CNRS Nantes University UFIP UFIP
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***  phacca  ***

elNémo ID: 210510183035130307

Job options:

ID        	=	 210510183035130307
JOBID     	=	 phacca
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -200
DQMAX     	=	 200
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER phacca

HEADER    RNA BINDING PROTEIN                     07-MAR-19   6QXN              
TITLE     CRYSTAL STRUCTURE OF THE CCA-ADDING ENZYME OF A PSYCHROPHILIC ORGANISM
TITLE    2 IN COMPLEX WITH CTP                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CCA-ADDING ENZYME;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.7.72;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLANOCOCCUS HALOCRYOPHILUS;                     
SOURCE   3 ORGANISM_TAXID: 1215089;                                             
SOURCE   4 GENE: BBI08_05760;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-30B(+)                                
KEYWDS    TRNA MATURATION, TRNA NUCLEOTIDYLTRANSFERASE, PSYCHROPHILIC ENZYME,   
KEYWDS   2 RNA BINDING PROTEIN                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.DE WIJN,K.ROLLET,A.BLUHM,O.HENNIG,H.BETAT,M.MOERL,B.LORBER,C.SAUTER 
REVDAT   1   25-MAR-20 6QXN    0                                                
JRNL        AUTH   R.DE WIJN,O.HENNIG,F.ERNST,H.BETAT,M.MOERL,C.SAUTER          
JRNL        TITL   CCA-ADDITION IN THE COLD: FUNCTIONAL AND STRUCTURAL          
JRNL        TITL 2 CHARACTERIZATION OF THE CCA-ADDING ENZYME FROM PLANOCOCCUS   
JRNL        TITL 3 HALOCRYOPHILUS                                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 63868                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3195                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.0736 -  5.2557    1.00     2938   156  0.1848 0.1959        
REMARK   3     2  5.2557 -  4.1723    1.00     2756   145  0.1489 0.1503        
REMARK   3     3  4.1723 -  3.6451    1.00     2721   144  0.1645 0.1722        
REMARK   3     4  3.6451 -  3.3119    1.00     2690   141  0.1969 0.2176        
REMARK   3     5  3.3119 -  3.0746    1.00     2684   141  0.2068 0.2198        
REMARK   3     6  3.0746 -  2.8933    1.00     2657   140  0.2131 0.2619        
REMARK   3     7  2.8933 -  2.7484    1.00     2640   139  0.2014 0.2377        
REMARK   3     8  2.7484 -  2.6288    1.00     2634   139  0.2077 0.2203        
REMARK   3     9  2.6288 -  2.5276    1.00     2632   138  0.2039 0.2148        
REMARK   3    10  2.5276 -  2.4404    1.00     2636   138  0.2041 0.2233        
REMARK   3    11  2.4404 -  2.3641    1.00     2615   139  0.2099 0.2415        
REMARK   3    12  2.3641 -  2.2965    1.00     2634   138  0.2170 0.2512        
REMARK   3    13  2.2965 -  2.2361    1.00     2622   138  0.2206 0.2610        
REMARK   3    14  2.2361 -  2.1815    1.00     2600   137  0.2325 0.2517        
REMARK   3    15  2.1815 -  2.1319    1.00     2595   137  0.2323 0.2725        
REMARK   3    16  2.1319 -  2.0865    1.00     2609   137  0.2372 0.2531        
REMARK   3    17  2.0865 -  2.0448    1.00     2603   137  0.2530 0.2691        
REMARK   3    18  2.0448 -  2.0062    1.00     2589   137  0.2856 0.3529        
REMARK   3    19  2.0062 -  1.9704    1.00     2612   137  0.3209 0.3559        
REMARK   3    20  1.9704 -  1.9370    1.00     2591   136  0.3807 0.3778        
REMARK   3    21  1.9370 -  1.9057    1.00     2587   137  0.4404 0.4100        
REMARK   3    22  1.9057 -  1.8764    1.00     2593   136  0.5301 0.5500        
REMARK   3    23  1.8764 -  1.8488    0.95     2435   128  0.5580 0.5514        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3186                                  
REMARK   3   ANGLE     :  0.979           4301                                  
REMARK   3   CHIRALITY :  0.060            475                                  
REMARK   3   PLANARITY :  0.006            540                                  
REMARK   3   DIHEDRAL  : 16.250           1200                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6QXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292101058.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5 - 7.5                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 20160617                       
REMARK 200  DATA SCALING SOFTWARE          : XSCALE 20160617                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63935                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.849                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 12.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.30                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.13_2998                                      
REMARK 200 STARTING MODEL: 1MIV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: BIPYRAMID                                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION AT 4.5 MG/ML IN50 MM    
REMARK 280  TRIS-HCL PH 7.5, 200 MM NACL, 5 MM MGCL2; RESERVOIR SOLUTION:       
REMARK 280  100 MM SODIUM ACETATE; PH 4.5 1 M DI-AMMONIUM HYDROGEN PHOSPHATE    
REMARK 280  REMARKS : SOAKING 30 SECONDS IN A DROP WITH 5 MM CTP AND            
REMARK 280  RESERVOIR SOLUTION + 18% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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      145.74500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       35.19000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       35.19000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      218.61750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       35.19000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       35.19000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       72.87250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       35.19000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.19000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      218.61750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       35.19000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.19000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       72.87250            
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      145.74500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -42                                                      
REMARK 465     HIS A   -41                                                      
REMARK 465     HIS A   -40                                                      
REMARK 465     HIS A   -39                                                      
REMARK 465     HIS A   -38                                                      
REMARK 465     HIS A   -37                                                      
REMARK 465     HIS A   -36                                                      
REMARK 465     SER A   -35                                                      
REMARK 465     SER A   -34                                                      
REMARK 465     GLY A   -33                                                      
REMARK 465     LEU A   -32                                                      
REMARK 465     VAL A   -31                                                      
REMARK 465     PRO A   -30                                                      
REMARK 465     ARG A   -29                                                      
REMARK 465     GLY A   -28                                                      
REMARK 465     SER A   -27                                                      
REMARK 465     GLY A   -26                                                      
REMARK 465     MET A   -25                                                      
REMARK 465     LYS A   -24                                                      
REMARK 465     GLU A   -23                                                      
REMARK 465     THR A   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     ALA A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     LYS A   -18                                                      
REMARK 465     PHE A   -17                                                      
REMARK 465     GLU A   -16                                                      
REMARK 465     ARG A   -15                                                      
REMARK 465     GLN A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     PRO A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     SER A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     THR A   377                                                      
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    VAL A 222       45.49     34.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CTP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 507                 
DBREF1 6QXN A    1   377  UNP                  A0A1C7DQ98_9BACL                 
DBREF2 6QXN A     A0A1C7DQ98                          1         377             
SEQADV 6QXN MET A  -42  UNP  A0A1C7DQ9           INITIATING METHIONINE          
SEQADV 6QXN HIS A  -41  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN HIS A  -40  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN HIS A  -39  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN HIS A  -38  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN HIS A  -37  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN HIS A  -36  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN SER A  -35  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN SER A  -34  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLY A  -33  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN LEU A  -32  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN VAL A  -31  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN PRO A  -30  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ARG A  -29  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLY A  -28  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN SER A  -27  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLY A  -26  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN MET A  -25  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN LYS A  -24  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLU A  -23  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN THR A  -22  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ALA A  -21  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ALA A  -20  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ALA A  -19  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN LYS A  -18  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN PHE A  -17  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLU A  -16  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ARG A  -15  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLN A  -14  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN HIS A  -13  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN MET A  -12  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ASP A  -11  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN SER A  -10  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN PRO A   -9  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ASP A   -8  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN LEU A   -7  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN GLY A   -6  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN THR A   -5  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ASP A   -4  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ASP A   -3  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ASP A   -2  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN ASP A   -1  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQADV 6QXN LYS A    0  UNP  A0A1C7DQ9           EXPRESSION TAG                 
SEQRES   1 A  420  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  420  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 A  420  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 A  420  ASP ASP ASP LYS MET ASN THR ALA ILE LYS VAL ILE HIS          
SEQRES   5 A  420  THR LEU LYS ALA ALA GLY PHE GLU ALA TYR ILE VAL GLY          
SEQRES   6 A  420  GLY ALA VAL ARG ASP LEU LEU LEU GLY LYS THR PRO HIS          
SEQRES   7 A  420  ASP VAL ASP VAL ALA SER SER ALA LEU PRO GLN GLN VAL          
SEQRES   8 A  420  LYS VAL LEU PHE ASP ARG THR VAL ASP THR GLY ILE ASP          
SEQRES   9 A  420  HIS GLY THR VAL LEU VAL LEU LEU ASP GLY GLU GLY ILE          
SEQRES  10 A  420  GLU VAL THR THR PHE ARG THR GLU SER SER TYR SER ASP          
SEQRES  11 A  420  ASN ARG ARG PRO ASP SER VAL GLU PHE VAL LEU SER LEU          
SEQRES  12 A  420  GLU GLU ASP LEU ARG ARG ARG ASP PHE THR ILE ASN ALA          
SEQRES  13 A  420  MET ALA MET THR GLU ASP LEU LYS ILE ILE ASP PRO PHE          
SEQRES  14 A  420  GLY GLY LYS GLU ASP LEU LYS ASN LYS VAL ILE ARG ALA          
SEQRES  15 A  420  VAL GLY ASP PRO ASP GLU ARG PHE GLU GLU ASP ALA LEU          
SEQRES  16 A  420  ARG MET LEU ARG ALA ILE ARG PHE SER GLY GLN LEU ASP          
SEQRES  17 A  420  PHE ILE ILE ASP MET LYS THR LEU LEU SER ILE ARG ARG          
SEQRES  18 A  420  HIS ALA ARG LEU ILE ARG PHE ILE ALA VAL GLU ARG LEU          
SEQRES  19 A  420  LYS SER GLU ILE ASP LYS ILE PHE VAL ASN PRO SER MET          
SEQRES  20 A  420  GLN LYS SER MET ALA TYR LEU LYS ASP SER VAL LEU THR          
SEQRES  21 A  420  ARG PHE LEU PRO VAL GLY GLY LEU PHE GLU VAL ASP TRP          
SEQRES  22 A  420  ILE THR TYR HIS THR ASP GLY ASN PRO THR TYR GLY TRP          
SEQRES  23 A  420  LEU TYR LEU LEU HIS GLN GLN LYS ARG GLN PHE THR ASP          
SEQRES  24 A  420  ILE LYS ASP TYR ARG PHE SER ASN GLU GLU LYS ARG LEU          
SEQRES  25 A  420  ILE GLU LYS SER LEU GLU LEU THR ALA LEU ASN THR TRP          
SEQRES  26 A  420  ASP GLN TRP THR PHE TYR LYS TYR THR LEU LYS GLN LEU          
SEQRES  27 A  420  GLU MET ALA SER ARG VAL THR GLY LYS LYS LYS ASP LEU          
SEQRES  28 A  420  ALA ALA ILE LYS ARG GLN LEU PRO ILE GLN SER ARG SER          
SEQRES  29 A  420  GLU LEU ALA VAL ASP GLY TRP ASP LEU ILE GLU TRP SER          
SEQRES  30 A  420  GLY ALA LYS SER GLY PRO TRP LEU LYS VAL TRP ILE GLU          
SEQRES  31 A  420  LYS ILE GLU ARG LEU ILE VAL TYR GLY ILE LEU LYS ASN          
SEQRES  32 A  420  ASP LYS GLU LEU ILE LYS ASP TRP PHE GLU ASP GLU TYR          
SEQRES  33 A  420  HIS SER HIS THR                                              
HET    CTP  A 501      29                                                       
HET    GOL  A 502       6                                                       
HET    GOL  A 503       6                                                       
HET    ACT  A 504       4                                                       
HET    ACT  A 505       4                                                       
HET    ACT  A 506       4                                                       
HET    PO4  A 507       5                                                       
HETNAM     CTP CYTIDINE-5'-TRIPHOSPHATE                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  CTP    C9 H16 N3 O14 P3                                             
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   5  ACT    3(C2 H3 O2 1-)                                               
FORMUL   8  PO4    O4 P 3-                                                      
FORMUL   9  HOH   *268(H2 O)                                                    
HELIX    1 AA1 ASP A   -1  ALA A   14  1                                  16    
HELIX    2 AA2 GLY A   22  LEU A   30  1                                   9    
HELIX    3 AA3 LEU A   44  PHE A   52  1                                   9    
HELIX    4 AA4 GLY A   59  HIS A   62  5                                   4    
HELIX    5 AA5 SER A   99  ARG A  105  1                                   7    
HELIX    6 AA6 PHE A  109  ALA A  113  5                                   5    
HELIX    7 AA7 GLY A  127  LYS A  135  1                                   9    
HELIX    8 AA8 ASP A  142  ASP A  150  1                                   9    
HELIX    9 AA9 ALA A  151  ASP A  165  1                                  15    
HELIX   10 AB1 ASP A  169  ALA A  180  1                                  12    
HELIX   11 AB2 ARG A  181  ILE A  186  5                                   6    
HELIX   12 AB3 ALA A  187  ASN A  201  1                                  15    
HELIX   13 AB4 SER A  203  SER A  214  1                                  12    
HELIX   14 AB5 VAL A  222  GLU A  227  5                                   6    
HELIX   15 AB6 ASN A  238  GLN A  250  1                                  13    
HELIX   16 AB7 GLN A  253  ARG A  261  5                                   9    
HELIX   17 AB8 SER A  263  ALA A  278  1                                  16    
HELIX   18 AB9 ASP A  283  TYR A  290  1                                   8    
HELIX   19 AC1 THR A  291  GLY A  303  1                                  13    
HELIX   20 AC2 ASP A  307  GLN A  314  1                                   8    
HELIX   21 AC3 SER A  319  LEU A  323  5                                   5    
HELIX   22 AC4 ASP A  326  GLY A  335  1                                  10    
HELIX   23 AC5 PRO A  340  TYR A  355  1                                  16    
HELIX   24 AC6 ASP A  361  TYR A  373  1                                  13    
SHEET    1 AA1 7 THR A  55  VAL A  56  0                                        
SHEET    2 AA1 7 THR A  64  LEU A  69 -1  O  LEU A  66   N  VAL A  56           
SHEET    3 AA1 7 GLU A  72  THR A  78 -1  O  VAL A  76   N  VAL A  65           
SHEET    4 AA1 7 ASP A  38  SER A  41  1  N  VAL A  39   O  GLU A  75           
SHEET    5 AA1 7 ALA A  18  VAL A  21 -1  N  TYR A  19   O  ALA A  40           
SHEET    6 AA1 7 ALA A 115  MET A 116 -1  O  MET A 116   N  ILE A  20           
SHEET    7 AA1 7 ILE A 122  ILE A 123 -1  O  ILE A 123   N  ALA A 115           
SHEET    1 AA2 2 ARG A  80  SER A  83  0                                        
SHEET    2 AA2 2 SER A  93  PHE A  96 -1  O  GLU A  95   N  THR A  81           
SHEET    1 AA3 2 VAL A 136  ILE A 137  0                                        
SHEET    2 AA3 2 ILE A 167  ILE A 168  1  O  ILE A 167   N  ILE A 137           
SITE     1 AC1 13 GLY A  22  GLY A  23  ARG A  26  ARG A 107                    
SITE     2 AC1 13 ASP A 108  ASN A 112  ASP A 150  ARG A 153                    
SITE     3 AC1 13 ARG A 156  ARG A 159  GLN A 163  HOH A 612                    
SITE     4 AC1 13 HOH A 627                                                     
SITE     1 AC2  6 LYS A 272  GLU A 275  LYS A 289  TYR A 290                    
SITE     2 AC2  6 PO4 A 507  HOH A 801                                          
SITE     1 AC3  9 TYR A 288  LYS A 289  TYR A 290  LYS A 312                    
SITE     2 AC3  9 PO4 A 507  HOH A 608  HOH A 613  HOH A 733                    
SITE     3 AC3  9 HOH A 749                                                     
SITE     1 AC4  1 ARG A 300                                                     
SITE     1 AC5  2 ARG A 268  LYS A 272                                          
SITE     1 AC6  3 VAL A  94  PHE A  96  HOH A 714                               
SITE     1 AC7 10 ARG A 268  LYS A 272  LYS A 289  TYR A 290                    
SITE     2 AC7 10 THR A 291  GLN A 294  GOL A 502  GOL A 503                    
SITE     3 AC7 10 HOH A 611  HOH A 660                                          
CRYST1   70.380   70.380  291.490  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014209  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014209  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003431        0.00000                         
ATOM      1  N   ASP A  -2      24.047  46.515  41.225  1.00 81.49           N  
ATOM      2  CA  ASP A  -2      23.264  46.922  40.055  1.00 72.23           C  
ATOM      3  C   ASP A  -2      22.373  48.117  40.389  1.00 70.76           C  
ATOM      4  O   ASP A  -2      21.750  48.723  39.500  1.00 61.68           O  
ATOM      5  CB  ASP A  -2      22.407  45.757  39.535  1.00 79.90           C  
ATOM      6  CG  ASP A  -2      23.236  44.672  38.859  1.00 97.92           C  
ATOM      7  OD1 ASP A  -2      24.486  44.727  38.937  1.00 89.51           O  
ATOM      8  OD2 ASP A  -2      22.632  43.764  38.240  1.00 94.48           O  
ATOM      9  N   ASP A  -1      22.280  48.430  41.684  1.00 42.42           N  
ATOM     10  CA  ASP A  -1      21.616  49.644  42.128  1.00 40.36           C  
ATOM     11  C   ASP A  -1      22.535  50.604  42.869  1.00 37.09           C  
ATOM     12  O   ASP A  -1      22.093  51.709  43.197  1.00 37.97           O  
ATOM     13  CB  ASP A  -1      20.418  49.321  43.039  1.00 52.91           C  
ATOM     14  CG  ASP A  -1      19.276  48.635  42.294  1.00 68.46           C  
ATOM     15  OD1 ASP A  -1      19.211  48.753  41.049  1.00 55.71           O  
ATOM     16  OD2 ASP A  -1      18.444  47.978  42.961  1.00 64.55           O  
ATOM     17  N   LYS A   0      23.791  50.228  43.134  1.00 41.73           N  
ATOM     18  CA  LYS A   0      24.613  51.108  43.966  1.00 38.62           C  
ATOM     19  C   LYS A   0      24.972  52.396  43.235  1.00 31.45           C  
ATOM     20  O   LYS A   0      24.855  53.485  43.804  1.00 34.22           O  
ATOM     21  CB  LYS A   0      25.884  50.394  44.428  1.00 40.32           C  
ATOM     22  CG  LYS A   0      25.667  49.387  45.542  1.00 50.40           C  
ATOM     23  CD  LYS A   0      27.009  48.964  46.134  1.00 58.24           C  
ATOM     24  CE  LYS A   0      27.095  49.268  47.630  1.00 72.92           C  
ATOM     25  NZ  LYS A   0      27.805  50.561  47.877  1.00 63.71           N  
ATOM     26  N   MET A   1      25.377  52.338  41.959  1.00 28.28           N  
ATOM     27  CA  MET A   1      25.708  53.576  41.254  1.00 31.74           C  
ATOM     28  C   MET A   1      24.504  54.514  41.201  1.00 34.85           C  
ATOM     29  O   MET A   1      24.642  55.725  41.404  1.00 31.27           O  
ATOM     30  CB  MET A   1      26.202  53.291  39.823  1.00 29.52           C  
ATOM     31  CG  MET A   1      27.645  52.792  39.678  1.00 41.70           C  
ATOM     32  SD  MET A   1      28.904  54.008  40.250  1.00 49.51           S  
ATOM     33  CE  MET A   1      28.192  55.541  39.663  1.00 49.06           C  
ATOM     34  N   ASN A   2      23.317  53.980  40.888  1.00 32.69           N  
ATOM     35  CA  ASN A   2      22.121  54.822  40.863  1.00 29.99           C  
ATOM     36  C   ASN A   2      21.894  55.496  42.208  1.00 27.98           C  
ATOM     37  O   ASN A   2      21.579  56.690  42.268  1.00 35.17           O  
ATOM     38  CB  ASN A   2      20.898  53.990  40.461  1.00 30.76           C  
ATOM     39  CG  ASN A   2      20.957  53.525  39.006  1.00 35.25           C  
ATOM     40  OD1 ASN A   2      21.696  54.087  38.196  1.00 33.16           O  
ATOM     41  ND2 ASN A   2      20.163  52.512  38.665  1.00 28.44           N  
ATOM     42  N   THR A   3      22.048  54.746  43.302  1.00 28.84           N  
ATOM     43  CA  THR A   3      21.842  55.322  44.626  1.00 30.29           C  
ATOM     44  C   THR A   3      22.882  56.401  44.921  1.00 36.18           C  
ATOM     45  O   THR A   3      22.550  57.457  45.470  1.00 31.35           O  
ATOM     46  CB  THR A   3      21.877  54.215  45.687  1.00 34.48           C  
ATOM     47  OG1 THR A   3      20.880  53.232  45.370  1.00 37.03           O  
ATOM     48  CG2 THR A   3      21.608  54.778  47.092  1.00 33.80           C  
ATOM     49  N   ALA A   4      24.147  56.151  44.560  1.00 31.99           N  
ATOM     50  CA  ALA A   4      25.177  57.175  44.731  1.00 29.92           C  
ATOM     51  C   ALA A   4      24.850  58.442  43.942  1.00 28.01           C  
ATOM     52  O   ALA A   4      25.045  59.558  44.444  1.00 33.36           O  
ATOM     53  CB  ALA A   4      26.540  56.620  44.309  1.00 32.00           C  
ATOM     54  N   ILE A   5      24.349  58.295  42.710  1.00 27.88           N  
ATOM     55  CA  ILE A   5      23.936  59.461  41.920  1.00 35.07           C  
ATOM     56  C   ILE A   5      22.813  60.223  42.628  1.00 40.58           C  
ATOM     57  O   ILE A   5      22.812  61.461  42.678  1.00 34.32           O  
ATOM     58  CB  ILE A   5      23.510  59.029  40.503  1.00 32.48           C  
ATOM     59  CG1 ILE A   5      24.703  58.479  39.694  1.00 38.35           C  
ATOM     60  CG2 ILE A   5      22.799  60.165  39.767  1.00 38.07           C  
ATOM     61  CD1 ILE A   5      25.792  59.521  39.354  1.00 39.46           C  
ATOM     62  N   LYS A   6      21.832  59.497  43.173  1.00 35.24           N  
ATOM     63  CA  LYS A   6      20.770  60.136  43.950  1.00 35.73           C  
ATOM     64  C   LYS A   6      21.321  60.847  45.192  1.00 37.72           C  
ATOM     65  O   LYS A   6      20.866  61.945  45.542  1.00 34.37           O  
ATOM     66  CB  LYS A   6      19.716  59.081  44.325  1.00 37.37           C  
ATOM     67  CG  LYS A   6      18.619  59.546  45.281  1.00 51.39           C  
ATOM     68  CD  LYS A   6      17.515  58.453  45.429  1.00 53.51           C  
ATOM     69  CE  LYS A   6      16.997  57.972  44.061  1.00 50.30           C  
ATOM     70  NZ  LYS A   6      15.776  57.072  44.147  1.00 44.18           N  
ATOM     71  N   VAL A   7      22.300  60.241  45.869  1.00 31.49           N  
ATOM     72  CA  VAL A   7      22.940  60.894  47.011  1.00 34.42           C  
ATOM     73  C   VAL A   7      23.613  62.196  46.570  1.00 37.31           C  
ATOM     74  O   VAL A   7      23.463  63.248  47.206  1.00 34.71           O  
ATOM     75  CB  VAL A   7      23.940  59.927  47.676  1.00 30.83           C  
ATOM     76  CG1 VAL A   7      24.886  60.658  48.632  1.00 28.87           C  
ATOM     77  CG2 VAL A   7      23.185  58.823  48.429  1.00 32.35           C  
ATOM     78  N   ILE A   8      24.350  62.144  45.463  1.00 33.78           N  
ATOM     79  CA  ILE A   8      25.012  63.334  44.948  1.00 31.76           C  
ATOM     80  C   ILE A   8      23.987  64.411  44.601  1.00 41.93           C  
ATOM     81  O   ILE A   8      24.157  65.588  44.937  1.00 35.64           O  
ATOM     82  CB  ILE A   8      25.875  62.958  43.734  1.00 36.45           C  
ATOM     83  CG1 ILE A   8      27.116  62.202  44.227  1.00 31.78           C  
ATOM     84  CG2 ILE A   8      26.181  64.176  42.872  1.00 36.81           C  
ATOM     85  CD1 ILE A   8      27.846  61.511  43.114  1.00 38.76           C  
ATOM     86  N   HIS A   9      22.912  64.021  43.909  1.00 36.14           N  
ATOM     87  CA  HIS A   9      21.880  64.992  43.566  1.00 37.98           C  
ATOM     88  C   HIS A   9      21.356  65.701  44.805  1.00 35.94           C  
ATOM     89  O   HIS A   9      21.164  66.923  44.795  1.00 40.66           O  
ATOM     90  CB  HIS A   9      20.736  64.303  42.818  1.00 47.42           C  
ATOM     91  CG  HIS A   9      19.771  65.259  42.191  1.00 45.96           C  
ATOM     92  ND1 HIS A   9      20.032  65.911  41.007  1.00 56.53           N  
ATOM     93  CD2 HIS A   9      18.551  65.692  42.598  1.00 48.12           C  
ATOM     94  CE1 HIS A   9      19.011  66.691  40.698  1.00 58.78           C  
ATOM     95  NE2 HIS A   9      18.099  66.577  41.648  1.00 55.42           N  
ATOM     96  N   THR A  10      21.125  64.948  45.886  1.00 36.55           N  
ATOM     97  CA  THR A  10      20.582  65.517  47.111  1.00 36.71           C  
ATOM     98  C   THR A  10      21.584  66.444  47.780  1.00 45.54           C  
ATOM     99  O   THR A  10      21.204  67.477  48.343  1.00 36.82           O  
ATOM    100  CB  THR A  10      20.189  64.398  48.077  1.00 37.87           C  
ATOM    101  OG1 THR A  10      19.147  63.602  47.501  1.00 43.16           O  
ATOM    102  CG2 THR A  10      19.732  64.966  49.415  1.00 41.84           C  
ATOM    103  N   LEU A  11      22.865  66.075  47.766  1.00 36.62           N  
ATOM    104  CA  LEU A  11      23.871  66.946  48.359  1.00 38.43           C  
ATOM    105  C   LEU A  11      23.995  68.240  47.572  1.00 36.81           C  
ATOM    106  O   LEU A  11      24.149  69.318  48.159  1.00 42.03           O  
ATOM    107  CB  LEU A  11      25.214  66.225  48.426  1.00 32.89           C  
ATOM    108  CG  LEU A  11      25.324  65.177  49.528  1.00 31.85           C  
ATOM    109  CD1 LEU A  11      26.415  64.163  49.177  1.00 34.60           C  
ATOM    110  CD2 LEU A  11      25.615  65.837  50.881  1.00 32.06           C  
ATOM    111  N   LYS A  12      23.924  68.153  46.244  1.00 32.75           N  
ATOM    112  CA  LYS A  12      24.069  69.347  45.418  1.00 39.15           C  
ATOM    113  C   LYS A  12      22.830  70.230  45.488  1.00 44.38           C  
ATOM    114  O   LYS A  12      22.948  71.456  45.459  1.00 42.71           O  
ATOM    115  CB  LYS A  12      24.387  68.953  43.976  1.00 37.73           C  
ATOM    116  CG  LYS A  12      25.780  68.349  43.840  1.00 36.39           C  
ATOM    117  CD  LYS A  12      25.994  67.721  42.477  1.00 38.82           C  
ATOM    118  CE  LYS A  12      25.990  68.759  41.382  1.00 45.97           C  
ATOM    119  NZ  LYS A  12      25.980  68.075  40.068  1.00 51.41           N  
ATOM    120  N   ALA A  13      21.641  69.635  45.606  1.00 43.47           N  
ATOM    121  CA  ALA A  13      20.436  70.439  45.812  1.00 48.11           C  
ATOM    122  C   ALA A  13      20.562  71.335  47.035  1.00 49.51           C  
ATOM    123  O   ALA A  13      19.996  72.434  47.068  1.00 53.78           O  
ATOM    124  CB  ALA A  13      19.209  69.537  45.957  1.00 45.63           C  
ATOM    125  N   ALA A  14      21.292  70.883  48.046  1.00 43.11           N  
ATOM    126  CA  ALA A  14      21.536  71.644  49.258  1.00 39.17           C  
ATOM    127  C   ALA A  14      22.719  72.598  49.135  1.00 42.59           C  
ATOM    128  O   ALA A  14      23.119  73.194  50.139  1.00 47.11           O  
ATOM    129  CB  ALA A  14      21.760  70.694  50.434  1.00 33.88           C  
ATOM    130  N   GLY A  15      23.304  72.731  47.944  1.00 46.86           N  
ATOM    131  CA  GLY A  15      24.387  73.662  47.712  1.00 44.44           C  
ATOM    132  C   GLY A  15      25.791  73.115  47.891  1.00 50.90           C  
ATOM    133  O   GLY A  15      26.751  73.890  47.802  1.00 41.42           O  
ATOM    134  N   PHE A  16      25.954  71.818  48.133  1.00 40.77           N  
ATOM    135  CA  PHE A  16      27.279  71.249  48.333  1.00 38.37           C  
ATOM    136  C   PHE A  16      27.812  70.644  47.041  1.00 39.87           C  
ATOM    137  O   PHE A  16      27.056  70.290  46.134  1.00 45.47           O  
ATOM    138  CB  PHE A  16      27.253  70.175  49.427  1.00 36.92           C  
ATOM    139  CG  PHE A  16      26.776  70.676  50.762  1.00 40.27           C  
ATOM    140  CD1 PHE A  16      27.552  71.553  51.507  1.00 39.69           C  
ATOM    141  CD2 PHE A  16      25.558  70.264  51.274  1.00 34.93           C  
ATOM    142  CE1 PHE A  16      27.112  72.016  52.744  1.00 40.39           C  
ATOM    143  CE2 PHE A  16      25.112  70.714  52.509  1.00 41.05           C  
ATOM    144  CZ  PHE A  16      25.884  71.588  53.243  1.00 47.59           C  
ATOM    145  N   GLU A  17      29.138  70.533  46.965  1.00 36.45           N  
ATOM    146  CA  GLU A  17      29.777  69.757  45.910  1.00 36.00           C  
ATOM    147  C   GLU A  17      29.743  68.281  46.282  1.00 29.63           C  
ATOM    148  O   GLU A  17      29.860  67.926  47.457  1.00 33.92           O  
ATOM    149  CB  GLU A  17      31.238  70.154  45.732  1.00 38.54           C  
ATOM    150  CG  GLU A  17      31.522  71.589  45.380  1.00 41.39           C  
ATOM    151  CD  GLU A  17      33.025  71.848  45.389  1.00 52.41           C  
ATOM    152  OE1 GLU A  17      33.463  72.761  46.118  1.00 64.80           O  
ATOM    153  OE2 GLU A  17      33.774  71.098  44.710  1.00 47.29           O  
ATOM    154  N   ALA A  18      29.614  67.423  45.268  1.00 30.91           N  
ATOM    155  CA  ALA A  18      29.611  65.989  45.529  1.00 32.96           C  
ATOM    156  C   ALA A  18      29.985  65.225  44.258  1.00 28.66           C  
ATOM    157  O   ALA A  18      29.559  65.587  43.163  1.00 33.05           O  
ATOM    158  CB  ALA A  18      28.238  65.536  46.059  1.00 30.08           C  
ATOM    159  N   TYR A  19      30.769  64.152  44.426  1.00 29.18           N  
ATOM    160  CA  TYR A  19      31.358  63.378  43.339  1.00 25.37           C  
ATOM    161  C   TYR A  19      31.450  61.913  43.739  1.00 26.29           C  
ATOM    162  O   TYR A  19      31.573  61.600  44.922  1.00 27.41           O  
ATOM    163  CB  TYR A  19      32.784  63.845  43.021  1.00 28.60           C  
ATOM    164  CG  TYR A  19      32.929  65.335  42.895  1.00 30.37           C  
ATOM    165  CD1 TYR A  19      33.200  66.127  44.010  1.00 35.37           C  
ATOM    166  CD2 TYR A  19      32.793  65.952  41.663  1.00 31.68           C  
ATOM    167  CE1 TYR A  19      33.332  67.513  43.888  1.00 30.82           C  
ATOM    168  CE2 TYR A  19      32.931  67.330  41.530  1.00 32.99           C  
ATOM    169  CZ  TYR A  19      33.192  68.097  42.647  1.00 35.54           C  
ATOM    170  OH  TYR A  19      33.315  69.465  42.516  1.00 41.05           O  
ATOM    171  N   ILE A  20      31.434  61.028  42.741  1.00 26.85           N  
ATOM    172  CA  ILE A  20      31.887  59.645  42.926  1.00 30.69           C  
ATOM    173  C   ILE A  20      33.413  59.650  42.939  1.00 25.81           C  
ATOM    174  O   ILE A  20      34.036  60.308  42.105  1.00 29.56           O  
ATOM    175  CB  ILE A  20      31.368  58.740  41.797  1.00 32.58           C  
ATOM    176  CG1 ILE A  20      29.849  58.884  41.614  1.00 37.55           C  
ATOM    177  CG2 ILE A  20      31.725  57.286  42.077  1.00 31.72           C  
ATOM    178  CD1 ILE A  20      29.075  58.334  42.748  1.00 37.25           C  
ATOM    179  N   VAL A  21      34.019  58.924  43.876  1.00 27.43           N  
ATOM    180  CA  VAL A  21      35.473  58.884  44.006  1.00 29.04           C  
ATOM    181  C   VAL A  21      35.925  57.454  44.262  1.00 34.70           C  
ATOM    182  O   VAL A  21      35.130  56.570  44.576  1.00 33.83           O  
ATOM    183  CB  VAL A  21      36.005  59.794  45.138  1.00 28.38           C  
ATOM    184  CG1 VAL A  21      35.781  61.262  44.794  1.00 34.40           C  
ATOM    185  CG2 VAL A  21      35.374  59.404  46.499  1.00 27.63           C  
ATOM    186  N   GLY A  22      37.237  57.245  44.162  1.00 37.56           N  
ATOM    187  CA  GLY A  22      37.811  55.980  44.582  1.00 32.79           C  
ATOM    188  C   GLY A  22      37.592  54.853  43.581  1.00 28.31           C  
ATOM    189  O   GLY A  22      37.568  55.056  42.364  1.00 30.50           O  
ATOM    190  N   GLY A  23      37.422  53.640  44.121  1.00 33.74           N  
ATOM    191  CA  GLY A  23      37.426  52.447  43.285  1.00 35.24           C  
ATOM    192  C   GLY A  23      36.297  52.390  42.275  1.00 37.05           C  
ATOM    193  O   GLY A  23      36.449  51.801  41.198  1.00 34.34           O  
ATOM    194  N   ALA A  24      35.156  53.001  42.590  1.00 30.69           N  
ATOM    195  CA  ALA A  24      34.017  52.951  41.677  1.00 32.45           C  
ATOM    196  C   ALA A  24      34.329  53.614  40.333  1.00 37.80           C  
ATOM    197  O   ALA A  24      33.870  53.140  39.288  1.00 35.20           O  
ATOM    198  CB  ALA A  24      32.788  53.594  42.330  1.00 34.61           C  
ATOM    199  N   VAL A  25      35.083  54.724  40.334  1.00 28.57           N  
ATOM    200  CA  VAL A  25      35.446  55.365  39.074  1.00 28.40           C  
ATOM    201  C   VAL A  25      36.377  54.463  38.276  1.00 37.12           C  
ATOM    202  O   VAL A  25      36.199  54.265  37.063  1.00 34.39           O  
ATOM    203  CB  VAL A  25      36.087  56.746  39.325  1.00 30.83           C  
ATOM    204  CG1 VAL A  25      36.261  57.500  37.998  1.00 31.24           C  
ATOM    205  CG2 VAL A  25      35.237  57.551  40.315  1.00 33.40           C  
ATOM    206  N   ARG A  26      37.328  53.856  38.977  1.00 33.98           N  
ATOM    207  CA  ARG A  26      38.265  52.930  38.357  1.00 36.62           C  
ATOM    208  C   ARG A  26      37.546  51.715  37.759  1.00 38.12           C  
ATOM    209  O   ARG A  26      37.869  51.289  36.650  1.00 38.45           O  
ATOM    210  CB  ARG A  26      39.315  52.471  39.371  1.00 35.52           C  
ATOM    211  CG  ARG A  26      40.123  51.263  38.925  1.00 41.26           C  
ATOM    212  CD  ARG A  26      39.892  50.075  39.845  1.00 52.40           C  
ATOM    213  NE  ARG A  26      40.415  50.314  41.187  1.00 47.35           N  
ATOM    214  CZ  ARG A  26      39.856  49.848  42.300  1.00 41.68           C  
ATOM    215  NH1 ARG A  26      38.752  49.116  42.234  1.00 41.04           N  
ATOM    216  NH2 ARG A  26      40.400  50.115  43.479  1.00 29.84           N  
ATOM    217  N   ASP A  27      36.575  51.157  38.484  1.00 35.86           N  
ATOM    218  CA  ASP A  27      35.848  49.998  37.982  1.00 39.64           C  
