARG A 134      31.951  48.173  30.479  1.00 21.21           C  
ATOM   1047  CG  ARG A 134      32.213  49.540  31.075  1.00 25.43           C  
ATOM   1048  CD  ARG A 134      33.687  49.728  31.399  1.00 24.51           C  
ATOM   1049  NE  ARG A 134      33.895  50.875  32.281  1.00 23.52           N  
ATOM   1050  CZ  ARG A 134      34.089  52.117  31.855  1.00 20.76           C  
ATOM   1051  NH1 ARG A 134      34.113  52.377  30.556  1.00 21.41           N  
ATOM   1052  NH2 ARG A 134      34.230  53.105  32.729  1.00 19.58           N  
ATOM   1053  N   ASN A 135      31.178  46.277  27.957  1.00 17.07           N  
ATOM   1054  CA  ASN A 135      30.884  44.931  27.485  1.00 21.95           C  
ATOM   1055  C   ASN A 135      31.899  44.501  26.428  1.00 17.48           C  
ATOM   1056  O   ASN A 135      32.287  43.333  26.366  1.00 15.35           O  
ATOM   1057  CB  ASN A 135      29.451  44.859  26.944  1.00 26.80           C  
ATOM   1058  CG  ASN A 135      29.159  43.547  26.238  1.00 31.24           C  
ATOM   1059  OD1 ASN A 135      28.995  43.516  25.017  1.00 31.66           O  
ATOM   1060  ND2 ASN A 135      29.117  42.456  26.994  1.00 31.57           N  
ATOM   1061  N   VAL A 136      32.331  45.448  25.602  1.00 17.91           N  
ATOM   1062  CA  VAL A 136      33.326  45.166  24.570  1.00 19.27           C  
ATOM   1063  C   VAL A 136      34.663  44.878  25.253  1.00 17.80           C  
ATOM   1064  O   VAL A 136      35.426  44.030  24.791  1.00 18.49           O  
ATOM   1065  CB  VAL A 136      33.506  46.355  23.596  1.00 19.28           C  
ATOM   1066  CG1 VAL A 136      34.635  46.071  22.613  1.00 17.26           C  
ATOM   1067  CG2 VAL A 136      32.225  46.604  22.836  1.00 20.48           C  
ATOM   1068  N   VAL A 137      34.932  45.568  26.360  1.00 12.12           N  
ATOM   1069  CA  VAL A 137      36.174  45.368  27.100  1.00 16.73           C  
ATOM   1070  C   VAL A 137      36.203  43.960  27.687  1.00 16.95           C  
ATOM   1071  O   VAL A 137      37.213  43.263  27.595  1.00 23.42           O  
ATOM   1072  CB  VAL A 137      36.337  46.397  28.249  1.00 16.97           C  
ATOM   1073  CG1 VAL A 137      37.662  46.180  28.968  1.00 13.62           C  
ATOM   1074  CG2 VAL A 137      36.268  47.812  27.705  1.00 18.79           C  
ATOM   1075  N   ALA A 138      35.085  43.545  28.276  1.00 15.81           N  
ATOM   1076  CA  ALA A 138      34.963  42.219  28.875  1.00 11.56           C  
ATOM   1077  C   ALA A 138      35.237  41.164  27.822  1.00 10.11           C  
ATOM   1078  O   ALA A 138      36.004  40.225  28.048  1.00 14.02           O  
ATOM   1079  CB  ALA A 138      33.561  42.023  29.466  1.00  7.89           C  
ATOM   1080  N   GLN A 139      34.626  41.338  26.656  1.00 11.76           N  
ATOM   1081  CA  GLN A 139      34.804  40.405  25.558  1.00 17.52           C  
ATOM   1082  C   GLN A 139      36.266  40.319  25.137  1.00 14.93           C  
ATOM   1083  O   GLN A 139      36.795  39.221  24.985  1.00 23.10           O  
ATOM   1084  CB  GLN A 139      33.909  40.785  24.380  1.00 20.15           C  
ATOM   1085  CG  GLN A 139      32.433  40.541  24.643  1.00 25.54           C  
ATOM   1086  CD  GLN A 139      31.537  41.157  23.587  1.00 34.53           C  
ATOM   1087  OE1 GLN A 139      31.089  40.479  22.659  1.00 37.58           O  
ATOM   1088  NE2 GLN A 139      31.268  42.451  23.722  1.00 39.79           N  
ATOM   1089  N   LEU A 140      36.927  41.465  24.988  1.00 11.76           N  
ATOM   1090  CA  LEU A 140      38.340  41.495  24.599  1.00  9.82           C  
ATOM   1091  C   LEU A 140      39.225  40.750  25.596  1.00 12.41           C  
ATOM   1092  O   LEU A 140      40.127  40.005  25.201  1.00  2.72           O  
ATOM   1093  CB  LEU A 140      38.840  42.932  24.469  1.00  7.36           C  
ATOM   1094  CG  LEU A 140      38.337  43.727  23.270  1.00  7.62           C  
ATOM   1095  CD1 LEU A 140      38.821  45.165  23.405  1.00 11.10           C  
ATOM   1096  CD2 LEU A 140      38.828  43.085  21.973  1.00  3.01           C  
ATOM   1097  N   VAL A 141      38.977  40.973  26.885  1.00 11.82           N  
ATOM   1098  CA  VAL A 141      39.738  40.322  27.943  1.00 14.02           C  
ATOM   1099  C   VAL A 141      39.546  38.806  27.876  1.00 18.94           C  
ATOM   1100  O   VAL A 141      40.518  38.047  27.825  1.00 21.41           O  
ATOM   1101  CB  VAL A 141      39.308  40.841  29.333  1.00 15.62           C  
ATOM   1102  CG1 VAL A 141      39.931  39.999  30.442  1.00 14.65           C  
ATOM   1103  CG2 VAL A 141      39.711  42.302  29.488  1.00  9.96           C  
ATOM   1104  N   ARG A 142      38.289  38.377  27.844  1.00 18.00           N  
ATOM   1105  CA  ARG A 142      37.947  36.959  27.777  1.00 14.33           C  
ATOM   1106  C   ARG A 142      38.602  36.302  26.561  1.00 15.46           C  
ATOM   1107  O   ARG A 142      39.098  35.173  26.624  1.00 14.71           O  
ATOM   1108  CB  ARG A 142      36.433  36.810  27.667  1.00 13.70           C  
ATOM   1109  CG  ARG A 142      35.884  35.602  28.376  1.00 17.09           C  
ATOM   1110  CD  ARG A 142      35.593  35.902  29.836  1.00 19.78           C  
ATOM   1111  NE  ARG A 142      36.776  35.961  30.692  1.00 19.91           N  
ATOM   1112  CZ  ARG A 142      37.098  37.006  31.449  1.00 23.50           C  
ATOM   1113  NH1 ARG A 142      36.337  38.093  31.445  1.00 25.19           N  
ATOM   1114  NH2 ARG A 142      38.134  36.941  32.274  1.00 22.85           N  
ATOM   1115  N   ARG A 143      38.593  37.027  25.454  1.00 10.36           N  
ATOM   1116  CA  ARG A 143      39.160  36.555  24.207  1.00 16.05           C  
ATOM   1117  C   ARG A 143      40.685  36.408  24.317  1.00 19.69           C  
ATOM   1118  O   ARG A 143      41.267  35.470  23.761  1.00 19.75           O  
ATOM   1119  CB  ARG A 143      38.767  37.532  23.095  1.00 16.76           C  
ATOM   1120  CG  ARG A 143      38.874  37.005  21.691  1.00 20.56           C  
ATOM   1121  CD  ARG A 143      38.295  38.009  20.708  1.00 26.81           C  
ATOM   1122  NE  ARG A 143      38.562  37.626  19.323  1.00 29.39           N  
ATOM   1123  CZ  ARG A 143      38.263  38.372  18.265  1.00 33.07           C  
ATOM   1124  NH1 ARG A 143      37.677  39.550  18.422  1.00 36.51           N  
ATOM   1125  NH2 ARG A 143      38.555  37.940  17.043  1.00 34.83           N  
ATOM   1126  N   ALA A 144      41.325  37.315  25.054  1.00 20.98           N  
ATOM   1127  CA  ALA A 144      42.778  37.277  25.240  1.00 18.27           C  
ATOM   1128  C   ALA A 144      43.178  36.103  26.120  1.00 17.03           C  
ATOM   1129  O   ALA A 144      44.159  35.419  25.830  1.00 18.08           O  
ATOM   1130  CB  ALA A 144      43.270  38.572  25.842  1.00 12.96           C  
ATOM   1131  N   GLU A 145      42.401  35.868  27.179  1.00 17.95           N  
ATOM   1132  CA  GLU A 145      42.640  34.765  28.114  1.00 20.10           C  
ATOM   1133  C   GLU A 145      42.593  33.415  27.399  1.00 26.43           C  
ATOM   1134  O   GLU A 145      43.405  32.526  27.675  1.00 27.29           O  
ATOM   1135  CB  GLU A 145      41.602  34.762  29.233  1.00 20.49           C  
ATOM   1136  CG  GLU A 145      41.824  35.799  30.323  1.00 27.40           C  
ATOM   1137  CD  GLU A 145      40.908  35.592  31.521  1.00 29.51           C  
ATOM   1138  OE1 GLU A 145      39.836  34.977  31.360  1.00 28.56           O  
ATOM   1139  OE2 GLU A 145      41.264  36.042  32.630  1.00 32.39           O  
ATOM   1140  N   ARG A 146      41.634  33.262  26.488  1.00 23.35           N  
ATOM   1141  CA  ARG A 146      41.507  32.024  25.732  1.00 23.77           C  
ATOM   1142  C   ARG A 146      42.746  31.809  24.882  1.00 20.18           C  
ATOM   1143  O   ARG A 146      43.278  30.705  24.833  1.00 25.16           O  
ATOM   1144  CB  ARG A 146      40.256  32.031  24.842  1.00 29.23           C  
ATOM   1145  CG  ARG A 146      38.946  32.047  25.609  1.00 40.73           C  
ATOM   1146  CD  ARG A 146      37.782  31.549  24.764  1.00 48.01           C  
ATOM   1147  NE  ARG A 146      37.592  32.327  23.540  1.00 55.68           N  
ATOM   1148  CZ  ARG A 146      36.789  33.385  23.437  1.00 58.32           C  
ATOM   1149  NH1 ARG A 146      36.091  33.810  24.486  1.00 55.66           N  
ATOM   1150  NH2 ARG A 146      36.675  34.014  22.273  1.00 61.05           N  
ATOM   1151  N   ALA A 147      43.227  32.876  24.249  1.00 13.11           N  
ATOM   1152  CA  ALA A 147      44.411  32.800  23.401  1.00 11.83           C  
ATOM   1153  C   ALA A 147      45.691  32.590  24.216  1.00 14.82           C  
ATOM   1154  O   ALA A 147      46.792  32.494  23.657  1.00  9.12           O  
ATOM   1155  CB  ALA A 147      44.527  34.041  22.542  1.00 16.87           C  
ATOM   1156  N   GLY A 148      45.544  32.546  25.539  1.00 12.19           N  
ATOM   1157  CA  GLY A 148      46.681  32.311  26.406  1.00 11.76           C  
ATOM   1158  C   GLY A 148      47.572  33.490  26.729  1.00 19.89           C  
ATOM   1159  O   GLY A 148      48.754  33.289  27.039  1.00 18.67           O  
ATOM   1160  N   PHE A 149      47.041  34.710  26.640  1.00 18.00           N  
ATOM   1161  CA  PHE A 149      47.830  35.894  26.967  1.00 12.88           C  
ATOM   1162  C   PHE A 149      47.990  35.940  28.482  1.00 18.00           C  
ATOM   1163  O   PHE A 149      47.014  35.755  29.223  1.00 18.49           O  
ATOM   1164  CB  PHE A 149      47.194  37.165  26.414  1.00 10.38           C  
ATOM   1165  CG  PHE A 149      47.409  37.347  24.933  1.00 11.55           C  
ATOM   1166  CD1 PHE A 149      46.963  36.390  24.034  1.00 12.95           C  
ATOM   1167  CD2 PHE A 149      48.085  38.458  24.443  1.00 10.38           C  
ATOM   1168  CE1 PHE A 149      47.194  36.542  22.664  1.00 17.14           C  
ATOM   1169  CE2 PHE A 149      48.322  38.619  23.077  1.00  8.39           C  
ATOM   1170  CZ  PHE A 149      47.878  37.662  22.188  1.00  9.01           C  
ATOM   1171  N   LYS A 150      49.226  36.180  28.918  1.00 11.70           N  
ATOM   1172  CA  LYS A 150      49.607  36.193  30.321  1.00  7.95           C  
ATOM   1173  C   LYS A 150      49.286  37.395  31.187  1.00 11.57           C  
ATOM   1174  O   LYS A 150      49.254  37.275  32.417  1.00 13.24           O  
ATOM   1175  CB  LYS A 150      51.101  35.884  30.431  1.00 12.92           C  
ATOM   1176  CG  LYS A 150      51.483  34.522  29.875  1.00 11.97           C  
ATOM   1177  CD  LYS A 150      50.719  33.428  30.591  1.00 10.24           C  
ATOM   1178  CE  LYS A 150      51.014  32.054  30.026  1.00 12.01           C  
ATOM   1179  NZ  LYS A 150      50.490  30.995  30.949  1.00 17.92           N  
ATOM   1180  N   ALA A 151      49.087  38.557  30.576  1.00 13.47           N  
ATOM   1181  CA  ALA A 151      48.784  39.759  31.345  1.00 10.84           C  
ATOM   1182  C   ALA A 151      48.100  40.853  30.527  1.00 12.54           C  
ATOM   1183  O   ALA A 151      48.123  40.834  29.290  1.00 15.11           O  
ATOM   1184  CB  ALA A 151      50.046  40.293  31.983  1.00  9.18           C  
ATOM   1185  N   ILE A 152      47.500  41.811  31.224  1.00 11.77           N  
ATOM   1186  CA  ILE A 152      46.807  42.916  30.571  1.00 16.30           C  
ATOM   1187  C   ILE A 152      47.560  44.197  30.887  1.00 19.43           C  
ATOM   1188  O   ILE A 152      47.840  44.488  32.052  1.00 23.85           O  
ATOM   1189  CB  ILE A 152      45.339  43.062  31.082  1.00 15.26           C  
ATOM   1190  CG1 ILE A 152      44.526  41.797  30.777  1.00 15.65           C  
ATOM   1191  CG2 ILE A 152      44.660  44.267  30.439  1.00  8.69           C  
ATOM   1192  CD1 ILE A 152      44.256  41.558  29.299  1.00 16.94           C  
ATOM   1193  N   ALA A 153      47.917  44.938  29.848  1.00 18.43           N  
ATOM   1194  CA  ALA A 153      48.629  46.197  29.998  1.00 17.20           C  
ATOM   1195  C   ALA A 153      47.623  47.317  29.715  1.00 15.26           C  
ATOM   1196  O   ALA A 153      47.240  47.547  28.561  1.00  9.51           O  
ATOM   1197  CB  ALA A 153      49.803  46.253  29.021  1.00 16.26           C  
ATOM   1198  N   LEU A 154      47.151  47.962  30.777  1.00 10.71           N  
ATOM   1199  CA  LEU A 154      46.179  49.044  30.668  1.00  7.75           C  
ATOM   1200  C   LEU A 154      46.877  50.374  30.436  1.00  9.13           C  
ATOM   1201  O   LEU A 154      47.677  50.814  31.263  1.00  6.78           O  
ATOM   1202  CB  LEU A 154      45.341  49.113  31.948  1.00  3.43           C  
ATOM   1203  CG  LEU A 154      44.431  50.325  32.136  1.00  8.39           C  
ATOM   1204  CD1 LEU A 154      43.401  50.391  31.013  1.00 16.28           C  
ATOM   1205  CD2 LEU A 154      43.751  50.251  33.493  1.00  8.65           C  
ATOM   1206  N   THR A 155      46.593  51.011  29.306  1.00 15.11           N  
ATOM   1207  CA  THR A 155      47.203  52.300  28.994  1.00 10.60           C  
ATOM   1208  C   THR A 155      46.337  53.420  29.543  1.00 11.93           C  
ATOM   1209  O   THR A 155      45.191  53.590  29.129  1.00 18.29           O  
ATOM   1210  CB  THR A 155      47.396  52.488  27.500  1.00  7.43           C  
ATOM   1211  OG1 THR A 155      48.167  51.396  26.985  1.00  5.37           O  
ATOM   1212  CG2 THR A 155      48.137  53.785  27.229  1.00  7.88           C  
ATOM   1213  N   VAL A 156      46.911  54.203  30.447  1.00  9.01           N  
ATOM   1214  CA  VAL A 156      46.208  55.295  31.103  1.00  8.37           C  
ATOM   1215  C   VAL A 156      46.649  56.714  30.711  1.00 11.87           C  
ATOM   1216  O   VAL A 156      46.345  57.672  31.423  1.00 13.58           O  
ATOM   1217  CB  VAL A 156      46.349  55.157  32.631  1.00  9.79           C  
ATOM   1218  CG1 VAL A 156      45.756  53.840  33.098  1.00  7.39           C  
ATOM   1219  CG2 VAL A 156      47.825  55.239  33.037  1.00  9.80           C  
ATOM   1220  N   ASP A 157      47.351  56.865  29.593  1.00  9.87           N  
ATOM   1221  CA  ASP A 157      47.813  58.193  29.188  1.00 14.23           C  
ATOM   1222  C   ASP A 157      47.150  58.772  27.935  1.00 13.44           C  
ATOM   1223  O   ASP A 157      47.619  59.765  27.377  1.00 12.58           O  
ATOM   1224  CB  ASP A 157      49.356  58.231  29.073  1.00  8.76           C  
ATOM   1225  CG  ASP A 157      49.907  57.398  27.909  1.00  8.76           C  
ATOM   1226  OD1 ASP A 157      49.141  56.936  27.036  1.00  3.08           O  
ATOM   1227  OD2 ASP A 157      51.145  57.233  27.854  1.00  8.98           O  
ATOM   1228  N   THR A 158      46.060  58.148  27.499  1.00 16.20           N  
ATOM   1229  CA  THR A 158      45.346  58.609  26.311  1.00 17.17           C  
ATOM   1230  C   THR A 158      43.842  58.869  26.544  1.00 16.65           C  
ATOM   1231  O   THR A 158      42.992  58.245  25.894  1.00 14.54           O  
ATOM   1232  CB  THR A 158      45.533  57.605  25.126  1.00 16.78           C  
ATOM   1233  OG1 THR A 158      46.919  57.267  25.008  1.00 10.30           O  
ATOM   1234  CG2 THR A 158      45.064  58.216  23.804  1.00 12.92           C  
ATOM   1235  N   PRO A 159      43.490  59.747  27.514  1.00 12.61           N  
ATOM   1236  CA  PRO A 159      42.062  60.012  27.732  1.00 11.76           C  
ATOM   1237  C   PRO A 159      41.544  60.692  26.465  1.00 14.08           C  
ATOM   1238  O   PRO A 159      40.370  60.575  26.105  1.00 12.25           O  
ATOM   1239  CB  PRO A 159      42.061  60.952  28.939  1.00 18.64           C  
ATOM   1240  CG  PRO A 159      43.399  61.625  28.878  1.00 18.24           C  
ATOM   1241  CD  PRO A 159      44.325  60.526  28.442  1.00 16.88           C  
ATOM   1242  N   ARG A 160      42.457  61.369  25.777  1.00 13.59           N  
ATOM   1243  CA  ARG A 160      42.169  62.043  24.522  1.00 11.29           C  
ATOM   1244  C   ARG A 160      43.457  61.948  23.717  1.00 13.20           C  
ATOM   1245  O   ARG A 160      44.545  61.902  24.296  1.00 18.18           O  
ATOM   1246  CB  ARG A 160      41.777  63.491  24.781  1.00 13.42           C  
ATOM   1247  CG  ARG A 160      40.459  63.618  25.523  1.00 20.59           C  
ATOM   1248  CD  ARG A 160      40.130  65.037  25.870  1.00 19.83           C  
ATOM   1249  NE  ARG A 160      40.079  65.873  24.679  1.00 23.99           N  
ATOM   1250  CZ  ARG A 160      39.690  67.142  24.678  1.00 25.02           C  
ATOM   1251  NH1 ARG A 160      39.300  67.723  25.810  1.00 21.48           N  
ATOM   1252  NH2 ARG A 160      39.745  67.843  23.552  1.00 25.74           N  
ATOM   1253  N   LEU A 161      43.336  61.810  22.403  1.00 14.43           N  
ATOM   1254  CA  LEU A 161      44.496  61.709  21.515  1.00 15.86           C  
ATOM   1255  C   LEU A 161      45.338  62.980  21.437  1.00 17.31           C  
ATOM   1256  O   LEU A 161      44.806  64.097  21.416  1.00 15.21           O  
ATOM   1257  CB  LEU A 161      44.051  61.369  20.096  1.00 12.94           C  
ATOM   1258  CG  LEU A 161      44.248  59.960  19.552  1.00 14.35           C  
ATOM   1259  CD1 LEU A 161      43.940  60.051  18.070  1.00 15.28           C  
ATOM   1260  CD2 LEU A 161      45.673  59.447  19.772  1.00 14.30           C  
ATOM   1261  N   GLY A 162      46.653  62.807  21.365  1.00 17.75           N  
ATOM   1262  CA  GLY A 162      47.530  63.957  21.248  1.00 14.77           C  
ATOM   1263  C   GLY A 162      47.457  64.485  19.824  1.00 15.93           C  
ATOM   1264  O   GLY A 162      46.923  63.812  18.931  1.00 11.33           O  
ATOM   1265  N   ARG A 163      47.971  65.689  19.595  1.00 14.53           N  
ATOM   1266  CA  ARG A 163      47.940  66.257  18.250  1.00 13.90           C  
ATOM   1267  C   ARG A 163      49.235  65.978  17.501  1.00 10.96           C  
ATOM   1268  O   ARG A 163      50.242  66.641  17.727  1.00 14.72           O  
ATOM   1269  CB  ARG A 163      47.718  67.770  18.288  1.00 10.70           C  
ATOM   1270  CG  ARG A 163      46.566  68.243  19.142  1.00 12.17           C  
ATOM   1271  CD  ARG A 163      46.405  69.749  19.030  1.00 11.60           C  
ATOM   1272  NE  ARG A 163      46.166  70.156  17.646  1.00 14.47           N  
ATOM   1273  CZ  ARG A 163      47.084  70.705  16.853  1.00 13.53           C  
ATOM   1274  NH1 ARG A 163      48.311  70.933  17.302  1.00  8.19           N  
ATOM   1275  NH2 ARG A 163      46.785  70.981  15.590  1.00 12.23           N  
ATOM   1276  N   ARG A 164      49.221  64.968  16.646  1.00  8.49           N  
ATOM   1277  CA  ARG A 164      50.384  64.637  15.838  1.00  6.88           C  
ATOM   1278  C   ARG A 164      50.040  65.346  14.536  1.00 12.28           C  
ATOM   1279  O   ARG A 164      49.300  64.827  13.691  1.00 14.57           O  
ATOM   1280  CB  ARG A 164      50.507  63.122  15.645  1.00  7.05           C  
ATOM   1281  CG  ARG A 164      50.606  62.336  16.956  1.00  8.22           C  
ATOM   1282  CD  ARG A 164      49.243  61.859  17.424  1.00  8.41           C  
ATOM   1283  NE  ARG A 164      49.282  61.201  18.731  1.00 13.36           N  
ATOM   1284  CZ  ARG A 164      49.245  59.879  18.918  1.00 12.43           C  
ATOM   1285  NH1 ARG A 164      49.173  59.046  17.884  1.00  4.25           N  
ATOM   1286  NH2 ARG A 164      49.249  59.387  20.150  1.00  6.95           N  
ATOM   1287  N   GLU A 165      50.563  66.553  14.394  1.00  8.04           N  
ATOM   1288  CA  GLU A 165      50.251  67.383  13.247  1.00  9.20           C  
ATOM   1289  C   GLU A 165      50.457  66.798  11.866  1.00  4.29           C  
ATOM   1290  O   GLU A 165      49.623  66.996  10.981  1.00  7.38           O  
ATOM   1291  CB  GLU A 165      50.895  68.763  13.407  1.00 11.74           C  
ATOM   1292  CG  GLU A 165      50.407  69.466  14.679  1.00  8.58           C  
ATOM   1293  CD  GLU A 165      51.004  70.844  14.896  1.00 13.99           C  
ATOM   1294  OE1 GLU A 165      51.477  71.460  13.921  1.00 12.69           O  
ATOM   1295  OE2 GLU A 165      50.988  71.319  16.054  1.00  8.79           O  
ATOM   1296  N   ALA A 166      51.511  66.020  11.686  1.00 12.91           N  
ATOM   1297  CA  ALA A 166      51.763  65.426  10.378  1.00 11.90           C  
ATOM   1298  C   ALA A 166      50.542  64.640   9.903  1.00 13.06           C  
ATOM   1299  O   ALA A 166      50.158  64.740   8.738  1.00 12.56           O  
ATOM   1300  CB  ALA A 166      52.978  64.533  10.421  1.00 12.40           C  
ATOM   1301  N   ASP A 167      49.904  63.909  10.821  1.00 12.16           N  