ATOM    219  C   ASP A  27      34.937  50.379  36.820  1.00 47.72           C  
ATOM    220  O   ASP A  27      34.919  49.692  35.793  1.00 43.38           O  
ATOM    221  CB  ASP A  27      35.072  49.345  39.121  1.00 36.12           C  
ATOM    222  CG  ASP A  27      35.997  48.696  40.153  1.00 47.68           C  
ATOM    223  OD1 ASP A  27      37.182  48.447  39.822  1.00 50.35           O  
ATOM    224  OD2 ASP A  27      35.549  48.439  41.290  1.00 52.60           O  
ATOM    225  N   LEU A  28      34.211  51.495  36.938  1.00 44.95           N  
ATOM    226  CA  LEU A  28      33.392  51.961  35.817  1.00 40.87           C  
ATOM    227  C   LEU A  28      34.211  52.097  34.541  1.00 48.67           C  
ATOM    228  O   LEU A  28      33.812  51.607  33.479  1.00 50.41           O  
ATOM    229  CB  LEU A  28      32.724  53.295  36.151  1.00 41.20           C  
ATOM    230  CG  LEU A  28      31.269  53.231  36.607  1.00 63.70           C  
ATOM    231  CD1 LEU A  28      30.657  54.634  36.655  1.00 55.52           C  
ATOM    232  CD2 LEU A  28      30.446  52.305  35.698  1.00 54.79           C  
ATOM    233  N   LEU A  29      35.351  52.785  34.614  1.00 39.30           N  
ATOM    234  CA  LEU A  29      36.168  52.961  33.421  1.00 40.76           C  
ATOM    235  C   LEU A  29      36.723  51.642  32.898  1.00 43.03           C  
ATOM    236  O   LEU A  29      37.055  51.549  31.709  1.00 51.94           O  
ATOM    237  CB  LEU A  29      37.306  53.940  33.699  1.00 39.43           C  
ATOM    238  CG  LEU A  29      36.912  55.418  33.789  1.00 47.18           C  
ATOM    239  CD1 LEU A  29      38.021  56.230  34.408  1.00 43.57           C  
ATOM    240  CD2 LEU A  29      36.584  55.963  32.413  1.00 46.19           C  
ATOM    241  N   LEU A  30      36.850  50.628  33.745  1.00 39.26           N  
ATOM    242  CA  LEU A  30      37.280  49.312  33.287  1.00 50.67           C  
ATOM    243  C   LEU A  30      36.126  48.464  32.775  1.00 54.47           C  
ATOM    244  O   LEU A  30      36.345  47.296  32.433  1.00 51.66           O  
ATOM    245  CB  LEU A  30      37.990  48.566  34.414  1.00 38.38           C  
ATOM    246  CG  LEU A  30      39.392  49.029  34.805  1.00 46.66           C  
ATOM    247  CD1 LEU A  30      39.794  48.345  36.090  1.00 35.25           C  
ATOM    248  CD2 LEU A  30      40.418  48.740  33.708  1.00 42.78           C  
ATOM    249  N   GLY A  31      34.912  49.006  32.734  1.00 52.43           N  
ATOM    250  CA  GLY A  31      33.764  48.230  32.327  1.00 56.75           C  
ATOM    251  C   GLY A  31      33.262  47.243  33.350  1.00 55.91           C  
ATOM    252  O   GLY A  31      32.484  46.352  32.990  1.00 63.54           O  
ATOM    253  N   LYS A  32      33.680  47.358  34.605  1.00 45.20           N  
ATOM    254  CA  LYS A  32      33.190  46.487  35.659  1.00 44.27           C  
ATOM    255  C   LYS A  32      32.064  47.163  36.432  1.00 52.69           C  
ATOM    256  O   LYS A  32      31.929  48.390  36.437  1.00 50.75           O  
ATOM    257  CB  LYS A  32      34.304  46.111  36.640  1.00 50.22           C  
ATOM    258  CG  LYS A  32      35.541  45.466  36.038  1.00 55.52           C  
ATOM    259  CD  LYS A  32      36.386  44.889  37.175  1.00 61.55           C  
ATOM    260  CE  LYS A  32      35.569  44.654  38.437  1.00 68.98           C  
ATOM    261  NZ  LYS A  32      36.023  43.402  39.125  1.00 75.81           N  
ATOM    262  N   THR A  33      31.259  46.338  37.103  1.00 46.77           N  
ATOM    263  CA  THR A  33      30.261  46.838  38.042  1.00 54.31           C  
ATOM    264  C   THR A  33      30.918  47.062  39.391  1.00 62.39           C  
ATOM    265  O   THR A  33      31.453  46.108  39.975  1.00 51.59           O  
ATOM    266  CB  THR A  33      29.111  45.855  38.196  1.00 58.11           C  
ATOM    267  OG1 THR A  33      28.428  45.714  36.947  1.00 56.61           O  
ATOM    268  CG2 THR A  33      28.133  46.345  39.252  1.00 56.81           C  
ATOM    269  N   PRO A  34      30.851  48.239  39.954  1.00 56.47           N  
ATOM    270  CA  PRO A  34      31.492  48.464  41.238  1.00 49.02           C  
ATOM    271  C   PRO A  34      30.950  47.682  42.398  1.00 45.20           C  
ATOM    272  O   PRO A  34      29.742  47.443  42.460  1.00 54.50           O  
ATOM    273  CB  PRO A  34      31.246  49.934  41.480  1.00 44.68           C  
ATOM    274  CG  PRO A  34      31.062  50.512  40.165  1.00 53.05           C  
ATOM    275  CD  PRO A  34      30.466  49.479  39.295  1.00 50.28           C  
ATOM    276  N   HIS A  35      31.800  47.319  43.325  1.00 49.21           N  
ATOM    277  CA  HIS A  35      31.625  46.627  44.574  1.00 56.82           C  
ATOM    278  C   HIS A  35      31.042  47.556  45.634  1.00 60.05           C  
ATOM    279  O   HIS A  35      30.344  47.138  46.564  1.00 45.85           O  
ATOM    280  CB  HIS A  35      32.967  46.110  45.067  1.00 74.40           C  
ATOM    281  CG  HIS A  35      33.341  44.750  44.544  1.00111.70           C  
ATOM    282  ND1 HIS A  35      33.045  44.327  43.266  1.00115.27           N  
ATOM    283  CD2 HIS A  35      33.971  43.708  45.139  1.00111.49           C  
ATOM    284  CE1 HIS A  35      33.487  43.094  43.096  1.00 98.87           C  
ATOM    285  NE2 HIS A  35      34.061  42.700  44.214  1.00110.94           N  
ATOM    286  N   ASP A  36      31.629  48.718  45.612  1.00 50.05           N  
ATOM    287  CA  ASP A  36      31.367  49.800  46.550  1.00 57.01           C  
ATOM    288  C   ASP A  36      31.430  51.097  45.772  1.00 43.43           C  
ATOM    289  O   ASP A  36      32.209  51.211  44.825  1.00 42.54           O  
ATOM    290  CB  ASP A  36      32.387  49.844  47.687  1.00 53.31           C  
ATOM    291  CG  ASP A  36      32.308  48.638  48.573  1.00 59.13           C  
ATOM    292  OD1 ASP A  36      31.310  48.512  49.313  1.00 61.59           O  
ATOM    293  OD2 ASP A  36      33.231  47.802  48.509  1.00 71.65           O  
ATOM    294  N   VAL A  37      30.607  52.061  46.156  1.00 43.98           N  
ATOM    295  CA  VAL A  37      30.599  53.362  45.506  1.00 41.35           C  
ATOM    296  C   VAL A  37      30.710  54.393  46.620  1.00 41.73           C  
ATOM    297  O   VAL A  37      29.800  54.516  47.442  1.00 42.28           O  
ATOM    298  CB  VAL A  37      29.346  53.588  44.650  1.00 37.36           C  
ATOM    299  CG1 VAL A  37      29.433  54.916  43.897  1.00 34.84           C  
ATOM    300  CG2 VAL A  37      29.178  52.439  43.654  1.00 42.33           C  
ATOM    301  N   ASP A  38      31.850  55.083  46.682  1.00 34.35           N  
ATOM    302  CA  ASP A  38      32.099  56.145  47.649  1.00 31.29           C  
ATOM    303  C   ASP A  38      31.768  57.494  47.028  1.00 29.07           C  
ATOM    304  O   ASP A  38      31.954  57.707  45.823  1.00 29.58           O  
ATOM    305  CB  ASP A  38      33.555  56.168  48.104  1.00 32.61           C  
ATOM    306  CG  ASP A  38      33.962  54.907  48.832  1.00 43.92           C  
ATOM    307  OD1 ASP A  38      33.064  54.229  49.370  1.00 45.04           O  
ATOM    308  OD2 ASP A  38      35.177  54.595  48.861  1.00 44.62           O  
ATOM    309  N   VAL A  39      31.297  58.406  47.872  1.00 28.13           N  
ATOM    310  CA  VAL A  39      31.004  59.778  47.477  1.00 28.16           C  
ATOM    311  C   VAL A  39      31.886  60.698  48.315  1.00 26.90           C  
ATOM    312  O   VAL A  39      32.027  60.497  49.524  1.00 30.84           O  
ATOM    313  CB  VAL A  39      29.508  60.114  47.663  1.00 28.83           C  
ATOM    314  CG1 VAL A  39      29.265  61.610  47.491  1.00 25.80           C  
ATOM    315  CG2 VAL A  39      28.666  59.345  46.636  1.00 28.41           C  
ATOM    316  N   ALA A  40      32.492  61.687  47.664  1.00 30.43           N  
ATOM    317  CA  ALA A  40      33.232  62.747  48.335  1.00 31.93           C  
ATOM    318  C   ALA A  40      32.444  64.043  48.191  1.00 26.67           C  
ATOM    319  O   ALA A  40      31.916  64.330  47.115  1.00 30.60           O  
ATOM    320  CB  ALA A  40      34.626  62.915  47.726  1.00 26.53           C  
ATOM    321  N   SER A  41      32.397  64.844  49.257  1.00 29.83           N  
ATOM    322  CA  SER A  41      31.533  66.020  49.245  1.00 31.95           C  
ATOM    323  C   SER A  41      32.173  67.165  50.026  1.00 30.95           C  
ATOM    324  O   SER A  41      32.948  66.939  50.953  1.00 31.37           O  
ATOM    325  CB  SER A  41      30.168  65.693  49.859  1.00 29.74           C  
ATOM    326  OG  SER A  41      29.303  66.803  49.748  1.00 35.18           O  
ATOM    327  N   SER A  42      31.790  68.397  49.690  1.00 31.42           N  
ATOM    328  CA  SER A  42      32.164  69.530  50.537  1.00 35.77           C  
ATOM    329  C   SER A  42      31.348  69.584  51.826  1.00 39.49           C  
ATOM    330  O   SER A  42      31.743  70.270  52.775  1.00 33.96           O  
ATOM    331  CB  SER A  42      32.008  70.846  49.766  1.00 35.45           C  
ATOM    332  OG  SER A  42      30.659  71.087  49.400  1.00 36.17           O  
ATOM    333  N   ALA A  43      30.231  68.858  51.888  1.00 34.72           N  
ATOM    334  CA  ALA A  43      29.458  68.781  53.122  1.00 38.33           C  
ATOM    335  C   ALA A  43      30.285  68.161  54.236  1.00 40.97           C  
ATOM    336  O   ALA A  43      31.057  67.223  54.013  1.00 35.78           O  
ATOM    337  CB  ALA A  43      28.178  67.964  52.912  1.00 32.50           C  
ATOM    338  N   LEU A  44      30.117  68.697  55.450  1.00 32.60           N  
ATOM    339  CA  LEU A  44      30.670  68.096  56.646  1.00 34.51           C  
ATOM    340  C   LEU A  44      29.707  67.049  57.191  1.00 33.10           C  
ATOM    341  O   LEU A  44      28.519  67.058  56.866  1.00 38.40           O  
ATOM    342  CB  LEU A  44      30.943  69.175  57.701  1.00 42.89           C  
ATOM    343  CG  LEU A  44      31.880  70.295  57.231  1.00 38.34           C  
ATOM    344  CD1 LEU A  44      31.784  71.524  58.146  1.00 39.74           C  
ATOM    345  CD2 LEU A  44      33.305  69.771  57.176  1.00 40.40           C  
ATOM    346  N   PRO A  45      30.198  66.129  58.020  1.00 33.54           N  
ATOM    347  CA  PRO A  45      29.358  64.983  58.430  1.00 39.33           C  
ATOM    348  C   PRO A  45      27.979  65.335  58.965  1.00 45.04           C  
ATOM    349  O   PRO A  45      26.995  64.702  58.564  1.00 38.69           O  
ATOM    350  CB  PRO A  45      30.227  64.303  59.489  1.00 38.48           C  
ATOM    351  CG  PRO A  45      31.627  64.594  59.034  1.00 35.92           C  
ATOM    352  CD  PRO A  45      31.595  65.980  58.458  1.00 35.62           C  
ATOM    353  N   GLN A  46      27.868  66.311  59.879  1.00 41.30           N  
ATOM    354  CA  GLN A  46      26.549  66.636  60.419  1.00 37.05           C  
ATOM    355  C   GLN A  46      25.647  67.276  59.376  1.00 38.41           C  
ATOM    356  O   GLN A  46      24.419  67.184  59.484  1.00 44.06           O  
ATOM    357  CB  GLN A  46      26.691  67.544  61.645  1.00 41.99           C  
ATOM    358  CG  GLN A  46      27.269  66.826  62.840  1.00 36.31           C  
ATOM    359  CD  GLN A  46      26.337  65.742  63.362  1.00 46.59           C  
ATOM    360  OE1 GLN A  46      25.127  65.775  63.105  1.00 45.42           O  
ATOM    361  NE2 GLN A  46      26.894  64.769  64.077  1.00 37.49           N  
ATOM    362  N   GLN A  47      26.219  67.924  58.358  1.00 32.74           N  
ATOM    363  CA  GLN A  47      25.392  68.438  57.275  1.00 36.08           C  
ATOM    364  C   GLN A  47      24.866  67.315  56.381  1.00 43.21           C  
ATOM    365  O   GLN A  47      23.760  67.427  55.837  1.00 40.74           O  
ATOM    366  CB  GLN A  47      26.177  69.465  56.462  1.00 36.70           C  
ATOM    367  CG  GLN A  47      26.697  70.628  57.321  1.00 41.57           C  
ATOM    368  CD  GLN A  47      27.588  71.578  56.551  1.00 45.29           C  
ATOM    369  OE1 GLN A  47      28.592  71.169  55.967  1.00 43.64           O  
ATOM    370  NE2 GLN A  47      27.217  72.861  56.529  1.00 42.31           N  
ATOM    371  N   VAL A  48      25.637  66.237  56.204  1.00 38.92           N  
ATOM    372  CA  VAL A  48      25.108  65.072  55.491  1.00 38.40           C  
ATOM    373  C   VAL A  48      23.929  64.487  56.264  1.00 40.64           C  
ATOM    374  O   VAL A  48      22.871  64.194  55.696  1.00 41.64           O  
ATOM    375  CB  VAL A  48      26.210  64.015  55.275  1.00 37.15           C  
ATOM    376  CG1 VAL A  48      25.636  62.807  54.510  1.00 35.10           C  
ATOM    377  CG2 VAL A  48      27.404  64.603  54.514  1.00 31.81           C  
ATOM    378  N   LYS A  49      24.100  64.315  57.578  1.00 39.77           N  
ATOM    379  CA  LYS A  49      23.052  63.712  58.398  1.00 48.37           C  
ATOM    380  C   LYS A  49      21.750  64.501  58.325  1.00 51.22           C  
ATOM    381  O   LYS A  49      20.666  63.919  58.443  1.00 50.24           O  
ATOM    382  CB  LYS A  49      23.526  63.590  59.846  1.00 43.84           C  
ATOM    383  CG  LYS A  49      24.626  62.553  60.039  1.00 45.63           C  
ATOM    384  CD  LYS A  49      25.149  62.521  61.467  1.00 47.50           C  
ATOM    385  CE  LYS A  49      24.202  61.768  62.392  1.00 57.10           C  
ATOM    386  NZ  LYS A  49      22.934  62.504  62.581  1.00 71.37           N  
ATOM    387  N   VAL A  50      21.832  65.819  58.130  1.00 44.28           N  
ATOM    388  CA  VAL A  50      20.625  66.626  58.003  1.00 44.19           C  
ATOM    389  C   VAL A  50      19.844  66.243  56.760  1.00 51.65           C  
ATOM    390  O   VAL A  50      18.610  66.327  56.743  1.00 41.05           O  
ATOM    391  CB  VAL A  50      20.986  68.125  57.997  1.00 45.04           C  
ATOM    392  CG1 VAL A  50      19.779  68.958  57.635  1.00 54.76           C  
ATOM    393  CG2 VAL A  50      21.535  68.543  59.346  1.00 48.55           C  
ATOM    394  N   LEU A  51      20.533  65.812  55.703  1.00 42.65           N  
ATOM    395  CA  LEU A  51      19.904  65.642  54.403  1.00 41.80           C  
ATOM    396  C   LEU A  51      19.329  64.251  54.168  1.00 42.23           C  
ATOM    397  O   LEU A  51      18.590  64.071  53.196  1.00 45.18           O  
ATOM    398  CB  LEU A  51      20.914  65.961  53.292  1.00 44.29           C  
ATOM    399  CG  LEU A  51      21.475  67.383  53.316  1.00 45.54           C  
ATOM    400  CD1 LEU A  51      22.434  67.596  52.169  1.00 38.90           C  
ATOM    401  CD2 LEU A  51      20.335  68.403  53.262  1.00 42.24           C  
ATOM    402  N   PHE A  52      19.646  63.269  55.006  1.00 40.79           N  
ATOM    403  CA  PHE A  52      19.239  61.887  54.764  1.00 46.71           C  
ATOM    404  C   PHE A  52      18.616  61.289  56.020  1.00 51.06           C  
ATOM    405  O   PHE A  52      19.139  61.455  57.127  1.00 50.39           O  
ATOM    406  CB  PHE A  52      20.442  61.029  54.298  1.00 38.13           C  
ATOM    407  CG  PHE A  52      21.061  61.512  53.003  1.00 37.43           C  
ATOM    408  CD1 PHE A  52      20.523  61.145  51.784  1.00 39.04           C  
ATOM    409  CD2 PHE A  52      22.165  62.349  53.019  1.00 37.85           C  
ATOM    410  CE1 PHE A  52      21.068  61.599  50.587  1.00 41.25           C  
ATOM    411  CE2 PHE A  52      22.725  62.810  51.836  1.00 32.91           C  
ATOM    412  CZ  PHE A  52      22.177  62.439  50.615  1.00 31.44           C  
ATOM    413  N   ASP A  53      17.507  60.566  55.835  1.00 55.69           N  
ATOM    414  CA  ASP A  53      16.759  60.036  56.977  1.00 63.11           C  
ATOM    415  C   ASP A  53      17.584  59.046  57.796  1.00 56.40           C  
ATOM    416  O   ASP A  53      17.542  59.067  59.031  1.00 52.12           O  
ATOM    417  CB  ASP A  53      15.475  59.359  56.498  1.00 60.03           C  
ATOM    418  CG  ASP A  53      14.554  60.311  55.772  1.00 70.04           C  
ATOM    419  OD1 ASP A  53      14.545  61.509  56.124  1.00 71.68           O  
ATOM    420  OD2 ASP A  53      13.850  59.864  54.839  1.00 82.41           O  
ATOM    421  N   ARG A  54      18.261  58.125  57.139  1.00 50.35           N  
ATOM    422  CA  ARG A  54      19.000  57.077  57.806  1.00 48.55           C  
ATOM    423  C   ARG A  54      20.453  57.079  57.508  1.00 49.14           C  
ATOM    424  O   ARG A  54      20.839  56.990  56.347  1.00 46.99           O  
ATOM    425  CB  ARG A  54      18.438  55.738  57.406  1.00 50.38           C  
ATOM    426  CG  ARG A  54      16.972  55.600  57.697  1.00 66.77           C  
ATOM    427  CD  ARG A  54      16.468  54.240  57.301  1.00 72.14           C  
ATOM    428  NE  ARG A  54      17.083  53.162  58.036  1.00 72.90           N  
ATOM    429  CZ  ARG A  54      17.434  52.027  57.472  1.00 75.53           C  
ATOM    430  NH1 ARG A  54      17.247  51.872  56.193  1.00 75.13           N  
ATOM    431  NH2 ARG A  54      17.982  51.067  58.164  1.00 75.97           N  
ATOM    432  N   THR A  55      21.252  57.109  58.534  1.00 40.90           N  
ATOM    433  CA  THR A  55      22.692  57.298  58.478  1.00 49.56           C  
ATOM    434  C   THR A  55      23.349  56.472  59.579  1.00 47.23           C  
ATOM    435  O   THR A  55      22.763  56.268  60.641  1.00 52.89           O  
ATOM    436  CB  THR A  55      23.019  58.787  58.646  1.00 53.94           C  
ATOM    437  OG1 THR A  55      22.824  59.470  57.400  1.00 55.67           O  
ATOM    438  CG2 THR A  55      24.424  58.978  59.145  1.00 62.30           C  
ATOM    439  N   VAL A  56      24.556  55.987  59.325  1.00 47.05           N  
ATOM    440  CA  VAL A  56      25.381  55.312  60.325  1.00 45.52           C  
ATOM    441  C   VAL A  56      26.638  56.143  60.534  1.00 54.56           C  
ATOM    442  O   VAL A  56      27.309  56.516  59.559  1.00 46.48           O  
ATOM    443  CB  VAL A  56      25.741  53.876  59.902  1.00 50.68           C  
ATOM    444  CG1 VAL A  56      26.683  53.245  60.921  1.00 44.61           C  
ATOM    445  CG2 VAL A  56      24.492  53.032  59.733  1.00 51.53           C  
ATOM    446  N   ASP A  57      26.977  56.409  61.802  1.00 48.80           N  
ATOM    447  CA  ASP A  57      27.892  57.485  62.163  1.00 45.65           C  
ATOM    448  C   ASP A  57      29.259  57.012  62.621  1.00 49.61           C  
ATOM    449  O   ASP A  57      30.035  57.822  63.142  1.00 54.47           O  
ATOM    450  CB  ASP A  57      27.282  58.349  63.267  1.00 56.83           C  
ATOM    451  CG  ASP A  57      26.044  59.064  62.815  1.00 59.55           C  
ATOM    452  OD1 ASP A  57      25.762  59.032  61.601  1.00 62.93           O  
ATOM    453  OD2 ASP A  57      25.353  59.652  63.664  1.00 73.58           O  
ATOM    454  N   THR A  58      29.582  55.733  62.454  1.00 42.06           N  
ATOM    455  CA  THR A  58      30.768  55.213  63.128  1.00 44.36           C  
ATOM    456  C   THR A  58      32.054  55.880  62.641  1.00 59.71           C  
ATOM    457  O   THR A  58      33.026  55.976  63.402  1.00 56.50           O  
ATOM    458  CB  THR A  58      30.834  53.696  62.958  1.00 59.14           C  
ATOM    459  OG1 THR A  58      30.906  53.373  61.567  1.00 67.29           O  
ATOM    460  CG2 THR A  58      29.580  53.053  63.542  1.00 60.56           C  
ATOM    461  N   GLY A  59      32.084  56.363  61.393  1.00 50.80           N  
ATOM    462  CA  GLY A  59      33.289  56.979  60.861  1.00 40.64           C  
ATOM    463  C   GLY A  59      33.330  58.499  60.900  1.00 47.66           C  
ATOM    464  O   GLY A  59      34.179  59.115  60.244  1.00 41.24           O  
ATOM    465  N   ILE A  60      32.438  59.117  61.680  1.00 40.35           N  
ATOM    466  CA  ILE A  60      32.265  60.569  61.623  1.00 50.97           C  
ATOM    467  C   ILE A  60      33.567  61.301  61.920  1.00 54.07           C  
ATOM    468  O   ILE A  60      33.859  62.337  61.306  1.00 42.59           O  
ATOM    469  CB  ILE A  60      31.148  61.019  62.578  1.00 52.13           C  
ATOM    470  CG1 ILE A  60      29.786  60.712  61.970  1.00 56.10           C  
ATOM    471  CG2 ILE A  60      31.267  62.507  62.865  1.00 57.89           C  
ATOM    472  CD1 ILE A  60      28.635  61.422  62.668  1.00 63.66           C  
ATOM    473  N   ASP A  61      34.353  60.796  62.880  1.00 51.29           N  
ATOM    474  CA  ASP A  61      35.611  61.451  63.255  1.00 49.29           C  
ATOM    475  C   ASP A  61      36.585  61.532  62.091  1.00 52.81           C  
ATOM    476  O   ASP A  61      37.458  62.410  62.079  1.00 55.69           O  
ATOM    477  CB  ASP A  61      36.286  60.707  64.408  1.00 54.90           C  
ATOM    478  CG  ASP A  61      35.493  60.776  65.686  1.00 75.20           C  
ATOM    479  OD1 ASP A  61      34.685  61.719  65.838  1.00 72.50           O  
ATOM    480  OD2 ASP A  61      35.686  59.885  66.542  1.00 98.60           O  
ATOM    481  N   HIS A  62      36.490  60.605  61.142  1.00 48.33           N  
ATOM    482  CA  HIS A  62      37.329  60.623  59.952  1.00 56.60           C  
ATOM    483  C   HIS A  62      36.665  61.334  58.782  1.00 47.28           C  
ATOM    484  O   HIS A  62      37.225  61.336  57.681  1.00 43.57           O  
ATOM    485  CB  HIS A  62      37.702  59.193  59.528  1.00 57.88           C  
ATOM    486  CG  HIS A  62      38.429  58.413  60.583  1.00 74.30           C  
ATOM    487  ND1 HIS A  62      38.873  58.979  61.760  1.00 88.33           N  
ATOM    488  CD2 HIS A  62      38.784  57.107  60.635  1.00 84.84           C  
ATOM    489  CE1 HIS A  62      39.471  58.055  62.491  1.00 89.63           C  
ATOM    490  NE2 HIS A  62      39.431  56.910  61.832  1.00107.23           N  
ATOM    491  N   GLY A  63      35.483  61.909  58.990  1.00 38.96           N  
ATOM    492  CA  GLY A  63      34.773  62.622  57.952  1.00 43.99           C  
ATOM    493  C   GLY A  63      33.719  61.834  57.211  1.00 39.10           C  
ATOM    494  O   GLY A  63      33.131  62.371  56.265  1.00 36.60           O  
ATOM    495  N   THR A  64      33.417  60.604  57.636  1.00 37.56           N  
ATOM    496  CA  THR A  64      32.591  59.684  56.858  1.00 39.63           C  
ATOM    497  C   THR A  64      31.261  59.395  57.539  1.00 37.33           C  
ATOM    498  O   THR A  64      31.215  59.086  58.736  1.00 40.66           O  
ATOM    499  CB  THR A  64      33.322  58.364  56.622  1.00 40.42           C  
ATOM    500  OG1 THR A  64      34.532  58.619  55.908  1.00 43.51           O  
ATOM    501  CG2 THR A  64      32.445  57.406  55.819  1.00 37.53           C  
ATOM    502  N   VAL A  65      30.194  59.467  56.749  1.00 35.18           N  
ATOM    503  CA  VAL A  65      28.843  59.092  57.132  1.00 37.96           C  
ATOM    504  C   VAL A  65      28.346  58.065  56.122  1.00 37.54           C  
ATOM    505  O   VAL A  65      28.472  58.278  54.914  1.00 34.01           O  
ATOM    506  CB  VAL A  65      27.922  60.328  57.156  1.00 40.26           C  
ATOM    507  CG1 VAL A  65      26.473  59.936  57.270  1.00 43.61           C  
ATOM    508  CG2 VAL A  65      28.324  61.251  58.312  1.00 47.63           C  
ATOM    509  N   LEU A  66      27.773  56.960  56.611  1.00 40.64           N  
ATOM    510  CA  LEU A  66      27.160  55.957  55.745  1.00 36.79           C  
ATOM    511  C   LEU A  66      25.683  56.289  55.551  1.00 37.07           C  
ATOM    512  O   LEU A  66      24.910  56.285  56.515  1.00 41.47           O  
ATOM    513  CB  LEU A  66      27.318  54.552  56.328  1.00 39.18           C  
ATOM    514  CG  LEU A  66      26.688  53.415  55.513  1.00 40.88           C  
ATOM    515  CD1 LEU A  66      27.349  53.284  54.156  1.00 35.72           C  
ATOM    516  CD2 LEU A  66      26.783  52.092  56.276  1.00 46.61           C  
ATOM    517  N   VAL A  67      25.294  56.566  54.312  1.00 33.27           N  
ATOM    518  CA  VAL A  67      23.927  56.929  53.957  1.00 33.72           C  
ATOM    519  C   VAL A  67      23.198  55.675  53.488  1.00 41.25           C  
ATOM    520  O   VAL A  67      23.678  54.964  52.597  1.00 40.32           O  
ATOM    521  CB  VAL A  67      23.913  58.014  52.871  1.00 35.98           C  
ATOM    522  CG1 VAL A  67      22.513  58.181  52.269  1.00 36.56           C  
ATOM    523  CG2 VAL A  67      24.444  59.340  53.435  1.00 35.40           C  
ATOM    524  N   LEU A  68      22.044  55.391  54.099  1.00 42.40           N  
ATOM    525  CA  LEU A  68      21.227  54.226  53.763  1.00 39.98           C  
ATOM    526  C   LEU A  68      20.065  54.707  52.912  1.00 36.92           C  
ATOM    527  O   LEU A  68      19.232  55.492  53.379  1.00 43.95           O  
ATOM    528  CB  LEU A  68      20.730  53.528  55.027  1.00 45.47           C  
ATOM    529  CG  LEU A  68      21.863  53.031  55.914  1.00 38.67           C  
ATOM    530  CD1 LEU A  68      21.318  52.430  57.194  1.00 50.04           C  
ATOM    531  CD2 LEU A  68      22.684  52.017  55.146  1.00 41.27           C  
ATOM    532  N   LEU A  69      20.023  54.260  51.661  1.00 37.38           N  
ATOM    533  CA  LEU A  69      19.044  54.757  50.710  1.00 42.75           C  
ATOM    534  C   LEU A  69      18.741  53.680  49.679  1.00 47.29           C  
ATOM    535  O   LEU A  69      19.653  53.029  49.164  1.00 42.73           O  
ATOM    536  CB  LEU A  69      19.558  56.027  50.020  1.00 39.61           C  
ATOM    537  CG  LEU A  69      18.543  56.849  49.235  1.00 45.77           C  
ATOM    538  CD1 LEU A  69      17.460  57.325  50.188  1.00 52.69           C  
ATOM    539  CD2 LEU A  69      19.216  58.027  48.557  1.00 41.75           C  
ATOM    540  N   ASP A  70      17.452  53.516  49.371  1.00 48.84           N  
ATOM    541  CA  ASP A  70      16.996  52.540  48.379  1.00 50.31           C  
ATOM    542  C   ASP A  70      17.584  51.154  48.630  1.00 45.42           C  
ATOM    543  O   ASP A  70      17.890  50.417  47.691  1.00 49.60           O  
ATOM    544  CB  ASP A  70      17.327  52.992  46.955  1.00 46.44           C  
ATOM    545  CG  ASP A  70      16.643  54.294  46.574  1.00 50.60           C  
ATOM    546  OD1 ASP A  70      15.973  54.898  47.435  1.00 50.83           O  
ATOM    547  OD2 ASP A  70      16.781  54.715  45.399  1.00 58.82           O  
ATOM    548  N   GLY A  71      17.769  50.790  49.898  1.00 42.90           N  
ATOM    549  CA  GLY A  71      18.319  49.491  50.227  1.00 48.14           C  
ATOM    550  C   GLY A  71      19.810  49.331  50.014  1.00 54.60           C  
ATOM    551  O   GLY A  71      20.313  48.204  50.090  1.00 49.83           O  
ATOM    552  N   GLU A  72      20.539  50.413  49.757  1.00 44.79           N  
ATOM    553  CA  GLU A  72      21.984  50.376  49.594  1.00 41.29           C  
ATOM    554  C   GLU A  72      22.638  51.212  50.684  1.00 43.75           C  
ATOM    555  O   GLU A  72      21.976  51.956  51.408  1.00 44.52           O  
ATOM    556  CB  GLU A  72      22.395  50.892  48.207  1.00 41.96           C  
ATOM    557  CG  GLU A  72      21.671  50.219  47.059  1.00 42.95           C  
ATOM    558  CD  GLU A  72      22.077  48.770  46.884  1.00 49.86           C  
ATOM    559  OE1 GLU A  72      23.143  48.364  47.416  1.00 48.67           O  
ATOM    560  OE2 GLU A  72      21.325  48.037  46.212  1.00 55.16           O  
ATOM    561  N   GLY A  73      23.954  51.064  50.804  1.00 44.34           N  
ATOM    562  CA  GLY A  73      24.736  51.914  51.677  1.00 42.01           C  
ATOM    563  C   GLY A  73      25.716  52.672  50.804  1.00 40.12           C  
ATOM    564  O   GLY A  73      26.362  52.076  49.935  1.00 42.14           O  
ATOM    565  N   ILE A  74      25.836  53.980  51.008  1.00 34.98           N  
ATOM    566  CA  ILE A  74      26.750  54.824  50.236  1.00 34.31           C  
ATOM    567  C   ILE A  74      27.555  55.599  51.279  1.00 35.12           C  
ATOM    568  O   ILE A  74      26.985  56.383  52.046  1.00 35.51           O  
ATOM    569  CB  ILE A  74      26.055  55.782  49.257  1.00 35.06           C  
ATOM    570  CG1 ILE A  74      25.160  55.013  48.267  1.00 36.27           C  
ATOM    571  CG2 ILE A  74      27.069  56.694  48.547  1.00 30.26           C  
ATOM    572  CD1 ILE A  74      25.900  53.999  47.397  1.00 33.34           C  
ATOM    573  N   GLU A  75      28.872  55.377  51.317  1.00 31.01           N  
ATOM    574  CA  GLU A  75      29.729  56.172  52.193  1.00 37.97           C  
ATOM    575  C   GLU A  75      29.912  57.574  51.626  1.00 35.85           C  
ATOM    576  O   GLU A  75      30.287  57.737  50.460  1.00 34.43           O  
ATOM    577  CB  GLU A  75      31.094  55.514  52.362  1.00 33.14           C  
ATOM    578  CG  GLU A  75      31.046  54.136  52.974  1.00 49.66           C  
ATOM    579  CD  GLU A  75      32.329  53.787  53.702  1.00 65.83           C  
ATOM    580  OE1 GLU A  75      32.312  52.821  54.490  1.00 69.99           O  
ATOM    581  OE2 GLU A  75      33.353  54.486  53.491  1.00 60.13           O  
ATOM    582  N   VAL A  76      29.642  58.588  52.448  1.00 31.86           N  
ATOM    583  CA  VAL A  76      29.813  59.987  52.067  1.00 29.10           C  
ATOM    584  C   VAL A  76      30.885  60.567  52.975  1.00 33.52           C  
ATOM    585  O   VAL A  76      30.723  60.590  54.207  1.00 31.44           O  
ATOM    586  CB  VAL A  76      28.505  60.783  52.184  1.00 33.67           C  
ATOM    587  CG1 VAL A  76      28.703  62.215  51.650  1.00 27.41           C  
ATOM    588  CG2 VAL A  76      27.368  60.074  51.453  1.00 32.18           C  
ATOM    589  N   THR A  77      31.991  61.010  52.383  1.00 32.02           N  
ATOM    590  CA  THR A  77      33.142  61.468  53.147  1.00 31.69           C  
ATOM    591  C   THR A  77      33.504  62.890  52.736  1.00 30.66           C  
ATOM    592  O   THR A  77      33.595  63.190  51.543  1.00 29.57           O  
ATOM    593  CB  THR A  77      34.318  60.523  52.940  1.00 37.18           C  
ATOM    594  OG1 THR A  77      33.904  59.197  53.307  1.00 37.30           O  
ATOM    595  CG2 THR A  77      35.503  60.955  53.793  1.00 37.81           C  
ATOM    596  N   THR A  78      33.722  63.755  53.723  1.00 36.88           N  
ATOM    597  CA  THR A  78      34.089  65.126  53.410  1.00 33.74           C  
ATOM    598  C   THR A  78      35.491  65.146  52.810  1.00 30.59           C  
ATOM    599  O   THR A  78      36.294  64.241  53.042  1.00 30.60           O  
ATOM    600  CB  THR A  78      34.007  66.004  54.671  1.00 33.81           C  
ATOM    601  OG1 THR A  78      33.885  67.374  54.277  1.00 35.60           O  
ATOM    602  CG2 THR A  78      35.247  65.842  55.530  1.00 37.75           C  
ATOM    603  N   PHE A  79      35.772  66.160  51.992  1.00 32.25           N  
ATOM    604  CA  PHE A  79      37.131  66.317  51.488  1.00 32.28           C  
ATOM    605  C   PHE A  79      38.098  66.270  52.672  1.00 35.26           C  
ATOM    606  O   PHE A  79      37.962  67.049  53.620  1.00 36.07           O  
ATOM    607  CB  PHE A  79      37.297  67.645  50.734  1.00 33.36           C  
ATOM    608  CG  PHE A  79      36.325  67.875  49.592  1.00 33.81           C  
ATOM    609  CD1 PHE A  79      35.871  66.841  48.778  1.00 28.24           C  
ATOM    610  CD2 PHE A  79      35.896  69.164  49.314  1.00 34.95           C  
ATOM    611  CE1 PHE A  79      34.994  67.108  47.720  1.00 34.56           C  
ATOM    612  CE2 PHE A  79      35.023  69.428  48.264  1.00 33.42           C  
ATOM    613  CZ  PHE A  79      34.574  68.404  47.471  1.00 33.83           C  
ATOM    614  N   ARG A  80      39.074  65.361  52.632  1.00 32.98           N  
ATOM    615  CA  ARG A  80      39.973  65.192  53.769  1.00 35.13           C  
ATOM    616  C   ARG A  80      41.310  64.646  53.305  1.00 35.62           C  
ATOM    617  O   ARG A  80      41.438  64.110  52.197  1.00 38.88           O  
ATOM    618  CB  ARG A  80      39.399  64.226  54.813  1.00 34.44           C  
ATOM    619  CG  ARG A  80      39.108  62.878  54.166  1.00 47.50           C  
ATOM    620  CD  ARG A  80      38.928  61.781  55.164  1.00 55.44           C  
ATOM    621  NE  ARG A  80      39.003  60.470  54.522  1.00 56.62           N  
ATOM    622  CZ  ARG A  80      38.752  59.325  55.152  1.00 60.18           C  
ATOM    623  NH1 ARG A  80      38.415  59.342  56.432  1.00 63.51           N  
ATOM    624  NH2 ARG A  80      38.841  58.169  54.508  1.00 69.19           N  
ATOM    625  N   THR A  81      42.311  64.785  54.176  1.00 31.13           N  
ATOM    626  CA  THR A  81      43.561  64.045  54.083  1.00 35.64           C  
ATOM    627  C   THR A  81      43.806  63.331  55.409  1.00 45.51           C  
ATOM    628  O   THR A  81      43.250  63.698  56.453  1.00 48.42           O  
ATOM    629  CB  THR A  81      44.773  64.938  53.750  1.00 40.16           C  
ATOM    630  OG1 THR A  81      45.022  65.829  54.842  1.00 45.86           O  
ATOM    631  CG2 THR A  81      44.546  65.733  52.475  1.00 41.28           C  
ATOM    632  N   GLU A  82      44.647  62.305  55.380  1.00 56.78           N  
ATOM    633  CA  GLU A  82      44.959  61.484  56.542  1.00 63.16           C  
ATOM    634  C   GLU A  82      46.451  61.197  56.602  1.00 70.20           C  
ATOM    635  O   GLU A  82      47.124  61.106  55.573  1.00 68.83           O  
ATOM    636  CB  GLU A  82      44.258  60.175  56.493  1.00 62.31           C  
ATOM    637  CG  GLU A  82      42.852  60.318  56.749  1.00 67.76           C  
ATOM    638  CD  GLU A  82      42.240  58.981  57.025  1.00 79.62           C  
ATOM    639  OE1 GLU A  82      42.064  58.617  58.217  1.00 80.33           O  
ATOM    640  OE2 GLU A  82      41.974  58.275  56.029  1.00 80.47           O  
ATOM    641  N   SER A  83      46.967  61.018  57.812  1.00 76.35           N  
ATOM    642  CA  SER A  83      48.352  60.592  57.950  1.00 82.07           C  
ATOM    643  C   SER A  83      48.441  59.587  59.079  1.00 88.11           C  
ATOM    644  O   SER A  83      47.725  59.702  60.067  1.00 88.21           O  
ATOM    645  CB  SER A  83      49.292  61.764  58.208  1.00 83.36           C  
ATOM    646  OG  SER A  83      50.566  61.474  57.663  1.00 85.26           O  
ATOM    647  N   SER A  84      49.297  58.591  58.907  1.00 94.01           N  
ATOM    648  CA  SER A  84      49.490  57.541  59.891  1.00105.51           C  
ATOM    649  C   SER A  84      50.794  57.793  60.617  1.00122.11           C  
ATOM    650  O   SER A  84      51.825  58.050  59.983  1.00115.95           O  
ATOM    651  CB  SER A  84      49.512  56.157  59.248  1.00100.13           C  
ATOM    652  OG  SER A  84      48.204  55.707  58.994  1.00 94.33           O  
ATOM    653  N   TYR A  85      50.729  57.731  61.943  1.00143.64           N  
ATOM    654  CA  TYR A  85      51.901  57.829  62.793  1.00157.08           C  
ATOM    655  C   TYR A  85      52.623  56.492  62.838  1.00162.53           C  
ATOM    656  O   TYR A  85      52.021  55.432  62.646  1.00158.21           O  
ATOM    657  CB  TYR A  85      51.505  58.250  64.207  1.00165.57           C  
ATOM    658  CG  TYR A  85      50.849  59.602  64.274  1.00166.72           C  
ATOM    659  CD1 TYR A  85      51.599  60.758  64.141  1.00167.81           C  
ATOM    660  CD2 TYR A  85      49.484  59.726  64.474  1.00161.46           C  
ATOM    661  CE1 TYR A  85      51.012  61.993  64.201  1.00163.87           C  
ATOM    662  CE2 TYR A  85      48.890  60.963  64.535  1.00153.80           C  
ATOM    663  CZ  TYR A  85      49.662  62.090  64.399  1.00155.14           C  
ATOM    664  OH  TYR A  85      49.086  63.328  64.456  1.00147.09           O  
ATOM    665  N   SER A  86      53.930  56.549  63.096  1.00167.54           N  
ATOM    666  CA  SER A  86      54.693  55.320  63.243  1.00164.80           C  
ATOM    667  C   SER A  86      54.151  54.448  64.364  1.00167.59           C  
ATOM    668  O   SER A  86      54.397  53.241  64.367  1.00163.03           O  
ATOM    669  CB  SER A  86      56.155  55.646  63.489  1.00161.30           C  
ATOM    670  OG  SER A  86      56.256  56.540  64.568  1.00170.91           O  
ATOM    671  N   ASP A  87      53.415  55.028  65.308  1.00174.75           N  
ATOM    672  CA  ASP A  87      52.700  54.274  66.334  1.00176.03           C  
ATOM    673  C   ASP A  87      51.281  54.007  65.833  1.00174.32           C  
ATOM    674  O   ASP A  87      50.489  54.945  65.683  1.00177.69           O  
ATOM    675  CB  ASP A  87      52.692  55.058  67.647  1.00178.49           C  
ATOM    676  CG  ASP A  87      51.892  54.379  68.743  1.00177.07           C  
ATOM    677  OD1 ASP A  87      51.488  53.219  68.565  1.00175.14           O1-
ATOM    678  OD2 ASP A  87      51.664  55.008  69.793  1.00178.48           O  
ATOM    679  N   ASN A  88      50.953  52.725  65.564  1.00166.60           N  
ATOM    680  CA  ASN A  88      49.624  52.380  65.066  1.00155.59           C  
ATOM    681  C   ASN A  88      48.596  52.188  66.184  1.00160.02           C  
ATOM    682  O   ASN A  88      47.579  51.521  65.967  1.00155.33           O  
ATOM    683  CB  ASN A  88      49.686  51.147  64.154  1.00135.93           C  
ATOM    684  CG  ASN A  88      49.879  49.852  64.900  1.00117.58           C  
ATOM    685  OD1 ASN A  88      48.937  49.283  65.418  1.00115.74           O  
ATOM    686  ND2 ASN A  88      51.091  49.347  64.896  1.00110.02           N  
ATOM    687  N   ARG A  89      48.843  52.774  67.362  1.00168.78           N  
ATOM    688  CA  ARG A  89      47.840  52.918  68.412  1.00169.00           C  
ATOM    689  C   ARG A  89      47.079  54.228  68.299  1.00169.90           C  
ATOM    690  O   ARG A  89      45.896  54.279  68.641  1.00168.93           O  
ATOM    691  CB  ARG A  89      48.489  52.853  69.800  1.00171.74           C  
ATOM    692  CG  ARG A  89      49.477  51.726  70.001  1.00169.29           C  
ATOM    693  CD  ARG A  89      50.106  51.765  71.381  1.00164.80           C  
ATOM    694  NE  ARG A  89      49.581  50.700  72.222  1.00158.94           N  
ATOM    695  CZ  ARG A  89      50.289  50.059  73.140  1.00153.41           C  
ATOM    696  NH1 ARG A  89      51.556  50.373  73.333  1.00150.70           N  
ATOM    697  NH2 ARG A  89      49.732  49.097  73.853  1.00150.90           N  
ATOM    698  N   ARG A  90      47.738  55.284  67.843  1.00171.14           N  
ATOM    699  CA  ARG A  90      47.134  56.606  67.709  1.00168.25           C  
ATOM    700  C   ARG A  90      46.236  56.638  66.477  1.00163.40           C  
ATOM    701  O   ARG A  90      46.703  56.314  65.379  1.00159.33           O  
ATOM    702  CB  ARG A  90      48.231  57.666  67.584  1.00171.18           C  
ATOM    703  CG  ARG A  90      49.417  57.418  68.504  1.00176.04           C  
ATOM    704  CD  ARG A  90      50.704  58.018  67.971  1.00179.71           C  
ATOM    705  NE  ARG A  90      50.603  59.456  67.773  1.00180.20           N  
ATOM    706  CZ  ARG A  90      51.641  60.244  67.532  1.00180.30           C  
ATOM    707  NH1 ARG A  90      52.857  59.733  67.466  1.00182.50           N  
ATOM    708  NH2 ARG A  90      51.463  61.542  67.360  1.00180.12           N  
ATOM    709  N   PRO A  91      44.960  57.027  66.605  1.00157.22           N  
ATOM    710  CA  PRO A  91      44.095  57.069  65.420  1.00144.76           C  
ATOM    711  C   PRO A  91      44.697  57.991  64.377  1.00131.76           C  
ATOM    712  O   PRO A  91      45.586  58.800  64.655  1.00131.28           O  
ATOM    713  CB  PRO A  91      42.759  57.602  65.950  1.00140.95           C  
ATOM    714  CG  PRO A  91      43.116  58.336  67.192  1.00145.56           C  
ATOM    715  CD  PRO A  91      44.317  57.646  67.779  1.00152.96           C  
ATOM    716  N   ASP A  92      44.256  57.818  63.147  1.00121.49           N  
ATOM    717  CA  ASP A  92      44.861  58.603  62.088  1.00114.13           C  
ATOM    718  C   ASP A  92      44.607  60.092  62.344  1.00104.20           C  
ATOM    719  O   ASP A  92      43.526  60.478  62.794  1.00103.93           O  
ATOM    720  CB  ASP A  92      44.310  58.146  60.724  1.00106.17           C  
ATOM    721  CG  ASP A  92      44.959  56.836  60.224  1.00106.27           C  
ATOM    722  OD1 ASP A  92      45.905  56.328  60.866  1.00104.79           O  
ATOM    723  OD2 ASP A  92      44.526  56.319  59.171  1.00101.63           O  
ATOM    724  N   SER A  93      45.630  60.928  62.103  1.00 97.53           N  
ATOM    725  CA  SER A  93      45.438  62.380  62.086  1.00 89.60           C  
ATOM    726  C   SER A  93      44.699  62.791  60.816  1.00 74.82           C  
ATOM    727  O   SER A  93      45.185  62.553  59.712  1.00 74.26           O  
ATOM    728  CB  SER A  93      46.775  63.105  62.160  1.00 96.36           C  
ATOM    729  OG  SER A  93      47.473  62.989  60.934  1.00 93.24           O  
ATOM    730  N   VAL A  94      43.534  63.407  60.975  1.00 67.41           N  
ATOM    731  CA  VAL A  94      42.588  63.667  59.898  1.00 60.99           C  
ATOM    732  C   VAL A  94      42.437  65.182  59.760  1.00 56.88           C  
ATOM    733  O   VAL A  94      42.136  65.871  60.734  1.00 55.70           O  
ATOM    734  CB  VAL A  94      41.236  62.983  60.182  1.00 63.54           C  
ATOM    735  CG1 VAL A  94      40.248  63.227  59.068  1.00 55.97           C  
ATOM    736  CG2 VAL A  94      41.430  61.486  60.423  1.00 68.69           C  
ATOM    737  N   GLU A  95      42.603  65.710  58.554  1.00 50.78           N  
ATOM    738  CA  GLU A  95      42.455  67.151  58.366  1.00 49.87           C  
ATOM    739  C   GLU A  95      41.492  67.526  57.240  1.00 51.41           C  
ATOM    740  O   GLU A  95      41.875  67.519  56.070  1.00 52.85           O  
ATOM    741  CB  GLU A  95      43.821  67.797  58.120  1.00 53.94           C  
ATOM    742  CG  GLU A  95      43.749  69.233  57.626  1.00 62.45           C  
ATOM    743  CD  GLU A  95      45.066  69.720  57.055  1.00 69.63           C  
ATOM    744  OE1 GLU A  95      46.126  69.356  57.606  1.00 68.98           O  
ATOM    745  OE2 GLU A  95      45.041  70.467  56.054  1.00 60.30           O  
ATOM    746  N   PHE A  96      40.248  67.860  57.583  1.00 34.95           N  
ATOM    747  CA  PHE A  96      39.294  68.248  56.552  1.00 39.36           C  
ATOM    748  C   PHE A  96      39.895  69.375  55.724  1.00 40.83           C  
ATOM    749  O   PHE A  96      40.548  70.275  56.264  1.00 46.54           O  
ATOM    750  CB  PHE A  96      37.962  68.695  57.167  1.00 40.84           C  
ATOM    751  CG  PHE A  96      37.274  67.638  57.994  1.00 40.38           C  
ATOM    752  CD1 PHE A  96      37.721  66.324  57.995  1.00 37.10           C  
ATOM    753  CD2 PHE A  96      36.171  67.965  58.775  1.00 34.96           C  
ATOM    754  CE1 PHE A  96      37.083  65.357  58.759  1.00 40.39           C  
ATOM    755  CE2 PHE A  96      35.526  67.000  59.539  1.00 41.77           C  
ATOM    756  CZ  PHE A  96      35.985  65.692  59.532  1.00 46.06           C  
ATOM    757  N   VAL A  97      39.714  69.298  54.405  1.00 36.54           N  
ATOM    758  CA  VAL A  97      40.246  70.275  53.471  1.00 37.59           C  
ATOM    759  C   VAL A  97      39.073  70.828  52.677  1.00 40.37           C  
ATOM    760  O   VAL A  97      37.968  70.281  52.687  1.00 39.10           O  
ATOM    761  CB  VAL A  97      41.342  69.683  52.547  1.00 42.39           C  
ATOM    762  CG1 VAL A  97      42.510  69.165  53.391  1.00 42.46           C  
ATOM    763  CG2 VAL A  97      40.797  68.557  51.640  1.00 35.27           C  
ATOM    764  N   LEU A  98      39.309  71.936  51.991  1.00 37.24           N  
ATOM    765  CA  LEU A  98      38.202  72.669  51.398  1.00 44.53           C  
ATOM    766  C   LEU A  98      37.986  72.383  49.914  1.00 38.92           C  
ATOM    767  O   LEU A  98      36.998  72.865  49.353  1.00 43.28           O  
ATOM    768  CB  LEU A  98      38.394  74.182  51.635  1.00 41.45           C  
ATOM    769  CG  LEU A  98      38.337  74.614  53.115  1.00 46.31           C  
ATOM    770  CD1 LEU A  98      38.572  76.114  53.262  1.00 50.80           C  
ATOM    771  CD2 LEU A  98      37.019  74.221  53.782  1.00 40.72           C  
ATOM    772  N   SER A  99      38.849  71.599  49.263  1.00 35.49           N  
ATOM    773  CA  SER A  99      38.692  71.329  47.838  1.00 34.86           C  
ATOM    774  C   SER A  99      38.865  69.843  47.539  1.00 32.42           C  
ATOM    775  O   SER A  99      39.540  69.109  48.266  1.00 33.66           O  
ATOM    776  CB  SER A  99      39.697  72.121  46.987  1.00 44.49           C  
ATOM    777  OG  SER A  99      41.007  71.599  47.154  1.00 45.39           O  
ATOM    778  N   LEU A 100      38.258  69.420  46.430  1.00 35.43           N  
ATOM    779  CA  LEU A 100      38.383  68.032  45.996  1.00 34.79           C  
ATOM    780  C   LEU A 100      39.830  67.675  45.702  1.00 37.39           C  
ATOM    781  O   LEU A 100      40.303  66.593  46.081  1.00 32.71           O  
ATOM    782  CB  LEU A 100      37.524  67.800  44.748  1.00 32.70           C  
ATOM    783  CG  LEU A 100      37.666  66.456  44.021  1.00 32.94           C  
ATOM    784  CD1 LEU A 100      37.178  65.319  44.904  1.00 34.06           C  
ATOM    785  CD2 LEU A 100      36.902  66.489  42.704  1.00 33.30           C  
ATOM    786  N   GLU A 101      40.551  68.553  45.000  1.00 37.15           N  
ATOM    787  CA  GLU A 101      41.873  68.131  44.543  1.00 42.72           C  
ATOM    788  C   GLU A 101      42.867  68.040  45.695  1.00 30.26           C  
ATOM    789  O   GLU A 101      43.803  67.234  45.626  1.00 40.44           O  
ATOM    790  CB  GLU A 101      42.384  69.059  43.431  1.00 47.48           C  
ATOM    791  CG  GLU A 101      41.341  69.288  42.335  1.00 66.22           C  
ATOM    792  CD  GLU A 101      41.911  69.412  40.922  1.00 87.70           C  
ATOM    793  OE1 GLU A 101      43.064  69.888  40.753  1.00 74.83           O  
ATOM    794  OE2 GLU A 101      41.193  69.026  39.972  1.00 80.77           O  
ATOM    795  N   GLU A 102      42.659  68.782  46.788  1.00 33.97           N  
ATOM    796  CA  GLU A 102      43.448  68.563  48.001  1.00 37.66           C  
ATOM    797  C   GLU A 102      43.230  67.163  48.561  1.00 41.74           C  
ATOM    798  O   GLU A 102      44.138  66.583  49.164  1.00 37.89           O  
ATOM    799  CB  GLU A 102      43.083  69.593  49.069  1.00 42.85           C  
ATOM    800  CG  GLU A 102      43.683  70.980  48.893  1.00 48.65           C  
ATOM    801  CD  GLU A 102      43.008  71.990  49.804  1.00 51.04           C  
ATOM    802  OE1 GLU A 102      41.940  72.519  49.417  1.00 49.92           O  
ATOM    803  OE2 GLU A 102      43.521  72.235  50.917  1.00 51.08           O  
ATOM    804  N   ASP A 103      42.017  66.631  48.408  1.00 35.96           N  
ATOM    805  CA  ASP A 103      41.725  65.262  48.822  1.00 30.84           C  
ATOM    806  C   ASP A 103      42.342  64.258  47.851  1.00 29.98           C  
ATOM    807  O   ASP A 103      43.046  63.325  48.266  1.00 34.94           O  
ATOM    808  CB  ASP A 103      40.199  65.106  48.930  1.00 30.65           C  
ATOM    809  CG  ASP A 103      39.762  63.708  49.329  1.00 39.62           C  
ATOM    810  OD1 ASP A 103      40.188  62.735  48.664  1.00 39.97           O  
ATOM    811  OD2 ASP A 103      38.969  63.591  50.298  1.00 36.94           O  
ATOM    812  N   LEU A 104      42.120  64.451  46.547  1.00 31.58           N  
ATOM    813  CA  LEU A 104      42.597  63.486  45.558  1.00 31.03           C  
ATOM    814  C   LEU A 104      44.120  63.373  45.563  1.00 34.30           C  
ATOM    815  O   LEU A 104      44.665  62.289  45.326  1.00 28.27           O  
ATOM    816  CB  LEU A 104      42.109  63.864  44.152  1.00 30.74           C  
ATOM    817  CG  LEU A 104      40.606  63.766  43.872  1.00 33.70           C  
ATOM    818  CD1 LEU A 104      40.290  64.219  42.449  1.00 34.59           C  
ATOM    819  CD2 LEU A 104      40.135  62.332  44.092  1.00 34.02           C  
ATOM    820  N   ARG A 105      44.827  64.483  45.804  1.00 33.80           N  
ATOM    821  CA  ARG A 105      46.275  64.444  45.591  1.00 34.69           C  
ATOM    822  C   ARG A 105      47.021  63.658  46.665  1.00 39.21           C  
ATOM    823  O   ARG A 105      48.243  63.468  46.541  1.00 36.93           O  
ATOM    824  CB  ARG A 105      46.837  65.867  45.490  1.00 37.75           C  
ATOM    825  CG  ARG A 105      46.870  66.645  46.783  1.00 37.78           C  
ATOM    826  CD  ARG A 105      47.316  68.088  46.512  1.00 45.34           C  
ATOM    827  NE  ARG A 105      47.362  68.887  47.734  1.00 59.43           N  
ATOM    828  CZ  ARG A 105      47.501  70.210  47.758  1.00 69.46           C  
ATOM    829  NH1 ARG A 105      47.608  70.895  46.621  1.00 59.10           N  
ATOM    830  NH2 ARG A 105      47.531  70.853  48.917  1.00 61.69           N  
ATOM    831  N   ARG A 106      46.335  63.169  47.695  1.00 32.87           N  
ATOM    832  CA  ARG A 106      46.981  62.352  48.707  1.00 35.72           C  
ATOM    833  C   ARG A 106      46.476  60.915  48.722  1.00 37.16           C  
ATOM    834  O   ARG A 106      46.782  60.177  49.668  1.00 34.24           O  
ATOM    835  CB  ARG A 106      46.813  63.000  50.077  1.00 37.47           C  
ATOM    836  CG  ARG A 106      47.117  64.497  50.043  1.00 44.50           C  
ATOM    837  CD  ARG A 106      48.586  64.741  50.195  1.00 44.84           C  
ATOM    838  NE  ARG A 106      48.922  64.590  51.605  1.00 58.39           N  
ATOM    839  CZ  ARG A 106      49.062  65.607  52.451  1.00 66.39           C  
ATOM    840  NH1 ARG A 106      48.935  66.855  52.015  1.00 66.68           N  
ATOM    841  NH2 ARG A 106      49.340  65.377  53.729  1.00 56.34           N  
ATOM    842  N   ARG A 107      45.727  60.493  47.697  1.00 31.50           N  
ATOM    843  CA  ARG A 107      45.309  59.100  47.617  1.00 28.88           C  
ATOM    844  C   ARG A 107      46.466  58.243  47.103  1.00 28.12           C  
ATOM    845  O   ARG A 107      47.491  58.753  46.645  1.00 33.95           O  
ATOM    846  CB  ARG A 107      44.053  58.973  46.740  1.00 30.99           C  
ATOM    847  CG  ARG A 107      42.860  59.705  47.371  1.00 32.69           C  
ATOM    848  CD  ARG A 107      41.593  59.684  46.519  1.00 33.28           C  
ATOM    849  NE  ARG A 107      40.489  60.317  47.249  1.00 34.94           N  
ATOM    850  CZ  ARG A 107      39.444  59.672  47.755  1.00 39.45           C  
ATOM    851  NH1 ARG A 107      39.325  58.353  47.606  1.00 32.15           N  
ATOM    852  NH2 ARG A 107      38.505  60.358  48.397  1.00 32.22           N  
ATOM    853  N   ASP A 108      46.296  56.919  47.166  1.00 28.17           N  
ATOM    854  CA  ASP A 108      47.445  56.032  46.970  1.00 29.22           C  
ATOM    855  C   ASP A 108      47.897  55.969  45.503  1.00 33.29           C  
ATOM    856  O   ASP A 108      49.068  56.244  45.202  1.00 31.32           O  
ATOM    857  CB  ASP A 108      47.173  54.628  47.542  1.00 26.34           C  
ATOM    858  CG  ASP A 108      45.870  53.989  47.057  1.00 33.51           C  
ATOM    859  OD1 ASP A 108      45.169  54.553  46.183  1.00 31.24           O  
ATOM    860  OD2 ASP A 108      45.567  52.867  47.558  1.00 31.45           O  
ATOM    861  N   PHE A 109      47.003  55.620  44.571  1.00 28.26           N  
ATOM    862  CA  PHE A 109      47.409  55.385  43.181  1.00 27.45           C  
ATOM    863  C   PHE A 109      46.526  56.160  42.207  1.00 33.76           C  
ATOM    864  O   PHE A 109      45.345  56.420  42.481  1.00 30.09           O  
ATOM    865  CB  PHE A 109      47.386  53.879  42.852  1.00 29.15           C  
ATOM    866  CG  PHE A 109      48.135  53.059  43.853  1.00 29.23           C  
ATOM    867  CD1 PHE A 109      49.513  53.211  43.987  1.00 30.66           C  
ATOM    868  CD2 PHE A 109      47.468  52.194  44.711  1.00 28.40           C  
ATOM    869  CE1 PHE A 109      50.215  52.495  44.957  1.00 35.68           C  
ATOM    870  CE2 PHE A 109      48.158  51.469  45.669  1.00 36.10           C  
ATOM    871  CZ  PHE A 109      49.537  51.626  45.800  1.00 31.78           C  
ATOM    872  N   THR A 110      47.113  56.517  41.054  1.00 28.53           N  
ATOM    873  CA  THR A 110      46.424  57.378  40.093  1.00 31.80           C  
ATOM    874  C   THR A 110      45.067  56.800  39.684  1.00 30.77           C  
ATOM    875  O   THR A 110      44.078  57.536  39.594  1.00 31.12           O  
ATOM    876  CB  THR A 110      47.308  57.632  38.858  1.00 31.01           C  
ATOM    877  OG1 THR A 110      47.605  56.404  38.188  1.00 27.26           O  
ATOM    878  CG2 THR A 110      48.605  58.313  39.258  1.00 32.49           C  
ATOM    879  N   ILE A 111      44.985  55.490  39.458  1.00 29.65           N  
ATOM    880  CA  ILE A 111      43.701  54.904  39.069  1.00 26.05           C  
ATOM    881  C   ILE A 111      42.660  54.979  40.184  1.00 35.45           C  
ATOM    882  O   ILE A 111      41.459  54.804  39.916  1.00 29.53           O  
ATOM    883  CB  ILE A 111      43.886  53.447  38.627  1.00 31.20           C  
ATOM    884  CG1 ILE A 111      44.443  52.630  39.794  1.00 28.46           C  
ATOM    885  CG2 ILE A 111      44.738  53.379  37.327  1.00 30.82           C  
ATOM    886  CD1 ILE A 111      44.684  51.182  39.483  1.00 32.60           C  
ATOM    887  N   ASN A 112      43.084  55.206  41.430  1.00 29.21           N  
ATOM    888  CA  ASN A 112      42.177  55.375  42.561  1.00 31.12           C  
ATOM    889  C   ASN A 112      41.960  56.828  42.925  1.00 31.97           C  
ATOM    890  O   ASN A 112      41.332  57.105  43.957  1.00 28.29           O  
ATOM    891  CB  ASN A 112      42.715  54.652  43.812  1.00 27.48           C  
ATOM    892  CG  ASN A 112      42.801  53.147  43.629  1.00 31.28           C  
ATOM    893  OD1 ASN A 112      42.089  52.581  42.814  1.00 31.29           O  
ATOM    894  ND2 ASN A 112      43.663  52.487  44.417  1.00 32.55           N  
ATOM    895  N   ALA A 113      42.515  57.757  42.150  1.00 26.31           N  
ATOM    896  CA  ALA A 113      42.523  59.172  42.513  1.00 30.69           C  
ATOM    897  C   ALA A 113      41.726  59.989  41.503  1.00 31.39           C  
ATOM    898  O   ALA A 113      42.069  61.138  41.200  1.00 29.09           O  
ATOM    899  CB  ALA A 113      43.957  59.710  42.629  1.00 27.60           C  
ATOM    900  N   MET A 114      40.662  59.403  40.971  1.00 27.08           N  
ATOM    901  CA  MET A 114      39.775  60.087  40.041  1.00 28.47           C  
ATOM    902  C   MET A 114      38.419  60.321  40.689  1.00 27.91           C  
ATOM    903  O   MET A 114      38.076  59.716  41.709  1.00 29.97           O  
ATOM    904  CB  MET A 114      39.604  59.279  38.750  1.00 25.47           C  
ATOM    905  CG  MET A 114      40.923  59.030  38.018  1.00 34.27           C  
ATOM    906  SD  MET A 114      40.729  58.150  36.444  1.00 35.80           S  
ATOM    907  CE  MET A 114      40.351  56.494  36.996  1.00 29.87           C  
ATOM    908  N   ALA A 115      37.669  61.250  40.103  1.00 31.09           N  
ATOM    909  CA  ALA A 115      36.321  61.572  40.539  1.00 31.30           C  
ATOM    910  C   ALA A 115      35.417  61.642  39.312  1.00 29.02           C  
ATOM    911  O   ALA A 115      35.870  61.912  38.197  1.00 31.99           O  
ATOM    912  CB  ALA A 115      36.274  62.909  41.313  1.00 28.93           C  
ATOM    913  N   MET A 116      34.129  61.386  39.525  1.00 33.34           N  
ATOM    914  CA  MET A 116      33.151  61.467  38.451  1.00 30.59           C  
ATOM    915  C   MET A 116      31.992  62.336  38.907  1.00 28.18           C  
ATOM    916  O   MET A 116      31.471  62.148  40.010  1.00 28.57           O  
ATOM    917  CB  MET A 116      32.632  60.086  38.040  1.00 33.05           C  
ATOM    918  CG  MET A 116      31.748  60.215  36.792  1.00 37.71           C  
ATOM    919  SD  MET A 116      31.176  58.639  36.139  1.00 41.29           S  
ATOM    920  CE  MET A 116      30.107  58.094  37.440  1.00 41.26           C  
ATOM    921  N   THR A 117      31.612  63.303  38.073  1.00 30.49           N  
ATOM    922  CA  THR A 117      30.504  64.167  38.425  1.00 32.16           C  
ATOM    923  C   THR A 117      29.179  63.463  38.143  1.00 39.67           C  
ATOM    924  O   THR A 117      29.122  62.406  37.503  1.00 32.72           O  
ATOM    925  CB  THR A 117      30.547  65.486  37.641  1.00 35.53           C  
ATOM    926  OG1 THR A 117      30.303  65.219  36.258  1.00 38.14           O  
ATOM    927  CG2 THR A 117      31.890  66.177  37.786  1.00 34.11           C  
ATOM    928  N   GLU A 118      28.095  64.098  38.607  1.00 35.52           N  
ATOM    929  CA  GLU A 118      26.748  63.610  38.330  1.00 35.23           C  
ATOM    930  C   GLU A 118      26.494  63.453  36.835  1.00 39.31           C  
ATOM    931  O   GLU A 118      25.715  62.583  36.433  1.00 40.81           O  
ATOM    932  CB  GLU A 118      25.730  64.573  38.953  1.00 35.96           C  
ATOM    933  CG  GLU A 118      24.363  63.980  39.247  1.00 52.37           C  
ATOM    934  CD  GLU A 118      23.369  65.038  39.726  1.00 55.20           C  
ATOM    935  OE1 GLU A 118      23.813  66.180  39.961  1.00 48.26           O  
ATOM    936  OE2 GLU A 118      22.151  64.737  39.843  1.00 45.98           O  
ATOM    937  N   ASP A 119      27.122  64.279  35.996  1.00 37.86           N  
ATOM    938  CA  ASP A 119      26.939  64.203  34.548  1.00 41.57           C  
ATOM    939  C   ASP A 119      27.981  63.331  33.853  1.00 46.53           C  
ATOM    940  O   ASP A 119      28.148  63.452  32.632  1.00 47.14           O  
ATOM    941  CB  ASP A 119      26.971  65.597  33.921  1.00 37.23           C  
ATOM    942  CG  ASP A 119      25.889  66.491  34.449  1.00 64.74           C  
ATOM    943  OD1 ASP A 119      24.703  66.088  34.389  1.00 65.09           O  
ATOM    944  OD2 ASP A 119      26.228  67.594  34.940  1.00 78.57           O  
ATOM    945  N   LEU A 120      28.697  62.482  34.597  1.00 38.94           N  
ATOM    946  CA  LEU A 120      29.651  61.508  34.064  1.00 38.07           C  
ATOM    947  C   LEU A 120      30.912  62.173  33.523  1.00 38.55           C  
ATOM    948  O   LEU A 120      31.595  61.599  32.663  1.00 45.31           O  
ATOM    949  CB  LEU A 120      29.043  60.681  32.918  1.00 45.42           C  
ATOM    950  CG  LEU A 120      27.656  60.087  33.216  1.00 45.76           C  
ATOM    951  CD1 LEU A 120      27.247  59.032  32.194  1.00 59.46           C  
ATOM    952  CD2 LEU A 120      27.598  59.518  34.584  1.00 45.49           C  
ATOM    953  N   LYS A 121      31.242  63.369  33.976  1.00 37.18           N  
ATOM    954  CA  LYS A 121      32.508  63.957  33.578  1.00 38.25           C  
ATOM    955  C   LYS A 121      33.558  63.408  34.546  1.00 39.32           C  
ATOM    956  O   LYS A 121      33.315  63.331  35.755  1.00 35.03           O  
ATOM    957  CB  LYS A 121      32.407  65.477  33.647  1.00 41.42           C  
ATOM    958  CG  LYS A 121      33.694  66.255  33.627  1.00 66.92           C  
ATOM    959  CD  LYS A 121      33.354  67.747  33.765  1.00 83.60           C  
ATOM    960  CE  LYS A 121      34.543  68.579  34.212  1.00 82.60           C  
ATOM    961  NZ  LYS A 121      34.096  69.723  35.063  1.00 79.89           N  
ATOM    962  N   ILE A 122      34.720  63.018  34.015  1.00 36.72           N  
ATOM    963  CA  ILE A 122      35.797  62.467  34.833  1.00 36.04           C  
ATOM    964  C   ILE A 122      36.772  63.578  35.196  1.00 39.29           C  
ATOM    965  O   ILE A 122      37.284  64.288  34.320  1.00 43.17           O  
ATOM    966  CB  ILE A 122      36.531  61.321  34.120  1.00 36.77           C  
ATOM    967  CG1 ILE A 122      35.567  60.205  33.725  1.00 43.93           C  
ATOM    968  CG2 ILE A 122      37.617  60.760  35.046  1.00 37.96           C  
ATOM    969  CD1 ILE A 122      35.138  59.352  34.880  1.00 40.67           C  
ATOM    970  N   ILE A 123      37.032  63.727  36.488  1.00 31.15           N  
ATOM    971  CA  ILE A 123      38.049  64.637  36.989  1.00 31.82           C  
ATOM    972  C   ILE A 123      39.279  63.794  37.295  1.00 37.31           C  
ATOM    973  O   ILE A 123      39.210  62.871  38.112  1.00 32.76           O  
ATOM    974  CB  ILE A 123      37.544  65.391  38.232  1.00 34.17           C  
ATOM    975  CG1 ILE A 123      36.375  66.303  37.828  1.00 37.75           C  
ATOM    976  CG2 ILE A 123      38.689  66.159  38.911  1.00 35.31           C  
ATOM    977  CD1 ILE A 123      35.465  66.666  38.971  1.00 42.86           C  
ATOM    978  N   ASP A 124      40.395  64.067  36.618  1.00 36.23           N  
ATOM    979  CA  ASP A 124      41.560  63.176  36.647  1.00 36.35           C  
ATOM    980  C   ASP A 124      42.846  63.992  36.614  1.00 34.97           C  
ATOM    981  O   ASP A 124      43.573  64.001  35.619  1.00 40.44           O  
ATOM    982  CB  ASP A 124      41.492  62.198  35.474  1.00 36.48           C  
ATOM    983  CG  ASP A 124      42.695  61.288  35.397  1.00 43.82           C  
ATOM    984  OD1 ASP A 124      43.310  61.028  36.452  1.00 40.23           O  
ATOM    985  OD2 ASP A 124      43.028  60.835  34.277  1.00 37.44           O  
ATOM    986  N   PRO A 125      43.164  64.696  37.701  1.00 35.55           N  
ATOM    987  CA  PRO A 125      44.370  65.542  37.688  1.00 39.60           C  
ATOM    988  C   PRO A 125      45.674  64.771  37.531  1.00 44.93           C  
ATOM    989  O   PRO A 125      46.669  65.364  37.094  1.00 40.30           O  
ATOM    990  CB  PRO A 125      44.309  66.272  39.038  1.00 37.10           C  
ATOM    991  CG  PRO A 125      43.378  65.458  39.891  1.00 43.89           C  
ATOM    992  CD  PRO A 125      42.398  64.822  38.954  1.00 40.38           C  
ATOM    993  N   PHE A 126      45.709  63.472  37.834  1.00 36.11           N  
ATOM    994  CA  PHE A 126      46.981  62.758  37.938  1.00 37.77           C  
ATOM    995  C   PHE A 126      47.150  61.677  36.877  1.00 44.41           C  
ATOM    996  O   PHE A 126      48.060  60.848  36.977  1.00 45.15           O  
ATOM    997  CB  PHE A 126      47.130  62.197  39.349  1.00 36.38           C  
ATOM    998  CG  PHE A 126      46.943  63.243  40.394  1.00 41.82           C  
ATOM    999  CD1 PHE A 126      47.864  64.270  40.523  1.00 50.84           C  
ATOM   1000  CD2 PHE A 126      45.817  63.258  41.193  1.00 43.35           C  
ATOM   1001  CE1 PHE A 126      47.686  65.267  41.459  1.00 49.75           C  
ATOM   1002  CE2 PHE A 126      45.627  64.265  42.126  1.00 42.38           C  
ATOM   1003  CZ  PHE A 126      46.566  65.263  42.261  1.00 45.98           C  
ATOM   1004  N   GLY A 127      46.322  61.687  35.839  1.00 38.38           N  
ATOM   1005  CA  GLY A 127      46.533  60.772  34.741  1.00 36.76           C  
ATOM   1006  C   GLY A 127      46.093  59.361  35.012  1.00 41.31           C  
ATOM   1007  O   GLY A 127      46.619  58.434  34.387  1.00 38.34           O  
ATOM   1008  N   GLY A 128      45.134  59.165  35.926  1.00 32.56           N  
ATOM   1009  CA  GLY A 128      44.616  57.826  36.164  1.00 31.94           C  
ATOM   1010  C   GLY A 128      44.036  57.173  34.917  1.00 31.33           C  
ATOM   1011  O   GLY A 128      44.098  55.949  34.765  1.00 35.20           O  
ATOM   1012  N   LYS A 129      43.423  57.964  34.026  1.00 35.81           N  
ATOM   1013  CA  LYS A 129      42.830  57.319  32.849  1.00 35.54           C  
ATOM   1014  C   LYS A 129      43.911  56.719  31.959  1.00 35.74           C  
ATOM   1015  O   LYS A 129      43.765  55.596  31.459  1.00 36.36           O  
ATOM   1016  CB  LYS A 129      41.975  58.313  32.050  1.00 40.54           C  
ATOM   1017  CG  LYS A 129      40.735  58.810  32.791  1.00 47.01           C  
ATOM   1018  CD  LYS A 129      39.646  59.333  31.826  1.00 49.00           C  
ATOM   1019  CE  LYS A 129      40.224  60.292  30.816  1.00 54.54           C  
ATOM   1020  NZ  LYS A 129      40.912  61.460  31.470  1.00 65.76           N  
ATOM   1021  N   GLU A 130      45.038  57.412  31.782  1.00 33.15           N  
ATOM   1022  CA  GLU A 130      46.062  56.789  30.950  1.00 40.04           C  
ATOM   1023  C   GLU A 130      46.735  55.631  31.678  1.00 40.33           C  
ATOM   1024  O   GLU A 130      46.958  54.569  31.083  1.00 36.45           O  
ATOM   1025  CB  GLU A 130      47.098  57.831  30.525  1.00 38.70           C  
ATOM   1026  CG  GLU A 130      46.599  58.892  29.547  1.00 68.36           C  
ATOM   1027  CD  GLU A 130      45.364  59.665  30.033  1.00 90.71           C  
ATOM   1028  OE1 GLU A 130      45.354  60.168  31.188  1.00 72.66           O  
ATOM   1029  OE2 GLU A 130      44.395  59.775  29.244  1.00 70.27           O  
ATOM   1030  N   ASP A 131      46.944  55.686  33.004  1.00 35.97           N  
ATOM   1031  CA  ASP A 131      47.484  54.522  33.707  1.00 32.15           C  
ATOM   1032  C   ASP A 131      46.518  53.350  33.665  1.00 34.62           C  
ATOM   1033  O   ASP A 131      46.944  52.193  33.580  1.00 32.48           O  
ATOM   1034  CB  ASP A 131      47.835  54.897  35.157  1.00 29.58           C  
ATOM   1035  CG  ASP A 131      49.080  55.738  35.232  1.00 37.86           C  
ATOM   1036  OD1 ASP A 131      49.897  55.655  34.279  1.00 43.31           O  
ATOM   1037  OD2 ASP A 131      49.263  56.496  36.196  1.00 36.68           O  
ATOM   1038  N   LEU A 132      45.215  53.626  33.721  1.00 31.94           N  
ATOM   1039  CA  LEU A 132      44.234  52.562  33.567  1.00 33.81           C  
ATOM   1040  C   LEU A 132      44.331  51.933  32.176  1.00 36.78           C  
ATOM   1041  O   LEU A 132      44.309  50.705  32.032  1.00 38.73           O  
ATOM   1042  CB  LEU A 132      42.834  53.132  33.811  1.00 35.71           C  
ATOM   1043  CG  LEU A 132      41.716  52.179  34.228  1.00 48.55           C  
ATOM   1044  CD1 LEU A 132      41.998  51.567  35.603  1.00 42.67           C  
ATOM   1045  CD2 LEU A 132      40.401  52.919  34.263  1.00 51.23           C  
ATOM   1046  N   LYS A 133      44.453  52.764  31.142  1.00 36.43           N  
ATOM   1047  CA  LYS A 133      44.544  52.183  29.801  1.00 38.38           C  
ATOM   1048  C   LYS A 133      45.851  51.422  29.628  1.00 37.97           C  
ATOM   1049  O   LYS A 133      45.872  50.332  29.046  1.00 41.64           O  
ATOM   1050  CB  LYS A 133      44.403  53.283  28.747  1.00 34.04           C  
ATOM   1051  CG  LYS A 133      44.853  52.884  27.319  1.00 44.78           C  
ATOM   1052  CD  LYS A 133      44.960  54.132  26.430  1.00 55.92           C  
ATOM   1053  CE  LYS A 133      44.888  53.786  24.945  1.00 69.36           C  
ATOM   1054  NZ  LYS A 133      44.580  54.994  24.125  1.00 78.33           N  
ATOM   1055  N   ASN A 134      46.948  51.894  30.209  1.00 36.85           N  
ATOM   1056  CA  ASN A 134      48.207  51.173  30.091  1.00 37.63           C  
ATOM   1057  C   ASN A 134      48.358  50.061  31.131  1.00 39.70           C  
ATOM   1058  O   ASN A 134      49.364  49.351  31.108  1.00 39.27           O  
ATOM   1059  CB  ASN A 134      49.375  52.166  30.169  1.00 38.22           C  
ATOM   1060  CG  ASN A 134      49.337  53.198  29.026  1.00 46.99           C  
ATOM   1061  OD1 ASN A 134      48.768  52.933  27.976  1.00 41.17           O  
ATOM   1062  ND2 ASN A 134      49.926  54.370  29.243  1.00 41.11           N  
ATOM   1063  N   LYS A 135      47.374  49.875  32.019  1.00 35.93           N  
ATOM   1064  CA  LYS A 135      47.411  48.820  33.037  1.00 37.92           C  
ATOM   1065  C   LYS A 135      48.601  48.998  33.983  1.00 32.77           C  
ATOM   1066  O   LYS A 135      49.390  48.077  34.204  1.00 32.42           O  
ATOM   1067  CB  LYS A 135      47.425  47.438  32.379  1.00 37.81           C  
ATOM   1068  CG  LYS A 135      46.189  47.154  31.523  1.00 41.57           C  
ATOM   1069  CD  LYS A 135      46.328  45.837  30.764  1.00 50.11           C  
ATOM   1070  CE  LYS A 135      45.078  45.552  29.926  1.00 58.28           C  
ATOM   1071  NZ  LYS A 135      45.283  44.415  28.973  1.00 83.16           N  
ATOM   1072  N   VAL A 136      48.712  50.199  34.557  1.00 33.65           N  
ATOM   1073  CA  VAL A 136      49.844  50.603  35.389  1.00 29.42           C  
ATOM   1074  C   VAL A 136      49.343  51.071  36.760  1.00 32.89           C  
ATOM   1075  O   VAL A 136      48.482  51.959  36.847  1.00 31.74           O  
ATOM   1076  CB  VAL A 136      50.663  51.711  34.703  1.00 35.27           C  
ATOM   1077  CG1 VAL A 136      51.660  52.321  35.673  1.00 31.88           C  
ATOM   1078  CG2 VAL A 136      51.405  51.147  33.447  1.00 32.40           C  
ATOM   1079  N   ILE A 137      49.892  50.480  37.820  1.00 30.08           N  
ATOM   1080  CA  ILE A 137      49.692  50.938  39.201  1.00 25.35           C  
ATOM   1081  C   ILE A 137      50.804  51.923  39.531  1.00 30.83           C  
ATOM   1082  O   ILE A 137      51.965  51.535  39.683  1.00 31.87           O  
ATOM   1083  CB  ILE A 137      49.680  49.760  40.187  1.00 26.55           C  
ATOM   1084  CG1 ILE A 137      48.458  48.881  39.934  1.00 30.50           C  
ATOM   1085  CG2 ILE A 137      49.682  50.264  41.656  1.00 26.60           C  
ATOM   1086  CD1 ILE A 137      48.689  47.419  40.230  1.00 35.13           C  
ATOM   1087  N   ARG A 138      50.453  53.203  39.658  1.00 26.26           N  
ATOM   1088  CA  ARG A 138      51.426  54.272  39.865  1.00 29.70           C  
ATOM   1089  C   ARG A 138      50.973  55.128  41.038  1.00 33.55           C  
ATOM   1090  O   ARG A 138      49.818  55.567  41.077  1.00 28.40           O  
ATOM   1091  CB  ARG A 138      51.575  55.150  38.614  1.00 30.42           C  
ATOM   1092  CG  ARG A 138      52.498  56.359  38.804  1.00 33.52           C  
ATOM   1093  CD  ARG A 138      52.366  57.409  37.679  1.00 35.26           C  
ATOM   1094  NE  ARG A 138      52.187  56.829  36.347  1.00 35.26           N  
ATOM   1095  CZ  ARG A 138      53.157  56.700  35.443  1.00 45.73           C  
ATOM   1096  NH1 ARG A 138      54.398  57.100  35.716  1.00 39.62           N  
ATOM   1097  NH2 ARG A 138      52.887  56.170  34.263  1.00 40.96           N  
ATOM   1098  N   ALA A 139      51.874  55.371  41.990  1.00 28.88           N  
ATOM   1099  CA  ALA A 139      51.533  56.252  43.103  1.00 32.17           C  
ATOM   1100  C   ALA A 139      51.153  57.641  42.593  1.00 34.18           C  
ATOM   1101  O   ALA A 139      51.642  58.097  41.557  1.00 33.44           O  
ATOM   1102  CB  ALA A 139      52.714  56.357  44.080  1.00 37.99           C  
ATOM   1103  N   VAL A 140      50.254  58.310  43.321  1.00 30.43           N  
ATOM   1104  CA  VAL A 140      49.946  59.712  43.048  1.00 33.82           C  
ATOM   1105  C   VAL A 140      51.097  60.591  43.521  1.00 35.37           C  
ATOM   1106  O   VAL A 140      51.538  60.496  44.674  1.00 34.26           O  
ATOM   1107  CB  VAL A 140      48.646  60.131  43.750  1.00 30.55           C  
ATOM   1108  CG1 VAL A 140      48.363  61.622  43.532  1.00 33.96           C  
ATOM   1109  CG2 VAL A 140      47.489  59.281  43.288  1.00 28.26           C  
ATOM   1110  N   GLY A 141      51.566  61.481  42.648  1.00 36.73           N  
ATOM   1111  CA  GLY A 141      52.574  62.439  43.079  1.00 35.62           C  
ATOM   1112  C   GLY A 141      53.880  61.735  43.385  1.00 35.04           C  
ATOM   1113  O   GLY A 141      54.323  60.846  42.655  1.00 36.50           O  
ATOM   1114  N   ASP A 142      54.494  62.119  44.490  1.00 39.80           N  
ATOM   1115  CA  ASP A 142      55.763  61.539  44.918  1.00 39.53           C  
ATOM   1116  C   ASP A 142      55.514  60.213  45.625  1.00 35.36           C  
ATOM   1117  O   ASP A 142      54.946  60.211  46.717  1.00 37.15           O  
ATOM   1118  CB  ASP A 142      56.478  62.512  45.855  1.00 42.42           C  
ATOM   1119  CG  ASP A 142      57.827  61.996  46.324  1.00 47.91           C  
ATOM   1120  OD1 ASP A 142      58.177  60.830  46.031  1.00 38.69           O  
ATOM   1121  OD2 ASP A 142      58.536  62.781  46.985  1.00 50.49           O  
ATOM   1122  N   PRO A 143      55.924  59.071  45.059  1.00 36.06           N  
ATOM   1123  CA  PRO A 143      55.629  57.795  45.730  1.00 34.52           C  
ATOM   1124  C   PRO A 143      56.189  57.713  47.139  1.00 39.25           C  
ATOM   1125  O   PRO A 143      55.565  57.078  48.002  1.00 34.29           O  
ATOM   1126  CB  PRO A 143      56.253  56.738  44.806  1.00 33.44           C  
ATOM   1127  CG  PRO A 143      57.163  57.503  43.879  1.00 41.62           C  
ATOM   1128  CD  PRO A 143      56.605  58.888  43.768  1.00 34.29           C  
ATOM   1129  N   ASP A 144      57.350  58.324  47.405  1.00 37.53           N  
ATOM   1130  CA  ASP A 144      57.890  58.296  48.763  1.00 37.78           C  
ATOM   1131  C   ASP A 144      56.913  58.921  49.753  1.00 41.12           C  
ATOM   1132  O   ASP A 144      56.776  58.442  50.883  1.00 37.14           O  
ATOM   1133  CB  ASP A 144      59.238  59.022  48.834  1.00 39.32           C  
ATOM   1134  CG  ASP A 144      60.262  58.513  47.812  1.00 44.62           C  
ATOM   1135  OD1 ASP A 144      60.193  57.349  47.357  1.00 37.88           O  
ATOM   1136  OD2 ASP A 144      61.160  59.310  47.464  1.00 46.00           O  
ATOM   1137  N   GLU A 145      56.234  59.997  49.356  1.00 33.73           N  
ATOM   1138  CA  GLU A 145      55.291  60.636  50.268  1.00 34.39           C  
ATOM   1139  C   GLU A 145      54.069  59.752  50.517  1.00 40.49           C  
ATOM   1140  O   GLU A 145      53.602  59.632  51.656  1.00 36.65           O  
ATOM   1141  CB  GLU A 145      54.865  61.994  49.722  1.00 39.77           C  
ATOM   1142  CG  GLU A 145      55.893  63.097  49.939  1.00 53.87           C  
ATOM   1143  CD  GLU A 145      55.546  64.374  49.191  1.00 57.89           C  
ATOM   1144  OE1 GLU A 145      54.340  64.656  48.992  1.00 60.82           O  