ATOM   1302  CA  ASP A 167      48.723  63.110  10.488  1.00 17.37           C  
ATOM   1303  C   ASP A 167      47.580  64.001  10.009  1.00 18.84           C  
ATOM   1304  O   ASP A 167      46.862  63.658   9.070  1.00 23.07           O  
ATOM   1305  CB  ASP A 167      48.264  62.269  11.693  1.00 17.53           C  
ATOM   1306  CG  ASP A 167      49.215  61.116  12.016  1.00 12.36           C  
ATOM   1307  OD1 ASP A 167      49.967  60.686  11.129  1.00 17.06           O  
ATOM   1308  OD2 ASP A 167      49.215  60.635  13.165  1.00 14.84           O  
ATOM   1309  N   ILE A 168      47.431  65.156  10.646  1.00 16.97           N  
ATOM   1310  CA  ILE A 168      46.387  66.107  10.290  1.00 13.47           C  
ATOM   1311  C   ILE A 168      46.640  66.657   8.883  1.00 14.28           C  
ATOM   1312  O   ILE A 168      45.743  66.680   8.038  1.00  9.24           O  
ATOM   1313  CB  ILE A 168      46.319  67.250  11.321  1.00 12.62           C  
ATOM   1314  CG1 ILE A 168      46.140  66.656  12.726  1.00 10.87           C  
ATOM   1315  CG2 ILE A 168      45.174  68.188  10.996  1.00  9.05           C  
ATOM   1316  CD1 ILE A 168      46.249  67.647  13.851  1.00  4.11           C  
ATOM   1317  N   LYS A 169      47.870  67.073   8.619  1.00 13.79           N  
ATOM   1318  CA  LYS A 169      48.196  67.584   7.301  1.00 16.38           C  
ATOM   1319  C   LYS A 169      48.060  66.509   6.232  1.00 19.36           C  
ATOM   1320  O   LYS A 169      47.705  66.810   5.088  1.00 21.53           O  
ATOM   1321  CB  LYS A 169      49.614  68.135   7.276  1.00 18.16           C  
ATOM   1322  CG  LYS A 169      49.777  69.442   7.993  1.00 17.46           C  
ATOM   1323  CD  LYS A 169      51.165  69.974   7.756  1.00 18.99           C  
ATOM   1324  CE  LYS A 169      51.259  71.417   8.147  1.00 20.79           C  
ATOM   1325  NZ  LYS A 169      50.906  71.572   9.576  1.00 27.63           N  
ATOM   1326  N   ASN A 170      48.388  65.270   6.597  1.00 21.94           N  
ATOM   1327  CA  ASN A 170      48.315  64.129   5.677  1.00 25.30           C  
ATOM   1328  C   ASN A 170      46.900  63.574   5.494  1.00 27.29           C  
ATOM   1329  O   ASN A 170      46.604  62.947   4.477  1.00 28.89           O  
ATOM   1330  CB  ASN A 170      49.209  62.977   6.164  1.00 23.99           C  
ATOM   1331  CG  ASN A 170      50.692  63.288   6.080  1.00 24.45           C  
ATOM   1332  OD1 ASN A 170      51.110  64.246   5.428  1.00 32.78           O  
ATOM   1333  ND2 ASN A 170      51.495  62.478   6.745  1.00 14.76           N  
ATOM   1334  N   ARG A 171      46.035  63.801   6.480  1.00 30.31           N  
ATOM   1335  CA  ARG A 171      44.666  63.289   6.465  1.00 36.82           C  
ATOM   1336  C   ARG A 171      44.769  61.764   6.481  1.00 34.45           C  
ATOM   1337  O   ARG A 171      44.343  61.070   5.555  1.00 29.41           O  
ATOM   1338  CB  ARG A 171      43.883  63.799   5.248  1.00 46.06           C  
ATOM   1339  CG  ARG A 171      43.800  65.323   5.166  1.00 58.07           C  
ATOM   1340  CD  ARG A 171      42.543  65.786   4.446  1.00 67.85           C  
ATOM   1341  NE  ARG A 171      41.339  65.421   5.192  1.00 79.41           N  
ATOM   1342  CZ  ARG A 171      40.127  65.281   4.654  1.00 84.52           C  
ATOM   1343  NH1 ARG A 171      39.935  65.476   3.353  1.00 85.16           N  
ATOM   1344  NH2 ARG A 171      39.099  64.934   5.421  1.00 85.76           N  
ATOM   1345  N   PHE A 172      45.373  61.269   7.557  1.00 30.73           N  
ATOM   1346  CA  PHE A 172      45.606  59.852   7.773  1.00 30.33           C  
ATOM   1347  C   PHE A 172      44.347  59.005   7.789  1.00 33.19           C  
ATOM   1348  O   PHE A 172      43.368  59.339   8.460  1.00 38.59           O  
ATOM   1349  CB  PHE A 172      46.373  59.656   9.080  1.00 30.93           C  
ATOM   1350  CG  PHE A 172      46.703  58.227   9.376  1.00 33.83           C  
ATOM   1351  CD1 PHE A 172      47.777  57.608   8.753  1.00 32.05           C  
ATOM   1352  CD2 PHE A 172      45.938  57.495  10.278  1.00 33.91           C  
ATOM   1353  CE1 PHE A 172      48.089  56.276   9.021  1.00 33.11           C  
ATOM   1354  CE2 PHE A 172      46.241  56.161  10.555  1.00 33.80           C  
ATOM   1355  CZ  PHE A 172      47.320  55.551   9.924  1.00 29.89           C  
ATOM   1356  N   VAL A 173      44.402  57.888   7.068  1.00 35.48           N  
ATOM   1357  CA  VAL A 173      43.298  56.933   6.967  1.00 34.42           C  
ATOM   1358  C   VAL A 173      43.894  55.525   6.886  1.00 38.31           C  
ATOM   1359  O   VAL A 173      44.985  55.334   6.342  1.00 36.30           O  
ATOM   1360  CB  VAL A 173      42.440  57.157   5.691  1.00 33.53           C  
ATOM   1361  CG1 VAL A 173      41.724  58.497   5.744  1.00 31.73           C  
ATOM   1362  CG2 VAL A 173      43.314  57.068   4.436  1.00 33.97           C  
ATOM   1363  N   LEU A 174      43.186  54.546   7.442  1.00 40.25           N  
ATOM   1364  CA  LEU A 174      43.646  53.161   7.423  1.00 37.80           C  
ATOM   1365  C   LEU A 174      43.476  52.625   6.010  1.00 36.99           C  
ATOM   1366  O   LEU A 174      42.416  52.782   5.412  1.00 38.34           O  
ATOM   1367  CB  LEU A 174      42.816  52.317   8.402  1.00 36.74           C  
ATOM   1368  CG  LEU A 174      43.053  50.802   8.480  1.00 34.42           C  
ATOM   1369  CD1 LEU A 174      44.450  50.506   8.995  1.00 33.05           C  
ATOM   1370  CD2 LEU A 174      42.029  50.165   9.394  1.00 31.63           C  
ATOM   1371  N   PRO A 175      44.554  52.071   5.422  1.00 40.22           N  
ATOM   1372  CA  PRO A 175      44.455  51.533   4.067  1.00 42.45           C  
ATOM   1373  C   PRO A 175      43.299  50.525   3.928  1.00 47.50           C  
ATOM   1374  O   PRO A 175      43.001  49.758   4.850  1.00 41.64           O  
ATOM   1375  CB  PRO A 175      45.837  50.885   3.843  1.00 41.42           C  
ATOM   1376  CG  PRO A 175      46.512  50.901   5.196  1.00 41.55           C  
ATOM   1377  CD  PRO A 175      45.942  52.079   5.899  1.00 41.22           C  
ATOM   1378  N   PRO A 176      42.676  50.489   2.735  1.00 52.62           N  
ATOM   1379  CA  PRO A 176      41.530  49.662   2.336  1.00 55.85           C  
ATOM   1380  C   PRO A 176      41.361  48.241   2.876  1.00 58.19           C  
ATOM   1381  O   PRO A 176      40.325  47.931   3.476  1.00 60.77           O  
ATOM   1382  CB  PRO A 176      41.633  49.660   0.798  1.00 55.12           C  
ATOM   1383  CG  PRO A 176      43.053  50.053   0.512  1.00 53.57           C  
ATOM   1384  CD  PRO A 176      43.299  51.097   1.557  1.00 54.49           C  
ATOM   1385  N   PHE A 177      42.358  47.387   2.680  1.00 53.47           N  
ATOM   1386  CA  PHE A 177      42.238  45.996   3.100  1.00 51.64           C  
ATOM   1387  C   PHE A 177      42.580  45.623   4.537  1.00 46.43           C  
ATOM   1388  O   PHE A 177      42.407  44.468   4.931  1.00 44.69           O  
ATOM   1389  CB  PHE A 177      43.006  45.107   2.121  1.00 59.31           C  
ATOM   1390  CG  PHE A 177      42.609  45.317   0.688  1.00 66.44           C  
ATOM   1391  CD1 PHE A 177      41.451  44.731   0.181  1.00 67.56           C  
ATOM   1392  CD2 PHE A 177      43.370  46.136  -0.145  1.00 68.98           C  
ATOM   1393  CE1 PHE A 177      41.052  44.958  -1.137  1.00 68.90           C  
ATOM   1394  CE2 PHE A 177      42.981  46.371  -1.466  1.00 71.25           C  
ATOM   1395  CZ  PHE A 177      41.817  45.780  -1.962  1.00 70.66           C  
ATOM   1396  N   LEU A 178      43.040  46.585   5.327  1.00 38.61           N  
ATOM   1397  CA  LEU A 178      43.402  46.289   6.706  1.00 32.79           C  
ATOM   1398  C   LEU A 178      42.201  46.407   7.621  1.00 29.23           C  
ATOM   1399  O   LEU A 178      41.281  47.166   7.340  1.00 27.18           O  
ATOM   1400  CB  LEU A 178      44.541  47.194   7.165  1.00 34.57           C  
ATOM   1401  CG  LEU A 178      45.807  47.099   6.307  1.00 32.53           C  
ATOM   1402  CD1 LEU A 178      46.910  47.888   6.970  1.00 29.50           C  
ATOM   1403  CD2 LEU A 178      46.228  45.647   6.122  1.00 31.40           C  
ATOM   1404  N   THR A 179      42.232  45.673   8.729  1.00 29.71           N  
ATOM   1405  CA  THR A 179      41.130  45.659   9.684  1.00 34.46           C  
ATOM   1406  C   THR A 179      41.596  45.461  11.124  1.00 30.88           C  
ATOM   1407  O   THR A 179      42.569  44.752  11.385  1.00 32.12           O  
ATOM   1408  CB  THR A 179      40.135  44.517   9.319  1.00 41.22           C  
ATOM   1409  OG1 THR A 179      39.394  44.883   8.151  1.00 51.20           O  
ATOM   1410  CG2 THR A 179      39.175  44.208  10.459  1.00 40.19           C  
ATOM   1411  N   LEU A 180      40.902  46.106  12.056  1.00 27.19           N  
ATOM   1412  CA  LEU A 180      41.211  45.972  13.475  1.00 27.38           C  
ATOM   1413  C   LEU A 180      40.584  44.630  13.878  1.00 27.47           C  
ATOM   1414  O   LEU A 180      39.513  44.571  14.483  1.00 26.58           O  
ATOM   1415  CB  LEU A 180      40.601  47.147  14.253  1.00 21.52           C  
ATOM   1416  CG  LEU A 180      40.933  48.536  13.682  1.00 21.19           C  
ATOM   1417  CD1 LEU A 180      40.252  49.640  14.459  1.00 15.30           C  
ATOM   1418  CD2 LEU A 180      42.430  48.752  13.695  1.00 24.73           C  
ATOM   1419  N   LYS A 181      41.274  43.551  13.528  1.00 25.45           N  
ATOM   1420  CA  LYS A 181      40.804  42.189  13.767  1.00 22.57           C  
ATOM   1421  C   LYS A 181      40.243  41.802  15.135  1.00 23.19           C  
ATOM   1422  O   LYS A 181      39.392  40.923  15.207  1.00 28.89           O  
ATOM   1423  CB  LYS A 181      41.865  41.182  13.324  1.00 20.52           C  
ATOM   1424  CG  LYS A 181      42.323  41.387  11.892  1.00 25.25           C  
ATOM   1425  CD  LYS A 181      41.186  41.166  10.920  1.00 31.58           C  
ATOM   1426  CE  LYS A 181      40.891  39.689  10.735  1.00 33.75           C  
ATOM   1427  NZ  LYS A 181      41.924  39.061   9.864  1.00 39.66           N  
ATOM   1428  N   ASN A 182      40.718  42.415  16.213  1.00 20.13           N  
ATOM   1429  CA  ASN A 182      40.209  42.084  17.544  1.00 20.02           C  
ATOM   1430  C   ASN A 182      38.781  42.559  17.741  1.00 22.19           C  
ATOM   1431  O   ASN A 182      38.069  42.067  18.609  1.00 24.91           O  
ATOM   1432  CB  ASN A 182      41.098  42.668  18.641  1.00 16.96           C  
ATOM   1433  CG  ASN A 182      42.442  41.987  18.722  1.00 21.21           C  
ATOM   1434  OD1 ASN A 182      42.528  40.755  18.742  1.00 27.20           O  
ATOM   1435  ND2 ASN A 182      43.501  42.776  18.753  1.00 17.95           N  
ATOM   1436  N   PHE A 183      38.369  43.531  16.940  1.00 29.35           N  
ATOM   1437  CA  PHE A 183      37.021  44.076  17.036  1.00 33.24           C  
ATOM   1438  C   PHE A 183      36.088  43.378  16.067  1.00 40.78           C  
ATOM   1439  O   PHE A 183      34.872  43.559  16.094  1.00 43.46           O  
ATOM   1440  CB  PHE A 183      37.054  45.577  16.803  1.00 28.49           C  
ATOM   1441  CG  PHE A 183      37.660  46.339  17.944  1.00 24.85           C  
ATOM   1442  CD1 PHE A 183      36.949  46.518  19.119  1.00 19.61           C  
ATOM   1443  CD2 PHE A 183      38.954  46.838  17.860  1.00 22.74           C  
ATOM   1444  CE1 PHE A 183      37.512  47.179  20.193  1.00 22.90           C  
ATOM   1445  CE2 PHE A 183      39.527  47.505  18.936  1.00 24.89           C  
ATOM   1446  CZ  PHE A 183      38.807  47.673  20.105  1.00 20.19           C  
ATOM   1447  N   GLU A 184      36.687  42.593  15.188  1.00 51.12           N  
ATOM   1448  CA  GLU A 184      35.933  41.820  14.231  1.00 56.13           C  
ATOM   1449  C   GLU A 184      35.613  40.511  14.951  1.00 58.57           C  
ATOM   1450  O   GLU A 184      36.515  39.767  15.348  1.00 57.93           O  
ATOM   1451  CB  GLU A 184      36.771  41.559  12.985  1.00 60.27           C  
ATOM   1452  CG  GLU A 184      35.991  40.948  11.849  1.00 64.41           C  
ATOM   1453  CD  GLU A 184      36.844  40.739  10.626  1.00 66.30           C  
ATOM   1454  OE1 GLU A 184      37.058  41.719   9.880  1.00 67.48           O  
ATOM   1455  OE2 GLU A 184      37.309  39.598  10.415  1.00 67.74           O  
ATOM   1456  N   GLY A 185      34.328  40.264  15.166  1.00 61.46           N  
ATOM   1457  CA  GLY A 185      33.915  39.052  15.848  1.00 67.18           C  
ATOM   1458  C   GLY A 185      33.085  39.359  17.079  1.00 72.95           C  
ATOM   1459  O   GLY A 185      32.764  38.462  17.860  1.00 76.23           O  
ATOM   1460  N   ILE A 186      33.172  40.096  17.799  1.00 76.87           N  
ATOM   1461  CA  ILE A 186      32.410  40.155  19.045  1.00 78.33           C  
ATOM   1462  C   ILE A 186      31.463  41.346  18.954  1.00 79.83           C  
ATOM   1463  O   ILE A 186      31.619  42.143  18.043  1.00 76.11           O  
ATOM   1464  CB  ILE A 186      33.379  40.329  20.218  1.00 77.64           C  
ATOM   1465  CG1 ILE A 186      34.223  41.600  20.126  1.00 74.17           C  
ATOM   1466  CG2 ILE A 186      34.382  39.179  20.339  1.00 78.15           C  
ATOM   1467  CD1 ILE A 186      35.183  41.764  21.307  1.00 74.94           C  
ATOM   1468  N   ASP A 187      30.538  41.392  19.902  1.00 82.31           N  
ATOM   1469  CA  ASP A 187      29.488  42.424  19.924  1.00 83.13           C  
ATOM   1470  C   ASP A 187      29.675  43.766  20.196  1.00 82.97           C  
ATOM   1471  O   ASP A 187      29.705  44.280  21.493  1.00 85.97           O  
ATOM   1472  CB  ASP A 187      28.570  42.220  21.131  1.00 86.74           C  
ATOM   1473  CG  ASP A 187      27.454  43.264  21.213  1.00 93.35           C  
ATOM   1474  OD1 ASP A 187      27.369  44.191  20.320  1.00 95.32           O  
ATOM   1475  OD2 ASP A 187      26.597  43.218  22.177  1.00 97.97           O  
ATOM   1476  N   LEU A 188      29.597  44.623  19.205  1.00 85.65           N  
ATOM   1477  CA  LEU A 188      29.882  45.953  19.255  1.00 86.04           C  
ATOM   1478  C   LEU A 188      28.417  46.804  19.571  1.00 88.86           C  
ATOM   1479  O   LEU A 188      28.187  47.601  20.241  1.00 91.65           O  
ATOM   1480  CB  LEU A 188      30.356  46.677  18.009  1.00 84.53           C  
ATOM   1481  CG  LEU A 188      31.801  45.966  17.646  1.00 82.08           C  
ATOM   1482  CD1 LEU A 188      32.193  46.596  16.376  1.00 81.86           C  
ATOM   1483  CD2 LEU A 188      32.720  46.459  18.746  1.00 79.98           C  
ATOM   1484  N   GLY A 198      35.028  52.767   9.239  1.00 92.38           N  
ATOM   1485  CA  GLY A 198      34.140  52.045  10.021  1.00 93.14           C  
ATOM   1486  C   GLY A 198      34.677  51.853  11.369  1.00 91.92           C  
ATOM   1487  O   GLY A 198      34.521  52.456  12.249  1.00 91.98           O  
ATOM   1488  N   LEU A 199      35.536  50.583  11.444  1.00 88.91           N  
ATOM   1489  CA  LEU A 199      36.142  50.215  12.721  1.00 85.53           C  
ATOM   1490  C   LEU A 199      37.066  51.306  13.256  1.00 85.93           C  
ATOM   1491  O   LEU A 199      37.050  51.545  14.496  1.00 85.64           O  
ATOM   1492  CB  LEU A 199      36.916  48.876  12.632  1.00 83.34           C  
ATOM   1493  CG  LEU A 199      36.728  47.456  12.507  1.00 81.83           C  
ATOM   1494  CD1 LEU A 199      35.544  46.554  12.567  1.00 80.82           C  
ATOM   1495  CD2 LEU A 199      37.752  46.919  11.543  1.00 80.27           C  
ATOM   1496  N   SER A 200      37.698  52.086  12.400  1.00 86.29           N  
ATOM   1497  CA  SER A 200      38.609  53.151  12.821  1.00 88.11           C  
ATOM   1498  C   SER A 200      37.881  54.307  13.463  1.00 87.53           C  
ATOM   1499  O   SER A 200      38.321  54.834  14.507  1.00 89.40           O  
ATOM   1500  CB  SER A 200      39.457  53.659  11.647  1.00 88.76           C  
ATOM   1501  OG  SER A 200      39.895  52.461  11.397  1.00 92.06           O  
ATOM   1502  N   SER A 201      36.478  54.417  13.034  1.00 87.49           N  
ATOM   1503  CA  SER A 201      35.977  55.677  13.574  1.00 87.48           C  
ATOM   1504  C   SER A 201      35.300  55.494  14.929  1.00 86.34           C  
ATOM   1505  O   SER A 201      35.505  56.293  15.839  1.00 84.45           O  
ATOM   1506  CB  SER A 201      35.057  56.337  12.536  1.00 88.66           C  
ATOM   1507  OG  SER A 201      35.776  56.564  11.338  1.00 89.73           O  
ATOM   1508  N   TYR A 202      34.586  54.382  15.070  1.00 85.85           N  
ATOM   1509  CA  TYR A 202      33.862  54.070  16.295  1.00 86.29           C  
ATOM   1510  C   TYR A 202      34.822  53.749  17.448  1.00 84.47           C  
ATOM   1511  O   TYR A 202      34.647  54.234  18.560  1.00 83.90           O  
ATOM   1512  CB  TYR A 202      32.900  52.896  16.022  1.00 88.82           C  
ATOM   1513  CG  TYR A 202      32.692  51.950  17.178  1.00 92.39           C  
ATOM   1514  CD1 TYR A 202      33.706  51.079  17.563  1.00 93.61           C  
ATOM   1515  CD2 TYR A 202      31.489  51.906  17.882  1.00 92.56           C  
ATOM   1516  CE1 TYR A 202      33.542  50.198  18.605  1.00 91.87           C  
ATOM   1517  CE2 TYR A 202      31.317  51.003  18.932  1.00 92.45           C  
ATOM   1518  CZ  TYR A 202      32.352  50.153  19.282  1.00 91.68           C  
ATOM   1519  OH  TYR A 202      32.194  49.228  20.291  1.00 91.42           O  
ATOM   1520  N   VAL A 203      35.810  52.897  17.188  1.00 82.06           N  
ATOM   1521  CA  VAL A 203      36.771  52.524  18.209  1.00 81.47           C  
ATOM   1522  C   VAL A 203      37.482  53.769  18.739  1.00 80.19           C  
ATOM   1523  O   VAL A 203      37.805  53.855  19.925  1.00 79.93           O  
ATOM   1524  CB  VAL A 203      37.786  51.481  17.702  1.00 83.16           C  
ATOM   1525  CG1 VAL A 203      37.157  50.111  17.693  1.00 80.86           C  
ATOM   1526  CG2 VAL A 203      38.262  51.855  16.305  1.00 87.04           C  
ATOM   1527  N   ALA A 204      37.722  54.727  17.847  1.00 78.49           N  
ATOM   1528  CA  ALA A 204      38.354  55.990  18.215  1.00 74.50           C  
ATOM   1529  C   ALA A 204      37.335  56.795  19.019  1.00 72.00           C  
ATOM   1530  O   ALA A 204      37.683  57.492  19.971  1.00 72.38           O  
ATOM   1531  CB  ALA A 204      38.778  56.760  16.983  1.00 72.98           C  
ATOM   1532  N   GLY A 205      36.068  56.678  18.638  1.00 69.14           N  
ATOM   1533  CA  GLY A 205      35.006  57.376  19.344  1.00 65.59           C  
ATOM   1534  C   GLY A 205      34.563  56.646  20.606  1.00 62.36           C  
ATOM   1535  O   GLY A 205      33.737  57.156  21.365  1.00 60.45           O  
ATOM   1536  N   GLN A 206      35.094  55.444  20.823  1.00 58.42           N  
ATOM   1537  CA  GLN A 206      34.759  54.644  21.996  1.00 52.93           C  
ATOM   1538  C   GLN A 206      35.626  54.961  23.206  1.00 46.68           C  
ATOM   1539  O   GLN A 206      35.425  54.395  24.283  1.00 44.29           O  
ATOM   1540  CB  GLN A 206      34.874  53.154  21.679  1.00 58.27           C  
ATOM   1541  CG  GLN A 206      33.562  52.494  21.308  1.00 60.82           C  
ATOM   1542  CD  GLN A 206      32.575  52.435  22.466  1.00 63.48           C  
ATOM   1543  OE1 GLN A 206      32.871  51.881  23.527  1.00 63.15           O  
ATOM   1544  NE2 GLN A 206      31.392  52.999  22.261  1.00 63.33           N  
ATOM   1545  N   ILE A 207      36.606  55.841  23.027  1.00 40.79           N  
ATOM   1546  CA  ILE A 207      37.492  56.213  24.123  1.00 37.50           C  
ATOM   1547  C   ILE A 207      36.679  56.827  25.253  1.00 34.23           C  
ATOM   1548  O   ILE A 207      35.898  57.760  25.041  1.00 32.55           O  
ATOM   1549  CB  ILE A 207      38.559  57.241  23.695  1.00 39.75           C  
ATOM   1550  CG1 ILE A 207      39.261  56.786  22.420  1.00 40.76           C  
ATOM   1551  CG2 ILE A 207      39.592  57.410  24.807  1.00 40.95           C  
ATOM   1552  CD1 ILE A 207      40.238  57.806  21.878  1.00 41.46           C  
ATOM   1553  N   ASP A 208      36.829  56.263  26.441  1.00 28.71           N  
ATOM   1554  CA  ASP A 208      36.125  56.759  27.607  1.00 28.47           C  
ATOM   1555  C   ASP A 208      37.068  57.678  28.381  1.00 29.62           C  
ATOM   1556  O   ASP A 208      38.068  57.227  28.949  1.00 33.61           O  
ATOM   1557  CB  ASP A 208      35.668  55.595  28.489  1.00 24.70           C  