ATOM   1145  OE2 GLU A 145      56.483  65.087  48.777  1.00 71.37           O  
ATOM   1146  N   ARG A 146      53.507  59.157  49.456  1.00 36.44           N  
ATOM   1147  CA  ARG A 146      52.354  58.275  49.636  1.00 30.22           C  
ATOM   1148  C   ARG A 146      52.681  57.120  50.581  1.00 33.41           C  
ATOM   1149  O   ARG A 146      51.860  56.748  51.421  1.00 33.92           O  
ATOM   1150  CB  ARG A 146      51.876  57.736  48.284  1.00 31.76           C  
ATOM   1151  CG  ARG A 146      51.510  58.807  47.264  1.00 31.62           C  
ATOM   1152  CD  ARG A 146      50.320  59.688  47.709  1.00 31.23           C  
ATOM   1153  NE  ARG A 146      50.685  60.789  48.604  1.00 36.24           N  
ATOM   1154  CZ  ARG A 146      51.278  61.918  48.221  1.00 38.71           C  
ATOM   1155  NH1 ARG A 146      51.624  62.094  46.946  1.00 34.46           N  
ATOM   1156  NH2 ARG A 146      51.544  62.863  49.114  1.00 36.93           N  
ATOM   1157  N   PHE A 147      53.876  56.543  50.466  1.00 31.85           N  
ATOM   1158  CA  PHE A 147      54.189  55.382  51.293  1.00 31.28           C  
ATOM   1159  C   PHE A 147      54.567  55.781  52.718  1.00 37.08           C  
ATOM   1160  O   PHE A 147      54.365  54.993  53.650  1.00 37.53           O  
ATOM   1161  CB  PHE A 147      55.292  54.553  50.627  1.00 32.86           C  
ATOM   1162  CG  PHE A 147      54.881  53.957  49.296  1.00 37.81           C  
ATOM   1163  CD1 PHE A 147      53.599  53.437  49.114  1.00 26.77           C  
ATOM   1164  CD2 PHE A 147      55.762  53.934  48.223  1.00 36.32           C  
ATOM   1165  CE1 PHE A 147      53.206  52.903  47.883  1.00 34.36           C  
ATOM   1166  CE2 PHE A 147      55.385  53.397  46.987  1.00 30.03           C  
ATOM   1167  CZ  PHE A 147      54.102  52.875  46.816  1.00 33.19           C  
ATOM   1168  N   GLU A 148      55.092  56.992  52.916  1.00 36.85           N  
ATOM   1169  CA  GLU A 148      55.300  57.486  54.272  1.00 38.52           C  
ATOM   1170  C   GLU A 148      53.976  57.834  54.938  1.00 42.38           C  
ATOM   1171  O   GLU A 148      53.839  57.692  56.156  1.00 37.60           O  
ATOM   1172  CB  GLU A 148      56.254  58.691  54.251  1.00 37.24           C  
ATOM   1173  CG  GLU A 148      57.685  58.280  53.898  1.00 42.16           C  
ATOM   1174  CD  GLU A 148      58.560  59.418  53.370  1.00 62.95           C  
ATOM   1175  OE1 GLU A 148      58.224  60.603  53.604  1.00 75.27           O  
ATOM   1176  OE2 GLU A 148      59.584  59.120  52.707  1.00 58.91           O  
ATOM   1177  N   GLU A 149      52.977  58.263  54.157  1.00 38.82           N  
ATOM   1178  CA  GLU A 149      51.674  58.557  54.739  1.00 35.60           C  
ATOM   1179  C   GLU A 149      50.984  57.291  55.235  1.00 38.27           C  
ATOM   1180  O   GLU A 149      50.289  57.324  56.254  1.00 40.10           O  
ATOM   1181  CB  GLU A 149      50.793  59.284  53.728  1.00 32.87           C  
ATOM   1182  CG  GLU A 149      51.144  60.753  53.553  1.00 37.05           C  
ATOM   1183  CD  GLU A 149      50.698  61.270  52.199  1.00 40.27           C  
ATOM   1184  OE1 GLU A 149      49.998  60.525  51.474  1.00 37.66           O  
ATOM   1185  OE2 GLU A 149      51.044  62.415  51.865  1.00 37.48           O  
ATOM   1186  N   ASP A 150      51.151  56.172  54.529  1.00 33.24           N  
ATOM   1187  CA  ASP A 150      50.535  54.911  54.959  1.00 36.01           C  
ATOM   1188  C   ASP A 150      51.395  53.848  54.271  1.00 33.35           C  
ATOM   1189  O   ASP A 150      51.384  53.740  53.040  1.00 34.99           O  
ATOM   1190  CB  ASP A 150      49.049  54.876  54.611  1.00 33.43           C  
ATOM   1191  CG  ASP A 150      48.380  53.557  55.004  1.00 41.05           C  
ATOM   1192  OD1 ASP A 150      49.021  52.758  55.711  1.00 33.55           O  
ATOM   1193  OD2 ASP A 150      47.215  53.322  54.606  1.00 38.85           O  
ATOM   1194  N   ALA A 151      52.099  53.048  55.078  1.00 32.17           N  
ATOM   1195  CA  ALA A 151      53.007  52.034  54.551  1.00 30.83           C  
ATOM   1196  C   ALA A 151      52.199  50.855  54.011  1.00 30.24           C  
ATOM   1197  O   ALA A 151      52.710  50.098  53.171  1.00 30.62           O  
ATOM   1198  CB  ALA A 151      53.973  51.550  55.650  1.00 31.22           C  
ATOM   1199  N   LEU A 152      50.953  50.668  54.466  1.00 29.62           N  
ATOM   1200  CA  LEU A 152      50.147  49.580  53.916  1.00 28.89           C  
ATOM   1201  C   LEU A 152      49.942  49.738  52.418  1.00 27.70           C  
ATOM   1202  O   LEU A 152      49.725  48.749  51.717  1.00 29.51           O  
ATOM   1203  CB  LEU A 152      48.786  49.507  54.605  1.00 27.17           C  
ATOM   1204  CG  LEU A 152      47.948  48.356  54.057  1.00 33.09           C  
ATOM   1205  CD1 LEU A 152      48.474  47.029  54.599  1.00 31.44           C  
ATOM   1206  CD2 LEU A 152      46.490  48.543  54.400  1.00 44.44           C  
ATOM   1207  N   ARG A 153      49.976  50.973  51.918  1.00 28.56           N  
ATOM   1208  CA  ARG A 153      49.853  51.205  50.481  1.00 25.72           C  
ATOM   1209  C   ARG A 153      50.886  50.429  49.679  1.00 30.19           C  
ATOM   1210  O   ARG A 153      50.625  50.069  48.529  1.00 29.54           O  
ATOM   1211  CB  ARG A 153      49.981  52.695  50.191  1.00 28.49           C  
ATOM   1212  CG  ARG A 153      48.751  53.471  50.604  1.00 29.15           C  
ATOM   1213  CD  ARG A 153      49.041  54.949  50.705  1.00 30.86           C  
ATOM   1214  NE  ARG A 153      47.806  55.722  50.807  1.00 32.41           N  
ATOM   1215  CZ  ARG A 153      47.766  57.049  50.829  1.00 35.50           C  
ATOM   1216  NH1 ARG A 153      48.904  57.747  50.804  1.00 31.62           N  
ATOM   1217  NH2 ARG A 153      46.597  57.677  50.883  1.00 34.66           N  
ATOM   1218  N   MET A 154      52.074  50.192  50.248  1.00 30.12           N  
ATOM   1219  CA  MET A 154      53.065  49.398  49.536  1.00 28.55           C  
ATOM   1220  C   MET A 154      52.531  48.012  49.222  1.00 31.42           C  
ATOM   1221  O   MET A 154      52.738  47.491  48.120  1.00 28.01           O  
ATOM   1222  CB  MET A 154      54.355  49.301  50.351  1.00 30.31           C  
ATOM   1223  CG  MET A 154      55.083  50.617  50.489  1.00 32.34           C  
ATOM   1224  SD  MET A 154      56.680  50.397  51.347  1.00 33.92           S  
ATOM   1225  CE  MET A 154      56.132  49.951  53.003  1.00 30.07           C  
ATOM   1226  N   LEU A 155      51.862  47.391  50.190  1.00 31.35           N  
ATOM   1227  CA  LEU A 155      51.285  46.064  50.002  1.00 27.84           C  
ATOM   1228  C   LEU A 155      50.003  46.115  49.184  1.00 25.82           C  
ATOM   1229  O   LEU A 155      49.706  45.167  48.441  1.00 26.56           O  
ATOM   1230  CB  LEU A 155      51.024  45.432  51.374  1.00 30.85           C  
ATOM   1231  CG  LEU A 155      50.402  44.046  51.483  1.00 30.15           C  
ATOM   1232  CD1 LEU A 155      51.247  43.055  50.720  1.00 31.05           C  
ATOM   1233  CD2 LEU A 155      50.256  43.620  52.998  1.00 27.45           C  
ATOM   1234  N   ARG A 156      49.239  47.208  49.295  1.00 27.89           N  
ATOM   1235  CA  ARG A 156      48.077  47.387  48.427  1.00 28.34           C  
ATOM   1236  C   ARG A 156      48.486  47.402  46.962  1.00 29.58           C  
ATOM   1237  O   ARG A 156      47.773  46.867  46.108  1.00 31.06           O  
ATOM   1238  CB  ARG A 156      47.330  48.681  48.766  1.00 30.36           C  
ATOM   1239  CG  ARG A 156      46.313  48.556  49.895  1.00 37.82           C  
ATOM   1240  CD  ARG A 156      45.756  49.918  50.373  1.00 29.06           C  
ATOM   1241  NE  ARG A 156      45.121  50.713  49.316  1.00 37.84           N  
ATOM   1242  CZ  ARG A 156      43.842  50.603  48.945  1.00 50.31           C  
ATOM   1243  NH1 ARG A 156      43.051  49.710  49.537  1.00 45.54           N  
ATOM   1244  NH2 ARG A 156      43.339  51.396  47.990  1.00 37.39           N  
ATOM   1245  N   ALA A 157      49.633  48.016  46.642  1.00 27.51           N  
ATOM   1246  CA  ALA A 157      50.100  47.991  45.255  1.00 30.44           C  
ATOM   1247  C   ALA A 157      50.265  46.561  44.767  1.00 28.92           C  
ATOM   1248  O   ALA A 157      49.857  46.227  43.648  1.00 30.00           O  
ATOM   1249  CB  ALA A 157      51.422  48.750  45.118  1.00 29.24           C  
ATOM   1250  N   ILE A 158      50.903  45.708  45.584  1.00 28.19           N  
ATOM   1251  CA  ILE A 158      51.069  44.296  45.229  1.00 29.12           C  
ATOM   1252  C   ILE A 158      49.709  43.656  44.978  1.00 31.31           C  
ATOM   1253  O   ILE A 158      49.507  42.929  43.996  1.00 32.94           O  
ATOM   1254  CB  ILE A 158      51.816  43.526  46.339  1.00 34.74           C  
ATOM   1255  CG1 ILE A 158      53.165  44.162  46.731  1.00 38.32           C  
ATOM   1256  CG2 ILE A 158      51.979  42.063  45.938  1.00 36.43           C  
ATOM   1257  CD1 ILE A 158      53.944  44.718  45.595  1.00 36.72           C  
ATOM   1258  N   ARG A 159      48.768  43.875  45.901  1.00 30.14           N  
ATOM   1259  CA  ARG A 159      47.456  43.245  45.786  1.00 28.75           C  
ATOM   1260  C   ARG A 159      46.726  43.713  44.529  1.00 32.93           C  
ATOM   1261  O   ARG A 159      46.107  42.903  43.824  1.00 33.89           O  
ATOM   1262  CB  ARG A 159      46.634  43.543  47.037  1.00 30.54           C  
ATOM   1263  CG  ARG A 159      45.278  42.844  47.051  1.00 33.68           C  
ATOM   1264  CD  ARG A 159      44.168  43.819  46.679  1.00 31.92           C  
ATOM   1265  NE  ARG A 159      43.950  44.794  47.734  1.00 32.24           N  
ATOM   1266  CZ  ARG A 159      42.919  45.633  47.785  1.00 37.52           C  
ATOM   1267  NH1 ARG A 159      41.996  45.613  46.828  1.00 36.07           N  
ATOM   1268  NH2 ARG A 159      42.801  46.480  48.798  1.00 35.55           N  
ATOM   1269  N   PHE A 160      46.778  45.019  44.233  1.00 29.89           N  
ATOM   1270  CA  PHE A 160      46.116  45.516  43.027  1.00 33.81           C  
ATOM   1271  C   PHE A 160      46.709  44.897  41.767  1.00 34.36           C  
ATOM   1272  O   PHE A 160      45.980  44.629  40.806  1.00 33.61           O  
ATOM   1273  CB  PHE A 160      46.193  47.048  42.952  1.00 28.22           C  
ATOM   1274  CG  PHE A 160      45.148  47.733  43.763  1.00 32.14           C  
ATOM   1275  CD1 PHE A 160      43.809  47.383  43.627  1.00 34.92           C  
ATOM   1276  CD2 PHE A 160      45.498  48.694  44.699  1.00 32.20           C  
ATOM   1277  CE1 PHE A 160      42.837  48.003  44.411  1.00 34.54           C  
ATOM   1278  CE2 PHE A 160      44.537  49.316  45.478  1.00 33.51           C  
ATOM   1279  CZ  PHE A 160      43.201  48.965  45.335  1.00 36.46           C  
ATOM   1280  N   SER A 161      48.025  44.652  41.744  1.00 31.77           N  
ATOM   1281  CA  SER A 161      48.626  44.104  40.527  1.00 34.51           C  
ATOM   1282  C   SER A 161      47.943  42.805  40.118  1.00 38.63           C  
ATOM   1283  O   SER A 161      47.636  42.606  38.935  1.00 34.18           O  
ATOM   1284  CB  SER A 161      50.133  43.888  40.700  1.00 32.29           C  
ATOM   1285  OG  SER A 161      50.417  42.785  41.546  1.00 37.23           O  
ATOM   1286  N   GLY A 162      47.677  41.921  41.079  1.00 37.64           N  
ATOM   1287  CA  GLY A 162      46.993  40.673  40.789  1.00 34.77           C  
ATOM   1288  C   GLY A 162      45.504  40.841  40.551  1.00 43.67           C  
ATOM   1289  O   GLY A 162      44.933  40.242  39.630  1.00 42.53           O  
ATOM   1290  N   GLN A 163      44.861  41.665  41.378  1.00 35.14           N  
ATOM   1291  CA  GLN A 163      43.423  41.880  41.249  1.00 39.38           C  
ATOM   1292  C   GLN A 163      43.058  42.419  39.863  1.00 41.06           C  
ATOM   1293  O   GLN A 163      42.035  42.035  39.284  1.00 36.19           O  
ATOM   1294  CB  GLN A 163      42.949  42.834  42.349  1.00 40.02           C  
ATOM   1295  CG  GLN A 163      41.514  43.350  42.220  1.00 39.44           C  
ATOM   1296  CD  GLN A 163      41.170  44.330  43.330  1.00 41.83           C  
ATOM   1297  OE1 GLN A 163      41.751  44.275  44.403  1.00 41.24           O  
ATOM   1298  NE2 GLN A 163      40.245  45.252  43.062  1.00 42.93           N  
ATOM   1299  N   LEU A 164      43.868  43.323  39.327  1.00 31.96           N  
ATOM   1300  CA  LEU A 164      43.560  43.988  38.067  1.00 43.69           C  
ATOM   1301  C   LEU A 164      44.352  43.434  36.884  1.00 39.57           C  
ATOM   1302  O   LEU A 164      44.065  43.809  35.741  1.00 38.83           O  
ATOM   1303  CB  LEU A 164      43.827  45.495  38.188  1.00 31.88           C  
ATOM   1304  CG  LEU A 164      43.173  46.277  39.339  1.00 33.27           C  
ATOM   1305  CD1 LEU A 164      43.749  47.686  39.414  1.00 34.34           C  
ATOM   1306  CD2 LEU A 164      41.660  46.334  39.174  1.00 38.55           C  
ATOM   1307  N   ASP A 165      45.330  42.560  37.131  1.00 39.25           N  
ATOM   1308  CA  ASP A 165      46.312  42.159  36.125  1.00 44.41           C  
ATOM   1309  C   ASP A 165      47.016  43.385  35.543  1.00 40.71           C  
ATOM   1310  O   ASP A 165      47.109  43.568  34.328  1.00 39.01           O  
ATOM   1311  CB  ASP A 165      45.660  41.318  35.022  1.00 41.29           C  
ATOM   1312  CG  ASP A 165      46.685  40.535  34.193  1.00 49.91           C  
ATOM   1313  OD1 ASP A 165      47.822  40.296  34.675  1.00 54.92           O  
ATOM   1314  OD2 ASP A 165      46.344  40.148  33.051  1.00 53.92           O  
ATOM   1315  N   PHE A 166      47.499  44.242  36.432  1.00 34.76           N  
ATOM   1316  CA  PHE A 166      48.320  45.392  36.097  1.00 31.70           C  
ATOM   1317  C   PHE A 166      49.762  45.125  36.513  1.00 37.69           C  
ATOM   1318  O   PHE A 166      50.043  44.244  37.327  1.00 38.58           O  
ATOM   1319  CB  PHE A 166      47.840  46.669  36.801  1.00 29.12           C  
ATOM   1320  CG  PHE A 166      46.602  47.306  36.204  1.00 34.30           C  
ATOM   1321  CD1 PHE A 166      45.760  46.606  35.343  1.00 36.50           C  
ATOM   1322  CD2 PHE A 166      46.296  48.626  36.509  1.00 30.38           C  
ATOM   1323  CE1 PHE A 166      44.623  47.222  34.794  1.00 36.07           C  
ATOM   1324  CE2 PHE A 166      45.165  49.251  35.975  1.00 35.05           C  
ATOM   1325  CZ  PHE A 166      44.326  48.546  35.112  1.00 36.51           C  
ATOM   1326  N   ILE A 167      50.672  45.926  35.977  1.00 32.72           N  
ATOM   1327  CA  ILE A 167      52.041  45.970  36.461  1.00 31.94           C  
ATOM   1328  C   ILE A 167      52.180  47.165  37.396  1.00 34.50           C  
ATOM   1329  O   ILE A 167      51.366  48.099  37.395  1.00 33.43           O  
ATOM   1330  CB  ILE A 167      53.065  46.037  35.295  1.00 41.50           C  
ATOM   1331  CG1 ILE A 167      52.782  47.237  34.407  1.00 40.53           C  
ATOM   1332  CG2 ILE A 167      53.015  44.770  34.459  1.00 40.26           C  
ATOM   1333  CD1 ILE A 167      53.441  48.493  34.857  1.00 44.15           C  
ATOM   1334  N   ILE A 168      53.236  47.152  38.203  1.00 30.59           N  
ATOM   1335  CA  ILE A 168      53.532  48.260  39.104  1.00 28.36           C  
ATOM   1336  C   ILE A 168      54.516  49.194  38.419  1.00 34.21           C  
ATOM   1337  O   ILE A 168      55.576  48.761  37.955  1.00 30.98           O  
ATOM   1338  CB  ILE A 168      54.077  47.764  40.457  1.00 30.83           C  
ATOM   1339  CG1 ILE A 168      53.047  46.830  41.111  1.00 33.56           C  
ATOM   1340  CG2 ILE A 168      54.381  48.961  41.364  1.00 25.82           C  
ATOM   1341  CD1 ILE A 168      53.510  46.199  42.452  1.00 34.01           C  
ATOM   1342  N   ASP A 169      54.162  50.480  38.366  1.00 30.17           N  
ATOM   1343  CA  ASP A 169      55.031  51.509  37.810  1.00 32.77           C  
ATOM   1344  C   ASP A 169      56.447  51.381  38.367  1.00 35.10           C  
ATOM   1345  O   ASP A 169      56.632  51.201  39.569  1.00 29.35           O  
ATOM   1346  CB  ASP A 169      54.454  52.883  38.152  1.00 28.15           C  
ATOM   1347  CG  ASP A 169      55.434  54.025  37.888  1.00 30.15           C  
ATOM   1348  OD1 ASP A 169      55.748  54.270  36.693  1.00 37.18           O  
ATOM   1349  OD2 ASP A 169      55.873  54.687  38.865  1.00 31.25           O  
ATOM   1350  N   MET A 170      57.450  51.517  37.490  1.00 35.25           N  
ATOM   1351  CA  MET A 170      58.834  51.272  37.901  1.00 30.64           C  
ATOM   1352  C   MET A 170      59.265  52.220  39.014  1.00 33.53           C  
ATOM   1353  O   MET A 170      59.783  51.787  40.053  1.00 32.95           O  
ATOM   1354  CB  MET A 170      59.765  51.380  36.681  1.00 36.53           C  
ATOM   1355  CG  MET A 170      61.239  51.289  37.007  1.00 45.66           C  
ATOM   1356  SD  MET A 170      61.636  49.690  37.735  1.00 45.89           S  
ATOM   1357  CE  MET A 170      61.061  48.582  36.440  1.00 49.00           C  
ATOM   1358  N   LYS A 171      59.064  53.520  38.832  1.00 31.93           N  
ATOM   1359  CA  LYS A 171      59.444  54.451  39.885  1.00 29.81           C  
ATOM   1360  C   LYS A 171      58.715  54.124  41.190  1.00 36.00           C  
ATOM   1361  O   LYS A 171      59.289  54.228  42.282  1.00 32.48           O  
ATOM   1362  CB  LYS A 171      59.156  55.884  39.448  1.00 33.17           C  
ATOM   1363  CG  LYS A 171      59.504  56.918  40.515  1.00 44.24           C  
ATOM   1364  CD  LYS A 171      58.963  58.306  40.157  1.00 53.41           C  
ATOM   1365  CE  LYS A 171      59.387  59.336  41.195  1.00 58.26           C  
ATOM   1366  NZ  LYS A 171      58.780  60.663  40.900  1.00 71.75           N  
ATOM   1367  N   THR A 172      57.444  53.728  41.094  1.00 33.43           N  
ATOM   1368  CA  THR A 172      56.690  53.359  42.285  1.00 31.92           C  
ATOM   1369  C   THR A 172      57.292  52.126  42.950  1.00 29.74           C  
ATOM   1370  O   THR A 172      57.465  52.095  44.175  1.00 31.70           O  
ATOM   1371  CB  THR A 172      55.219  53.126  41.913  1.00 31.78           C  
ATOM   1372  OG1 THR A 172      54.655  54.372  41.469  1.00 30.32           O  
ATOM   1373  CG2 THR A 172      54.414  52.623  43.136  1.00 31.07           C  
ATOM   1374  N   LEU A 173      57.622  51.106  42.153  1.00 29.90           N  
ATOM   1375  CA  LEU A 173      58.170  49.866  42.696  1.00 33.85           C  
ATOM   1376  C   LEU A 173      59.521  50.106  43.362  1.00 35.77           C  
ATOM   1377  O   LEU A 173      59.794  49.579  44.449  1.00 32.97           O  
ATOM   1378  CB  LEU A 173      58.294  48.830  41.576  1.00 31.97           C  
ATOM   1379  CG  LEU A 173      58.782  47.418  41.909  1.00 36.50           C  
ATOM   1380  CD1 LEU A 173      57.897  46.768  42.981  1.00 32.80           C  
ATOM   1381  CD2 LEU A 173      58.824  46.556  40.642  1.00 34.84           C  
ATOM   1382  N   LEU A 174      60.375  50.912  42.730  1.00 34.25           N  
ATOM   1383  CA  LEU A 174      61.653  51.264  43.346  1.00 37.26           C  
ATOM   1384  C   LEU A 174      61.445  51.992  44.663  1.00 37.53           C  
ATOM   1385  O   LEU A 174      62.229  51.825  45.604  1.00 34.80           O  
ATOM   1386  CB  LEU A 174      62.483  52.116  42.383  1.00 30.86           C  
ATOM   1387  CG  LEU A 174      62.895  51.404  41.094  1.00 32.70           C  
ATOM   1388  CD1 LEU A 174      63.597  52.370  40.128  1.00 35.69           C  
ATOM   1389  CD2 LEU A 174      63.784  50.197  41.390  1.00 37.12           C  
ATOM   1390  N   SER A 175      60.414  52.833  44.743  1.00 34.34           N  
ATOM   1391  CA  SER A 175      60.107  53.490  46.006  1.00 34.12           C  
ATOM   1392  C   SER A 175      59.658  52.484  47.065  1.00 33.79           C  
ATOM   1393  O   SER A 175      60.003  52.632  48.244  1.00 35.87           O  
ATOM   1394  CB  SER A 175      59.040  54.568  45.807  1.00 35.20           C  
ATOM   1395  OG  SER A 175      58.798  55.232  47.031  1.00 36.36           O  
ATOM   1396  N   ILE A 176      58.885  51.461  46.683  1.00 31.32           N  
ATOM   1397  CA  ILE A 176      58.515  50.442  47.668  1.00 32.18           C  
ATOM   1398  C   ILE A 176      59.768  49.786  48.224  1.00 34.46           C  
ATOM   1399  O   ILE A 176      59.908  49.605  49.438  1.00 30.36           O  
ATOM   1400  CB  ILE A 176      57.574  49.387  47.065  1.00 35.71           C  
ATOM   1401  CG1 ILE A 176      56.237  50.017  46.649  1.00 30.91           C  
ATOM   1402  CG2 ILE A 176      57.302  48.278  48.112  1.00 30.59           C  
ATOM   1403  CD1 ILE A 176      55.366  49.049  45.876  1.00 30.59           C  
ATOM   1404  N   ARG A 177      60.692  49.413  47.333  1.00 33.21           N  
ATOM   1405  CA  ARG A 177      61.923  48.758  47.759  1.00 38.05           C  
ATOM   1406  C   ARG A 177      62.670  49.608  48.773  1.00 39.62           C  
ATOM   1407  O   ARG A 177      63.170  49.087  49.777  1.00 36.79           O  
ATOM   1408  CB  ARG A 177      62.805  48.465  46.546  1.00 37.16           C  
ATOM   1409  CG  ARG A 177      62.312  47.301  45.730  1.00 35.79           C  
ATOM   1410  CD  ARG A 177      62.731  47.387  44.310  1.00 49.99           C  
ATOM   1411  NE  ARG A 177      64.179  47.413  44.118  1.00 51.60           N  
ATOM   1412  CZ  ARG A 177      64.934  46.328  44.003  1.00 73.65           C  
ATOM   1413  NH1 ARG A 177      64.390  45.114  44.102  1.00 72.76           N  
ATOM   1414  NH2 ARG A 177      66.236  46.458  43.797  1.00 82.87           N  
ATOM   1415  N   ARG A 178      62.746  50.923  48.537  1.00 37.67           N  
ATOM   1416  CA  ARG A 178      63.450  51.802  49.464  1.00 37.35           C  
ATOM   1417  C   ARG A 178      62.718  51.954  50.792  1.00 44.51           C  
ATOM   1418  O   ARG A 178      63.363  52.178  51.820  1.00 39.98           O  
ATOM   1419  CB  ARG A 178      63.660  53.179  48.831  1.00 41.61           C  
ATOM   1420  CG  ARG A 178      64.697  53.207  47.719  1.00 49.19           C  
ATOM   1421  CD  ARG A 178      65.072  54.642  47.369  1.00 54.93           C  
ATOM   1422  NE  ARG A 178      63.885  55.448  47.101  1.00 59.45           N  
ATOM   1423  CZ  ARG A 178      63.314  55.571  45.905  1.00 58.87           C  
ATOM   1424  NH1 ARG A 178      63.824  54.945  44.846  1.00 58.67           N  
ATOM   1425  NH2 ARG A 178      62.233  56.322  45.764  1.00 51.05           N  
ATOM   1426  N   HIS A 179      61.383  51.850  50.804  1.00 35.23           N  
ATOM   1427  CA  HIS A 179      60.609  52.101  52.014  1.00 32.33           C  
ATOM   1428  C   HIS A 179      60.038  50.839  52.641  1.00 34.07           C  
ATOM   1429  O   HIS A 179      59.222  50.938  53.567  1.00 34.15           O  
ATOM   1430  CB  HIS A 179      59.470  53.078  51.725  1.00 35.29           C  
ATOM   1431  CG  HIS A 179      59.935  54.454  51.371  1.00 42.10           C  
ATOM   1432  ND1 HIS A 179      60.346  54.795  50.100  1.00 49.20           N  
ATOM   1433  CD2 HIS A 179      60.064  55.572  52.122  1.00 48.08           C  
ATOM   1434  CE1 HIS A 179      60.706  56.066  50.084  1.00 44.00           C  
ATOM   1435  NE2 HIS A 179      60.540  56.561  51.298  1.00 52.86           N  
ATOM   1436  N   ALA A 180      60.449  49.659  52.170  1.00 31.86           N  
ATOM   1437  CA  ALA A 180      59.800  48.424  52.598  1.00 32.20           C  
ATOM   1438  C   ALA A 180      59.894  48.214  54.106  1.00 38.52           C  
ATOM   1439  O   ALA A 180      59.022  47.561  54.690  1.00 31.44           O  
ATOM   1440  CB  ALA A 180      60.396  47.231  51.858  1.00 33.32           C  
ATOM   1441  N   ARG A 181      60.938  48.746  54.757  1.00 35.19           N  
ATOM   1442  CA  ARG A 181      61.112  48.598  56.199  1.00 36.52           C  
ATOM   1443  C   ARG A 181      59.935  49.187  56.969  1.00 36.90           C  
ATOM   1444  O   ARG A 181      59.640  48.751  58.089  1.00 38.78           O  
ATOM   1445  CB  ARG A 181      62.435  49.246  56.631  1.00 34.16           C  
ATOM   1446  CG  ARG A 181      62.864  48.862  58.020  1.00 60.50           C  
ATOM   1447  CD  ARG A 181      64.278  49.334  58.354  1.00 71.76           C  
ATOM   1448  NE  ARG A 181      64.468  49.353  59.806  1.00 85.45           N  
ATOM   1449  CZ  ARG A 181      64.370  48.287  60.597  1.00 70.71           C  
ATOM   1450  NH1 ARG A 181      64.096  47.077  60.087  1.00 61.05           N  
ATOM   1451  NH2 ARG A 181      64.559  48.431  61.910  1.00 70.12           N  
ATOM   1452  N   LEU A 182      59.317  50.229  56.410  1.00 32.13           N  
ATOM   1453  CA  LEU A 182      58.199  50.877  57.072  1.00 30.96           C  
ATOM   1454  C   LEU A 182      57.018  49.940  57.286  1.00 34.16           C  
ATOM   1455  O   LEU A 182      56.134  50.260  58.084  1.00 35.71           O  
ATOM   1456  CB  LEU A 182      57.741  52.094  56.272  1.00 34.77           C  
ATOM   1457  CG  LEU A 182      58.762  53.221  56.141  1.00 39.12           C  
ATOM   1458  CD1 LEU A 182      58.176  54.377  55.347  1.00 37.53           C  
ATOM   1459  CD2 LEU A 182      59.223  53.681  57.535  1.00 40.60           C  
ATOM   1460  N   ILE A 183      56.968  48.801  56.593  1.00 30.29           N  
ATOM   1461  CA  ILE A 183      55.828  47.909  56.785  1.00 33.77           C  
ATOM   1462  C   ILE A 183      55.759  47.395  58.225  1.00 35.47           C  
ATOM   1463  O   ILE A 183      54.690  46.954  58.678  1.00 33.66           O  
ATOM   1464  CB  ILE A 183      55.873  46.740  55.783  1.00 32.62           C  
ATOM   1465  CG1 ILE A 183      54.468  46.148  55.599  1.00 34.78           C  
ATOM   1466  CG2 ILE A 183      56.846  45.646  56.262  1.00 32.35           C  
ATOM   1467  CD1 ILE A 183      53.514  47.066  54.809  1.00 31.75           C  
ATOM   1468  N   ARG A 184      56.872  47.453  58.969  1.00 33.12           N  
ATOM   1469  CA  ARG A 184      56.860  46.953  60.342  1.00 39.67           C  
ATOM   1470  C   ARG A 184      55.903  47.733  61.233  1.00 37.82           C  
ATOM   1471  O   ARG A 184      55.471  47.210  62.263  1.00 36.41           O  
ATOM   1472  CB  ARG A 184      58.273  46.984  60.935  1.00 38.61           C  
ATOM   1473  CG  ARG A 184      58.807  48.366  61.242  1.00 39.29           C  
ATOM   1474  CD  ARG A 184      60.307  48.281  61.510  1.00 44.93           C  
ATOM   1475  NE  ARG A 184      60.869  49.490  62.098  1.00 45.27           N  
ATOM   1476  CZ  ARG A 184      61.320  50.529  61.397  1.00 62.31           C  
ATOM   1477  NH1 ARG A 184      61.253  50.530  60.064  1.00 49.21           N  
ATOM   1478  NH2 ARG A 184      61.831  51.579  62.032  1.00 60.03           N  
ATOM   1479  N   PHE A 185      55.560  48.968  60.864  1.00 35.38           N  
ATOM   1480  CA  PHE A 185      54.660  49.774  61.671  1.00 37.16           C  
ATOM   1481  C   PHE A 185      53.178  49.482  61.434  1.00 42.58           C  
ATOM   1482  O   PHE A 185      52.333  50.012  62.166  1.00 40.13           O  
ATOM   1483  CB  PHE A 185      54.944  51.251  61.416  1.00 39.83           C  
ATOM   1484  CG  PHE A 185      56.331  51.675  61.826  1.00 49.68           C  
ATOM   1485  CD1 PHE A 185      56.742  51.561  63.150  1.00 53.67           C  
ATOM   1486  CD2 PHE A 185      57.224  52.176  60.888  1.00 47.65           C  
ATOM   1487  CE1 PHE A 185      58.023  51.950  63.538  1.00 46.08           C  
ATOM   1488  CE2 PHE A 185      58.507  52.569  61.270  1.00 50.75           C  
ATOM   1489  CZ  PHE A 185      58.903  52.454  62.597  1.00 49.81           C  
ATOM   1490  N   ILE A 186      52.833  48.640  60.476  1.00 32.36           N  
ATOM   1491  CA  ILE A 186      51.433  48.422  60.123  1.00 32.26           C  
ATOM   1492  C   ILE A 186      50.845  47.309  60.981  1.00 34.91           C  
ATOM   1493  O   ILE A 186      51.461  46.253  61.170  1.00 32.65           O  
ATOM   1494  CB  ILE A 186      51.290  48.101  58.621  1.00 30.55           C  
ATOM   1495  CG1 ILE A 186      51.800  49.280  57.774  1.00 30.80           C  
ATOM   1496  CG2 ILE A 186      49.834  47.700  58.278  1.00 28.96           C  
ATOM   1497  CD1 ILE A 186      51.088  50.590  58.032  1.00 35.98           C  
ATOM   1498  N   ALA A 187      49.624  47.532  61.465  1.00 34.25           N  
ATOM   1499  CA  ALA A 187      48.941  46.523  62.264  1.00 34.08           C  
ATOM   1500  C   ALA A 187      48.815  45.235  61.469  1.00 37.29           C  
ATOM   1501  O   ALA A 187      48.453  45.252  60.288  1.00 33.74           O  
ATOM   1502  CB  ALA A 187      47.563  47.029  62.692  1.00 37.56           C  
ATOM   1503  N   VAL A 188      49.109  44.113  62.129  1.00 30.88           N  
ATOM   1504  CA  VAL A 188      49.169  42.833  61.446  1.00 30.97           C  
ATOM   1505  C   VAL A 188      47.811  42.422  60.892  1.00 37.54           C  
ATOM   1506  O   VAL A 188      47.747  41.680  59.909  1.00 33.90           O  
ATOM   1507  CB  VAL A 188      49.761  41.781  62.414  1.00 39.95           C  
ATOM   1508  CG1 VAL A 188      48.693  41.206  63.344  1.00 37.54           C  
ATOM   1509  CG2 VAL A 188      50.477  40.692  61.659  1.00 44.88           C  
ATOM   1510  N   GLU A 189      46.715  42.926  61.476  1.00 32.55           N  
ATOM   1511  CA  GLU A 189      45.381  42.650  60.940  1.00 34.43           C  
ATOM   1512  C   GLU A 189      45.200  43.226  59.535  1.00 31.31           C  
ATOM   1513  O   GLU A 189      44.499  42.641  58.700  1.00 32.99           O  
ATOM   1514  CB  GLU A 189      44.314  43.225  61.871  1.00 40.67           C  
ATOM   1515  CG  GLU A 189      44.270  42.579  63.260  1.00 43.13           C  
ATOM   1516  CD  GLU A 189      45.315  43.128  64.228  1.00 49.79           C  
ATOM   1517  OE1 GLU A 189      45.982  44.141  63.916  1.00 40.02           O  
ATOM   1518  OE2 GLU A 189      45.458  42.545  65.329  1.00 54.82           O  
ATOM   1519  N   ARG A 190      45.764  44.408  59.284  1.00 31.92           N  
ATOM   1520  CA  ARG A 190      45.702  45.003  57.955  1.00 35.12           C  
ATOM   1521  C   ARG A 190      46.586  44.248  56.973  1.00 32.77           C  
ATOM   1522  O   ARG A 190      46.226  44.089  55.798  1.00 33.21           O  
ATOM   1523  CB  ARG A 190      46.119  46.476  58.019  1.00 34.60           C  
ATOM   1524  CG  ARG A 190      45.273  47.323  58.966  1.00 38.04           C  
ATOM   1525  CD  ARG A 190      45.739  48.780  58.971  1.00 35.21           C  
ATOM   1526  NE  ARG A 190      45.439  49.451  57.706  1.00 41.43           N  
ATOM   1527  CZ  ARG A 190      46.161  50.445  57.188  1.00 48.47           C  
ATOM   1528  NH1 ARG A 190      47.246  50.869  57.814  1.00 40.15           N  
ATOM   1529  NH2 ARG A 190      45.818  50.998  56.027  1.00 42.92           N  
ATOM   1530  N   LEU A 191      47.763  43.794  57.427  1.00 31.79           N  
ATOM   1531  CA  LEU A 191      48.608  42.972  56.565  1.00 31.15           C  
ATOM   1532  C   LEU A 191      47.884  41.698  56.156  1.00 31.55           C  
ATOM   1533  O   LEU A 191      47.864  41.332  54.971  1.00 30.70           O  
ATOM   1534  CB  LEU A 191      49.922  42.633  57.280  1.00 29.91           C  
ATOM   1535  CG  LEU A 191      50.781  43.839  57.680  1.00 34.46           C  
ATOM   1536  CD1 LEU A 191      52.062  43.390  58.393  1.00 31.24           C  
ATOM   1537  CD2 LEU A 191      51.115  44.690  56.453  1.00 29.97           C  
ATOM   1538  N   LYS A 192      47.282  41.005  57.132  1.00 28.61           N  
ATOM   1539  CA  LYS A 192      46.609  39.749  56.828  1.00 31.25           C  
ATOM   1540  C   LYS A 192      45.454  39.973  55.862  1.00 30.61           C  
ATOM   1541  O   LYS A 192      45.229  39.169  54.954  1.00 31.95           O  
ATOM   1542  CB  LYS A 192      46.097  39.064  58.107  1.00 34.15           C  
ATOM   1543  CG  LYS A 192      45.399  37.740  57.765  1.00 33.64           C  
ATOM   1544  CD  LYS A 192      45.015  36.909  58.981  1.00 43.03           C  
ATOM   1545  CE  LYS A 192      44.457  35.557  58.522  1.00 39.96           C  
ATOM   1546  NZ  LYS A 192      43.031  35.669  58.107  1.00 38.56           N  
ATOM   1547  N   SER A 193      44.710  41.056  56.049  1.00 28.91           N  
ATOM   1548  CA  SER A 193      43.591  41.351  55.169  1.00 31.88           C  
ATOM   1549  C   SER A 193      44.047  41.468  53.716  1.00 33.64           C  
ATOM   1550  O   SER A 193      43.414  40.913  52.811  1.00 30.55           O  
ATOM   1551  CB  SER A 193      42.909  42.632  55.646  1.00 35.85           C  
ATOM   1552  OG  SER A 193      41.858  43.009  54.784  1.00 42.49           O  
ATOM   1553  N   GLU A 194      45.171  42.150  53.477  1.00 31.00           N  
ATOM   1554  CA  GLU A 194      45.673  42.302  52.112  1.00 29.53           C  
ATOM   1555  C   GLU A 194      46.184  40.981  51.557  1.00 33.56           C  
ATOM   1556  O   GLU A 194      45.939  40.653  50.390  1.00 29.66           O  
ATOM   1557  CB  GLU A 194      46.789  43.348  52.066  1.00 29.63           C  
ATOM   1558  CG  GLU A 194      46.301  44.778  52.219  1.00 30.19           C  
ATOM   1559  CD  GLU A 194      45.361  45.195  51.097  1.00 40.23           C  
ATOM   1560  OE1 GLU A 194      45.672  44.922  49.923  1.00 33.40           O  
ATOM   1561  OE2 GLU A 194      44.298  45.780  51.390  1.00 36.75           O  
ATOM   1562  N   ILE A 195      46.898  40.213  52.378  1.00 30.48           N  
ATOM   1563  CA  ILE A 195      47.422  38.931  51.927  1.00 31.52           C  
ATOM   1564  C   ILE A 195      46.287  37.964  51.622  1.00 30.36           C  
ATOM   1565  O   ILE A 195      46.346  37.209  50.646  1.00 29.53           O  
ATOM   1566  CB  ILE A 195      48.404  38.368  52.972  1.00 27.71           C  
ATOM   1567  CG1 ILE A 195      49.663  39.251  52.998  1.00 31.62           C  
ATOM   1568  CG2 ILE A 195      48.778  36.938  52.649  1.00 31.84           C  
ATOM   1569  CD1 ILE A 195      50.468  39.101  54.283  1.00 39.72           C  
ATOM   1570  N   ASP A 196      45.232  37.974  52.442  1.00 30.43           N  
ATOM   1571  CA  ASP A 196      44.085  37.113  52.158  1.00 32.30           C  
ATOM   1572  C   ASP A 196      43.486  37.440  50.795  1.00 33.81           C  
ATOM   1573  O   ASP A 196      43.081  36.536  50.053  1.00 32.23           O  
ATOM   1574  CB  ASP A 196      43.026  37.252  53.258  1.00 32.69           C  
ATOM   1575  CG  ASP A 196      43.421  36.560  54.575  1.00 39.96           C  
ATOM   1576  OD1 ASP A 196      44.375  35.741  54.613  1.00 32.21           O  
ATOM   1577  OD2 ASP A 196      42.753  36.844  55.587  1.00 35.49           O  
ATOM   1578  N   LYS A 197      43.410  38.729  50.452  1.00 32.61           N  
ATOM   1579  CA  LYS A 197      42.929  39.124  49.131  1.00 31.64           C  
ATOM   1580  C   LYS A 197      43.823  38.564  48.034  1.00 33.32           C  
ATOM   1581  O   LYS A 197      43.339  37.953  47.077  1.00 31.91           O  
ATOM   1582  CB  LYS A 197      42.840  40.649  49.036  1.00 33.47           C  
ATOM   1583  CG  LYS A 197      41.748  41.265  49.888  1.00 31.26           C  
ATOM   1584  CD  LYS A 197      41.819  42.795  49.829  1.00 33.74           C  
ATOM   1585  CE  LYS A 197      40.475  43.419  50.160  1.00 47.82           C  
ATOM   1586  NZ  LYS A 197      39.989  42.948  51.468  1.00 59.17           N  
ATOM   1587  N   ILE A 198      45.139  38.748  48.166  1.00 31.16           N  
ATOM   1588  CA  ILE A 198      46.074  38.212  47.173  1.00 30.12           C  
ATOM   1589  C   ILE A 198      45.858  36.717  46.966  1.00 36.37           C  
ATOM   1590  O   ILE A 198      45.888  36.211  45.833  1.00 33.45           O  
ATOM   1591  CB  ILE A 198      47.521  38.510  47.612  1.00 29.51           C  
ATOM   1592  CG1 ILE A 198      47.791  40.014  47.551  1.00 29.26           C  
ATOM   1593  CG2 ILE A 198      48.520  37.722  46.741  1.00 28.71           C  
ATOM   1594  CD1 ILE A 198      49.115  40.436  48.201  1.00 30.92           C  
ATOM   1595  N   PHE A 199      45.625  35.988  48.062  1.00 32.56           N  
ATOM   1596  CA  PHE A 199      45.534  34.529  48.019  1.00 30.20           C  
ATOM   1597  C   PHE A 199      44.330  34.036  47.218  1.00 32.73           C  
ATOM   1598  O   PHE A 199      44.354  32.913  46.701  1.00 37.54           O  
ATOM   1599  CB  PHE A 199      45.468  33.972  49.456  1.00 29.37           C  
ATOM   1600  CG  PHE A 199      46.805  33.872  50.137  1.00 34.01           C  
ATOM   1601  CD1 PHE A 199      47.979  34.045  49.414  1.00 37.44           C  
ATOM   1602  CD2 PHE A 199      46.892  33.579  51.498  1.00 33.70           C  
ATOM   1603  CE1 PHE A 199      49.215  33.933  50.030  1.00 34.46           C  
ATOM   1604  CE2 PHE A 199      48.119  33.463  52.113  1.00 32.69           C  
ATOM   1605  CZ  PHE A 199      49.282  33.637  51.382  1.00 30.82           C  
ATOM   1606  N   VAL A 200      43.264  34.823  47.127  1.00 33.12           N  
ATOM   1607  CA  VAL A 200      42.072  34.397  46.402  1.00 35.80           C  
ATOM   1608  C   VAL A 200      41.895  35.124  45.071  1.00 37.70           C  
ATOM   1609  O   VAL A 200      40.967  34.784  44.328  1.00 37.08           O  
ATOM   1610  CB  VAL A 200      40.802  34.538  47.268  1.00 35.87           C  
ATOM   1611  CG1 VAL A 200      40.947  33.795  48.604  1.00 34.54           C  
ATOM   1612  CG2 VAL A 200      40.439  36.001  47.498  1.00 33.68           C  
ATOM   1613  N   ASN A 201      42.757  36.091  44.736  1.00 33.91           N  
ATOM   1614  CA  ASN A 201      42.621  36.894  43.524  1.00 34.63           C  
ATOM   1615  C   ASN A 201      43.361  36.264  42.358  1.00 40.77           C  
ATOM   1616  O   ASN A 201      44.225  35.392  42.525  1.00 37.93           O  
ATOM   1617  CB  ASN A 201      43.159  38.302  43.764  1.00 36.28           C  
ATOM   1618  CG  ASN A 201      42.145  39.211  44.414  1.00 44.93           C  
ATOM   1619  OD1 ASN A 201      40.988  38.845  44.566  1.00 42.72           O  
ATOM   1620  ND2 ASN A 201      42.580  40.422  44.798  1.00 43.34           N  
ATOM   1621  N   PRO A 202      43.068  36.719  41.138  1.00 36.83           N  
ATOM   1622  CA  PRO A 202      43.771  36.202  39.960  1.00 37.29           C  
ATOM   1623  C   PRO A 202      45.234  36.611  39.968  1.00 48.55           C  
ATOM   1624  O   PRO A 202      45.667  37.484  40.729  1.00 39.24           O  
ATOM   1625  CB  PRO A 202      43.034  36.849  38.778  1.00 41.35           C  
ATOM   1626  CG  PRO A 202      41.807  37.451  39.330  1.00 42.09           C  
ATOM   1627  CD  PRO A 202      42.036  37.705  40.788  1.00 36.40           C  
ATOM   1628  N   SER A 203      45.995  35.970  39.082  1.00 39.20           N  
ATOM   1629  CA  SER A 203      47.406  36.292  38.883  1.00 44.00           C  
ATOM   1630  C   SER A 203      48.160  36.353  40.209  1.00 42.85           C  
ATOM   1631  O   SER A 203      49.029  37.201  40.410  1.00 38.16           O  
ATOM   1632  CB  SER A 203      47.563  37.614  38.127  1.00 41.09           C  
ATOM   1633  OG  SER A 203      46.879  37.588  36.886  1.00 45.60           O  
ATOM   1634  N   MET A 204      47.843  35.433  41.126  1.00 39.94           N  
ATOM   1635  CA  MET A 204      48.476  35.514  42.439  1.00 36.15           C  
ATOM   1636  C   MET A 204      49.971  35.219  42.355  1.00 40.13           C  
ATOM   1637  O   MET A 204      50.756  35.800  43.115  1.00 40.88           O  
ATOM   1638  CB  MET A 204      47.756  34.589  43.431  1.00 39.22           C  
ATOM   1639  CG  MET A 204      48.054  33.111  43.292  1.00 35.23           C  
ATOM   1640  SD  MET A 204      49.551  32.681  44.189  1.00 41.91           S  
ATOM   1641  CE  MET A 204      49.130  33.177  45.885  1.00 35.99           C  
ATOM   1642  N   GLN A 205      50.398  34.370  41.407  1.00 40.64           N  
ATOM   1643  CA  GLN A 205      51.831  34.103  41.268  1.00 39.95           C  
ATOM   1644  C   GLN A 205      52.616  35.365  40.920  1.00 39.73           C  
ATOM   1645  O   GLN A 205      53.760  35.527  41.366  1.00 40.73           O  
ATOM   1646  CB  GLN A 205      52.096  33.026  40.219  1.00 43.72           C  
ATOM   1647  CG  GLN A 205      51.574  31.638  40.567  1.00 44.11           C  
ATOM   1648  CD  GLN A 205      50.083  31.503  40.303  1.00 48.62           C  
ATOM   1649  OE1 GLN A 205      49.465  32.391  39.708  1.00 44.71           O  
ATOM   1650  NE2 GLN A 205      49.497  30.391  40.747  1.00 44.84           N  
ATOM   1651  N   LYS A 206      52.019  36.274  40.147  1.00 38.86           N  
ATOM   1652  CA  LYS A 206      52.629  37.569  39.849  1.00 47.72           C  
ATOM   1653  C   LYS A 206      52.659  38.472  41.083  1.00 44.85           C  
ATOM   1654  O   LYS A 206      53.600  39.256  41.260  1.00 34.50           O  
ATOM   1655  CB  LYS A 206      51.889  38.249  38.693  1.00 43.99           C  
ATOM   1656  CG  LYS A 206      52.553  38.008  37.311  1.00 61.36           C  
ATOM   1657  CD  LYS A 206      51.526  37.583  36.239  1.00 69.69           C  
ATOM   1658  CE  LYS A 206      52.047  37.787  34.807  1.00 67.80           C  
ATOM   1659  NZ  LYS A 206      50.945  37.667  33.799  1.00 55.75           N  
ATOM   1660  N   SER A 207      51.578  38.444  41.865  1.00 35.78           N  
ATOM   1661  CA  SER A 207      51.575  39.180  43.125  1.00 38.87           C  
ATOM   1662  C   SER A 207      52.685  38.701  44.053  1.00 32.34           C  
ATOM   1663  O   SER A 207      53.385  39.511  44.670  1.00 31.87           O  
ATOM   1664  CB  SER A 207      50.220  39.036  43.813  1.00 39.73           C  
ATOM   1665  OG  SER A 207      49.206  39.658  43.057  1.00 42.55           O  
ATOM   1666  N   MET A 208      52.864  37.384  44.168  1.00 35.85           N  
ATOM   1667  CA  MET A 208      53.868  36.872  45.090  1.00 33.64           C  
ATOM   1668  C   MET A 208      55.281  37.170  44.596  1.00 41.61           C  
ATOM   1669  O   MET A 208      56.210  37.294  45.407  1.00 32.45           O  
ATOM   1670  CB  MET A 208      53.659  35.372  45.297  1.00 33.47           C  
ATOM   1671  CG  MET A 208      52.264  35.014  45.862  1.00 33.75           C  
ATOM   1672  SD  MET A 208      51.830  35.907  47.397  1.00 38.36           S  
ATOM   1673  CE  MET A 208      53.180  35.394  48.449  1.00 32.85           C  
ATOM   1674  N   ALA A 209      55.468  37.291  43.275  1.00 34.43           N  
ATOM   1675  CA  ALA A 209      56.775  37.691  42.761  1.00 30.76           C  
ATOM   1676  C   ALA A 209      57.049  39.155  43.069  1.00 31.02           C  
ATOM   1677  O   ALA A 209      58.172  39.519  43.437  1.00 34.80           O  
ATOM   1678  CB  ALA A 209      56.866  37.421  41.250  1.00 36.51           C  
ATOM   1679  N   TYR A 210      56.031  40.012  42.943  1.00 28.34           N  
ATOM   1680  CA  TYR A 210      56.197  41.404  43.360  1.00 28.17           C  
ATOM   1681  C   TYR A 210      56.446  41.504  44.863  1.00 30.90           C  
ATOM   1682  O   TYR A 210      57.207  42.362  45.318  1.00 34.57           O  
ATOM   1683  CB  TYR A 210      54.959  42.222  42.993  1.00 29.85           C  
ATOM   1684  CG  TYR A 210      54.924  42.820  41.601  1.00 38.24           C  
ATOM   1685  CD1 TYR A 210      56.035  43.453  41.057  1.00 36.07           C  
ATOM   1686  CD2 TYR A 210      53.748  42.789  40.851  1.00 34.01           C  
ATOM   1687  CE1 TYR A 210      55.974  44.039  39.776  1.00 37.39           C  
ATOM   1688  CE2 TYR A 210      53.679  43.353  39.576  1.00 36.20           C  
ATOM   1689  CZ  TYR A 210      54.792  43.977  39.051  1.00 37.32           C  
ATOM   1690  OH  TYR A 210      54.717  44.540  37.801  1.00 39.96           O  
ATOM   1691  N   LEU A 211      55.781  40.662  45.653  1.00 30.59           N  
ATOM   1692  CA  LEU A 211      56.011  40.675  47.098  1.00 31.64           C  
ATOM   1693  C   LEU A 211      57.498  40.502  47.412  1.00 29.97           C  
ATOM   1694  O   LEU A 211      58.042  41.197  48.272  1.00 30.23           O  
ATOM   1695  CB  LEU A 211      55.189  39.575  47.768  1.00 28.80           C  
ATOM   1696  CG  LEU A 211      54.959  39.765  49.278  1.00 32.09           C  
ATOM   1697  CD1 LEU A 211      54.054  40.982  49.494  1.00 25.17           C  
ATOM   1698  CD2 LEU A 211      54.361  38.503  49.874  1.00 28.48           C  
ATOM   1699  N   LYS A 212      58.162  39.585  46.713  1.00 32.86           N  
ATOM   1700  CA  LYS A 212      59.598  39.370  46.892  1.00 36.51           C  
ATOM   1701  C   LYS A 212      60.417  40.487  46.247  1.00 38.37           C  
ATOM   1702  O   LYS A 212      61.299  41.077  46.892  1.00 35.74           O  
ATOM   1703  CB  LYS A 212      59.971  38.006  46.304  1.00 35.94           C  
ATOM   1704  CG  LYS A 212      61.444  37.616  46.355  1.00 41.03           C  
ATOM   1705  CD  LYS A 212      61.594  36.193  45.816  1.00 39.71           C  
ATOM   1706  CE  LYS A 212      63.002  35.624  45.997  1.00 50.65           C  
ATOM   1707  NZ  LYS A 212      64.034  36.379  45.239  1.00 66.12           N  
ATOM   1708  N   ASP A 213      60.124  40.808  44.974  1.00 33.84           N  
ATOM   1709  CA  ASP A 213      60.910  41.811  44.250  1.00 40.07           C  
ATOM   1710  C   ASP A 213      60.830  43.175  44.908  1.00 36.21           C  
ATOM   1711  O   ASP A 213      61.765  43.975  44.805  1.00 36.74           O  
ATOM   1712  CB  ASP A 213      60.429  41.938  42.795  1.00 42.27           C  
ATOM   1713  CG  ASP A 213      60.467  40.632  42.034  1.00 51.33           C  
ATOM   1714  OD1 ASP A 213      61.075  39.651  42.514  1.00 47.47           O  
ATOM   1715  OD2 ASP A 213      59.872  40.597  40.926  1.00 60.46           O  
ATOM   1716  N   SER A 214      59.714  43.473  45.569  1.00 33.79           N  
ATOM   1717  CA  SER A 214      59.534  44.746  46.239  1.00 30.08           C  
ATOM   1718  C   SER A 214      60.283  44.836  47.564  1.00 30.42           C  
ATOM   1719  O   SER A 214      60.268  45.902  48.180  1.00 29.71           O  
ATOM   1720  CB  SER A 214      58.048  44.978  46.516  1.00 34.80           C  
ATOM   1721  OG  SER A 214      57.625  44.042  47.490  1.00 32.18           O  
ATOM   1722  N   VAL A 215      60.900  43.744  48.008  1.00 32.45           N  
ATOM   1723  CA  VAL A 215      61.595  43.632  49.295  1.00 35.90           C  
ATOM   1724  C   VAL A 215      60.565  43.799  50.416  1.00 44.48           C  
ATOM   1725  O   VAL A 215      60.917  44.132  51.552  1.00 42.35           O  
ATOM   1726  CB  VAL A 215      62.590  44.797  49.496  1.00 33.96           C  
ATOM   1727  CG1 VAL A 215      63.395  44.597  50.804  1.00 33.59           C  
ATOM   1728  CG2 VAL A 215      63.542  44.857  48.307  1.00 34.22           C  
ATOM   1729  N   LEU A 216      59.329  43.362  50.219  1.00 32.46           N  
ATOM   1730  CA  LEU A 216      58.389  43.386  51.336  1.00 31.79           C  
ATOM   1731  C   LEU A 216      58.587  42.065  52.079  1.00 30.33           C  
ATOM   1732  O   LEU A 216      58.402  42.017  53.307  1.00 33.04           O  
ATOM   1733  CB  LEU A 216      56.942  43.532  50.859  1.00 27.20           C  
ATOM   1734  CG  LEU A 216      56.531  44.993  50.627  1.00 30.16           C  
ATOM   1735  CD1 LEU A 216      55.171  45.081  49.902  1.00 33.46           C  
ATOM   1736  CD2 LEU A 216      56.486  45.772  51.944  1.00 31.76           C  
ATOM   1737  N   THR A 217      58.952  40.987  51.377  1.00 31.20           N  
ATOM   1738  CA  THR A 217      59.139  39.713  52.069  1.00 35.46           C  
ATOM   1739  C   THR A 217      60.336  39.736  53.015  1.00 37.56           C  
ATOM   1740  O   THR A 217      60.433  38.865  53.886  1.00 34.57           O  
ATOM   1741  CB  THR A 217      59.323  38.553  51.084  1.00 32.79           C  
ATOM   1742  OG1 THR A 217      60.454  38.802  50.234  1.00 33.60           O  
ATOM   1743  CG2 THR A 217      58.066  38.317  50.240  1.00 33.02           C  
ATOM   1744  N   ARG A 218      61.252  40.697  52.859  1.00 31.20           N  
ATOM   1745  CA  ARG A 218      62.353  40.829  53.810  1.00 35.65           C  
ATOM   1746  C   ARG A 218      61.863  41.315  55.172  1.00 37.62           C  
ATOM   1747  O   ARG A 218      62.460  40.981  56.201  1.00 35.29           O  
ATOM   1748  CB  ARG A 218      63.418  41.783  53.258  1.00 35.81           C  
ATOM   1749  CG  ARG A 218      64.613  42.010  54.183  1.00 37.07           C  
ATOM   1750  CD  ARG A 218      65.778  42.733  53.456  1.00 36.25           C  
ATOM   1751  NE  ARG A 218      66.315  41.929  52.354  1.00 37.04           N  
ATOM   1752  CZ  ARG A 218      67.225  40.969  52.504  1.00 40.05           C  
ATOM   1753  NH1 ARG A 218      67.712  40.690  53.704  1.00 41.45           N  
ATOM   1754  NH2 ARG A 218      67.648  40.278  51.454  1.00 40.40           N  
ATOM   1755  N   PHE A 219      60.789  42.109  55.203  1.00 33.62           N  
ATOM   1756  CA  PHE A 219      60.401  42.804  56.421  1.00 30.89           C  
ATOM   1757  C   PHE A 219      59.018  42.453  56.949  1.00 33.35           C  
ATOM   1758  O   PHE A 219      58.754  42.718  58.130  1.00 32.95           O  
ATOM   1759  CB  PHE A 219      60.479  44.324  56.214  1.00 35.31           C  
ATOM   1760  CG  PHE A 219      61.855  44.807  55.856  1.00 36.30           C  
ATOM   1761  CD1 PHE A 219      62.874  44.788  56.808  1.00 39.88           C  
ATOM   1762  CD2 PHE A 219      62.138  45.265  54.574  1.00 34.60           C  
ATOM   1763  CE1 PHE A 219      64.157  45.231  56.490  1.00 40.45           C  
ATOM   1764  CE2 PHE A 219      63.416  45.721  54.237  1.00 37.01           C  
ATOM   1765  CZ  PHE A 219      64.429  45.701  55.199  1.00 42.78           C  
ATOM   1766  N   LEU A 220      58.144  41.853  56.138  1.00 31.71           N  
ATOM   1767  CA  LEU A 220      56.861  41.374  56.645  1.00 29.52           C  
ATOM   1768  C   LEU A 220      57.080  40.361  57.767  1.00 31.84           C  
ATOM   1769  O   LEU A 220      58.104  39.664  57.792  1.00 29.06           O  
ATOM   1770  CB  LEU A 220      56.051  40.701  55.537  1.00 29.68           C  
ATOM   1771  CG  LEU A 220      55.355  41.652  54.560  1.00 30.66           C  
ATOM   1772  CD1 LEU A 220      54.939  40.908  53.282  1.00 29.41           C  
ATOM   1773  CD2 LEU A 220      54.168  42.306  55.230  1.00 27.26           C  
ATOM   1774  N   PRO A 221      56.108  40.208  58.666  1.00 35.00           N  
ATOM   1775  CA  PRO A 221      56.209  39.141  59.675  1.00 37.81           C  
ATOM   1776  C   PRO A 221      56.410  37.796  58.992  1.00 36.54           C  
ATOM   1777  O   PRO A 221      55.700  37.447  58.037  1.00 32.14           O  
ATOM   1778  CB  PRO A 221      54.869  39.228  60.424  1.00 33.44           C  
ATOM   1779  CG  PRO A 221      54.439  40.676  60.237  1.00 34.25           C  
ATOM   1780  CD  PRO A 221      54.871  40.997  58.814  1.00 28.73           C  
ATOM   1781  N   VAL A 222      57.423  37.061  59.467  1.00 31.99           N  
ATOM   1782  CA  VAL A 222      57.967  35.839  58.858  1.00 29.55           C  
ATOM   1783  C   VAL A 222      57.912  35.901  57.332  1.00 28.33           C  
ATOM   1784  O   VAL A 222      57.566  34.919  56.666  1.00 32.83           O  
ATOM   1785  CB  VAL A 222      57.273  34.575  59.403  1.00 32.59           C  
ATOM   1786  CG1 VAL A 222      57.615  34.369  60.881  1.00 32.48           C  
ATOM   1787  CG2 VAL A 222      55.740  34.642  59.210  1.00 33.66           C  
ATOM   1788  N   GLY A 223      58.322  37.041  56.768  1.00 30.86           N  
ATOM   1789  CA  GLY A 223      58.091  37.307  55.354  1.00 30.97           C  
ATOM   1790  C   GLY A 223      58.788  36.344  54.413  1.00 31.65           C  
ATOM   1791  O   GLY A 223      58.295  36.075  53.316  1.00 31.18           O  
ATOM   1792  N   GLY A 224      59.935  35.802  54.824  1.00 31.36           N  
ATOM   1793  CA  GLY A 224      60.616  34.836  53.987  1.00 31.99           C  
ATOM   1794  C   GLY A 224      59.791  33.608  53.664  1.00 35.00           C  
ATOM   1795  O   GLY A 224      60.030  32.971  52.636  1.00 36.09           O  
ATOM   1796  N   LEU A 225      58.817  33.263  54.516  1.00 33.79           N  
ATOM   1797  CA  LEU A 225      57.979  32.091  54.261  1.00 33.36           C  
ATOM   1798  C   LEU A 225      57.045  32.273  53.064  1.00 36.57           C  
ATOM   1799  O   LEU A 225      56.497  31.281  52.570  1.00 34.93           O  
ATOM   1800  CB  LEU A 225      57.150  31.753  55.506  1.00 32.20           C  
ATOM   1801  CG  LEU A 225      57.930  31.569  56.813  1.00 34.65           C  
ATOM   1802  CD1 LEU A 225      57.000  31.182  57.961  1.00 35.75           C  
ATOM   1803  CD2 LEU A 225      59.039  30.539  56.644  1.00 36.24           C  
ATOM   1804  N   PHE A 226      56.823  33.502  52.600  1.00 34.04           N  
ATOM   1805  CA  PHE A 226      56.033  33.684  51.385  1.00 35.77           C  
ATOM   1806  C   PHE A 226      56.802  33.342  50.117  1.00 41.74           C  
ATOM   1807  O   PHE A 226      56.193  33.265  49.041  1.00 36.00           O  
ATOM   1808  CB  PHE A 226      55.510  35.120  51.288  1.00 31.34           C  
ATOM   1809  CG  PHE A 226      54.589  35.500  52.428  1.00 34.64           C  
ATOM   1810  CD1 PHE A 226      53.297  34.986  52.499  1.00 31.76           C  
ATOM   1811  CD2 PHE A 226      55.019  36.363  53.424  1.00 35.70           C  
ATOM   1812  CE1 PHE A 226      52.447  35.324  53.555  1.00 35.07           C  
ATOM   1813  CE2 PHE A 226      54.178  36.701  54.488  1.00 37.24           C  
ATOM   1814  CZ  PHE A 226      52.877  36.174  54.542  1.00 32.35           C  
ATOM   1815  N   GLU A 227      58.114  33.133  50.211  1.00 38.98           N  
ATOM   1816  CA  GLU A 227      58.940  32.850  49.035  1.00 36.53           C  
ATOM   1817  C   GLU A 227      58.956  31.340  48.811  1.00 45.44           C  
ATOM   1818  O   GLU A 227      59.960  30.663  49.011  1.00 56.29           O  
ATOM   1819  CB  GLU A 227      60.349  33.396  49.237  1.00 34.00           C  
ATOM   1820  CG  GLU A 227      60.382  34.889  49.483  1.00 33.03           C  
ATOM   1821  CD  GLU A 227      61.795  35.445  49.587  1.00 41.09           C  
ATOM   1822  OE1 GLU A 227      62.760  34.653  49.585  1.00 44.56           O  
ATOM   1823  OE2 GLU A 227      61.938  36.679  49.695  1.00 37.58           O  
ATOM   1824  N   VAL A 228      57.807  30.808  48.407  1.00 40.20           N  
ATOM   1825  CA  VAL A 228      57.695  29.412  48.022  1.00 38.01           C  
ATOM   1826  C   VAL A 228      57.344  29.411  46.539  1.00 39.81           C  
ATOM   1827  O   VAL A 228      57.044  30.448  45.948  1.00 44.68           O  
ATOM   1828  CB  VAL A 228      56.649  28.623  48.841  1.00 45.35           C  
ATOM   1829  CG1 VAL A 228      57.000  28.645  50.314  1.00 47.58           C  
ATOM   1830  CG2 VAL A 228      55.253  29.200  48.626  1.00 42.68           C  
ATOM   1831  N   ASP A 229      57.373  28.229  45.938  1.00 39.76           N  
ATOM   1832  CA  ASP A 229      56.925  28.078  44.560  1.00 42.90           C  
ATOM   1833  C   ASP A 229      55.401  28.009  44.540  1.00 43.62           C  
ATOM   1834  O   ASP A 229      54.811  27.078  45.101  1.00 47.59           O  
ATOM   1835  CB  ASP A 229      57.544  26.825  43.950  1.00 45.20           C  
ATOM   1836  CG  ASP A 229      57.304  26.721  42.452  1.00 51.40           C  
ATOM   1837  OD1 ASP A 229      56.604  27.586  41.875  1.00 51.47           O  
ATOM   1838  OD2 ASP A 229      57.831  25.765  41.851  1.00 63.50           O  
ATOM   1839  N   TRP A 230      54.757  28.992  43.912  1.00 36.34           N  
ATOM   1840  CA  TRP A 230      53.303  29.078  43.901  1.00 35.00           C  
ATOM   1841  C   TRP A 230      52.670  28.502  42.632  1.00 40.93           C  
ATOM   1842  O   TRP A 230      51.456  28.629  42.449  1.00 37.38           O  
ATOM   1843  CB  TRP A 230      52.870  30.533  44.086  1.00 33.73           C  
ATOM   1844  CG  TRP A 230      53.159  31.073  45.471  1.00 40.25           C  
ATOM   1845  CD1 TRP A 230      54.257  31.785  45.867  1.00 37.46           C  
ATOM   1846  CD2 TRP A 230      52.324  30.940  46.626  1.00 35.49           C  
ATOM   1847  NE1 TRP A 230      54.151  32.111  47.201  1.00 34.65           N  
ATOM   1848  CE2 TRP A 230      52.971  31.605  47.689  1.00 39.59           C  
ATOM   1849  CE3 TRP A 230      51.085  30.326  46.863  1.00 36.08           C  
ATOM   1850  CZ2 TRP A 230      52.429  31.658  48.982  1.00 38.25           C  
ATOM   1851  CZ3 TRP A 230      50.538  30.390  48.147  1.00 34.27           C  
ATOM   1852  CH2 TRP A 230      51.218  31.045  49.190  1.00 37.72           C  
ATOM   1853  N   ILE A 231      53.446  27.847  41.763  1.00 39.30           N  
ATOM   1854  CA  ILE A 231      53.071  27.272  40.466  1.00 50.23           C  
ATOM   1855  C   ILE A 231      51.746  26.511  40.558  1.00 40.24           C  
ATOM   1856  O   ILE A 231      50.907  26.600  39.656  1.00 45.76           O  
ATOM   1857  CB  ILE A 231      54.208  26.387  39.917  1.00 48.65           C  
ATOM   1858  CG1 ILE A 231      54.018  26.158  38.415  1.00 63.59           C  
ATOM   1859  CG2 ILE A 231      54.262  25.078  40.651  1.00 69.42           C  
ATOM   1860  CD1 ILE A 231      53.645  27.414  37.662  1.00 54.92           C  
ATOM   1861  N   THR A 232      51.838  25.533  41.464  1.00 44.93           N  
ATOM   1862  CA  THR A 232      50.749  24.566  41.609  1.00 42.42           C  
ATOM   1863  C   THR A 232      49.693  24.990  42.633  1.00 48.70           C  
ATOM   1864  O   THR A 232      48.868  24.158  43.033  1.00 45.62           O  
ATOM   1865  CB  THR A 232      51.292  23.177  41.970  1.00 47.74           C  
ATOM   1866  OG1 THR A 232      51.898  23.210  43.265  1.00 50.55           O  
ATOM   1867  CG2 THR A 232      52.328  22.710  40.933  1.00 47.82           C  
ATOM   1868  N   TYR A 233      49.694  26.256  43.061  1.00 45.98           N  
ATOM   1869  CA  TYR A 233      48.633  26.775  43.919  1.00 43.85           C  
ATOM   1870  C   TYR A 233      47.448  27.221  43.072  1.00 40.74           C  
ATOM   1871  O   TYR A 233      47.612  28.006  42.133  1.00 40.44           O  
ATOM   1872  CB  TYR A 233      49.140  27.956  44.750  1.00 37.57           C  
ATOM   1873  CG  TYR A 233      48.053  28.653  45.544  1.00 38.67           C  
ATOM   1874  CD1 TYR A 233      47.599  28.127  46.761  1.00 37.32           C  
ATOM   1875  CD2 TYR A 233      47.482  29.831  45.084  1.00 34.26           C  
ATOM   1876  CE1 TYR A 233      46.592  28.774  47.498  1.00 31.32           C  
ATOM   1877  CE2 TYR A 233      46.492  30.482  45.807  1.00 35.05           C  
ATOM   1878  CZ  TYR A 233      46.052  29.954  47.014  1.00 32.30           C  
ATOM   1879  OH  TYR A 233      45.067  30.608  47.709  1.00 33.64           O  
ATOM   1880  N   HIS A 234      46.256  26.732  43.417  1.00 38.52           N  
ATOM   1881  CA  HIS A 234      45.007  27.150  42.784  1.00 41.59           C  
ATOM   1882  C   HIS A 234      43.981  27.403  43.872  1.00 41.34           C  
ATOM   1883  O   HIS A 234      43.601  26.476  44.593  1.00 35.38           O  
ATOM   1884  CB  HIS A 234      44.491  26.093  41.799  1.00 41.28           C  
ATOM   1885  CG  HIS A 234      45.502  25.707  40.764  1.00 48.47           C  
ATOM   1886  ND1 HIS A 234      45.782  26.499  39.671  1.00 47.97           N  
ATOM   1887  CD2 HIS A 234      46.323  24.634  40.675  1.00 48.76           C  
ATOM   1888  CE1 HIS A 234      46.725  25.925  38.946  1.00 51.43           C  
ATOM   1889  NE2 HIS A 234      47.071  24.791  39.532  1.00 57.49           N  
ATOM   1890  N   THR A 235      43.519  28.647  43.975  1.00 39.17           N  
ATOM   1891  CA  THR A 235      42.650  29.024  45.077  1.00 38.54           C  
ATOM   1892  C   THR A 235      41.344  28.240  45.026  1.00 50.19           C  
ATOM   1893  O   THR A 235      40.813  27.933  43.952  1.00 41.89           O  
ATOM   1894  CB  THR A 235      42.357  30.524  45.029  1.00 37.60           C  
ATOM   1895  OG1 THR A 235      41.516  30.886  46.125  1.00 38.61           O  
ATOM   1896  CG2 THR A 235      41.660  30.897  43.703  1.00 38.17           C  
ATOM   1897  N   ASP A 236      40.828  27.912  46.205  1.00 38.25           N  
ATOM   1898  CA  ASP A 236      39.478  27.383  46.334  1.00 38.14           C  
ATOM   1899  C   ASP A 236      38.481  28.457  46.722  1.00 39.08           C  
ATOM   1900  O   ASP A 236      37.351  28.132  47.083  1.00 45.08           O  
ATOM   1901  CB  ASP A 236      39.439  26.241  47.357  1.00 40.53           C  
ATOM   1902  CG  ASP A 236      39.766  26.700  48.776  1.00 46.22           C  
ATOM   1903  OD1 ASP A 236      40.099  27.889  48.977  1.00 45.49           O  
ATOM   1904  OD2 ASP A 236      39.699  25.861  49.705  1.00 49.59           O  
ATOM   1905  N   GLY A 237      38.871  29.730  46.667  1.00 38.93           N  
ATOM   1906  CA  GLY A 237      38.036  30.810  47.153  1.00 34.05           C  
ATOM   1907  C   GLY A 237      38.205  31.143  48.620  1.00 41.48           C  
ATOM   1908  O   GLY A 237      37.711  32.185  49.067  1.00 36.00           O  
ATOM   1909  N   ASN A 238      38.880  30.289  49.384  1.00 34.80           N  
ATOM   1910  CA  ASN A 238      39.083  30.479  50.809  1.00 37.61           C  
ATOM   1911  C   ASN A 238      40.525  30.897  51.037  1.00 33.86           C  
ATOM   1912  O   ASN A 238      41.435  30.123  50.708  1.00 34.90           O  
ATOM   1913  CB  ASN A 238      38.775  29.184  51.563  1.00 38.32           C  
ATOM   1914  CG  ASN A 238      38.966  29.310  53.071  1.00 39.54           C  
ATOM   1915  OD1 ASN A 238      39.352  30.360  53.583  1.00 36.59           O  
ATOM   1916  ND2 ASN A 238      38.671  28.233  53.790  1.00 41.03           N  
ATOM   1917  N   PRO A 239      40.802  32.080  51.579  1.00 32.39           N  
ATOM   1918  CA  PRO A 239      42.205  32.478  51.749  1.00 33.92           C  
ATOM   1919  C   PRO A 239      42.979  31.564  52.676  1.00 34.31           C  
ATOM   1920  O   PRO A 239      44.210  31.515  52.576  1.00 33.33           O  
ATOM   1921  CB  PRO A 239      42.114  33.904  52.306  1.00 32.22           C  
ATOM   1922  CG  PRO A 239      40.704  34.057  52.804  1.00 38.91           C  
ATOM   1923  CD  PRO A 239      39.870  33.170  51.916  1.00 31.58           C  
ATOM   1924  N   THR A 240      42.306  30.830  53.569  1.00 35.18           N  
ATOM   1925  CA  THR A 240      43.018  29.923  54.458  1.00 36.78           C  
ATOM   1926  C   THR A 240      43.823  28.894  53.673  1.00 32.90           C  
ATOM   1927  O   THR A 240      44.889  28.452  54.126  1.00 33.81           O  
ATOM   1928  CB  THR A 240      42.021  29.226  55.407  1.00 34.09           C  
ATOM   1929  OG1 THR A 240      41.349  30.211  56.207  1.00 37.46           O  
ATOM   1930  CG2 THR A 240      42.741  28.285  56.339  1.00 34.37           C  
ATOM   1931  N   TYR A 241      43.332  28.493  52.505  1.00 32.44           N  
ATOM   1932  CA  TYR A 241      44.070  27.511  51.719  1.00 33.43           C  
ATOM   1933  C   TYR A 241      45.430  28.052  51.281  1.00 34.22           C  
ATOM   1934  O   TYR A 241      46.395  27.287  51.171  1.00 33.34           O  
ATOM   1935  CB  TYR A 241      43.240  27.071  50.509  1.00 34.88           C  
ATOM   1936  CG  TYR A 241      43.997  26.095  49.651  1.00 34.78           C  
ATOM   1937  CD1 TYR A 241      44.428  24.886  50.177  1.00 39.18           C  
ATOM   1938  CD2 TYR A 241      44.318  26.396  48.325  1.00 36.44           C  
ATOM   1939  CE1 TYR A 241      45.145  23.987  49.408  1.00 35.99           C  
ATOM   1940  CE2 TYR A 241      45.039  25.502  47.540  1.00 31.17           C  
ATOM   1941  CZ  TYR A 241      45.446  24.304  48.086  1.00 41.86           C  
ATOM   1942  OH  TYR A 241      46.164  23.406  47.334  1.00 40.26           O  
ATOM   1943  N   GLY A 242      45.549  29.365  51.062  1.00 34.03           N  
ATOM   1944  CA  GLY A 242      46.868  29.925  50.761  1.00 32.06           C  
ATOM   1945  C   GLY A 242      47.860  29.753  51.903  1.00 35.65           C  
ATOM   1946  O   GLY A 242      49.032  29.419  51.684  1.00 34.46           O  
ATOM   1947  N   TRP A 243      47.409  29.997  53.139  1.00 33.02           N  
ATOM   1948  CA  TRP A 243      48.283  29.798  54.291  1.00 29.55           C  
ATOM   1949  C   TRP A 243      48.640  28.326  54.462  1.00 31.50           C  
ATOM   1950  O   TRP A 243      49.797  27.996  54.744  1.00 36.05           O  
ATOM   1951  CB  TRP A 243      47.615  30.348  55.559  1.00 30.20           C  
ATOM   1952  CG  TRP A 243      47.381  31.835  55.516  1.00 31.52           C  
ATOM   1953  CD1 TRP A 243      46.221  32.486  55.171  1.00 31.79           C  
ATOM   1954  CD2 TRP A 243      48.345  32.861  55.809  1.00 27.52           C  
ATOM   1955  NE1 TRP A 243      46.414  33.856  55.243  1.00 31.09           N  
ATOM   1956  CE2 TRP A 243      47.707  34.103  55.634  1.00 29.64           C  
ATOM   1957  CE3 TRP A 243      49.693  32.845  56.178  1.00 27.64           C  
ATOM   1958  CZ2 TRP A 243      48.370  35.321  55.841  1.00 32.70           C  
ATOM   1959  CZ3 TRP A 243      50.339  34.055  56.396  1.00 27.36           C  
ATOM   1960  CH2 TRP A 243      49.681  35.269  56.230  1.00 27.86           C  
ATOM   1961  N   LEU A 244      47.668  27.428  54.279  1.00 29.48           N  
ATOM   1962  CA  LEU A 244      47.954  25.996  54.345  1.00 30.32           C  
ATOM   1963  C   LEU A 244      48.960  25.576  53.275  1.00 33.08           C  
ATOM   1964  O   LEU A 244      49.911  24.830  53.548  1.00 35.68           O  
ATOM   1965  CB  LEU A 244      46.657  25.202  54.191  1.00 31.48           C  
ATOM   1966  CG  LEU A 244      46.915  23.692  54.174  1.00 43.09           C  
ATOM   1967  CD1 LEU A 244      47.252  23.181  55.570  1.00 37.66           C  
ATOM   1968  CD2 LEU A 244      45.758  22.921  53.591  1.00 40.93           C  
ATOM   1969  N   TYR A 245      48.769  26.046  52.064  1.00 34.17           N  
ATOM   1970  CA  TYR A 245      49.665  25.726  50.971  1.00 34.20           C  
ATOM   1971  C   TYR A 245      51.080  26.148  51.281  1.00 35.41           C  
ATOM   1972  O   TYR A 245      52.008  25.422  51.083  1.00 35.49           O  
ATOM   1973  CB  TYR A 245      49.208  26.407  49.701  1.00 33.75           C  
ATOM   1974  CG  TYR A 245      50.082  26.172  48.494  1.00 37.12           C  
ATOM   1975  CD1 TYR A 245      51.180  26.949  48.253  1.00 35.31           C  
ATOM   1976  CD2 TYR A 245      49.782  25.191  47.582  1.00 41.16           C  
ATOM   1977  CE1 TYR A 245      51.967  26.742  47.154  1.00 35.20           C  
ATOM   1978  CE2 TYR A 245      50.560  24.980  46.470  1.00 38.47           C  
ATOM   1979  CZ  TYR A 245      51.648  25.765  46.270  1.00 39.70           C  
ATOM   1980  OH  TYR A 245      52.415  25.569  45.187  1.00 44.15           O  
ATOM   1981  N   LEU A 246      51.210  27.376  51.773  1.00 28.91           N  
ATOM   1982  CA  LEU A 246      52.508  27.939  52.118  1.00 35.63           C  
ATOM   1983  C   LEU A 246      53.239  27.069  53.131  1.00 43.18           C  
ATOM   1984  O   LEU A 246      54.423  26.774  52.968  1.00 40.16           O  
ATOM   1985  CB  LEU A 246      52.348  29.359  52.665  1.00 39.49           C  
ATOM   1986  CG  LEU A 246      53.611  30.018  53.222  1.00 49.15           C  
ATOM   1987  CD1 LEU A 246      53.530  31.532  53.091  1.00 46.38           C  
ATOM   1988  CD2 LEU A 246      53.834  29.613  54.671  1.00 37.64           C  
ATOM   1989  N   LEU A 247      52.524  26.671  54.178  1.00 35.36           N  
ATOM   1990  CA  LEU A 247      53.091  25.845  55.236  1.00 37.01           C  
ATOM   1991  C   LEU A 247      53.442  24.440  54.760  1.00 39.25           C  
ATOM   1992  O   LEU A 247      54.499  23.910  55.101  1.00 38.26           O  
ATOM   1993  CB  LEU A 247      52.131  25.769  56.426  1.00 34.41           C  
ATOM   1994  CG  LEU A 247      51.960  27.052  57.242  1.00 31.40           C  
ATOM   1995  CD1 LEU A 247      50.963  26.842  58.371  1.00 36.79           C  
ATOM   1996  CD2 LEU A 247      53.300  27.526  57.786  1.00 31.04           C  
ATOM   1997  N   HIS A 248      52.555  23.836  53.975  1.00 37.46           N  
ATOM   1998  CA  HIS A 248      52.799  22.487  53.478  1.00 42.83           C  
ATOM   1999  C   HIS A 248      54.008  22.441  52.547  1.00 47.55           C  
ATOM   2000  O   HIS A 248      54.832  21.527  52.635  1.00 43.61           O  
ATOM   2001  CB  HIS A 248      51.552  21.962  52.762  1.00 41.49           C  
ATOM   2002  CG  HIS A 248      51.715  20.583  52.211  1.00 43.13           C  
ATOM   2003  ND1 HIS A 248      51.911  20.338  50.872  1.00 45.00           N  
ATOM   2004  CD2 HIS A 248      51.726  19.375  52.822  1.00 45.64           C  
ATOM   2005  CE1 HIS A 248      52.030  19.036  50.677  1.00 47.15           C  
ATOM   2006  NE2 HIS A 248      51.919  18.430  51.845  1.00 51.22           N  
ATOM   2007  N   GLN A 249      54.132  23.426  51.653  1.00 40.63           N  
ATOM   2008  CA  GLN A 249      55.261  23.473  50.729  1.00 43.36           C  
ATOM   2009  C   GLN A 249      56.594  23.481  51.456  1.00 47.74           C  
ATOM   2010  O   GLN A 249      57.578  22.934  50.952  1.00 53.01           O  
ATOM   2011  CB  GLN A 249      55.156  24.711  49.847  1.00 46.03           C  
ATOM   2012  CG  GLN A 249      54.150  24.572  48.743  1.00 60.83           C  
ATOM   2013  CD  GLN A 249      54.708  23.794  47.576  1.00 61.55           C  
ATOM   2014  OE1 GLN A 249      54.122  22.798  47.134  1.00 52.24           O  
ATOM   2015  NE2 GLN A 249      55.847  24.246  47.065  1.00 55.22           N  
ATOM   2016  N   GLN A 250      56.657  24.104  52.626  1.00 43.65           N  
ATOM   2017  CA  GLN A 250      57.903  24.220  53.366  1.00 44.74           C  
ATOM   2018  C   GLN A 250      58.004  23.241  54.518  1.00 41.89           C  
ATOM   2019  O   GLN A 250      58.939  23.342  55.309  1.00 39.79           O  
ATOM   2020  CB  GLN A 250      58.063  25.635  53.904  1.00 49.44           C  
ATOM   2021  CG  GLN A 250      58.144  26.647  52.821  1.00 54.15           C  
ATOM   2022  CD  GLN A 250      58.026  28.030  53.371  1.00 42.11           C  
ATOM   2023  OE1 GLN A 250      59.024  28.686  53.629  1.00 47.05           O  
ATOM   2024  NE2 GLN A 250      56.796  28.495  53.546  1.00 36.84           N  
ATOM   2025  N   LYS A 251      57.055  22.315  54.647  1.00 41.44           N  
ATOM   2026  CA  LYS A 251      57.060  21.375  55.761  1.00 46.76           C  
ATOM   2027  C   LYS A 251      57.123  22.113  57.098  1.00 50.20           C  
ATOM   2028  O   LYS A 251      57.860  21.739  58.012  1.00 42.11           O  
ATOM   2029  CB  LYS A 251      58.217  20.387  55.627  1.00 50.37           C  
ATOM   2030  CG  LYS A 251      58.140  19.516  54.388  1.00 50.21           C  
ATOM   2031  CD  LYS A 251      59.169  18.396  54.450  1.00 65.41           C  
ATOM   2032  CE  LYS A 251      58.974  17.391  53.320  1.00 81.23           C  
ATOM   2033  NZ  LYS A 251      59.204  17.984  51.968  1.00 75.84           N  
ATOM   2034  N   ARG A 252      56.341  23.184  57.219  1.00 45.08           N  
ATOM   2035  CA  ARG A 252      56.275  23.939  58.460  1.00 40.20           C  
ATOM   2036  C   ARG A 252      54.894  23.811  59.093  1.00 40.69           C  
ATOM   2037  O   ARG A 252      53.935  23.329  58.480  1.00 38.34           O  
ATOM   2038  CB  ARG A 252      56.653  25.406  58.224  1.00 36.95           C  
ATOM   2039  CG  ARG A 252      58.156  25.587  57.958  1.00 44.90           C  
ATOM   2040  CD  ARG A 252      58.578  27.055  57.887  1.00 45.26           C  
ATOM   2041  NE  ARG A 252      60.032  27.221  57.778  1.00 44.64           N  
ATOM   2042  CZ  ARG A 252      60.858  27.313  58.819  1.00 47.81           C  
ATOM   2043  NH1 ARG A 252      60.389  27.243  60.053  1.00 45.53           N  
ATOM   2044  NH2 ARG A 252      62.159  27.465  58.628  1.00 52.90           N  
ATOM   2045  N   GLN A 253      54.814  24.242  60.351  1.00 41.53           N  
ATOM   2046  CA  GLN A 253      53.627  24.098  61.184  1.00 36.79           C  
ATOM   2047  C   GLN A 253      52.987  25.455  61.446  1.00 39.38           C  
ATOM   2048  O   GLN A 253      53.573  26.511  61.193  1.00 37.92           O  
ATOM   2049  CB  GLN A 253      53.978  23.425  62.518  1.00 41.49           C  
ATOM   2050  CG  GLN A 253      54.683  22.092  62.368  1.00 45.79           C  
ATOM   2051  CD  GLN A 253      53.793  21.035  61.759  1.00 56.16           C  
ATOM   2052  OE1 GLN A 253      52.614  20.922  62.106  1.00 60.22           O  
ATOM   2053  NE2 GLN A 253      54.346  20.256  60.829  1.00 59.28           N  
ATOM   2054  N   PHE A 254      51.774  25.415  62.006  1.00 35.89           N  
ATOM   2055  CA  PHE A 254      51.006  26.643  62.158  1.00 34.27           C  
ATOM   2056  C   PHE A 254      51.725  27.669  63.027  1.00 35.38           C  
ATOM   2057  O   PHE A 254      51.564  28.880  62.815  1.00 33.96           O  
ATOM   2058  CB  PHE A 254      49.625  26.348  62.741  1.00 35.28           C  
ATOM   2059  CG  PHE A 254      48.881  27.588  63.126  1.00 36.92           C  
ATOM   2060  CD1 PHE A 254      48.096  28.248  62.193  1.00 36.81           C  
ATOM   2061  CD2 PHE A 254      49.021  28.135  64.400  1.00 34.95           C  
ATOM   2062  CE1 PHE A 254      47.435  29.421  62.532  1.00 33.53           C  
ATOM   2063  CE2 PHE A 254      48.365  29.304  64.747  1.00 33.43           C  
ATOM   2064  CZ  PHE A 254      47.571  29.955  63.799  1.00 32.16           C  
ATOM   2065  N   THR A 255      52.496  27.220  64.026  1.00 32.35           N  
ATOM   2066  CA  THR A 255      53.107  28.179  64.936  1.00 34.90           C  
ATOM   2067  C   THR A 255      54.014  29.159  64.202  1.00 34.13           C  
ATOM   2068  O   THR A 255      54.221  30.283  64.674  1.00 35.16           O  
ATOM   2069  CB  THR A 255      53.885  27.454  66.044  1.00 39.59           C  
ATOM   2070  OG1 THR A 255      54.390  28.417  66.978  1.00 43.59           O  