ATOM   1558  CG  ASP A 208      34.815  56.053  29.658  1.00 27.37           C  
ATOM   1559  OD1 ASP A 208      34.291  57.185  29.603  1.00 27.37           O  
ATOM   1560  OD2 ASP A 208      34.663  55.283  30.631  1.00 28.82           O  
ATOM   1561  N   ARG A 209      36.745  58.963  28.424  1.00 23.68           N  
ATOM   1562  CA  ARG A 209      37.586  59.919  29.127  1.00 23.86           C  
ATOM   1563  C   ARG A 209      37.186  60.188  30.580  1.00 21.53           C  
ATOM   1564  O   ARG A 209      37.683  61.123  31.211  1.00 24.85           O  
ATOM   1565  CB  ARG A 209      37.696  61.219  28.324  1.00 21.25           C  
ATOM   1566  CG  ARG A 209      36.394  61.700  27.752  1.00 20.54           C  
ATOM   1567  CD  ARG A 209      36.559  63.014  27.025  1.00 24.38           C  
ATOM   1568  NE  ARG A 209      37.002  62.858  25.644  1.00 25.32           N  
ATOM   1569  CZ  ARG A 209      36.885  63.816  24.723  1.00 31.47           C  
ATOM   1570  NH1 ARG A 209      36.341  64.986  25.040  1.00 30.27           N  
ATOM   1571  NH2 ARG A 209      37.324  63.619  23.485  1.00 35.21           N  
ATOM   1572  N   SER A 210      36.307  59.358  31.124  1.00 19.15           N  
ATOM   1573  CA  SER A 210      35.881  59.537  32.506  1.00 18.78           C  
ATOM   1574  C   SER A 210      36.593  58.576  33.437  1.00 21.18           C  
ATOM   1575  O   SER A 210      36.356  58.582  34.653  1.00 24.43           O  
ATOM   1576  CB  SER A 210      34.375  59.343  32.633  1.00 20.59           C  
ATOM   1577  OG  SER A 210      33.953  58.207  31.903  1.00 19.17           O  
ATOM   1578  N   LEU A 211      37.468  57.757  32.861  1.00 19.92           N  
ATOM   1579  CA  LEU A 211      38.224  56.765  33.614  1.00 17.49           C  
ATOM   1580  C   LEU A 211      38.954  57.345  34.797  1.00 17.11           C  
ATOM   1581  O   LEU A 211      39.559  58.411  34.707  1.00 23.13           O  
ATOM   1582  CB  LEU A 211      39.248  56.071  32.723  1.00 16.42           C  
ATOM   1583  CG  LEU A 211      38.750  55.222  31.563  1.00 17.46           C  
ATOM   1584  CD1 LEU A 211      39.956  54.628  30.851  1.00 18.89           C  
ATOM   1585  CD2 LEU A 211      37.833  54.130  32.074  1.00 15.07           C  
ATOM   1586  N   SER A 212      38.905  56.628  35.909  1.00 17.19           N  
ATOM   1587  CA  SER A 212      39.590  57.036  37.120  1.00 16.69           C  
ATOM   1588  C   SER A 212      40.007  55.754  37.809  1.00 20.30           C  
ATOM   1589  O   SER A 212      39.708  54.663  37.321  1.00 26.65           O  
ATOM   1590  CB  SER A 212      38.678  57.861  38.014  1.00 17.23           C  
ATOM   1591  OG  SER A 212      37.565  57.099  38.417  1.00 26.58           O  
ATOM   1592  N   TRP A 213      40.668  55.868  38.952  1.00 23.70           N  
ATOM   1593  CA  TRP A 213      41.134  54.688  39.664  1.00 24.41           C  
ATOM   1594  C   TRP A 213      40.111  53.593  39.966  1.00 28.39           C  
ATOM   1595  O   TRP A 213      40.486  52.423  40.067  1.00 32.96           O  
ATOM   1596  CB  TRP A 213      41.909  55.091  40.919  1.00 28.92           C  
ATOM   1597  CG  TRP A 213      43.181  55.852  40.600  1.00 35.42           C  
ATOM   1598  CD1 TRP A 213      43.385  57.199  40.724  1.00 37.40           C  
ATOM   1599  CD2 TRP A 213      44.408  55.307  40.087  1.00 35.51           C  
ATOM   1600  NE1 TRP A 213      44.661  57.526  40.321  1.00 36.43           N  
ATOM   1601  CE2 TRP A 213      45.311  56.385  39.925  1.00 35.05           C  
ATOM   1602  CE3 TRP A 213      44.834  54.017  39.747  1.00 33.37           C  
ATOM   1603  CZ2 TRP A 213      46.610  56.211  39.444  1.00 31.34           C  
ATOM   1604  CZ3 TRP A 213      46.133  53.844  39.266  1.00 33.82           C  
ATOM   1605  CH2 TRP A 213      47.001  54.937  39.121  1.00 31.39           C  
ATOM   1606  N   LYS A 214      38.830  53.937  40.080  1.00 32.58           N  
ATOM   1607  CA  LYS A 214      37.814  52.926  40.367  1.00 33.18           C  
ATOM   1608  C   LYS A 214      37.602  51.997  39.174  1.00 31.01           C  
ATOM   1609  O   LYS A 214      37.204  50.839  39.337  1.00 32.27           O  
ATOM   1610  CB  LYS A 214      36.484  53.562  40.818  1.00 42.15           C  
ATOM   1611  CG  LYS A 214      35.418  53.775  39.737  1.00 47.67           C  
ATOM   1612  CD  LYS A 214      35.771  54.916  38.814  1.00 54.43           C  
ATOM   1613  CE  LYS A 214      34.644  55.240  37.844  1.00 60.66           C  
ATOM   1614  NZ  LYS A 214      35.028  56.353  36.920  1.00 61.28           N  
ATOM   1615  N   ASP A 215      37.890  52.496  37.976  1.00 24.21           N  
ATOM   1616  CA  ASP A 215      37.743  51.689  36.780  1.00 17.91           C  
ATOM   1617  C   ASP A 215      38.864  50.667  36.708  1.00 20.64           C  
ATOM   1618  O   ASP A 215      38.745  49.646  36.022  1.00 18.85           O  
ATOM   1619  CB  ASP A 215      37.732  52.565  35.536  1.00 22.35           C  
ATOM   1620  CG  ASP A 215      36.437  53.320  35.374  1.00 25.82           C  
ATOM   1621  OD1 ASP A 215      35.358  52.693  35.487  1.00 30.62           O  
ATOM   1622  OD2 ASP A 215      36.492  54.542  35.133  1.00 25.66           O  
ATOM   1623  N   VAL A 216      39.958  50.945  37.412  1.00 23.48           N  
ATOM   1624  CA  VAL A 216      41.084  50.021  37.447  1.00 27.21           C  
ATOM   1625  C   VAL A 216      40.612  48.820  38.253  1.00 24.95           C  
ATOM   1626  O   VAL A 216      40.832  47.671  37.866  1.00 26.37           O  
ATOM   1627  CB  VAL A 216      42.318  50.659  38.107  1.00 29.28           C  
ATOM   1628  CG1 VAL A 216      43.406  49.613  38.335  1.00 29.64           C  
ATOM   1629  CG2 VAL A 216      42.845  51.780  37.222  1.00 31.32           C  
ATOM   1630  N   ALA A 217      39.901  49.115  39.339  1.00 22.84           N  
ATOM   1631  CA  ALA A 217      39.332  48.106  40.225  1.00 23.90           C  
ATOM   1632  C   ALA A 217      38.336  47.280  39.426  1.00 25.06           C  
ATOM   1633  O   ALA A 217      38.306  46.053  39.525  1.00 32.45           O  
ATOM   1634  CB  ALA A 217      38.627  48.779  41.400  1.00 20.81           C  
ATOM   1635  N   TRP A 218      37.518  47.958  38.629  1.00 20.51           N  
ATOM   1636  CA  TRP A 218      36.538  47.274  37.806  1.00 18.08           C  
ATOM   1637  C   TRP A 218      37.196  46.218  36.923  1.00 17.58           C  
ATOM   1638  O   TRP A 218      36.668  45.118  36.783  1.00 19.21           O  
ATOM   1639  CB  TRP A 218      35.771  48.261  36.925  1.00 12.87           C  
ATOM   1640  CG  TRP A 218      34.917  47.556  35.911  1.00 17.63           C  
ATOM   1641  CD1 TRP A 218      33.676  47.024  36.117  1.00 13.44           C  
ATOM   1642  CD2 TRP A 218      35.252  47.283  34.543  1.00 19.68           C  
ATOM   1643  NE1 TRP A 218      33.218  46.441  34.962  1.00 13.69           N  
ATOM   1644  CE2 TRP A 218      34.160  46.584  33.975  1.00 16.41           C  
ATOM   1645  CE3 TRP A 218      36.367  47.560  33.734  1.00 20.96           C  
ATOM   1646  CZ2 TRP A 218      34.146  46.158  32.639  1.00 17.76           C  
ATOM   1647  CZ3 TRP A 218      36.356  47.135  32.401  1.00 21.33           C  
ATOM   1648  CH2 TRP A 218      35.249  46.442  31.869  1.00 20.47           C  
ATOM   1649  N   LEU A 219      38.311  46.568  36.289  1.00 20.06           N  
ATOM   1650  CA  LEU A 219      39.009  45.628  35.418  1.00 21.34           C  
ATOM   1651  C   LEU A 219      39.415  44.405  36.223  1.00 18.72           C  
ATOM   1652  O   LEU A 219      39.312  43.269  35.756  1.00 20.11           O  
ATOM   1653  CB  LEU A 219      40.257  46.267  34.808  1.00 21.86           C  
ATOM   1654  CG  LEU A 219      40.384  46.347  33.283  1.00 23.53           C  
ATOM   1655  CD1 LEU A 219      41.851  46.556  32.945  1.00 24.36           C  
ATOM   1656  CD2 LEU A 219      39.874  45.079  32.607  1.00 20.82           C  
ATOM   1657  N   GLN A 220      39.839  44.651  37.454  1.00 20.49           N  
ATOM   1658  CA  GLN A 220      40.271  43.586  38.340  1.00 26.29           C  
ATOM   1659  C   GLN A 220      39.142  42.637  38.750  1.00 26.83           C  
ATOM   1660  O   GLN A 220      39.415  41.548  39.252  1.00 27.20           O  
ATOM   1661  CB  GLN A 220      40.974  44.169  39.570  1.00 29.65           C  
ATOM   1662  CG  GLN A 220      42.272  44.902  39.240  1.00 35.16           C  
ATOM   1663  CD  GLN A 220      42.926  45.519  40.461  1.00 41.03           C  
ATOM   1664  OE1 GLN A 220      42.394  46.455  41.064  1.00 45.47           O  
ATOM   1665  NE2 GLN A 220      44.084  44.999  40.833  1.00 41.98           N  
ATOM   1666  N   THR A 221      37.884  43.045  38.568  1.00 25.43           N  
ATOM   1667  CA  THR A 221      36.767  42.165  38.916  1.00 23.09           C  
ATOM   1668  C   THR A 221      36.278  41.338  37.735  1.00 20.21           C  
ATOM   1669  O   THR A 221      35.394  40.501  37.899  1.00 24.88           O  
ATOM   1670  CB  THR A 221      35.558  42.898  39.562  1.00 20.41           C  
ATOM   1671  OG1 THR A 221      35.054  43.906  38.681  1.00 20.46           O  
ATOM   1672  CG2 THR A 221      35.942  43.520  40.892  1.00 23.15           C  
ATOM   1673  N   ILE A 222      36.848  41.567  36.551  1.00 19.68           N  
ATOM   1674  CA  ILE A 222      36.454  40.799  35.369  1.00 17.14           C  
ATOM   1675  C   ILE A 222      37.607  39.963  34.806  1.00 17.75           C  
ATOM   1676  O   ILE A 222      37.464  39.303  33.778  1.00 19.84           O  
ATOM   1677  CB  ILE A 222      35.881  41.685  34.240  1.00 19.29           C  
ATOM   1678  CG1 ILE A 222      36.999  42.485  33.572  1.00 21.73           C  
ATOM   1679  CG2 ILE A 222      34.789  42.606  34.782  1.00 16.46           C  
ATOM   1680  CD1 ILE A 222      36.625  43.037  32.221  1.00 25.52           C  
ATOM   1681  N   THR A 223      38.762  40.015  35.457  1.00 19.63           N  
ATOM   1682  CA  THR A 223      39.917  39.231  35.022  1.00 19.92           C  
ATOM   1683  C   THR A 223      40.860  39.031  36.196  1.00 18.56           C  
ATOM   1684  O   THR A 223      40.897  39.844  37.114  1.00 18.52           O  
ATOM   1685  CB  THR A 223      40.681  39.880  33.849  1.00 18.79           C  
ATOM   1686  OG1 THR A 223      41.638  38.946  33.337  1.00 16.48           O  
ATOM   1687  CG2 THR A 223      41.414  41.139  34.295  1.00 19.98           C  
ATOM   1688  N   SER A 224      41.575  37.913  36.182  1.00 24.76           N  
ATOM   1689  CA  SER A 224      42.510  37.582  37.249  1.00 24.51           C  
ATOM   1690  C   SER A 224      43.940  37.793  36.774  1.00 22.81           C  
ATOM   1691  O   SER A 224      44.897  37.534  37.508  1.00 24.19           O  
ATOM   1692  CB  SER A 224      42.303  36.129  37.686  1.00 24.66           C  
ATOM   1693  OG  SER A 224      40.938  35.885  37.979  1.00 27.61           O  
ATOM   1694  N   LEU A 225      44.077  38.210  35.520  1.00 19.15           N  
ATOM   1695  CA  LEU A 225      45.385  38.461  34.947  1.00 19.90           C  
ATOM   1696  C   LEU A 225      45.997  39.704  35.601  1.00 17.07           C  
ATOM   1697  O   LEU A 225      45.280  40.613  36.040  1.00 16.31           O  
ATOM   1698  CB  LEU A 225      45.269  38.688  33.429  1.00 16.06           C  
ATOM   1699  CG  LEU A 225      44.805  37.536  32.539  1.00 16.85           C  
ATOM   1700  CD1 LEU A 225      44.672  37.987  31.091  1.00 18.31           C  
ATOM   1701  CD2 LEU A 225      45.794  36.404  32.632  1.00 16.72           C  
ATOM   1702  N   PRO A 226      47.328  39.711  35.760  1.00 14.08           N  
ATOM   1703  CA  PRO A 226      48.046  40.840  36.353  1.00 13.88           C  
ATOM   1704  C   PRO A 226      47.807  42.064  35.459  1.00 12.15           C  
ATOM   1705  O   PRO A 226      47.843  41.964  34.230  1.00  9.35           O  
ATOM   1706  CB  PRO A 226      49.504  40.394  36.267  1.00 17.36           C  
ATOM   1707  CG  PRO A 226      49.426  38.914  36.355  1.00 17.14           C  
ATOM   1708  CD  PRO A 226      48.238  38.580  35.504  1.00 19.83           C  
ATOM   1709  N   ILE A 227      47.550  43.209  36.077  1.00 10.14           N  
ATOM   1710  CA  ILE A 227      47.294  44.436  35.333  1.00  9.12           C  
ATOM   1711  C   ILE A 227      48.510  45.355  35.402  1.00  8.11           C  
ATOM   1712  O   ILE A 227      48.985  45.681  36.494  1.00 11.59           O  
ATOM   1713  CB  ILE A 227      46.070  45.192  35.911  1.00  9.45           C  
ATOM   1714  CG1 ILE A 227      44.885  44.234  36.075  1.00  8.58           C  
ATOM   1715  CG2 ILE A 227      45.684  46.352  35.005  1.00  4.93           C  
ATOM   1716  CD1 ILE A 227      44.429  43.590  34.798  1.00 10.99           C  
ATOM   1717  N   LEU A 228      49.021  45.751  34.242  1.00  5.34           N  
ATOM   1718  CA  LEU A 228      50.167  46.652  34.168  1.00  9.82           C  
ATOM   1719  C   LEU A 228      49.676  48.027  33.720  1.00 10.72           C  
ATOM   1720  O   LEU A 228      48.992  48.138  32.694  1.00 10.76           O  
ATOM   1721  CB  LEU A 228      51.206  46.132  33.166  1.00 12.62           C  
ATOM   1722  CG  LEU A 228      51.931  44.813  33.456  1.00 13.01           C  
ATOM   1723  CD1 LEU A 228      52.805  44.442  32.276  1.00 11.89           C  
ATOM   1724  CD2 LEU A 228      52.779  44.945  34.703  1.00 16.46           C  
ATOM   1725  N   VAL A 229      49.951  49.055  34.518  1.00  6.65           N  
ATOM   1726  CA  VAL A 229      49.549  50.412  34.162  1.00  9.89           C  
ATOM   1727  C   VAL A 229      50.634  51.037  33.280  1.00  7.97           C  
ATOM   1728  O   VAL A 229      51.782  51.189  33.700  1.00 10.05           O  
ATOM   1729  CB  VAL A 229      49.305  51.299  35.413  1.00 12.89           C  
ATOM   1730  CG1 VAL A 229      48.087  50.818  36.165  1.00 10.23           C  
ATOM   1731  CG2 VAL A 229      50.525  51.283  36.332  1.00 18.65           C  
ATOM   1732  N   LYS A 230      50.270  51.398  32.059  1.00  2.00           N  
ATOM   1733  CA  LYS A 230      51.212  51.977  31.127  1.00  6.05           C  
ATOM   1734  C   LYS A 230      50.921  53.461  30.963  1.00 13.01           C  
ATOM   1735  O   LYS A 230      49.813  53.849  30.575  1.00 21.31           O  
ATOM   1736  CB  LYS A 230      51.098  51.242  29.791  1.00  5.81           C  
ATOM   1737  CG  LYS A 230      51.964  51.747  28.645  1.00  2.99           C  
ATOM   1738  CD  LYS A 230      51.726  50.861  27.427  1.00  2.78           C  
ATOM   1739  CE  LYS A 230      52.590  51.228  26.251  1.00  2.00           C  
ATOM   1740  NZ  LYS A 230      52.160  52.470  25.617  1.00  6.47           N  
ATOM   1741  N   GLY A 231      51.909  54.293  31.279  1.00 13.43           N  
ATOM   1742  CA  GLY A 231      51.739  55.730  31.149  1.00  9.48           C  
ATOM   1743  C   GLY A 231      51.839  56.513  32.449  1.00  7.88           C  
ATOM   1744  O   GLY A 231      51.224  57.564  32.595  1.00 11.70           O  
ATOM   1745  N   VAL A 232      52.571  55.983  33.417  1.00  6.55           N  
ATOM   1746  CA  VAL A 232      52.758  56.663  34.691  1.00 13.79           C  
ATOM   1747  C   VAL A 232      54.120  57.368  34.667  1.00 18.48           C  
ATOM   1748  O   VAL A 232      55.136  56.743  34.347  1.00 15.32           O  
ATOM   1749  CB  VAL A 232      52.747  55.651  35.860  1.00 14.23           C  
ATOM   1750  CG1 VAL A 232      53.033  56.351  37.181  1.00 16.23           C  
ATOM   1751  CG2 VAL A 232      51.417  54.922  35.915  1.00 14.05           C  
ATOM   1752  N   ILE A 233      54.148  58.667  34.960  1.00 21.34           N  
ATOM   1753  CA  ILE A 233      55.426  59.376  34.976  1.00 18.56           C  
ATOM   1754  C   ILE A 233      55.673  60.280  36.177  1.00 16.22           C  
ATOM   1755  O   ILE A 233      56.637  61.044  36.181  1.00 24.95           O  
ATOM   1756  CB  ILE A 233      55.696  60.177  33.689  1.00 19.13           C  
ATOM   1757  CG1 ILE A 233      54.640  61.252  33.498  1.00 18.03           C  
ATOM   1758  CG2 ILE A 233      55.817  59.249  32.492  1.00 17.69           C  
ATOM   1759  CD1 ILE A 233      55.057  62.297  32.500  1.00 27.26           C  
ATOM   1760  N   THR A 234      54.808  60.210  37.185  1.00 13.42           N  
ATOM   1761  CA  THR A 234      54.985  61.005  38.404  1.00  9.70           C  
ATOM   1762  C   THR A 234      54.962  60.056  39.596  1.00 11.76           C  
ATOM   1763  O   THR A 234      54.326  59.004  39.544  1.00 15.89           O  
ATOM   1764  CB  THR A 234      53.869  62.063  38.592  1.00 12.55           C  
ATOM   1765  OG1 THR A 234      52.593  61.413  38.692  1.00 12.88           O  
ATOM   1766  CG2 THR A 234      53.849  63.052  37.425  1.00  8.10           C  
ATOM   1767  N   ALA A 235      55.645  60.422  40.672  1.00 11.66           N  
ATOM   1768  CA  ALA A 235      55.698  59.589  41.867  1.00  9.31           C  
ATOM   1769  C   ALA A 235      54.339  59.488  42.542  1.00 13.35           C  
ATOM   1770  O   ALA A 235      54.047  58.496  43.209  1.00 17.41           O  
ATOM   1771  CB  ALA A 235      56.711  60.142  42.841  1.00  9.25           C  
ATOM   1772  N   GLU A 236      53.500  60.498  42.333  1.00 12.05           N  
ATOM   1773  CA  GLU A 236      52.172  60.548  42.930  1.00 16.20           C  
ATOM   1774  C   GLU A 236      51.272  59.453  42.369  1.00 17.12           C  
ATOM   1775  O   GLU A 236      50.578  58.762  43.114  1.00 17.12           O  
ATOM   1776  CB  GLU A 236      51.532  61.920  42.706  1.00 16.36           C  
ATOM   1777  CG  GLU A 236      52.335  63.097  43.260  1.00 22.96           C  
ATOM   1778  CD  GLU A 236      53.419  63.578  42.310  1.00 27.03           C  
ATOM   1779  OE1 GLU A 236      53.133  64.466  41.479  1.00 32.15           O  
ATOM   1780  OE2 GLU A 236      54.557  63.075  42.389  1.00 29.92           O  
ATOM   1781  N   ASP A 237      51.293  59.296  41.051  1.00 16.17           N  
ATOM   1782  CA  ASP A 237      50.486  58.284  40.397  1.00 12.11           C  
ATOM   1783  C   ASP A 237      51.071  56.894  40.643  1.00 19.48           C  
ATOM   1784  O   ASP A 237      50.326  55.926  40.812  1.00 19.47           O  
ATOM   1785  CB  ASP A 237      50.361  58.583  38.901  1.00 12.21           C  
ATOM   1786  CG  ASP A 237      49.498  59.811  38.619  1.00 14.80           C  
ATOM   1787  OD1 ASP A 237      48.424  59.964  39.249  1.00 12.55           O  
ATOM   1788  OD2 ASP A 237      49.891  60.628  37.762  1.00 16.94           O  
ATOM   1789  N   ALA A 238      52.398  56.803  40.716  1.00 18.56           N  
ATOM   1790  CA  ALA A 238      53.064  55.526  40.966  1.00 16.28           C  
ATOM   1791  C   ALA A 238      52.575  54.915  42.275  1.00 15.43           C  
ATOM   1792  O   ALA A 238      52.341  53.709  42.351  1.00 19.35           O  
ATOM   1793  CB  ALA A 238      54.580  55.706  40.996  1.00 16.33           C  
ATOM   1794  N   ARG A 239      52.405  55.747  43.300  1.00 18.77           N  
ATOM   1795  CA  ARG A 239      51.924  55.271  44.598  1.00 20.59           C  
ATOM   1796  C   ARG A 239      50.474  54.794  44.494  1.00 20.31           C  
ATOM   1797  O   ARG A 239      50.105  53.771  45.061  1.00 17.59           O  
ATOM   1798  CB  ARG A 239      52.027  56.369  45.651  1.00 23.66           C  
ATOM   1799  CG  ARG A 239      53.439  56.836  45.934  1.00 31.43           C  
ATOM   1800  CD  ARG A 239      53.444  57.791  47.111  1.00 38.11           C  
ATOM   1801  NE  ARG A 239      54.756  58.396  47.323  1.00 43.69           N  
ATOM   1802  CZ  ARG A 239      55.109  59.596  46.872  1.00 44.81           C  
ATOM   1803  NH1 ARG A 239      54.252  60.335  46.175  1.00 44.80           N  
ATOM   1804  NH2 ARG A 239      56.320  60.064  47.132  1.00 49.32           N  
ATOM   1805  N   LEU A 240      49.656  55.553  43.772  1.00 19.01           N  
ATOM   1806  CA  LEU A 240      48.259  55.206  43.572  1.00 15.50           C  
ATOM   1807  C   LEU A 240      48.164  53.885  42.808  1.00 18.56           C  
ATOM   1808  O   LEU A 240      47.338  53.034  43.128  1.00 20.90           O  
ATOM   1809  CB  LEU A 240      47.543  56.321  42.803  1.00 12.94           C  
ATOM   1810  CG  LEU A 240      47.259  57.637  43.533  1.00  8.24           C  
ATOM   1811  CD1 LEU A 240      46.832  58.698  42.538  1.00  5.15           C  
ATOM   1812  CD2 LEU A 240      46.176  57.419  44.561  1.00  3.40           C  
ATOM   1813  N   ALA A 241      49.014  53.711  41.802  1.00 18.56           N  
ATOM   1814  CA  ALA A 241      49.013  52.485  41.020  1.00 15.35           C  
ATOM   1815  C   ALA A 241      49.277  51.314  41.958  1.00 15.87           C  
ATOM   1816  O   ALA A 241      48.631  50.277  41.852  1.00 15.67           O  
ATOM   1817  CB  ALA A 241      50.064  52.551  39.931  1.00 12.57           C  
ATOM   1818  N   VAL A 242      50.193  51.502  42.904  1.00 18.72           N  
ATOM   1819  CA  VAL A 242      50.506  50.454  43.872  1.00 23.70           C  
ATOM   1820  C   VAL A 242      49.290  50.185  44.765  1.00 25.42           C  
ATOM   1821  O   VAL A 242      48.855  49.038  44.902  1.00 33.07           O  
ATOM   1822  CB  VAL A 242      51.725  50.824  44.750  1.00 20.49           C  
ATOM   1823  CG1 VAL A 242      51.942  49.768  45.813  1.00 21.42           C  
ATOM   1824  CG2 VAL A 242      52.977  50.939  43.895  1.00 20.93           C  
ATOM   1825  N   GLN A 243      48.721  51.243  45.335  1.00 21.35           N  
ATOM   1826  CA  GLN A 243      47.551  51.114  46.205  1.00 27.42           C  
ATOM   1827  C   GLN A 243      46.379  50.400  45.535  1.00 25.82           C  
ATOM   1828  O   GLN A 243      45.635  49.668  46.187  1.00 24.84           O  
ATOM   1829  CB  GLN A 243      47.049  52.485  46.654  1.00 34.50           C  
ATOM   1830  CG  GLN A 243      47.921  53.217  47.645  1.00 46.44           C  
ATOM   1831  CD  GLN A 243      47.264  54.504  48.128  1.00 53.06           C  
ATOM   1832  OE1 GLN A 243      46.030  54.621  48.153  1.00 53.23           O  
ATOM   1833  NE2 GLN A 243      48.082  55.478  48.508  1.00 54.40           N  
ATOM   1834  N   HIS A 244      46.203  50.637  44.240  1.00 19.84           N  
ATOM   1835  CA  HIS A 244      45.104  50.049  43.492  1.00 19.99           C  
ATOM   1836  C   HIS A 244      45.393  48.713  42.810  1.00 20.39           C  
ATOM   1837  O   HIS A 244      44.895  48.433  41.716  1.00 21.83           O  
ATOM   1838  CB  HIS A 244      44.542  51.079  42.514  1.00 28.47           C  
ATOM   1839  CG  HIS A 244      43.938  52.269  43.193  1.00 36.28           C  
ATOM   1840  ND1 HIS A 244      42.637  52.285  43.633  1.00 38.19           N  
ATOM   1841  CD2 HIS A 244      44.469  53.463  43.554  1.00 37.91           C  
ATOM   1842  CE1 HIS A 244      42.385  53.432  44.238  1.00 37.02           C  
ATOM   1843  NE2 HIS A 244      43.481  54.164  44.206  1.00 34.44           N  
ATOM   1844  N   GLY A 245      46.216  47.903  43.468  1.00 18.10           N  
ATOM   1845  CA  GLY A 245      46.550  46.574  42.981  1.00 16.62           C  
ATOM   1846  C   GLY A 245      47.216  46.382  41.632  1.00 16.32           C  
ATOM   1847  O   GLY A 245      47.015  45.343  40.985  1.00 11.37           O  
ATOM   1848  N   ALA A 246      48.008  47.354  41.194  1.00 16.96           N  
ATOM   1849  CA  ALA A 246      48.694  47.218  39.918  1.00 14.83           C  
ATOM   1850  C   ALA A 246      49.765  46.149  40.096  1.00 15.62           C  
ATOM   1851  O   ALA A 246      50.395  46.060  41.154  1.00 13.65           O  
ATOM   1852  CB  ALA A 246      49.320  48.534  39.494  1.00 15.53           C  
ATOM   1853  N   ALA A 247      49.921  45.310  39.081  1.00  9.31           N  
ATOM   1854  CA  ALA A 247      50.906  44.242  39.101  1.00 15.88           C  
ATOM   1855  C   ALA A 247      52.286  44.786  38.736  1.00 18.51           C  
ATOM   1856  O   ALA A 247      53.308  44.150  39.001  1.00 18.34           O  
ATOM   1857  CB  ALA A 247      50.502  43.151  38.122  1.00 18.65           C  
ATOM   1858  N   GLY A 248      52.303  45.949  38.095  1.00 17.84           N  
ATOM   1859  CA  GLY A 248      53.550  46.569  37.696  1.00 14.43           C  
ATOM   1860  C   GLY A 248      53.260  47.894  37.033  1.00 13.56           C  
ATOM   1861  O   GLY A 248      52.146  48.124  36.554  1.00 13.29           O  
ATOM   1862  N   ILE A 249      54.260  48.764  36.994  1.00  9.44           N  
ATOM   1863  CA  ILE A 249      54.106  50.085  36.395  1.00  6.67           C  
ATOM   1864  C   ILE A 249      55.027  50.230  35.201  1.00  6.62           C  
ATOM   1865  O   ILE A 249      56.179  49.800  35.248  1.00 11.05           O  
ATOM   1866  CB  ILE A 249      54.469  51.194  37.412  1.00  2.08           C  
ATOM   1867  CG1 ILE A 249      53.555  51.104  38.631  1.00  6.03           C  
ATOM   1868  CG2 ILE A 249      54.352  52.555  36.775  1.00  5.36           C  
ATOM   1869  CD1 ILE A 249      53.879  52.089  39.729  1.00  6.32           C  
ATOM   1870  N   ILE A 250      54.526  50.811  34.121  1.00  6.77           N  
ATOM   1871  CA  ILE A 250      55.358  51.034  32.948  1.00 11.90           C  
ATOM   1872  C   ILE A 250      55.528  52.543  32.735  1.00 17.04           C  
ATOM   1873  O   ILE A 250      54.586  53.221  32.278  1.00 10.63           O  
ATOM   1874  CB  ILE A 250      54.753  50.432  31.667  1.00 12.85           C  
ATOM   1875  CG1 ILE A 250      54.505  48.934  31.840  1.00 13.60           C  
ATOM   1876  CG2 ILE A 250      55.693  50.664  30.489  1.00 10.08           C  
ATOM   1877  CD1 ILE A 250      53.991  48.254  30.580  1.00 16.31           C  
ATOM   1878  N   VAL A 251      56.697  53.068  33.121  1.00 11.40           N  
ATOM   1879  CA  VAL A 251      57.006  54.484  32.939  1.00  5.33           C  
ATOM   1880  C   VAL A 251      57.043  54.695  31.431  1.00  5.12           C  
ATOM   1881  O   VAL A 251      57.897  54.137  30.730  1.00  2.59           O  
ATOM   1882  CB  VAL A 251      58.376  54.869  33.536  1.00  5.38           C  
ATOM   1883  CG1 VAL A 251      58.743  56.269  33.141  1.00  2.00           C  
ATOM   1884  CG2 VAL A 251      58.337  54.771  35.034  1.00  7.33           C  
ATOM   1885  N   SER A 252      56.105  55.495  30.938  1.00  5.36           N  
ATOM   1886  CA  SER A 252      55.991  55.748  29.512  1.00  4.10           C  
ATOM   1887  C   SER A 252      55.342  57.096  29.233  1.00  4.24           C  
ATOM   1888  O   SER A 252      54.513  57.562  30.013  1.00 10.33           O  
ATOM   1889  CB  SER A 252      55.142  54.637  28.884  1.00  2.70           C  
ATOM   1890  OG  SER A 252      54.818  54.900  27.529  1.00  6.36           O  
ATOM   1891  N   ASN A 253      55.748  57.729  28.139  1.00  2.00           N  
ATOM   1892  CA  ASN A 253      55.179  58.995  27.719  1.00  2.00           C  
ATOM   1893  C   ASN A 253      54.595  58.800  26.328  1.00  5.66           C  
ATOM   1894  O   ASN A 253      54.540  59.723  25.504  1.00  3.50           O  
ATOM   1895  CB  ASN A 253      56.188  60.148  27.774  1.00  4.91           C  
ATOM   1896  CG  ASN A 253      57.420  59.918  26.914  1.00  6.41           C  
ATOM   1897  OD1 ASN A 253      57.345  59.385  25.807  1.00  2.21           O  
ATOM   1898  ND2 ASN A 253      58.561  60.392  27.402  1.00  7.69           N  
ATOM   1899  N   HIS A 254      54.221  57.545  26.072  1.00  4.72           N  
ATOM   1900  CA  HIS A 254      53.596  57.110  24.833  1.00  4.02           C  
ATOM   1901  C   HIS A 254      54.450  57.364  23.608  1.00  5.25           C  
ATOM   1902  O   HIS A 254      53.919  57.559  22.525  1.00 12.53           O  
ATOM   1903  CB  HIS A 254      52.221  57.790  24.681  1.00  6.55           C  
ATOM   1904  CG  HIS A 254      51.207  56.967  23.945  1.00  9.12           C  
ATOM   1905  ND1 HIS A 254      50.233  56.232  24.585  1.00  5.76           N  
ATOM   1906  CD2 HIS A 254      50.982  56.806  22.614  1.00 11.84           C  
ATOM   1907  CE1 HIS A 254      49.450  55.653  23.688  1.00  6.84           C  
ATOM   1908  NE2 HIS A 254      49.886  55.990  22.486  1.00 11.63           N  
ATOM   1909  N   GLY A 255      55.767  57.300  23.754  1.00  7.46           N  
ATOM   1910  CA  GLY A 255      56.634  57.543  22.616  1.00  2.00           C  
ATOM   1911  C   GLY A 255      56.544  58.999  22.205  1.00  2.63           C  
ATOM   1912  O   GLY A 255      56.730  59.323  21.035  1.00  2.00           O  
ATOM   1913  N   ALA A 256      56.260  59.865  23.182  1.00  2.00           N  
ATOM   1914  CA  ALA A 256      56.139  61.313  22.983  1.00  8.55           C  
ATOM   1915  C   ALA A 256      55.044  61.728  22.000  1.00  4.93           C  
ATOM   1916  O   ALA A 256      55.130  62.783  21.368  1.00  4.86           O  
ATOM   1917  CB  ALA A 256      57.488  61.902  22.555  1.00  2.68           C  
ATOM   1918  N   ARG A 257      53.976  60.946  21.928  1.00  6.11           N  
ATOM   1919  CA  ARG A 257      52.892  61.246  20.995  1.00  8.34           C  
ATOM   1920  C   ARG A 257      51.648  61.861  21.640  1.00  5.20           C  
ATOM   1921  O   ARG A 257      50.693  62.217  20.952  1.00  5.75           O  
ATOM   1922  CB  ARG A 257      52.520  59.989  20.216  1.00  3.60           C  
ATOM   1923  CG  ARG A 257      53.639  58.974  20.175  1.00 10.87           C  
ATOM   1924  CD  ARG A 257      53.895  58.429  18.807  1.00 12.01           C  
ATOM   1925  NE  ARG A 257      52.726  57.785  18.231  1.00 10.68           N  
ATOM   1926  CZ  ARG A 257      52.634  57.486  16.942  1.00 17.98           C  
ATOM   1927  NH1 ARG A 257      53.648  57.771  16.136  1.00 21.51           N  
ATOM   1928  NH2 ARG A 257      51.523  56.956  16.450  1.00 17.07           N  
ATOM   1929  N   GLN A 258      51.679  62.034  22.951  1.00  2.34           N  
ATOM   1930  CA  GLN A 258      50.540  62.598  23.654  1.00  5.22           C  
ATOM   1931  C   GLN A 258      50.715  64.064  24.065  1.00  5.61           C  
ATOM   1932  O   GLN A 258      50.388  64.986  23.306  1.00  6.34           O  
ATOM   1933  CB  GLN A 258      50.208  61.718  24.864  1.00  6.91           C  
ATOM   1934  CG  GLN A 258      49.592  60.391  24.470  1.00  2.00           C  
ATOM   1935  CD  GLN A 258      48.216  60.574  23.860  1.00  4.15           C  
ATOM   1936  OE1 GLN A 258      48.053  60.595  22.636  1.00  2.41           O  
ATOM   1937  NE2 GLN A 258      47.218  60.733  24.714  1.00  4.38           N  
ATOM   1938  N   LEU A 259      51.198  64.278  25.279  1.00  2.00           N  
ATOM   1939  CA  LEU A 259      51.403  65.621  25.776  1.00  4.40           C  
ATOM   1940  C   LEU A 259      52.879  65.982  25.617  1.00  8.80           C  
ATOM   1941  O   LEU A 259      53.746  65.360  26.226  1.00 15.58           O  
ATOM   1942  CB  LEU A 259      50.994  65.696  27.247  1.00  2.00           C  
ATOM   1943  CG  LEU A 259      51.276  66.996  27.993  1.00  2.08           C  
ATOM   1944  CD1 LEU A 259      50.505  68.135  27.364  1.00  3.82           C  
ATOM   1945  CD2 LEU A 259      50.897  66.835  29.445  1.00  2.00           C  
ATOM   1946  N   ASP A 260      53.178  66.944  24.755  1.00  9.67           N  
ATOM   1947  CA  ASP A 260      54.556  67.349  24.570  1.00  8.37           C  
ATOM   1948  C   ASP A 260      55.029  68.103  25.804  1.00 11.93           C  
ATOM   1949  O   ASP A 260      54.221  68.688  26.528  1.00 13.33           O  
ATOM   1950  CB  ASP A 260      54.711  68.220  23.335  1.00  6.33           C  
ATOM   1951  CG  ASP A 260      56.128  68.217  22.802  1.00  5.07           C  
ATOM   1952  OD1 ASP A 260      56.966  67.495  23.376  1.00  7.01           O  
ATOM   1953  OD2 ASP A 260      56.409  68.919  21.806  1.00  2.00           O  
ATOM   1954  N   TYR A 261      56.337  68.070  26.038  1.00  8.61           N  
ATOM   1955  CA  TYR A 261      56.970  68.720  27.179  1.00  5.76           C  
ATOM   1956  C   TYR A 261      56.903  67.927  28.478  1.00  8.97           C  
ATOM   1957  O   TYR A 261      57.011  68.487  29.577  1.00  7.46           O  
ATOM   1958  CB  TYR A 261      56.502  70.168  27.349  1.00  7.19           C  
ATOM   1959  CG  TYR A 261      57.008  71.052  26.234  1.00  7.74           C  
ATOM   1960  CD1 TYR A 261      58.369  71.333  26.119  1.00 10.74           C  
ATOM   1961  CD2 TYR A 261      56.143  71.575  25.277  1.00  5.71           C  
ATOM   1962  CE1 TYR A 261      58.860  72.111  25.079  1.00  7.81           C  
ATOM   1963  CE2 TYR A 261      56.622  72.354  24.227  1.00 10.98           C  
ATOM   1964  CZ  TYR A 261      57.984  72.615  24.139  1.00  8.60           C  
ATOM   1965  OH  TYR A 261      58.479  73.365  23.112  1.00 11.73           O  
ATOM   1966  N   VAL A 262      56.635  66.629  28.347  1.00  8.13           N  
ATOM   1967  CA  VAL A 262      56.664  65.719  29.493  1.00  6.57           C  
ATOM   1968  C   VAL A 262      58.134  65.268  29.433  1.00  7.04           C  
ATOM   1969  O   VAL A 262      58.725  65.207  28.346  1.00  5.21           O  
ATOM   1970  CB  VAL A 262      55.692  64.522  29.340  1.00  5.32           C  
ATOM   1971  CG1 VAL A 262      54.245  64.995  29.482  1.00  8.37           C  
ATOM   1972  CG2 VAL A 262      55.867  63.853  28.005  1.00  8.74           C  
ATOM   1973  N   PRO A 263      58.771  65.031  30.587  1.00  5.94           N  
ATOM   1974  CA  PRO A 263      60.173  64.613  30.541  1.00  7.04           C  
ATOM   1975  C   PRO A 263      60.446  63.286  29.834  1.00  9.31           C  
ATOM   1976  O   PRO A 263      59.528  62.515  29.536  1.00 13.26           O  
ATOM   1977  CB  PRO A 263      60.558  64.570  32.016  1.00  2.00           C  
ATOM   1978  CG  PRO A 263      59.291  64.215  32.689  1.00  2.53           C  
ATOM   1979  CD  PRO A 263      58.265  65.037  31.967  1.00  8.22           C  
ATOM   1980  N   ALA A 264      61.716  63.060  29.518  1.00 11.21           N  
ATOM   1981  CA  ALA A 264      62.142  61.827  28.877  1.00 10.41           C  
ATOM   1982  C   ALA A 264      61.931  60.737  29.916  1.00 10.40           C  
ATOM   1983  O   ALA A 264      62.210  60.942  31.106  1.00  4.23           O  
ATOM   1984  CB  ALA A 264      63.608  61.915  28.504  1.00 13.46           C  
ATOM   1985  N   THR A 265      61.443  59.584  29.480  1.00  9.61           N  
ATOM   1986  CA  THR A 265      61.182  58.484  30.405  1.00 10.19           C  
ATOM   1987  C   THR A 265      62.385  58.121  31.264  1.00  6.83           C  
ATOM   1988  O   THR A 265      62.244  57.837  32.451  1.00  8.50           O  
ATOM   1989  CB  THR A 265      60.658  57.247  29.672  1.00 13.07           C  
ATOM   1990  OG1 THR A 265      61.396  57.048  28.459  1.00 16.16           O  
ATOM   1991  CG2 THR A 265      59.183  57.428  29.352  1.00 11.79           C  
ATOM   1992  N   ILE A 266      63.573  58.211  30.688  1.00  2.89           N  
ATOM   1993  CA  ILE A 266      64.788  57.897  31.421  1.00  8.48           C  
ATOM   1994  C   ILE A 266      65.026  58.855  32.586  1.00  7.97           C  
ATOM   1995  O   ILE A 266      65.592  58.468  33.604  1.00 13.05           O  
ATOM   1996  CB  ILE A 266      65.999  57.893  30.487  1.00 11.77           C  
ATOM   1997  CG1 ILE A 266      67.204  57.303  31.212  1.00 12.70           C  
ATOM   1998  CG2 ILE A 266      66.262  59.283  29.962  1.00  7.91           C  
ATOM   1999  CD1 ILE A 266      66.957  55.914  31.762  1.00  8.20           C  
ATOM   2000  N   MET A 267      64.582  60.098  32.439  1.00 14.43           N  
ATOM   2001  CA  MET A 267      64.734  61.110  33.486  1.00 14.90           C  
ATOM   2002  C   MET A 267      63.691  60.939  34.585  1.00 14.42           C  
ATOM   2003  O   MET A 267      63.967  61.199  35.763  1.00 14.08           O  
ATOM   2004  CB  MET A 267      64.590  62.514  32.898  1.00 24.75           C  
ATOM   2005  CG  MET A 267      65.602  62.850  31.838  1.00 35.28           C  
ATOM   2006  SD  MET A 267      67.249  62.950  32.520  1.00 50.51           S  
ATOM   2007  CE  MET A 267      67.244  64.691  33.032  1.00 50.78           C  
ATOM   2008  N   ALA A 268      62.478  60.553  34.196  1.00 11.38           N  
ATOM   2009  CA  ALA A 268      61.388  60.370  35.149  1.00  8.90           C  
ATOM   2010  C   ALA A 268      61.442  59.051  35.905  1.00  7.42           C  
ATOM   2011  O   ALA A 268      60.978  58.960  37.040  1.00 12.82           O  
ATOM   2012  CB  ALA A 268      60.053  60.508  34.441  1.00 11.94           C  
ATOM   2013  N   LEU A 269      62.022  58.038  35.272  1.00  9.72           N  
ATOM   2014  CA  LEU A 269      62.143  56.691  35.828  1.00  9.42           C  
ATOM   2015  C   LEU A 269      62.472  56.539  37.314  1.00 12.44           C  
ATOM   2016  O   LEU A 269      61.716  55.898  38.053  1.00 17.31           O  
ATOM   2017  CB  LEU A 269      63.151  55.889  35.001  1.00  8.65           C  
ATOM   2018  CG  LEU A 269      63.553  54.499  35.488  1.00  5.22           C  
ATOM   2019  CD1 LEU A 269      62.336  53.604  35.620  1.00  9.88           C  
ATOM   2020  CD2 LEU A 269      64.526  53.910  34.506  1.00  3.87           C  
ATOM   2021  N   GLU A 270      63.586  57.120  37.751  1.00  9.33           N  
ATOM   2022  CA  GLU A 270      64.028  57.010  39.140  1.00 13.42           C  
ATOM   2023  C   GLU A 270      62.996  57.485  40.155  1.00 14.89           C  
ATOM   2024  O   GLU A 270      62.843  56.891  41.219  1.00 20.75           O  
ATOM   2025  CB  GLU A 270      65.359  57.744  39.343  1.00 11.80           C  
ATOM   2026  CG  GLU A 270      66.032  57.442  40.673  1.00 14.57           C  
ATOM   2027  CD  GLU A 270      67.502  57.852  40.705  1.00 19.12           C  
ATOM   2028  OE1 GLU A 270      67.801  59.056  40.537  1.00 13.42           O  
ATOM   2029  OE2 GLU A 270      68.360  56.963  40.908  1.00 19.53           O  
ATOM   2030  N   GLU A 271      62.268  58.534  39.815  1.00 18.59           N  
ATOM   2031  CA  GLU A 271      61.251  59.063  40.709  1.00 22.67           C  
ATOM   2032  C   GLU A 271      60.158  58.010  40.906  1.00 19.65           C  
ATOM   2033  O   GLU A 271      59.650  57.819  42.014  1.00 19.69           O  
ATOM   2034  CB  GLU A 271      60.656  60.334  40.102  1.00 27.27           C  
ATOM   2035  CG  GLU A 271      59.692  61.083  41.002  1.00 35.53           C  
ATOM   2036  CD  GLU A 271      58.923  62.169  40.261  1.00 40.21           C  
ATOM   2037  OE1 GLU A 271      59.451  62.736  39.275  1.00 42.21           O  
ATOM   2038  OE2 GLU A 271      57.783  62.456  40.671  1.00 40.98           O  
ATOM   2039  N   VAL A 272      59.806  57.331  39.821  1.00 16.53           N  
ATOM   2040  CA  VAL A 272      58.773  56.303  39.844  1.00 14.10           C  
ATOM   2041  C   VAL A 272      59.263  55.051  40.570  1.00 14.63           C  
ATOM   2042  O   VAL A 272      58.521  54.439  41.333  1.00 11.95           O  
ATOM   2043  CB  VAL A 272      58.322  55.950  38.405  1.00 12.60           C  
ATOM   2044  CG1 VAL A 272      57.323  54.801  38.417  1.00  8.84           C  
ATOM   2045  CG2 VAL A 272      57.715  57.182  37.739  1.00 10.71           C  
ATOM   2046  N   VAL A 273      60.523  54.693  40.344  1.00 17.66           N  
ATOM   2047  CA  VAL A 273      61.118  53.525  40.986  1.00 19.89           C  
ATOM   2048  C   VAL A 273      61.077  53.698  42.506  1.00 20.73           C  
ATOM   2049  O   VAL A 273      60.661  52.790  43.234  1.00 24.45           O  
ATOM   2050  CB  VAL A 273      62.590  53.305  40.509  1.00 21.86           C  
ATOM   2051  CG1 VAL A 273      63.238  52.142  41.254  1.00 19.73           C  
ATOM   2052  CG2 VAL A 273      62.623  53.025  39.020  1.00 23.62           C  
ATOM   2053  N   LYS A 274      61.475  54.874  42.979  1.00 20.16           N  
ATOM   2054  CA  LYS A 274      61.484  55.158  44.412  1.00 24.24           C  
ATOM   2055  C   LYS A 274      60.096  55.164  45.022  1.00 20.48           C  
ATOM   2056  O   LYS A 274      59.911  54.729  46.155  1.00 19.53           O  
ATOM   2057  CB  LYS A 274      62.174  56.488  44.706  1.00 28.87           C  
ATOM   2058  CG  LYS A 274      63.676  56.455  44.487  1.00 43.45           C  
ATOM   2059  CD  LYS A 274      64.375  57.477  45.363  1.00 55.66           C  
ATOM   2060  CE  LYS A 274      64.115  57.197  46.843  1.00 63.18           C  
ATOM   2061  NZ  LYS A 274      64.742  58.229  47.718  1.00 69.21           N  
ATOM   2062  N   ALA A 275      59.121  55.643  44.261  1.00 19.83           N  
ATOM   2063  CA  ALA A 275      57.749  55.702  44.735  1.00 21.17           C  
ATOM   2064  C   ALA A 275      57.199  54.295  44.927  1.00 21.82           C  
ATOM   2065  O   ALA A 275      56.462  54.041  45.880  1.00 23.96           O  
ATOM   2066  CB  ALA A 275      56.886  56.481  43.753  1.00 25.89           C  
ATOM   2067  N   ALA A 276      57.573  53.386  44.028  1.00 20.26           N  
ATOM   2068  CA  ALA A 276      57.121  51.996  44.083  1.00 24.82           C  
ATOM   2069  C   ALA A 276      57.645  51.232  45.300  1.00 26.67           C  