ATOM   2071  CG2 THR A 255      55.046  26.665  65.466  1.00 44.24           C  
ATOM   2072  N   ASP A 256      54.545  28.772  63.041  1.00 36.15           N  
ATOM   2073  CA  ASP A 256      55.443  29.675  62.327  1.00 36.68           C  
ATOM   2074  C   ASP A 256      54.729  30.897  61.745  1.00 35.08           C  
ATOM   2075  O   ASP A 256      55.381  31.907  61.474  1.00 36.61           O  
ATOM   2076  CB  ASP A 256      56.177  28.905  61.230  1.00 38.20           C  
ATOM   2077  CG  ASP A 256      57.241  27.975  61.790  1.00 40.85           C  
ATOM   2078  OD1 ASP A 256      57.716  28.231  62.915  1.00 38.80           O  
ATOM   2079  OD2 ASP A 256      57.601  26.998  61.114  1.00 44.62           O  
ATOM   2080  N   ILE A 257      53.414  30.853  61.559  1.00 34.29           N  
ATOM   2081  CA  ILE A 257      52.700  31.999  61.002  1.00 35.81           C  
ATOM   2082  C   ILE A 257      51.772  32.640  62.024  1.00 37.29           C  
ATOM   2083  O   ILE A 257      50.937  33.475  61.657  1.00 31.75           O  
ATOM   2084  CB  ILE A 257      51.919  31.626  59.727  1.00 34.57           C  
ATOM   2085  CG1 ILE A 257      50.893  30.528  60.025  1.00 29.35           C  
ATOM   2086  CG2 ILE A 257      52.889  31.225  58.577  1.00 28.64           C  
ATOM   2087  CD1 ILE A 257      49.998  30.171  58.835  1.00 33.12           C  
ATOM   2088  N   LYS A 258      51.901  32.285  63.309  1.00 32.30           N  
ATOM   2089  CA  LYS A 258      50.893  32.748  64.253  1.00 28.22           C  
ATOM   2090  C   LYS A 258      50.948  34.252  64.495  1.00 33.80           C  
ATOM   2091  O   LYS A 258      49.976  34.804  65.019  1.00 34.28           O  
ATOM   2092  CB  LYS A 258      50.997  31.975  65.581  1.00 33.98           C  
ATOM   2093  CG  LYS A 258      52.216  32.250  66.426  1.00 39.66           C  
ATOM   2094  CD  LYS A 258      52.053  31.552  67.800  1.00 42.72           C  
ATOM   2095  CE  LYS A 258      53.252  31.769  68.706  1.00 46.31           C  
ATOM   2096  NZ  LYS A 258      53.100  31.030  70.007  1.00 60.45           N  
ATOM   2097  N   ASP A 259      52.022  34.935  64.084  1.00 34.76           N  
ATOM   2098  CA  ASP A 259      52.071  36.395  64.191  1.00 35.29           C  
ATOM   2099  C   ASP A 259      50.892  37.081  63.496  1.00 36.52           C  
ATOM   2100  O   ASP A 259      50.566  38.228  63.831  1.00 32.90           O  
ATOM   2101  CB  ASP A 259      53.364  36.947  63.578  1.00 40.66           C  
ATOM   2102  CG  ASP A 259      54.611  36.610  64.385  1.00 58.20           C  
ATOM   2103  OD1 ASP A 259      54.541  36.615  65.628  1.00 44.85           O  
ATOM   2104  OD2 ASP A 259      55.668  36.366  63.754  1.00 51.45           O  
ATOM   2105  N   TYR A 260      50.280  36.439  62.489  1.00 30.64           N  
ATOM   2106  CA  TYR A 260      49.202  37.099  61.754  1.00 29.64           C  
ATOM   2107  C   TYR A 260      47.851  37.051  62.466  1.00 35.13           C  
ATOM   2108  O   TYR A 260      46.873  37.572  61.917  1.00 32.95           O  
ATOM   2109  CB  TYR A 260      49.089  36.510  60.336  1.00 28.51           C  
ATOM   2110  CG  TYR A 260      50.228  37.014  59.474  1.00 34.46           C  
ATOM   2111  CD1 TYR A 260      50.146  38.250  58.839  1.00 34.03           C  
ATOM   2112  CD2 TYR A 260      51.397  36.272  59.327  1.00 26.74           C  
ATOM   2113  CE1 TYR A 260      51.183  38.733  58.070  1.00 34.87           C  
ATOM   2114  CE2 TYR A 260      52.458  36.757  58.553  1.00 30.78           C  
ATOM   2115  CZ  TYR A 260      52.338  37.988  57.937  1.00 34.52           C  
ATOM   2116  OH  TYR A 260      53.369  38.483  57.180  1.00 31.29           O  
ATOM   2117  N   ARG A 261      47.774  36.466  63.665  1.00 34.80           N  
ATOM   2118  CA  ARG A 261      46.601  36.581  64.546  1.00 35.14           C  
ATOM   2119  C   ARG A 261      45.329  35.970  63.955  1.00 32.21           C  
ATOM   2120  O   ARG A 261      44.291  36.617  63.819  1.00 34.51           O  
ATOM   2121  CB  ARG A 261      46.380  38.042  64.950  1.00 34.32           C  
ATOM   2122  CG  ARG A 261      47.473  38.522  65.873  1.00 35.44           C  
ATOM   2123  CD  ARG A 261      47.230  39.925  66.374  1.00 48.77           C  
ATOM   2124  NE  ARG A 261      48.317  40.357  67.245  1.00 55.08           N  
ATOM   2125  CZ  ARG A 261      48.549  41.623  67.578  1.00 69.22           C  
ATOM   2126  NH1 ARG A 261      47.766  42.595  67.110  1.00 56.69           N  
ATOM   2127  NH2 ARG A 261      49.567  41.916  68.376  1.00 66.81           N  
ATOM   2128  N   PHE A 262      45.436  34.694  63.605  1.00 33.53           N  
ATOM   2129  CA  PHE A 262      44.301  33.949  63.072  1.00 33.08           C  
ATOM   2130  C   PHE A 262      43.213  33.730  64.124  1.00 36.36           C  
ATOM   2131  O   PHE A 262      43.497  33.613  65.318  1.00 34.87           O  
ATOM   2132  CB  PHE A 262      44.776  32.591  62.554  1.00 36.39           C  
ATOM   2133  CG  PHE A 262      45.672  32.680  61.358  1.00 34.15           C  
ATOM   2134  CD1 PHE A 262      47.035  32.904  61.507  1.00 34.88           C  
ATOM   2135  CD2 PHE A 262      45.149  32.566  60.078  1.00 37.54           C  
ATOM   2136  CE1 PHE A 262      47.862  32.996  60.382  1.00 34.58           C  
ATOM   2137  CE2 PHE A 262      45.971  32.654  58.954  1.00 37.15           C  
ATOM   2138  CZ  PHE A 262      47.326  32.873  59.113  1.00 34.27           C  
ATOM   2139  N   SER A 263      41.966  33.634  63.668  1.00 35.59           N  
ATOM   2140  CA  SER A 263      40.900  33.215  64.565  1.00 40.20           C  
ATOM   2141  C   SER A 263      41.137  31.776  65.004  1.00 45.12           C  
ATOM   2142  O   SER A 263      41.851  31.010  64.348  1.00 36.52           O  
ATOM   2143  CB  SER A 263      39.536  33.332  63.887  1.00 39.75           C  
ATOM   2144  OG  SER A 263      39.381  32.369  62.852  1.00 42.05           O  
ATOM   2145  N   ASN A 264      40.541  31.404  66.139  1.00 42.28           N  
ATOM   2146  CA  ASN A 264      40.664  30.015  66.567  1.00 44.65           C  
ATOM   2147  C   ASN A 264      40.133  29.079  65.492  1.00 37.44           C  
ATOM   2148  O   ASN A 264      40.668  27.982  65.291  1.00 33.39           O  
ATOM   2149  CB  ASN A 264      39.931  29.795  67.889  1.00 48.32           C  
ATOM   2150  CG  ASN A 264      40.662  30.410  69.057  1.00 52.57           C  
ATOM   2151  OD1 ASN A 264      41.890  30.537  69.044  1.00 55.04           O  
ATOM   2152  ND2 ASN A 264      39.910  30.796  70.080  1.00 63.92           N  
ATOM   2153  N   GLU A 265      39.090  29.513  64.784  1.00 34.57           N  
ATOM   2154  CA  GLU A 265      38.471  28.693  63.756  1.00 45.61           C  
ATOM   2155  C   GLU A 265      39.398  28.527  62.554  1.00 44.36           C  
ATOM   2156  O   GLU A 265      39.560  27.416  62.033  1.00 35.81           O  
ATOM   2157  CB  GLU A 265      37.135  29.316  63.336  1.00 45.28           C  
ATOM   2158  CG  GLU A 265      36.059  29.348  64.450  1.00 56.57           C  
ATOM   2159  CD  GLU A 265      36.343  30.347  65.597  1.00 69.84           C  
ATOM   2160  OE1 GLU A 265      37.125  31.312  65.414  1.00 49.58           O  
ATOM   2161  OE2 GLU A 265      35.770  30.158  66.700  1.00 75.94           O  
ATOM   2162  N   GLU A 266      40.044  29.592  62.150  1.00 34.61           N  
ATOM   2163  CA  GLU A 266      40.968  29.516  61.063  1.00 35.67           C  
ATOM   2164  C   GLU A 266      42.172  28.687  61.471  1.00 36.34           C  
ATOM   2165  O   GLU A 266      42.608  27.820  60.718  1.00 32.91           O  
ATOM   2166  CB  GLU A 266      41.342  30.906  60.572  1.00 32.58           C  
ATOM   2167  CG  GLU A 266      42.041  30.895  59.237  1.00 59.51           C  
ATOM   2168  CD  GLU A 266      42.112  32.250  58.550  1.00 75.67           C  
ATOM   2169  OE1 GLU A 266      41.649  33.223  59.190  1.00 62.06           O  
ATOM   2170  OE2 GLU A 266      42.597  32.286  57.397  1.00 55.34           O  
ATOM   2171  N   LYS A 267      42.694  28.913  62.648  1.00 31.70           N  
ATOM   2172  CA  LYS A 267      43.825  28.145  63.157  1.00 30.80           C  
ATOM   2173  C   LYS A 267      43.524  26.650  63.153  1.00 36.86           C  
ATOM   2174  O   LYS A 267      44.370  25.838  62.761  1.00 32.52           O  
ATOM   2175  CB  LYS A 267      44.176  28.628  64.568  1.00 35.27           C  
ATOM   2176  CG  LYS A 267      45.104  27.706  65.345  1.00 35.19           C  
ATOM   2177  CD  LYS A 267      45.358  28.242  66.758  1.00 32.67           C  
ATOM   2178  CE  LYS A 267      46.180  27.249  67.573  1.00 39.31           C  
ATOM   2179  NZ  LYS A 267      46.583  27.785  68.900  1.00 47.15           N  
ATOM   2180  N   ARG A 268      42.318  26.270  63.585  1.00 33.69           N  
ATOM   2181  CA  ARG A 268      41.960  24.855  63.644  1.00 38.63           C  
ATOM   2182  C   ARG A 268      41.939  24.225  62.257  1.00 35.04           C  
ATOM   2183  O   ARG A 268      42.453  23.113  62.067  1.00 33.46           O  
ATOM   2184  CB  ARG A 268      40.593  24.687  64.314  1.00 36.75           C  
ATOM   2185  CG  ARG A 268      40.285  23.240  64.678  1.00 37.57           C  
ATOM   2186  CD  ARG A 268      38.939  23.079  65.385  1.00 38.55           C  
ATOM   2187  NE  ARG A 268      38.785  21.712  65.876  1.00 37.98           N  
ATOM   2188  CZ  ARG A 268      39.155  21.312  67.092  1.00 46.38           C  
ATOM   2189  NH1 ARG A 268      39.676  22.182  67.944  1.00 44.62           N  
ATOM   2190  NH2 ARG A 268      38.997  20.046  67.460  1.00 39.41           N  
ATOM   2191  N   LEU A 269      41.325  24.908  61.281  1.00 32.90           N  
ATOM   2192  CA  LEU A 269      41.300  24.401  59.907  1.00 37.25           C  
ATOM   2193  C   LEU A 269      42.707  24.110  59.408  1.00 33.49           C  
ATOM   2194  O   LEU A 269      42.977  23.028  58.870  1.00 34.91           O  
ATOM   2195  CB  LEU A 269      40.596  25.407  58.986  1.00 40.43           C  
ATOM   2196  CG  LEU A 269      40.431  25.042  57.507  1.00 37.51           C  
ATOM   2197  CD1 LEU A 269      39.737  23.682  57.372  1.00 38.68           C  
ATOM   2198  CD2 LEU A 269      39.632  26.102  56.776  1.00 35.99           C  
ATOM   2199  N   ILE A 270      43.628  25.055  59.601  1.00 32.85           N  
ATOM   2200  CA  ILE A 270      45.014  24.858  59.169  1.00 31.37           C  
ATOM   2201  C   ILE A 270      45.654  23.678  59.895  1.00 37.65           C  
ATOM   2202  O   ILE A 270      46.223  22.777  59.264  1.00 35.11           O  
ATOM   2203  CB  ILE A 270      45.829  26.146  59.383  1.00 32.35           C  
ATOM   2204  CG1 ILE A 270      45.284  27.281  58.530  1.00 32.99           C  
ATOM   2205  CG2 ILE A 270      47.294  25.899  59.073  1.00 31.05           C  
ATOM   2206  CD1 ILE A 270      45.917  28.639  58.856  1.00 33.16           C  
ATOM   2207  N   GLU A 271      45.596  23.678  61.238  1.00 31.22           N  
ATOM   2208  CA  GLU A 271      46.311  22.657  62.000  1.00 30.16           C  
ATOM   2209  C   GLU A 271      45.760  21.268  61.721  1.00 35.60           C  
ATOM   2210  O   GLU A 271      46.523  20.303  61.609  1.00 36.09           O  
ATOM   2211  CB  GLU A 271      46.232  22.949  63.501  1.00 34.67           C  
ATOM   2212  CG  GLU A 271      47.051  24.159  63.942  1.00 37.58           C  
ATOM   2213  CD  GLU A 271      47.110  24.301  65.457  1.00 45.82           C  
ATOM   2214  OE1 GLU A 271      46.084  24.044  66.127  1.00 37.53           O  
ATOM   2215  OE2 GLU A 271      48.189  24.667  65.964  1.00 45.01           O  
ATOM   2216  N   LYS A 272      44.432  21.139  61.652  1.00 30.27           N  
ATOM   2217  CA  LYS A 272      43.846  19.829  61.388  1.00 37.07           C  
ATOM   2218  C   LYS A 272      44.094  19.395  59.942  1.00 37.73           C  
ATOM   2219  O   LYS A 272      44.327  18.209  59.681  1.00 34.83           O  
ATOM   2220  CB  LYS A 272      42.351  19.847  61.721  1.00 32.55           C  
ATOM   2221  CG  LYS A 272      42.024  20.225  63.205  1.00 35.34           C  
ATOM   2222  CD  LYS A 272      42.657  19.264  64.240  1.00 31.81           C  
ATOM   2223  CE  LYS A 272      42.312  19.656  65.695  1.00 33.75           C  
ATOM   2224  NZ  LYS A 272      43.023  18.792  66.694  1.00 40.49           N  
ATOM   2225  N   SER A 273      44.105  20.335  58.997  1.00 34.62           N  
ATOM   2226  CA  SER A 273      44.454  19.968  57.623  1.00 34.57           C  
ATOM   2227  C   SER A 273      45.892  19.477  57.528  1.00 37.17           C  
ATOM   2228  O   SER A 273      46.170  18.474  56.854  1.00 40.26           O  
ATOM   2229  CB  SER A 273      44.214  21.148  56.680  1.00 36.34           C  
ATOM   2230  OG  SER A 273      42.834  21.437  56.604  1.00 38.25           O  
ATOM   2231  N   LEU A 274      46.823  20.152  58.211  1.00 36.60           N  
ATOM   2232  CA  LEU A 274      48.213  19.712  58.178  1.00 39.50           C  
ATOM   2233  C   LEU A 274      48.385  18.336  58.813  1.00 47.36           C  
ATOM   2234  O   LEU A 274      49.145  17.506  58.296  1.00 41.87           O  
ATOM   2235  CB  LEU A 274      49.116  20.733  58.867  1.00 47.33           C  
ATOM   2236  CG  LEU A 274      49.547  21.959  58.057  1.00 44.65           C  
ATOM   2237  CD1 LEU A 274      50.260  22.935  58.965  1.00 45.67           C  
ATOM   2238  CD2 LEU A 274      50.439  21.578  56.860  1.00 41.39           C  
ATOM   2239  N   GLU A 275      47.707  18.073  59.940  1.00 39.75           N  
ATOM   2240  CA  GLU A 275      47.724  16.717  60.497  1.00 42.07           C  
ATOM   2241  C   GLU A 275      47.359  15.693  59.432  1.00 36.35           C  
ATOM   2242  O   GLU A 275      48.034  14.671  59.275  1.00 39.68           O  
ATOM   2243  CB  GLU A 275      46.756  16.588  61.682  1.00 37.51           C  
ATOM   2244  CG  GLU A 275      47.133  17.343  62.932  1.00 46.25           C  
ATOM   2245  CD  GLU A 275      46.164  17.075  64.088  1.00 48.82           C  
ATOM   2246  OE1 GLU A 275      45.135  16.377  63.881  1.00 43.94           O  
ATOM   2247  OE2 GLU A 275      46.424  17.567  65.206  1.00 50.32           O  
ATOM   2248  N   LEU A 276      46.269  15.943  58.701  1.00 35.12           N  
ATOM   2249  CA  LEU A 276      45.826  14.990  57.688  1.00 40.51           C  
ATOM   2250  C   LEU A 276      46.891  14.779  56.612  1.00 49.06           C  
ATOM   2251  O   LEU A 276      47.069  13.657  56.119  1.00 42.62           O  
ATOM   2252  CB  LEU A 276      44.508  15.456  57.071  1.00 34.81           C  
ATOM   2253  CG  LEU A 276      43.285  15.335  57.997  1.00 37.06           C  
ATOM   2254  CD1 LEU A 276      42.088  16.061  57.418  1.00 32.69           C  
ATOM   2255  CD2 LEU A 276      42.939  13.877  58.231  1.00 37.66           C  
ATOM   2256  N   THR A 277      47.620  15.837  56.237  1.00 40.44           N  
ATOM   2257  CA  THR A 277      48.627  15.658  55.194  1.00 41.60           C  
ATOM   2258  C   THR A 277      49.765  14.767  55.662  1.00 42.95           C  
ATOM   2259  O   THR A 277      50.424  14.140  54.827  1.00 47.36           O  
ATOM   2260  CB  THR A 277      49.206  16.997  54.714  1.00 38.41           C  
ATOM   2261  OG1 THR A 277      50.039  17.568  55.729  1.00 42.52           O  
ATOM   2262  CG2 THR A 277      48.104  17.979  54.340  1.00 39.08           C  
ATOM   2263  N   ALA A 278      50.005  14.692  56.965  1.00 39.98           N  
ATOM   2264  CA  ALA A 278      51.045  13.833  57.510  1.00 42.66           C  
ATOM   2265  C   ALA A 278      50.526  12.460  57.917  1.00 52.55           C  
ATOM   2266  O   ALA A 278      51.301  11.642  58.422  1.00 52.13           O  
ATOM   2267  CB  ALA A 278      51.713  14.517  58.708  1.00 41.24           C  
ATOM   2268  N   LEU A 279      49.239  12.193  57.723  1.00 46.84           N  
ATOM   2269  CA  LEU A 279      48.644  10.916  58.094  1.00 46.49           C  
ATOM   2270  C   LEU A 279      48.720   9.982  56.898  1.00 47.53           C  
ATOM   2271  O   LEU A 279      48.141  10.269  55.842  1.00 46.61           O  
ATOM   2272  CB  LEU A 279      47.196  11.110  58.543  1.00 47.87           C  
ATOM   2273  CG  LEU A 279      46.492   9.898  59.145  1.00 58.09           C  
ATOM   2274  CD1 LEU A 279      47.166   9.485  60.449  1.00 55.75           C  
ATOM   2275  CD2 LEU A 279      45.017  10.212  59.372  1.00 42.98           C  
ATOM   2276  N   ASN A 280      49.431   8.865  57.060  1.00 50.10           N  
ATOM   2277  CA  ASN A 280      49.725   8.071  55.871  1.00 57.09           C  
ATOM   2278  C   ASN A 280      48.472   7.402  55.316  1.00 60.56           C  
ATOM   2279  O   ASN A 280      48.250   7.406  54.099  1.00 55.80           O  
ATOM   2280  CB  ASN A 280      50.802   7.034  56.184  1.00 63.54           C  
ATOM   2281  CG  ASN A 280      51.385   6.413  54.929  1.00 80.10           C  
ATOM   2282  OD1 ASN A 280      51.387   7.031  53.861  1.00 79.57           O  
ATOM   2283  ND2 ASN A 280      51.907   5.192  55.055  1.00 86.04           N  
ATOM   2284  N   THR A 281      47.577   6.889  56.158  1.00 60.14           N  
ATOM   2285  CA  THR A 281      46.364   6.244  55.667  1.00 63.10           C  
ATOM   2286  C   THR A 281      45.140   6.826  56.358  1.00 41.56           C  
ATOM   2287  O   THR A 281      45.099   6.925  57.585  1.00 48.13           O  
ATOM   2288  CB  THR A 281      46.426   4.729  55.879  1.00 68.37           C  
ATOM   2289  OG1 THR A 281      46.958   4.461  57.179  1.00 73.16           O  
ATOM   2290  CG2 THR A 281      47.322   4.078  54.815  1.00 60.60           C  
ATOM   2291  N   TRP A 282      44.162   7.234  55.562  1.00 44.74           N  
ATOM   2292  CA  TRP A 282      42.874   7.688  56.058  1.00 39.10           C  
ATOM   2293  C   TRP A 282      41.904   6.513  56.012  1.00 46.10           C  
ATOM   2294  O   TRP A 282      41.782   5.841  54.985  1.00 43.70           O  
ATOM   2295  CB  TRP A 282      42.337   8.843  55.213  1.00 40.83           C  
ATOM   2296  CG  TRP A 282      43.253  10.048  55.107  1.00 35.40           C  
ATOM   2297  CD1 TRP A 282      44.496  10.191  55.646  1.00 39.96           C  
ATOM   2298  CD2 TRP A 282      42.966  11.276  54.430  1.00 32.48           C  
ATOM   2299  NE1 TRP A 282      45.007  11.432  55.343  1.00 37.98           N  
ATOM   2300  CE2 TRP A 282      44.085  12.117  54.598  1.00 35.54           C  
ATOM   2301  CE3 TRP A 282      41.873  11.743  53.694  1.00 40.79           C  
ATOM   2302  CZ2 TRP A 282      44.144  13.395  54.055  1.00 39.60           C  
ATOM   2303  CZ3 TRP A 282      41.933  13.018  53.153  1.00 43.72           C  
ATOM   2304  CH2 TRP A 282      43.062  13.831  53.337  1.00 44.09           C  
ATOM   2305  N   ASP A 283      41.234   6.245  57.130  1.00 36.86           N  
ATOM   2306  CA  ASP A 283      40.235   5.187  57.165  1.00 39.98           C  
ATOM   2307  C   ASP A 283      38.966   5.759  57.803  1.00 38.19           C  
ATOM   2308  O   ASP A 283      38.833   6.969  58.047  1.00 36.31           O  
ATOM   2309  CB  ASP A 283      40.778   3.967  57.933  1.00 38.78           C  
ATOM   2310  CG  ASP A 283      40.873   4.201  59.432  1.00 44.70           C  
ATOM   2311  OD1 ASP A 283      40.541   5.314  59.927  1.00 43.11           O  
ATOM   2312  OD2 ASP A 283      41.282   3.250  60.127  1.00 42.61           O  
ATOM   2313  N   GLN A 284      37.996   4.881  58.072  1.00 35.23           N  
ATOM   2314  CA  GLN A 284      36.696   5.338  58.568  1.00 40.37           C  
ATOM   2315  C   GLN A 284      36.800   6.276  59.769  1.00 31.90           C  
ATOM   2316  O   GLN A 284      36.035   7.241  59.878  1.00 34.31           O  
ATOM   2317  CB  GLN A 284      35.811   4.136  58.916  1.00 34.17           C  
ATOM   2318  CG  GLN A 284      35.281   3.364  57.705  1.00 35.71           C  
ATOM   2319  CD  GLN A 284      36.286   2.369  57.137  1.00 35.91           C  
ATOM   2320  OE1 GLN A 284      37.386   2.189  57.666  1.00 36.16           O  
ATOM   2321  NE2 GLN A 284      35.895   1.700  56.047  1.00 42.72           N  
ATOM   2322  N   TRP A 285      37.734   6.002  60.678  1.00 33.46           N  
ATOM   2323  CA  TRP A 285      37.899   6.837  61.866  1.00 36.47           C  
ATOM   2324  C   TRP A 285      38.428   8.216  61.496  1.00 39.88           C  
ATOM   2325  O   TRP A 285      38.024   9.223  62.092  1.00 33.50           O  
ATOM   2326  CB  TRP A 285      38.829   6.146  62.856  1.00 31.79           C  
ATOM   2327  CG  TRP A 285      38.864   6.789  64.211  1.00 37.48           C  
ATOM   2328  CD1 TRP A 285      39.930   7.407  64.797  1.00 35.89           C  
ATOM   2329  CD2 TRP A 285      37.788   6.860  65.155  1.00 33.34           C  
ATOM   2330  NE1 TRP A 285      39.586   7.861  66.053  1.00 34.61           N  
ATOM   2331  CE2 TRP A 285      38.275   7.541  66.293  1.00 40.29           C  
ATOM   2332  CE3 TRP A 285      36.461   6.420  65.144  1.00 33.04           C  
ATOM   2333  CZ2 TRP A 285      37.480   7.790  67.413  1.00 35.99           C  
ATOM   2334  CZ3 TRP A 285      35.669   6.667  66.259  1.00 35.13           C  
ATOM   2335  CH2 TRP A 285      36.181   7.347  67.377  1.00 33.09           C  
ATOM   2336  N   THR A 286      39.327   8.278  60.509  1.00 36.38           N  
ATOM   2337  CA  THR A 286      39.759   9.556  59.949  1.00 32.22           C  
ATOM   2338  C   THR A 286      38.573  10.359  59.428  1.00 34.77           C  
ATOM   2339  O   THR A 286      38.411  11.536  59.768  1.00 32.79           O  
ATOM   2340  CB  THR A 286      40.767   9.324  58.812  1.00 40.16           C  
ATOM   2341  OG1 THR A 286      41.773   8.394  59.235  1.00 33.83           O  
ATOM   2342  CG2 THR A 286      41.434  10.649  58.414  1.00 33.02           C  
ATOM   2343  N   PHE A 287      37.763   9.757  58.550  1.00 31.72           N  
ATOM   2344  CA  PHE A 287      36.658  10.501  57.949  1.00 34.76           C  
ATOM   2345  C   PHE A 287      35.617  10.891  58.997  1.00 36.51           C  
ATOM   2346  O   PHE A 287      34.940  11.918  58.847  1.00 33.62           O  
ATOM   2347  CB  PHE A 287      36.026   9.680  56.816  1.00 32.69           C  
ATOM   2348  CG  PHE A 287      36.780   9.786  55.509  1.00 32.63           C  
ATOM   2349  CD1 PHE A 287      37.909   9.022  55.279  1.00 33.70           C  
ATOM   2350  CD2 PHE A 287      36.368  10.676  54.532  1.00 34.46           C  
ATOM   2351  CE1 PHE A 287      38.622   9.144  54.078  1.00 33.91           C  
ATOM   2352  CE2 PHE A 287      37.071  10.795  53.338  1.00 40.28           C  
ATOM   2353  CZ  PHE A 287      38.198  10.035  53.116  1.00 37.89           C  
ATOM   2354  N   TYR A 288      35.485  10.094  60.056  1.00 33.88           N  
ATOM   2355  CA  TYR A 288      34.515  10.388  61.111  1.00 35.75           C  
ATOM   2356  C   TYR A 288      34.953  11.584  61.950  1.00 33.82           C  
ATOM   2357  O   TYR A 288      34.155  12.496  62.205  1.00 36.79           O  
ATOM   2358  CB  TYR A 288      34.325   9.147  61.990  1.00 33.00           C  
ATOM   2359  CG  TYR A 288      33.435   9.313  63.218  1.00 34.15           C  
ATOM   2360  CD1 TYR A 288      32.048   9.385  63.096  1.00 35.64           C  
ATOM   2361  CD2 TYR A 288      33.981   9.356  64.500  1.00 33.71           C  
ATOM   2362  CE1 TYR A 288      31.221   9.503  64.227  1.00 36.30           C  
ATOM   2363  CE2 TYR A 288      33.160   9.479  65.642  1.00 35.09           C  
ATOM   2364  CZ  TYR A 288      31.786   9.555  65.490  1.00 35.00           C  
ATOM   2365  OH  TYR A 288      30.978   9.668  66.605  1.00 34.29           O  
ATOM   2366  N   LYS A 289      36.225  11.603  62.379  1.00 32.39           N  
ATOM   2367  CA  LYS A 289      36.671  12.561  63.395  1.00 34.36           C  
ATOM   2368  C   LYS A 289      37.022  13.925  62.811  1.00 40.22           C  
ATOM   2369  O   LYS A 289      36.899  14.937  63.511  1.00 34.10           O  
ATOM   2370  CB  LYS A 289      37.879  12.008  64.156  1.00 29.62           C  
ATOM   2371  CG  LYS A 289      37.574  10.790  65.021  1.00 31.81           C  
ATOM   2372  CD  LYS A 289      36.676  11.148  66.210  1.00 33.49           C  
ATOM   2373  CE  LYS A 289      37.435  11.904  67.305  1.00 35.17           C  
ATOM   2374  NZ  LYS A 289      36.508  12.270  68.436  1.00 38.00           N  
ATOM   2375  N   TYR A 290      37.472  13.979  61.561  1.00 32.36           N  
ATOM   2376  CA  TYR A 290      37.805  15.241  60.912  1.00 32.04           C  
ATOM   2377  C   TYR A 290      36.597  15.811  60.175  1.00 30.43           C  
ATOM   2378  O   TYR A 290      35.670  15.090  59.808  1.00 36.80           O  
ATOM   2379  CB  TYR A 290      38.969  15.045  59.945  1.00 33.77           C  
ATOM   2380  CG  TYR A 290      40.283  14.818  60.649  1.00 32.51           C  
ATOM   2381  CD1 TYR A 290      40.644  13.553  61.102  1.00 32.63           C  
ATOM   2382  CD2 TYR A 290      41.160  15.872  60.879  1.00 28.38           C  
ATOM   2383  CE1 TYR A 290      41.827  13.344  61.741  1.00 33.52           C  
ATOM   2384  CE2 TYR A 290      42.354  15.670  61.537  1.00 31.82           C  
ATOM   2385  CZ  TYR A 290      42.684  14.409  61.960  1.00 34.78           C  
ATOM   2386  OH  TYR A 290      43.880  14.203  62.603  1.00 35.83           O  
ATOM   2387  N   THR A 291      36.608  17.130  59.973  1.00 32.94           N  
ATOM   2388  CA  THR A 291      35.521  17.745  59.232  1.00 32.01           C  
ATOM   2389  C   THR A 291      35.751  17.586  57.734  1.00 34.22           C  
ATOM   2390  O   THR A 291      36.874  17.391  57.267  1.00 33.80           O  
ATOM   2391  CB  THR A 291      35.376  19.233  59.565  1.00 32.04           C  
ATOM   2392  OG1 THR A 291      36.480  19.956  59.012  1.00 33.52           O  
ATOM   2393  CG2 THR A 291      35.318  19.445  61.106  1.00 33.27           C  
ATOM   2394  N   LEU A 292      34.654  17.661  56.979  1.00 33.82           N  
ATOM   2395  CA  LEU A 292      34.748  17.571  55.524  1.00 37.58           C  
ATOM   2396  C   LEU A 292      35.618  18.691  54.961  1.00 41.74           C  
ATOM   2397  O   LEU A 292      36.384  18.481  54.014  1.00 40.41           O  
ATOM   2398  CB  LEU A 292      33.344  17.599  54.912  1.00 34.00           C  
ATOM   2399  CG  LEU A 292      33.256  17.456  53.393  1.00 38.03           C  
ATOM   2400  CD1 LEU A 292      33.858  16.136  52.961  1.00 37.61           C  
ATOM   2401  CD2 LEU A 292      31.810  17.559  52.941  1.00 43.27           C  
ATOM   2402  N   LYS A 293      35.531  19.885  55.539  1.00 37.34           N  
ATOM   2403  CA  LYS A 293      36.381  20.945  55.010  1.00 42.70           C  
ATOM   2404  C   LYS A 293      37.856  20.675  55.296  1.00 38.65           C  
ATOM   2405  O   LYS A 293      38.717  20.933  54.447  1.00 37.14           O  
ATOM   2406  CB  LYS A 293      35.943  22.294  55.579  1.00 42.24           C  
ATOM   2407  CG  LYS A 293      34.567  22.727  55.135  1.00 66.43           C  
ATOM   2408  CD  LYS A 293      33.533  21.636  55.396  1.00 78.83           C  
ATOM   2409  CE  LYS A 293      33.438  21.319  56.875  1.00 43.63           C  
ATOM   2410  NZ  LYS A 293      32.318  20.381  57.174  1.00 45.64           N  
ATOM   2411  N   GLN A 294      38.198  20.051  56.422  1.00 34.35           N  
ATOM   2412  CA  GLN A 294      39.596  19.697  56.654  1.00 35.91           C  
ATOM   2413  C   GLN A 294      40.048  18.592  55.703  1.00 38.68           C  
ATOM   2414  O   GLN A 294      41.141  18.660  55.127  1.00 35.24           O  
ATOM   2415  CB  GLN A 294      39.801  19.280  58.115  1.00 34.34           C  
ATOM   2416  CG  GLN A 294      39.526  20.411  59.123  1.00 37.91           C  
ATOM   2417  CD  GLN A 294      39.185  19.897  60.526  1.00 40.77           C  
ATOM   2418  OE1 GLN A 294      39.222  18.691  60.785  1.00 34.28           O  
ATOM   2419  NE2 GLN A 294      38.842  20.817  61.432  1.00 31.82           N  
ATOM   2420  N   LEU A 295      39.223  17.554  55.534  1.00 34.55           N  
ATOM   2421  CA  LEU A 295      39.544  16.502  54.578  1.00 39.29           C  
ATOM   2422  C   LEU A 295      39.738  17.077  53.175  1.00 39.22           C  
ATOM   2423  O   LEU A 295      40.708  16.740  52.492  1.00 38.90           O  
ATOM   2424  CB  LEU A 295      38.446  15.436  54.589  1.00 37.74           C  
ATOM   2425  CG  LEU A 295      38.292  14.662  55.908  1.00 39.25           C  
ATOM   2426  CD1 LEU A 295      36.904  14.064  56.056  1.00 32.03           C  
ATOM   2427  CD2 LEU A 295      39.354  13.574  56.033  1.00 37.11           C  
ATOM   2428  N   GLU A 296      38.850  17.981  52.751  1.00 34.80           N  
ATOM   2429  CA  GLU A 296      38.956  18.550  51.411  1.00 37.28           C  
ATOM   2430  C   GLU A 296      40.212  19.407  51.259  1.00 44.98           C  
ATOM   2431  O   GLU A 296      40.896  19.328  50.230  1.00 39.40           O  
ATOM   2432  CB  GLU A 296      37.696  19.350  51.080  1.00 40.25           C  
ATOM   2433  CG  GLU A 296      36.512  18.451  50.761  1.00 44.48           C  
ATOM   2434  CD  GLU A 296      35.212  19.198  50.535  1.00 49.57           C  
ATOM   2435  OE1 GLU A 296      35.134  20.396  50.887  1.00 57.46           O  
ATOM   2436  OE2 GLU A 296      34.261  18.576  50.013  1.00 57.65           O  
ATOM   2437  N   MET A 297      40.549  20.215  52.272  1.00 36.97           N  
ATOM   2438  CA  MET A 297      41.718  21.079  52.137  1.00 35.42           C  
ATOM   2439  C   MET A 297      43.007  20.269  52.131  1.00 38.93           C  
ATOM   2440  O   MET A 297      43.920  20.541  51.335  1.00 36.76           O  
ATOM   2441  CB  MET A 297      41.743  22.132  53.247  1.00 39.78           C  
ATOM   2442  CG  MET A 297      42.784  23.221  52.989  1.00 54.05           C  
ATOM   2443  SD  MET A 297      42.625  24.752  53.957  1.00 48.00           S  
ATOM   2444  CE  MET A 297      40.967  25.228  53.521  1.00 37.91           C  
ATOM   2445  N   ALA A 298      43.111  19.282  53.023  1.00 35.14           N  
ATOM   2446  CA  ALA A 298      44.261  18.385  53.005  1.00 37.99           C  
ATOM   2447  C   ALA A 298      44.377  17.659  51.664  1.00 37.76           C  
ATOM   2448  O   ALA A 298      45.486  17.472  51.150  1.00 40.27           O  
ATOM   2449  CB  ALA A 298      44.168  17.376  54.152  1.00 39.51           C  
ATOM   2450  N   SER A 299      43.247  17.220  51.097  1.00 40.41           N  
ATOM   2451  CA  SER A 299      43.294  16.542  49.802  1.00 44.47           C  
ATOM   2452  C   SER A 299      43.756  17.488  48.711  1.00 45.38           C  
ATOM   2453  O   SER A 299      44.555  17.109  47.852  1.00 45.87           O  
ATOM   2454  CB  SER A 299      41.929  15.969  49.429  1.00 39.74           C  
ATOM   2455  OG  SER A 299      41.628  14.841  50.216  1.00 46.28           O  
ATOM   2456  N   ARG A 300      43.255  18.721  48.737  1.00 38.41           N  
ATOM   2457  CA  ARG A 300      43.608  19.699  47.725  1.00 38.55           C  
ATOM   2458  C   ARG A 300      45.103  19.964  47.710  1.00 42.87           C  
ATOM   2459  O   ARG A 300      45.710  20.074  46.638  1.00 43.44           O  
ATOM   2460  CB  ARG A 300      42.832  20.990  47.970  1.00 35.97           C  
ATOM   2461  CG  ARG A 300      43.026  22.023  46.900  1.00 37.51           C  
ATOM   2462  CD  ARG A 300      42.114  23.206  47.131  1.00 40.35           C  
ATOM   2463  NE  ARG A 300      42.115  24.070  45.964  1.00 38.45           N  
ATOM   2464  CZ  ARG A 300      41.229  23.971  44.976  1.00 52.39           C  
ATOM   2465  NH1 ARG A 300      40.264  23.060  45.037  1.00 41.37           N  
ATOM   2466  NH2 ARG A 300      41.313  24.780  43.931  1.00 42.77           N  
ATOM   2467  N   VAL A 301      45.718  20.071  48.886  1.00 40.04           N  
ATOM   2468  CA  VAL A 301      47.124  20.464  48.943  1.00 45.07           C  
ATOM   2469  C   VAL A 301      48.066  19.295  48.698  1.00 45.88           C  
ATOM   2470  O   VAL A 301      49.247  19.518  48.394  1.00 41.94           O  
ATOM   2471  CB  VAL A 301      47.465  21.129  50.288  1.00 46.78           C  
ATOM   2472  CG1 VAL A 301      47.809  20.074  51.330  1.00 37.93           C  
ATOM   2473  CG2 VAL A 301      48.613  22.137  50.113  1.00 38.63           C  
ATOM   2474  N   THR A 302      47.594  18.056  48.835  1.00 41.60           N  
ATOM   2475  CA  THR A 302      48.392  16.892  48.475  1.00 48.41           C  
ATOM   2476  C   THR A 302      48.087  16.389  47.070  1.00 52.22           C  
ATOM   2477  O   THR A 302      48.728  15.435  46.620  1.00 50.68           O  
ATOM   2478  CB  THR A 302      48.184  15.744  49.475  1.00 42.11           C  
ATOM   2479  OG1 THR A 302      46.803  15.371  49.487  1.00 45.59           O  
ATOM   2480  CG2 THR A 302      48.623  16.144  50.879  1.00 47.06           C  
ATOM   2481  N   GLY A 303      47.112  16.985  46.383  1.00 46.29           N  
ATOM   2482  CA  GLY A 303      46.817  16.637  45.007  1.00 52.65           C  
ATOM   2483  C   GLY A 303      45.873  15.469  44.800  1.00 64.93           C  
ATOM   2484  O   GLY A 303      45.759  14.989  43.667  1.00 67.70           O  
ATOM   2485  N   LYS A 304      45.199  14.990  45.845  1.00 59.26           N  
ATOM   2486  CA  LYS A 304      44.232  13.909  45.683  1.00 61.27           C  
ATOM   2487  C   LYS A 304      42.889  14.459  45.216  1.00 66.15           C  
ATOM   2488  O   LYS A 304      42.593  15.650  45.352  1.00 65.58           O  
ATOM   2489  CB  LYS A 304      44.049  13.137  46.986  1.00 62.92           C  
ATOM   2490  CG  LYS A 304      45.342  12.649  47.602  1.00 67.79           C  
ATOM   2491  CD  LYS A 304      46.260  12.048  46.561  1.00 64.56           C  
ATOM   2492  CE  LYS A 304      47.190  11.026  47.192  1.00 77.03           C  
ATOM   2493  NZ  LYS A 304      47.808  11.524  48.451  1.00 64.06           N  
ATOM   2494  N   LYS A 305      42.097  13.566  44.637  1.00 69.53           N  
ATOM   2495  CA  LYS A 305      40.801  13.920  44.089  1.00 75.77           C  
ATOM   2496  C   LYS A 305      39.644  13.009  44.461  1.00 78.31           C  
ATOM   2497  O   LYS A 305      38.726  12.844  43.721  1.00 83.63           O  
ATOM   2498  CB  LYS A 305      40.907  13.932  42.579  1.00 80.79           C  
ATOM   2499  CG  LYS A 305      42.044  14.754  42.061  1.00 82.90           C  
ATOM   2500  CD  LYS A 305      41.545  15.973  41.319  1.00 86.15           C  
ATOM   2501  CE  LYS A 305      42.719  16.640  40.645  1.00 83.56           C  
ATOM   2502  NZ  LYS A 305      43.907  16.691  41.524  1.00 74.93           N  
ATOM   2503  N   LYS A 306      39.676  12.428  45.623  1.00 70.28           N  
ATOM   2504  CA  LYS A 306      38.640  11.481  46.011  1.00 62.37           C  
ATOM   2505  C   LYS A 306      37.310  12.198  46.257  1.00 58.33           C  
ATOM   2506  O   LYS A 306      37.249  13.417  46.442  1.00 60.61           O  
ATOM   2507  CB  LYS A 306      39.066  10.705  47.262  1.00 67.83           C  
ATOM   2508  CG  LYS A 306      40.493  10.144  47.199  1.00 75.18           C  
ATOM   2509  CD  LYS A 306      41.171  10.086  48.582  1.00 72.57           C  
ATOM   2510  CE  LYS A 306      40.514   9.056  49.508  1.00 74.18           C  
ATOM   2511  NZ  LYS A 306      41.262   8.840  50.798  1.00 60.09           N  
ATOM   2512  N   ASP A 307      36.229  11.418  46.242  1.00 55.81           N  
ATOM   2513  CA  ASP A 307      34.901  11.918  46.599  1.00 64.08           C  
ATOM   2514  C   ASP A 307      34.770  11.831  48.118  1.00 58.56           C  
ATOM   2515  O   ASP A 307      34.183  10.903  48.682  1.00 51.01           O  
ATOM   2516  CB  ASP A 307      33.811  11.127  45.887  1.00 61.42           C  
ATOM   2517  CG  ASP A 307      32.413  11.665  46.164  1.00 70.17           C  
ATOM   2518  OD1 ASP A 307      32.274  12.683  46.888  1.00 63.55           O  
ATOM   2519  OD2 ASP A 307      31.445  11.064  45.648  1.00 78.73           O  
ATOM   2520  N   LEU A 308      35.347  12.829  48.789  1.00 51.16           N  
ATOM   2521  CA  LEU A 308      35.413  12.807  50.248  1.00 43.33           C  
ATOM   2522  C   LEU A 308      34.027  12.882  50.873  1.00 43.03           C  
ATOM   2523  O   LEU A 308      33.758  12.207  51.872  1.00 46.52           O  
ATOM   2524  CB  LEU A 308      36.295  13.956  50.733  1.00 41.38           C  
ATOM   2525  CG  LEU A 308      37.700  13.875  50.136  1.00 43.23           C  
ATOM   2526  CD1 LEU A 308      38.483  15.154  50.372  1.00 43.05           C  
ATOM   2527  CD2 LEU A 308      38.444  12.676  50.682  1.00 37.10           C  
ATOM   2528  N   ALA A 309      33.132  13.691  50.300  1.00 45.51           N  
ATOM   2529  CA  ALA A 309      31.808  13.860  50.892  1.00 50.77           C  
ATOM   2530  C   ALA A 309      31.046  12.544  50.938  1.00 53.48           C  
ATOM   2531  O   ALA A 309      30.338  12.265  51.915  1.00 46.48           O  
ATOM   2532  CB  ALA A 309      31.009  14.904  50.117  1.00 48.53           C  
ATOM   2533  N   ALA A 310      31.171  11.725  49.892  1.00 47.72           N  