ATOM   2070  O   ALA A 276      57.064  50.224  45.693  1.00 22.18           O  
ATOM   2071  CB  ALA A 276      57.499  51.261  42.795  1.00 23.80           C  
ATOM   2072  N   GLN A 277      58.765  51.682  45.859  1.00 31.13           N  
ATOM   2073  CA  GLN A 277      59.362  51.048  47.037  1.00 35.18           C  
ATOM   2074  C   GLN A 277      59.587  49.536  46.911  1.00 36.31           C  
ATOM   2075  O   GLN A 277      59.447  48.795  47.886  1.00 36.49           O  
ATOM   2076  CB  GLN A 277      58.519  51.340  48.278  1.00 38.86           C  
ATOM   2077  CG  GLN A 277      58.366  52.810  48.585  1.00 45.22           C  
ATOM   2078  CD  GLN A 277      57.661  53.058  49.901  1.00 49.37           C  
ATOM   2079  OE1 GLN A 277      56.510  52.666  50.086  1.00 51.74           O  
ATOM   2080  NE2 GLN A 277      58.346  53.725  50.822  1.00 50.15           N  
ATOM   2081  N   GLY A 278      59.915  49.084  45.704  1.00 36.15           N  
ATOM   2082  CA  GLY A 278      60.171  47.674  45.466  1.00 32.95           C  
ATOM   2083  C   GLY A 278      58.982  46.747  45.619  1.00 34.06           C  
ATOM   2084  O   GLY A 278      59.138  45.522  45.618  1.00 38.23           O  
ATOM   2085  N   ARG A 279      57.787  47.317  45.711  1.00 32.94           N  
ATOM   2086  CA  ARG A 279      56.574  46.531  45.869  1.00 31.34           C  
ATOM   2087  C   ARG A 279      56.160  45.840  44.578  1.00 29.30           C  
ATOM   2088  O   ARG A 279      55.622  44.732  44.603  1.00 32.05           O  
ATOM   2089  CB  ARG A 279      55.442  47.412  46.394  1.00 34.87           C  
ATOM   2090  CG  ARG A 279      55.658  47.870  47.820  1.00 43.77           C  
ATOM   2091  CD  ARG A 279      54.514  48.743  48.300  1.00 58.05           C  
ATOM   2092  NE  ARG A 279      54.478  48.843  49.757  1.00 69.12           N  
ATOM   2093  CZ  ARG A 279      54.183  47.830  50.571  1.00 75.53           C  
ATOM   2094  NH1 ARG A 279      53.896  46.629  50.077  1.00 78.49           N  
ATOM   2095  NH2 ARG A 279      54.174  48.018  51.883  1.00 78.71           N  
ATOM   2096  N   ILE A 280      56.416  46.489  43.449  1.00 19.44           N  
ATOM   2097  CA  ILE A 280      56.066  45.934  42.148  1.00 21.79           C  
ATOM   2098  C   ILE A 280      57.107  46.368  41.127  1.00 19.22           C  
ATOM   2099  O   ILE A 280      57.805  47.366  41.333  1.00 21.70           O  
ATOM   2100  CB  ILE A 280      54.657  46.408  41.663  1.00 21.72           C  
ATOM   2101  CG1 ILE A 280      54.564  47.936  41.675  1.00 21.96           C  
ATOM   2102  CG2 ILE A 280      53.565  45.799  42.518  1.00 23.49           C  
ATOM   2103  CD1 ILE A 280      53.267  48.474  41.107  1.00 21.08           C  
ATOM   2104  N   PRO A 281      57.256  45.607  40.030  1.00 15.20           N  
ATOM   2105  CA  PRO A 281      58.233  45.950  38.994  1.00 14.46           C  
ATOM   2106  C   PRO A 281      57.885  47.235  38.255  1.00 14.51           C  
ATOM   2107  O   PRO A 281      56.712  47.524  37.997  1.00 18.74           O  
ATOM   2108  CB  PRO A 281      58.179  44.744  38.047  1.00  8.25           C  
ATOM   2109  CG  PRO A 281      56.796  44.227  38.218  1.00  6.86           C  
ATOM   2110  CD  PRO A 281      56.596  44.326  39.711  1.00 10.22           C  
ATOM   2111  N   VAL A 282      58.913  48.011  37.938  1.00 12.72           N  
ATOM   2112  CA  VAL A 282      58.746  49.252  37.194  1.00 11.88           C  
ATOM   2113  C   VAL A 282      59.533  49.054  35.900  1.00 13.30           C  
ATOM   2114  O   VAL A 282      60.709  48.673  35.943  1.00 18.59           O  
ATOM   2115  CB  VAL A 282      59.315  50.470  37.965  1.00  8.58           C  
ATOM   2116  CG1 VAL A 282      59.064  51.752  37.181  1.00  2.00           C  
ATOM   2117  CG2 VAL A 282      58.692  50.556  39.345  1.00  6.75           C  
ATOM   2118  N   PHE A 283      58.869  49.241  34.763  1.00  8.66           N  
ATOM   2119  CA  PHE A 283      59.497  49.086  33.454  1.00  8.46           C  
ATOM   2120  C   PHE A 283      59.565  50.456  32.786  1.00 10.45           C  
ATOM   2121  O   PHE A 283      59.083  51.442  33.345  1.00 15.12           O  
ATOM   2122  CB  PHE A 283      58.683  48.123  32.578  1.00 12.48           C  
ATOM   2123  CG  PHE A 283      58.492  46.759  33.178  1.00 15.05           C  
ATOM   2124  CD1 PHE A 283      59.443  45.760  32.993  1.00 15.94           C  
ATOM   2125  CD2 PHE A 283      57.360  46.473  33.932  1.00 16.90           C  
ATOM   2126  CE1 PHE A 283      59.268  44.499  33.549  1.00 17.75           C  
ATOM   2127  CE2 PHE A 283      57.176  45.214  34.490  1.00 19.76           C  
ATOM   2128  CZ  PHE A 283      58.132  44.225  34.300  1.00 16.41           C  
ATOM   2129  N   LEU A 284      60.119  50.508  31.576  1.00  8.54           N  
ATOM   2130  CA  LEU A 284      60.254  51.757  30.833  1.00  2.00           C  
ATOM   2131  C   LEU A 284      60.262  51.515  29.331  1.00  2.89           C  
ATOM   2132  O   LEU A 284      60.608  50.429  28.867  1.00  9.37           O  
ATOM   2133  CB  LEU A 284      61.566  52.462  31.234  1.00  6.00           C  
ATOM   2134  CG  LEU A 284      62.110  53.689  30.463  1.00  7.42           C  
ATOM   2135  CD1 LEU A 284      63.077  54.447  31.331  1.00  9.64           C  
ATOM   2136  CD2 LEU A 284      62.818  53.300  29.173  1.00  2.00           C  
ATOM   2137  N   ASP A 285      59.834  52.519  28.579  1.00  2.00           N  
ATOM   2138  CA  ASP A 285      59.860  52.470  27.128  1.00  2.00           C  
ATOM   2139  C   ASP A 285      60.044  53.900  26.636  1.00  2.60           C  
ATOM   2140  O   ASP A 285      59.925  54.844  27.420  1.00  3.16           O  
ATOM   2141  CB  ASP A 285      58.613  51.787  26.520  1.00 10.09           C  
ATOM   2142  CG  ASP A 285      57.308  52.562  26.738  1.00 11.83           C  
ATOM   2143  OD1 ASP A 285      57.330  53.750  27.104  1.00 11.82           O  
ATOM   2144  OD2 ASP A 285      56.235  51.956  26.513  1.00 13.01           O  
ATOM   2145  N   GLY A 286      60.335  54.062  25.352  1.00  2.48           N  
ATOM   2146  CA  GLY A 286      60.533  55.384  24.795  1.00  4.14           C  
ATOM   2147  C   GLY A 286      61.991  55.774  24.635  1.00  4.89           C  
ATOM   2148  O   GLY A 286      62.699  56.015  25.620  1.00  2.00           O  
ATOM   2149  N   GLY A 287      62.451  55.790  23.387  1.00  4.54           N  
ATOM   2150  CA  GLY A 287      63.823  56.173  23.105  1.00  8.95           C  
ATOM   2151  C   GLY A 287      64.875  55.078  23.142  1.00  7.74           C  
ATOM   2152  O   GLY A 287      66.009  55.304  22.735  1.00 10.33           O  
ATOM   2153  N   VAL A 288      64.523  53.903  23.649  1.00  7.80           N  
ATOM   2154  CA  VAL A 288      65.467  52.796  23.718  1.00  5.71           C  
ATOM   2155  C   VAL A 288      65.853  52.353  22.305  1.00 11.02           C  
ATOM   2156  O   VAL A 288      65.000  51.963  21.508  1.00  8.34           O  
ATOM   2157  CB  VAL A 288      64.882  51.609  24.486  1.00  2.00           C  
ATOM   2158  CG1 VAL A 288      65.932  50.515  24.622  1.00  4.40           C  
ATOM   2159  CG2 VAL A 288      64.382  52.065  25.846  1.00  2.00           C  
ATOM   2160  N   ARG A 289      67.143  52.429  22.003  1.00  9.98           N  
ATOM   2161  CA  ARG A 289      67.638  52.069  20.689  1.00 12.02           C  
ATOM   2162  C   ARG A 289      69.001  51.378  20.749  1.00 15.01           C  
ATOM   2163  O   ARG A 289      69.460  50.817  19.747  1.00 16.09           O  
ATOM   2164  CB  ARG A 289      67.758  53.327  19.820  1.00 14.04           C  
ATOM   2165  CG  ARG A 289      66.473  54.146  19.652  1.00 15.04           C  
ATOM   2166  CD  ARG A 289      65.398  53.400  18.877  1.00 12.25           C  
ATOM   2167  NE  ARG A 289      64.223  54.232  18.639  1.00  9.22           N  
ATOM   2168  CZ  ARG A 289      63.180  54.345  19.464  1.00 12.71           C  
ATOM   2169  NH1 ARG A 289      63.136  53.676  20.614  1.00  7.08           N  
ATOM   2170  NH2 ARG A 289      62.171  55.146  19.137  1.00 11.62           N  
ATOM   2171  N   ARG A 290      69.631  51.398  21.923  1.00 12.67           N  
ATOM   2172  CA  ARG A 290      70.965  50.806  22.095  1.00  7.12           C  
ATOM   2173  C   ARG A 290      71.072  49.977  23.366  1.00  6.19           C  
ATOM   2174  O   ARG A 290      70.364  50.240  24.343  1.00 11.37           O  
ATOM   2175  CB  ARG A 290      72.018  51.922  22.179  1.00  7.18           C  
ATOM   2176  CG  ARG A 290      72.321  52.665  20.894  1.00  2.00           C  
ATOM   2177  CD  ARG A 290      73.561  52.073  20.285  1.00 10.16           C  
ATOM   2178  NE  ARG A 290      74.102  52.836  19.166  1.00  5.81           N  
ATOM   2179  CZ  ARG A 290      74.651  52.268  18.099  1.00  5.49           C  
ATOM   2180  NH1 ARG A 290      74.710  50.942  18.023  1.00  2.00           N  
ATOM   2181  NH2 ARG A 290      75.190  53.019  17.141  1.00  3.23           N  
ATOM   2182  N   GLY A 291      72.006  49.027  23.382  1.00  4.55           N  
ATOM   2183  CA  GLY A 291      72.218  48.209  24.560  1.00  2.00           C  
ATOM   2184  C   GLY A 291      72.661  49.095  25.713  1.00  2.31           C  
ATOM   2185  O   GLY A 291      72.352  48.809  26.876  1.00  7.53           O  
ATOM   2186  N   THR A 292      73.390  50.170  25.404  1.00  2.00           N  
ATOM   2187  CA  THR A 292      73.827  51.115  26.430  1.00  2.00           C  
ATOM   2188  C   THR A 292      72.579  51.757  27.049  1.00  2.00           C  
ATOM   2189  O   THR A 292      72.532  52.024  28.255  1.00  5.81           O  
ATOM   2190  CB  THR A 292      74.789  52.211  25.866  1.00  6.04           C  
ATOM   2191  OG1 THR A 292      74.198  52.843  24.724  1.00  7.44           O  
ATOM   2192  CG2 THR A 292      76.128  51.616  25.453  1.00  2.00           C  
ATOM   2193  N   ASP A 293      71.548  51.967  26.229  1.00  4.45           N  
ATOM   2194  CA  ASP A 293      70.296  52.538  26.729  1.00  5.62           C  
ATOM   2195  C   ASP A 293      69.702  51.565  27.726  1.00  3.52           C  
ATOM   2196  O   ASP A 293      69.280  51.964  28.817  1.00  3.23           O  
ATOM   2197  CB  ASP A 293      69.290  52.778  25.595  1.00  3.24           C  
ATOM   2198  CG  ASP A 293      69.727  53.864  24.630  1.00  3.35           C  
ATOM   2199  OD1 ASP A 293      70.617  54.676  24.989  1.00  3.48           O  
ATOM   2200  OD2 ASP A 293      69.171  53.913  23.518  1.00  2.00           O  
ATOM   2201  N   VAL A 294      69.716  50.283  27.368  1.00  2.00           N  
ATOM   2202  CA  VAL A 294      69.173  49.230  28.223  1.00  2.00           C  
ATOM   2203  C   VAL A 294      69.896  49.149  29.568  1.00  5.70           C  
ATOM   2204  O   VAL A 294      69.252  49.085  30.621  1.00  7.84           O  
ATOM   2205  CB  VAL A 294      69.217  47.856  27.524  1.00  4.24           C  
ATOM   2206  CG1 VAL A 294      68.493  46.809  28.367  1.00  4.24           C  
ATOM   2207  CG2 VAL A 294      68.603  47.948  26.124  1.00  2.00           C  
ATOM   2208  N   PHE A 295      71.229  49.184  29.545  1.00  8.00           N  
ATOM   2209  CA  PHE A 295      72.004  49.124  30.780  1.00  2.00           C  
ATOM   2210  C   PHE A 295      71.657  50.297  31.704  1.00  2.00           C  
ATOM   2211  O   PHE A 295      71.508  50.117  32.911  1.00  3.23           O  
ATOM   2212  CB  PHE A 295      73.509  49.107  30.466  1.00  4.33           C  
ATOM   2213  CG  PHE A 295      74.392  48.875  31.679  1.00  5.09           C  
ATOM   2214  CD1 PHE A 295      74.691  49.915  32.560  1.00  4.93           C  
ATOM   2215  CD2 PHE A 295      74.916  47.616  31.938  1.00  3.15           C  
ATOM   2216  CE1 PHE A 295      75.496  49.701  33.676  1.00  9.33           C  
ATOM   2217  CE2 PHE A 295      75.729  47.390  33.058  1.00  6.48           C  
ATOM   2218  CZ  PHE A 295      76.018  48.434  33.925  1.00  8.49           C  
ATOM   2219  N   LYS A 296      71.513  51.500  31.146  1.00  3.15           N  
ATOM   2220  CA  LYS A 296      71.196  52.669  31.977  1.00  2.00           C  
ATOM   2221  C   LYS A 296      69.814  52.580  32.624  1.00  5.98           C  
ATOM   2222  O   LYS A 296      69.659  52.896  33.807  1.00  5.75           O  
ATOM   2223  CB  LYS A 296      71.325  53.954  31.171  1.00  2.91           C  
ATOM   2224  CG  LYS A 296      72.724  54.167  30.639  1.00  6.45           C  
ATOM   2225  CD  LYS A 296      72.760  55.270  29.609  1.00  2.22           C  
ATOM   2226  CE  LYS A 296      74.164  55.500  29.124  1.00  2.00           C  
ATOM   2227  NZ  LYS A 296      74.212  56.555  28.094  1.00  7.13           N  
ATOM   2228  N   ALA A 297      68.817  52.130  31.861  1.00  5.17           N  
ATOM   2229  CA  ALA A 297      67.462  51.996  32.389  1.00  5.60           C  
ATOM   2230  C   ALA A 297      67.435  51.016  33.557  1.00  9.06           C  
ATOM   2231  O   ALA A 297      66.780  51.265  34.573  1.00  4.27           O  
ATOM   2232  CB  ALA A 297      66.510  51.542  31.299  1.00 10.14           C  
ATOM   2233  N   LEU A 298      68.170  49.911  33.417  1.00  9.78           N  
ATOM   2234  CA  LEU A 298      68.228  48.896  34.467  1.00 10.50           C  
ATOM   2235  C   LEU A 298      69.043  49.346  35.673  1.00 11.69           C  
ATOM   2236  O   LEU A 298      68.691  49.038  36.817  1.00 18.01           O  
ATOM   2237  CB  LEU A 298      68.762  47.564  33.925  1.00 13.63           C  
ATOM   2238  CG  LEU A 298      67.713  46.551  33.449  1.00  7.32           C  
ATOM   2239  CD1 LEU A 298      66.942  47.088  32.254  1.00  8.08           C  
ATOM   2240  CD2 LEU A 298      68.392  45.255  33.084  1.00  7.40           C  
ATOM   2241  N   ALA A 299      70.107  50.103  35.422  1.00  8.66           N  
ATOM   2242  CA  ALA A 299      70.954  50.620  36.495  1.00  7.00           C  
ATOM   2243  C   ALA A 299      70.178  51.641  37.314  1.00  9.44           C  
ATOM   2244  O   ALA A 299      70.523  51.919  38.459  1.00  8.67           O  
ATOM   2245  CB  ALA A 299      72.199  51.263  35.919  1.00  6.58           C  
ATOM   2246  N   LEU A 300      69.135  52.203  36.708  1.00 14.38           N  
ATOM   2247  CA  LEU A 300      68.297  53.196  37.364  1.00 13.57           C  
ATOM   2248  C   LEU A 300      67.117  52.576  38.111  1.00 13.25           C  
ATOM   2249  O   LEU A 300      66.343  53.292  38.752  1.00  9.08           O  
ATOM   2250  CB  LEU A 300      67.800  54.219  36.346  1.00 14.49           C  
ATOM   2251  CG  LEU A 300      68.195  55.682  36.559  1.00 13.59           C  
ATOM   2252  CD1 LEU A 300      69.508  55.824  37.321  1.00 15.31           C  
ATOM   2253  CD2 LEU A 300      68.293  56.336  35.199  1.00 14.00           C  
ATOM   2254  N   GLY A 301      66.985  51.252  38.032  1.00  8.02           N  
ATOM   2255  CA  GLY A 301      65.902  50.579  38.731  1.00  8.68           C  
ATOM   2256  C   GLY A 301      64.900  49.788  37.905  1.00  9.04           C  
ATOM   2257  O   GLY A 301      64.186  48.945  38.447  1.00  8.05           O  
ATOM   2258  N   ALA A 302      64.832  50.044  36.602  1.00 10.82           N  
ATOM   2259  CA  ALA A 302      63.885  49.339  35.737  1.00  9.51           C  
ATOM   2260  C   ALA A 302      64.131  47.828  35.695  1.00 12.23           C  
ATOM   2261  O   ALA A 302      65.276  47.377  35.637  1.00 21.05           O  
ATOM   2262  CB  ALA A 302      63.927  49.916  34.335  1.00  2.00           C  
ATOM   2263  N   ALA A 303      63.047  47.057  35.703  1.00  9.66           N  
ATOM   2264  CA  ALA A 303      63.122  45.597  35.660  1.00  4.72           C  
ATOM   2265  C   ALA A 303      63.294  45.095  34.229  1.00  3.89           C  
ATOM   2266  O   ALA A 303      63.640  43.934  33.999  1.00  4.84           O  
ATOM   2267  CB  ALA A 303      61.875  44.993  36.277  1.00  2.64           C  
ATOM   2268  N   GLY A 304      63.014  45.970  33.272  1.00  2.41           N  
ATOM   2269  CA  GLY A 304      63.145  45.626  31.872  1.00  2.00           C  
ATOM   2270  C   GLY A 304      62.647  46.795  31.054  1.00  5.36           C  
ATOM   2271  O   GLY A 304      62.124  47.769  31.613  1.00  9.41           O  
ATOM   2272  N   VAL A 305      62.771  46.702  29.737  1.00  3.81           N  
ATOM   2273  CA  VAL A 305      62.328  47.780  28.865  1.00  4.40           C  
ATOM   2274  C   VAL A 305      61.530  47.269  27.676  1.00  5.07           C  
ATOM   2275  O   VAL A 305      61.558  46.077  27.356  1.00  6.71           O  
ATOM   2276  CB  VAL A 305      63.532  48.638  28.346  1.00  8.00           C  
ATOM   2277  CG1 VAL A 305      64.148  49.461  29.486  1.00  7.01           C  
ATOM   2278  CG2 VAL A 305      64.582  47.754  27.688  1.00  2.54           C  
ATOM   2279  N   PHE A 306      60.820  48.182  27.024  1.00  2.00           N  
ATOM   2280  CA  PHE A 306      60.006  47.849  25.863  1.00  6.27           C  
ATOM   2281  C   PHE A 306      60.397  48.760  24.716  1.00  7.55           C  
ATOM   2282  O   PHE A 306      60.744  49.927  24.933  1.00 13.09           O  
ATOM   2283  CB  PHE A 306      58.521  48.067  26.164  1.00  9.20           C  
ATOM   2284  CG  PHE A 306      57.928  47.057  27.093  1.00  5.22           C  
ATOM   2285  CD1 PHE A 306      57.995  47.238  28.471  1.00  2.27           C  
ATOM   2286  CD2 PHE A 306      57.289  45.922  26.590  1.00 10.35           C  
ATOM   2287  CE1 PHE A 306      57.425  46.293  29.347  1.00 13.50           C  
ATOM   2288  CE2 PHE A 306      56.716  44.965  27.455  1.00 12.62           C  
ATOM   2289  CZ  PHE A 306      56.786  45.152  28.837  1.00  9.87           C  
ATOM   2290  N   ILE A 307      60.348  48.234  23.498  1.00  7.62           N  
ATOM   2291  CA  ILE A 307      60.685  49.017  22.315  1.00 10.32           C  
ATOM   2292  C   ILE A 307      59.490  49.082  21.370  1.00 11.32           C  
ATOM   2293  O   ILE A 307      58.766  48.093  21.188  1.00 14.17           O  
ATOM   2294  CB  ILE A 307      61.923  48.454  21.570  1.00  9.24           C  
ATOM   2295  CG1 ILE A 307      61.737  46.973  21.244  1.00 13.71           C  
ATOM   2296  CG2 ILE A 307      63.167  48.659  22.408  1.00 15.47           C  
ATOM   2297  CD1 ILE A 307      62.841  46.393  20.379  1.00 11.17           C  
ATOM   2298  N   GLY A 308      59.276  50.256  20.784  1.00  5.81           N  
ATOM   2299  CA  GLY A 308      58.160  50.436  19.877  1.00  3.69           C  
ATOM   2300  C   GLY A 308      58.541  50.612  18.420  1.00  2.00           C  
ATOM   2301  O   GLY A 308      58.654  49.637  17.678  1.00  2.95           O  
ATOM   2302  N   ARG A 309      58.791  51.860  18.024  1.00  2.11           N  
ATOM   2303  CA  ARG A 309      59.142  52.201  16.648  1.00  3.03           C  
ATOM   2304  C   ARG A 309      60.140  51.281  15.932  1.00  8.50           C  
ATOM   2305  O   ARG A 309      59.958  50.977  14.744  1.00  5.73           O  
ATOM   2306  CB  ARG A 309      59.609  53.651  16.558  1.00  4.50           C  
ATOM   2307  CG  ARG A 309      58.541  54.669  16.904  1.00  6.97           C  
ATOM   2308  CD  ARG A 309      59.074  56.076  16.708  1.00  2.00           C  
ATOM   2309  NE  ARG A 309      58.083  57.109  17.004  1.00  3.28           N  
ATOM   2310  CZ  ARG A 309      57.778  57.534  18.227  1.00  2.17           C  
ATOM   2311  NH1 ARG A 309      58.371  57.008  19.290  1.00  6.03           N  
ATOM   2312  NH2 ARG A 309      56.931  58.540  18.384  1.00  2.00           N  
ATOM   2313  N   PRO A 310      61.220  50.849  16.620  1.00  5.13           N  
ATOM   2314  CA  PRO A 310      62.204  49.967  15.981  1.00  6.09           C  
ATOM   2315  C   PRO A 310      61.558  48.746  15.320  1.00 11.01           C  
ATOM   2316  O   PRO A 310      62.009  48.293  14.258  1.00  9.86           O  
ATOM   2317  CB  PRO A 310      63.096  49.556  17.147  1.00  5.42           C  
ATOM   2318  CG  PRO A 310      63.092  50.770  18.014  1.00  5.88           C  
ATOM   2319  CD  PRO A 310      61.653  51.217  17.982  1.00  5.63           C  
ATOM   2320  N   VAL A 311      60.491  48.233  15.935  1.00  8.83           N  
ATOM   2321  CA  VAL A 311      59.783  47.072  15.403  1.00 10.16           C  
ATOM   2322  C   VAL A 311      59.128  47.368  14.049  1.00 11.66           C  
ATOM   2323  O   VAL A 311      59.390  46.676  13.068  1.00 16.52           O  
ATOM   2324  CB  VAL A 311      58.717  46.558  16.392  1.00  9.11           C  
ATOM   2325  CG1 VAL A 311      57.948  45.420  15.767  1.00  5.93           C  
ATOM   2326  CG2 VAL A 311      59.381  46.116  17.703  1.00  4.21           C  
ATOM   2327  N   VAL A 312      58.326  48.426  13.982  1.00  8.71           N  
ATOM   2328  CA  VAL A 312      57.654  48.786  12.736  1.00  6.94           C  
ATOM   2329  C   VAL A 312      58.612  49.202  11.620  1.00  8.88           C  
ATOM   2330  O   VAL A 312      58.365  48.893  10.446  1.00 11.61           O  
ATOM   2331  CB  VAL A 312      56.534  49.855  12.945  1.00  4.96           C  
ATOM   2332  CG1 VAL A 312      55.343  49.221  13.636  1.00  2.79           C  
ATOM   2333  CG2 VAL A 312      57.029  51.012  13.781  1.00  8.66           C  
ATOM   2334  N   PHE A 313      59.704  49.881  11.971  1.00  8.66           N  
ATOM   2335  CA  PHE A 313      60.678  50.297  10.960  1.00  5.49           C  
ATOM   2336  C   PHE A 313      61.379  49.077  10.373  1.00  7.17           C  
ATOM   2337  O   PHE A 313      61.454  48.928   9.151  1.00 12.85           O  
ATOM   2338  CB  PHE A 313      61.714  51.265  11.534  1.00  3.10           C  
ATOM   2339  CG  PHE A 313      61.149  52.607  11.918  1.00  3.97           C  
ATOM   2340  CD1 PHE A 313      60.115  53.179  11.189  1.00  2.00           C  
ATOM   2341  CD2 PHE A 313      61.643  53.291  13.029  1.00  3.61           C  
ATOM   2342  CE1 PHE A 313      59.574  54.409  11.563  1.00  3.42           C  
ATOM   2343  CE2 PHE A 313      61.111  54.517  13.415  1.00  2.00           C  
ATOM   2344  CZ  PHE A 313      60.073  55.080  12.679  1.00  4.57           C  
ATOM   2345  N   SER A 314      61.865  48.186  11.232  1.00  9.67           N  
ATOM   2346  CA  SER A 314      62.554  46.986  10.758  1.00 11.25           C  
ATOM   2347  C   SER A 314      61.607  46.095   9.972  1.00 13.21           C  
ATOM   2348  O   SER A 314      62.001  45.482   8.971  1.00 16.14           O  
ATOM   2349  CB  SER A 314      63.168  46.212  11.919  1.00 11.41           C  
ATOM   2350  OG  SER A 314      62.195  45.828  12.874  1.00 19.52           O  
ATOM   2351  N   LEU A 315      60.352  46.064  10.412  1.00 12.05           N  
ATOM   2352  CA  LEU A 315      59.304  45.277   9.771  1.00 13.81           C  
ATOM   2353  C   LEU A 315      59.095  45.748   8.332  1.00 12.32           C  
ATOM   2354  O   LEU A 315      58.978  44.939   7.410  1.00 11.57           O  
ATOM   2355  CB  LEU A 315      58.009  45.427  10.568  1.00 15.01           C  
ATOM   2356  CG  LEU A 315      56.903  44.399  10.379  1.00 19.19           C  
ATOM   2357  CD1 LEU A 315      57.460  42.991  10.516  1.00 21.99           C  
ATOM   2358  CD2 LEU A 315      55.829  44.645  11.420  1.00 17.22           C  
ATOM   2359  N   ALA A 316      59.061  47.063   8.148  1.00 10.83           N  
ATOM   2360  CA  ALA A 316      58.879  47.648   6.831  1.00 11.39           C  
ATOM   2361  C   ALA A 316      60.060  47.345   5.927  1.00 18.53           C  
ATOM   2362  O   ALA A 316      59.886  47.074   4.739  1.00 26.49           O  
ATOM   2363  CB  ALA A 316      58.696  49.145   6.946  1.00 11.58           C  
ATOM   2364  N   ALA A 317      61.260  47.375   6.494  1.00 22.17           N  
ATOM   2365  CA  ALA A 317      62.478  47.128   5.735  1.00 21.53           C  
ATOM   2366  C   ALA A 317      62.729  45.678   5.346  1.00 24.02           C  
ATOM   2367  O   ALA A 317      63.026  45.392   4.181  1.00 25.81           O  
ATOM   2368  CB  ALA A 317      63.680  47.674   6.492  1.00 25.54           C  
ATOM   2369  N   GLU A 318      62.615  44.764   6.306  1.00 23.88           N  
ATOM   2370  CA  GLU A 318      62.887  43.354   6.043  1.00 24.30           C  
ATOM   2371  C   GLU A 318      61.899  42.372   6.666  1.00 23.53           C  
ATOM   2372  O   GLU A 318      62.245  41.209   6.882  1.00 31.24           O  
ATOM   2373  CB  GLU A 318      64.286  42.997   6.557  1.00 28.72           C  
ATOM   2374  CG  GLU A 318      65.418  43.891   6.075  1.00 31.55           C  
ATOM   2375  CD  GLU A 318      66.705  43.656   6.845  1.00 32.75           C  
ATOM   2376  OE1 GLU A 318      66.655  43.024   7.923  1.00 32.99           O  
ATOM   2377  OE2 GLU A 318      67.769  44.113   6.380  1.00 36.34           O  
ATOM   2378  N   GLY A 319      60.680  42.809   6.952  1.00 21.95           N  
ATOM   2379  CA  GLY A 319      59.717  41.902   7.553  1.00 17.83           C  
ATOM   2380  C   GLY A 319      60.279  41.248   8.807  1.00 19.60           C  
ATOM   2381  O   GLY A 319      61.082  41.864   9.524  1.00 13.14           O  
ATOM   2382  N   GLU A 320      59.917  39.983   9.032  1.00 13.32           N  
ATOM   2383  CA  GLU A 320      60.372  39.250  10.218  1.00 13.28           C  
ATOM   2384  C   GLU A 320      61.887  39.275  10.432  1.00 12.51           C  
ATOM   2385  O   GLU A 320      62.352  39.483  11.554  1.00 12.00           O  
ATOM   2386  CB  GLU A 320      59.883  37.809  10.170  1.00 12.58           C  
ATOM   2387  CG  GLU A 320      60.119  37.021  11.444  1.00 17.88           C  
ATOM   2388  CD  GLU A 320      59.590  35.600  11.344  1.00 23.19           C  
ATOM   2389  OE1 GLU A 320      58.482  35.420  10.793  1.00 30.50           O  
ATOM   2390  OE2 GLU A 320      60.279  34.666  11.798  1.00 23.46           O  
ATOM   2391  N   ALA A 321      62.653  39.085   9.360  1.00  7.96           N  
ATOM   2392  CA  ALA A 321      64.106  39.100   9.451  1.00  7.46           C  
ATOM   2393  C   ALA A 321      64.561  40.412  10.093  1.00 15.43           C  
ATOM   2394  O   ALA A 321      65.454  40.419  10.951  1.00 14.28           O  
ATOM   2395  CB  ALA A 321      64.711  38.959   8.080  1.00  3.31           C  
ATOM   2396  N   GLY A 322      63.915  41.511   9.697  1.00 14.59           N  
ATOM   2397  CA  GLY A 322      64.255  42.811  10.245  1.00 10.75           C  
ATOM   2398  C   GLY A 322      64.038  42.835  11.746  1.00 13.33           C  
ATOM   2399  O   GLY A 322      64.916  43.275  12.499  1.00 13.63           O  
ATOM   2400  N   VAL A 323      62.892  42.327  12.191  1.00 10.83           N  
ATOM   2401  CA  VAL A 323      62.572  42.302  13.613  1.00  9.88           C  
ATOM   2402  C   VAL A 323      63.554  41.395  14.358  1.00  8.07           C  
ATOM   2403  O   VAL A 323      64.023  41.736  15.441  1.00  9.91           O  
ATOM   2404  CB  VAL A 323      61.110  41.856  13.870  1.00  5.61           C  
ATOM   2405  CG1 VAL A 323      60.697  42.180  15.312  1.00  2.00           C  
ATOM   2406  CG2 VAL A 323      60.175  42.529  12.883  1.00  2.00           C  
ATOM   2407  N   LYS A 324      63.887  40.256  13.767  1.00 10.75           N  
ATOM   2408  CA  LYS A 324      64.844  39.354  14.395  1.00 16.83           C  
ATOM   2409  C   LYS A 324      66.192  40.067  14.502  1.00 14.19           C  
ATOM   2410  O   LYS A 324      66.885  39.966  15.518  1.00  8.61           O  
ATOM   2411  CB  LYS A 324      65.025  38.075  13.575  1.00 21.99           C  
ATOM   2412  CG  LYS A 324      63.864  37.111  13.623  1.00 29.41           C  
ATOM   2413  CD  LYS A 324      64.361  35.704  13.309  1.00 40.04           C  
ATOM   2414  CE  LYS A 324      63.224  34.717  13.105  1.00 42.84           C  
ATOM   2415  NZ  LYS A 324      62.295  34.640  14.269  1.00 46.82           N  
ATOM   2416  N   LYS A 325      66.546  40.801  13.453  1.00 12.03           N  
ATOM   2417  CA  LYS A 325      67.802  41.537  13.406  1.00 13.22           C  
ATOM   2418  C   LYS A 325      67.854  42.605  14.502  1.00 14.20           C  
ATOM   2419  O   LYS A 325      68.870  42.758  15.186  1.00 13.59           O  
ATOM   2420  CB  LYS A 325      67.976  42.166  12.024  1.00 17.40           C  
ATOM   2421  CG  LYS A 325      69.411  42.543  11.671  1.00 31.70           C  
ATOM   2422  CD  LYS A 325      69.589  42.699  10.155  1.00 39.59           C  
ATOM   2423  CE  LYS A 325      69.153  41.427   9.408  1.00 44.77           C  
ATOM   2424  NZ  LYS A 325      69.263  41.530   7.925  1.00 48.04           N  
ATOM   2425  N   VAL A 326      66.745  43.311  14.699  1.00 13.19           N  
ATOM   2426  CA  VAL A 326      66.678  44.354  15.721  1.00 13.02           C  
ATOM   2427  C   VAL A 326      66.863  43.754  17.116  1.00 13.05           C  
ATOM   2428  O   VAL A 326      67.630  44.273  17.929  1.00 14.25           O  
ATOM   2429  CB  VAL A 326      65.336  45.153  15.633  1.00 12.60           C  
ATOM   2430  CG1 VAL A 326      65.061  45.928  16.922  1.00  4.02           C  
ATOM   2431  CG2 VAL A 326      65.394  46.120  14.466  1.00  6.91           C  
ATOM   2432  N   LEU A 327      66.194  42.640  17.377  1.00 11.04           N  
ATOM   2433  CA  LEU A 327      66.292  41.994  18.675  1.00 14.28           C  
ATOM   2434  C   LEU A 327      67.686  41.419  18.951  1.00 17.90           C  
ATOM   2435  O   LEU A 327      68.179  41.484  20.080  1.00 21.55           O  
ATOM   2436  CB  LEU A 327      65.212  40.920  18.802  1.00 14.91           C  
ATOM   2437  CG  LEU A 327      63.780  41.448  18.942  1.00  7.79           C  
ATOM   2438  CD1 LEU A 327      62.787  40.322  18.750  1.00  9.57           C  
ATOM   2439  CD2 LEU A 327      63.605  42.092  20.312  1.00  6.69           C  
ATOM   2440  N   GLN A 328      68.332  40.881  17.920  1.00 17.22           N  
ATOM   2441  CA  GLN A 328      69.672  40.321  18.073  1.00 16.07           C  
ATOM   2442  C   GLN A 328      70.681  41.440  18.344  1.00 15.32           C  
ATOM   2443  O   GLN A 328      71.473  41.359  19.288  1.00 10.74           O  
ATOM   2444  CB  GLN A 328      70.084  39.548  16.820  1.00 16.78           C  
ATOM   2445  CG  GLN A 328      71.362  38.743  16.990  1.00 24.04           C  
ATOM   2446  CD  GLN A 328      71.262  37.709  18.107  1.00 30.18           C  
ATOM   2447  OE1 GLN A 328      70.474  36.765  18.026  1.00 33.61           O  
ATOM   2448  NE2 GLN A 328      72.049  37.892  19.159  1.00 26.93           N  
ATOM   2449  N   MET A 329      70.640  42.488  17.522  1.00 14.66           N  
ATOM   2450  CA  MET A 329      71.547  43.625  17.690  1.00 10.49           C  
ATOM   2451  C   MET A 329      71.450  44.168  19.105  1.00  9.82           C  
ATOM   2452  O   MET A 329      72.468  44.333  19.789  1.00  3.93           O  
ATOM   2453  CB  MET A 329      71.243  44.747  16.693  1.00  6.73           C  
ATOM   2454  CG  MET A 329      71.542  44.398  15.244  1.00  6.60           C  
ATOM   2455  SD  MET A 329      71.512  45.862  14.176  1.00 10.92           S  
ATOM   2456  CE  MET A 329      69.747  46.123  14.024  1.00  9.76           C  
ATOM   2457  N   MET A 330      70.225  44.397  19.568  1.00  7.60           N  
ATOM   2458  CA  MET A 330      70.051  44.923  20.910  1.00  9.68           C  
ATOM   2459  C   MET A 330      70.603  44.019  22.007  1.00 14.16           C  
ATOM   2460  O   MET A 330      71.284  44.515  22.900  1.00 15.83           O  
ATOM   2461  CB  MET A 330      68.601  45.301  21.182  1.00 12.37           C  
ATOM   2462  CG  MET A 330      68.092  46.427  20.299  1.00 13.98           C  
ATOM   2463  SD  MET A 330      66.791  47.347  21.100  1.00 13.63           S  
ATOM   2464  CE  MET A 330      67.729  48.033  22.459  1.00 14.66           C  
ATOM   2465  N   ARG A 331      70.361  42.706  21.941  1.00 17.31           N  
ATOM   2466  CA  ARG A 331      70.892  41.819  22.987  1.00 19.71           C  
ATOM   2467  C   ARG A 331      72.419  41.771  22.929  1.00 14.44           C  
ATOM   2468  O   ARG A 331      73.080  41.741  23.965  1.00  8.59           O  
ATOM   2469  CB  ARG A 331      70.308  40.398  22.921  1.00 18.23           C  
ATOM   2470  CG  ARG A 331      71.008  39.461  21.962  1.00 27.46           C  
ATOM   2471  CD  ARG A 331      70.584  38.014  22.186  1.00 35.28           C  
ATOM   2472  NE  ARG A 331      71.290  37.361  23.289  1.00 36.55           N  
ATOM   2473  CZ  ARG A 331      70.723  36.507  24.142  1.00 43.08           C  
ATOM   2474  NH1 ARG A 331      69.433  36.206  24.033  1.00 43.91           N  
ATOM   2475  NH2 ARG A 331      71.454  35.907  25.075  1.00 42.84           N  
ATOM   2476  N   ASP A 332      72.966  41.792  21.717  1.00 12.35           N  
ATOM   2477  CA  ASP A 332      74.411  41.772  21.529  1.00 13.82           C  
ATOM   2478  C   ASP A 332      75.021  43.014  22.161  1.00 13.87           C  
ATOM   2479  O   ASP A 332      75.977  42.928  22.938  1.00 14.09           O  
ATOM   2480  CB  ASP A 332      74.764  41.733  20.039  1.00 11.22           C  
ATOM   2481  CG  ASP A 332      74.534  40.369  19.418  1.00 17.15           C  
ATOM   2482  OD1 ASP A 332      74.473  39.377  20.171  1.00 23.12           O  
ATOM   2483  OD2 ASP A 332      74.420  40.276  18.177  1.00 17.54           O  
ATOM   2484  N   GLU A 333      74.438  44.169  21.854  1.00  8.66           N  
ATOM   2485  CA  GLU A 333      74.935  45.422  22.384  1.00  3.56           C  
ATOM   2486  C   GLU A 333      74.824  45.462  23.887  1.00  2.00           C  
ATOM   2487  O   GLU A 333      75.746  45.908  24.575  1.00  6.21           O  
ATOM   2488  CB  GLU A 333      74.212  46.607  21.745  1.00  2.00           C  
ATOM   2489  CG  GLU A 333      74.471  46.741  20.245  1.00  2.13           C  
ATOM   2490  CD  GLU A 333      73.842  47.986  19.641  1.00  2.00           C  
ATOM   2491  OE1 GLU A 333      73.503  48.912  20.402  1.00  4.48           O  
ATOM   2492  OE2 GLU A 333      73.698  48.042  18.401  1.00  2.00           O  
ATOM   2493  N   PHE A 334      73.724  44.938  24.402  1.00  4.07           N  
ATOM   2494  CA  PHE A 334      73.503  44.923  25.843  1.00 10.46           C  
ATOM   2495  C   PHE A 334      74.536  44.025  26.535  1.00 12.95           C  
ATOM   2496  O   PHE A 334      75.088  44.391  27.580  1.00 16.34           O  
ATOM   2497  CB  PHE A 334      72.072  44.460  26.155  1.00  6.93           C  
ATOM   2498  CG  PHE A 334      71.762  44.409  27.619  1.00  4.93           C  
ATOM   2499  CD1 PHE A 334      71.960  45.527  28.422  1.00  2.00           C  
ATOM   2500  CD2 PHE A 334      71.328  43.223  28.206  1.00  2.00           C  
ATOM   2501  CE1 PHE A 334      71.740  45.463  29.794  1.00  2.00           C  
ATOM   2502  CE2 PHE A 334      71.108  43.148  29.578  1.00  2.00           C  
ATOM   2503  CZ  PHE A 334      71.312  44.269  30.373  1.00  2.00           C  
ATOM   2504  N   GLU A 335      74.820  42.875  25.927  1.00 13.02           N  
ATOM   2505  CA  GLU A 335      75.782  41.924  26.468  1.00 12.12           C  
ATOM   2506  C   GLU A 335      77.160  42.553  26.555  1.00 15.72           C  
ATOM   2507  O   GLU A 335      77.799  42.535  27.607  1.00 16.90           O  
ATOM   2508  CB  GLU A 335      75.862  40.675  25.594  1.00 13.70           C  
ATOM   2509  CG  GLU A 335      76.855  39.643  26.123  1.00 19.62           C  
ATOM   2510  CD  GLU A 335      76.879  38.377  25.304  1.00 18.63           C  
ATOM   2511  OE1 GLU A 335      75.883  37.626  25.332  1.00 26.14           O  
ATOM   2512  OE2 GLU A 335      77.894  38.125  24.634  1.00 19.88           O  
ATOM   2513  N   LEU A 336      77.611  43.113  25.441  1.00 16.35           N  
ATOM   2514  CA  LEU A 336      78.913  43.754  25.386  1.00 14.41           C  
ATOM   2515  C   LEU A 336      79.011  44.894  26.403  1.00 14.77           C  
ATOM   2516  O   LEU A 336      80.100  45.168  26.927  1.00 15.88           O  
ATOM   2517  CB  LEU A 336      79.194  44.267  23.977  1.00 11.40           C  
ATOM   2518  CG  LEU A 336      80.476  45.081  23.785  1.00 14.77           C  
ATOM   2519  CD1 LEU A 336      81.708  44.275  24.198  1.00 12.72           C  
ATOM   2520  CD2 LEU A 336      80.557  45.526  22.330  1.00 13.32           C  
ATOM   2521  N   THR A 337      77.888  45.548  26.694  1.00  7.58           N  
ATOM   2522  CA  THR A 337      77.893  46.638  27.657  1.00  6.92           C  
ATOM   2523  C   THR A 337      78.087  46.078  29.051  1.00 10.23           C  
ATOM   2524  O   THR A 337      78.877  46.607  29.829  1.00 14.79           O  
ATOM   2525  CB  THR A 337      76.611  47.486  27.581  1.00 10.06           C  
ATOM   2526  OG1 THR A 337      76.510  48.083  26.279  1.00  7.87           O  
ATOM   2527  CG2 THR A 337      76.637  48.595  28.629  1.00  8.31           C  
ATOM   2528  N   MET A 338      77.402  44.978  29.349  1.00 14.99           N  
ATOM   2529  CA  MET A 338      77.525  44.330  30.655  1.00 12.74           C  
ATOM   2530  C   MET A 338      78.956  43.850  30.846  1.00  9.54           C  
ATOM   2531  O   MET A 338      79.552  44.049  31.908  1.00  4.15           O  
ATOM   2532  CB  MET A 338      76.569  43.143  30.752  1.00 13.22           C  
ATOM   2533  CG  MET A 338      75.150  43.529  31.100  1.00 14.99           C  
ATOM   2534  SD  MET A 338      74.069  42.094  31.159  1.00  6.44           S  
ATOM   2535  CE  MET A 338      74.400  41.499  32.764  1.00  9.68           C  
ATOM   2536  N   ALA A 339      79.499  43.247  29.792  1.00  7.05           N  
ATOM   2537  CA  ALA A 339      80.862  42.738  29.786  1.00  8.71           C  
ATOM   2538  C   ALA A 339      81.856  43.851  30.103  1.00 10.08           C  
ATOM   2539  O   ALA A 339      82.665  43.714  31.017  1.00 11.34           O  
ATOM   2540  CB  ALA A 339      81.183  42.126  28.429  1.00  7.94           C  
ATOM   2541  N   LEU A 340      81.774  44.959  29.367  1.00 11.17           N  
ATOM   2542  CA  LEU A 340      82.675  46.092  29.580  1.00  9.08           C  
ATOM   2543  C   LEU A 340      82.458  46.837  30.900  1.00  4.74           C  
ATOM   2544  O   LEU A 340      83.343  47.543  31.367  1.00 11.12           O  
ATOM   2545  CB  LEU A 340      82.620  47.057  28.391  1.00  7.47           C  
ATOM   2546  CG  LEU A 340      83.132  46.473  27.069  1.00  9.82           C  
ATOM   2547  CD1 LEU A 340      82.843  47.407  25.911  1.00  3.52           C  
ATOM   2548  CD2 LEU A 340      84.630  46.161  27.168  1.00 15.20           C  
ATOM   2549  N   SER A 341      81.283  46.692  31.493  1.00  9.96           N  
ATOM   2550  CA  SER A 341      80.988  47.338  32.768  1.00  9.24           C  
ATOM   2551  C   SER A 341      81.399  46.443  33.937  1.00 12.66           C  
ATOM   2552  O   SER A 341      81.527  46.914  35.072  1.00 16.14           O  
ATOM   2553  CB  SER A 341      79.499  47.678  32.862  1.00  7.49           C  
ATOM   2554  OG  SER A 341      79.096  48.475  31.761  1.00  8.01           O  
ATOM   2555  N   GLY A 342      81.585  45.154  33.654  1.00 12.08           N  
ATOM   2556  CA  GLY A 342      81.986  44.205  34.679  1.00  7.67           C  
ATOM   2557  C   GLY A 342      80.817  43.551  35.382  1.00  7.48           C  
ATOM   2558  O   GLY A 342      80.915  43.192  36.559  1.00  9.56           O  
ATOM   2559  N   CYS A 343      79.715  43.375  34.661  1.00  9.50           N  
ATOM   2560  CA  CYS A 343      78.509  42.768  35.218  1.00 10.22           C  
ATOM   2561  C   CYS A 343      78.194  41.433  34.560  1.00 14.15           C  
ATOM   2562  O   CYS A 343      77.897  41.372  33.367  1.00 12.34           O  
ATOM   2563  CB  CYS A 343      77.328  43.718  35.053  1.00  9.43           C  
ATOM   2564  SG  CYS A 343      77.658  45.366  35.695  1.00 14.40           S  
ATOM   2565  N   ARG A 344      78.241  40.368  35.353  1.00 18.93           N  
ATOM   2566  CA  ARG A 344      77.978  39.024  34.857  1.00 23.30           C  
ATOM   2567  C   ARG A 344      76.507  38.594  34.844  1.00 23.49           C  
ATOM   2568  O   ARG A 344      76.146  37.616  34.192  1.00 24.54           O  
ATOM   2569  CB  ARG A 344      78.831  38.006  35.614  1.00 26.69           C  
ATOM   2570  CG  ARG A 344      80.317  38.085  35.278  1.00 28.85           C  
ATOM   2571  CD  ARG A 344      80.997  39.210  36.035  1.00 31.55           C  
ATOM   2572  NE  ARG A 344      80.970  38.965  37.473  1.00 34.73           N  
ATOM   2573  CZ  ARG A 344      81.747  38.088  38.104  1.00 36.46           C  
ATOM   2574  NH1 ARG A 344      82.632  37.365  37.431  1.00 34.93           N  
ATOM   2575  NH2 ARG A 344      81.611  37.906  39.411  1.00 36.83           N  
ATOM   2576  N   SER A 345      75.660  39.325  35.554  1.00 18.77           N  
ATOM   2577  CA  SER A 345      74.237  39.013  35.590  1.00 17.53           C  
ATOM   2578  C   SER A 345      73.496  40.317  35.822  1.00 20.15           C  
ATOM   2579  O   SER A 345      74.111  41.321  36.204  1.00 20.15           O  
ATOM   2580  CB  SER A 345      73.927  38.014  36.710  1.00 12.67           C  
ATOM   2581  OG  SER A 345      74.182  38.568  37.997  1.00  8.69           O  
ATOM   2582  N   LEU A 346      72.186  40.312  35.606  1.00 17.83           N  