ATOM   2534  CA  ALA A 310      30.416  10.480  49.841  1.00 42.38           C  
ATOM   2535  C   ALA A 310      30.928   9.485  50.871  1.00 42.90           C  
ATOM   2536  O   ALA A 310      30.138   8.775  51.504  1.00 44.41           O  
ATOM   2537  CB  ALA A 310      30.482   9.879  48.432  1.00 53.83           C  
ATOM   2538  N   ILE A 311      32.252   9.425  51.052  1.00 41.75           N  
ATOM   2539  CA  ILE A 311      32.841   8.520  52.035  1.00 40.50           C  
ATOM   2540  C   ILE A 311      32.374   8.888  53.440  1.00 39.09           C  
ATOM   2541  O   ILE A 311      31.947   8.027  54.217  1.00 39.10           O  
ATOM   2542  CB  ILE A 311      34.374   8.541  51.929  1.00 44.49           C  
ATOM   2543  CG1 ILE A 311      34.817   8.049  50.539  1.00 48.50           C  
ATOM   2544  CG2 ILE A 311      35.000   7.715  53.047  1.00 37.47           C  
ATOM   2545  CD1 ILE A 311      36.248   8.393  50.212  1.00 44.99           C  
ATOM   2546  N   LYS A 312      32.448  10.179  53.784  1.00 40.13           N  
ATOM   2547  CA  LYS A 312      32.020  10.615  55.111  1.00 42.15           C  
ATOM   2548  C   LYS A 312      30.530  10.370  55.306  1.00 40.17           C  
ATOM   2549  O   LYS A 312      30.092   9.944  56.381  1.00 41.08           O  
ATOM   2550  CB  LYS A 312      32.367  12.099  55.309  1.00 38.15           C  
ATOM   2551  CG  LYS A 312      32.194  12.615  56.760  1.00 35.15           C  
ATOM   2552  CD  LYS A 312      32.907  13.961  56.966  1.00 34.09           C  
ATOM   2553  CE  LYS A 312      32.597  14.588  58.337  1.00 33.23           C  
ATOM   2554  NZ  LYS A 312      33.178  13.854  59.512  1.00 29.99           N  
ATOM   2555  N   ARG A 313      29.740  10.611  54.259  1.00 40.19           N  
ATOM   2556  CA  ARG A 313      28.293  10.477  54.359  1.00 39.38           C  
ATOM   2557  C   ARG A 313      27.860   9.030  54.596  1.00 44.82           C  
ATOM   2558  O   ARG A 313      26.816   8.793  55.218  1.00 44.78           O  
ATOM   2559  CB  ARG A 313      27.658  11.047  53.091  1.00 44.50           C  
ATOM   2560  CG  ARG A 313      26.149  11.122  53.120  1.00 69.00           C  
ATOM   2561  CD  ARG A 313      25.605  11.839  51.882  1.00 75.93           C  
ATOM   2562  NE  ARG A 313      26.115  11.265  50.638  1.00 76.77           N  
ATOM   2563  CZ  ARG A 313      26.924  11.899  49.793  1.00 73.21           C  
ATOM   2564  NH1 ARG A 313      27.321  13.145  50.047  1.00 58.52           N  
ATOM   2565  NH2 ARG A 313      27.329  11.287  48.688  1.00 68.61           N  
ATOM   2566  N   GLN A 314      28.645   8.053  54.140  1.00 42.30           N  
ATOM   2567  CA  GLN A 314      28.247   6.650  54.213  1.00 41.75           C  
ATOM   2568  C   GLN A 314      28.821   5.923  55.431  1.00 46.53           C  
ATOM   2569  O   GLN A 314      28.800   4.686  55.478  1.00 42.36           O  
ATOM   2570  CB  GLN A 314      28.622   5.930  52.916  1.00 39.56           C  
ATOM   2571  CG  GLN A 314      27.815   6.454  51.723  1.00 55.21           C  
ATOM   2572  CD  GLN A 314      27.872   5.555  50.495  1.00 66.59           C  
ATOM   2573  OE1 GLN A 314      28.742   4.690  50.379  1.00 60.80           O  
ATOM   2574  NE2 GLN A 314      26.938   5.759  49.569  1.00 73.80           N  
ATOM   2575  N   LEU A 315      29.314   6.661  56.426  1.00 40.41           N  
ATOM   2576  CA  LEU A 315      29.680   6.055  57.692  1.00 37.91           C  
ATOM   2577  C   LEU A 315      28.412   5.659  58.446  1.00 35.28           C  
ATOM   2578  O   LEU A 315      27.342   6.214  58.204  1.00 39.56           O  
ATOM   2579  CB  LEU A 315      30.511   7.027  58.528  1.00 35.65           C  
ATOM   2580  CG  LEU A 315      31.834   7.485  57.900  1.00 40.61           C  
ATOM   2581  CD1 LEU A 315      32.458   8.665  58.666  1.00 37.59           C  
ATOM   2582  CD2 LEU A 315      32.819   6.325  57.820  1.00 39.36           C  
ATOM   2583  N   PRO A 316      28.506   4.701  59.371  1.00 37.72           N  
ATOM   2584  CA  PRO A 316      27.298   4.293  60.109  1.00 42.30           C  
ATOM   2585  C   PRO A 316      26.712   5.399  60.970  1.00 43.69           C  
ATOM   2586  O   PRO A 316      25.488   5.452  61.149  1.00 40.90           O  
ATOM   2587  CB  PRO A 316      27.792   3.113  60.958  1.00 40.99           C  
ATOM   2588  CG  PRO A 316      29.045   2.665  60.304  1.00 35.82           C  
ATOM   2589  CD  PRO A 316      29.675   3.902  59.754  1.00 34.99           C  
ATOM   2590  N   ILE A 317      27.548   6.291  61.506  1.00 38.85           N  
ATOM   2591  CA  ILE A 317      27.086   7.461  62.248  1.00 36.23           C  
ATOM   2592  C   ILE A 317      27.959   8.641  61.860  1.00 37.72           C  
ATOM   2593  O   ILE A 317      29.084   8.476  61.383  1.00 34.67           O  
ATOM   2594  CB  ILE A 317      27.129   7.248  63.773  1.00 38.84           C  
ATOM   2595  CG1 ILE A 317      28.551   6.903  64.230  1.00 36.68           C  
ATOM   2596  CG2 ILE A 317      26.133   6.167  64.179  1.00 40.61           C  
ATOM   2597  CD1 ILE A 317      28.726   6.910  65.752  1.00 40.85           C  
ATOM   2598  N   GLN A 318      27.423   9.848  62.064  1.00 38.60           N  
ATOM   2599  CA  GLN A 318      28.130  11.083  61.747  1.00 38.28           C  
ATOM   2600  C   GLN A 318      28.857  11.705  62.930  1.00 35.52           C  
ATOM   2601  O   GLN A 318      29.899  12.335  62.724  1.00 37.28           O  
ATOM   2602  CB  GLN A 318      27.161  12.121  61.165  1.00 38.05           C  
ATOM   2603  CG  GLN A 318      26.685  11.775  59.769  1.00 41.56           C  
ATOM   2604  CD  GLN A 318      27.846  11.482  58.840  1.00 39.77           C  
ATOM   2605  OE1 GLN A 318      28.741  12.309  58.672  1.00 45.80           O  
ATOM   2606  NE2 GLN A 318      27.845  10.295  58.242  1.00 39.28           N  
ATOM   2607  N   SER A 319      28.349  11.570  64.159  1.00 35.48           N  
ATOM   2608  CA  SER A 319      28.993  12.228  65.290  1.00 38.08           C  
ATOM   2609  C   SER A 319      28.572  11.579  66.605  1.00 34.69           C  
ATOM   2610  O   SER A 319      27.629  10.787  66.669  1.00 39.98           O  
ATOM   2611  CB  SER A 319      28.672  13.725  65.321  1.00 45.07           C  
ATOM   2612  OG  SER A 319      27.299  13.925  65.615  1.00 41.12           O  
ATOM   2613  N   ARG A 320      29.285  11.964  67.662  1.00 34.48           N  
ATOM   2614  CA  ARG A 320      29.126  11.380  68.991  1.00 38.27           C  
ATOM   2615  C   ARG A 320      27.687  11.440  69.496  1.00 39.84           C  
ATOM   2616  O   ARG A 320      27.239  10.534  70.209  1.00 35.44           O  
ATOM   2617  CB  ARG A 320      30.071  12.101  69.955  1.00 41.28           C  
ATOM   2618  CG  ARG A 320      29.845  11.845  71.453  1.00 41.84           C  
ATOM   2619  CD  ARG A 320      30.215  10.430  71.837  1.00 39.95           C  
ATOM   2620  NE  ARG A 320      31.639  10.135  71.655  1.00 39.38           N  
ATOM   2621  CZ  ARG A 320      32.558  10.289  72.608  1.00 39.27           C  
ATOM   2622  NH1 ARG A 320      32.204  10.767  73.804  1.00 40.49           N  
ATOM   2623  NH2 ARG A 320      33.826   9.976  72.378  1.00 33.38           N  
ATOM   2624  N   SER A 321      26.940  12.482  69.124  1.00 39.97           N  
ATOM   2625  CA  SER A 321      25.592  12.639  69.663  1.00 48.88           C  
ATOM   2626  C   SER A 321      24.646  11.537  69.209  1.00 49.05           C  
ATOM   2627  O   SER A 321      23.589  11.364  69.823  1.00 43.30           O  
ATOM   2628  CB  SER A 321      25.014  14.000  69.275  1.00 42.40           C  
ATOM   2629  OG  SER A 321      24.896  14.106  67.875  1.00 48.75           O  
ATOM   2630  N   GLU A 322      24.994  10.787  68.156  1.00 39.94           N  
ATOM   2631  CA  GLU A 322      24.183   9.647  67.736  1.00 38.34           C  
ATOM   2632  C   GLU A 322      24.500   8.368  68.498  1.00 35.68           C  
ATOM   2633  O   GLU A 322      23.758   7.388  68.364  1.00 38.72           O  
ATOM   2634  CB  GLU A 322      24.367   9.356  66.239  1.00 41.78           C  
ATOM   2635  CG  GLU A 322      23.936  10.449  65.293  1.00 40.59           C  
ATOM   2636  CD  GLU A 322      24.329  10.126  63.857  1.00 48.61           C  
ATOM   2637  OE1 GLU A 322      23.885   9.094  63.316  1.00 44.61           O  
ATOM   2638  OE2 GLU A 322      25.103  10.895  63.274  1.00 47.29           O  
ATOM   2639  N   LEU A 323      25.584   8.332  69.267  1.00 36.28           N  
ATOM   2640  CA  LEU A 323      25.954   7.103  69.963  1.00 43.20           C  
ATOM   2641  C   LEU A 323      24.842   6.662  70.911  1.00 53.76           C  
ATOM   2642  O   LEU A 323      24.280   7.477  71.652  1.00 36.61           O  
ATOM   2643  CB  LEU A 323      27.253   7.310  70.736  1.00 43.12           C  
ATOM   2644  CG  LEU A 323      28.120   6.077  70.969  1.00 47.23           C  
ATOM   2645  CD1 LEU A 323      28.504   5.475  69.631  1.00 49.95           C  
ATOM   2646  CD2 LEU A 323      29.355   6.463  71.749  1.00 43.81           C  
ATOM   2647  N   ALA A 324      24.536   5.366  70.901  1.00 40.25           N  
ATOM   2648  CA  ALA A 324      23.413   4.844  71.670  1.00 44.93           C  
ATOM   2649  C   ALA A 324      23.738   4.626  73.147  1.00 48.89           C  
ATOM   2650  O   ALA A 324      22.872   4.146  73.886  1.00 49.79           O  
ATOM   2651  CB  ALA A 324      22.922   3.530  71.048  1.00 40.06           C  
ATOM   2652  N   VAL A 325      24.942   4.979  73.600  1.00 38.21           N  
ATOM   2653  CA  VAL A 325      25.367   4.763  74.973  1.00 35.65           C  
ATOM   2654  C   VAL A 325      26.128   6.001  75.436  1.00 44.33           C  
ATOM   2655  O   VAL A 325      26.679   6.754  74.627  1.00 40.45           O  
ATOM   2656  CB  VAL A 325      26.244   3.493  75.085  1.00 40.79           C  
ATOM   2657  CG1 VAL A 325      27.514   3.672  74.279  1.00 41.81           C  
ATOM   2658  CG2 VAL A 325      26.576   3.187  76.497  1.00 47.90           C  
ATOM   2659  N   ASP A 326      26.149   6.218  76.758  1.00 41.57           N  
ATOM   2660  CA  ASP A 326      26.919   7.315  77.340  1.00 35.62           C  
ATOM   2661  C   ASP A 326      27.555   6.843  78.641  1.00 36.26           C  
ATOM   2662  O   ASP A 326      27.346   5.714  79.081  1.00 37.33           O  
ATOM   2663  CB  ASP A 326      26.050   8.574  77.517  1.00 44.98           C  
ATOM   2664  CG  ASP A 326      24.978   8.431  78.601  1.00 43.53           C  
ATOM   2665  OD1 ASP A 326      25.079   7.565  79.497  1.00 40.22           O  
ATOM   2666  OD2 ASP A 326      24.020   9.227  78.560  1.00 52.02           O  
ATOM   2667  N   GLY A 327      28.359   7.720  79.253  1.00 33.03           N  
ATOM   2668  CA  GLY A 327      29.103   7.338  80.438  1.00 31.92           C  
ATOM   2669  C   GLY A 327      28.232   6.812  81.561  1.00 29.93           C  
ATOM   2670  O   GLY A 327      28.659   5.954  82.329  1.00 34.96           O  
ATOM   2671  N   TRP A 328      27.003   7.299  81.673  1.00 35.87           N  
ATOM   2672  CA  TRP A 328      26.175   6.823  82.780  1.00 40.36           C  
ATOM   2673  C   TRP A 328      25.664   5.403  82.544  1.00 41.66           C  
ATOM   2674  O   TRP A 328      25.433   4.668  83.508  1.00 36.25           O  
ATOM   2675  CB  TRP A 328      25.037   7.810  83.040  1.00 39.92           C  
ATOM   2676  CG  TRP A 328      25.577   9.042  83.763  1.00 44.91           C  
ATOM   2677  CD1 TRP A 328      25.884   9.150  85.102  1.00 43.43           C  
ATOM   2678  CD2 TRP A 328      25.919  10.303  83.172  1.00 44.71           C  
ATOM   2679  NE1 TRP A 328      26.383  10.408  85.374  1.00 40.72           N  
ATOM   2680  CE2 TRP A 328      26.417  11.133  84.209  1.00 42.38           C  
ATOM   2681  CE3 TRP A 328      25.845  10.817  81.872  1.00 43.79           C  
ATOM   2682  CZ2 TRP A 328      26.834  12.448  83.979  1.00 42.50           C  
ATOM   2683  CZ3 TRP A 328      26.257  12.119  81.646  1.00 51.16           C  
ATOM   2684  CH2 TRP A 328      26.748  12.919  82.693  1.00 45.16           C  
ATOM   2685  N   ASP A 329      25.516   4.982  81.285  1.00 38.07           N  
ATOM   2686  CA  ASP A 329      25.287   3.563  81.024  1.00 37.72           C  
ATOM   2687  C   ASP A 329      26.460   2.723  81.511  1.00 35.93           C  
ATOM   2688  O   ASP A 329      26.269   1.685  82.158  1.00 38.69           O  
ATOM   2689  CB  ASP A 329      25.052   3.330  79.532  1.00 37.54           C  
ATOM   2690  CG  ASP A 329      23.832   4.049  79.016  1.00 41.70           C  
ATOM   2691  OD1 ASP A 329      22.749   3.924  79.635  1.00 44.81           O  
ATOM   2692  OD2 ASP A 329      23.954   4.747  77.991  1.00 41.22           O  
ATOM   2693  N   LEU A 330      27.689   3.168  81.234  1.00 31.92           N  
ATOM   2694  CA  LEU A 330      28.859   2.405  81.658  1.00 33.97           C  
ATOM   2695  C   LEU A 330      28.966   2.351  83.181  1.00 38.59           C  
ATOM   2696  O   LEU A 330      29.344   1.319  83.745  1.00 36.95           O  
ATOM   2697  CB  LEU A 330      30.131   3.003  81.054  1.00 34.34           C  
ATOM   2698  CG  LEU A 330      30.243   3.088  79.515  1.00 45.12           C  
ATOM   2699  CD1 LEU A 330      31.695   3.228  79.080  1.00 37.51           C  
ATOM   2700  CD2 LEU A 330      29.591   1.903  78.812  1.00 38.00           C  
ATOM   2701  N   ILE A 331      28.667   3.462  83.866  1.00 34.60           N  
ATOM   2702  CA  ILE A 331      28.661   3.444  85.332  1.00 32.39           C  
ATOM   2703  C   ILE A 331      27.710   2.363  85.847  1.00 33.59           C  
ATOM   2704  O   ILE A 331      28.071   1.561  86.719  1.00 40.33           O  
ATOM   2705  CB  ILE A 331      28.301   4.838  85.886  1.00 34.71           C  
ATOM   2706  CG1 ILE A 331      29.450   5.815  85.635  1.00 34.93           C  
ATOM   2707  CG2 ILE A 331      28.016   4.775  87.419  1.00 31.03           C  
ATOM   2708  CD1 ILE A 331      29.045   7.285  85.743  1.00 38.23           C  
ATOM   2709  N   GLU A 332      26.483   2.324  85.315  1.00 37.98           N  
ATOM   2710  CA  GLU A 332      25.507   1.313  85.730  1.00 43.15           C  
ATOM   2711  C   GLU A 332      26.032  -0.102  85.516  1.00 47.37           C  
ATOM   2712  O   GLU A 332      26.012  -0.936  86.431  1.00 42.07           O  
ATOM   2713  CB  GLU A 332      24.197   1.498  84.964  1.00 41.04           C  
ATOM   2714  CG  GLU A 332      23.381   2.668  85.442  1.00 71.67           C  
ATOM   2715  CD  GLU A 332      23.163   2.628  86.949  1.00 80.10           C  
ATOM   2716  OE1 GLU A 332      22.470   1.696  87.430  1.00 80.26           O  
ATOM   2717  OE2 GLU A 332      23.712   3.509  87.650  1.00 49.80           O  
ATOM   2718  N   TRP A 333      26.498  -0.389  84.299  1.00 41.05           N  
ATOM   2719  CA  TRP A 333      26.896  -1.747  83.939  1.00 42.05           C  
ATOM   2720  C   TRP A 333      28.144  -2.180  84.695  1.00 43.72           C  
ATOM   2721  O   TRP A 333      28.279  -3.350  85.069  1.00 47.47           O  
ATOM   2722  CB  TRP A 333      27.123  -1.819  82.431  1.00 43.57           C  
ATOM   2723  CG  TRP A 333      25.910  -1.450  81.634  1.00 38.50           C  
ATOM   2724  CD1 TRP A 333      24.613  -1.470  82.057  1.00 40.64           C  
ATOM   2725  CD2 TRP A 333      25.879  -1.002  80.274  1.00 38.33           C  
ATOM   2726  NE1 TRP A 333      23.778  -1.062  81.050  1.00 39.44           N  
ATOM   2727  CE2 TRP A 333      24.530  -0.775  79.940  1.00 38.84           C  
ATOM   2728  CE3 TRP A 333      26.862  -0.778  79.305  1.00 36.79           C  
ATOM   2729  CZ2 TRP A 333      24.135  -0.323  78.684  1.00 45.87           C  
ATOM   2730  CZ3 TRP A 333      26.467  -0.340  78.049  1.00 41.52           C  
ATOM   2731  CH2 TRP A 333      25.115  -0.116  77.749  1.00 43.70           C  
ATOM   2732  N   SER A 334      29.067  -1.251  84.934  1.00 37.17           N  
ATOM   2733  CA  SER A 334      30.312  -1.585  85.613  1.00 35.78           C  
ATOM   2734  C   SER A 334      30.164  -1.665  87.128  1.00 40.42           C  
ATOM   2735  O   SER A 334      30.921  -2.388  87.782  1.00 40.23           O  
ATOM   2736  CB  SER A 334      31.377  -0.541  85.286  1.00 44.17           C  
ATOM   2737  OG  SER A 334      30.992   0.723  85.822  1.00 41.89           O  
ATOM   2738  N   GLY A 335      29.241  -0.907  87.712  1.00 41.16           N  
ATOM   2739  CA  GLY A 335      29.285  -0.743  89.154  1.00 36.15           C  
ATOM   2740  C   GLY A 335      30.456   0.063  89.665  1.00 48.59           C  
ATOM   2741  O   GLY A 335      30.680   0.099  90.882  1.00 42.15           O  
ATOM   2742  N   ALA A 336      31.221   0.712  88.777  1.00 44.29           N  
ATOM   2743  CA  ALA A 336      32.331   1.574  89.169  1.00 38.73           C  
ATOM   2744  C   ALA A 336      31.901   3.037  89.136  1.00 39.82           C  
ATOM   2745  O   ALA A 336      31.006   3.420  88.378  1.00 38.96           O  
ATOM   2746  CB  ALA A 336      33.535   1.377  88.247  1.00 37.60           C  
ATOM   2747  N   LYS A 337      32.564   3.857  89.952  1.00 39.44           N  
ATOM   2748  CA  LYS A 337      32.233   5.276  90.029  1.00 41.42           C  
ATOM   2749  C   LYS A 337      32.741   6.035  88.811  1.00 37.37           C  
ATOM   2750  O   LYS A 337      33.751   5.670  88.201  1.00 37.25           O  
ATOM   2751  CB  LYS A 337      32.829   5.908  91.284  1.00 37.09           C  
ATOM   2752  CG  LYS A 337      32.396   5.253  92.593  1.00 35.63           C  
ATOM   2753  CD  LYS A 337      33.090   5.916  93.772  1.00 38.61           C  
ATOM   2754  CE  LYS A 337      32.589   5.350  95.108  1.00 39.78           C  
ATOM   2755  NZ  LYS A 337      33.314   5.952  96.242  1.00 39.52           N  
ATOM   2756  N   SER A 338      32.051   7.128  88.489  1.00 36.53           N  
ATOM   2757  CA  SER A 338      32.476   8.019  87.412  1.00 37.81           C  
ATOM   2758  C   SER A 338      33.950   8.381  87.548  1.00 35.77           C  
ATOM   2759  O   SER A 338      34.455   8.590  88.654  1.00 34.19           O  
ATOM   2760  CB  SER A 338      31.626   9.291  87.423  1.00 32.11           C  
ATOM   2761  OG  SER A 338      32.019  10.171  86.389  1.00 36.73           O  
ATOM   2762  N   GLY A 339      34.646   8.433  86.405  1.00 34.40           N  
ATOM   2763  CA  GLY A 339      36.050   8.784  86.351  1.00 34.72           C  
ATOM   2764  C   GLY A 339      36.518   8.930  84.913  1.00 33.22           C  
ATOM   2765  O   GLY A 339      35.763   8.679  83.977  1.00 32.63           O  
ATOM   2766  N   PRO A 340      37.766   9.358  84.708  1.00 34.50           N  
ATOM   2767  CA  PRO A 340      38.274   9.496  83.331  1.00 36.65           C  
ATOM   2768  C   PRO A 340      38.213   8.201  82.519  1.00 38.05           C  
ATOM   2769  O   PRO A 340      38.202   8.259  81.283  1.00 36.99           O  
ATOM   2770  CB  PRO A 340      39.722   9.968  83.538  1.00 38.96           C  
ATOM   2771  CG  PRO A 340      39.698  10.662  84.888  1.00 39.25           C  
ATOM   2772  CD  PRO A 340      38.695   9.906  85.716  1.00 36.20           C  
ATOM   2773  N   TRP A 341      38.144   7.036  83.173  1.00 40.27           N  
ATOM   2774  CA  TRP A 341      38.065   5.781  82.433  1.00 39.76           C  
ATOM   2775  C   TRP A 341      36.880   5.755  81.478  1.00 34.95           C  
ATOM   2776  O   TRP A 341      36.941   5.087  80.442  1.00 35.85           O  
ATOM   2777  CB  TRP A 341      37.993   4.603  83.408  1.00 35.62           C  
ATOM   2778  CG  TRP A 341      36.692   4.496  84.157  1.00 36.66           C  
ATOM   2779  CD1 TRP A 341      36.353   5.134  85.330  1.00 37.24           C  
ATOM   2780  CD2 TRP A 341      35.564   3.688  83.805  1.00 40.30           C  
ATOM   2781  NE1 TRP A 341      35.084   4.777  85.707  1.00 36.28           N  
ATOM   2782  CE2 TRP A 341      34.579   3.887  84.795  1.00 37.36           C  
ATOM   2783  CE3 TRP A 341      35.292   2.809  82.750  1.00 37.92           C  
ATOM   2784  CZ2 TRP A 341      33.344   3.245  84.762  1.00 42.12           C  
ATOM   2785  CZ3 TRP A 341      34.057   2.176  82.717  1.00 41.59           C  
ATOM   2786  CH2 TRP A 341      33.101   2.395  83.718  1.00 43.94           C  
ATOM   2787  N   LEU A 342      35.798   6.480  81.793  1.00 33.16           N  
ATOM   2788  CA  LEU A 342      34.617   6.470  80.931  1.00 37.76           C  
ATOM   2789  C   LEU A 342      34.943   6.943  79.518  1.00 37.03           C  
ATOM   2790  O   LEU A 342      34.409   6.410  78.541  1.00 33.36           O  
ATOM   2791  CB  LEU A 342      33.517   7.351  81.521  1.00 32.05           C  
ATOM   2792  CG  LEU A 342      32.961   6.890  82.870  1.00 35.32           C  
ATOM   2793  CD1 LEU A 342      32.007   7.948  83.407  1.00 29.62           C  
ATOM   2794  CD2 LEU A 342      32.241   5.561  82.702  1.00 35.49           C  
ATOM   2795  N   LYS A 343      35.777   7.974  79.394  1.00 34.26           N  
ATOM   2796  CA  LYS A 343      36.117   8.481  78.069  1.00 38.74           C  
ATOM   2797  C   LYS A 343      36.861   7.424  77.259  1.00 34.33           C  
ATOM   2798  O   LYS A 343      36.644   7.289  76.048  1.00 34.94           O  
ATOM   2799  CB  LYS A 343      36.958   9.752  78.199  1.00 37.88           C  
ATOM   2800  CG  LYS A 343      36.308  10.863  79.029  1.00 46.39           C  
ATOM   2801  CD  LYS A 343      37.222  12.101  79.106  1.00 54.54           C  
ATOM   2802  CE  LYS A 343      36.692  13.133  80.116  1.00 64.59           C  
ATOM   2803  NZ  LYS A 343      37.547  14.368  80.192  1.00 57.70           N  
ATOM   2804  N   VAL A 344      37.736   6.667  77.922  1.00 35.67           N  
ATOM   2805  CA  VAL A 344      38.500   5.617  77.253  1.00 36.33           C  
ATOM   2806  C   VAL A 344      37.563   4.559  76.688  1.00 44.18           C  
ATOM   2807  O   VAL A 344      37.687   4.148  75.527  1.00 36.20           O  
ATOM   2808  CB  VAL A 344      39.525   5.005  78.221  1.00 37.71           C  
ATOM   2809  CG1 VAL A 344      40.273   3.860  77.551  1.00 42.32           C  
ATOM   2810  CG2 VAL A 344      40.490   6.076  78.717  1.00 41.81           C  
ATOM   2811  N   TRP A 345      36.604   4.107  77.502  1.00 37.39           N  
ATOM   2812  CA  TRP A 345      35.699   3.038  77.093  1.00 37.13           C  
ATOM   2813  C   TRP A 345      34.631   3.517  76.118  1.00 37.67           C  
ATOM   2814  O   TRP A 345      34.244   2.776  75.211  1.00 35.11           O  
ATOM   2815  CB  TRP A 345      35.071   2.387  78.330  1.00 32.09           C  
ATOM   2816  CG  TRP A 345      36.010   1.421  78.929  1.00 37.98           C  
ATOM   2817  CD1 TRP A 345      37.046   1.695  79.775  1.00 41.38           C  
ATOM   2818  CD2 TRP A 345      36.066   0.013  78.664  1.00 39.78           C  
ATOM   2819  NE1 TRP A 345      37.728   0.534  80.075  1.00 45.36           N  
ATOM   2820  CE2 TRP A 345      37.144  -0.507  79.405  1.00 39.90           C  
ATOM   2821  CE3 TRP A 345      35.299  -0.855  77.884  1.00 42.08           C  
ATOM   2822  CZ2 TRP A 345      37.472  -1.860  79.390  1.00 50.64           C  
ATOM   2823  CZ3 TRP A 345      35.628  -2.194  77.867  1.00 43.05           C  
ATOM   2824  CH2 TRP A 345      36.703  -2.684  78.616  1.00 47.96           C  
ATOM   2825  N   ILE A 346      34.130   4.744  76.272  1.00 32.90           N  
ATOM   2826  CA  ILE A 346      33.227   5.264  75.254  1.00 31.11           C  
ATOM   2827  C   ILE A 346      33.919   5.307  73.891  1.00 32.51           C  
ATOM   2828  O   ILE A 346      33.300   5.035  72.857  1.00 31.19           O  
ATOM   2829  CB  ILE A 346      32.683   6.647  75.666  1.00 31.69           C  
ATOM   2830  CG1 ILE A 346      31.672   6.487  76.815  1.00 36.59           C  
ATOM   2831  CG2 ILE A 346      32.034   7.332  74.464  1.00 33.87           C  
ATOM   2832  CD1 ILE A 346      30.350   5.824  76.389  1.00 35.55           C  
ATOM   2833  N   GLU A 347      35.206   5.661  73.855  1.00 35.72           N  
ATOM   2834  CA  GLU A 347      35.859   5.729  72.551  1.00 33.19           C  
ATOM   2835  C   GLU A 347      36.085   4.337  71.962  1.00 31.28           C  
ATOM   2836  O   GLU A 347      36.003   4.165  70.740  1.00 35.22           O  
ATOM   2837  CB  GLU A 347      37.183   6.482  72.626  1.00 33.75           C  
ATOM   2838  CG  GLU A 347      37.874   6.530  71.248  1.00 38.21           C  
ATOM   2839  CD  GLU A 347      39.021   7.517  71.199  1.00 46.34           C  
ATOM   2840  OE1 GLU A 347      38.778   8.725  71.408  1.00 52.07           O  
ATOM   2841  OE2 GLU A 347      40.161   7.087  70.937  1.00 51.94           O  
ATOM   2842  N   LYS A 348      36.414   3.344  72.798  1.00 32.64           N  
ATOM   2843  CA  LYS A 348      36.483   1.967  72.300  1.00 37.37           C  
ATOM   2844  C   LYS A 348      35.199   1.599  71.573  1.00 40.91           C  
ATOM   2845  O   LYS A 348      35.217   1.087  70.445  1.00 33.76           O  
ATOM   2846  CB  LYS A 348      36.708   0.982  73.450  1.00 39.87           C  
ATOM   2847  CG  LYS A 348      38.093   0.902  74.046  1.00 42.32           C  
ATOM   2848  CD  LYS A 348      38.052  -0.116  75.209  1.00 49.10           C  
ATOM   2849  CE  LYS A 348      39.280  -0.050  76.123  1.00 53.92           C  
ATOM   2850  NZ  LYS A 348      40.526  -0.309  75.348  1.00 62.45           N  
ATOM   2851  N   ILE A 349      34.063   1.877  72.221  1.00 34.31           N  
ATOM   2852  CA  ILE A 349      32.752   1.553  71.666  1.00 33.14           C  
ATOM   2853  C   ILE A 349      32.489   2.363  70.406  1.00 37.87           C  
ATOM   2854  O   ILE A 349      32.024   1.832  69.391  1.00 36.49           O  
ATOM   2855  CB  ILE A 349      31.662   1.799  72.730  1.00 30.70           C  
ATOM   2856  CG1 ILE A 349      31.759   0.769  73.841  1.00 37.22           C  
ATOM   2857  CG2 ILE A 349      30.260   1.814  72.102  1.00 35.22           C  
ATOM   2858  CD1 ILE A 349      31.073   1.229  75.127  1.00 33.57           C  
ATOM   2859  N   GLU A 350      32.777   3.669  70.462  1.00 32.18           N  
ATOM   2860  CA  GLU A 350      32.553   4.527  69.308  1.00 31.66           C  
ATOM   2861  C   GLU A 350      33.321   4.018  68.088  1.00 32.16           C  
ATOM   2862  O   GLU A 350      32.800   4.021  66.973  1.00 33.18           O  
ATOM   2863  CB  GLU A 350      32.977   5.950  69.659  1.00 30.64           C  
ATOM   2864  CG  GLU A 350      32.552   7.020  68.687  1.00 31.74           C  
ATOM   2865  CD  GLU A 350      32.938   8.412  69.200  1.00 36.31           C  
ATOM   2866  OE1 GLU A 350      33.912   8.505  69.984  1.00 34.90           O  
ATOM   2867  OE2 GLU A 350      32.269   9.395  68.825  1.00 33.98           O  
ATOM   2868  N   ARG A 351      34.567   3.589  68.282  1.00 35.43           N  
ATOM   2869  CA  ARG A 351      35.355   3.076  67.167  1.00 33.76           C  
ATOM   2870  C   ARG A 351      34.696   1.847  66.551  1.00 37.45           C  
ATOM   2871  O   ARG A 351      34.604   1.726  65.323  1.00 34.02           O  
ATOM   2872  CB  ARG A 351      36.767   2.749  67.640  1.00 39.04           C  
ATOM   2873  CG  ARG A 351      37.663   3.951  67.815  1.00 32.44           C  
ATOM   2874  CD  ARG A 351      39.001   3.505  68.364  1.00 40.66           C  
ATOM   2875  NE  ARG A 351      39.861   4.646  68.641  1.00 48.33           N  
ATOM   2876  CZ  ARG A 351      40.730   5.144  67.768  1.00 56.16           C  
ATOM   2877  NH1 ARG A 351      40.853   4.587  66.563  1.00 43.09           N  
ATOM   2878  NH2 ARG A 351      41.467   6.197  68.107  1.00 47.14           N  
ATOM   2879  N   LEU A 352      34.233   0.922  67.394  1.00 34.34           N  
ATOM   2880  CA  LEU A 352      33.586  -0.288  66.898  1.00 35.21           C  
ATOM   2881  C   LEU A 352      32.311   0.028  66.137  1.00 44.83           C  
ATOM   2882  O   LEU A 352      31.979  -0.662  65.165  1.00 39.84           O  
ATOM   2883  CB  LEU A 352      33.315  -1.245  68.060  1.00 35.17           C  
ATOM   2884  CG  LEU A 352      34.605  -1.833  68.644  1.00 42.42           C  
ATOM   2885  CD1 LEU A 352      34.332  -2.629  69.903  1.00 38.90           C  
ATOM   2886  CD2 LEU A 352      35.326  -2.703  67.603  1.00 42.96           C  
ATOM   2887  N   ILE A 353      31.597   1.085  66.533  1.00 33.84           N  
ATOM   2888  CA  ILE A 353      30.405   1.475  65.793  1.00 32.38           C  
ATOM   2889  C   ILE A 353      30.781   2.144  64.474  1.00 36.19           C  
ATOM   2890  O   ILE A 353      30.143   1.906  63.446  1.00 37.97           O  
ATOM   2891  CB  ILE A 353      29.513   2.379  66.667  1.00 36.53           C  
ATOM   2892  CG1 ILE A 353      28.834   1.545  67.768  1.00 41.44           C  
ATOM   2893  CG2 ILE A 353      28.504   3.123  65.832  1.00 32.32           C  
ATOM   2894  CD1 ILE A 353      28.181   2.389  68.854  1.00 38.42           C  
ATOM   2895  N   VAL A 354      31.802   3.007  64.483  1.00 34.12           N  
ATOM   2896  CA  VAL A 354      32.182   3.722  63.267  1.00 33.73           C  
ATOM   2897  C   VAL A 354      32.764   2.769  62.223  1.00 34.02           C  
ATOM   2898  O   VAL A 354      32.587   2.978  61.020  1.00 34.21           O  
ATOM   2899  CB  VAL A 354      33.162   4.859  63.601  1.00 34.02           C  
ATOM   2900  CG1 VAL A 354      33.850   5.374  62.342  1.00 32.42           C  
ATOM   2901  CG2 VAL A 354      32.424   6.000  64.326  1.00 33.54           C  
ATOM   2902  N   TYR A 355      33.465   1.731  62.653  1.00 37.81           N  
ATOM   2903  CA  TYR A 355      33.949   0.704  61.739  1.00 41.94           C  
ATOM   2904  C   TYR A 355      32.867  -0.298  61.339  1.00 45.98           C  
ATOM   2905  O   TYR A 355      33.161  -1.243  60.598  1.00 46.31           O  
ATOM   2906  CB  TYR A 355      35.128  -0.032  62.372  1.00 33.73           C  
ATOM   2907  CG  TYR A 355      36.416   0.757  62.386  1.00 35.48           C  
ATOM   2908  CD1 TYR A 355      37.041   1.131  61.198  1.00 42.76           C  
ATOM   2909  CD2 TYR A 355      37.026   1.101  63.577  1.00 39.20           C  
ATOM   2910  CE1 TYR A 355      38.226   1.845  61.210  1.00 38.29           C  
ATOM   2911  CE2 TYR A 355      38.214   1.812  63.601  1.00 37.01           C  
ATOM   2912  CZ  TYR A 355      38.807   2.183  62.413  1.00 39.09           C  
ATOM   2913  OH  TYR A 355      39.988   2.886  62.448  1.00 41.93           O  
ATOM   2914  N   GLY A 356      31.632  -0.123  61.800  1.00 35.95           N  
ATOM   2915  CA  GLY A 356      30.570  -1.037  61.427  1.00 36.42           C  
ATOM   2916  C   GLY A 356      30.721  -2.435  61.975  1.00 38.69           C  
ATOM   2917  O   GLY A 356      30.155  -3.372  61.411  1.00 40.94           O  
ATOM   2918  N   ILE A 357      31.463  -2.605  63.067  1.00 33.84           N  
ATOM   2919  CA  ILE A 357      31.608  -3.912  63.701  1.00 36.71           C  
ATOM   2920  C   ILE A 357      30.549  -4.131  64.781  1.00 48.84           C  
ATOM   2921  O   ILE A 357      29.952  -5.209  64.864  1.00 42.39           O  
ATOM   2922  CB  ILE A 357      33.032  -4.053  64.262  1.00 38.60           C  
ATOM   2923  CG1 ILE A 357      34.044  -4.159  63.107  1.00 39.59           C  
ATOM   2924  CG2 ILE A 357      33.127  -5.231  65.237  1.00 37.63           C  
ATOM   2925  CD1 ILE A 357      35.480  -3.988  63.541  1.00 42.89           C  
ATOM   2926  N   LEU A 358      30.297  -3.128  65.616  1.00 39.89           N  
ATOM   2927  CA  LEU A 358      29.329  -3.207  66.707  1.00 37.95           C  
ATOM   2928  C   LEU A 358      28.111  -2.372  66.341  1.00 36.89           C  
ATOM   2929  O   LEU A 358      28.251  -1.252  65.831  1.00 43.17           O  
ATOM   2930  CB  LEU A 358      29.967  -2.713  68.009  1.00 49.06           C  
ATOM   2931  CG  LEU A 358      29.185  -2.605  69.316  1.00 43.62           C  
ATOM   2932  CD1 LEU A 358      28.627  -3.954  69.733  1.00 40.13           C  
ATOM   2933  CD2 LEU A 358      30.135  -2.062  70.373  1.00 45.10           C  
ATOM   2934  N   LYS A 359      26.921  -2.922  66.549  1.00 33.92           N  
ATOM   2935  CA  LYS A 359      25.723  -2.179  66.188  1.00 38.96           C  
ATOM   2936  C   LYS A 359      25.491  -1.049  67.189  1.00 37.79           C  
ATOM   2937  O   LYS A 359      25.763  -1.197  68.385  1.00 37.88           O  
ATOM   2938  CB  LYS A 359      24.504  -3.102  66.146  1.00 38.84           C  
ATOM   2939  CG  LYS A 359      23.297  -2.483  65.479  1.00 42.49           C  
ATOM   2940  CD  LYS A 359      22.145  -3.481  65.431  1.00 47.62           C  
ATOM   2941  CE  LYS A 359      20.936  -2.897  64.731  1.00 54.39           C  
ATOM   2942  NZ  LYS A 359      19.822  -3.892  64.671  1.00 58.86           N  
ATOM   2943  N   ASN A 360      25.007   0.089  66.688  1.00 37.77           N  
ATOM   2944  CA  ASN A 360      24.731   1.253  67.534  1.00 47.87           C  
ATOM   2945  C   ASN A 360      23.393   1.028  68.239  1.00 37.11           C  
ATOM   2946  O   ASN A 360      22.368   1.637  67.930  1.00 38.64           O  
ATOM   2947  CB  ASN A 360      24.726   2.534  66.710  1.00 40.08           C  
ATOM   2948  CG  ASN A 360      24.692   3.787  67.583  1.00 38.35           C  
ATOM   2949  OD1 ASN A 360      25.201   3.783  68.698  1.00 38.68           O  
ATOM   2950  ND2 ASN A 360      24.102   4.857  67.072  1.00 36.61           N  
ATOM   2951  N   ASP A 361      23.414   0.105  69.194  1.00 41.56           N  
ATOM   2952  CA  ASP A 361      22.213  -0.350  69.888  1.00 49.62           C  
ATOM   2953  C   ASP A 361      22.554  -0.592  71.347  1.00 41.04           C  
ATOM   2954  O   ASP A 361      23.497  -1.328  71.653  1.00 38.68           O  
ATOM   2955  CB  ASP A 361      21.653  -1.632  69.248  1.00 46.80           C  
ATOM   2956  CG  ASP A 361      20.557  -2.269  70.085  1.00 43.68           C  
ATOM   2957  OD1 ASP A 361      20.873  -3.065  70.993  1.00 50.63           O  
ATOM   2958  OD2 ASP A 361      19.375  -1.944  69.848  1.00 57.13           O  
ATOM   2959  N   LYS A 362      21.797   0.031  72.252  1.00 44.04           N  
ATOM   2960  CA  LYS A 362      22.203   0.031  73.656  1.00 36.88           C  
ATOM   2961  C   LYS A 362      22.349  -1.389  74.193  1.00 39.36           C  
ATOM   2962  O   LYS A 362      23.343  -1.718  74.853  1.00 39.32           O  
ATOM   2963  CB  LYS A 362      21.205   0.823  74.501  1.00 43.51           C  
ATOM   2964  CG  LYS A 362      21.567   0.820  75.975  1.00 46.35           C  
ATOM   2965  CD  LYS A 362      20.681   1.761  76.790  1.00 51.45           C  
ATOM   2966  CE  LYS A 362      21.059   3.216  76.560  1.00 55.02           C  
ATOM   2967  NZ  LYS A 362      20.626   4.053  77.728  1.00 72.74           N  
ATOM   2968  N   GLU A 363      21.362  -2.248  73.925  1.00 41.71           N  
ATOM   2969  CA  GLU A 363      21.392  -3.597  74.488  1.00 43.34           C  
ATOM   2970  C   GLU A 363      22.558  -4.407  73.933  1.00 38.61           C  
ATOM   2971  O   GLU A 363      23.204  -5.164  74.668  1.00 44.00           O  
ATOM   2972  CB  GLU A 363      20.060  -4.298  74.217  1.00 57.31           C  
ATOM   2973  CG  GLU A 363      19.809  -5.512  75.099  1.00 75.69           C  
ATOM   2974  CD  GLU A 363      19.895  -5.183  76.585  1.00 78.47           C  
ATOM   2975  OE1 GLU A 363      20.397  -6.034  77.356  1.00 69.95           O  
ATOM   2976  OE2 GLU A 363      19.468  -4.072  76.979  1.00 63.35           O  
ATOM   2977  N   LEU A 364      22.855  -4.254  72.638  1.00 44.08           N  
ATOM   2978  CA  LEU A 364      23.987  -4.977  72.064  1.00 40.55           C  
ATOM   2979  C   LEU A 364      25.312  -4.414  72.558  1.00 40.97           C  
ATOM   2980  O   LEU A 364      26.264  -5.166  72.787  1.00 36.36           O  
ATOM   2981  CB  LEU A 364      23.913  -4.944  70.540  1.00 42.59           C  
ATOM   2982  CG  LEU A 364      22.750  -5.786  70.027  1.00 48.11           C  
ATOM   2983  CD1 LEU A 364      22.534  -5.556  68.542  1.00 49.08           C  
ATOM   2984  CD2 LEU A 364      23.039  -7.250  70.320  1.00 44.74           C  
ATOM   2985  N   ILE A 365      25.393  -3.091  72.745  1.00 40.56           N  
ATOM   2986  CA  ILE A 365      26.597  -2.514  73.343  1.00 40.25           C  
ATOM   2987  C   ILE A 365      26.783  -3.018  74.771  1.00 37.94           C  
ATOM   2988  O   ILE A 365      27.908  -3.305  75.207  1.00 40.47           O  
ATOM   2989  CB  ILE A 365      26.540  -0.974  73.286  1.00 37.63           C  
ATOM   2990  CG1 ILE A 365      26.534  -0.493  71.830  1.00 38.67           C  
ATOM   2991  CG2 ILE A 365      27.710  -0.382  74.059  1.00 36.46           C  
ATOM   2992  CD1 ILE A 365      26.055   0.939  71.654  1.00 39.94           C  
ATOM   2993  N   LYS A 366      25.687  -3.122  75.529  1.00 41.61           N  
ATOM   2994  CA  LYS A 366      25.756  -3.664  76.888  1.00 43.19           C  
ATOM   2995  C   LYS A 366      26.383  -5.055  76.885  1.00 39.74           C  
ATOM   2996  O   LYS A 366      27.296  -5.346  77.669  1.00 41.41           O  