ATOM   2583  CA  LEU A 346      71.386  41.515  35.793  1.00 17.35           C  
ATOM   2584  C   LEU A 346      71.462  42.023  37.225  1.00 17.42           C  
ATOM   2585  O   LEU A 346      71.469  43.229  37.472  1.00 18.72           O  
ATOM   2586  CB  LEU A 346      69.934  41.250  35.421  1.00 15.90           C  
ATOM   2587  CG  LEU A 346      69.652  40.964  33.952  1.00 17.29           C  
ATOM   2588  CD1 LEU A 346      68.171  41.152  33.706  1.00 18.52           C  
ATOM   2589  CD2 LEU A 346      70.454  41.919  33.077  1.00 23.87           C  
ATOM   2590  N   LYS A 347      71.546  41.088  38.161  1.00 19.36           N  
ATOM   2591  CA  LYS A 347      71.622  41.396  39.581  1.00 21.89           C  
ATOM   2592  C   LYS A 347      72.893  42.182  39.902  1.00 18.70           C  
ATOM   2593  O   LYS A 347      72.965  42.879  40.911  1.00 15.57           O  
ATOM   2594  CB  LYS A 347      71.609  40.087  40.367  1.00 27.02           C  
ATOM   2595  CG  LYS A 347      71.301  40.196  41.847  1.00 38.75           C  
ATOM   2596  CD  LYS A 347      72.099  39.171  42.667  1.00 48.92           C  
ATOM   2597  CE  LYS A 347      72.206  37.788  41.998  1.00 53.30           C  
ATOM   2598  NZ  LYS A 347      73.307  37.692  40.977  1.00 54.23           N  
ATOM   2599  N   GLU A 348      73.905  42.048  39.052  1.00 20.46           N  
ATOM   2600  CA  GLU A 348      75.167  42.753  39.276  1.00 22.08           C  
ATOM   2601  C   GLU A 348      75.180  44.208  38.829  1.00 18.52           C  
ATOM   2602  O   GLU A 348      76.112  44.942  39.147  1.00 19.59           O  
ATOM   2603  CB  GLU A 348      76.321  42.018  38.612  1.00 18.99           C  
ATOM   2604  CG  GLU A 348      76.508  40.619  39.138  1.00 26.11           C  
ATOM   2605  CD  GLU A 348      77.886  40.072  38.866  1.00 26.80           C  
ATOM   2606  OE1 GLU A 348      78.735  40.797  38.306  1.00 23.33           O  
ATOM   2607  OE2 GLU A 348      78.124  38.907  39.235  1.00 37.86           O  
ATOM   2608  N   ILE A 349      74.183  44.615  38.052  1.00 18.71           N  
ATOM   2609  CA  ILE A 349      74.118  45.986  37.584  1.00 15.98           C  
ATOM   2610  C   ILE A 349      73.677  46.840  38.760  1.00 20.79           C  
ATOM   2611  O   ILE A 349      72.745  46.487  39.480  1.00 27.71           O  
ATOM   2612  CB  ILE A 349      73.131  46.123  36.432  1.00 14.82           C  
ATOM   2613  CG1 ILE A 349      73.606  45.277  35.248  1.00 12.36           C  
ATOM   2614  CG2 ILE A 349      72.972  47.583  36.045  1.00 13.90           C  
ATOM   2615  CD1 ILE A 349      72.676  45.322  34.048  1.00 13.67           C  
ATOM   2616  N   SER A 350      74.354  47.956  38.971  1.00 18.90           N  
ATOM   2617  CA  SER A 350      74.015  48.810  40.089  1.00 19.20           C  
ATOM   2618  C   SER A 350      74.050  50.277  39.722  1.00 17.78           C  
ATOM   2619  O   SER A 350      74.634  50.658  38.705  1.00 18.43           O  
ATOM   2620  CB  SER A 350      74.972  48.544  41.246  1.00 25.10           C  
ATOM   2621  OG  SER A 350      76.322  48.737  40.841  1.00 38.16           O  
ATOM   2622  N   ARG A 351      73.460  51.095  40.586  1.00 17.41           N  
ATOM   2623  CA  ARG A 351      73.408  52.539  40.408  1.00 13.76           C  
ATOM   2624  C   ARG A 351      74.822  53.139  40.335  1.00  8.81           C  
ATOM   2625  O   ARG A 351      75.053  54.141  39.672  1.00 11.49           O  
ATOM   2626  CB  ARG A 351      72.647  53.153  41.582  1.00 17.86           C  
ATOM   2627  CG  ARG A 351      71.572  54.150  41.184  1.00 22.91           C  
ATOM   2628  CD  ARG A 351      72.173  55.309  40.431  1.00 21.21           C  
ATOM   2629  NE  ARG A 351      71.270  56.445  40.350  1.00 22.85           N  
ATOM   2630  CZ  ARG A 351      71.625  57.628  39.865  1.00 25.10           C  
ATOM   2631  NH1 ARG A 351      72.857  57.816  39.426  1.00 25.81           N  
ATOM   2632  NH2 ARG A 351      70.745  58.616  39.803  1.00 32.04           N  
ATOM   2633  N   SER A 352      75.769  52.498  41.005  1.00 11.79           N  
ATOM   2634  CA  SER A 352      77.155  52.953  41.035  1.00 13.60           C  
ATOM   2635  C   SER A 352      77.908  52.708  39.733  1.00 11.94           C  
ATOM   2636  O   SER A 352      79.036  53.173  39.569  1.00 11.03           O  
ATOM   2637  CB  SER A 352      77.890  52.292  42.195  1.00 15.93           C  
ATOM   2638  OG  SER A 352      77.121  52.388  43.382  1.00 25.27           O  
ATOM   2639  N   HIS A 353      77.299  51.952  38.827  1.00  8.97           N  
ATOM   2640  CA  HIS A 353      77.915  51.663  37.538  1.00 11.51           C  
ATOM   2641  C   HIS A 353      77.539  52.767  36.556  1.00 12.67           C  
ATOM   2642  O   HIS A 353      77.979  52.767  35.403  1.00 15.84           O  
ATOM   2643  CB  HIS A 353      77.392  50.337  36.979  1.00 12.01           C  
ATOM   2644  CG  HIS A 353      78.073  49.126  37.529  1.00 11.46           C  
ATOM   2645  ND1 HIS A 353      77.554  48.388  38.566  1.00 14.61           N  
ATOM   2646  CD2 HIS A 353      79.213  48.500  37.151  1.00 13.10           C  
ATOM   2647  CE1 HIS A 353      78.342  47.354  38.807  1.00 18.21           C  
ATOM   2648  NE2 HIS A 353      79.355  47.402  37.964  1.00 16.48           N  
ATOM   2649  N   ILE A 354      76.728  53.706  37.025  1.00 15.98           N  
ATOM   2650  CA  ILE A 354      76.234  54.787  36.190  1.00 16.05           C  
ATOM   2651  C   ILE A 354      76.465  56.147  36.866  1.00 16.73           C  
ATOM   2652  O   ILE A 354      76.723  56.218  38.074  1.00 12.19           O  
ATOM   2653  CB  ILE A 354      74.716  54.529  35.884  1.00 17.25           C  
ATOM   2654  CG1 ILE A 354      74.423  54.736  34.407  1.00 19.91           C  
ATOM   2655  CG2 ILE A 354      73.795  55.362  36.779  1.00 19.46           C  
ATOM   2656  CD1 ILE A 354      74.997  53.667  33.535  1.00 22.39           C  
ATOM   2657  N   ALA A 355      76.393  57.214  36.074  1.00 17.25           N  
ATOM   2658  CA  ALA A 355      76.586  58.578  36.569  1.00 21.37           C  
ATOM   2659  C   ALA A 355      75.707  59.524  35.765  1.00 22.75           C  
ATOM   2660  O   ALA A 355      75.961  59.782  34.588  1.00 21.46           O  
ATOM   2661  CB  ALA A 355      78.049  58.986  36.445  1.00 20.54           C  
ATOM   2662  N   ALA A 356      74.664  60.037  36.402  1.00 27.63           N  
ATOM   2663  CA  ALA A 356      73.733  60.933  35.732  1.00 29.07           C  
ATOM   2664  C   ALA A 356      74.117  62.398  35.844  1.00 30.34           C  
ATOM   2665  O   ALA A 356      74.677  62.830  36.851  1.00 23.34           O  
ATOM   2666  CB  ALA A 356      72.337  60.716  36.270  1.00 27.84           C  
ATOM   2667  N   ASP A 357      73.784  63.160  34.806  1.00 34.07           N  
ATOM   2668  CA  ASP A 357      74.073  64.589  34.768  1.00 38.43           C  
ATOM   2669  C   ASP A 357      73.395  65.321  35.903  1.00 38.60           C  
ATOM   2670  O   ASP A 357      73.757  66.447  36.213  1.00 44.69           O  
ATOM   2671  CB  ASP A 357      73.628  65.200  33.437  1.00 44.56           C  
ATOM   2672  CG  ASP A 357      74.752  65.267  32.408  1.00 50.57           C  
ATOM   2673  OD1 ASP A 357      75.630  64.373  32.392  1.00 55.22           O  
ATOM   2674  OD2 ASP A 357      74.753  66.222  31.603  1.00 52.86           O  
ATOM   2675  N   TRP A 358      72.400  64.688  36.510  1.00 40.02           N  
ATOM   2676  CA  TRP A 358      71.672  65.297  37.613  1.00 39.65           C  
ATOM   2677  C   TRP A 358      72.127  64.795  38.982  1.00 42.52           C  
ATOM   2678  O   TRP A 358      71.420  64.963  39.974  1.00 44.65           O  
ATOM   2679  CB  TRP A 358      70.177  65.050  37.441  1.00 37.56           C  
ATOM   2680  CG  TRP A 358      69.782  63.603  37.484  1.00 36.54           C  
ATOM   2681  CD1 TRP A 358      69.488  62.862  38.599  1.00 37.40           C  
ATOM   2682  CD2 TRP A 358      69.540  62.748  36.366  1.00 33.10           C  
ATOM   2683  NE1 TRP A 358      69.063  61.611  38.240  1.00 35.21           N  
ATOM   2684  CE2 TRP A 358      69.083  61.511  36.872  1.00 34.75           C  
ATOM   2685  CE3 TRP A 358      69.659  62.906  34.980  1.00 33.62           C  
ATOM   2686  CZ2 TRP A 358      68.738  60.441  36.046  1.00 34.96           C  
ATOM   2687  CZ3 TRP A 358      69.318  61.843  34.157  1.00 34.06           C  
ATOM   2688  CH2 TRP A 358      68.863  60.626  34.694  1.00 37.15           C  
ATOM   2689  N   ASP A 359      73.280  64.143  39.024  1.00 49.27           N  
ATOM   2690  CA  ASP A 359      73.819  63.619  40.273  1.00 56.64           C  
ATOM   2691  C   ASP A 359      74.651  64.675  40.990  1.00 62.90           C  
ATOM   2692  O   ASP A 359      74.812  64.550  42.224  1.00 65.44           O  
ATOM   2693  CB  ASP A 359      74.688  62.383  40.015  1.00 55.07           C  
ATOM   2694  CG  ASP A 359      73.873  61.145  39.691  1.00 51.95           C  
ATOM   2695  OD1 ASP A 359      72.632  61.234  39.581  1.00 53.98           O  
ATOM   2696  OD2 ASP A 359      74.489  60.070  39.554  1.00 48.78           O  
ATOM   2697  OXT ASP A 359      75.151  65.600  40.308  1.00 66.51           O  
TER    2698      ASP A 359                                                      
HETATM 2699  N1  FMN A 360      50.791  52.528  22.961  1.00  2.00           N  
HETATM 2700  C2  FMN A 360      49.726  51.780  23.428  1.00  5.42           C  
HETATM 2701  O2  FMN A 360      49.473  51.741  24.627  1.00  2.80           O  
HETATM 2702  N3  FMN A 360      49.000  51.120  22.435  1.00  2.70           N  
HETATM 2703  C4  FMN A 360      49.244  51.218  21.063  1.00  6.24           C  
HETATM 2704  O4  FMN A 360      48.533  50.569  20.298  1.00  3.45           O  
HETATM 2705  C4A FMN A 360      50.304  52.130  20.706  1.00  2.00           C  
HETATM 2706  N5  FMN A 360      50.476  52.275  19.355  1.00  3.88           N  
HETATM 2707  C5A FMN A 360      51.528  53.018  18.924  1.00  4.57           C  
HETATM 2708  C6  FMN A 360      51.713  53.094  17.580  1.00  3.69           C  
HETATM 2709  C7  FMN A 360      52.847  53.681  17.086  1.00  2.00           C  
HETATM 2710  C7M FMN A 360      52.989  53.866  15.596  1.00  2.00           C  
HETATM 2711  C8  FMN A 360      53.803  54.180  17.952  1.00  6.73           C  
HETATM 2712  C8M FMN A 360      55.040  54.866  17.397  1.00  7.57           C  
HETATM 2713  C9  FMN A 360      53.614  54.112  19.318  1.00  2.49           C  
HETATM 2714  C9A FMN A 360      52.465  53.541  19.811  1.00  4.51           C  
HETATM 2715  N10 FMN A 360      52.272  53.421  21.178  1.00  8.09           N  
HETATM 2716  C10 FMN A 360      51.140  52.754  21.626  1.00  3.71           C  
HETATM 2717  C1' FMN A 360      53.277  53.717  22.026  1.00 10.41           C  
HETATM 2718  C2' FMN A 360      53.874  52.553  22.824  1.00 10.60           C  
HETATM 2719  O2' FMN A 360      53.812  51.301  22.194  1.00 15.36           O  
HETATM 2720  C3' FMN A 360      55.241  52.726  23.366  1.00  9.77           C  
HETATM 2721  O3' FMN A 360      55.192  53.563  24.492  1.00 12.49           O  
HETATM 2722  C4' FMN A 360      56.400  53.015  22.358  1.00 11.97           C  
HETATM 2723  O4' FMN A 360      56.093  53.645  21.150  1.00  2.00           O  
HETATM 2724  C5' FMN A 360      57.774  53.279  23.050  1.00 11.60           C  
HETATM 2725  O5' FMN A 360      58.644  54.194  22.505  1.00  5.13           O  
HETATM 2726  P   FMN A 360      59.584  54.025  21.254  1.00 15.96           P  
HETATM 2727  O1P FMN A 360      60.394  55.239  21.440  1.00 13.36           O  
HETATM 2728  O2P FMN A 360      58.749  54.042  20.048  1.00 11.12           O  
HETATM 2729  O3P FMN A 360      60.289  52.776  21.460  1.00 16.10           O  
HETATM 2730  N1  HST A 361      47.018  53.092  19.948  1.00 13.94           N  
HETATM 2731  N2  HST A 361      47.488  53.656  21.075  1.00 14.80           N  
HETATM 2732  N3  HST A 361      48.228  54.735  20.770  1.00 12.41           N  
HETATM 2733  CB1 HST A 361      47.468  53.840  18.892  1.00 13.98           C  
HETATM 2734  CB2 HST A 361      48.241  54.874  19.395  1.00 13.63           C  
HETATM 2735  CB3 HST A 361      49.230  55.783  18.668  1.00 12.71           C  
HETATM 2736  O1  HST A 361      49.940  56.593  19.247  1.00 17.69           O  
HETATM 2737  O2  HST A 361      49.057  55.832  17.322  1.00  7.68           O  
HETATM 2738  S   HST A 361      46.756  53.876  17.299  1.00 23.80           S  
HETATM 2739  C1  HST A 361      44.243  58.389  13.633  1.00 47.81           C  
HETATM 2740  C2  HST A 361      45.068  57.101  13.782  1.00 49.29           C  
HETATM 2741  C3  HST A 361      44.728  56.279  15.039  1.00 45.60           C  
HETATM 2742  C4  HST A 361      44.849  57.074  16.357  1.00 41.12           C  
HETATM 2743  C5  HST A 361      45.497  56.262  17.491  1.00 31.19           C  
HETATM 2744  C6  HST A 361      45.182  54.754  17.480  1.00 28.97           C  
HETATM 2745  C7  HST A 361      44.467  54.198  18.740  1.00 35.16           C  
HETATM 2746  C8  HST A 361      44.222  55.243  19.846  1.00 40.15           C  
HETATM 2747  C9  HST A 361      42.750  55.287  20.290  1.00 42.16           C  
HETATM 2748  C10 HST A 361      42.545  55.011  21.789  1.00 47.52           C  
HETATM 2749  C11 HST A 361      41.378  54.059  22.095  1.00 50.72           C  
HETATM 2750  O   HOH A 362      50.784  45.103  19.034  1.00 11.19           O  
HETATM 2751  O   HOH A 363      61.539  52.356  23.722  1.00  2.00           O  
HETATM 2752  O   HOH A 364      87.850  45.492  39.498  1.00 10.03           O  
HETATM 2753  O   HOH A 365      55.362  71.291  21.549  1.00  4.63           O  
HETATM 2754  O   HOH A 366      63.813  58.149  27.848  1.00  2.00           O  
HETATM 2755  O   HOH A 367      52.585  59.687  28.920  1.00  9.68           O  
HETATM 2756  O   HOH A 368      71.553  56.068  22.819  1.00  2.00           O  
HETATM 2757  O   HOH A 369      74.067  46.160  16.550  1.00 25.28           O  
HETATM 2758  O   HOH A 370      57.325  56.606  26.164  1.00  2.00           O  
HETATM 2759  O   HOH A 371      55.058  36.115  20.119  1.00  2.00           O  
HETATM 2760  O   HOH A 372      72.542  54.693  16.339  1.00 15.64           O  
HETATM 2761  O   HOH A 373      84.920  44.737  32.499  1.00  2.00           O  
HETATM 2762  O   HOH A 374      51.372  34.150  26.136  1.00 43.73           O  
HETATM 2763  O   HOH A 375      58.168  34.110  24.693  1.00 15.00           O  
HETATM 2764  O   HOH A 376      75.855  52.910  22.497  1.00 10.16           O  
HETATM 2765  O   HOH A 377      60.848  58.649  15.556  1.00 23.09           O  
HETATM 2766  O   HOH A 378      62.352  59.084  20.816  1.00 23.69           O  
HETATM 2767  O   HOH A 379      67.243  36.960  22.781  1.00 30.99           O  
HETATM 2768  O   HOH A 380      51.935  61.857  27.597  1.00 17.31           O  
HETATM 2769  O   HOH A 381      73.325  55.220  25.832  1.00 18.84           O  
HETATM 2770  O   HOH A 382      57.756  58.216   3.888  1.00 26.09           O  
HETATM 2771  O   HOH A 383      51.124  68.425  23.874  1.00  6.81           O  
HETATM 2772  O   HOH A 384      65.648  58.790  36.213  1.00 11.72           O  
HETATM 2773  O   HOH A 385      71.343  49.822  17.827  1.00 25.02           O  
HETATM 2774  O   HOH A 386      66.710  67.281  23.634  1.00 37.57           O  
HETATM 2775  O   HOH A 387      40.370  59.193  32.135  1.00  8.84           O  
HETATM 2776  O   HOH A 388      43.953  43.401   8.829  1.00 19.59           O  
HETATM 2777  O   HOH A 389      74.882  49.639  22.923  1.00  6.97           O  
HETATM 2778  O   HOH A 390      52.087  60.656  35.971  1.00 12.98           O  
HETATM 2779  O   HOH A 391      51.496  61.248  30.769  1.00 37.19           O  
HETATM 2780  O   HOH A 392      64.418  67.835  22.641  1.00 41.00           O  
HETATM 2781  O   HOH A 393      42.000  53.082  28.736  1.00 33.37           O  
HETATM 2782  O   HOH A 395      47.766  70.788  22.920  1.00 19.45           O  
HETATM 2783  O   HOH A 396      52.024  54.850  26.970  1.00  4.87           O  
HETATM 2784  O   HOH A 397      53.597  62.592  25.131  1.00  7.58           O  
HETATM 2785  O   HOH A 398      60.007  57.949  21.735  1.00 18.29           O  
HETATM 2786  O   HOH A 399      70.944  52.384  16.929  1.00 35.70           O  
HETATM 2787  O   HOH A 400      78.635  41.157  21.780  1.00 39.90           O  
HETATM 2788  O   HOH A 401      60.604  48.179  41.272  1.00  2.00           O  
HETATM 2789  O   HOH A 402      87.309  45.608  31.334  1.00 42.23           O  
HETATM 2790  O   HOH A 403      89.657  43.794  32.130  1.00 14.81           O  
HETATM 2791  O   HOH A 404      79.099  50.721  33.538  1.00 44.96           O  
HETATM 2792  O   HOH A 405      54.615  65.584  12.925  1.00 28.30           O  
HETATM 2793  O   HOH A 406      41.366  55.852  27.621  1.00 29.74           O  
HETATM 2794  O   HOH A 407      65.070  54.653  15.635  1.00 32.56           O  
HETATM 2795  O   HOH A 409      48.098  57.906  22.458  1.00109.91           O  
HETATM 2796  O   HOH A 410      53.842  41.712  40.467  1.00 23.11           O  
HETATM 2797  O   HOH A 411      49.566  33.679  23.700  1.00 32.59           O  
HETATM 2798  O   HOH A 412      53.424  66.698  15.381  1.00 12.43           O  
HETATM 2799  O   HOH A 413      45.146  39.528  10.092  1.00 17.97           O  
HETATM 2800  O   HOH A 414      29.562  49.291  20.853  1.00 56.00           O  
HETATM 2801  O   HOH A 415      51.434  60.411  33.371  1.00 44.47           O  
HETATM 2802  O   HOH A 416      62.086  66.074  17.279  1.00 16.76           O  
HETATM 2803  O   HOH A 417      55.376  49.098  26.111  1.00 15.97           O  
HETATM 2804  O   HOH A 418      79.165  48.386  24.759  1.00  4.24           O  
HETATM 2805  O   HOH A 420      46.522  43.168  39.053  1.00 13.07           O  
HETATM 2806  O   HOH A 421      77.051  62.698  34.486  1.00 46.81           O  
HETATM 2807  O   HOH A 422      38.983  54.612  26.620  1.00 19.75           O  
HETATM 2808  O   HOH A 423      66.616  37.600  17.900  1.00 21.02           O  
HETATM 2809  O   HOH A 424      86.099  48.714  31.247  1.00 19.45           O  
HETATM 2810  O   HOH A 425      76.527  34.772  35.557  1.00 30.44           O  
HETATM 2811  O   HOH A 426      42.237  44.624  16.460  1.00 19.16           O  
HETATM 2812  O   HOH A 427      64.736  48.398  41.012  1.00 30.46           O  
HETATM 2813  O   HOH A 428      87.806  41.178  39.975  1.00 13.01           O  
HETATM 2814  O   HOH A 429      50.379  60.467   8.632  1.00  2.00           O  
HETATM 2815  O   HOH A 430      49.066  66.836  22.154  1.00 24.57           O  
HETATM 2816  O   HOH A 431      40.795  62.351  21.619  1.00 59.14           O  
HETATM 2817  O   HOH A 432      63.600  65.101  29.962  1.00 22.24           O  
HETATM 2818  O   HOH A 433      60.929  50.062  43.497  1.00 33.16           O  
HETATM 2819  O   HOH A 434      61.575  47.794  38.743  1.00  3.65           O  
HETATM 2820  O   HOH A 435      70.280  37.740  35.487  1.00  3.60           O  
HETATM 2821  O   HOH A 436      86.131  38.794  38.684  1.00 28.39           O  
HETATM 2822  O   HOH A 437      56.053  36.327  22.683  1.00 18.61           O  
HETATM 2823  O   HOH A 438      58.495  38.606   6.540  1.00 44.86           O  
HETATM 2824  O   HOH A 439      62.992  59.247  18.273  1.00 35.23           O  
HETATM 2825  O   HOH A 440      29.983  41.799  29.733  1.00 28.18           O  
HETATM 2826  O   HOH A 441      44.032  64.717  17.592  1.00 25.44           O  
HETATM 2827  O   HOH A 442      59.078  51.666  -1.714  1.00 27.74           O  
HETATM 2828  O   HOH A 443      56.399  73.932  21.475  1.00  2.69           O  
HETATM 2829  O   HOH A 444      72.046  35.255  29.084  1.00 22.51           O  
HETATM 2830  O   HOH A 445      61.192  70.747  19.397  1.00 46.05           O  
HETATM 2831  O   HOH A 446      71.489  58.867  23.221  1.00 21.12           O  
HETATM 2832  O   HOH A 447      28.818  45.212  22.450  1.00 28.94           O  
HETATM 2833  O   HOH A 448      64.514  52.336  14.024  1.00  5.47           O  
HETATM 2834  O   HOH A 449      78.727  35.698  27.640  1.00 32.49           O  
HETATM 2835  O   HOH A 450      68.860  51.474  41.072  1.00 34.00           O  
HETATM 2836  O   HOH A 451      40.919  33.523  21.850  1.00 38.37           O  
HETATM 2837  O   HOH A 452      69.925  45.951  39.302  1.00 61.19           O  
HETATM 2838  O   HOH A 453      44.423  56.154  28.528  1.00 39.51           O  
HETATM 2839  O   HOH A 454      75.009  43.685  16.962  1.00 22.77           O  
HETATM 2840  O   HOH A 455      78.415  65.160  32.581  1.00 44.89           O  
HETATM 2841  O   HOH A 456      59.450  31.407  15.420  1.00 30.77           O  
HETATM 2842  O   HOH A 457      58.705  55.746  -0.048  1.00 38.34           O  
HETATM 2843  O   HOH A 458      65.721  58.341   4.921  1.00 40.02           O  
HETATM 2844  O   HOH A 459      30.572  53.448  31.205  1.00 48.43           O  
HETATM 2845  O   HOH A 460      80.835  51.242  38.960  1.00  9.44           O  
HETATM 2846  O   HOH A 461      66.087  63.770  36.768  1.00 49.62           O  
HETATM 2847  O   HOH A 462      45.050  30.330  18.397  1.00 62.18           O  
HETATM 2848  O   HOH A 463      69.613  34.419  27.832  1.00 29.87           O  
HETATM 2849  O   HOH A 464      86.851  42.712  32.995  1.00 24.14           O  
HETATM 2850  O   HOH A 465      49.281  62.045  28.492  1.00 29.15           O  
HETATM 2851  O   HOH A 466      57.980  62.091   5.709  1.00 27.86           O  
HETATM 2852  O   HOH A 467      55.377  32.929  17.552  1.00 23.64           O  
HETATM 2853  O   HOH A 468      46.081  32.857  29.901  1.00 44.78           O  
HETATM 2854  O   HOH A 469      34.047  55.824  34.088  1.00 51.48           O  
HETATM 2855  O   HOH A 470      72.947  34.748  37.381  1.00 46.50           O  
HETATM 2856  O   HOH A 471      60.535  73.121  20.740  1.00 26.82           O  
HETATM 2857  O   HOH A 472      63.092  45.842  40.435  1.00 69.29           O  
HETATM 2858  O   HOH A 473      56.793  30.547  15.897  1.00 40.47           O  
HETATM 2859  O   HOH A 474      67.230  46.589  37.767  1.00  8.91           O  
HETATM 2860  O   HOH A 475      71.742  49.515  42.569  1.00 23.99           O  
HETATM 2861  O   HOH A 476      64.312  35.893  16.961  1.00 25.69           O  
HETATM 2862  O   HOH A 477      81.155  45.359  38.132  1.00 16.83           O  
HETATM 2863  O   HOH A 478      81.883  35.104  34.047  1.00 28.14           O  
HETATM 2864  O   HOH A 479      74.699  54.628  11.578  1.00 36.30           O  
HETATM 2865  O   HOH A 480      40.948  35.906  13.326  1.00 46.43           O  
HETATM 2866  O   HOH A 481      64.671  42.304  36.442  1.00 12.48           O  
HETATM 2867  O   HOH A 482      46.408  61.102  14.050  1.00 28.00           O  
HETATM 2868  O   HOH A 483      56.929  46.732   3.217  1.00 53.75           O  
HETATM 2869  O   HOH A 484      59.859  59.044  44.713  1.00 53.84           O  
HETATM 2870  O   HOH A 485      54.683  67.235   8.734  1.00 61.91           O  
HETATM 2871  O   HOH A 486      56.816  43.603   1.856  1.00 89.80           O  
HETATM 2872  O   HOH A 487      63.941  59.155   2.907  1.00 91.48           O  
HETATM 2873  O   HOH A 488      81.735  37.552  27.396  1.00 31.81           O  
HETATM 2874  O   HOH A 489      67.075  37.708  10.553  1.00 37.06           O  
HETATM 2875  O   HOH A 490      53.588  45.225  19.239  1.00 11.42           O  
HETATM 2876  O   HOH A 491      38.283  61.002  23.364  1.00 58.50           O  
HETATM 2877  O   HOH A 492      56.249  47.560  18.551  1.00 18.40           O  
HETATM 2878  O   HOH A 493      68.341  52.689  43.576  1.00 58.53           O  
HETATM 2879  O   HOH A 494      62.739  56.601  16.011  1.00 79.99           O  
HETATM 2880  O   HOH A 495      50.310  46.419  43.818  1.00 35.58           O  
HETATM 2881  O   HOH A 496      68.000  40.590  38.237  1.00 40.61           O  
HETATM 2882  O   HOH A 497      40.101  35.988  35.006  1.00 40.50           O  
HETATM 2883  O   HOH A 498      72.491  31.951  30.598  1.00 36.20           O  
HETATM 2884  O   HOH A 499      87.913  32.609  30.036  1.00 39.06           O  
HETATM 2885  O   HOH A 500      46.392  64.170  16.075  1.00 18.29           O  
HETATM 2886  O   HOH A 501      36.742  60.030  21.138  1.00 54.37           O  
HETATM 2887  O   HOH A 502      38.528  38.356  13.822  1.00 87.51           O  
HETATM 2888  O   HOH A 503      30.450  58.884  31.941  1.00 47.44           O  
HETATM 2889  O   HOH A 504      54.410  29.933  33.870  1.00 66.17           O  
HETATM 2890  O   HOH A 505      67.102  62.438  19.158  1.00 29.52           O  
HETATM 2891  O   HOH A 506      54.068  67.907  11.582  1.00 69.81           O  
HETATM 2892  O   HOH A 507      52.163  46.066  46.913  1.00 52.30           O  
HETATM 2893  O   HOH A 508      31.042  51.129  34.091  1.00 79.67           O  
HETATM 2894  O   HOH A 509      49.730  45.718  16.632  1.00 17.25           O  
HETATM 2895  O   HOH A 510      34.128  37.089  24.241  1.00 55.19           O  
HETATM 2896  O   HOH A 511      74.291  37.786  22.495  1.00 20.11           O  
HETATM 2897  O   HOH A 512      29.045  48.492  28.034  1.00 49.95           O  
HETATM 2898  O   HOH A 513      56.199  55.940  48.909  1.00 44.79           O  
HETATM 2899  O   HOH A 514      71.628  54.812   7.427  1.00 51.72           O  
HETATM 2900  O   HOH A 515      49.732  35.354  34.461  1.00 44.36           O  
HETATM 2901  O   HOH A 516      29.393  53.094  20.136  1.00 85.50           O  
HETATM 2902  O   HOH A 517      59.683  75.543  18.443  1.00100.65           O  
HETATM 2903  O   HOH A 518      28.738  50.066  30.775  1.00 35.88           O  
HETATM 2904  O   HOH A 519      56.916  27.466  33.796  1.00113.79           O  
HETATM 2905  O   HOH A 520      73.505  40.996  15.792  1.00 27.42           O  
HETATM 2906  O   HOH A 521      50.387  50.474   3.545  1.00 54.83           O  
HETATM 2907  O   HOH A 522      40.350  51.295  43.636  1.00 84.73           O  
HETATM 2908  O   HOH A 523      61.751  29.287  29.689  1.00 74.72           O  
HETATM 2909  O   HOH A 524      38.435  45.395  42.744  1.00 45.81           O  
HETATM 2910  O   HOH A 525      74.212  33.030  28.825  1.00 69.05           O  
HETATM 2911  O   HOH A 526      65.462  46.230   2.947  1.00 49.58           O  
HETATM 2912  O   HOH A 527      41.182  40.520  41.414  1.00 30.36           O  
HETATM 2913  O   HOH A 528      46.523  41.214   5.611  1.00 56.72           O  
HETATM 2914  O   HOH A 529      43.701  41.448  38.435  1.00 23.79           O  
HETATM 2915  O   HOH A 530      38.335  59.471   6.679  1.00 75.28           O  
HETATM 2916  O   HOH A 531      58.612  30.501  30.644  1.00 58.03           O  
HETATM 2917  O   HOH A 532      59.242  44.575  42.038  1.00 86.27           O  
HETATM 2918  O   HOH A 533      81.540  58.758  34.663  1.00 75.21           O  
HETATM 2919  O   HOH A 534      31.768  54.589  19.710  1.00 66.15           O  
HETATM 2920  O   HOH A 535      63.722  61.929  17.880  1.00 48.41           O  
HETATM 2921  O   HOH A 536      63.217  51.403  46.172  1.00 69.18           O  
HETATM 2922  O   HOH A 537      73.891  36.029  27.154  1.00 41.07           O  
HETATM 2923  O   HOH A 538      68.730  57.914   5.039  1.00100.39           O  
HETATM 2924  O   HOH A 539      78.945  65.970  29.915  1.00 46.89           O  
HETATM 2925  O   HOH A 540      49.787  47.455  48.112  1.00 97.23           O  
HETATM 2926  O   HOH A 541      76.812  32.107  30.361  1.00 99.39           O  
HETATM 2927  O   HOH A 542      57.334  63.457  11.940  1.00 49.86           O  
HETATM 2928  O   HOH A 543      52.429  66.697   6.098  1.00 43.88           O  
HETATM 2929  O   HOH A 544      54.585  42.383  42.977  1.00 50.04           O  
HETATM 2930  O   HOH A 545      60.112  63.015   7.228  1.00 70.75           O  
HETATM 2931  O   HOH A 546      59.952  32.179  25.352  1.00 82.11           O  
HETATM 2932  O   HOH A 548      61.891  28.645  35.769  1.00 68.60           O  
HETATM 2933  O   HOH A 549      40.142  62.165   4.200  1.00 78.12           O  
HETATM 2934  O   HOH A 551      43.563  60.682   2.678  1.00 35.70           O  
HETATM 2935  O   HOH A 552      85.182  47.818  44.272  1.00 36.72           O  
HETATM 2936  O   HOH A 553      69.740  57.965  13.378  1.00 94.08           O  
HETATM 2937  O   HOH A 554      29.291  48.519  34.256  1.00 76.77           O  
HETATM 2938  O   HOH A 555      66.683  66.966  37.116  1.00114.34           O  
HETATM 2939  O   HOH A 556      31.784  60.866  33.497  1.00 86.40           O  
HETATM 2940  O   HOH A 557      39.926  53.936   6.456  1.00 66.05           O  
HETATM 2941  O   HOH A 558      35.489  59.092  37.573  1.00 37.32           O  
HETATM 2942  O   HOH A 559      43.002  56.878  45.407  1.00 30.21           O  
HETATM 2943  O   HOH A 560      31.623  56.333  31.375  1.00 54.01           O  
HETATM 2944  O   HOH A 561      35.024  50.604  41.522  1.00 70.24           O  
HETATM 2945  O   HOH A 562      60.503  66.137  14.921  1.00111.49           O  
HETATM 2946  O   HOH A 563      63.559  60.503  38.465  1.00 39.76           O  
HETATM 2947  O   HOH A 564      61.227  62.061  10.210  1.00 73.83           O  
HETATM 2948  O   HOH A 565      57.663  40.649  37.987  1.00 49.96           O  
HETATM 2949  O   HOH A 566      72.062  51.134   5.039  1.00 66.38           O  
HETATM 2950  O   HOH A 567      42.379  70.303  19.126  1.00 88.10           O  
HETATM 2951  O   HOH A 568      64.806  62.926  45.783  1.00 41.88           O  
HETATM 2952  O   HOH A 569      67.497  54.065  41.537  1.00 26.70           O  
HETATM 2953  O   HOH A 570      69.924  54.901   4.477  1.00 90.14           O  
HETATM 2954  O   HOH A 571      62.952  64.356  40.887  1.00127.38           O  
HETATM 2955  O   HOH A 572      65.110  31.358  29.580  1.00 43.16           O  
HETATM 2956  O   HOH A 573      32.609  41.610  13.050  1.00 50.20           O  
HETATM 2957  O   HOH A 574      59.809  44.205   4.176  1.00 69.87           O  
HETATM 2958  O   HOH A 575      40.163  50.151   5.757  1.00 33.33           O  
HETATM 2959  O   HOH A 576      77.169  56.838  41.120  1.00 78.01           O  
HETATM 2960  O   HOH A 577      69.816  53.010   6.610  1.00 44.55           O  
HETATM 2961  O   HOH A 578      69.326  37.466  13.179  1.00 25.33           O  
HETATM 2962  O   HOH A 579      69.859  68.433  37.790  1.00 92.74           O  
HETATM 2963  O   HOH A 580      51.367  53.672  48.154  1.00 49.86           O  
HETATM 2964  O   HOH A 581      68.486  44.093  36.393  1.00 63.92           O  
HETATM 2965  O   HOH A 582      48.323  42.893   4.360  1.00 74.27           O  
HETATM 2966  O   HOH A 583      64.661  31.273  25.450  1.00 94.20           O  
HETATM 2967  O   HOH A 584      38.918  48.592   9.450  1.00 69.97           O  
HETATM 2968  O   HOH A 585      63.745  69.549  20.217  1.00 87.26           O  
HETATM 2969  O   HOH A 586      71.925  69.237  28.116  1.00135.66           O  
HETATM 2970  O   HOH A 587      34.818  56.798  42.954  1.00 92.00           O  
HETATM 2971  O   HOH A 588      86.532  44.092  42.282  1.00 52.46           O  
HETATM 2972  O   HOH A 589      62.267  61.128  43.247  1.00 93.86           O  
HETATM 2973  O   HOH A 590      41.702  57.308  30.427  1.00 34.35           O  
HETATM 2974  O   HOH A 591      76.168  36.710  38.843  1.00 66.40           O  
HETATM 2975  O   HOH A 592      66.942  58.664  16.329  1.00 51.30           O  
HETATM 2976  O   HOH A 594      37.879  51.316   8.716  1.00112.94           O  
HETATM 2977  O   HOH A 595      69.966  48.662  40.556  1.00 65.37           O  
HETATM 2978  O   HOH A 596      77.656  63.441  37.065  1.00 62.74           O  
HETATM 2979  O   HOH A 597      65.230  72.327  25.238  1.00 59.31           O  
HETATM 2980  O   HOH A 598      71.589  61.079  20.647  1.00 90.14           O  
HETATM 2981  O   HOH A 599      71.995  60.091  42.371  1.00 65.56           O  
HETATM 2982  O   HOH A 600      71.680  57.161  17.439  1.00 35.99           O  
HETATM 2983  O   HOH A 601      50.526  43.234  43.427  1.00123.32           O  
HETATM 2984  O   HOH A 602      62.127  60.768  46.675  1.00 56.59           O  
HETATM 2985  O   HOH A 603      38.129  56.064  41.507  1.00 94.38           O  
HETATM 2986  O   HOH A 604      83.396  29.566  31.934  1.00 55.29           O  
HETATM 2987  O   HOH A 605      46.242  61.513  17.182  1.00124.38           O  
HETATM 2988  O   HOH A 606      70.816  37.902  38.258  1.00 29.59           O  
HETATM 2989  O   HOH A 607      80.872  49.858  41.696  1.00 28.56           O  
HETATM 2990  O   HOH A 608      71.136  56.103  11.220  1.00 86.61           O  
HETATM 2991  O   HOH A 609      58.542  37.792  38.376  1.00 60.57           O  
HETATM 2992  O   HOH A 610      49.204  41.079  41.234  1.00 72.56           O  
HETATM 2993  O   HOH A 611      43.414  40.970   7.596  1.00126.38           O  
HETATM 2994  O   HOH A 612      70.783  47.812   2.426  1.00 48.64           O  
HETATM 2995  O   HOH A 613      56.824  49.622  -0.068  1.00 77.84           O  
HETATM 2996  O   HOH A 614      61.598  46.140  42.796  1.00 91.90           O  
HETATM 2997  O   HOH A 615      34.073  59.626  27.617  1.00 47.32           O  
HETATM 2998  O   HOH A 616      28.702  51.366  16.535  1.00 94.64           O  
HETATM 2999  O   HOH A 617      78.371  45.492  41.092  1.00128.68           O  
HETATM 3000  O   HOH A 618      78.160  67.813  27.646  1.00 31.51           O  
HETATM 3001  O   HOH A 619      76.494  44.753  12.685  1.00 73.51           O  
HETATM 3002  O   HOH A 620      40.171  57.882  41.727  1.00 55.42           O  
HETATM 3003  O   HOH A 621      72.757  45.231   5.664  1.00 76.58           O  
HETATM 3004  O   HOH A 622      61.225  38.240   6.141  1.00 57.18           O  
HETATM 3005  O   HOH A 623      54.234  31.638  36.073  1.00 64.38           O  
HETATM 3006  O   HOH A 624      32.148  44.084  14.194  1.00 48.49           O  
HETATM 3007  O   HOH A 625      55.979  69.753  14.331  1.00 39.31           O  
HETATM 3008  O   HOH A 626      31.169  45.103  11.800  1.00 72.55           O  
HETATM 3009  O   HOH A 627      31.583  44.314  31.172  1.00103.29           O  
HETATM 3010  O   HOH A 628      46.949  43.047  42.314  1.00 33.19           O  
HETATM 3011  O   HOH A 629      27.043  40.248  24.205  1.00 84.17           O  
HETATM 3012  O   HOH A 630      53.726  70.614  12.404  1.00 35.81           O  
HETATM 3013  O   HOH A 631      80.632  63.921  35.734  1.00143.67           O  
HETATM 3014  O   HOH A 632      72.849  55.534  13.517  1.00 22.24           O  
HETATM 3015  O   HOH A 633      28.837  49.716  13.274  1.00 78.52           O  
HETATM 3016  O   HOH A 634      63.669  57.780  -0.982  1.00 62.41           O  
HETATM 3017  O   HOH A 635      68.214  37.353  20.095  1.00 24.60           O  
HETATM 3018  O   HOH A 636      54.642  52.420  47.451  1.00 26.80           O  
HETATM 3019  O   HOH A 637      42.247  65.997  19.721  1.00 65.16           O  
HETATM 3020  O   HOH A 638      60.969  42.380   1.808  1.00 58.61           O  
HETATM 3021  O   HOH A 639      67.499  34.710  35.654  1.00 73.97           O  
HETATM 3022  O   HOH A 640      49.442  59.928  45.418  1.00 25.39           O  
HETATM 3023  O   HOH A 641      70.489  30.897  33.671  1.00 69.81           O  
HETATM 3024  O   HOH A 642      52.431  43.588  45.890  1.00100.14           O  
HETATM 3025  O   HOH A 643      51.881  26.670  15.551  1.00 58.62           O  
HETATM 3026  O   HOH A 644      61.211  49.558  -2.834  1.00112.84           O  
HETATM 3027  O   HOH A 645      54.812  44.759  -0.283  1.00 88.61           O  
HETATM 3028  O   HOH A 646      30.545  45.252  33.590  1.00 15.50           O  
HETATM 3029  O   HOH A 647      52.448  37.713  37.722  1.00 57.34           O  
HETATM 3030  O   HOH A 648      49.394  39.502   2.182  1.00 66.08           O  
HETATM 3031  O   HOH A 649      72.157  43.538   7.918  1.00 73.23           O  
HETATM 3032  O   HOH A 650      58.908  57.514  47.516  1.00 47.80           O  
HETATM 3033  O   HOH A 652      56.567  27.112  16.072  1.00 79.02           O  
HETATM 3034  O   HOH A 653      67.994  46.629   4.794  1.00 54.01           O  
HETATM 3035  O   HOH A 654      43.394  69.140  16.556  1.00 88.35           O  
HETATM 3036  O   HOH A 655      40.294  58.496   8.654  1.00113.02           O  
HETATM 3037  O   HOH A 656      56.038  37.412  39.923  1.00 81.69           O  
HETATM 3038  O   HOH A 657      52.321  34.784  36.787  1.00 79.13           O  
HETATM 3039  O   HOH A 658      61.489  63.558   0.561  0.50 34.02           O  
HETATM 3040  O   HOH A 659      44.977  51.162  20.378  1.00 14.75           O  
HETATM 3041  O   HOH A 660      56.923  65.206  21.562  1.00  2.79           O  
CONECT 2699 2700 2716                                                           
CONECT 2700 2699 2701 2702                                                      
CONECT 2701 2700                                                                
CONECT 2702 2700 2703                                                           
CONECT 2703 2702 2704 2705                                                      
CONECT 2704 2703                                                                
CONECT 2705 2703 2706 2716                                                      
CONECT 2706 2705 2707                                                           
CONECT 2707 2706 2708 2714                                                      
CONECT 2708 2707 2709                                                           
CONECT 2709 2708 2710 2711                                                      
CONECT 2710 2709                                                                
CONECT 2711 2709 2712 2713                                                      
CONECT 2712 2711                                                                
CONECT 2713 2711 2714                                                           
CONECT 2714 2707 2713 2715                                                      
CONECT 2715 2714 2716 2717                                                      
CONECT 2716 2699 2705 2715                                                      
CONECT 2717 2715 2718                                                           
CONECT 2718 2717 2719 2720                                                      
CONECT 2719 2718                                                                
CONECT 2720 2718 2721 2722                                                      
CONECT 2721 2720                                                                
CONECT 2722 2720 2723 2724                                                      
CONECT 2723 2722                                                                
CONECT 2724 2722 2725                                                           
CONECT 2725 2724 2726                                                           
CONECT 2726 2725 2727 2728 2729                                                 
CONECT 2727 2726                                                                
CONECT 2728 2726                                                                
CONECT 2729 2726                                                                
CONECT 2730 2731 2733                                                           
CONECT 2731 2730 2732                                                           
CONECT 2732 2731 2734                                                           
CONECT 2733 2730 2734 2738                                                      
CONECT 2734 2732 2733 2735                                                      
CONECT 2735 2734 2736 2737                                                      
CONECT 2736 2735                                                                
CONECT 2737 2735                                                                
CONECT 2738 2733 2744                                                           
CONECT 2739 2740                                                                
CONECT 2740 2739 2741                                                           
CONECT 2741 2740 2742                                                           
CONECT 2742 2741 2743                                                           
CONECT 2743 2742 2744                                                           
CONECT 2744 2738 2743 2745                                                      
CONECT 2745 2744 2746                                                           
CONECT 2746 2745 2747                                                           
CONECT 2747 2746 2748                                                           
CONECT 2748 2747 2749                                                           
CONECT 2749 2748                                                                
MASTER      471    0    2   17   12    0    9    6 3040    1   51   28          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.