ATOM   2997  CB  LYS A 366      24.346  -3.700  77.494  1.00 40.92           C  
ATOM   2998  CG  LYS A 366      24.268  -4.078  78.980  1.00 48.03           C  
ATOM   2999  CD  LYS A 366      22.797  -4.217  79.387  1.00 47.16           C  
ATOM   3000  CE  LYS A 366      22.610  -4.334  80.896  1.00 52.11           C  
ATOM   3001  NZ  LYS A 366      23.355  -5.486  81.472  1.00 56.94           N  
ATOM   3002  N   ASP A 367      25.900  -5.926  75.993  1.00 47.56           N  
ATOM   3003  CA  ASP A 367      26.462  -7.265  75.855  1.00 48.35           C  
ATOM   3004  C   ASP A 367      27.960  -7.204  75.584  1.00 47.65           C  
ATOM   3005  O   ASP A 367      28.754  -7.863  76.264  1.00 48.21           O  
ATOM   3006  CB  ASP A 367      25.744  -8.017  74.731  1.00 49.48           C  
ATOM   3007  CG  ASP A 367      24.282  -8.272  75.039  1.00 57.44           C  
ATOM   3008  OD1 ASP A 367      23.915  -8.349  76.234  1.00 65.24           O  
ATOM   3009  OD2 ASP A 367      23.493  -8.397  74.079  1.00 71.80           O  
ATOM   3010  N   TRP A 368      28.364  -6.409  74.593  1.00 43.13           N  
ATOM   3011  CA  TRP A 368      29.786  -6.252  74.316  1.00 44.74           C  
ATOM   3012  C   TRP A 368      30.539  -5.795  75.561  1.00 48.55           C  
ATOM   3013  O   TRP A 368      31.584  -6.356  75.914  1.00 43.83           O  
ATOM   3014  CB  TRP A 368      29.994  -5.260  73.165  1.00 42.48           C  
ATOM   3015  CG  TRP A 368      31.447  -5.043  72.863  1.00 46.27           C  
ATOM   3016  CD1 TRP A 368      32.214  -5.741  71.975  1.00 48.61           C  
ATOM   3017  CD2 TRP A 368      32.321  -4.082  73.478  1.00 48.10           C  
ATOM   3018  NE1 TRP A 368      33.508  -5.273  71.996  1.00 46.67           N  
ATOM   3019  CE2 TRP A 368      33.599  -4.257  72.910  1.00 44.70           C  
ATOM   3020  CE3 TRP A 368      32.143  -3.090  74.454  1.00 48.14           C  
ATOM   3021  CZ2 TRP A 368      34.696  -3.479  73.279  1.00 51.12           C  
ATOM   3022  CZ3 TRP A 368      33.238  -2.319  74.825  1.00 40.26           C  
ATOM   3023  CH2 TRP A 368      34.496  -2.518  74.238  1.00 52.55           C  
ATOM   3024  N   PHE A 369      30.018  -4.771  76.245  1.00 48.95           N  
ATOM   3025  CA  PHE A 369      30.744  -4.196  77.376  1.00 39.50           C  
ATOM   3026  C   PHE A 369      30.877  -5.199  78.518  1.00 43.97           C  
ATOM   3027  O   PHE A 369      31.953  -5.347  79.110  1.00 45.38           O  
ATOM   3028  CB  PHE A 369      30.049  -2.914  77.857  1.00 38.31           C  
ATOM   3029  CG  PHE A 369      30.705  -2.288  79.056  1.00 40.08           C  
ATOM   3030  CD1 PHE A 369      31.857  -1.525  78.917  1.00 33.56           C  
ATOM   3031  CD2 PHE A 369      30.172  -2.467  80.326  1.00 42.51           C  
ATOM   3032  CE1 PHE A 369      32.466  -0.948  80.020  1.00 40.30           C  
ATOM   3033  CE2 PHE A 369      30.779  -1.889  81.447  1.00 45.60           C  
ATOM   3034  CZ  PHE A 369      31.925  -1.132  81.294  1.00 39.76           C  
ATOM   3035  N   GLU A 370      29.791  -5.889  78.858  1.00 49.34           N  
ATOM   3036  CA  GLU A 370      29.876  -6.839  79.965  1.00 50.97           C  
ATOM   3037  C   GLU A 370      30.861  -7.958  79.657  1.00 59.91           C  
ATOM   3038  O   GLU A 370      31.549  -8.451  80.560  1.00 59.71           O  
ATOM   3039  CB  GLU A 370      28.489  -7.390  80.286  1.00 48.76           C  
ATOM   3040  CG  GLU A 370      27.664  -6.410  81.109  1.00 59.09           C  
ATOM   3041  CD  GLU A 370      26.218  -6.832  81.261  1.00 72.30           C  
ATOM   3042  OE1 GLU A 370      25.801  -7.816  80.605  1.00 70.77           O  
ATOM   3043  OE2 GLU A 370      25.496  -6.165  82.036  1.00 72.74           O  
ATOM   3044  N   ASP A 371      30.968  -8.344  78.385  1.00 53.48           N  
ATOM   3045  CA  ASP A 371      31.954  -9.343  77.987  1.00 57.90           C  
ATOM   3046  C   ASP A 371      33.372  -8.777  78.017  1.00 59.96           C  
ATOM   3047  O   ASP A 371      34.312  -9.460  78.442  1.00 55.00           O  
ATOM   3048  CB  ASP A 371      31.611  -9.869  76.595  1.00 65.45           C  
ATOM   3049  CG  ASP A 371      32.635 -10.853  76.084  1.00 74.88           C  
ATOM   3050  OD1 ASP A 371      32.665 -11.992  76.601  1.00 88.50           O  
ATOM   3051  OD2 ASP A 371      33.416 -10.490  75.179  1.00 80.61           O  
ATOM   3052  N   GLU A 372      33.552  -7.531  77.575  1.00 53.24           N  
ATOM   3053  CA  GLU A 372      34.898  -6.979  77.468  1.00 42.81           C  
ATOM   3054  C   GLU A 372      35.412  -6.440  78.794  1.00 50.09           C  
ATOM   3055  O   GLU A 372      36.624  -6.464  79.039  1.00 49.09           O  
ATOM   3056  CB  GLU A 372      34.930  -5.870  76.419  1.00 49.80           C  
ATOM   3057  CG  GLU A 372      36.319  -5.526  75.947  1.00 59.31           C  
ATOM   3058  CD  GLU A 372      36.832  -6.503  74.900  1.00 68.97           C  
ATOM   3059  OE1 GLU A 372      36.102  -7.465  74.562  1.00 68.77           O  
ATOM   3060  OE2 GLU A 372      37.964  -6.302  74.412  1.00 73.54           O  
ATOM   3061  N   TYR A 373      34.528  -5.940  79.646  1.00 55.02           N  
ATOM   3062  CA  TYR A 373      34.944  -5.277  80.876  1.00 56.09           C  
ATOM   3063  C   TYR A 373      35.143  -6.271  82.019  1.00 50.36           C  
ATOM   3064  O   TYR A 373      36.156  -6.229  82.718  1.00 57.30           O  
ATOM   3065  CB  TYR A 373      33.910  -4.211  81.258  1.00 53.36           C  
ATOM   3066  CG  TYR A 373      34.260  -3.394  82.480  1.00 51.38           C  
ATOM   3067  CD1 TYR A 373      35.061  -2.261  82.380  1.00 51.18           C  
ATOM   3068  CD2 TYR A 373      33.775  -3.746  83.733  1.00 54.72           C  
ATOM   3069  CE1 TYR A 373      35.375  -1.511  83.495  1.00 53.91           C  
ATOM   3070  CE2 TYR A 373      34.084  -3.002  84.857  1.00 50.35           C  
ATOM   3071  CZ  TYR A 373      34.884  -1.892  84.729  1.00 53.82           C  
ATOM   3072  OH  TYR A 373      35.186  -1.160  85.841  1.00 50.10           O  
TER    3073      TYR A 373                                                      
HETATM 3074  N1  CTP A 501      42.837  54.768  49.669  0.76 33.72           N  
HETATM 3075  C2  CTP A 501      44.100  55.289  49.897  0.76 33.22           C  
HETATM 3076  N3  CTP A 501      44.978  54.658  50.767  0.76 30.92           N  
HETATM 3077  C4  CTP A 501      44.609  53.448  51.326  0.76 44.51           C  
HETATM 3078  C5  CTP A 501      43.320  52.946  51.110  0.76 35.94           C  
HETATM 3079  C6  CTP A 501      42.399  53.700  50.399  0.76 33.55           C  
HETATM 3080  O2  CTP A 501      44.415  56.324  49.310  0.76 31.33           O  
HETATM 3081  N4  CTP A 501      45.461  52.764  52.088  0.76 46.05           N  
HETATM 3082  C1' CTP A 501      41.867  55.602  48.942  0.76 30.45           C  
HETATM 3083  C2' CTP A 501      41.945  55.271  47.460  0.76 30.29           C  
HETATM 3084  O2' CTP A 501      41.450  56.375  46.732  0.76 30.33           O  
HETATM 3085  C3' CTP A 501      40.912  54.178  47.340  0.76 36.58           C  
HETATM 3086  C4' CTP A 501      39.827  54.735  48.247  0.76 36.94           C  
HETATM 3087  O4' CTP A 501      40.544  55.277  49.348  0.76 33.33           O  
HETATM 3088  O3' CTP A 501      40.443  54.033  46.024  0.76 38.60           O  
HETATM 3089  C5' CTP A 501      38.830  53.658  48.659  0.76 41.91           C  
HETATM 3090  O5' CTP A 501      39.503  52.698  49.444  0.76 54.52           O  
HETATM 3091  PA  CTP A 501      38.982  51.177  49.544  0.76 51.14           P  
HETATM 3092  O1A CTP A 501      40.026  50.309  50.222  0.76 45.38           O  
HETATM 3093  O2A CTP A 501      37.701  51.168  50.348  0.76 47.99           O1-
HETATM 3094  O3A CTP A 501      38.561  50.814  48.021  0.76 53.67           O  
HETATM 3095  PB  CTP A 501      39.520  50.311  46.818  0.76 51.65           P  
HETATM 3096  O1B CTP A 501      38.737  50.035  45.567  0.76 58.63           O  
HETATM 3097  O2B CTP A 501      40.598  51.321  46.539  0.76 50.89           O1-
HETATM 3098  O3B CTP A 501      40.021  48.891  47.376  0.76 63.15           O  
HETATM 3099  PG  CTP A 501      39.096  47.635  46.947  0.76 64.01           P  
HETATM 3100  O1G CTP A 501      39.128  47.427  45.450  0.76 46.44           O1-
HETATM 3101  O2G CTP A 501      37.660  47.938  47.328  0.76 71.61           O1-
HETATM 3102  O3G CTP A 501      39.537  46.408  47.708  0.76 56.45           O  
HETATM 3103  C1  GOL A 502      40.286  14.665  64.922  1.00 34.36           C  
HETATM 3104  O1  GOL A 502      39.916  13.987  66.091  1.00 32.03           O  
HETATM 3105  C2  GOL A 502      41.326  15.742  65.249  1.00 39.59           C  
HETATM 3106  O2  GOL A 502      40.844  16.660  66.202  1.00 36.57           O  
HETATM 3107  C3  GOL A 502      42.609  15.127  65.807  1.00 36.77           C  
HETATM 3108  O3  GOL A 502      43.573  16.134  66.019  1.00 37.17           O  
HETATM 3109  C1  GOL A 503      34.109  15.734  64.686  0.78 41.77           C  
HETATM 3110  O1  GOL A 503      33.811  16.997  65.217  0.78 59.68           O  
HETATM 3111  C2  GOL A 503      33.176  15.492  63.499  0.78 58.04           C  
HETATM 3112  O2  GOL A 503      31.903  15.950  63.871  0.78 44.01           O  
HETATM 3113  C3  GOL A 503      33.669  16.196  62.237  0.78 35.26           C  
HETATM 3114  O3  GOL A 503      32.624  16.249  61.303  0.78 34.05           O  
HETATM 3115  C   ACT A 504      38.739  24.185  42.101  1.00 75.26           C  
HETATM 3116  O   ACT A 504      39.489  24.747  41.258  1.00 79.49           O  
HETATM 3117  OXT ACT A 504      37.999  24.877  42.856  1.00 77.33           O1-
HETATM 3118  CH3 ACT A 504      38.732  22.660  42.206  1.00 57.24           C  
HETATM 3119  C   ACT A 505      40.755  20.082  70.342  1.00 73.02           C  
HETATM 3120  O   ACT A 505      39.956  19.105  70.262  1.00 71.88           O1-
HETATM 3121  OXT ACT A 505      40.442  21.098  71.019  1.00 73.15           O  
HETATM 3122  CH3 ACT A 505      42.098  20.033  69.614  1.00 49.29           C  
HETATM 3123  C   ACT A 506      39.779  -2.136  61.919  1.00 67.23           C  
HETATM 3124  O   ACT A 506      39.764  -1.629  60.776  1.00 59.33           O1-
HETATM 3125  OXT ACT A 506      39.156  -3.186  62.186  1.00 71.05           O  
HETATM 3126  CH3 ACT A 506      40.569  -1.463  63.003  1.00 57.48           C  
HETATM 3127  P   PO4 A 507      38.230  18.274  64.158  1.00 36.60           P  
HETATM 3128  O1  PO4 A 507      39.365  17.871  63.218  1.00 36.99           O  
HETATM 3129  O2  PO4 A 507      36.991  17.549  63.695  1.00 35.68           O  
HETATM 3130  O3  PO4 A 507      37.979  19.769  64.020  1.00 35.62           O  
HETATM 3131  O4  PO4 A 507      38.585  17.873  65.563  1.00 35.30           O  
HETATM 3132  O   HOH A 601      32.110  18.307  58.104  1.00 40.42           O  
HETATM 3133  O   HOH A 602      57.411  24.747  61.740  1.00 43.33           O  
HETATM 3134  O   HOH A 603      25.409  13.479  64.205  1.00 42.27           O  
HETATM 3135  O   HOH A 604      43.688  23.935  66.495  1.00 49.51           O  
HETATM 3136  O   HOH A 605      52.782  63.622  53.079  1.00 45.12           O  
HETATM 3137  O   HOH A 606      49.401  25.593  67.932  1.00 51.52           O  
HETATM 3138  O   HOH A 607      38.131  10.255  73.271  1.00 47.75           O  
HETATM 3139  O   HOH A 608      31.724  18.550  60.887  1.00 44.03           O  
HETATM 3140  O   HOH A 609      60.842  62.065  47.655  1.00 56.44           O  
HETATM 3141  O   HOH A 610      30.526   3.184  51.334  1.00 51.06           O  
HETATM 3142  O   HOH A 611      35.677  20.820  64.289  1.00 44.49           O  
HETATM 3143  O   HOH A 612      40.218  47.808  49.784  1.00 55.68           O  
HETATM 3144  O   HOH A 613      30.372  17.035  65.606  1.00 45.89           O  
HETATM 3145  O   HOH A 614      40.947  38.657  55.653  1.00 55.09           O  
HETATM 3146  O   HOH A 615      37.535  25.838  62.042  1.00 49.57           O  
HETATM 3147  O   HOH A 616      43.202  62.408  32.167  1.00 53.87           O  
HETATM 3148  O   HOH A 617      47.808  53.922  38.864  1.00 29.41           O  
HETATM 3149  O   HOH A 618      48.975  20.495  62.421  1.00 46.65           O  
HETATM 3150  O   HOH A 619      37.410  32.923  61.265  1.00 60.18           O  
HETATM 3151  O   HOH A 620      42.523  45.009  53.112  1.00 44.60           O  
HETATM 3152  O   HOH A 621      24.985  48.898  49.158  1.00 51.65           O  
HETATM 3153  O   HOH A 622      36.301  22.530  59.303  1.00 42.87           O  
HETATM 3154  O   HOH A 623      25.302  -0.401  88.876  1.00 48.34           O  
HETATM 3155  O   HOH A 624      20.639  62.758  39.087  1.00 52.30           O  
HETATM 3156  O   HOH A 625      34.222  54.180  45.074  1.00 32.46           O  
HETATM 3157  O   HOH A 626      42.570  29.813  48.260  1.00 32.90           O  
HETATM 3158  O   HOH A 627      38.840  43.912  47.379  1.00 60.20           O  
HETATM 3159  O   HOH A 628      36.007   4.645  89.030  1.00 44.33           O  
HETATM 3160  O   HOH A 629      30.604  64.864  52.977  1.00 39.49           O  
HETATM 3161  O   HOH A 630      58.301  54.717  36.313  1.00 34.64           O  
HETATM 3162  O   HOH A 631      44.926  19.922  44.142  1.00 50.41           O  
HETATM 3163  O   HOH A 632      40.680  34.366  41.756  1.00 48.34           O  
HETATM 3164  O   HOH A 633      43.592  48.231  52.003  1.00 38.74           O  
HETATM 3165  O   HOH A 634      27.975   9.025  74.386  1.00 45.86           O  
HETATM 3166  O   HOH A 635      57.020  35.845  47.449  1.00 39.94           O  
HETATM 3167  O   HOH A 636      18.912  68.323  49.322  1.00 45.47           O  
HETATM 3168  O   HOH A 637      39.869   4.208  74.056  1.00 40.06           O  
HETATM 3169  O   HOH A 638      42.861  71.946  56.121  1.00 43.60           O  
HETATM 3170  O   HOH A 639      30.644  62.980  55.627  1.00 39.18           O  
HETATM 3171  O   HOH A 640      43.287  62.465  50.750  1.00 36.15           O  
HETATM 3172  O   HOH A 641      29.937  56.416  59.288  1.00 49.43           O  
HETATM 3173  O   HOH A 642      36.879  34.092  47.431  1.00 54.48           O  
HETATM 3174  O   HOH A 643      27.573  67.366  37.209  1.00 44.33           O  
HETATM 3175  O   HOH A 644      54.720  34.005  63.001  1.00 42.60           O  
HETATM 3176  O   HOH A 645      45.520  40.397  44.481  1.00 37.56           O  
HETATM 3177  O   HOH A 646      41.183  37.148  59.313  1.00 61.78           O  
HETATM 3178  O   HOH A 647      42.337   6.019  61.756  1.00 43.28           O  
HETATM 3179  O   HOH A 648      17.470  51.762  52.361  1.00 55.14           O  
HETATM 3180  O   HOH A 649      43.799  61.700  38.984  1.00 36.99           O  
HETATM 3181  O   HOH A 650      38.498  32.005  55.500  1.00 51.84           O  
HETATM 3182  O   HOH A 651      29.744  11.094  85.348  1.00 42.55           O  
HETATM 3183  O   HOH A 652      18.046  63.797  58.926  1.00 55.86           O  
HETATM 3184  O   HOH A 653      18.039  61.559  48.815  1.00 52.95           O  
HETATM 3185  O   HOH A 654      42.868  40.612  59.320  1.00 44.28           O  
HETATM 3186  O   HOH A 655      45.050  12.033  63.645  1.00 49.15           O  
HETATM 3187  O   HOH A 656      41.567   2.073  74.709  1.00 51.74           O  
HETATM 3188  O   HOH A 657      55.924  57.306  38.311  1.00 39.34           O  
HETATM 3189  O   HOH A 658      25.912   8.407  58.771  1.00 43.74           O  
HETATM 3190  O   HOH A 659      34.642  73.054  50.622  1.00 44.43           O  
HETATM 3191  O   HOH A 660      37.262  16.455  67.417  1.00 49.24           O  
HETATM 3192  O   HOH A 661      34.145  71.443  53.025  1.00 37.66           O  
HETATM 3193  O   HOH A 662      23.031  66.774  61.756  1.00 42.98           O  
HETATM 3194  O   HOH A 663      48.789  54.347  25.682  1.00 53.91           O  
HETATM 3195  O   HOH A 664      49.455  43.572  32.998  1.00 53.19           O  
HETATM 3196  O   HOH A 665      36.551  62.417  50.527  1.00 34.68           O  
HETATM 3197  O   HOH A 666      39.389  58.979  44.040  1.00 34.32           O  
HETATM 3198  O   HOH A 667      50.818  55.027  31.819  1.00 41.14           O  
HETATM 3199  O   HOH A 668      55.557  33.641  42.107  1.00 46.50           O  
HETATM 3200  O   HOH A 669      36.012  52.919  46.901  1.00 43.93           O  
HETATM 3201  O   HOH A 670      42.629   8.863  61.765  1.00 40.76           O  
HETATM 3202  O   HOH A 671      18.435  57.978  54.119  1.00 45.93           O  
HETATM 3203  O   HOH A 672      43.471  40.907  66.191  1.00 49.27           O  
HETATM 3204  O   HOH A 673      42.018  26.611  67.214  1.00 43.98           O  
HETATM 3205  O   HOH A 674      58.070  30.063  64.895  1.00 44.47           O  
HETATM 3206  O   HOH A 675      38.727  29.981  56.896  1.00 50.40           O  
HETATM 3207  O   HOH A 676      39.951  10.736  69.999  1.00 49.71           O  
HETATM 3208  O   HOH A 677      62.486  40.437  49.440  1.00 39.47           O  
HETATM 3209  O   HOH A 678      45.642  55.387  53.772  1.00 54.39           O  
HETATM 3210  O   HOH A 679      41.725  45.067  35.118  1.00 46.40           O  
HETATM 3211  O   HOH A 680      51.962  15.747  52.350  1.00 53.79           O  
HETATM 3212  O   HOH A 681      47.728  45.171  65.765  1.00 49.48           O  
HETATM 3213  O   HOH A 682      38.247  13.415  70.227  1.00 55.23           O  
HETATM 3214  O   HOH A 683      47.401  33.437  65.062  1.00 34.15           O  
HETATM 3215  O   HOH A 684      51.398  39.793  65.936  1.00 40.04           O  
HETATM 3216  O   HOH A 685      47.393  60.561  52.889  1.00 37.93           O  
HETATM 3217  O   HOH A 686      40.135   9.729  79.981  1.00 41.74           O  
HETATM 3218  O   HOH A 687      30.354   3.409  48.546  1.00 55.19           O  
HETATM 3219  O   HOH A 688      62.749  52.530  58.897  1.00 61.45           O  
HETATM 3220  O   HOH A 689      53.735  20.879  57.232  1.00 51.29           O  
HETATM 3221  O   HOH A 690      61.443  55.863  43.160  1.00 42.24           O  
HETATM 3222  O   HOH A 691      40.807  40.076  53.157  1.00 36.58           O  
HETATM 3223  O   HOH A 692      20.834  68.618  42.641  1.00 46.18           O  
HETATM 3224  O   HOH A 693      24.747  73.661  57.478  1.00 47.36           O  
HETATM 3225  O   HOH A 694      34.103  11.012  75.798  1.00 42.66           O  
HETATM 3226  O   HOH A 695      46.326  67.972  50.143  1.00 42.20           O  
HETATM 3227  O   HOH A 696      36.224  10.031  70.052  1.00 36.71           O  
HETATM 3228  O   HOH A 697      49.797  59.093  35.378  1.00 48.15           O  
HETATM 3229  O   HOH A 698      25.255  55.539  63.797  1.00 50.49           O  
HETATM 3230  O   HOH A 699      41.649  28.036  41.300  1.00 49.39           O  
HETATM 3231  O   HOH A 700      37.581  -0.159  69.660  1.00 40.32           O  
HETATM 3232  O   HOH A 701      29.860  63.757  30.456  1.00 55.00           O  
HETATM 3233  O   HOH A 702      28.755  66.121  40.549  1.00 35.97           O  
HETATM 3234  O   HOH A 703      30.168  -7.220  66.784  1.00 54.42           O  
HETATM 3235  O   HOH A 704      46.399  24.208  44.598  1.00 39.39           O  
HETATM 3236  O   HOH A 705      33.581  11.854  68.665  1.00 34.01           O  
HETATM 3237  O   HOH A 706      38.509  33.483  44.576  1.00 49.21           O  
HETATM 3238  O   HOH A 707      39.577  18.769  47.832  1.00 45.37           O  
HETATM 3239  O   HOH A 708      27.888   0.177  63.456  1.00 39.77           O  
HETATM 3240  O   HOH A 709      50.488  23.028  62.688  1.00 40.75           O  
HETATM 3241  O   HOH A 710      44.443  32.931  43.835  1.00 40.74           O  
HETATM 3242  O   HOH A 711      46.697  30.293  40.723  1.00 51.17           O  
HETATM 3243  O   HOH A 712      42.900  48.496  31.025  1.00 46.42           O  
HETATM 3244  O   HOH A 713      61.109  27.665  55.224  1.00 49.63           O  
HETATM 3245  O   HOH A 714      40.746   0.427  59.134  1.00 50.71           O  
HETATM 3246  O   HOH A 715      36.537  71.287  45.186  1.00 39.52           O  
HETATM 3247  O   HOH A 716      22.545   6.933  80.547  1.00 52.59           O  
HETATM 3248  O   HOH A 717      60.484  60.085  44.593  1.00 57.69           O  
HETATM 3249  O   HOH A 718      50.612  41.480  37.377  1.00 44.61           O  
HETATM 3250  O   HOH A 719      38.317  25.793  52.168  1.00 49.03           O  
HETATM 3251  O   HOH A 720      35.496  14.705  67.420  1.00 51.57           O  
HETATM 3252  O   HOH A 721      29.826  67.717  35.022  1.00 47.03           O  
HETATM 3253  O   HOH A 722      50.437  64.751  45.299  1.00 47.03           O  
HETATM 3254  O   HOH A 723      45.108  34.112  37.137  1.00 51.32           O  
HETATM 3255  O   HOH A 724      63.150  50.377  54.063  1.00 45.55           O  
HETATM 3256  O   HOH A 725      35.777   9.499  74.497  1.00 36.64           O  
HETATM 3257  O   HOH A 726      31.128  11.968  60.193  1.00 36.00           O  
HETATM 3258  O   HOH A 727      39.535  56.616  40.956  1.00 29.40           O  
HETATM 3259  O   HOH A 728      44.158  45.903  55.081  1.00 50.29           O  
HETATM 3260  O   HOH A 729      28.435  13.475  56.095  1.00 43.95           O  
HETATM 3261  O   HOH A 730      34.580   2.644  91.553  1.00 46.40           O  
HETATM 3262  O   HOH A 731      39.853  23.042  50.065  1.00 45.00           O  
HETATM 3263  O   HOH A 732      35.668  69.628  54.233  1.00 41.03           O  
HETATM 3264  O   HOH A 733      32.195  12.964  64.286  1.00 38.10           O  
HETATM 3265  O   HOH A 734      55.985  30.999  42.308  1.00 46.25           O  
HETATM 3266  O   HOH A 735      23.110  61.514  36.005  1.00 51.25           O  
HETATM 3267  O   HOH A 736      29.010  15.066  59.349  1.00 45.28           O  
HETATM 3268  O   HOH A 737      39.286  21.793  47.399  1.00 54.81           O  
HETATM 3269  O   HOH A 738      33.666  58.326  50.390  1.00 43.26           O  
HETATM 3270  O   HOH A 739      51.065  61.553  39.836  1.00 52.65           O  
HETATM 3271  O   HOH A 740      18.579  53.676  43.430  1.00 46.59           O  
HETATM 3272  O   HOH A 741      32.160   5.182  53.973  1.00 46.47           O  
HETATM 3273  O   HOH A 742      37.851  23.421  60.763  1.00 49.64           O  
HETATM 3274  O   HOH A 743      44.535  31.596  67.070  1.00 50.35           O  
HETATM 3275  O   HOH A 744      30.396  72.813  54.450  1.00 55.17           O  
HETATM 3276  O   HOH A 745      43.806  27.319  69.475  1.00 56.96           O  
HETATM 3277  O   HOH A 746      44.572  39.286  61.751  1.00 38.32           O  
HETATM 3278  O   HOH A 747      18.200  62.800  44.881  1.00 49.54           O  
HETATM 3279  O   HOH A 748      26.402  -5.603  67.460  1.00 49.32           O  
HETATM 3280  O   HOH A 749      29.849  15.609  61.725  1.00 52.31           O  
HETATM 3281  O   HOH A 750      46.112  33.188  40.604  1.00 47.30           O  
HETATM 3282  O   HOH A 751      28.714  10.528  78.699  1.00 45.38           O  
HETATM 3283  O   HOH A 752      46.436  37.876  43.486  1.00 40.11           O  
HETATM 3284  O   HOH A 753      51.855  46.561  64.950  1.00 58.42           O  
HETATM 3285  O   HOH A 754      58.260  37.758  62.145  1.00 41.61           O  
HETATM 3286  O   HOH A 755      19.576   1.729  71.508  1.00 45.99           O  
HETATM 3287  O   HOH A 756      65.124  41.439  49.757  1.00 36.94           O  
HETATM 3288  O   HOH A 757      44.530   6.777  52.720  1.00 54.26           O  
HETATM 3289  O   HOH A 758      35.139  63.311  31.155  1.00 47.85           O  
HETATM 3290  O   HOH A 759      37.172  56.698  48.651  1.00 41.90           O  
HETATM 3291  O   HOH A 760      54.413  24.982  43.120  1.00 49.95           O  
HETATM 3292  O   HOH A 761      54.426  58.495  40.789  1.00 48.65           O  
HETATM 3293  O   HOH A 762      22.628   4.617  64.561  1.00 53.74           O  
HETATM 3294  O   HOH A 763      48.220  25.909  70.437  1.00 60.06           O  
HETATM 3295  O   HOH A 764      36.197  59.868  50.131  1.00 38.40           O  
HETATM 3296  O   HOH A 765      48.350  30.087  68.490  1.00 45.39           O  
HETATM 3297  O   HOH A 766      38.505  45.709  40.746  1.00 47.58           O  
HETATM 3298  O   HOH A 767      44.706  30.864  42.452  1.00 39.11           O  
HETATM 3299  O   HOH A 768      55.523  40.096  39.193  1.00 49.15           O  
HETATM 3300  O   HOH A 769      39.516   6.754  85.766  1.00 37.43           O  
HETATM 3301  O   HOH A 770      23.249  51.334  39.590  1.00 32.77           O  
HETATM 3302  O   HOH A 771      19.994   4.305  73.236  1.00 53.21           O  
HETATM 3303  O   HOH A 772      17.287  62.167  51.347  1.00 50.48           O  
HETATM 3304  O   HOH A 773      50.100  44.492  64.891  1.00 40.74           O  
HETATM 3305  O   HOH A 774      34.688  10.721  82.124  1.00 46.40           O  
HETATM 3306  O   HOH A 775      43.867  50.727  53.815  1.00 50.59           O  
HETATM 3307  O   HOH A 776      40.604  66.346  34.736  1.00 45.02           O  
HETATM 3308  O   HOH A 777      31.691   5.251  98.622  1.00 48.92           O  
HETATM 3309  O   HOH A 778      22.985  70.230  55.254  1.00 43.44           O  
HETATM 3310  O   HOH A 779      53.181  64.484  46.131  1.00 42.56           O  
HETATM 3311  O   HOH A 780      39.108  33.520  67.656  1.00 45.80           O  
HETATM 3312  O   HOH A 781      41.026   9.716  67.877  1.00 47.51           O  
HETATM 3313  O   HOH A 782      48.280  50.092  60.760  1.00 43.49           O  
HETATM 3314  O   HOH A 783      52.272  24.597  65.416  1.00 43.04           O  
HETATM 3315  O   HOH A 784      44.811  61.228  52.609  1.00 37.92           O  
HETATM 3316  O   HOH A 785      67.988  42.465  56.085  1.00 44.89           O  
HETATM 3317  O   HOH A 786      20.522  60.882  59.709  1.00 52.20           O  
HETATM 3318  O   HOH A 787      64.990  50.929  44.908  1.00 44.32           O  
HETATM 3319  O   HOH A 788      40.626  10.249  63.173  1.00 34.20           O  
HETATM 3320  O   HOH A 789      52.939  28.052  69.578  1.00 57.66           O  
HETATM 3321  O   HOH A 790      39.595  25.186  68.010  1.00 45.74           O  
HETATM 3322  O   HOH A 791      42.873   5.125  64.403  1.00 51.50           O  
HETATM 3323  O   HOH A 792      25.281   0.626  63.742  1.00 43.27           O  
HETATM 3324  O   HOH A 793      39.171  39.732  46.793  1.00 61.33           O  
HETATM 3325  O   HOH A 794      69.357  37.875  52.072  1.00 52.30           O  
HETATM 3326  O   HOH A 795      18.499  51.758  41.063  1.00 40.52           O  
HETATM 3327  O   HOH A 796      22.086  10.351  80.581  1.00 57.16           O  
HETATM 3328  O   HOH A 797      31.983  13.193  67.081  1.00 39.68           O  
HETATM 3329  O   HOH A 798      30.027  14.412  54.018  1.00 46.80           O  
HETATM 3330  O   HOH A 799      26.588  10.257  73.147  1.00 56.18           O  
HETATM 3331  O   HOH A 800      41.369  75.439  49.952  1.00 54.11           O  
HETATM 3332  O   HOH A 801      41.389  11.356  65.739  1.00 38.46           O  
HETATM 3333  O   HOH A 802      56.966  47.272  64.911  1.00 56.18           O  
HETATM 3334  O   HOH A 803      40.533  42.196  46.262  1.00 45.98           O  
HETATM 3335  O   HOH A 804      50.396  35.011  37.873  1.00 42.53           O  
HETATM 3336  O   HOH A 805      52.686  54.213  57.853  1.00 40.03           O  
HETATM 3337  O   HOH A 806      44.761   5.425  60.256  1.00 55.32           O  
HETATM 3338  O   HOH A 807      54.608  55.399  58.067  1.00 59.70           O  
HETATM 3339  O   HOH A 808      38.267  23.066  52.263  1.00 43.16           O  
HETATM 3340  O   HOH A 809      40.150  60.952  51.384  1.00 45.56           O  
HETATM 3341  O   HOH A 810      33.265   2.827  54.837  1.00 42.34           O  
HETATM 3342  O   HOH A 811      25.714   2.181  89.625  1.00 46.80           O  
HETATM 3343  O   HOH A 812      17.048  59.583  52.915  1.00 49.64           O  
HETATM 3344  O   HOH A 813      43.566   7.351  66.079  1.00 57.17           O  
HETATM 3345  O   HOH A 814      28.196  15.289  68.447  1.00 51.12           O  
HETATM 3346  O   HOH A 815      40.206   3.346  71.490  1.00 43.81           O  
HETATM 3347  O   HOH A 816      20.945  -4.942  61.913  1.00 53.46           O  
HETATM 3348  O   HOH A 817      29.581  68.938  42.497  1.00 35.02           O  
HETATM 3349  O   HOH A 818      51.074   8.280  59.695  1.00 55.78           O  
HETATM 3350  O   HOH A 819      37.638  -4.981  85.312  1.00 59.63           O  
HETATM 3351  O   HOH A 820      57.443  46.092  36.899  1.00 48.85           O  
HETATM 3352  O   HOH A 821      40.151  34.363  56.514  1.00 51.97           O  
HETATM 3353  O   HOH A 822      39.993  37.284  50.923  1.00 46.83           O  
HETATM 3354  O   HOH A 823      47.103  57.984  54.264  1.00 44.54           O  
HETATM 3355  O   HOH A 824      51.824  42.352  65.874  1.00 54.07           O  
HETATM 3356  O   HOH A 825      33.836  22.885  58.998  1.00 51.10           O  
HETATM 3357  O   HOH A 826      25.830  72.734  44.026  1.00 58.43           O  
HETATM 3358  O   HOH A 827      40.405   1.159  66.370  1.00 50.48           O  
HETATM 3359  O   HOH A 828      41.259   6.604  74.257  1.00 51.42           O  
HETATM 3360  O   HOH A 829      39.926   8.422  75.409  1.00 48.33           O  
HETATM 3361  O   HOH A 830      33.700  13.285  71.009  1.00 46.51           O  
HETATM 3362  O   HOH A 831      44.703   9.712  51.337  1.00 60.21           O  
HETATM 3363  O   HOH A 832      29.884   9.949  76.884  1.00 51.38           O  
HETATM 3364  O   HOH A 833      30.851  54.492  58.137  1.00 55.86           O  
HETATM 3365  O   HOH A 834      40.246  47.275  52.214  1.00 61.38           O  
HETATM 3366  O   HOH A 835      37.571  26.552  66.613  1.00 55.24           O  
HETATM 3367  O   HOH A 836      29.581  68.772  39.813  1.00 48.14           O  
HETATM 3368  O   HOH A 837      44.604  22.751  43.449  1.00 44.48           O  
HETATM 3369  O   HOH A 838      49.286  52.186  60.718  1.00 57.02           O  
HETATM 3370  O   HOH A 839      30.101  10.630  80.980  1.00 47.78           O  
HETATM 3371  O   HOH A 840      35.905  26.605  51.724  1.00 53.44           O  
HETATM 3372  O   HOH A 841      23.277  69.737  62.159  1.00 44.29           O  
HETATM 3373  O   HOH A 842      32.523   4.595  51.314  1.00 44.65           O  
HETATM 3374  O   HOH A 843      32.414   9.876  77.609  1.00 48.90           O  
HETATM 3375  O   HOH A 844      31.152  15.562  67.753  1.00 51.05           O  
HETATM 3376  O   HOH A 845      50.391  28.273  67.808  1.00 48.32           O  
HETATM 3377  O   HOH A 846      41.770  59.431  50.983  1.00 48.18           O  
HETATM 3378  O   HOH A 847      29.993  17.067  56.847  1.00 50.33           O  
HETATM 3379  O   HOH A 848      46.046  50.229  62.411  1.00 50.52           O  
HETATM 3380  O   HOH A 849      24.791  75.327  54.219  1.00 58.58           O  
HETATM 3381  O   HOH A 850      28.247  49.217  34.652  1.00 63.64           O  
HETATM 3382  O   HOH A 851      32.754  10.780  80.116  1.00 43.29           O  
HETATM 3383  O   HOH A 852      42.387   8.604  80.927  1.00 46.36           O  
HETATM 3384  O   HOH A 853      13.328  52.497  49.684  1.00 63.74           O  
HETATM 3385  O   HOH A 854      63.459  52.806  56.028  1.00 58.20           O  
HETATM 3386  O   HOH A 855      39.803   0.788  70.581  1.00 42.26           O  
HETATM 3387  O   HOH A 856      38.355  -0.408  67.074  1.00 50.56           O  
HETATM 3388  O   HOH A 857      55.108  40.670  64.034  1.00 47.63           O  
HETATM 3389  O   HOH A 858      46.951  31.970  67.437  1.00 41.17           O  
HETATM 3390  O   HOH A 859      23.125  71.640  57.663  1.00 48.06           O  
HETATM 3391  O   HOH A 860      36.179  25.838  64.525  1.00 58.73           O  
HETATM 3392  O   HOH A 861      40.788   9.983  77.238  1.00 49.98           O  
HETATM 3393  O   HOH A 862      44.720   9.694  63.056  1.00 53.79           O  
HETATM 3394  O   HOH A 863      17.821  61.909  42.012  1.00 43.12           O  
HETATM 3395  O   HOH A 864      57.093  23.925  64.654  1.00 55.07           O  
HETATM 3396  O   HOH A 865      53.924  43.142  64.147  1.00 49.25           O  
HETATM 3397  O   HOH A 866      38.784  38.783  49.303  1.00 49.63           O  
HETATM 3398  O   HOH A 867      54.915  23.402  65.897  1.00 49.68           O  
HETATM 3399  O   HOH A 868      21.161  71.639  54.401  1.00 47.51           O  
CONECT 3074 3075 3079 3082                                                      
CONECT 3075 3074 3076 3080                                                      
CONECT 3076 3075 3077                                                           
CONECT 3077 3076 3078 3081                                                      
CONECT 3078 3077 3079                                                           
CONECT 3079 3074 3078                                                           
CONECT 3080 3075                                                                
CONECT 3081 3077                                                                
CONECT 3082 3074 3083 3087                                                      
CONECT 3083 3082 3084 3085                                                      
CONECT 3084 3083                                                                
CONECT 3085 3083 3086 3088                                                      
CONECT 3086 3085 3087 3089                                                      
CONECT 3087 3082 3086                                                           
CONECT 3088 3085                                                                
CONECT 3089 3086 3090                                                           
CONECT 3090 3089 3091                                                           
CONECT 3091 3090 3092 3093 3094                                                 
CONECT 3092 3091                                                                
CONECT 3093 3091                                                                
CONECT 3094 3091 3095                                                           
CONECT 3095 3094 3096 3097 3098                                                 
CONECT 3096 3095                                                                
CONECT 3097 3095                                                                
CONECT 3098 3095 3099                                                           
CONECT 3099 3098 3100 3101 3102                                                 
CONECT 3100 3099                                                                
CONECT 3101 3099                                                                
CONECT 3102 3099                                                                
CONECT 3103 3104 3105                                                           
CONECT 3104 3103                                                                
CONECT 3105 3103 3106 3107                                                      
CONECT 3106 3105                                                                
CONECT 3107 3105 3108                                                           
CONECT 3108 3107                                                                
CONECT 3109 3110 3111                                                           
CONECT 3110 3109                                                                
CONECT 3111 3109 3112 3113                                                      
CONECT 3112 3111                                                                
CONECT 3113 3111 3114                                                           
CONECT 3114 3113                                                                
CONECT 3115 3116 3117 3118                                                      
CONECT 3116 3115                                                                
CONECT 3117 3115                                                                
CONECT 3118 3115                                                                
CONECT 3119 3120 3121 3122                                                      
CONECT 3120 3119                                                                
CONECT 3121 3119                                                                
CONECT 3122 3119                                                                
CONECT 3123 3124 3125 3126                                                      
CONECT 3124 3123                                                                
CONECT 3125 3123                                                                
CONECT 3126 3123                                                                
CONECT 3127 3128 3129 3130 3131                                                 
CONECT 3128 3127                                                                
CONECT 3129 3127                                                                
CONECT 3130 3127                                                                
CONECT 3131 3127                                                                
MASTER      332    0    7   24   11    0   15    6 3398    1   58   33          
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.